|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15061 |
PRK15061 |
catalase/peroxidase; |
3-715 |
0e+00 |
|
catalase/peroxidase;
Pssm-ID: 237891 [Multi-domain] Cd Length: 726 Bit Score: 1370.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 3 RSNQDWWPDQLQVEILDQNAQQVDPMGEEFDYAEEFQKLDFEAVKEDIEEVMTSSQDWWPADYGTYGPLFIRMAWHSAGT 82
Cdd:PRK15061 16 TSNRDWWPNQLNLDILHQHSSKSNPMGEDFDYAEEFKKLDLEALKKDLKALMTDSQDWWPADYGHYGPLFIRMAWHSAGT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 83 YRTFDGRGGASGGHQRLPPVDSWPDNANLDKARRLLWPVKQKYGRQLSWGDLIVLAGNVALESMGFETFGFGGGREDDYT 162
Cdd:PRK15061 96 YRIGDGRGGAGGGQQRFAPLNSWPDNVNLDKARRLLWPIKQKYGNKISWADLMILAGNVALESMGFKTFGFAGGREDVWE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 163 PDAAVDWGPEDEFeMSSEERFDEEGNLKWPLGNTVMGLIYVNPEGPNGEPDLEGSAKNIRESFGQMAMNDEETVALIAGG 242
Cdd:PRK15061 176 PEEDVYWGPEKEW-LGGDERYSGERDLENPLAAVQMGLIYVNPEGPNGNPDPLAAARDIRETFARMAMNDEETVALIAGG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 243 HTFGKVHGADDPDeHVGSEPAAAPIEEQGLGWESDFGEGKGPDTITSGIEGPWNTTPTQWDMSYVDNLLDHEWVPEKGPG 322
Cdd:PRK15061 255 HTFGKTHGAGDAS-HVGPEPEAAPIEEQGLGWKNSYGSGKGADTITSGLEGAWTTTPTQWDNGYFENLFGYEWELTKSPA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 323 GAWQWTTEEGELDNAAPGVQDPSDKEDVMMLTTDVALKRDPDYREVLEHFQENPRDFQEAFAKAWYKLIHRDMGPPERFL 402
Cdd:PRK15061 334 GAWQWVPKDGAAEDTVPDAHDPSKKHAPTMLTTDLALRFDPEYEKISRRFLENPEEFADAFARAWFKLTHRDMGPKSRYL 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 403 GPEVPDEVMIWQDPVPDADYDLIGEAEIAELKEEVLASELSISQLVKTAWASASTYRDSDKRGGANGARLRLEPQKSWEM 482
Cdd:PRK15061 414 GPEVPKEDLIWQDPVPAVDHELIDDADIAALKAKILASGLSVSELVSTAWASASTFRGSDKRGGANGARIRLAPQKDWEV 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 483 NEPAELESVLSTLEEIREEFNGSRSDDVRVSLADLIVLGGNAAVEQAAADAGYDVTIPFEPGRTDATQEQTDVESFEALK 562
Cdd:PRK15061 494 NEPAQLAKVLAVLEGIQAEFNAAQSGGKKVSLADLIVLGGNAAVEQAAKAAGHDVTVPFTPGRTDATQEQTDVESFAVLE 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 563 PNADGFRNYLGDDLERQPEELLVDKAELLNLTANEMTVMVGGMRALGANYQDSDLGVFTDQPETLTNDFFVNLLDMDYEW 642
Cdd:PRK15061 574 PKADGFRNYLKKGYSVSPEELLVDKAQLLTLTAPEMTVLVGGLRVLGANYGGSKHGVFTDRPGVLTNDFFVNLLDMGTEW 653
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2279600791 643 EPVSDSNEVFEVRDRETGAVEWEASRVDLIFGSNSRLRTISEVYGSDDAEEKFVQDFADTWNKVMMLDRFDLE 715
Cdd:PRK15061 654 KPTDEDEEVYEGRDRKTGEVKWTATRVDLVFGSNSQLRALAEVYASDDAKEKFVRDFVAAWTKVMNLDRFDLA 726
|
|
| KatG |
COG0376 |
Catalase (peroxidase I) [Inorganic ion transport and metabolism]; |
3-714 |
0e+00 |
|
Catalase (peroxidase I) [Inorganic ion transport and metabolism];
Pssm-ID: 440145 [Multi-domain] Cd Length: 731 Bit Score: 1351.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 3 RSNQDWWPDQLQVEILDQNAQQVDPMGEEFDYAEEFQKLDFEAVKEDIEEVMTSSQDWWPADYGTYGPLFIRMAWHSAGT 82
Cdd:COG0376 22 TSNRDWWPNQLNLSILHQHSPKSNPMGEDFDYAEAFKKLDLDAVKKDLKALMTDSQDWWPADYGHYGPLFIRMAWHSAGT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 83 YRTFDGRGGASGGHQRLPPVDSWPDNANLDKARRLLWPVKQKYGRQLSWGDLIVLAGNVALESMGFETFGFGGGREDDYT 162
Cdd:COG0376 102 YRIGDGRGGAGGGQQRFAPLNSWPDNANLDKARRLLWPIKQKYGNKISWADLMILAGNVALESMGFKTFGFAGGREDVWE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 163 PDAAVDWGPEDEFEMSseERFDEEGNLKWPLGNTVMGLIYVNPEGPNGEPDLEGSAKNIRESFGQMAMNDEETVALIAGG 242
Cdd:COG0376 182 PEEDVYWGPETEWLGD--ERYSGDRELENPLAAVQMGLIYVNPEGPNGNPDPLAAARDIRETFGRMAMNDEETVALIAGG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 243 HTFGKVHGADDPDeHVGSEPAAAPIEEQGLGWESDFGEGKGPDTITSGIEGPWNTTPTQWDMSYVDNLLDHEWVPEKGPG 322
