|
Name |
Accession |
Description |
Interval |
E-value |
| KatG |
COG0376 |
Catalase (peroxidase I) [Inorganic ion transport and metabolism]; |
19-740 |
0e+00 |
|
Catalase (peroxidase I) [Inorganic ion transport and metabolism];
Pssm-ID: 440145 [Multi-domain] Cd Length: 731 Bit Score: 1552.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 19 AMSSGAVMAKGNMTDNQFWWPEQLNLAPLRQHSIENNPYGPGYNYAEQFKTLDLAAVKADIETLLKTSQDWWPADWGHYG 98
Cdd:COG0376 9 FMHGAAAAAAGGGTSNRDWWPNQLNLSILHQHSPKSNPMGEDFDYAEAFKKLDLDAVKKDLKALMTDSQDWWPADYGHYG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 99 PFMIRMAWHSAGVYRIFDGRGGANGGQQRFEPLNSWPDNANLDKARRLLWPIKQKYGSKISWADLMVLTGNVALESMGFK 178
Cdd:COG0376 89 PLFIRMAWHSAGTYRIGDGRGGAGGGQQRFAPLNSWPDNANLDKARRLLWPIKQKYGNKISWADLMILAGNVALESMGFK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 179 TFGFAGGRTDDWEAEI-VNWGSEKEWLDNKRYNEKGELARPLGATQMGLIYVNPEGPNGVPDPLASAKEIRDTFGRMAMT 257
Cdd:COG0376 169 TFGFAGGREDVWEPEEdVYWGPETEWLGDERYSGDRELENPLAAVQMGLIYVNPEGPNGNPDPLAAARDIRETFGRMAMN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 258 DEETVALIAGGHTFGKAHGAHKPqDCTGKEPAAAGLEEQGMGWTNKCGKGNAEDTVTSGLEGAWSANPTAWTTQYLDNLF 337
Cdd:COG0376 249 DEETVALIAGGHTFGKTHGAGDA-EHVGPEPEAAPIEEQGLGWKNSFGSGKGEDTITSGLEGAWTPTPTQWDNGYFDNLF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 338 AFDWVQTKSPGGHIQWIPANGQAANLVPDAHIPGKRSAPIMFTTDIALKEDPIYREISLRFKEDPKQFELAFAKAWFKLT 417
Cdd:COG0376 328 GYEWELTKSPAGAHQWVPKDGAAADTVPDAHDPSKRHAPMMLTTDLALRFDPAYEKISRRFLENPEEFADAFARAWFKLT 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 418 HRDMGPISRYLGTEVPKEALIWQDPIPAVDYKLIESRDINALKGKLLSSGLTVQQLVKTAWASAASFRGTDMRGGANGAR 497
Cdd:COG0376 408 HRDMGPKSRYLGPEVPAEELIWQDPIPAVDHELIDDADIAALKAKILASGLSVSELVSTAWASASTFRGSDKRGGANGAR 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 498 LRLEPQKDWAANDPQELAQVLAVLEKVQTDFNKTLRGGKKVSLADVIVLGGAAAIEKAAKDAGFNITVPFTPGRTDATQA 577
Cdd:COG0376 488 IRLAPQKDWEVNEPEQLAKVLAVLEGIQKDFNAAQSGGKKVSLADLIVLGGCAAVEKAAKDAGHDVTVPFTPGRTDATQE 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 578 QTDAESFAVLEPKADGFRNYYSSDAMYSPAEALVDRANMLTLTVPEMTVLVGGLRVLDVNSGGSKHGVFTDKPGQLSNDF 657
Cdd:COG0376 568 QTDVESFAVLEPKADGFRNYLKKGYSVSAEELLVDKAQLLTLTAPEMTVLVGGLRVLGANYGGSKHGVFTDRPGTLTNDF 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 658 FVNLLDMSTRWAKA-EQEGLYDGFDRKSGERKYTATPVDLVFGSHAELRAVAEVYAANDGKEKFVRDFVAAWNKVMTLDR 736
Cdd:COG0376 648 FVNLLDMGTEWKPSsDDEGLFEGRDRKTGEVKWTATRVDLVFGSNSELRALAEVYASDDAKEKFVKDFVAAWTKVMNLDR 727
|
....
gi 496273277 737 FDLK 740
Cdd:COG0376 728 FDLA 731
|
|
| PRK15061 |
PRK15061 |
catalase/peroxidase; |
29-740 |
0e+00 |
|
catalase/peroxidase;
Pssm-ID: 237891 [Multi-domain] Cd Length: 726 Bit Score: 1501.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 29 GNMTDNQFWWPEQLNLAPLRQHSIENNPYGPGYNYAEQFKTLDLAAVKADIETLLKTSQDWWPADWGHYGPFMIRMAWHS 108
Cdd:PRK15061 13 GGGTSNRDWWPNQLNLDILHQHSSKSNPMGEDFDYAEEFKKLDLEALKKDLKALMTDSQDWWPADYGHYGPLFIRMAWHS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 109 AGVYRIFDGRGGANGGQQRFEPLNSWPDNANLDKARRLLWPIKQKYGSKISWADLMVLTGNVALESMGFKTFGFAGGRTD 188
Cdd:PRK15061 93 AGTYRIGDGRGGAGGGQQRFAPLNSWPDNVNLDKARRLLWPIKQKYGNKISWADLMILAGNVALESMGFKTFGFAGGRED 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 189 DWEAEI-VNWGSEKEWLD-NKRYNEKGELARPLGATQMGLIYVNPEGPNGVPDPLASAKEIRDTFGRMAMTDEETVALIA 266
Cdd:PRK15061 173 VWEPEEdVYWGPEKEWLGgDERYSGERDLENPLAAVQMGLIYVNPEGPNGNPDPLAAARDIRETFARMAMNDEETVALIA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 267 GGHTFGKAHGAHKPqDCTGKEPAAAGLEEQGMGWTNKCGKGNAEDTVTSGLEGAWSANPTAWTTQYLDNLFAFDWVQTKS 346
Cdd:PRK15061 253 GGHTFGKTHGAGDA-SHVGPEPEAAPIEEQGLGWKNSYGSGKGADTITSGLEGAWTTTPTQWDNGYFENLFGYEWELTKS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 347 PGGHIQWIPANGQAANLVPDAHIPGKRSAPIMFTTDIALKEDPIYREISLRFKEDPKQFELAFAKAWFKLTHRDMGPISR 426
Cdd:PRK15061 332 PAGAWQWVPKDGAAEDTVPDAHDPSKKHAPTMLTTDLALRFDPEYEKISRRFLENPEEFADAFARAWFKLTHRDMGPKSR 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 427 YLGTEVPKEALIWQDPIPAVDYKLIESRDINALKGKLLSSGLTVQQLVKTAWASAASFRGTDMRGGANGARLRLEPQKDW 506
Cdd:PRK15061 412 YLGPEVPKEDLIWQDPVPAVDHELIDDADIAALKAKILASGLSVSELVSTAWASASTFRGSDKRGGANGARIRLAPQKDW 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 507 AANDPQELAQVLAVLEKVQTDFNKTLRGGKKVSLADVIVLGGAAAIEKAAKDAGFNITVPFTPGRTDATQAQTDAESFAV 586
Cdd:PRK15061 492 EVNEPAQLAKVLAVLEGIQAEFNAAQSGGKKVSLADLIVLGGNAAVEQAAKAAGHDVTVPFTPGRTDATQEQTDVESFAV 571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 587 LEPKADGFRNYYSSDAMYSPAEALVDRANMLTLTVPEMTVLVGGLRVLDVNSGGSKHGVFTDKPGQLSNDFFVNLLDMST 666
