The query sequence for this search has been filtered. Filtering
eliminates low complexity regions that commonly give spuriously high
scores that reflect compositional bias rather than significant
position-by-position alignment. Filtering can eliminate these potentially
confounding matches (e.g., hits against proline-rich regions or poly-A
tails) from the blast reports, leaving regions whose blast statistics
reflect the specificity of their pairwise alignment.

BLASTX 2.1.1 [Aug-8-2000]


Reference: Altschul, Stephen F., Thomas L. Madden, Alejandro A. Schaffer, 
Jinghui Zhang, Zheng Zhang, Webb Miller, and David J. Lipman (1997), 
"Gapped BLAST and PSI-BLAST: a new generation of protein database search
programs",  Nucleic Acids Res. 25:3389-3402.

Query= Contig4.seq Contig4
         (854 letters)

Database: nr
           565,281 sequences; 177,575,912 total letters


                                                                   Score     E
Sequences producing significant alignments:                        (bits)  Value

ref|NP_012992.1|  Cytochrome-c peroxidase; Ccp1p >gi|543969|...   190  2e-47
pdb|2CYP|     Cytochrome c Peroxidase (E.C.1.11.1.5) (Ferroc...   190  2e-47
pdb|1CCK|     Altering Substrate Specificity Of Cytochrome C...   188  6e-47
pdb|1CYF|     Mol_id: 1; Molecule: Cytochrome C Peroxidase; ...   187  1e-46
pdb|3CCP|     Yeast Cytochrome c Peroxidase (E.C.1.11.1.5) M...   187  1e-46
pdb|1A2F|     Probing The Strength And Character Of An Asp-H...   187  1e-46
pdb|1BES|     Interaction Between Proximal And Distals Regio...   187  1e-46
pdb|2CEP|     Cytochrome C Peroxidase (E.C.1.11.1.5) Mutant ...   187  2e-46
pdb|2CCP|     Yeast Cytochrome c Peroxidase (E.C.1.11.1.5) M...   187  2e-46
pdb|1CPG|     Cytochrome C Peroxidase (E.C.1.11.1.5) Mutant ...   187  2e-46
pdb|2PCC|A  Chain A, Yeast Cytochrome C Peroxidase (Ccp) Com...   187  2e-46
gb|AAA88709.1|  (J01468) cytochrome c peroxidase [Saccharomy...   187  2e-46
pdb|1BEM|     Interaction Between Proximal And Distals Regio...   187  2e-46
pdb|1A2G|     Probing The Strength And Character Of An Asp-H...   187  2e-46
pdb|1BEP|     Effect Of Unnatural Heme Substitution On Kinet...   187  2e-46
pdb|1CCA|     Cytochrome C Peroxidase (Ccp-Mkt) (E.C.1.11.1....   187  2e-46
pdb|1CCC|     Cytochrome C Peroxidase (Ccp-Mkt) (E.C.1.11.1....   187  2e-46
pdb|1CCB|     Cytochrome C Peroxidase (Ccp-Mkt) (E.C.1.11.1....   187  2e-46
pdb|1CPE|     Cytochrome C Peroxidase (E.C.1.11.1.5) Mutant ...   186  3e-46
pdb|1AC4|     Variation In The Strength Of A Ch To O Hydroge...   186  3e-46
pdb|1CMU|     Cytochrome C Peroxidase (Ccp-Mkt) (E.C.1.11.1....   186  3e-46
pdb|1AA4|     Specificity Of Ligand Binding In A Buried Pola...   186  3e-46
pdb|1BEJ|     Interaction Between Proximal And Distals Regio...   186  3e-46
pdb|6CCP|     Cytochrome C Peroxidase (E.C.1.11.1.5) Mutant ...   185  4e-46
pdb|4CCX|     Cytochrome C Peroxidase (E.C.1.11.1.5) (Ccp-Mk...   185  7e-46
pdb|1CCL|     Probing The Strength And Character Of An Asp-H...   185  7e-46
pdb|1BEK|     Effect Of Unnatural Heme Substitution On Kinet...   185  7e-46
pdb|3CCX|     Cytochrome C Peroxidase (E.C.1.11.1.5) (Ccp-Mk...   184  9e-46
pdb|1CCJ|     Conformer Selection By Ligand Binding Observed...   184  9e-46
pdb|1DJ5|A  Chain A, Crystal Structure Of R48a Mutant Of Cyt...   184  9e-46
pdb|7CCP|     Cytochrome C Peroxidase (E.C.1.11.1.5) Mutant ...   184  1e-45
pdb|4CCP|     Yeast Cytochrome c Peroxidase (E.C.1.11.1.5) M...   183  3e-45
pdb|1CCG|     Cytochrome C Peroxidase (E.C.1.11.1.5) (Ccp-Mk...   183  3e-45
pdb|5CCP|     Cytochrome C Peroxidase (E.C.1.11.1.5) Mutant ...   182  3e-45
pdb|1BVA|A  Chain A, Manganese Binding Mutant In Cytochrome ...   179  3e-44
gb|AAC08576.1|  (AF053474) cytosolic ascorbate peroxidase [Z...   166  2e-40
pir||S20866  L-ascorbate peroxidase (EC 1.11.1.11) precursor...   163  3e-39
sp|Q05431|APX1_ARATH  L-ASCORBATE PEROXIDASE, CYTOSOLIC (AP)...   161  7e-39
pir||T03595  probable L-ascorbate peroxidase (EC 1.11.1.11) ...   160  2e-38
pir||S43157  L-ascorbate peroxidase (EC 1.11.1.11) - radish ...   160  2e-38
pir||S49914  L-ascorbate peroxidase (EC 1.11.1.11), cytosoli...   159  4e-38
pir||T10189  L-ascorbate peroxidase (EC 1.11.1.11), cytosoli...   158  6e-38
pir||JE0232  L-ascorbate peroxidase (EC 1.11.1.11) - garden ...   158  6e-38
gb|AAD41404.1|AF159629_1  (AF159629) cytosolic ascorbate per...   158  6e-38
emb|CAA06996.1|  (AJ006358) ascorbate peroxidase [Hordeum vu...   158  6e-38
gb|AAD41407.1|AF159632_1  (AF159632) cytosolic ascorbate per...   158  9e-38
gb|AAD41402.1|AF159627_1  (AF159627) cytosolic ascorbate per...   158  9e-38
gb|AAB94574.1|  (AF022213) cytosolic ascorbate peroxidase [F...   157  1e-37
gb|AAF23294.1|AC016661_19  (AC016661) putative ascorbate per...   157  1e-37
emb|CAA56340.1|  (X80036) ascorbate peroxidase [Arabidopsis ...   157  1e-37
emb|CAA72247.1|  (Y11461) L-ascorbate peroxidase [Brassica n...   154  1e-36
pir||S68465  L-ascorbate peroxidase (EC 1.11.1.11), cytosoli...   153  2e-36
pir||T09845  L-ascorbate peroxidase (EC 1.11.1.11), glyoxyso...   153  2e-36
emb|CAA57140.1|  (X81376) L-ascorbate peroxidase [Capsicum a...   153  2e-36
dbj|BAA12918.1|  (D85912) cytosolic ascorbate peroxidase [Ni...   153  3e-36
gb|AAD30294.1|AF139190_1  (AF139190) cytosolic ascorbate per...   153  3e-36
pdb|1APX|A  Chain A, Crystal Structure Of Recombinant Ascorb...   152  5e-36
sp|P48534|APX1_PEA  L-ASCORBATE PEROXIDASE, CYTOSOLIC (AP) >...   152  5e-36
gb|AAA86689.1|  (U15933) ascorbate peroxidase [Nicotiana tab...   150  1e-35
pir||T09125  L-ascorbate peroxidase (EC 1.11.1.11) - spinach...   150  1e-35
gb|AAB03844.1|  (U61379) ascorbate peroxidase [Vigna unguicu...   150  2e-35
pir||S71279  L-ascorbate peroxidase (EC 1.11.1.11) - Arabido...   150  2e-35
emb|CAB58361.1|  (Y16773) ascorbate peroxidase [Lycopersicon...   149  3e-35
emb|CAA06823.1|  (AJ006030) ascorbate peroxidase [Arabidopsi...   149  3e-35
gb|AAD43334.1|AF159254_1  (AF159254) ascorbate peroxidase [Z...   149  4e-35
pir||T07056  L-ascorbate peroxidase (EC 1.11.1.11) 2 - soybe...   149  4e-35
gb|AAA61779.1|  (L10292) ascorbate peroxidase [Glycine max]       147  2e-34
gb|AAF22246.1|  (AF159380) ascorbate peroxidase [Pimpinella ...   145  5e-34
pir||S17553  ascorbate peroxidase (EC 1.11.1.-) - garden pea      144  1e-33
gb|AAD20022.1|  (AF127804) ascorbate peroxidase [Glycine max]     143  2e-33
pir||T08071  L-ascorbate peroxidase (EC 1.11.1.11) - leaf mu...   139  3e-32
pir||T08103  L-ascorbate peroxidase (EC 1.11.1.11) precursor...   139  3e-32
pir||T04707  L-ascorbate peroxidase (EC 1.11.1.11) T19K4.100...   139  4e-32
dbj|BAA83595.1|  (AB009084) chloroplast ascorbate peroxidase...   139  5e-32
pir||T12286  L-ascorbate peroxidase (EC 1.11.1.11) precursor...   136  3e-31
pir||T12282  L-ascorbate peroxidase (EC 1.11.1.11) precursor...   136  3e-31
dbj|BAA78552.1|  (AB022273) thylakoid-bound ascorbate peroxi...   134  1e-30
dbj|BAA78553.1|  (AB022274) stromal ascorbate peroxidase [Ni...   134  1e-30
emb|CAA67426.1|  (X98926) thylakoid-bound ascorbate peroxida...   134  2e-30
gb|AAF07783.1|AC010704_8  (AC010704) thylakoid-bound ascorba...   134  2e-30
gb|AAB82778.1|  (AF001529) ripening-associated protein [Musa...   131  1e-29
pir||T10700  L-ascorbate peroxidase (EC 1.11.1.11) precursor...   131  1e-29
pir||T10190  L-ascorbate peroxidase (EC 1.11.1.11) precursor...   131  1e-29
emb|CAA03952.1|  (AJ000223) ascorbate peroxidase [Hordeum vu...   131  1e-29
dbj|BAA19611.1|  (D77997) thylakoid-bound ascorbate peroxida...   130  2e-29
pir||S71330  L-ascorbate peroxidase (EC 1.11.1.11) precursor...   130  2e-29
pir||S71331  L-ascorbate peroxidase (EC 1.11.1.11) precursor...   130  2e-29
dbj|BAA24610.1|  (AB002467) stromal ascorbate peroxidase [Sp...   129  3e-29
dbj|BAA24609.1|  (AB002467) thylakoid-bound ascorbate peroxi...   129  3e-29
pir||T14193  L-ascorbate peroxidase (EC 1.11.1.11) - Arabido...   127  2e-28
emb|CAA67425.1|  (X98925) stromal ascorbate peroxidase [Arab...   126  3e-28
pir||S66265  L-ascorbate peroxidase (EC 1.11.1.11) - spinach...   123  3e-27
pir||T12334  L-ascorbate peroxidase (EC 1.11.1.11) - common ...   120  2e-26
pir||T12389  L-ascorbate peroxidase (EC 1.11.1.11) - common ...   113  3e-24
dbj|BAA76419.1|  (AB024991) ascorbate peroxidase [Cicer arie...   108  1e-22
pir||T12338  L-ascorbate peroxidase (EC 1.11.1.11) - common ...   105  6e-22
sp|Q9WXB9|CATA_LEGPN  PEROXIDASE/CATALASE (CATALASE-PEROXIDA...   102  5e-21
dbj|BAB04625.1|  (AP001510) catalase [Bacillus halodurans]        101  9e-21