Cdd:COG0376 260 HTFGKTHGAGDAE-HVGPEPEAAPIEEQGLGWKNSFGSGKGEDTITSGLEGAWTPTPTQWDNGYFDNLFGYEWELTKSPA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 323 GAWQWTTEEGELDNAAPGVQDPSDKEDVMMLTTDVALKRDPDYREVLEHFQENPRDFQEAFAKAWYKLIHRDMGPPERFL 402
Cdd:COG0376 339 GAHQWVPKDGAAADTVPDAHDPSKRHAPMMLTTDLALRFDPAYEKISRRFLENPEEFADAFARAWFKLTHRDMGPKSRYL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 403 GPEVPDEVMIWQDPVPDADYDLIGEAEIAELKEEVLASELSISQLVKTAWASASTYRDSDKRGGANGARLRLEPQKSWEM 482
Cdd:COG0376 419 GPEVPAEELIWQDPIPAVDHELIDDADIAALKAKILASGLSVSELVSTAWASASTFRGSDKRGGANGARIRLAPQKDWEV 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 483 NEPAELESVLSTLEEIREEFNGSRSDDVRVSLADLIVLGGNAAVEQAAADAGYDVTIPFEPGRTDATQEQTDVESFEALK 562
Cdd:COG0376 499 NEPEQLAKVLAVLEGIQKDFNAAQSGGKKVSLADLIVLGGCAAVEKAAKDAGHDVTVPFTPGRTDATQEQTDVESFAVLE 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 563 PNADGFRNYLGDDLERQPEELLVDKAELLNLTANEMTVMVGGMRALGANYQDSDLGVFTDQPETLTNDFFVNLLDMDYEW 642
Cdd:COG0376 579 PKADGFRNYLKKGYSVSAEELLVDKAQLLTLTAPEMTVLVGGLRVLGANYGGSKHGVFTDRPGTLTNDFFVNLLDMGTEW 658
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2279600791 643 EPVSDSNEVFEVRDRETGAVEWEASRVDLIFGSNSRLRTISEVYGSDDAEEKFVQDFADTWNKVMMLDRFDL 714
Cdd:COG0376 659 KPSSDDEGLFEGRDRKTGEVKWTATRVDLVFGSNSELRALAEVYASDDAKEKFVKDFVAAWTKVMNLDRFDL 730
|
|
| cat_per_HPI |
TIGR00198 |
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ... |
5-714 |
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: 955.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 5 NQDWWPDQLQVEILDQNAQQVDPMGEEFDYAEEFQKLDFEAVKEDIEEVMTSSQDWWPADYGTYGPLFIRMAWHSAGTYR 84
Cdd:TIGR00198 16 TGDWWPNALNLDILHQHDRKTNPMGEDFDYAEEFQQLDLAAVKQDLKHLMTDSQSWWPADWGHYGGLFIRMAWHAAGTYR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 85 TFDGRGGASGGHQRLPPVDSWPDNANLDKARRLLWPVKQKYGRQLSWGDLIVLAGNVALESMGFETFGFGGGREDDYTPD 164
Cdd:TIGR00198 96 IADGRGGAATGNQRFAPLNSWPDNVNLDKARRLLWPIKKKYGNKLSWADLIILAGTVAYESMGLKVFGFAGGREDIWEPD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 165 AAVDWGPEDEFEMSSEErfdEEGNLKWPLGNTVMGLIYVNPEGPNGEPDLEGSAKNIRESFGQMAMNDEETVALIAGGHT 244
Cdd:TIGR00198 176 KDIYWGAEKEWLTSSRE---DRESLENPLAATEMGLIYVNPEGPDGHPDPLCTAQDIRTTFARMGMNDEETVALIAGGHT 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 245 FGKVHGADdPDEHVGSEPAAAPIEEQGLGWESDFGEGKGPDTITSGIEGPWNTTPTQWDMSYVDNLLDHEWVPEKGPGGA 324
Cdd:TIGR00198 253 VGKCHGAG-PAELIGPDPEGAPIEEQGLGWHNQYGKGVGRDTMTSGLEVAWTTTPTQWDNGYFYMLFNYEWELKKSPAGA 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 325 WQWttEEGELDNAAPGVQDPSDKEDVMMLTTDVALKRDPDYREVLEHFQENPRDFQEAFAKAWYKLIHRDMGPPERFLGP 404
Cdd:TIGR00198 332 WQW--EAVDAPEIIPDVEDPNKKHNPIMLDADLALRFDPEFRKISRRFLREPDYFAEAFAKAWFKLTHRDMGPKSRYIGP 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 405 EVPDEVMIWQDPVPDADYDLIgEAEIAELKEEVLASELSISQLVKTAWASASTYRDSDKRGGANGARLRLEPQKSWEMNE 484
Cdd:TIGR00198 410 DVPQEDLIWQDPLPPVDYTLS-EGDIKELKQQILASGLSVSELVCTAWASASTFRSSDYRGGANGARIRLEPQKNWPVNE 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 485 PAELESVLSTLEEIREEFNGSRsddvrVSLADLIVLGGNAAVEQAAADAGYDVTIPFEPGRTDATQEQTDVESFEALKPN 564
Cdd:TIGR00198 489 PTRLAKVLAVLEKIQAEFAKGP-----VSLADLIVLGGGAAVEKAALDAGISVNVPFLPGRVDATQAMTDAESFTPLEPI 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 565 ADGFRNYLGDDLERQPEELLVDKAELLNLTANEMTVMVGGMRALGANYQDSDLGVFTDQPETLTNDFFVNLLDMDYEWEP 644
Cdd:TIGR00198 564 ADGFRNYLKRDYAVTPEELLLDKAQLLTLTAPEMTVLIGGMRVLGANHGGSKHGVFTDRVGVLSNDFFVNLLDMAYEWRA 643
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 645 VSDSNEVFEVRDRETGAVEWEASRVDLIFGSNSRLRTISEVYGSDDAEEKFVQDFADTWNKVMMLDRFDL 714
Cdd:TIGR00198 644 ADNNRYLFEGGDRQTGEVKWTATRVDLVFGSNSILRAVAEVYAQDDAREKFVKDFVAAWTKVMNLDRFDL 713
|
|
| catalase_peroxidase_1 |
cd00649 |