Cdd:PRK15061 572 LEPKADGFRNYLKKGYSVSPEELLVDKAQLLTLTAPEMTVLVGGLRVLGANYGGSKHGVFTDRPGVLTNDFFVNLLDMGT 651
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496273277 667 RWAKA-EQEGLYDGFDRKSGERKYTATPVDLVFGSHAELRAVAEVYAANDGKEKFVRDFVAAWNKVMTLDRFDLK 740
Cdd:PRK15061 652 EWKPTdEDEEVYEGRDRKTGEVKWTATRVDLVFGSNSQLRALAEVYASDDAKEKFVRDFVAAWTKVMNLDRFDLA 726
|
|
| cat_per_HPI |
TIGR00198 |
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ... |
20-739 |
0e+00 |
|
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules of hydrogen peroxide to dioxygen and two molecules of water. As a peroxidase, it uses hydrogen peroxide to oxidize donor compounds and produce water. KatG from E. coli is a homotetramer with two non-covalently associated iron protoheme IX groups per tetramer, but the ortholog from Synechococcus sp. is a homodimer with one protoheme. Important sites (numbered according to E. coli KatG) include heme ligands His-106 and His-267 and active site Trp-318. Note that the translation PID:g296476 from accession X71420 from Rhodobacter capsulatus B10 contains extensive frameshift differences from the rest of the orthologous family. [Cellular processes, Detoxification]
Pssm-ID: 272957 [Multi-domain] Cd Length: 716 Bit Score: 1045.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 20 MSSGAVMAKGNMT-DNQFWWPEQLNLAPLRQHSIENNPYGPGYNYAEQFKTLDLAAVKADIETLLKTSQDWWPADWGHYG 98
Cdd:TIGR00198 1 ASQGGVMHGANTTgQTGDWWPNALNLDILHQHDRKTNPMGEDFDYAEEFQQLDLAAVKQDLKHLMTDSQSWWPADWGHYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 99 PFMIRMAWHSAGVYRIFDGRGGANGGQQRFEPLNSWPDNANLDKARRLLWPIKQKYGSKISWADLMVLTGNVALESMGFK 178
Cdd:TIGR00198 81 GLFIRMAWHAAGTYRIADGRGGAATGNQRFAPLNSWPDNVNLDKARRLLWPIKKKYGNKLSWADLIILAGTVAYESMGLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 179 TFGFAGGRTDDWEAEI-VNWGSEKEWLDNKRyNEKGELARPLGATQMGLIYVNPEGPNGVPDPLASAKEIRDTFGRMAMT 257
Cdd:TIGR00198 161 VFGFAGGREDIWEPDKdIYWGAEKEWLTSSR-EDRESLENPLAATEMGLIYVNPEGPDGHPDPLCTAQDIRTTFARMGMN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 258 DEETVALIAGGHTFGKAHGAhKPQDCTGKEPAAAGLEEQGMGWTNKCGKGNAEDTVTSGLEGAWSANPTAWTTQYLDNLF 337
Cdd:TIGR00198 240 DEETVALIAGGHTVGKCHGA-GPAELIGPDPEGAPIEEQGLGWHNQYGKGVGRDTMTSGLEVAWTTTPTQWDNGYFYMLF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 338 AFDWVQTKSPGGHIQWIPANgqAANLVPDAHIPGKRSAPIMFTTDIALKEDPIYREISLRFKEDPKQFELAFAKAWFKLT 417
Cdd:TIGR00198 319 NYEWELKKSPAGAWQWEAVD--APEIIPDVEDPNKKHNPIMLDADLALRFDPEFRKISRRFLREPDYFAEAFAKAWFKLT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 418 HRDMGPISRYLGTEVPKEALIWQDPIPAVDYKLIEsRDINALKGKLLSSGLTVQQLVKTAWASAASFRGTDMRGGANGAR 497
Cdd:TIGR00198 397 HRDMGPKSRYIGPDVPQEDLIWQDPLPPVDYTLSE-GDIKELKQQILASGLSVSELVCTAWASASTFRSSDYRGGANGAR 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 498 LRLEPQKDWAANDPQELAQVLAVLEKVQTDFNKtlrggKKVSLADVIVLGGAAAIEKAAKDAGFNITVPFTPGRTDATQA 577
Cdd:TIGR00198 476 IRLEPQKNWPVNEPTRLAKVLAVLEKIQAEFAK-----GPVSLADLIVLGGGAAVEKAALDAGISVNVPFLPGRVDATQA 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 578 QTDAESFAVLEPKADGFRNYYSSDAMYSPAEALVDRANMLTLTVPEMTVLVGGLRVLDVNSGGSKHGVFTDKPGQLSNDF 657
Cdd:TIGR00198 551 MTDAESFTPLEPIADGFRNYLKRDYAVTPEELLLDKAQLLTLTAPEMTVLIGGMRVLGANHGGSKHGVFTDRVGVLSNDF 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 658 FVNLLDMSTRW-AKAEQEGLYDGFDRKSGERKYTATPVDLVFGSHAELRAVAEVYAANDGKEKFVRDFVAAWNKVMTLDR 736
Cdd:TIGR00198 631 FVNLLDMAYEWrAADNNRYLFEGGDRQTGEVKWTATRVDLVFGSNSILRAVAEVYAQDDAREKFVKDFVAAWTKVMNLDR 710
|
...
gi 496273277 737 FDL 739
Cdd:TIGR00198 711 FDL 713
|
|
| catalase_peroxidase_1 |
cd00649 |
N-terminal catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ... |
29-437 |
0e+00 |
|
N-terminal catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Catalase-peroxidases can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. These enzymes are found in many archaeal and bacterial organisms, where they neutralize potentially lethal hydrogen peroxide molecules generated during photosynthesis or stationary phase. Along with related intracellular fungal and plant peroxidases, catalase-peroxidases belong to class I of the plant peroxidase superfamily. Unlike the eukaryotic enzymes, they are typically comprised of two homologous domains that probably arose via a single gene duplication event. The heme binding motif is present only in the N-terminal domain; the function of the C-terminal domain is not clear.