dbj|BAA37056.1|  (AB020144) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37035.1|  (AB020123) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37068.1|  (AB020156) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37078.1|  (AB020235) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37038.1|  (AB020126) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37067.1|  (AB020155) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37061.1|  (AB020149) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37066.1|  (AB020154) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37057.1|  (AB020145) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37073.1|  (AB020161) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37036.1|  (AB020124) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37074.1|  (AB020162) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37047.1|  (AB020135) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37052.1|  (AB020140) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37051.1|  (AB020139) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37034.1|  (AB020122) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37048.1|  (AB020136) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37062.1|  (AB020150) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37076.1|  (AB020164) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37069.1|  (AB020157) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37043.1|  (AB020131) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37037.1|  (AB020125) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37046.1|  (AB020134) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37075.1|  (AB020163) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37039.1|  (AB020127) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37040.1|  (AB020128) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37077.1|  (AB020165) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37054.1|  (AB020142) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37041.1|  (AB020129) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37060.1|  (AB020148) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37058.1|  (AB020146) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37064.1|  (AB020152) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37072.1|  (AB020160) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37063.1|  (AB020151) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37049.1|  (AB020137) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37059.1|  (AB020147) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37050.1|  (AB020138) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37042.1|  (AB020130) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37044.1|  (AB020132) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37055.1|  (AB020143) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37071.1|  (AB020159) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37053.1|  (AB020141) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37045.1|  (AB020133) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37065.1|  (AB020153) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37070.1|  (AB020158) catalase [Bacillus stearothermop...   100  2e-20
dbj|BAA37029.1|  (AB020117) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA37028.1|  (AB020116) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA37015.1|  (AB020103) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA37018.1|  (AB020106) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA37012.1|  (AB020100) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA37033.1|  (AB020121) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA37001.1|  (AB020089) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA36982.1|  (AB020070) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA36980.1|  (AB020068) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA37007.1|  (AB020095) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA36977.1|  (AB020065) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA37032.1|  (AB020120) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA37027.1|  (AB020115) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA37004.1|  (AB020092) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA36979.1|  (AB020067) catalase [Bacillus stearothermop...    99  7e-20
sp|P14412|CATA_BACST  PEROXIDASE/CATALASE (CATALASE-PEROXIDA...    99  7e-20
dbj|BAA37023.1|  (AB020111) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA37020.1|  (AB020108) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA37026.1|  (AB020114) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA37019.1|  (AB020107) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA36994.1|  (AB020082) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA36997.1|  (AB020085) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA37009.1|  (AB020097) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA36976.1|  (AB020064) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA37000.1|  (AB020088) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA36988.1|  (AB020076) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA37002.1|  (AB020090) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA36995.1|  (AB020083) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA36993.1|  (AB020081) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA37005.1|  (AB020093) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA37025.1|  (AB020113) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA36999.1|  (AB020087) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA36989.1|  (AB020077) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA36985.1|  (AB020073) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA37017.1|  (AB020105) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA36986.1|  (AB020074) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA37008.1|  (AB020096) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA37021.1|  (AB020109) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA37014.1|  (AB020102) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA36992.1|  (AB020080) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA37003.1|  (AB020091) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA36987.1|  (AB020075) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA37010.1|  (AB020098) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA36984.1|  (AB020072) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA37011.1|  (AB020099) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA36991.1|  (AB020079) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA37024.1|  (AB020112) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA36978.1|  (AB020066) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA37030.1|  (AB020118) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA36983.1|  (AB020071) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA37016.1|  (AB020104) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA36998.1|  (AB020086) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA37022.1|  (AB020110) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA36996.1|  (AB020084) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA37013.1|  (AB020101) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA36990.1|  (AB020078) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA37006.1|  (AB020094) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA37031.1|  (AB020119) catalase [Bacillus stearothermop...    99  7e-20
dbj|BAA36981.1|  (AB020069) catalase [Bacillus stearothermop...    99  7e-20
sp|O59651|CATA_HALMA  PEROXIDASE/CATALASE (CATALASE-PEROXIDA...    94  2e-18
sp|Q9X6B0|CATA_YERPE  PEROXIDASE/CATALASE (CATALASE-PEROXIDA...    92  6e-18
gb|AAA24040.1|  (M21516) catalase HP1 [Escherichia coli]           88  1e-16
sp|P13029|CATA_ECOLI  PEROXIDASE/CATALASE HPI (CATALASE-PERO...    88  1e-16
gb|AAB03074.1|  (L19201) catalase hydroperoxidase I [Escheri...    88  1e-16
gb|AAF78102.1|AF126956_2  (AF126956) catalase-peroxidase [St...    86  4e-16
sp|P46817|CATA_MYCBO  PEROXIDASE/CATALASE (CATALASE-PEROXIDA...    85  9e-16
emb|CAA48213.1|  (X68081) catalase-peroxidase [Mycobacterium...    85  9e-16
pir||T00313  catalase (EC 1.11.1.6) HPI katP - Escherichia c...    85  9e-16
gb|AAA85170.1|  (U41304) catalase-peroxidase [Mycobacterium ...    84  2e-15
gb|AAA18235.1|  (U06265) catalase [Mycobacterium tuberculosis]     84  2e-15
gb|AAA18233.1|  (U06262) catalase [Mycobacterium tuberculosis]     84  2e-15
gb|AAA18234.1|  (U06264) catalase [Mycobacterium tuberculosis]     84  2e-15
gb|AAA18239.1|  (U06269) catalase [Mycobacterium tuberculosis]     84  2e-15
gb|AAA85169.1|  (U40595) catalase-peroxidase [Mycobacterium ...    84  2e-15
gb|AAA85176.1|  (U41310) catalase-peroxidase [Mycobacterium ...    84  2e-15
gb|AAA85173.1|  (U41307) catalase-peroxidase [Mycobacterium ...    84  2e-15
gb|AAA18231.1|  (U06260) catalase [Mycobacterium tuberculosis]     84  2e-15
gb|AAA85175.1|  (U41309) catalase-peroxidase [Mycobacterium ...    84  2e-15
gb|AAA85174.1|  (U41308) catalase-peroxidase [Mycobacterium ...    84  2e-15
gb|AAA85177.1|  (U41311) catalase-peroxidase [Mycobacterium ...    84  2e-15
gb|AAA85167.1|  (U40593) catalase-peroxidase [Mycobacterium ...    84  2e-15
gb|AAA18238.1|  (U06268) catalase [Mycobacterium tuberculosis]     84  2e-15
gb|AAA18237.1|  (U06267) catalase [Mycobacterium tuberculosis]     84  2e-15
sp|Q08129|CATA_MYCTU  PEROXIDASE/CATALASE T >gi|7427829|pir|...    84  2e-15
gb|AAA85171.1|  (U41305) catalase-peroxidase [Mycobacterium ...    84  2e-15
sp|O28050|CATA_ARCFU  PEROXIDASE/CATALASE (CATALASE-PEROXIDA...    84  2e-15
gb|AAA18230.1|  (U06259) catalase [Mycobacterium tuberculosis]     83  3e-15
gb|AAA18236.1|  (U06266) catalase [Mycobacterium tuberculosis]     83  3e-15
sp|O87864|CATB_STRRE  PEROXIDASE/CATALASE (CATALASE-PEROXIDA...    83  3e-15
gb|AAA18232.1|  (U06261) catalase [Mycobacterium tuberculosis]     83  3e-15
gb|AAC45850.1|  (AF027168) catalase-peroxidase [Caulobacter ...    83  3e-15
pir||S71130  catalase (EC 1.11.1.6) - Synechococcus sp. (str...    83  4e-15
sp|Q9RJH9|CATB_STRCO  PEROXIDASE/CATALASE (CATALASE-PEROXIDA...    83  5e-15
gb|AAA18240.1|  (U06270) catalase [Mycobacterium tuberculosis]     83  5e-15
emb|CAA67268.1|  (X98718) T-catalase [Mycobacterium smegmatis]     82  8e-15
gb|AAF94714.1|  (AE004233) catalase/peroxidase [Vibrio chole...    82  8e-15
sp|O73955|CATA_HALSA  PEROXIDASE/CATALASE (CATALASE-PEROXIDA...    82  1e-14
gb|AAC45275.1|  (U46844) catalase-peroxidase [Mycobacterium ...    82  1e-14
gb|AAD50682.1|  (AF146521) ascorbate peroxidase [Musa acumin...    81  2e-14
gb|AAA18241.1|  (U06271) catalase [Mycobacterium tuberculosis]     80  4e-14
sp|Q04657|CATA_MYCIT  PEROXIDASE/CATALASE (CATALASE-PEROXIDA...    78  2e-13
pir||A47685  catalase (EC 1.11.1.6) HPI - Mycobacterium intr...    78  2e-13
gb|AAF85031.1|AE004035_10  (AE004035) catalase/peroxidase [X...    76  4e-13
sp|P17750|CATA_SALTY  PEROXIDASE/CATALASE HPI (CATALASE-PERO...    76  4e-13
dbj|BAB03310.1|  (AB011415) catalase [Sphingomonas sp.]            75  1e-12
emb|CAA69193.1|  (Y07866) catalase-peroxidase [Mycobacterium...    75  1e-12
gb|AAF20142.1|  (AF207899) catalase-peroxidase [Mycobacteriu...    74  2e-12