N-terminal catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ... |
3-411 |
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: 702.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 3 RSNQDWWPDQLQVEILDQNAQQVDPMGEEFDYAEEFQKLDFEAVKEDIEEVMTSSQDWWPADYGTYGPLFIRMAWHSAGT 82
Cdd:cd00649 4 TSNQDWWPNRLNLKILHQHSPKSNPMGEDFNYAEEFKKLDLEALKEDLKALMTDSQDWWPADYGHYGPLFIRMAWHSAGT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 83 YRTFDGRGGASGGHQRLPPVDSWPDNANLDKARRLLWPVKQKYGRQLSWGDLIVLAGNVALESMGFETFGFGGGREDDYT 162
Cdd:cd00649 84 YRIADGRGGAGTGQQRFAPLNSWPDNVNLDKARRLLWPIKQKYGNKISWADLMILAGNVALESMGFKTFGFAGGREDVWE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 163 PDAAVDWGPEDEFEmsSEERFDEEGNLKWPLGNTVMGLIYVNPEGPNGEPDLEGSAKNIRESFGQMAMNDEETVALIAGG 242
Cdd:cd00649 164 PDEDVYWGPEKEWL--ADKRYSGDRDLENPLAAVQMGLIYVNPEGPDGNPDPLAAAKDIRETFARMAMNDEETVALIAGG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 243 HTFGKVHGADDPDeHVGSEPAAAPIEEQGLGWESDFGEGKGPDTITSGIEGPWNTTPTQWDMSYVDNLLDHEWVPEKGPG 322
Cdd:cd00649 242 HTFGKTHGAGPAS-HVGPEPEAAPIEQQGLGWKNSYGTGKGKDTITSGLEGAWTPTPTKWDNNYLKNLFGYEWELTKSPA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 323 GAWQWTTEEGELDNAAPGVQDPSDKEDVMMLTTDVALKRDPDYREVLEHFQENPRDFQEAFAKAWYKLIHRDMGPPERFL 402
Cdd:cd00649 321 GAWQWVPKNAAGENTVPDAHDPSKKHAPMMLTTDLALRFDPEYEKISRRFLENPDEFADAFAKAWFKLTHRDMGPKSRYL 400
|
....*....
gi 2279600791 403 GPEVPDEVM 411
Cdd:cd00649 401 GPEVPEEDL 409
|
|
| peroxidase |
pfam00141 |
Peroxidase; |
61-249 |
1.39e-26 |
|
Peroxidase;
Pssm-ID: 425483 [Multi-domain] Cd Length: 187 Bit Score: 107.27 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 61 WPADYGTYGPLFIRMAWHSAGTyrtfdgrGGASGGHQRLPPVD--SWPDNANLDKARRLLWPVKQKY----GRQLSWGDL 134
Cdd:pfam00141 8 AFKADPTMGPSLLRLHFHDCFV-------GGCDGSVLLDGFKPekDAPPNLGLRKGFEVIDDIKAKLeaacPGVVSCADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 135 IVLAGNVALESMGFETFGFGGGREDDYTPDaAVDWGpedefemsseerfdeegnlkwplgntvmgliyvnpegpNGEPDL 214
Cdd:pfam00141 81 LALAARDAVELAGGPSWPVPLGRRDGTVSS-AVEAN--------------------------------------SNLPAP 121
|
170 180 190
....*....|....*....|....*....|....*
gi 2279600791 215 EGSAKNIRESFGQMAMNDEETVALiAGGHTFGKVH 249
Cdd:pfam00141 122 TDSLDQLRDRFARKGLTAEDLVAL-SGAHTIGRAH 155
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15061 |
PRK15061 |
catalase/peroxidase; |
3-715 |
0e+00 |
|
catalase/peroxidase;
Pssm-ID: 237891 [Multi-domain] Cd Length: 726 Bit Score: 1370.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 3 RSNQDWWPDQLQVEILDQNAQQVDPMGEEFDYAEEFQKLDFEAVKEDIEEVMTSSQDWWPADYGTYGPLFIRMAWHSAGT 82
Cdd:PRK15061 16 TSNRDWWPNQLNLDILHQHSSKSNPMGEDFDYAEEFKKLDLEALKKDLKALMTDSQDWWPADYGHYGPLFIRMAWHSAGT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 83 YRTFDGRGGASGGHQRLPPVDSWPDNANLDKARRLLWPVKQKYGRQLSWGDLIVLAGNVALESMGFETFGFGGGREDDYT 162
Cdd:PRK15061 96 YRIGDGRGGAGGGQQRFAPLNSWPDNVNLDKARRLLWPIKQKYGNKISWADLMILAGNVALESMGFKTFGFAGGREDVWE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 163 PDAAVDWGPEDEFeMSSEERFDEEGNLKWPLGNTVMGLIYVNPEGPNGEPDLEGSAKNIRESFGQMAMNDEETVALIAGG 242
Cdd:PRK15061 176 PEEDVYWGPEKEW-LGGDERYSGERDLENPLAAVQMGLIYVNPEGPNGNPDPLAAARDIRETFARMAMNDEETVALIAGG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 243 HTFGKVHGADDPDeHVGSEPAAAPIEEQGLGWESDFGEGKGPDTITSGIEGPWNTTPTQWDMSYVDNLLDHEWVPEKGPG 322
Cdd:PRK15061 255 HTFGKTHGAGDAS-HVGPEPEAAPIEEQGLGWKNSYGSGKGADTITSGLEGAWTTTPTQWDNGYFENLFGYEWELTKSPA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 323 GAWQWTTEEGELDNAAPGVQDPSDKEDVMMLTTDVALKRDPDYREVLEHFQENPRDFQEAFAKAWYKLIHRDMGPPERFL 402