Pssm-ID: 173824 [Multi-domain] Cd Length: 409 Bit Score: 788.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 29 GNMTDNQFWWPEQLNLAPLRQHSIENNPYGPGYNYAEQFKTLDLAAVKADIETLLKTSQDWWPADWGHYGPFMIRMAWHS 108
Cdd:cd00649 1 GGGTSNQDWWPNRLNLKILHQHSPKSNPMGEDFNYAEEFKKLDLEALKEDLKALMTDSQDWWPADYGHYGPLFIRMAWHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 109 AGVYRIFDGRGGANGGQQRFEPLNSWPDNANLDKARRLLWPIKQKYGSKISWADLMVLTGNVALESMGFKTFGFAGGRTD 188
Cdd:cd00649 81 AGTYRIADGRGGAGTGQQRFAPLNSWPDNVNLDKARRLLWPIKQKYGNKISWADLMILAGNVALESMGFKTFGFAGGRED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 189 DWEAEI-VNWGSEKEWLDNKRYNEKGELARPLGATQMGLIYVNPEGPNGVPDPLASAKEIRDTFGRMAMTDEETVALIAG 267
Cdd:cd00649 161 VWEPDEdVYWGPEKEWLADKRYSGDRDLENPLAAVQMGLIYVNPEGPDGNPDPLAAAKDIRETFARMAMNDEETVALIAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 268 GHTFGKAHGAhKPQDCTGKEPAAAGLEEQGMGWTNKCGKGNAEDTVTSGLEGAWSANPTAWTTQYLDNLFAFDWVQTKSP 347
Cdd:cd00649 241 GHTFGKTHGA-GPASHVGPEPEAAPIEQQGLGWKNSYGTGKGKDTITSGLEGAWTPTPTKWDNNYLKNLFGYEWELTKSP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 348 GGHIQWIPANGQAANLVPDAHIPGKRSAPIMFTTDIALKEDPIYREISLRFKEDPKQFELAFAKAWFKLTHRDMGPISRY 427
Cdd:cd00649 320 AGAWQWVPKNAAGENTVPDAHDPSKKHAPMMLTTDLALRFDPEYEKISRRFLENPDEFADAFAKAWFKLTHRDMGPKSRY 399
|
410
....*....|
gi 496273277 428 LGTEVPKEAL 437
Cdd:cd00649 400 LGPEVPEEDL 409
|
|
| peroxidase |
pfam00141 |
Peroxidase; |
75-275 |
5.23e-42 |
|
Peroxidase;
Pssm-ID: 425483 [Multi-domain] Cd Length: 187 Bit Score: 151.18 E-value: 5.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 75 VKADIETLLKTsqdwwpadWGHYGPFMIRMAWHSAGVyrifdgrGGANGGQQR--FEPLNSWPDNANLDKARRLLWPIKQ 152
Cdd:pfam00141 1 VRSVVRAAFKA--------DPTMGPSLLRLHFHDCFV-------GGCDGSVLLdgFKPEKDAPPNLGLRKGFEVIDDIKA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 153 KYGS----KISWADLMVLTGNVALESMGFKTFGFAGGRTDDWEAEIVNWGSEkewldnkrynekgelarplgatqmgliy 228
Cdd:pfam00141 66 KLEAacpgVVSCADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSN---------------------------- 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 496273277 229 vnpegpngVPDPLASAKEIRDTFGRMAMTDEETVALiAGGHTFGKAH 275
Cdd:pfam00141 118 --------LPAPTDSLDQLRDRFARKGLTAEDLVAL-SGAHTIGRAH 155
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| KatG |
COG0376 |
Catalase (peroxidase I) [Inorganic ion transport and metabolism]; |
19-740 |
0e+00 |
|
Catalase (peroxidase I) [Inorganic ion transport and metabolism];
Pssm-ID: 440145 [Multi-domain] Cd Length: 731 Bit Score: 1552.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 19 AMSSGAVMAKGNMTDNQFWWPEQLNLAPLRQHSIENNPYGPGYNYAEQFKTLDLAAVKADIETLLKTSQDWWPADWGHYG 98
Cdd:COG0376 9 FMHGAAAAAAGGGTSNRDWWPNQLNLSILHQHSPKSNPMGEDFDYAEAFKKLDLDAVKKDLKALMTDSQDWWPADYGHYG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 99 PFMIRMAWHSAGVYRIFDGRGGANGGQQRFEPLNSWPDNANLDKARRLLWPIKQKYGSKISWADLMVLTGNVALESMGFK 178
Cdd:COG0376 89 PLFIRMAWHSAGTYRIGDGRGGAGGGQQRFAPLNSWPDNANLDKARRLLWPIKQKYGNKISWADLMILAGNVALESMGFK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 179 TFGFAGGRTDDWEAEI-VNWGSEKEWLDNKRYNEKGELARPLGATQMGLIYVNPEGPNGVPDPLASAKEIRDTFGRMAMT 257
Cdd:COG0376 169 TFGFAGGREDVWEPEEdVYWGPETEWLGDERYSGDRELENPLAAVQMGLIYVNPEGPNGNPDPLAAARDIRETFGRMAMN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 258 DEETVALIAGGHTFGKAHGAHKPqDCTGKEPAAAGLEEQGMGWTNKCGKGNAEDTVTSGLEGAWSANPTAWTTQYLDNLF 337
Cdd:COG0376 249 DEETVALIAGGHTFGKTHGAGDA-EHVGPEPEAAPIEEQGLGWKNSFGSGKGEDTITSGLEGAWTPTPTQWDNGYFDNLF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 338 AFDWVQTKSPGGHIQWIPANGQAANLVPDAHIPGKRSAPIMFTTDIALKEDPIYREISLRFKEDPKQFELAFAKAWFKLT 417
Cdd:COG0376 328 GYEWELTKSPAGAHQWVPKDGAAADTVPDAHDPSKRHAPMMLTTDLALRFDPAYEKISRRFLENPEEFADAFARAWFKLT 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 418 HRDMGPISRYLGTEVPKEALIWQDPIPAVDYKLIESRDINALKGKLLSSGLTVQQLVKTAWASAASFRGTDMRGGANGAR 497
Cdd:COG0376 408 HRDMGPKSRYLGPEVPAEELIWQDPIPAVDHELIDDADIAALKAKILASGLSVSELVSTAWASASTFRGSDKRGGANGAR 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 498 LRLEPQKDWAANDPQELAQVLAVLEKVQTDFNKTLRGGKKVSLADVIVLGGAAAIEKAAKDAGFNITVPFTPGRTDATQA 577
Cdd:COG0376 488 IRLAPQKDWEVNEPEQLAKVLAVLEGIQKDFNAAQSGGKKVSLADLIVLGGCAAVEKAAKDAGHDVTVPFTPGRTDATQE 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 578 QTDAESFAVLEPKADGFRNYYSSDAMYSPAEALVDRANMLTLTVPEMTVLVGGLRVLDVNSGGSKHGVFTDKPGQLSNDF 657
Cdd:COG0376 568 QTDVESFAVLEPKADGFRNYLKKGYSVSAEELLVDKAQLLTLTAPEMTVLVGGLRVLGANYGGSKHGVFTDRPGTLTNDF 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 658 FVNLLDMSTRWAKA-EQEGLYDGFDRKSGERKYTATPVDLVFGSHAELRAVAEVYAANDGKEKFVRDFVAAWNKVMTLDR 736
Cdd:COG0376 648 FVNLLDMGTEWKPSsDDEGLFEGRDRKTGEVKWTATRVDLVFGSNSELRALAEVYASDDAKEKFVKDFVAAWTKVMNLDR 727
|
....