>ref|NP_012992.1| Cytochrome-c peroxidase; Ccp1p
 sp|P00431|CCPR_YEAST CYTOCHROME C PEROXIDASE PRECURSOR (CCP)
 pir||OPBYC cytochrome-c peroxidase (EC 1.11.1.5) precursor - yeast
           (Saccharomyces cerevisiae)
 emb|CAA44288.1| (X62422) Cytochrome  c peroxidase [Saccharomyces cerevisiae]
 emb|CAA82145.1| (Z28291) ORF YKR066c [Saccharomyces cerevisiae]
          Length = 361

 Score =  190 bits (477), Expect = 2e-47
 Identities = 99/191 (51%), Positives = 122/191 (63%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD Y  YGPVLVRLAWH SGT+DK   TGGS G T RF 
Sbjct: 82  SYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHTSGTWDKHDNTGGSYGGTYRFK 141

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 142 KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 201

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPDA K  D++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 202 EDTTPDNGRLPDADKDADYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGAA 261

Query: 768 PTVLT-DYYFRLL 803
             V T ++Y  LL
Sbjct: 262 NNVFTNEFYLNLL 274



>pdb|2CYP|    Cytochrome c Peroxidase (E.C.1.11.1.5) (Ferrocytochrome c (Colon)
           H2O2 Reductase)
          Length = 294

 Score =  190 bits (477), Expect = 2e-47
 Identities = 99/191 (51%), Positives = 122/191 (63%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD Y  YGPVLVRLAWH SGT+DK   TGGS G T RF 
Sbjct: 15  SYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHTSGTWDKHDNTGGSYGGTYRFK 74

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 75  KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 134

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPDA K  D++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 135 EDTTPDNGRLPDADKDADYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGAA 194

Query: 768 PTVLT-DYYFRLL 803
             V T ++Y  LL
Sbjct: 195 NNVFTNEFYLNLL 207



>pdb|1CCK|    Altering Substrate Specificity Of Cytochrome C Peroxidase Towards
           A Small Molecular Substrate Peroxidase By Substituting
           Tyrosine For Phe 202
          Length = 291

 Score =  188 bits (473), Expect = 6e-47
 Identities = 99/191 (51%), Positives = 121/191 (62%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD Y  YGPVLVRLAWH SGT+DK   TGGS G T RF 
Sbjct: 12  SYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWDKHDNTGGSYGGTYRFK 71

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 72  KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 131

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPDA K   ++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 132 EDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGAA 191

Query: 768 PTVLT-DYYFRLL 803
             V T +YY  LL
Sbjct: 192 NNVFTNEYYLNLL 204



>pdb|1CYF|    Mol_id: 1; Molecule: Cytochrome C Peroxidase; Chain: Null; Ec:
           1.11.1.5; Engineered: Yes; Mutation: Ins(Met Ile At
           N-Terminus), C128a, A193c
          Length = 296

 Score =  187 bits (471), Expect = 1e-46
 Identities = 98/191 (51%), Positives = 121/191 (63%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD Y  YGPVLVRLAWH SGT+DK   TGGS G T RF 
Sbjct: 17  SYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWDKHDNTGGSYGGTYRFK 76

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 77  KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRAGRVDTP 136

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPDA K   ++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 137 EDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGCA 196

Query: 768 PTVLT-DYYFRLL 803
             V T ++Y  LL
Sbjct: 197 NNVFTNEFYLNLL 209



>pdb|3CCP|    Yeast Cytochrome c Peroxidase (E.C.1.11.1.5) Mutant With Trp 191
           Replaced By Phe (W191F)
 pdb|1DCC|   Cytochrome C Peroxidase (E.C.1.11.1.5) Mutant With Met Ile Added
           At N-Terminus And Trp 191 Replaced By Phe (Mi,W191f)
           Complexed With Dioxygen
          Length = 296

 Score =  187 bits (471), Expect = 1e-46
 Identities = 98/191 (51%), Positives = 121/191 (63%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD Y  YGPVLVRLAWH SGT+DK   TGGS G T RF 
Sbjct: 17  SYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWDKHDNTGGSYGGTYRFK 76

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 77  KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 136

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPDA K   ++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 137 EDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPFGAA 196

Query: 768 PTVLT-DYYFRLL 803
             V T ++Y  LL
Sbjct: 197 NNVFTNEFYLNLL 209



>pdb|1A2F|    Probing The Strength And Character Of An Asp-His-X Hydrogen Bond
           By Introducing Buried Charges
          Length = 291

 Score =  187 bits (470), Expect = 1e-46
 Identities = 98/191 (51%), Positives = 121/191 (63%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD Y  YGPVLVRLAWH SGT+DK   TGGS G T RF 
Sbjct: 12  SYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWDKHDNTGGSYGGTYRFK 71

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 72  KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 131

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPDA K   ++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 132 EDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALKGAHALGKTHLKNSGYEGPWGAA 191

Query: 768 PTVLT-DYYFRLL 803
             V T ++Y  LL
Sbjct: 192 NNVFTNEFYLNLL 204



>pdb|1BES|    Interaction Between Proximal And Distals Regions Of Cytochrome C
           Peroxidase
 pdb|1BEQ|   Interaction Between Proximal And Distals Regions Of Cytochrome C
           Peroxidase
          Length = 291

 Score =  187 bits (470), Expect = 1e-46
 Identities = 98/191 (51%), Positives = 121/191 (63%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD Y  YGPVLVRLAWH SGT+DK   TGGS G T RF 
Sbjct: 12  SYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWDKHDNTGGSYGGTYRFK 71

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 72  KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 131

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPDA K   ++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 132 EDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPYGAA 191

Query: 768 PTVLT-DYYFRLL 803
             V T ++Y  LL
Sbjct: 192 NNVFTNEFYLNLL 204



>pdb|2CEP|    Cytochrome C Peroxidase (E.C.1.11.1.5) Mutant With Met Ile Added
           At N-Terminus And Met 230 Replaced By Ile (Mi,M230i)
          Length = 296

 Score =  187 bits (469), Expect = 2e-46
 Identities = 98/191 (51%), Positives = 121/191 (63%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD Y  YGPVLVRLAWH SGT+DK   TGGS G T RF 
Sbjct: 17  SYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWDKHDNTGGSYGGTYRFK 76

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 77  KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 136

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPDA K   ++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 137 EDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGAA 196

Query: 768 PTVLT-DYYFRLL 803
             V T ++Y  LL
Sbjct: 197 NNVFTNEFYLNLL 209



>pdb|2CCP|    Yeast Cytochrome c Peroxidase (E.C.1.11.1.5) Mutant With Asp 235
           Replaced By Asn (D235N)
          Length = 296

 Score =  187 bits (469), Expect = 2e-46
 Identities = 98/191 (51%), Positives = 121/191 (63%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD Y  YGPVLVRLAWH SGT+DK   TGGS G T RF 
Sbjct: 17  SYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWDKHDNTGGSYGGTYRFK 76

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 77  KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 136

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPDA K   ++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 137 EDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGAA 196

Query: 768 PTVLT-DYYFRLL 803
             V T ++Y  LL
Sbjct: 197 NNVFTNEFYLNLL 209



>pdb|1CPG|    Cytochrome C Peroxidase (E.C.1.11.1.5) Mutant With Met Ile Added
           At N-Terminus And Trp 191 Replaced By Gln (Mi,W191q)
          Length = 296

 Score =  187 bits (469), Expect = 2e-46
 Identities = 98/191 (51%), Positives = 121/191 (63%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD Y  YGPVLVRLAWH SGT+DK   TGGS G T RF 
Sbjct: 17  SYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWDKHDNTGGSYGGTYRFK 76

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 77  KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 136

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPDA K   ++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 137 EDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPQGAA 196

Query: 768 PTVLT-DYYFRLL 803
             V T ++Y  LL
Sbjct: 197 NNVFTNEFYLNLL 209



>pdb|2PCC|A Chain A, Yeast Cytochrome C Peroxidase (Ccp) Complex With Yeast
           Iso-1-Cytochrome C
 pdb|2PCC|C Chain C, Yeast Cytochrome C Peroxidase (Ccp) Complex With Yeast
           Iso-1-Cytochrome C
 pdb|2PCB|A Chain A, Yeast Cytochrome C Peroxidase (Ccp) Complex With Horse
           Heart Cytochrome C
 pdb|2PCB|C Chain C, Yeast Cytochrome C Peroxidase (Ccp) Complex With Horse
           Heart Cytochrome C
 pdb|1CCP|   Yeast Cytochrome c Peroxidase (E.C.1.11.1.5)
          Length = 296

 Score =  187 bits (469), Expect = 2e-46
 Identities = 98/191 (51%), Positives = 121/191 (63%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD Y  YGPVLVRLAWH SGT+DK   TGGS G T RF 
Sbjct: 17  SYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWDKHDNTGGSYGGTYRFK 76

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 77  KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 136

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPDA K   ++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 137 EDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGAA 196

Query: 768 PTVLT-DYYFRLL 803
             V T ++Y  LL
Sbjct: 197 NNVFTNEFYLNLL 209



>gb|AAA88709.1| (J01468) cytochrome c peroxidase [Saccharomyces cerevisiae]
          Length = 362

 Score =  187 bits (469), Expect = 2e-46
 Identities = 98/191 (51%), Positives = 121/191 (63%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD Y  YGPVLVRLAWH SGT+DK   TGGS G T RF 
Sbjct: 83  SYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWDKHDNTGGSYGGTYRFK 142

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 143 KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 202

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPDA K   ++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 203 EDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGAA 262

Query: 768 PTVLT-DYYFRLL 803
             V T ++Y  LL
Sbjct: 263 NNVFTNEFYLNLL 275



>pdb|1BEM|    Interaction Between Proximal And Distals Regions Of Cytochrome C
           Peroxidase
          Length = 291

 Score =  187 bits (469), Expect = 2e-46
 Identities = 98/191 (51%), Positives = 121/191 (63%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD Y  YGPVLVRLAWH SGT+DK   TGGS G T RF 
Sbjct: 12  SYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWDKHDNTGGSYGGTYRFK 71

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 72  KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 131

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPDA K   ++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 132 EDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPQGAA 191

Query: 768 PTVLT-DYYFRLL 803
             V T ++Y  LL
Sbjct: 192 NNVFTNEFYLNLL 204



>pdb|1A2G|    Probing The Strength And Character Of An Asp-His-X Hydrogen Bond
           By Introducing Buried Charges
          Length = 291

 Score =  187 bits (469), Expect = 2e-46
 Identities = 98/191 (51%), Positives = 121/191 (63%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD Y  YGPVLVRLAWH SGT+DK   TGGS G T RF 
Sbjct: 12  SYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWDKHDNTGGSYGGTYRFK 71

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 72  KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 131

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPDA K   ++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 132 EDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGAA 191

Query: 768 PTVLT-DYYFRLL 803
             V T ++Y  LL
Sbjct: 192 NNVFTNEFYLNLL 204



>pdb|1BEP|    Effect Of Unnatural Heme Substitution On Kinetics Of Electron
           Transfer In Cytochrome C Peroxidase
 pdb|1BJ9|   Effect Of Unnatural Heme Substitution On Kinetics Of Electron
           Transfer In Cytochrome C Peroxidase
          Length = 291

 Score =  187 bits (469), Expect = 2e-46
 Identities = 98/191 (51%), Positives = 121/191 (63%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD Y  YGPVLVRLAWH SGT+DK   TGGS G T RF 
Sbjct: 12  SYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWDKHDNTGGSYGGTYRFK 71

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 72  KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 131

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPDA K   ++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 132 EDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGAA 191

Query: 768 PTVLT-DYYFRLL 803
             V T ++Y  LL
Sbjct: 192 NNVFTNEFYLNLL 204



>pdb|1CCA|    Cytochrome C Peroxidase (Ccp-Mkt) (E.C.1.11.1.5) Wild Type
          Length = 297

 Score =  187 bits (469), Expect = 2e-46
 Identities = 98/191 (51%), Positives = 121/191 (63%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD Y  YGPVLVRLAWH SGT+DK   TGGS G T RF 
Sbjct: 18  SYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWDKHDNTGGSYGGTYRFK 77

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 78  KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 137

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPDA K   ++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 138 EDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGAA 197

Query: 768 PTVLT-DYYFRLL 803
             V T ++Y  LL
Sbjct: 198 NNVFTNEFYLNLL 210



>pdb|1CCC|    Cytochrome C Peroxidase (Ccp-Mkt) (E.C.1.11.1.5) Mutant With Asp
           235 Replaced By Ala (D235a)
          Length = 297

 Score =  187 bits (469), Expect = 2e-46
 Identities = 98/191 (51%), Positives = 121/191 (63%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD Y  YGPVLVRLAWH SGT+DK   TGGS G T RF 
Sbjct: 18  SYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWDKHDNTGGSYGGTYRFK 77

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 78  KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 137

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPDA K   ++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 138 EDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGAA 197

Query: 768 PTVLT-DYYFRLL 803
             V T ++Y  LL
Sbjct: 198 NNVFTNEFYLNLL 210



>pdb|1CCB|    Cytochrome C Peroxidase (Ccp-Mkt) (E.C.1.11.1.5) Mutant With Asp
           235 Replaced By Glu (D235e)
          Length = 297

 Score =  187 bits (469), Expect = 2e-46
 Identities = 98/191 (51%), Positives = 121/191 (63%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD Y  YGPVLVRLAWH SGT+DK   TGGS G T RF 
Sbjct: 18  SYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWDKHDNTGGSYGGTYRFK 77

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 78  KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 137

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPDA K   ++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 138 EDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGAA 197

Query: 768 PTVLT-DYYFRLL 803
             V T ++Y  LL
Sbjct: 198 NNVFTNEFYLNLL 210



>pdb|1CPE|    Cytochrome C Peroxidase (E.C.1.11.1.5) Mutant With Met Ile Added
           At N-Terminus And Trp 191 Replaced By Gly (Mi,W191g)
           Complexed With A Potassium Ion (K+)
 pdb|1CPD|   Cytochrome C Peroxidase (E.C.1.11.1.5) Mutant With Met Ile Added
           At N-Terminus And Trp 191 Replaced By Gly (Mi,W191g)
           Complexed With An Ammonium Ion (Nh4+)
 pdb|1CPF|   Cytochrome C Peroxidase (E.C.1.11.1.5) Mutant With Met Ile Added
           At N-Terminus And Trp 191 Replaced By Gly (Mi,W191g)
           Complexed With A Tris (+) Ion
          Length = 296

 Score =  186 bits (467), Expect = 3e-46
 Identities = 98/191 (51%), Positives = 121/191 (63%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD Y  YGPVLVRLAWH SGT+DK   TGGS G T RF 
Sbjct: 17  SYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWDKHDNTGGSYGGTYRFK 76

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 77  KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 136

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPDA K   ++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 137 EDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPGGAA 196

Query: 768 PTVLT-DYYFRLL 803
             V T ++Y  LL
Sbjct: 197 NNVFTNEFYLNLL 209



>pdb|1AC4|    Variation In The Strength Of A Ch To O Hydrogen Bond In An
           Artificial Protein Cavity (2,3,4-Trimethyl-1,3-Thiazole)
 pdb|1AC8|   Variation In The Strength Of A Ch To O Hydrogen Bond In An
           Artificial Protein Cavity (3,4,5-Trimethylthiazole)
 pdb|1AEB|   Specificity Of Ligand Binding To A Buried Polar Cavity At The
           Active Site Of Cytochrome C Peroxidase
           (3-Methylthiazole)
 pdb|1AED|   Specificity Of Ligand Binding To A Buried Polar Cavity At The
           Active Site Of Cytochrome C Peroxidase
           (3,4-Dimethylthiazole)
 pdb|1AEE|   Specificity Of Ligand Binding To A Buried Polar Cavity At The
           Active Site Of Cytochrome C Peroxidase (Aniline)
 pdb|1AEF|   Specificity Of Ligand Binding To A Buried Polar Cavity At The
           Active Site Of Cytochrome C Peroxidase (3-Aminopyridine)
 pdb|1AEG|   Specificity Of Ligand Binding To A Buried Polar Cavity At The
           Active Site Of Cytochrome C Peroxidase (4-Aminopyridine)
 pdb|1AEH|   Specificity Of Ligand Binding To A Buried Polar Cavity At The
           Active Site Of Cytochrome C Peroxidase
           (2-Amino-4-Methylthiazole)
 pdb|1AEJ|   Specificity Of Ligand Binding To A Buried Polar Cavity At The
           Active Site Of Cytochrome C Peroxidase
           (1-Vinylimidazole)
 pdb|1AEK|   Specificity Of Ligand Binding To A Buried Polar Cavity At The
           Active Site Of Cytochrome C Peroxidase (Indoline)
 pdb|1AEM|   Specificity Of Ligand Binding To A Buried Polar Cavity At The
           Active Site Of Cytochrome C Peroxidase
           (Imidazo[1,2-A]pyridine)
 pdb|1AEN|   Specificity Of Ligand Binding To A Buried Polar Cavity At The
           Active Site Of Cytochrome C Peroxidase
           (2-Amino-5-Methylthiazole)
 pdb|1AEO|   Specificity Of Ligand Binding To A Buried Polar Cavity At The
           Active Site Of Cytochrome C Peroxidase (2-Aminopyridine)
 pdb|1AEQ|   Variation In The Strength Of A Ch To O Hydrogen Bond In An
           Artificial Protein Cavity (2-Ethylimidazole)
 pdb|1AES|   Specificity Of Ligand Binding To A Buried Polar Cavity At The
           Active Site Of Cytochrome C Peroxidase (Imidazole)
 pdb|1AET|   Variation In The Strength Of A Ch To O Hydrogen Bond In An
           Artificial Protein Cavity (1-Methylimidazole)
 pdb|1AEU|   Specificity Of Ligand Binding In A Polar Cavity Of Cytochrome C
           Peroxidase (2-Methylimidazole)
 pdb|1AEV|   Introduction Of Novel Substrate Oxidation Into Cytochrome C
           Peroxidase By Cavity Complementation: Oxidation Of
           2-Aminothiazole And Covalent Modification Of The Enzyme
           (2-Aminothiazole)
          Length = 294

 Score =  186 bits (467), Expect = 3e-46
 Identities = 98/191 (51%), Positives = 121/191 (63%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD Y  YGPVLVRLAWH SGT+DK   TGGS G T RF 
Sbjct: 15  SYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWDKHDNTGGSYGGTYRFK 74

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 75  KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 134

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPDA K   ++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 135 EDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPGGAA 194

Query: 768 PTVLT-DYYFRLL 803
             V T ++Y  LL
Sbjct: 195 NNVFTNEFYLNLL 207



>pdb|1CMU|    Cytochrome C Peroxidase (Ccp-Mkt) (E.C.1.11.1.5) Mutant With
           Initial Met, Lys, Thr And With Trp 191 Replaced By Gly
           And Asp 235 Replaced By Asn (Ins(M1,K2,T3),W191g,D235n)
           And Soaked In 40 Millimolar Potassium (K+)
          Length = 294

 Score =  186 bits (467), Expect = 3e-46
 Identities = 98/191 (51%), Positives = 121/191 (63%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD Y  YGPVLVRLAWH SGT+DK   TGGS G T RF 
Sbjct: 15  SYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWDKHDNTGGSYGGTYRFK 74

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 75  KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 134

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPDA K   ++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 135 EDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPGGAA 194

Query: 768 PTVLT-DYYFRLL 803
             V T ++Y  LL
Sbjct: 195 NNVFTNEFYLNLL 207