Cdd:PRK15061 334 GAWQWVPKDGAAEDTVPDAHDPSKKHAPTMLTTDLALRFDPEYEKISRRFLENPEEFADAFARAWFKLTHRDMGPKSRYL 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 403 GPEVPDEVMIWQDPVPDADYDLIGEAEIAELKEEVLASELSISQLVKTAWASASTYRDSDKRGGANGARLRLEPQKSWEM 482
Cdd:PRK15061 414 GPEVPKEDLIWQDPVPAVDHELIDDADIAALKAKILASGLSVSELVSTAWASASTFRGSDKRGGANGARIRLAPQKDWEV 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 483 NEPAELESVLSTLEEIREEFNGSRSDDVRVSLADLIVLGGNAAVEQAAADAGYDVTIPFEPGRTDATQEQTDVESFEALK 562
Cdd:PRK15061 494 NEPAQLAKVLAVLEGIQAEFNAAQSGGKKVSLADLIVLGGNAAVEQAAKAAGHDVTVPFTPGRTDATQEQTDVESFAVLE 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 563 PNADGFRNYLGDDLERQPEELLVDKAELLNLTANEMTVMVGGMRALGANYQDSDLGVFTDQPETLTNDFFVNLLDMDYEW 642
Cdd:PRK15061 574 PKADGFRNYLKKGYSVSPEELLVDKAQLLTLTAPEMTVLVGGLRVLGANYGGSKHGVFTDRPGVLTNDFFVNLLDMGTEW 653
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2279600791 643 EPVSDSNEVFEVRDRETGAVEWEASRVDLIFGSNSRLRTISEVYGSDDAEEKFVQDFADTWNKVMMLDRFDLE 715
Cdd:PRK15061 654 KPTDEDEEVYEGRDRKTGEVKWTATRVDLVFGSNSQLRALAEVYASDDAKEKFVRDFVAAWTKVMNLDRFDLA 726
|
|
| KatG |
COG0376 |
Catalase (peroxidase I) [Inorganic ion transport and metabolism]; |
3-714 |
0e+00 |
|
Catalase (peroxidase I) [Inorganic ion transport and metabolism];
Pssm-ID: 440145 [Multi-domain] Cd Length: 731 Bit Score: 1351.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 3 RSNQDWWPDQLQVEILDQNAQQVDPMGEEFDYAEEFQKLDFEAVKEDIEEVMTSSQDWWPADYGTYGPLFIRMAWHSAGT 82
Cdd:COG0376 22 TSNRDWWPNQLNLSILHQHSPKSNPMGEDFDYAEAFKKLDLDAVKKDLKALMTDSQDWWPADYGHYGPLFIRMAWHSAGT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 83 YRTFDGRGGASGGHQRLPPVDSWPDNANLDKARRLLWPVKQKYGRQLSWGDLIVLAGNVALESMGFETFGFGGGREDDYT 162
Cdd:COG0376 102 YRIGDGRGGAGGGQQRFAPLNSWPDNANLDKARRLLWPIKQKYGNKISWADLMILAGNVALESMGFKTFGFAGGREDVWE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 163 PDAAVDWGPEDEFEMSseERFDEEGNLKWPLGNTVMGLIYVNPEGPNGEPDLEGSAKNIRESFGQMAMNDEETVALIAGG 242
Cdd:COG0376 182 PEEDVYWGPETEWLGD--ERYSGDRELENPLAAVQMGLIYVNPEGPNGNPDPLAAARDIRETFGRMAMNDEETVALIAGG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 243 HTFGKVHGADDPDeHVGSEPAAAPIEEQGLGWESDFGEGKGPDTITSGIEGPWNTTPTQWDMSYVDNLLDHEWVPEKGPG 322
Cdd:COG0376 260 HTFGKTHGAGDAE-HVGPEPEAAPIEEQGLGWKNSFGSGKGEDTITSGLEGAWTPTPTQWDNGYFDNLFGYEWELTKSPA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 323 GAWQWTTEEGELDNAAPGVQDPSDKEDVMMLTTDVALKRDPDYREVLEHFQENPRDFQEAFAKAWYKLIHRDMGPPERFL 402
Cdd:COG0376 339 GAHQWVPKDGAAADTVPDAHDPSKRHAPMMLTTDLALRFDPAYEKISRRFLENPEEFADAFARAWFKLTHRDMGPKSRYL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 403 GPEVPDEVMIWQDPVPDADYDLIGEAEIAELKEEVLASELSISQLVKTAWASASTYRDSDKRGGANGARLRLEPQKSWEM 482
Cdd:COG0376 419 GPEVPAEELIWQDPIPAVDHELIDDADIAALKAKILASGLSVSELVSTAWASASTFRGSDKRGGANGARIRLAPQKDWEV 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 483 NEPAELESVLSTLEEIREEFNGSRSDDVRVSLADLIVLGGNAAVEQAAADAGYDVTIPFEPGRTDATQEQTDVESFEALK 562
Cdd:COG0376 499 NEPEQLAKVLAVLEGIQKDFNAAQSGGKKVSLADLIVLGGCAAVEKAAKDAGHDVTVPFTPGRTDATQEQTDVESFAVLE 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 563 PNADGFRNYLGDDLERQPEELLVDKAELLNLTANEMTVMVGGMRALGANYQDSDLGVFTDQPETLTNDFFVNLLDMDYEW 642
Cdd:COG0376 579 PKADGFRNYLKKGYSVSAEELLVDKAQLLTLTAPEMTVLVGGLRVLGANYGGSKHGVFTDRPGTLTNDFFVNLLDMGTEW 658
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2279600791 643 EPVSDSNEVFEVRDRETGAVEWEASRVDLIFGSNSRLRTISEVYGSDDAEEKFVQDFADTWNKVMMLDRFDL 714
Cdd:COG0376 659 KPSSDDEGLFEGRDRKTGEVKWTATRVDLVFGSNSELRALAEVYASDDAKEKFVKDFVAAWTKVMNLDRFDL 730
|
|
| cat_per_HPI |
TIGR00198 |
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ... |
5-714 |