gi 496273277 737 FDLK 740
Cdd:COG0376 728 FDLA 731
|
|
| PRK15061 |
PRK15061 |
catalase/peroxidase; |
29-740 |
0e+00 |
|
catalase/peroxidase;
Pssm-ID: 237891 [Multi-domain] Cd Length: 726 Bit Score: 1501.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 29 GNMTDNQFWWPEQLNLAPLRQHSIENNPYGPGYNYAEQFKTLDLAAVKADIETLLKTSQDWWPADWGHYGPFMIRMAWHS 108
Cdd:PRK15061 13 GGGTSNRDWWPNQLNLDILHQHSSKSNPMGEDFDYAEEFKKLDLEALKKDLKALMTDSQDWWPADYGHYGPLFIRMAWHS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 109 AGVYRIFDGRGGANGGQQRFEPLNSWPDNANLDKARRLLWPIKQKYGSKISWADLMVLTGNVALESMGFKTFGFAGGRTD 188
Cdd:PRK15061 93 AGTYRIGDGRGGAGGGQQRFAPLNSWPDNVNLDKARRLLWPIKQKYGNKISWADLMILAGNVALESMGFKTFGFAGGRED 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 189 DWEAEI-VNWGSEKEWLD-NKRYNEKGELARPLGATQMGLIYVNPEGPNGVPDPLASAKEIRDTFGRMAMTDEETVALIA 266
Cdd:PRK15061 173 VWEPEEdVYWGPEKEWLGgDERYSGERDLENPLAAVQMGLIYVNPEGPNGNPDPLAAARDIRETFARMAMNDEETVALIA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 267 GGHTFGKAHGAHKPqDCTGKEPAAAGLEEQGMGWTNKCGKGNAEDTVTSGLEGAWSANPTAWTTQYLDNLFAFDWVQTKS 346
Cdd:PRK15061 253 GGHTFGKTHGAGDA-SHVGPEPEAAPIEEQGLGWKNSYGSGKGADTITSGLEGAWTTTPTQWDNGYFENLFGYEWELTKS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 347 PGGHIQWIPANGQAANLVPDAHIPGKRSAPIMFTTDIALKEDPIYREISLRFKEDPKQFELAFAKAWFKLTHRDMGPISR 426
Cdd:PRK15061 332 PAGAWQWVPKDGAAEDTVPDAHDPSKKHAPTMLTTDLALRFDPEYEKISRRFLENPEEFADAFARAWFKLTHRDMGPKSR 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 427 YLGTEVPKEALIWQDPIPAVDYKLIESRDINALKGKLLSSGLTVQQLVKTAWASAASFRGTDMRGGANGARLRLEPQKDW 506
Cdd:PRK15061 412 YLGPEVPKEDLIWQDPVPAVDHELIDDADIAALKAKILASGLSVSELVSTAWASASTFRGSDKRGGANGARIRLAPQKDW 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 507 AANDPQELAQVLAVLEKVQTDFNKTLRGGKKVSLADVIVLGGAAAIEKAAKDAGFNITVPFTPGRTDATQAQTDAESFAV 586
Cdd:PRK15061 492 EVNEPAQLAKVLAVLEGIQAEFNAAQSGGKKVSLADLIVLGGNAAVEQAAKAAGHDVTVPFTPGRTDATQEQTDVESFAV 571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 587 LEPKADGFRNYYSSDAMYSPAEALVDRANMLTLTVPEMTVLVGGLRVLDVNSGGSKHGVFTDKPGQLSNDFFVNLLDMST 666
Cdd:PRK15061 572 LEPKADGFRNYLKKGYSVSPEELLVDKAQLLTLTAPEMTVLVGGLRVLGANYGGSKHGVFTDRPGVLTNDFFVNLLDMGT 651
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496273277 667 RWAKA-EQEGLYDGFDRKSGERKYTATPVDLVFGSHAELRAVAEVYAANDGKEKFVRDFVAAWNKVMTLDRFDLK 740
Cdd:PRK15061 652 EWKPTdEDEEVYEGRDRKTGEVKWTATRVDLVFGSNSQLRALAEVYASDDAKEKFVRDFVAAWTKVMNLDRFDLA 726
|
|
| cat_per_HPI |
TIGR00198 |
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ... |
20-739 |
0e+00 |
|
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules of hydrogen peroxide to dioxygen and two molecules of water. As a peroxidase, it uses hydrogen peroxide to oxidize donor compounds and produce water. KatG from E. coli is a homotetramer with two non-covalently associated iron protoheme IX groups per tetramer, but the ortholog from Synechococcus sp. is a homodimer with one protoheme. Important sites (numbered according to E. coli KatG) include heme ligands His-106 and His-267 and active site Trp-318. Note that the translation PID:g296476 from accession X71420 from Rhodobacter capsulatus B10 contains extensive frameshift differences from the rest of the orthologous family. [Cellular processes, Detoxification]
Pssm-ID: 272957 [Multi-domain] Cd Length: 716 Bit Score: 1045.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 20 MSSGAVMAKGNMT-DNQFWWPEQLNLAPLRQHSIENNPYGPGYNYAEQFKTLDLAAVKADIETLLKTSQDWWPADWGHYG 98
Cdd:TIGR00198 1 ASQGGVMHGANTTgQTGDWWPNALNLDILHQHDRKTNPMGEDFDYAEEFQQLDLAAVKQDLKHLMTDSQSWWPADWGHYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 99 PFMIRMAWHSAGVYRIFDGRGGANGGQQRFEPLNSWPDNANLDKARRLLWPIKQKYGSKISWADLMVLTGNVALESMGFK 178
Cdd:TIGR00198 81 GLFIRMAWHAAGTYRIADGRGGAATGNQRFAPLNSWPDNVNLDKARRLLWPIKKKYGNKLSWADLIILAGTVAYESMGLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 179 TFGFAGGRTDDWEAEI-VNWGSEKEWLDNKRyNEKGELARPLGATQMGLIYVNPEGPNGVPDPLASAKEIRDTFGRMAMT 257
Cdd:TIGR00198 161 VFGFAGGREDIWEPDKdIYWGAEKEWLTSSR-EDRESLENPLAATEMGLIYVNPEGPDGHPDPLCTAQDIRTTFARMGMN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 258 DEETVALIAGGHTFGKAHGAhKPQDCTGKEPAAAGLEEQGMGWTNKCGKGNAEDTVTSGLEGAWSANPTAWTTQYLDNLF 337
Cdd:TIGR00198 240 DEETVALIAGGHTVGKCHGA-GPAELIGPDPEGAPIEEQGLGWHNQYGKGVGRDTMTSGLEVAWTTTPTQWDNGYFYMLF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 338 AFDWVQTKSPGGHIQWIPANgqAANLVPDAHIPGKRSAPIMFTTDIALKEDPIYREISLRFKEDPKQFELAFAKAWFKLT 417
Cdd:TIGR00198 319 NYEWELKKSPAGAWQWEAVD--APEIIPDVEDPNKKHNPIMLDADLALRFDPEFRKISRRFLREPDYFAEAFAKAWFKLT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 418 HRDMGPISRYLGTEVPKEALIWQDPIPAVDYKLIEsRDINALKGKLLSSGLTVQQLVKTAWASAASFRGTDMRGGANGAR 497
Cdd:TIGR00198 397 HRDMGPKSRYIGPDVPQEDLIWQDPLPPVDYTLSE-GDIKELKQQILASGLSVSELVCTAWASASTFRSSDYRGGANGAR 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 498 LRLEPQKDWAANDPQELAQVLAVLEKVQTDFNKtlrggKKVSLADVIVLGGAAAIEKAAKDAGFNITVPFTPGRTDATQA 577
Cdd:TIGR00198 476 IRLEPQKNWPVNEPTRLAKVLAVLEKIQAEFAK-----GPVSLADLIVLGGGAAVEKAALDAGISVNVPFLPGRVDATQA 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 578 QTDAESFAVLEPKADGFRNYYSSDAMYSPAEALVDRANMLTLTVPEMTVLVGGLRVLDVNSGGSKHGVFTDKPGQLSNDF 657
Cdd:TIGR00198 551 MTDAESFTPLEPIADGFRNYLKRDYAVTPEELLLDKAQLLTLTAPEMTVLIGGMRVLGANHGGSKHGVFTDRVGVLSNDF 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 658 FVNLLDMSTRW-AKAEQEGLYDGFDRKSGERKYTATPVDLVFGSHAELRAVAEVYAANDGKEKFVRDFVAAWNKVMTLDR 736
Cdd:TIGR00198 631 FVNLLDMAYEWrAADNNRYLFEGGDRQTGEVKWTATRVDLVFGSNSILRAVAEVYAQDDAREKFVKDFVAAWTKVMNLDR 710
|
...