>pdb|1AA4|    Specificity Of Ligand Binding In A Buried Polar Cavity Of
           Cytochrome C Peroxidase
 pdb|1RYC|   Cytochrome C Peroxidase W191g From Saccharomyces Cerevisiae
 pdb|1CMP|   Cytochrome C Peroxidase (Recombinant Yeast, Ccp-Mkt)
           (E.C.1.11.1.5) Mutant With Trp 191 Replaced By Gly
           (W191g) Complexed With 1,2-Dimethylimadazole
 pdb|1CMT|   Cytochrome C Peroxidase (Ccp-Mkt) (E.C.1.11.1.5) Mutant With
           Initial Met, Lys, Thr And With Trp 191 Replaced By Gly
           (Ins(M1,K2,T3),W191g) And Soaked In 40 Millimolar
           Potassium (K+)
 pdb|1CMQ|   Cytochrome C Peroxidase (Recombinant Yeast, Ccp-Mkt)
           (E.C.1.11.1.5) Mutant With Trp 191 Replaced By Gly
           (W191g)
          Length = 294

 Score =  186 bits (467), Expect = 3e-46
 Identities = 98/191 (51%), Positives = 121/191 (63%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD Y  YGPVLVRLAWH SGT+DK   TGGS G T RF 
Sbjct: 15  SYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWDKHDNTGGSYGGTYRFK 74

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 75  KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 134

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPDA K   ++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 135 EDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPGGAA 194

Query: 768 PTVLT-DYYFRLL 803
             V T ++Y  LL
Sbjct: 195 NNVFTNEFYLNLL 207



>pdb|1BEJ|    Interaction Between Proximal And Distals Regions Of Cytochrome C
           Peroxidase
          Length = 291

 Score =  186 bits (467), Expect = 3e-46
 Identities = 98/191 (51%), Positives = 121/191 (63%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD Y  YGPVLVRLAWH SGT+DK   TGGS G T RF 
Sbjct: 12  SYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWDKHDNTGGSYGGTYRFK 71

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 72  KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 131

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPDA K   ++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 132 EDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPGGAA 191

Query: 768 PTVLT-DYYFRLL 803
             V T ++Y  LL
Sbjct: 192 NNVFTNEFYLNLL 204



>pdb|6CCP|    Cytochrome C Peroxidase (E.C.1.11.1.5) Mutant With Met Ile Added
           At N-Terminus And Arg 48 Replaced By Lys (Mi,R48k)
          Length = 296

 Score =  185 bits (466), Expect = 4e-46
 Identities = 97/191 (50%), Positives = 121/191 (62%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD Y  YGPVLV+LAWH SGT+DK   TGGS G T RF 
Sbjct: 17  SYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVKLAWHISGTWDKHDNTGGSYGGTYRFK 76

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 77  KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 136

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPDA K   ++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 137 EDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGAA 196

Query: 768 PTVLT-DYYFRLL 803
             V T ++Y  LL
Sbjct: 197 NNVFTNEFYLNLL 209



>pdb|4CCX|    Cytochrome C Peroxidase (E.C.1.11.1.5) (Ccp-Mkt) Mutant With
           Met-Lys-Thr Inserted At The N-Terminus, Thr 53 Replaced
           By Ile, Ala 147 Replaced By Met, Asp 152 Replaced By Gly
           (Ins(M1,K2,T3),T53i,A147m,D152g)
          Length = 294

 Score =  185 bits (464), Expect = 7e-46
 Identities = 97/191 (50%), Positives = 120/191 (62%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD Y  YGPVLVRLAWH SGT+DK   TGGS G T RF 
Sbjct: 15  SYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWDKHDNTGGSYGGTYRFK 74

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 75  KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 134

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPD  K   ++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 135 EDTTPDNGRLPDMDKDAGYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGAA 194

Query: 768 PTVLT-DYYFRLL 803
             V T ++Y  LL
Sbjct: 195 NNVFTNEFYLNLL 207



>pdb|1CCL|    Probing The Strength And Character Of An Asp-His-X Hydrogen Bond
           By Introducing Buried Charges
          Length = 291

 Score =  185 bits (464), Expect = 7e-46
 Identities = 98/191 (51%), Positives = 120/191 (62%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD Y  YGPVLVRLAWH SGT+DK   TGGS G T RF 
Sbjct: 12  SYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWDKHDNTGGSYGGTYRFK 71

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 72  KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 131

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPDA K   ++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 132 EDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGAA 191

Query: 768 PTVLT-DYYFRLL 803
             V T + Y  LL
Sbjct: 192 NNVFTNEKYLNLL 204



>pdb|1BEK|    Effect Of Unnatural Heme Substitution On Kinetics Of Electron
           Transfer In Cytochrome C Peroxidase
          Length = 291

 Score =  185 bits (464), Expect = 7e-46
 Identities = 97/191 (50%), Positives = 120/191 (62%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYDYG-SYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD    YGPVLVRLAWH SGT+DK   TGGS G T RF 
Sbjct: 12  SYEDFQKVYNAIALKLREDDEYDNAIGYGPVLVRLAWHISGTWDKHDNTGGSYGGTYRFK 71

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 72  KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 131

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPDA K   ++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 132 EDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGAA 191

Query: 768 PTVLT-DYYFRLL 803
             V T ++Y  LL
Sbjct: 192 NNVFTNEFYLNLL 204



>pdb|3CCX|    Cytochrome C Peroxidase (E.C.1.11.1.5) (Ccp-Mkt) Mutant With
           Met-Lys-Thr Inserted At The N-Terminus, Thr 52 Replaced
           By Ile, Ala 147 Replaced By Tyr, Asp 152 Replaced By Gly
           (Ins(M1,K2,T3),T52i,A147y,D152g)
          Length = 294

 Score =  184 bits (463), Expect = 9e-46
 Identities = 97/191 (50%), Positives = 120/191 (62%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD Y  YGPVLVRLAWH SGT+DK   TGGS G T RF 
Sbjct: 15  SYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWDKHDNTGGSYGGTYRFK 74

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 75  KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 134

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPD  K   ++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 135 EDTTPDNGRLPDYDKDAGYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGAA 194

Query: 768 PTVLT-DYYFRLL 803
             V T ++Y  LL
Sbjct: 195 NNVFTNEFYLNLL 207



>pdb|1CCJ|    Conformer Selection By Ligand Binding Observed With Protein
           Crystallography
 pdb|1CCI|   How Flexible Are Proteins? Trapping Of A Flexible Loop
          Length = 294

 Score =  184 bits (463), Expect = 9e-46
 Identities = 98/191 (51%), Positives = 120/191 (62%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD Y  YGPVLVRLAWH SGT+DK   TGGS G T RF 
Sbjct: 15  SYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWDKHDNTGGSYGGTYRFK 74

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 75  KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 134

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPDA K   ++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 135 EDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGAA 194

Query: 768 PTVLT-DYYFRLL 803
             V T + Y  LL
Sbjct: 195 NNVFTNEGYLNLL 207



>pdb|1DJ5|A Chain A, Crystal Structure Of R48a Mutant Of Cytochrome C
           Peroxidase With N-Hydroxyguanidine Bound
 pdb|1DJ1|A Chain A, Crystal Structure Of R48a Mutant Of Cytochrome C
           Peroxidase
          Length = 291

 Score =  184 bits (463), Expect = 9e-46
 Identities = 97/191 (50%), Positives = 120/191 (62%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD Y  YGPVLV LAWH SGT+DK   TGGS G T RF 
Sbjct: 12  SYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVALAWHISGTWDKHDNTGGSYGGTYRFK 71

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 72  KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 131

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPDA K   ++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 132 EDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGAA 191

Query: 768 PTVLT-DYYFRLL 803
             V T ++Y  LL
Sbjct: 192 NNVFTNEFYLNLL 204



>pdb|7CCP|    Cytochrome C Peroxidase (E.C.1.11.1.5) Mutant With Met Ile Added
           At N-Terminus And Arg 48 Replaced By Leu (Mi,R48l)
          Length = 296

 Score =  184 bits (462), Expect = 1e-45
 Identities = 97/191 (50%), Positives = 120/191 (62%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD Y  YGPVLV LAWH SGT+DK   TGGS G T RF 
Sbjct: 17  SYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVLLAWHISGTWDKHDNTGGSYGGTYRFK 76

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 77  KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 136

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPDA K   ++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 137 EDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGAA 196

Query: 768 PTVLT-DYYFRLL 803
             V T ++Y  LL
Sbjct: 197 NNVFTNEFYLNLL 209



>pdb|4CCP|    Yeast Cytochrome c Peroxidase (E.C.1.11.1.5) Mutant With Trp 51
           Replaced By Phe (W51F)
          Length = 293

 Score =  183 bits (459), Expect = 3e-45
 Identities = 97/191 (50%), Positives = 121/191 (62%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD Y  YGPVLVRLA+H SGT+DK   TGGS G T RF 
Sbjct: 14  SYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAFHISGTWDKHDNTGGSYGGTYRFK 73

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 74  KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 133

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPDA K   ++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 134 EDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGAA 193

Query: 768 PTVLT-DYYFRLL 803
             V T ++Y  LL
Sbjct: 194 NNVFTNEFYLNLL 206



>pdb|1CCG|    Cytochrome C Peroxidase (E.C.1.11.1.5) (Ccp-Mkt) Mutant With His
           175 Replaced By Gly (H175g) Complexed With Imidazole
 pdb|1CCE|   Cytochrome C Peroxidase (E.C.1.11.1.5) (Ccp-Mkt) Mutant With His
           175 Replaced By Gly (H175g)
          Length = 291

 Score =  183 bits (459), Expect = 3e-45
 Identities = 97/191 (50%), Positives = 120/191 (62%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD Y  YGPVLVRLAWH SGT+DK   TGGS G T RF 
Sbjct: 12  SYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWDKHDNTGGSYGGTYRFK 71

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 72  KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 131

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPDA K   ++R  F R+  ND+E+VAL  A ALG+ H   S Y G     
Sbjct: 132 EDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAGALGKTHLKNSGYEGPWGAA 191

Query: 768 PTVLT-DYYFRLL 803
             V T ++Y  LL
Sbjct: 192 NNVFTNEFYLNLL 204