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: 955.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 5 NQDWWPDQLQVEILDQNAQQVDPMGEEFDYAEEFQKLDFEAVKEDIEEVMTSSQDWWPADYGTYGPLFIRMAWHSAGTYR 84
Cdd:TIGR00198 16 TGDWWPNALNLDILHQHDRKTNPMGEDFDYAEEFQQLDLAAVKQDLKHLMTDSQSWWPADWGHYGGLFIRMAWHAAGTYR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 85 TFDGRGGASGGHQRLPPVDSWPDNANLDKARRLLWPVKQKYGRQLSWGDLIVLAGNVALESMGFETFGFGGGREDDYTPD 164
Cdd:TIGR00198 96 IADGRGGAATGNQRFAPLNSWPDNVNLDKARRLLWPIKKKYGNKLSWADLIILAGTVAYESMGLKVFGFAGGREDIWEPD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 165 AAVDWGPEDEFEMSSEErfdEEGNLKWPLGNTVMGLIYVNPEGPNGEPDLEGSAKNIRESFGQMAMNDEETVALIAGGHT 244
Cdd:TIGR00198 176 KDIYWGAEKEWLTSSRE---DRESLENPLAATEMGLIYVNPEGPDGHPDPLCTAQDIRTTFARMGMNDEETVALIAGGHT 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 245 FGKVHGADdPDEHVGSEPAAAPIEEQGLGWESDFGEGKGPDTITSGIEGPWNTTPTQWDMSYVDNLLDHEWVPEKGPGGA 324
Cdd:TIGR00198 253 VGKCHGAG-PAELIGPDPEGAPIEEQGLGWHNQYGKGVGRDTMTSGLEVAWTTTPTQWDNGYFYMLFNYEWELKKSPAGA 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 325 WQWttEEGELDNAAPGVQDPSDKEDVMMLTTDVALKRDPDYREVLEHFQENPRDFQEAFAKAWYKLIHRDMGPPERFLGP 404
Cdd:TIGR00198 332 WQW--EAVDAPEIIPDVEDPNKKHNPIMLDADLALRFDPEFRKISRRFLREPDYFAEAFAKAWFKLTHRDMGPKSRYIGP 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 405 EVPDEVMIWQDPVPDADYDLIgEAEIAELKEEVLASELSISQLVKTAWASASTYRDSDKRGGANGARLRLEPQKSWEMNE 484
Cdd:TIGR00198 410 DVPQEDLIWQDPLPPVDYTLS-EGDIKELKQQILASGLSVSELVCTAWASASTFRSSDYRGGANGARIRLEPQKNWPVNE 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 485 PAELESVLSTLEEIREEFNGSRsddvrVSLADLIVLGGNAAVEQAAADAGYDVTIPFEPGRTDATQEQTDVESFEALKPN 564
Cdd:TIGR00198 489 PTRLAKVLAVLEKIQAEFAKGP-----VSLADLIVLGGGAAVEKAALDAGISVNVPFLPGRVDATQAMTDAESFTPLEPI 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 565 ADGFRNYLGDDLERQPEELLVDKAELLNLTANEMTVMVGGMRALGANYQDSDLGVFTDQPETLTNDFFVNLLDMDYEWEP 644
Cdd:TIGR00198 564 ADGFRNYLKRDYAVTPEELLLDKAQLLTLTAPEMTVLIGGMRVLGANHGGSKHGVFTDRVGVLSNDFFVNLLDMAYEWRA 643
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 645 VSDSNEVFEVRDRETGAVEWEASRVDLIFGSNSRLRTISEVYGSDDAEEKFVQDFADTWNKVMMLDRFDL 714
Cdd:TIGR00198 644 ADNNRYLFEGGDRQTGEVKWTATRVDLVFGSNSILRAVAEVYAQDDAREKFVKDFVAAWTKVMNLDRFDL 713
|
|
| catalase_peroxidase_1 |
cd00649 |
N-terminal catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ... |
3-411 |
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: 702.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 3 RSNQDWWPDQLQVEILDQNAQQVDPMGEEFDYAEEFQKLDFEAVKEDIEEVMTSSQDWWPADYGTYGPLFIRMAWHSAGT 82
Cdd:cd00649 4 TSNQDWWPNRLNLKILHQHSPKSNPMGEDFNYAEEFKKLDLEALKEDLKALMTDSQDWWPADYGHYGPLFIRMAWHSAGT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 83 YRTFDGRGGASGGHQRLPPVDSWPDNANLDKARRLLWPVKQKYGRQLSWGDLIVLAGNVALESMGFETFGFGGGREDDYT 162
Cdd:cd00649 84 YRIADGRGGAGTGQQRFAPLNSWPDNVNLDKARRLLWPIKQKYGNKISWADLMILAGNVALESMGFKTFGFAGGREDVWE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 163 PDAAVDWGPEDEFEmsSEERFDEEGNLKWPLGNTVMGLIYVNPEGPNGEPDLEGSAKNIRESFGQMAMNDEETVALIAGG 242
Cdd:cd00649 164 PDEDVYWGPEKEWL--ADKRYSGDRDLENPLAAVQMGLIYVNPEGPDGNPDPLAAAKDIRETFARMAMNDEETVALIAGG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 243 HTFGKVHGADDPDeHVGSEPAAAPIEEQGLGWESDFGEGKGPDTITSGIEGPWNTTPTQWDMSYVDNLLDHEWVPEKGPG 322
Cdd:cd00649 242 HTFGKTHGAGPAS-HVGPEPEAAPIEQQGLGWKNSYGTGKGKDTITSGLEGAWTPTPTKWDNNYLKNLFGYEWELTKSPA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 323 GAWQWTTEEGELDNAAPGVQDPSDKEDVMMLTTDVALKRDPDYREVLEHFQENPRDFQEAFAKAWYKLIHRDMGPPERFL 402
Cdd:cd00649 321 GAWQWVPKNAAGENTVPDAHDPSKKHAPMMLTTDLALRFDPEYEKISRRFLENPDEFADAFAKAWFKLTHRDMGPKSRYL 400
|
....*....