gi 496273277 737 FDL 739
Cdd:TIGR00198 711 FDL 713
|
|
| catalase_peroxidase_1 |
cd00649 |
N-terminal catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ... |
29-437 |
0e+00 |
|
N-terminal catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Catalase-peroxidases can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. These enzymes are found in many archaeal and bacterial organisms, where they neutralize potentially lethal hydrogen peroxide molecules generated during photosynthesis or stationary phase. Along with related intracellular fungal and plant peroxidases, catalase-peroxidases belong to class I of the plant peroxidase superfamily. Unlike the eukaryotic enzymes, they are typically comprised of two homologous domains that probably arose via a single gene duplication event. The heme binding motif is present only in the N-terminal domain; the function of the C-terminal domain is not clear.
Pssm-ID: 173824 [Multi-domain] Cd Length: 409 Bit Score: 788.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 29 GNMTDNQFWWPEQLNLAPLRQHSIENNPYGPGYNYAEQFKTLDLAAVKADIETLLKTSQDWWPADWGHYGPFMIRMAWHS 108
Cdd:cd00649 1 GGGTSNQDWWPNRLNLKILHQHSPKSNPMGEDFNYAEEFKKLDLEALKEDLKALMTDSQDWWPADYGHYGPLFIRMAWHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 109 AGVYRIFDGRGGANGGQQRFEPLNSWPDNANLDKARRLLWPIKQKYGSKISWADLMVLTGNVALESMGFKTFGFAGGRTD 188
Cdd:cd00649 81 AGTYRIADGRGGAGTGQQRFAPLNSWPDNVNLDKARRLLWPIKQKYGNKISWADLMILAGNVALESMGFKTFGFAGGRED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 189 DWEAEI-VNWGSEKEWLDNKRYNEKGELARPLGATQMGLIYVNPEGPNGVPDPLASAKEIRDTFGRMAMTDEETVALIAG 267
Cdd:cd00649 161 VWEPDEdVYWGPEKEWLADKRYSGDRDLENPLAAVQMGLIYVNPEGPDGNPDPLAAAKDIRETFARMAMNDEETVALIAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 268 GHTFGKAHGAhKPQDCTGKEPAAAGLEEQGMGWTNKCGKGNAEDTVTSGLEGAWSANPTAWTTQYLDNLFAFDWVQTKSP 347
Cdd:cd00649 241 GHTFGKTHGA-GPASHVGPEPEAAPIEQQGLGWKNSYGTGKGKDTITSGLEGAWTPTPTKWDNNYLKNLFGYEWELTKSP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 348 GGHIQWIPANGQAANLVPDAHIPGKRSAPIMFTTDIALKEDPIYREISLRFKEDPKQFELAFAKAWFKLTHRDMGPISRY 427
Cdd:cd00649 320 AGAWQWVPKNAAGENTVPDAHDPSKKHAPMMLTTDLALRFDPEYEKISRRFLENPDEFADAFAKAWFKLTHRDMGPKSRY 399
|
410
....*....|
gi 496273277 428 LGTEVPKEAL 437
Cdd:cd00649 400 LGPEVPEEDL 409
|
|
| catalase_peroxidase_2 |
cd08200 |
C-terminal non-catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ... |
441-736 |
0e+00 |
|
C-terminal non-catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Catalase-peroxidases can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. These enzymes are found in many archaeal and bacterial organisms where they neutralize potentially lethal hydrogen peroxide molecules generated during photosynthesis or stationary phase. Along with related intracellular fungal and plant peroxidases, catalase-peroxidases belong to plant peroxidase superfamily. Unlike the eukaryotic enzymes, they are typically comprised of two homologous domains that probably arose via a single gene duplication event. The heme binding motif is present only in the N-terminal domain; the function of the C-terminal domain is not clear.
Pssm-ID: 173828 Cd Length: 297 Bit Score: 586.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 441 DPIPAVDYKLIESRDINALKGKLLSSGLTVQQLVKTAWASAASFRGTDMRGGANGARLRLEPQKDWAANDPQELAQVLAV 520
Cdd:cd08200 1 DPIPAVDYELIDDADIAALKAKILASGLTVSELVSTAWASASTFRNSDKRGGANGARIRLAPQKDWEVNEPEELAKVLAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 521 LEKVQTDFNKTLRGGKKVSLADVIVLGGAAAIEKAAKDAGFNITVPFTPGRTDATQAQTDAESFAVLEPKADGFRNYYSS 600
Cdd:cd08200 81 LEGIQKEFNESQSGGKKVSLADLIVLGGCAAVEKAAKDAGVDIKVPFTPGRTDATQEQTDVESFEVLEPKADGFRNYLKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 601 DAMYSPAEALVDRANMLTLTVPEMTVLVGGLRVLDVNSGGSKHGVFTDKPGQLSNDFFVNLLDMSTRWAKAEQ-EGLYDG 679
Cdd:cd08200 161 GYRVPPEEMLVDKAQLLTLTAPEMTVLVGGLRVLGANYGGSKHGVFTDRPGVLTNDFFVNLLDMSTEWKPADEdDGLFEG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 496273277 680 FDRKSGERKYTATPVDLVFGSHAELRAVAEVYAANDGKEKFVRDFVAAWNKVMTLDR 736
Cdd:cd08200 241 RDRKTGEVKWTATRVDLVFGSNSELRAVAEVYASDDAQEKFVKDFVAAWTKVMNLDR 297
|
|
| plant_peroxidase_like |
cd00314 |
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ... |
74-418 |
7.17e-55 |
|
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these enzymes belong to a group of peroxidases containing a heme prosthetic group (ferriprotoporphyrin IX), which catalyzes a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. The plant peroxidase-like superfamily is found in all three kingdoms of life and carries out a variety of biosynthetic and degradative functions. Several sub-families can be identified. Class I includes intracellular peroxidases present in fungi, plants, archaea and bacteria, called catalase-peroxidases, that can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. Catalase-peroxidases are typically comprised of two homologous domains that probably arose via a single gene duplication event. Class II includes ligninase and other extracellular fungal peroxidases, while class III is comprised of classic extracellular plant peroxidases, like horseradish peroxidase.