>pdb|5CCP|    Cytochrome C Peroxidase (E.C.1.11.1.5) Mutant With Met Ile Added
           At N-Terminus And His 52 Replaced By Leu (Mi,H52l)
          Length = 296

 Score =  182 bits (458), Expect = 3e-45
 Identities = 97/191 (50%), Positives = 120/191 (62%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+YD Y  YGPVLVRLAW  SGT+DK   TGGS G T RF 
Sbjct: 17  SYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWLISGTWDKHDNTGGSYGGTYRFK 76

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 77  KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 136

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPDA K   ++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 137 EDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGAA 196

Query: 768 PTVLT-DYYFRLL 803
             V T ++Y  LL
Sbjct: 197 NNVFTNEFYLNLL 209



>pdb|1BVA|A Chain A, Manganese Binding Mutant In Cytochrome C Peroxidase
          Length = 294

 Score =  179 bits (450), Expect = 3e-44
 Identities = 95/191 (49%), Positives = 119/191 (61%), Gaps = 2/191 (1%)
 Frame = +3

Query: 231 SKEDYQKVDNEIAARLEEKDDYD-YGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFA 407
           S ED+QKV N IA +L E D+Y+ Y  YG  LVRLAWH SGT+DK   TGGS G T RF 
Sbjct: 15  SYEDFQKVYNAIALKLREDDEYENYIGYGDDLVRLAWHISGTWDKHDNTGGSYGGTYRFK 74

Query: 408 PESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRD 587
            E +  +NAGL     FL+P+ ++FPWI+  DL+ L GV A+QEM GP IP+R GR D  
Sbjct: 75  KEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTP 134

Query: 588 VSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELL 767
                 +GRLPDA K   ++R  F R+  ND+E+VAL  AHALG+ H   S Y G     
Sbjct: 135 EDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGAA 194

Query: 768 PTVLT-DYYFRLL 803
             V T ++Y  LL
Sbjct: 195 NNVFTNEFYLNLL 207



>gb|AAC08576.1| (AF053474) cytosolic ascorbate peroxidase [Zantedeschia aethiopica]
          Length = 250

 Score =  166 bits (417), Expect = 2e-40
 Identities = 91/196 (46%), Positives = 123/196 (62%), Gaps = 5/196 (2%)
 Frame = +3

Query: 216 KVFNPSKEDYQ----KVDNEIAARLEEKDDYDYGSYGPVLVRLAWHASGTYDKETGTGGS 383
           K +    E+YQ    K   ++ A + EK+        P+++RLAWH++GTYD  T TGG 
Sbjct: 3   KSYPAVSEEYQTAVGKAKRKLRALIAEKN------CAPLMLRLAWHSAGTYDVSTRTGGP 56

Query: 384 NGATMRFAPESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPY 563
            G TMRF  E  HGAN G+  A   L+P+KE+FP ++Y+D + LAGV A++   GP IP+
Sbjct: 57  FG-TMRFQAELAHGANNGIDIAVRLLEPIKEQFPILSYADFYQLAGVVAVEVTGGPEIPF 115

Query: 564 RPGRSDRDVSGCTPHGRLPDASKRQDHLRXIFG-RMGFNDQEIVALSCAHALGRCHTDRS 740
            PGR D+        GRLPDA+K  DHLR +F  +MG NDQ+IVALS AH LGRCH +RS
Sbjct: 116 HPGREDKPAP--PVEGRLPDATKGSDHLRQVFSQQMGLNDQDIVALSGAHTLGRCHKERS 173

Query: 741 SYSGTLELLPTVLTDYYFRLL 803
            + G     P +  + YF+ L
Sbjct: 174 GFEGAWTTNPLIFDNSYFKEL 194



>pir||S20866 L-ascorbate peroxidase (EC 1.11.1.11) precursor - Arabidopsis
           thaliana (fragment)
          Length = 263

 Score =  163 bits (408), Expect = 3e-39
 Identities = 90/204 (44%), Positives = 126/204 (61%), Gaps = 5/204 (2%)
 Frame = +3

Query: 192 NSASSATAKVFNPSKEDYQKVDNEIAARLE----EKDDYDYGSYGPVLVRLAWHASGTYD 359
           N + +   K +    EDY+K   +   +L     EK+        P++VRLAWH++GT+D
Sbjct: 8   NKSLAKMTKNYPTVSEDYKKAVEKCRRKLRGLIAEKN------CAPIMVRLAWHSAGTFD 61

Query: 360 KETGTGGSNGATMRFAPESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQE 539
            ++ TGG  G TMRF  E  HGAN+G+  A   L P++E+FP I+++D   LAGV A++ 
Sbjct: 62  CQSRTGGPFG-TMRFDAEQAHGANSGIHIALRLLDPIREQFPTISFADFHQLAGVVAVEV 120

Query: 540 MLGPAIPYRPGRSDRDVSGCTPHGRLPDASKRQDHLRXIFGR-MGFNDQEIVALSCAHAL 716
             GP IP+ PGR D+      P GRLPDA+K  DHLR +F + MG +D++IVALS AH L
Sbjct: 121 TGGPDIPFHPGREDKPQP--PPEGRLPDATKGCDHLRDVFAKQMGLSDKDIVALSGAHTL 178

Query: 717 GRCHTDRSSYSGTLELLPTVLTDYYFRLL 803
           GRCH DRS + G     P +  + YF+ L
Sbjct: 179 GRCHKDRSGFEGAWTSNPLIFDNSYFKEL 207



>sp|Q05431|APX1_ARATH L-ASCORBATE PEROXIDASE, CYTOSOLIC (AP)
 pir||S28856 L-ascorbate peroxidase (EC 1.11.1.11), cytosolic - Arabidopsis
           thaliana
 emb|CAA42168.1| (X59600) L-ascorbate peroxidase [Arabidopsis thaliana]
 dbj|BAA03334.1| (D14442) ascorbate peroxidase [Arabidopsis thaliana]
 gb|AAB07880.1| (U63815) ascorbate peroxidase [Arabidopsis thaliana]
 gb|AAF75066.1|AC007583_2 (AC007583) Strong similarity to L-ascorbate peroxidase from
           Arabidopsis thaliana gi|728873.  ESTs gb|T04087,
           gb|H37385,gb|H36515 and gb|R90494 come from this gene.
          Length = 250

 Score =  161 bits (404), Expect = 7e-39
 Identities = 88/189 (46%), Positives = 121/189 (63%), Gaps = 5/189 (2%)
 Frame = +3

Query: 237 EDYQKVDNEIAARLE----EKDDYDYGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRF 404
           EDY+K   +   +L     EK+        P++VRLAWH++GT+D ++ TGG  G TMRF
Sbjct: 10  EDYKKAVEKCRRKLRGLIAEKN------CAPIMVRLAWHSAGTFDCQSRTGGPFG-TMRF 62

Query: 405 APESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDR 584
             E  HGAN+G+  A   L P++E+FP I+++D   LAGV A++   GP IP+ PGR D+
Sbjct: 63  DAEQAHGANSGIHIALRLLDPIREQFPTISFADFHQLAGVVAVEVTGGPDIPFHPGREDK 122

Query: 585 DVSGCTPHGRLPDASKRQDHLRXIFGR-MGFNDQEIVALSCAHALGRCHTDRSSYSGTLE 761
                 P GRLPDA+K  DHLR +F + MG +D++IVALS AH LGRCH DRS + G   
Sbjct: 123 PQP--PPEGRLPDATKGCDHLRDVFAKQMGLSDKDIVALSGAHTLGRCHKDRSGFEGAWT 180

Query: 762 LLPTVLTDYYFRLL 803
             P +  + YF+ L
Sbjct: 181 SNPLIFDNSYFKEL 194



>pir||T03595 probable L-ascorbate peroxidase (EC 1.11.1.11) - rice
 dbj|BAA08264.1| (D45423) ascorbate peroxidase [Oryza sativa]
          Length = 250

 Score =  160 bits (401), Expect = 2e-38
 Identities = 85/187 (45%), Positives = 117/187 (62%), Gaps = 1/187 (0%)
 Frame = +3

Query: 234 KEDYQKVDNEIAARLEEKDDYDYGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFAPE 413
           +E  +K   ++ A + EK      S  P+++RLAWH++GT+D  + TGG  G TM+   E
Sbjct: 13  QEAVEKARQKLRALIAEK------SCAPLMLRLAWHSAGTFDVSSKTGGPFG-TMKTPAE 65

Query: 414 SDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRDVS 593
             H ANAGL  A   L+P+KE+ P I+Y+D + LAGV A++   GPA+P+ PGR D+   
Sbjct: 66  LSHAANAGLDIAVRMLEPIKEEIPTISYADFYQLAGVVAVEVSGGPAVPFHPGREDKPAP 125

Query: 594 GCTPHGRLPDASKRQDHLRXIFG-RMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELLP 770
              P GRLPDA+K  DHLR +FG +MG +DQ+IVALS  H LGRCH +RS + G     P
Sbjct: 126 --PPEGRLPDATKGSDHLRQVFGAQMGLSDQDIVALSGGHTLGRCHKERSGFEGPWTRNP 183

Query: 771 TVLTDYYF 794
               + YF
Sbjct: 184 LQFDNSYF 191



>pir||S43157 L-ascorbate peroxidase (EC 1.11.1.11) - radish
 emb|CAA55209.1| (X78452) L-ascorbate peroxidase [Raphanus sativus]
          Length = 250

 Score =  160 bits (400), Expect = 2e-38
 Identities = 86/190 (45%), Positives = 119/190 (62%), Gaps = 1/190 (0%)
 Frame = +3

Query: 234 KEDYQKVDNEIAARLEEKDDYDYGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFAPE 413
           +++ +K   ++   + EK+        P++VRLAWH++GT+D  + TGG  G TMRF  E
Sbjct: 13  QKEIEKCKRKLRGLIAEKN------CAPIMVRLAWHSAGTFDCASRTGGPFG-TMRFDDE 65

Query: 414 SDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRDVS 593
             HGAN GL  A   L+P++E+FP I+++D   LAGV A++   GP IP+ PGR D+   
Sbjct: 66  LAHGANNGLHIALRLLEPIREQFPTISHADFHQLAGVVAVEVTGGPEIPFHPGREDKPQP 125