gi 2279600791 403 GPEVPDEVM 411
Cdd:cd00649 401 GPEVPEEDL 409
|
|
| catalase_peroxidase_2 |
cd08200 |
C-terminal non-catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ... |
415-711 |
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: 538.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 415 DPVPDADYDLIGEAEIAELKEEVLASELSISQLVKTAWASASTYRDSDKRGGANGARLRLEPQKSWEMNEPAELESVLST 494
Cdd:cd08200 1 DPIPAVDYELIDDADIAALKAKILASGLTVSELVSTAWASASTFRNSDKRGGANGARIRLAPQKDWEVNEPEELAKVLAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 495 LEEIREEFNGSRSDDVRVSLADLIVLGGNAAVEQAAADAGYDVTIPFEPGRTDATQEQTDVESFEALKPNADGFRNYLGD 574
Cdd:cd08200 81 LEGIQKEFNESQSGGKKVSLADLIVLGGCAAVEKAAKDAGVDIKVPFTPGRTDATQEQTDVESFEVLEPKADGFRNYLKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 575 DLERQPEELLVDKAELLNLTANEMTVMVGGMRALGANYQDSDLGVFTDQPETLTNDFFVNLLDMDYEWEPVSDSNEVFEV 654
Cdd:cd08200 161 GYRVPPEEMLVDKAQLLTLTAPEMTVLVGGLRVLGANYGGSKHGVFTDRPGVLTNDFFVNLLDMSTEWKPADEDDGLFEG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2279600791 655 RDRETGAVEWEASRVDLIFGSNSRLRTISEVYGSDDAEEKFVQDFADTWNKVMMLDR 711
Cdd:cd08200 241 RDRKTGEVKWTATRVDLVFGSNSELRAVAEVYASDDAQEKFVKDFVAAWTKVMNLDR 297
|
|
| plant_peroxidase_like |
cd00314 |
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ... |
44-392 |
1.16e-52 |
|
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: 182.74 E-value: 1.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 44 EAVKEDIEEVMTSsqdwwpadYGTYGPLFIRMAWHSAGTYRTFDGRGGASGGHQRLPPVDSWPDNANLDKARRLLWPVKQ 123
Cdd:cd00314 1 DAIKAILEDLITQ--------AGALAGSLLRLAFHDAGTYDIADGKGGGADGSIRFEPELDRPENGGLDKALRALEPIKS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 124 KYGR--QLSWGDLIVLAGNVALESMGFetfgfgggreddYTPDAAVDWGPEDEFEMSseerfdeegnlkwplgntvmgLI 201
Cdd:cd00314 73 AYDGgnPVSRADLIALAGAVAVESTFG------------GGPLIPFRFGRLDATEPD---------------------LG 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 202 YVNPEGPNGEPDLegSAKNIRESFGQMAMNDEETVALIAGGHTF-GKVHGADDPDEHvgsepaaapieeqglgwesdfge 280
Cdd:cd00314 120 VPDPEGLLPNETS--SATELRDKFKRMGLSPSELVALSAGAHTLgGKNHGDLLNYEG----------------------- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 281 gkgpdtitsgiEGPWNTTPTQWDMSYVDNLLDHEWVPEKGPGgawqwtteegeldnaapgvqDPSDKEDVMMLTTDVALK 360
Cdd:cd00314 175 -----------SGLWTSTPFTFDNAYFKNLLDMNWEWRVGSP--------------------DPDGVKGPGLLPSDYALL 223
|
330 340 350
....*....|....*....|....*....|..
gi 2279600791 361 RDPDYREVLEHFQENPRDFQEAFAKAWYKLIH 392
Cdd:cd00314 224 SDSETRALVERYASDQEKFFEDFAKAWIKMVN 255
|
|
| plant_peroxidase_like |
cd00314 |
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ... |
431-707 |
7.79e-47 |
|
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: 166.56 E-value: 7.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 431 AELKEEVLASELSISQLVKTAWASASTYRDSDKRGGANGARLRLEPQKSWEMNEPaeLESVLSTLEEIREEFNGSRSddv 510
Cdd:cd00314 5 AILEDLITQAGALAGSLLRLAFHDAGTYDIADGKGGGADGSIRFEPELDRPENGG--LDKALRALEPIKSAYDGGNP--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 511 rVSLADLIVLGGNaavEQAAADAGYDVTIPFEPGRTDATQEQTDVESFEALKPNadgfrnylgddlERQPEELLVDKAEL 590
Cdd:cd00314 80 -VSRADLIALAGA---VAVESTFGGGPLIPFRFGRLDATEPDLGVPDPEGLLPN------------ETSSATELRDKFKR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 591 LNLTANEMTVMVGGMRAL-GANYQDSD----LGVFTDQPETLTNDFFVNLLDMDYEWEPVSdsnevfevrDRETGAVEWE 665
Cdd:cd00314 144 MGLSPSELVALSAGAHTLgGKNHGDLLnyegSGLWTSTPFTFDNAYFKNLLDMNWEWRVGS---------PDPDGVKGPG 214
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2279600791 666 ASRVDLIFGSNSRLRTISEVYGSDdaEEKFVQDFADTWNKVM 707
Cdd:cd00314 215 LLPSDYALLSDSETRALVERYASD--QEKFFEDFAKAWIKMV 254
|
|
| ascorbate_peroxidase |
cd00691 |
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ... |
42-391 |
9.04e-45 |
|
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: 160.83 E-value: 9.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 42 DFEAVKEDIEEVMtssqdwwpaDYGTYGPLFIRMAWHSAGTYRTFDGRGGaSGGHQRLPPVDSWPDNANLDKARRLLWPV 121