Pssm-ID: 173823 [Multi-domain] Cd Length: 255 Bit Score: 188.90 E-value: 7.17e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 74 AVKADIETLLktsqdwwpADWGHYGPFMIRMAWHSAGVYRIFDGRGGANGGQQRFEPLNSWPDNANLDKARRLLWPIKQK 153
Cdd:cd00314 2 AIKAILEDLI--------TQAGALAGSLLRLAFHDAGTYDIADGKGGGADGSIRFEPELDRPENGGLDKALRALEPIKSA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 154 YGS--KISWADLMVLTGNVALESM--GFKTFGFAGGRTDdweaeivnwgsekewldnkrynekgelarplgATQMGLIYV 229
Cdd:cd00314 74 YDGgnPVSRADLIALAGAVAVESTfgGGPLIPFRFGRLD--------------------------------ATEPDLGVP 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 230 NPEGPngVPDPLASAKEIRDTFGRMAMTDEETVALIAGGHTF-GKAHGAHKPQDCtgkepaaagleeqgmgwtnkcgkgn 308
Cdd:cd00314 122 DPEGL--LPNETSSATELRDKFKRMGLSPSELVALSAGAHTLgGKNHGDLLNYEG------------------------- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 309 aedtvtsglEGAWSANPTAWTTQYLDNLFAFDWvqtkspgghiQWIPANGQAANLVPdahipgkrsaPIMFTTDIALKED 388
Cdd:cd00314 175 ---------SGLWTSTPFTFDNAYFKNLLDMNW----------EWRVGSPDPDGVKG----------PGLLPSDYALLSD 225
|
330 340 350
....*....|....*....|....*....|
gi 496273277 389 PIYREISLRFKEDPKQFELAFAKAWFKLTH 418
Cdd:cd00314 226 SETRALVERYASDQEKFFEDFAKAWIKMVN 255
|
|
| plant_peroxidase_like |
cd00314 |
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ... |
473-732 |
5.04e-44 |
|
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these enzymes belong to a group of peroxidases containing a heme prosthetic group (ferriprotoporphyrin IX), which catalyzes a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. The plant peroxidase-like superfamily is found in all three kingdoms of life and carries out a variety of biosynthetic and degradative functions. Several sub-families can be identified. Class I includes intracellular peroxidases present in fungi, plants, archaea and bacteria, called catalase-peroxidases, that can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. Catalase-peroxidases are typically comprised of two homologous domains that probably arose via a single gene duplication event. Class II includes ligninase and other extracellular fungal peroxidases, while class III is comprised of classic extracellular plant peroxidases, like horseradish peroxidase.
Pssm-ID: 173823 [Multi-domain] Cd Length: 255 Bit Score: 159.24 E-value: 5.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 473 LVKTAWASAASFRGTDMRGGANGARLRLEPQKDWAANdpQELAQVLAVLEKVQTDFNktlrGGKKVSLADVIVLGGAAAI 552
Cdd:cd00314 21 LLRLAFHDAGTYDIADGKGGGADGSIRFEPELDRPEN--GGLDKALRALEPIKSAYD----GGNPVSRADLIALAGAVAV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 553 EKAakdAGFNITVPFTPGRTDATqaqtdAESFAVLEPkadgfrnYYSSDAMYSPAEALVDRANMLTLTVPEMTVLVGGLR 632
Cdd:cd00314 95 EST---FGGGPLIPFRFGRLDAT-----EPDLGVPDP-------EGLLPNETSSATELRDKFKRMGLSPSELVALSAGAH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 633 VLD-----VNSGGSKHGVFTDKPGQLSNDFFVNLLDMSTRWAKAEqeglydgfDRKSGERKYTATPVDLVFGSHAELRAV 707
Cdd:cd00314 160 TLGgknhgDLLNYEGSGLWTSTPFTFDNAYFKNLLDMNWEWRVGS--------PDPDGVKGPGLLPSDYALLSDSETRAL 231
|
250 260
....*....|....*....|....*
gi 496273277 708 AEVYAANdgKEKFVRDFVAAWNKVM 732
Cdd:cd00314 232 VERYASD--QEKFFEDFAKAWIKMV 254
|
|
| ascorbate_peroxidase |
cd00691 |
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ... |
71-417 |
6.78e-44 |
|
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Along with related catalase-peroxidases, ascorbate peroxidases belong to class I of the plant superfamily. Ascorbate peroxidases are found in the chloroplasts and/or cytosol of algae and plants, where they have been shown to control the concentration of lethal hydrogen peroxide molecules. The yeast cytochrome c peroxidase is a divergent member of the family; it forms a complex with cytochrome c to catalyze the reduction of hydrogen peroxide to water.
Pssm-ID: 173825 [Multi-domain] Cd Length: 253 Bit Score: 158.52 E-value: 6.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 71 DLAAVKADIETLLKTsqdwwpadwGHYGPFMIRMAWHSAGVYRIFDGRGGANGGqQRFEPLNSWPDNANLDKARRLLWPI 150
Cdd:cd00691 12 DLEAARNDIAKLIDD---------KNCAPILVRLAWHDSGTYDKETKTGGSNGT-IRFDPELNHGANAGLDIARKLLEPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 151 KQKYgSKISWADLMVLTGNVALESMGFKTFGFAGGRTDDWEAEivnwgsekewldnkrynekgelarplgatqmgliYVN 230
Cdd:cd00691 82 KKKY-PDISYADLWQLAGVVAIEEMGGPKIPFRPGRVDASDPE----------------------------------ECP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 231 PEGpnGVPDPLASAKEIRDTFGRMAMTDEETVALIaGGHTFGKAHgahkpqdctgKEpaaagleeqgmgwtnkcgkgnae 310
Cdd:cd00691 127 PEG--RLPDASKGADHLRDVFYRMGFNDQEIVALS-GAHTLGRCH----------KE----------------------- 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 311 dtvTSGLEGAWSANPTAWTTQYLDNLFAFDWvQTKSPGghiqwipangqaanLvpdahipgkrsapIMFTTDIALKEDPI 390
Cdd:cd00691 171 ---RSGYDGPWTKNPLKFDNSYFKELLEEDW-KLPTPG--------------L-------------LMLPTDKALLEDPK 219
|
330 340
....*....|....*....|....*..