Query: 594 GCTPHGRLPDASKRQDHLRXIF-GRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLELLP 770
              P GRLPDA+K  DHLR +F  +MG  DQ+IVALS AH LGRCH DRS + G     P
Sbjct: 126 --PPEGRLPDATKACDHLRQVFLKQMGLTDQDIVALSGAHTLGRCHKDRSGFEGAWTSNP 183

Query: 771 TVLTDYYFRLL 803
            +  + YF+ L
Sbjct: 184 LIFDNSYFKEL 194



>pir||S49914 L-ascorbate peroxidase (EC 1.11.1.11), cytosolic isozyme - maize
 emb|CAA84406.1| (Z34934) cytosolic ascorbate peroxidase [Zea mays]
 prf||2111423A ascorbate peroxidase [Zea mays]
          Length = 250

 Score =  159 bits (398), Expect = 4e-38
 Identities = 88/196 (44%), Positives = 121/196 (60%), Gaps = 5/196 (2%)
 Frame = +3

Query: 216 KVFNPSKEDYQKVDNEIAARLE----EKDDYDYGSYGPVLVRLAWHASGTYDKETGTGGS 383
           K +    EDY K  ++   +L     EK+        P+++RLAWH+ GT+D  T TGG 
Sbjct: 3   KAYPTVNEDYLKAVDKAKRKLRGLIAEKN------CAPLMLRLAWHSVGTFDVVTKTGGP 56

Query: 384 NGATMRFAPESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPY 563
            G TM+   E  HGANAGL  A   L+P+KE+FP ++Y+D + LAGV A++   GP +P+
Sbjct: 57  FG-TMKNPVEQAHGANAGLEIAIRLLEPIKEQFPILSYADFYQLAGVVAVEVTGGPDVPF 115

Query: 564 RPGRSDRDVSGCTPHGRLPDASKRQDHLRXIFG-RMGFNDQEIVALSCAHALGRCHTDRS 740
            PGR D+      P GRLPDA++  DHLR +F  +MG +DQ+IVALS  H LGRCH DRS
Sbjct: 116 HPGRQDKPEP--PPEGRLPDATQGSDHLRQVFSTQMGLSDQDIVALSGGHTLGRCHKDRS 173

Query: 741 SYSGTLELLPTVLTDYYFRLL 803
            + G     P +  + YF+ L
Sbjct: 174 GFEGAWTSNPLIFDNSYFKEL 194



>pir||T10189 L-ascorbate peroxidase (EC 1.11.1.11), cytosolic - cucumber
 dbj|BAA13671.1| (D88649) cytosolic ascorbate peroxidase [Cucumis sativus]
          Length = 249

 Score =  158 bits (396), Expect = 6e-38
 Identities = 86/193 (44%), Positives = 118/193 (60%), Gaps = 4/193 (2%)
 Frame = +3

Query: 216 KVFNPSKEDYQKVDNEIAARLE----EKDDYDYGSYGPVLVRLAWHASGTYDKETGTGGS 383
           K +    E+YQK   +   +L     EK+        P+++RLAWH++GT+ K++ TGG 
Sbjct: 3   KCYPVVSEEYQKAIEKAKRKLRGFIAEKN------CAPLMLRLAWHSAGTFCKDSKTGGP 56

Query: 384 NGATMRFAPESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPY 563
            G TMRF  E  HGAN GL  A   L+P+KE+FP ++Y+D + LAGV A++   GP +P+
Sbjct: 57  FG-TMRFKSELAHGANNGLDIAVRLLEPIKEQFPILSYADFYQLAGVVAVEVTGGPDVPF 115

Query: 564 RPGRSDRDVSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSS 743
            PGR D+      P GRLPDA+K  DHLR +F  MG +DQ+IVALS  H LGR H +RS 
Sbjct: 116 HPGREDKPEP--PPEGRLPDATKGSDHLRDVFYTMGLSDQDIVALSGGHTLGRAHKERSG 173

Query: 744 YSGTLELLPTVLTDYYF 794
           + G     P +    YF
Sbjct: 174 FEGPWTTNPLIFDKSYF 190



>pir||JE0232 L-ascorbate peroxidase (EC 1.11.1.11) - garden strawberry
 gb|AAB95222.1| (AF039953) cytosolic ascorbate peroxidase [Fragaria x ananassa]
 gb|AAD43336.1| (AF158652) cytosolic ascorbate peroxidase APX20 [Fragaria x
           ananassa]
          Length = 250

 Score =  158 bits (396), Expect = 6e-38
 Identities = 87/196 (44%), Positives = 123/196 (62%), Gaps = 5/196 (2%)
 Frame = +3

Query: 216 KVFNPSKEDYQKVDNEIAARLE----EKDDYDYGSYGPVLVRLAWHASGTYDKETGTGGS 383
           K +    E+Y+K  ++   +L     EK+        P+++RLAWH++GTYD +T TGG 
Sbjct: 3   KCYPTVSEEYKKAIDKAKRKLRGLIAEKN------CAPLMLRLAWHSAGTYDVKTKTGGP 56

Query: 384 NGATMRFAPESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPY 563
            G TM+ + E  HGAN GL  A   L+P+KE+FP ++Y+D + LAGV A++   GP +P+
Sbjct: 57  FG-TMKQSAELAHGANNGLDIAVRLLEPIKEQFPILSYADFYQLAGVVAVEVTGGPDVPF 115

Query: 564 RPGRSDRDVSGCTPHGRLPDASKRQDHLRXIFGR-MGFNDQEIVALSCAHALGRCHTDRS 740
            PGR D+      P GRLPDA K  DHLR +FG+ MG +DQ+IVALS  H LGR H +RS
Sbjct: 116 HPGREDKPEP--PPEGRLPDAGKGSDHLREVFGKTMGLSDQDIVALSGGHTLGRAHKERS 173

Query: 741 SYSGTLELLPTVLTDYYFRLL 803
            + G     P +  + YF +L
Sbjct: 174 GFEGPWTPNPLIFDNSYFTVL 194



>gb|AAD41404.1|AF159629_1 (AF159629) cytosolic ascorbate peroxidase [Fragaria x ananassa]
 gb|AAD41406.1|AF159631_1 (AF159631) cytosolic ascorbate peroxidase [Fragaria x ananassa]
 gb|AAD43337.1| (AF158653) cytosolic ascorbate peroxidase APX19 [Fragaria x
           ananassa]
          Length = 250

 Score =  158 bits (396), Expect = 6e-38
 Identities = 87/196 (44%), Positives = 123/196 (62%), Gaps = 5/196 (2%)
 Frame = +3

Query: 216 KVFNPSKEDYQKVDNEIAARLE----EKDDYDYGSYGPVLVRLAWHASGTYDKETGTGGS 383
           K +    E+Y+K  ++   +L     EK+        P+++RLAWH++GTYD +T TGG 
Sbjct: 3   KCYPTVSEEYKKAIDKAKRKLRGLIAEKN------CAPLMLRLAWHSAGTYDVKTKTGGP 56

Query: 384 NGATMRFAPESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPY 563
            G TM+ + E  HGAN GL  A   L+P+KE+FP ++Y+D + LAGV A++   GP +P+
Sbjct: 57  FG-TMKQSAELAHGANNGLDIAVRLLEPIKEQFPILSYADFYQLAGVVAVEVTGGPDVPF 115

Query: 564 RPGRSDRDVSGCTPHGRLPDASKRQDHLRXIFGR-MGFNDQEIVALSCAHALGRCHTDRS 740
            PGR D+      P GRLPDA K  DHLR +FG+ MG +DQ+IVALS  H LGR H +RS
Sbjct: 116 HPGREDKPEP--PPEGRLPDAGKGSDHLREVFGKTMGLSDQDIVALSGGHTLGRAHKERS 173

Query: 741 SYSGTLELLPTVLTDYYFRLL 803
            + G     P +  + YF +L
Sbjct: 174 GFEGPWTPNPLIFDNSYFTVL 194



>emb|CAA06996.1| (AJ006358) ascorbate peroxidase [Hordeum vulgare]
          Length = 250

 Score =  158 bits (396), Expect = 6e-38
 Identities = 85/186 (45%), Positives = 116/186 (61%), Gaps = 1/186 (0%)
 Frame = +3

Query: 237 EDYQKVDNEIAARLEEKDDYDYGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFAPES 416
           E  +K   ++ A + EK+        P+++RLAWH++GT+D  + TGG  G TM+   E 
Sbjct: 14  EAVEKARQKLRALIAEKN------CSPLMLRLAWHSAGTFDVSSKTGGPFG-TMKKPAEQ 66

Query: 417 DHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRDVSG 596
            H ANAGL  A   L+P+KE+ P I+Y+DL+ LAGV A++   GP IP+ PGR D+    
Sbjct: 67  AHAANAGLDIAVRMLEPIKEEIPTISYADLYQLAGVVAVEVSGGPVIPFHPGREDKPQP- 125

Query: 597 CTPHGRLPDASKRQDHLRXIFGR-MGFNDQEIVALSCAHALGRCHTDRSSYSGTLELLPT 773
             P GRLPDA+K  DHLR +FG+ MG +DQ+IVALS  H LGRCH +RS + G     P 
Sbjct: 126 -PPEGRLPDATKGSDHLRQVFGKQMGLSDQDIVALSGGHTLGRCHKERSGFEGPWTRNPL 184

Query: 774 VLTDYYF 794
              + YF
Sbjct: 185 KFDNSYF 191



>gb|AAD41407.1|AF159632_1 (AF159632) cytosolic ascorbate peroxidase [Fragaria x ananassa]
 gb|AAD41408.1|AF159633_1 (AF159633) cytosolic ascorbate peroxidase [Fragaria x ananassa]
 gb|AAD43338.1| (AF158654) cytosolic ascorbate peroxidase APX26 [Fragaria x
           ananassa]
          Length = 250

 Score =  158 bits (395), Expect = 9e-38
 Identities = 80/163 (49%), Positives = 109/163 (66%), Gaps = 1/163 (0%)
 Frame = +3