Cdd:cd00691 12 DLEAARNDIAKLI---------DDKNCAPILVRLAWHDSGTYDKETKTGG-SNGTIRFDPELNHGANAGLDIARKLLEPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 122 KQKYgRQLSWGDLIVLAGNVALESMGFetfgfgggreddytPDAAVDWGPEDEfemSSEERFDEEGNLkwplgntvmgli 201
Cdd:cd00691 82 KKKY-PDISYADLWQLAGVVAIEEMGG--------------PKIPFRPGRVDA---SDPEECPPEGRL------------ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 202 yvnpegpngePDLEGSAKNIRESFGQMAMNDEETVALIaGGHTFGKVHgaddPDEhvgsepaaapieeqglgwesdfgeg 281
Cdd:cd00691 132 ----------PDASKGADHLRDVFYRMGFNDQEIVALS-GAHTLGRCH----KER------------------------- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 282 kgpdtitSGIEGPWNTTPTQWDMSYVDNLLDHEWVPEKGpggawqwtteegeldnaapgvqdpsdkeDVMMLTTDVALKR 361
Cdd:cd00691 172 -------SGYDGPWTKNPLKFDNSYFKELLEEDWKLPTP----------------------------GLLMLPTDKALLE 216
|
330 340 350
....*....|....*....|....*....|
gi 2279600791 362 DPDYREVLEHFQENPRDFQEAFAKAWYKLI 391
Cdd:cd00691 217 DPKFRPYVELYAKDQDAFFKDYAEAHKKLS 246
|
|
| peroxidase |
pfam00141 |
Peroxidase; |
61-249 |
1.39e-26 |
|
Peroxidase;
Pssm-ID: 425483 [Multi-domain] Cd Length: 187 Bit Score: 107.27 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 61 WPADYGTYGPLFIRMAWHSAGTyrtfdgrGGASGGHQRLPPVD--SWPDNANLDKARRLLWPVKQKY----GRQLSWGDL 134
Cdd:pfam00141 8 AFKADPTMGPSLLRLHFHDCFV-------GGCDGSVLLDGFKPekDAPPNLGLRKGFEVIDDIKAKLeaacPGVVSCADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 135 IVLAGNVALESMGFETFGFGGGREDDYTPDaAVDWGpedefemsseerfdeegnlkwplgntvmgliyvnpegpNGEPDL 214
Cdd:pfam00141 81 LALAARDAVELAGGPSWPVPLGRRDGTVSS-AVEAN--------------------------------------SNLPAP 121
|
170 180 190
....*....|....*....|....*....|....*
gi 2279600791 215 EGSAKNIRESFGQMAMNDEETVALiAGGHTFGKVH 249
Cdd:pfam00141 122 TDSLDQLRDRFARKGLTAEDLVAL-SGAHTIGRAH 155
|
|
| peroxidase |
pfam00141 |
Peroxidase; |
465-689 |
8.21e-18 |
|
Peroxidase;
Pssm-ID: 425483 [Multi-domain] Cd Length: 187 Bit Score: 81.84 E-value: 8.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 465 GGANGARLR--LEPQKSWEMNepAELESVLSTLEEIREEFNgsRSDDVRVSLADLIVLGGNaaveqaaadagyDV----- 537
Cdd:pfam00141 30 GGCDGSVLLdgFKPEKDAPPN--LGLRKGFEVIDDIKAKLE--AACPGVVSCADILALAAR------------DAvelag 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 538 --TIPFEPGRTDATQEQTdVESFEAL-KPNADgfrnylgddlerqPEELLvDKAELLNLTANEMTVMvGGMRALGANYqd 614
Cdd:pfam00141 94 gpSWPVPLGRRDGTVSSA-VEANSNLpAPTDS-------------LDQLR-DRFARKGLTAEDLVAL-SGAHTIGRAH-- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2279600791 615 sdlgvftdqpetltndffVNLLDmdyewepvsdsnevfevrdretgavEWEASRVDLIFGSNSRLRTISEVYGSD 689
Cdd:pfam00141 156 ------------------KNLLD-------------------------GRGLLTSDQALLSDPRTRALVERYAAD 187
|
|
| PLN02608 |
PLN02608 |
L-ascorbate peroxidase |
70-390 |
1.79e-16 |
|
L-ascorbate peroxidase
Pssm-ID: 178218 [Multi-domain] Cd Length: 289 Bit Score: 80.58 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 70 PLFIRMAWHSAGTYRTFDGRGGASGGhQRLPPVDSWPDNANLDKARRLLWPVKQKYGRqLSWGDLIVLAGNVALEsmgfe 149
Cdd:PLN02608 32 PIMLRLAWHDAGTYDAKTKTGGPNGS-IRNEEEYSHGANNGLKIAIDLCEPVKAKHPK-ITYADLYQLAGVVAVE----- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 150 tfgfgggreddytpdaaVDWGPEDEFEMSSEERFD--EEGNLkwplgntvmgliyvnpegpngePDLEGSAKNIRESFGQ 227
Cdd:PLN02608 105 -----------------VTGGPTIDFVPGRKDSNAcpEEGRL----------------------PDAKKGAKHLRDVFYR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 228 MAMNDEETVALiAGGHTFGKVHgaddPDEhvgsepaaapieeqglgwesdfgegkgpdtitSGIEGPWNTTPTQWDMSYV 307
Cdd:PLN02608 146 MGLSDKDIVAL-SGGHTLGRAH----PER--------------------------------SGFDGPWTKEPLKFDNSYF 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 308 DNLLdhewvpeKGpggawqwtteegeldnaapgvqdpsDKEDVMMLTTDVALKRDPDYREVLEHFQENPRDFQEAFAKAW 387
Cdd:PLN02608 189 VELL-------KG-------------------------ESEGLLKLPTDKALLEDPEFRPYVELYAKDEDAFFRDYAESH 236
|
...