gi 496273277 391 YREISLRFKEDPKQFELAFAKAWFKLT 417
Cdd:cd00691 220 FRPYVELYAKDQDAFFKDYAEAHKKLS 246
|
|
| peroxidase |
pfam00141 |
Peroxidase; |
75-275 |
5.23e-42 |
|
Peroxidase;
Pssm-ID: 425483 [Multi-domain] Cd Length: 187 Bit Score: 151.18 E-value: 5.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 75 VKADIETLLKTsqdwwpadWGHYGPFMIRMAWHSAGVyrifdgrGGANGGQQR--FEPLNSWPDNANLDKARRLLWPIKQ 152
Cdd:pfam00141 1 VRSVVRAAFKA--------DPTMGPSLLRLHFHDCFV-------GGCDGSVLLdgFKPEKDAPPNLGLRKGFEVIDDIKA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 153 KYGS----KISWADLMVLTGNVALESMGFKTFGFAGGRTDDWEAEIVNWGSEkewldnkrynekgelarplgatqmgliy 228
Cdd:pfam00141 66 KLEAacpgVVSCADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSN---------------------------- 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 496273277 229 vnpegpngVPDPLASAKEIRDTFGRMAMTDEETVALiAGGHTFGKAH 275
Cdd:pfam00141 118 --------LPAPTDSLDQLRDRFARKGLTAEDLVAL-SGAHTIGRAH 155
|
|
| peroxidase |
pfam00141 |
Peroxidase; |
491-714 |
3.84e-27 |
|
Peroxidase;
Pssm-ID: 425483 [Multi-domain] Cd Length: 187 Bit Score: 108.81 E-value: 3.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 491 GGANGARLR--LEPQKDWAANDpqELAQVLAVLEKVQTDFNKtlRGGKKVSLADVIVLGGAAAIEKAakdAGFNItvPFT 568
Cdd:pfam00141 30 GGCDGSVLLdgFKPEKDAPPNL--GLRKGFEVIDDIKAKLEA--ACPGVVSCADILALAARDAVELA---GGPSW--PVP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 569 PGRTDATQAQTdAESFAVL-EPKADgfrnyyssdamyspAEALVDRANMLTLTVPEMTVLVGGlRVLDVNSggskhgvft 647
Cdd:pfam00141 101 LGRRDGTVSSA-VEANSNLpAPTDS--------------LDQLRDRFARKGLTAEDLVALSGA-HTIGRAH--------- 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496273277 648 dkpgqlsndffVNLLDmstrwakaeqeglydgfdrksgerKYTATPVDLVFGSHAELRAVAEVYAAN 714
Cdd:pfam00141 156 -----------KNLLD------------------------GRGLLTSDQALLSDPRTRALVERYAAD 187
|
|
| PLN02608 |
PLN02608 |
L-ascorbate peroxidase |
99-275 |
8.57e-20 |
|
L-ascorbate peroxidase
Pssm-ID: 178218 [Multi-domain] Cd Length: 289 Bit Score: 90.21 E-value: 8.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 99 PFMIRMAWHSAGVYRIFDGRGGANgGQQRFEPLNSWPDNANLDKARRLLWPIKQKYgSKISWADLMVLTGNVALESMGFK 178
Cdd:PLN02608 32 PIMLRLAWHDAGTYDAKTKTGGPN-GSIRNEEEYSHGANNGLKIAIDLCEPVKAKH-PKITYADLYQLAGVVAVEVTGGP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 179 TFGFAGGRTDDWEAEivnwgsekewldnkrynEKGELarplgatqmgliyvnpegpngvPDPLASAKEIRDTFGRMAMTD 258
Cdd:PLN02608 110 TIDFVPGRKDSNACP-----------------EEGRL----------------------PDAKKGAKHLRDVFYRMGLSD 150
|
170
....*....|....*..
gi 496273277 259 EETVALiAGGHTFGKAH 275
Cdd:PLN02608 151 KDIVAL-SGGHTLGRAH 166
|
|
| PLN02879 |
PLN02879 |
L-ascorbate peroxidase |
96-417 |
2.80e-18 |
|
L-ascorbate peroxidase
Pssm-ID: 178467 [Multi-domain] Cd Length: 251 Bit Score: 85.11 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 96 HYGPFMIRMAWHSAGVYRIFDGRGGANGGQQRFEPLNSWPDNAnLDKARRLLWPIKQKYgSKISWADLMVLTGNVALESM 175
Cdd:PLN02879 32 HCAPIVLRLAWHSAGTFDVKTKTGGPFGTIRHPQELAHDANNG-LDIAVRLLDPIKELF-PILSYADFYQLAGVVAVEIT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 176 GFKTFGFAGGRTDDWEAEivnwgsekewldnkrynekgelarplgatqmgliyvnPEGPngVPDPLASAKEIRDTFGRMA 255
Cdd:PLN02879 110 GGPEIPFHPGRLDKVEPP-------------------------------------PEGR--LPQATKGVDHLRDVFGRMG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 256 MTDEETVALiAGGHTFGKAHgahkpqdctgKEpaaagleeqgmgwtnkcgkgnaedtvTSGLEGAWSANPTAWTTQYLDN 335
Cdd:PLN02879 151 LNDKDIVAL-SGGHTLGRCH----------KE--------------------------RSGFEGAWTPNPLIFDNSYFKE 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 336 LFAfdwvqtkspgghiqwipangqaanlvpdahipGKRSAPIMFTTDIALKEDPIYREISLRFKEDPKQFELAFAKAWFK 415
Cdd:PLN02879 194 ILS--------------------------------GEKEGLLQLPTDKALLDDPLFLPFVEKYAADEDAFFEDYTEAHLK 241
|
..
gi 496273277 416 LT 417
Cdd:PLN02879 242 LS 243
|
|
| PLN02364 |
PLN02364 |
L-ascorbate peroxidase 1 |
98-417 |
5.21e-18 |
|
L-ascorbate peroxidase 1
Pssm-ID: 166005 Cd Length: 250 Bit Score: 84.36 E-value: 5.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 98 GPFMIRMAWHSAGVYRIfDGRGGANGGQQRFEPLNSWPDNANLDKARRLLWPIKQKYGSkISWADLMVLTGNVALESMGF 177
Cdd:PLN02364 33 APIMVRLAWHSAGTFDC-QSRTGGPFGTMRFDAEQAHGANSGIHIALRLLDPIREQFPT-ISFADFHQLAGVVAVEVTGG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 178 KTFGFAGGRTDDWEAEivnwgsekewldnkrynekgelarplgatqmgliyvnPEGPngVPDPLASAKEIRDTFGR-MAM 256
Cdd:PLN02364 111 PDIPFHPGREDKPQPP-------------------------------------PEGR--LPDATKGCDHLRDVFAKqMGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 257 TDEETVALiAGGHTFGKAHGAHkpqdctgkepaaagleeqgmgwtnkcgkgnaedtvtSGLEGAWSANPTAWTTQYLDNL 336
Cdd:PLN02364 152 SDKDIVAL-SGAHTLGRCHKDR------------------------------------SGFEGAWTSNPLIFDNSYFKEL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 337 FAfdwvqtkspgghiqwipangqaanlvpdahipGKRSAPIMFTTDIALKEDPIYREISLRFKEDPKQFELAFAKAWFKL 416
Cdd:PLN02364 195 LS--------------------------------GEKEGLLQLVSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHMKL 242
|
.
gi 496273277 417 T 417
Cdd:PLN02364 243 S 243
|
|
| catalase_peroxidase_2 |
cd08200 |
C-terminal non-catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ... |
71-188 |
1.64e-14 |
|
C-terminal non-catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Catalase-peroxidases can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. These enzymes are found in many archaeal and bacterial organisms where they neutralize potentially lethal hydrogen peroxide molecules generated during photosynthesis or stationary phase. Along with related intracellular fungal and plant peroxidases, catalase-peroxidases belong to plant peroxidase superfamily. Unlike the eukaryotic enzymes, they are typically comprised of two homologous domains that probably arose via a single gene duplication event. The heme binding motif is present only in the N-terminal domain; the function of the C-terminal domain is not clear.
Pssm-ID: 173828 Cd Length: 297 Bit Score: 74.96 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 71 DLAAVKADI-ETLLKTSQdwwpadwghygpfMIRMAWHSAGVYRIFDGRGGANGGQQRFEPLNSWPDN--ANLDKARRLL 147
Cdd:cd08200 15 DIAALKAKIlASGLTVSE-------------LVSTAWASASTFRNSDKRGGANGARIRLAPQKDWEVNepEELAKVLAVL 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 496273277 148 WPIKQKY------GSKISWADLMVLTGNVALES----MGFK-TFGFAGGRTD 188
Cdd:cd08200 82 EGIQKEFnesqsgGKKVSLADLIVLGGCAAVEKaakdAGVDiKVPFTPGRTD 133
|
|
| ascorbate_peroxidase |
cd00691 |
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ... |
473-734 |
1.03e-11 |
|
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Along with related catalase-peroxidases, ascorbate peroxidases belong to class I of the plant superfamily. Ascorbate peroxidases are found in the chloroplasts and/or cytosol of algae and plants, where they have been shown to control the concentration of lethal hydrogen peroxide molecules. The yeast cytochrome c peroxidase is a divergent member of the family; it forms a complex with cytochrome c to catalyze the reduction of hydrogen peroxide to water.