Query: 315 PVLVRLAWHASGTYDKETGTGGSNGATMRFAPESDHGANAGLAAARDFLQPVKEKFPWIT 494
           P+++RLAWH++GTYD +T TGG  G TM+ + E  HGAN GL  A   L+P+KE+FP ++
Sbjct: 34  PLMLRLAWHSAGTYDVKTKTGGPFG-TMKQSAELAHGANNGLDIAVRLLEPIKEQFPILS 92

Query: 495 YSDLWILAGVCAIQEMLGPAIPYRPGRSDRDVSGCTPHGRLPDASKRQDHLRXIFGR-MG 671
           Y+D + LAGV A++   GP +P+ PGR D+      P GRLPDA K  DHLR +FG+ MG
Sbjct: 93  YADFYQLAGVVAVEVTGGPDVPFHPGREDKPEP--PPEGRLPDAGKGSDHLREVFGKTMG 150

Query: 672 FNDQEIVALSCAHALGRCHTDRSSYSGTLELLPTVLTDYYFRLL 803
            +DQ+IVALS  H LGR H +RS + G     P +  + YF +L
Sbjct: 151 LSDQDIVALSGGHTLGRAHKERSGFEGPWTPNPLIFDNSYFTVL 194



>gb|AAD41402.1|AF159627_1 (AF159627) cytosolic ascorbate peroxidase [Fragaria x ananassa]
 gb|AAD41403.1|AF159628_1 (AF159628) cytosolic ascorbate peroxidase [Fragaria x ananassa]
          Length = 250

 Score =  158 bits (395), Expect = 9e-38
 Identities = 80/163 (49%), Positives = 109/163 (66%), Gaps = 1/163 (0%)
 Frame = +3

Query: 315 PVLVRLAWHASGTYDKETGTGGSNGATMRFAPESDHGANAGLAAARDFLQPVKEKFPWIT 494
           P+++RLAWH++GTYD +T TGG  G TM+ + E  HGAN GL  A   L+P+KE+FP ++
Sbjct: 34  PLMLRLAWHSAGTYDVKTKTGGPFG-TMKQSAELAHGANNGLDIAVRLLEPIKEQFPILS 92

Query: 495 YSDLWILAGVCAIQEMLGPAIPYRPGRSDRDVSGCTPHGRLPDASKRQDHLRXIFGR-MG 671
           Y+D + LAGV A++   GP +P+ PGR D+      P GRLPDA K  DHLR +FG+ MG
Sbjct: 93  YADFYQLAGVVAVEVTGGPDVPFHPGREDKPEP--PPEGRLPDAGKGSDHLREVFGKTMG 150

Query: 672 FNDQEIVALSCAHALGRCHTDRSSYSGTLELLPTVLTDYYFRLL 803
            +DQ+IVALS  H LGR H +RS + G     P +  + YF +L
Sbjct: 151 LSDQDIVALSGGHTLGRAHKERSGFEGPWTPNPLIFDNSYFTVL 194



>gb|AAB94574.1| (AF022213) cytosolic ascorbate peroxidase [Fragaria x ananassa]
 gb|AAD41405.1|AF159630_1 (AF159630) cytosolic ascorbate peroxidase [Fragaria x ananassa]
          Length = 250

 Score =  157 bits (394), Expect = 1e-37
 Identities = 87/196 (44%), Positives = 122/196 (61%), Gaps = 5/196 (2%)
 Frame = +3

Query: 216 KVFNPSKEDYQKVDNEIAARLE----EKDDYDYGSYGPVLVRLAWHASGTYDKETGTGGS 383
           K +    E+Y+K  ++   +L     EK+        P+++RLAWH++GTYD +T TGG 
Sbjct: 3   KCYPTVSEEYKKAIDKAKRKLRGLIAEKN------CAPLMLRLAWHSAGTYDVKTKTGGP 56

Query: 384 NGATMRFAPESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPY 563
            G TM+   E  HGAN GL  A   L+P+KE+FP ++Y+D + LAGV A++   GP +P+
Sbjct: 57  FG-TMKQPAELAHGANNGLDIAVRLLEPIKEQFPILSYADFYQLAGVVAVEVTGGPDVPF 115

Query: 564 RPGRSDRDVSGCTPHGRLPDASKRQDHLRXIFGR-MGFNDQEIVALSCAHALGRCHTDRS 740
            PGR D+      P GRLPDA K  DHLR +FG+ MG +DQ+IVALS  H LGR H +RS
Sbjct: 116 HPGREDKPEP--PPEGRLPDAGKGSDHLREVFGKTMGLSDQDIVALSGGHTLGRAHKERS 173

Query: 741 SYSGTLELLPTVLTDYYFRLL 803
            + G     P +  + YF +L
Sbjct: 174 GFEGPWTPNPLIFDNSYFTVL 194



>gb|AAF23294.1|AC016661_19 (AC016661) putative ascorbate peroxidase [Arabidopsis thaliana]
          Length = 246

 Score =  157 bits (394), Expect = 1e-37
 Identities = 85/194 (43%), Positives = 117/194 (59%)
 Frame = +3

Query: 216 KVFNPSKEDYQKVDNEIAARLEEKDDYDYGSYGPVLVRLAWHASGTYDKETGTGGSNGAT 395
           K +   KE+Y+K       +L       + +  P+++RLAWH++GT+D +T TGG  G T
Sbjct: 4   KSYPEVKEEYKKAVQRCKRKLRGLIAEKHCA--PIVLRLAWHSAGTFDVKTKTGGPFG-T 60

Query: 396 MRFAPESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGR 575
           +R   E  H AN GL  A   L P+KE FP ++Y+D + LAGV A++   GP IP+ PGR
Sbjct: 61  IRHPQELAHDANNGLDIAVRLLDPIKELFPILSYADFYQLAGVVAVEITGGPEIPFHPGR 120

Query: 576 SDRDVSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGT 755
            D+      P GRLP A+K  DHLR +FGRMG ND++IVALS  H LGRCH +RS + G 
Sbjct: 121 LDKVEP--PPEGRLPQATKGVDHLRDVFGRMGLNDKDIVALSGGHTLGRCHKERSGFEGA 178

Query: 756 LELLPTVLTDYYFR 797
               P +  + YF+
Sbjct: 179 WTPNPLIFDNSYFK 192



>emb|CAA56340.1| (X80036) ascorbate peroxidase [Arabidopsis thaliana]
 emb|CAA66925.1| (X98275) L-ascorbate peroxidase [Arabidopsis thaliana]
          Length = 251

 Score =  157 bits (394), Expect = 1e-37
 Identities = 85/194 (43%), Positives = 117/194 (59%)
 Frame = +3

Query: 216 KVFNPSKEDYQKVDNEIAARLEEKDDYDYGSYGPVLVRLAWHASGTYDKETGTGGSNGAT 395
           K +   KE+Y+K       +L       + +  P+++RLAWH++GT+D +T TGG  G T
Sbjct: 4   KSYPEVKEEYKKAVQRCKRKLRGLIAEKHCA--PIVLRLAWHSAGTFDVKTKTGGPFG-T 60

Query: 396 MRFAPESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGR 575
           +R   E  H AN GL  A   L P+KE FP ++Y+D + LAGV A++   GP IP+ PGR
Sbjct: 61  IRHPQELAHDANNGLDIAVRLLDPIKELFPILSYADFYQLAGVVAVEITGGPEIPFHPGR 120

Query: 576 SDRDVSGCTPHGRLPDASKRQDHLRXIFGRMGFNDQEIVALSCAHALGRCHTDRSSYSGT 755
            D+      P GRLP A+K  DHLR +FGRMG ND++IVALS  H LGRCH +RS + G 
Sbjct: 121 LDKVEP--PPEGRLPQATKGVDHLRDVFGRMGLNDKDIVALSGGHTLGRCHKERSGFEGA 178

Query: 756 LELLPTVLTDYYFR 797
               P +  + YF+
Sbjct: 179 WTPNPLIFDNSYFK 192



>emb|CAA72247.1| (Y11461) L-ascorbate peroxidase [Brassica napus]
          Length = 250

 Score =  154 bits (385), Expect = 1e-36
 Identities = 88/189 (46%), Positives = 118/189 (61%), Gaps = 5/189 (2%)
 Frame = +3

Query: 237 EDYQKVDNEIAARLE----EKDDYDYGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRF 404
           E+YQK   +   +L     EK+        P++VRLAWH++GT+D  + TG   G TMRF
Sbjct: 10  EEYQKAIEKCKRKLRGLIAEKN------CAPIMVRLAWHSAGTFDCASRTGVPFG-TMRF 62

Query: 405 APESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDR 584
             E  HGAN+GL  A   L+P++E+FP I+++D   LAGV A++   GP IP+ PGR D+
Sbjct: 63  DGELAHGANSGLHIALRLLEPIREQFPTISHADFHQLAGVVAVEVTGGPEIPFHPGREDK 122

Query: 585 DVSGCTPHGRLPDASKRQDHLRXIF-GRMGFNDQEIVALSCAHALGRCHTDRSSYSGTLE 761
                 P GRLPDA+K  DHLR +F  +M   DQ+IVALS AH LGRCH DRS + G   
Sbjct: 123 PQP--PPEGRLPDATKACDHLRQVFLKQMVLTDQDIVALSGAHTLGRCHKDRSGFEGAWT 180

Query: 762 LLPTVLTDYYFRLL 803
             P +  + YF+ L
Sbjct: 181 SNPLIFDNSYFKEL 194



>pir||S68465 L-ascorbate peroxidase (EC 1.11.1.11), cytosolic isoform - pepper
          Length = 250

 Score =  153 bits (384), Expect = 2e-36
 Identities = 78/163 (47%), Positives = 107/163 (64%), Gaps = 1/163 (0%)
 Frame = +3

Query: 315 PVLVRLAWHASGTYDKETGTGGSNGATMRFAPESDHGANAGLAAARDFLQPVKEKFPWIT 494
           P+++RLAWH++GTYD  + TGG  G TMRF  E  HGAN G+  A   L+P+ E+FP ++
Sbjct: 34  PLMLRLAWHSAGTYDVCSKTGGPFG-TMRFKTEQSHGANNGIDIALRLLEPLGEQFPIVS 92

Query: 495 YSDLWILAGVCAIQEMLGPAI