Pssm-ID: 173825 [Multi-domain] Cd Length: 253 Bit Score: 65.69 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 473 LVKTAWASAASFRGTDMRGGANGArLRLEPQKDWAANDPQELAqvLAVLEKVQTDFnktlrggKKVSLADVIVLGGAAAI 552
Cdd:cd00691 33 LVRLAWHDSGTYDKETKTGGSNGT-IRFDPELNHGANAGLDIA--RKLLEPIKKKY-------PDISYADLWQLAGVVAI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 553 EKAAkdagfNITVPFTPGRTDATQAQTDAESFAVlePKADGfrnyyssdamysPAEALVDRANMLTLTVPEMTVLVGGL- 631
Cdd:cd00691 103 EEMG-----GPKIPFRPGRVDASDPEECPPEGRL--PDASK------------GADHLRDVFYRMGFNDQEIVALSGAHt 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 632 --RVLDVNSGgsKHGVFTDKPGQLSNDFFVNLLDmstRWAKAEQEGLydgfdrksgerkyTATPVDLVFGSHAELRAVAE 709
Cdd:cd00691 164 lgRCHKERSG--YDGPWTKNPLKFDNSYFKELLE---EDWKLPTPGL-------------LMLPTDKALLEDPKFRPYVE 225
|
250 260
....*....|....*....|....*
gi 496273277 710 VYAANdgKEKFVRDFVAAWNKVMTL 734
Cdd:cd00691 226 LYAKD--QDAFFKDYAEAHKKLSEL 248
|
|
| plant_peroxidase_like_1 |
cd08201 |
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ... |
91-281 |
1.08e-07 |
|
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent peroxidases similar to plant peroxidases. Along with animal peroxidases, these enzymes belong to a group of peroxidases containing a heme prosthetic group (ferriprotoporphyrin IX) which catalyzes a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. The plant peroxidase-like superfamily is found in all three kingdoms of life and carries out a variety of biosynthetic and degradative functions.
Pssm-ID: 173829 Cd Length: 264 Bit Score: 54.01 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 91 PADWghygpfmIRMAWHSAGVYRIFDGRGGANGGQQrFEpLNSwPDN--ANLDKARRLLWPIkqkYGSKISWADLMVLTG 168
Cdd:cd08201 42 AAEW-------LRTAFHDMATHNVDDGTGGLDASIQ-YE-LDR-PENigSGFNTTLNFFVNF---YSPRSSMADLIAMGV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 169 NVALESMGFKTFGFAGGRTDDWEAeivnwgsekewldnkrynekgelarplgatqmgliyvnpeGPNGVPDPLASAKEIR 248
Cdd:cd08201 109 VTSVASCGGPVVPFRAGRIDATEA----------------------------------------GQAGVPEPQTDLGTTT 148
|
170 180 190
....*....|....*....|....*....|...
gi 496273277 249 DTFGRMAMTDEETVALIAGGHTFGKAHGAHKPQ 281
Cdd:cd08201 149 ESFRRQGFSTSEMIALVACGHTLGGVHSEDFPE 181
|
|
| catalase_peroxidase_1 |
cd00649 |
N-terminal catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ... |
474-580 |
1.45e-06 |
|
N-terminal catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Catalase-peroxidases can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. These enzymes are found in many archaeal and bacterial organisms, where they neutralize potentially lethal hydrogen peroxide molecules generated during photosynthesis or stationary phase. Along with related intracellular fungal and plant peroxidases, catalase-peroxidases belong to class I of the plant peroxidase superfamily. Unlike the eukaryotic enzymes, they are typically comprised of two homologous domains that probably arose via a single gene duplication event. The heme binding motif is present only in the N-terminal domain; the function of the C-terminal domain is not clear.
Pssm-ID: 173824 [Multi-domain] Cd Length: 409 Bit Score: 51.15 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 474 VKTAWASAASFRGTDMRGGANGARLRLEPQKDWAANDPQELAQVLavLEKVQTDFnktlrgGKKVSLADVIVLGGAAAIE 553
Cdd:cd00649 74 IRMAWHSAGTYRIADGRGGAGTGQQRFAPLNSWPDNVNLDKARRL--LWPIKQKY------GNKISWADLMILAGNVALE 145
|
90 100
....*....|....*....|....*..
gi 496273277 554 kaakDAGFNiTVPFTPGRTDATQAQTD 580
Cdd:cd00649 146 ----SMGFK-TFGFAGGREDVWEPDED 167
|
|
| secretory_peroxidase |
cd00693 |
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ... |
238-275 |
5.47e-04 |
|
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong to class III of the plant heme-dependent peroxidase superfamily. All members of the superfamily share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Class III peroxidases are found in the extracellular space or in the vacuole in plants where they have been implicated in hydrogen peroxide detoxification, auxin catabolism and lignin biosynthesis, and stress response. Class III peroxidases contain four conserved disulphide bridges and two conserved calcium binding sites.
Pssm-ID: 173827 [Multi-domain] Cd Length: 298 Bit Score: 42.50 E-value: 5.47e-04
10 20 30
....*....|....*....|....*....|....*...
gi 496273277 238 PDPLASAKEIRDTFGRMAMTDEETVALiAGGHTFGKAH 275
Cdd:cd00693 137 PSPFFSVSQLISLFASKGLTVTDLVAL-SGAHTIGRAH 173
|
|
| PLN02364 |
PLN02364 |
L-ascorbate peroxidase 1 |
442-734 |
1.22e-03 |
|
L-ascorbate peroxidase 1
Pssm-ID: 166005 Cd Length: 250 Bit Score: 41.22 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 442 PIPAVDYKLIESRDINALKGkLLSSGLTVQQLVKTAWASAASFRGTDMRGGANGArLRLEPQKDWAANDPQELAqvLAVL 521
Cdd:PLN02364 6 PTVSEDYKKAVEKCRRKLRG-LIAEKNCAPIMVRLAWHSAGTFDCQSRTGGPFGT-MRFDAEQAHGANSGIHIA--LRLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 522 EKVQTDFnktlrggKKVSLADVIVLGGAAAIEKAAKDagfniTVPFTPGRTDATQAQTDAEsFAVLEPKADGFRNYYssd 601
Cdd:PLN02364 82 DPIREQF-------PTISFADFHQLAGVVAVEVTGGP-----DIPFHPGREDKPQPPPEGR-LPDATKGCDHLRDVF--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496273277 602 amyspaealvdrANMLTLTVPEMTVLVGGLRVLDVNSGGSK-HGVFTDKPGQLSNDFFVNLLdmstrwaKAEQEGLYDGF 680
Cdd:PLN02364 146 ------------AKQMGLSDKDIVALSGAHTLGRCHKDRSGfEGAWTSNPLIFDNSYFKELL-------SGEKEGLLQLV 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 496273277 681 DRKsgerkytATPVDLVFgshaelRAVAEVYAANDgkEKFVRDFVAAWNKVMTL 734
Cdd:PLN02364 207 SDK-------ALLDDPVF------RPLVEKYAADE--DAFFADYAEAHMKLSEL 245
|
|
| |