gi 2279600791 388 YKL 390
Cdd:PLN02608 237 KKL 239
|
|
| PLN02879 |
PLN02879 |
L-ascorbate peroxidase |
69-390 |
8.79e-14 |
|
L-ascorbate peroxidase
Pssm-ID: 178467 [Multi-domain] Cd Length: 251 Bit Score: 71.63 E-value: 8.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 69 GPLFIRMAWHSAGTYRTFDGRGGASGGhQRLPPVDSWPDNANLDKARRLLWPVKQKYgRQLSWGDLIVLAGNVALEsmgf 148
Cdd:PLN02879 34 APIVLRLAWHSAGTFDVKTKTGGPFGT-IRHPQELAHDANNGLDIAVRLLDPIKELF-PILSYADFYQLAGVVAVE---- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 149 etfgfgggreddytpdaaVDWGPEDEFEMSseeRFDEegnlkwplgntvmgliyVNPEGPNGEPDLEGSAKNIRESFGQM 228
Cdd:PLN02879 108 ------------------ITGGPEIPFHPG---RLDK-----------------VEPPPEGRLPQATKGVDHLRDVFGRM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 229 AMNDEETVALiAGGHTFGKVHGAddpdehvgsepaaapieeqglgwesdfgegkgpdtiTSGIEGPWNTTPTQWDMSYVD 308
Cdd:PLN02879 150 GLNDKDIVAL-SGGHTLGRCHKE------------------------------------RSGFEGAWTPNPLIFDNSYFK 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 309 NLLDHEwvpekgpggawqwtteegeldnaapgvqdpsdKEDVMMLTTDVALKRDPDYREVLEHFQENPRDFQEAFAKAWY 388
Cdd:PLN02879 193 EILSGE--------------------------------KEGLLQLPTDKALLDDPLFLPFVEKYAADEDAFFEDYTEAHL 240
|
..
gi 2279600791 389 KL 390
Cdd:PLN02879 241 KL 242
|
|
| ascorbate_peroxidase |
cd00691 |
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ... |
447-643 |
3.54e-13 |
|
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: 69.93 E-value: 3.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 447 LVKTAWASASTYRDSDKRGGANGArLRLEPqkswEMNEPAE--LESVLSTLEEIREEFNgsrsddvRVSLADLIVLGGna 524
Cdd:cd00691 33 LVRLAWHDSGTYDKETKTGGSNGT-IRFDP----ELNHGANagLDIARKLLEPIKKKYP-------DISYADLWQLAG-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 525 aveqaaadagydVT---------IPFEPGRTDATQEQTDVEsfEALKPNADGFRNYLGDDLERqpeellvdkaelLNLTA 595
Cdd:cd00691 99 ------------VVaieemggpkIPFRPGRVDASDPEECPP--EGRLPDASKGADHLRDVFYR------------MGFND 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2279600791 596 NEMTVMVGGmRALGANYQD-SDL-GVFTDQPETLTNDFFVNLLDMDYEWE 643
Cdd:cd00691 153 QEIVALSGA-HTLGRCHKErSGYdGPWTKNPLKFDNSYFKELLEEDWKLP 201
|
|
| PLN02364 |
PLN02364 |
L-ascorbate peroxidase 1 |
69-390 |
2.30e-12 |
|
L-ascorbate peroxidase 1
Pssm-ID: 166005 Cd Length: 250 Bit Score: 67.41 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 69 GPLFIRMAWHSAGTYRTfDGRGGASGGHQRLPPVDSWPDNANLDKARRLLWPVKQKYgRQLSWGDLIVLAGNVALESMGF 148
Cdd:PLN02364 33 APIMVRLAWHSAGTFDC-QSRTGGPFGTMRFDAEQAHGANSGIHIALRLLDPIREQF-PTISFADFHQLAGVVAVEVTGG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 149 etfgfgggreddytPDAAVDWGPEDEFEMSSEERFdeegnlkwplgntvmgliyvnpegpngePDLEGSAKNIRESFG-Q 227
Cdd:PLN02364 111 --------------PDIPFHPGREDKPQPPPEGRL----------------------------PDATKGCDHLRDVFAkQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 228 MAMNDEETVALiAGGHTFGKVHGAddpdehvgsepaaapieeqglgwesdfgegkgpdtiTSGIEGPWNTTPTQWDMSYV 307
Cdd:PLN02364 149 MGLSDKDIVAL-SGAHTLGRCHKD------------------------------------RSGFEGAWTSNPLIFDNSYF 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 308 DNLLDHEwvpekgpggawqwtteegeldnaapgvqdpsdKEDVMMLTTDVALKRDPDYREVLEHFQENPRDFQEAFAKAW 387
Cdd:PLN02364 192 KELLSGE--------------------------------KEGLLQLVSDKALLDDPVFRPLVEKYAADEDAFFADYAEAH 239
|
...
gi 2279600791 388 YKL 390
Cdd:PLN02364 240 MKL 242
|
|
| catalase_peroxidase_2 |
cd08200 |
C-terminal non-catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ... |
72-144 |
1.79e-11 |
|
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: 65.71 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 72 FIRMAWHSAGTYRTFDGRGGASGGHQRLPPVDSWPDN--ANLDKARRLLWPVKQKY------GRQLSWGDLIVLAGNVAL 143
Cdd:cd08200 33 LVSTAWASASTFRNSDKRGGANGARIRLAPQKDWEVNepEELAKVLAVLEGIQKEFnesqsgGKKVSLADLIVLGGCAAV 112
|
.
gi 2279600791 144 E 144
Cdd:cd08200 113 E 113
|
|
| catalase_peroxidase_1 |
cd00649 |
N-terminal catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ... |
448-555 |
6.71e-07 |
|
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: 52.31 E-value: 6.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 448 VKTAWASASTYRDSDKRGGANGARLRLEPQKSWEMNepAELESVLSTLEEIREEFnGSrsddvRVSLADLIVLGGNaave 527
Cdd:cd00649 74 IRMAWHSAGTYRIADGRGGAGTGQQRFAPLNSWPDN--VNLDKARRLLWPIKQKY-GN-----KISWADLMILAGN---- 141
|
90 100
....*....|....*....|....*...
gi 2279600791 528 QAAADAGYDvTIPFEPGRTDATQEQTDV 555
Cdd:cd00649 142 VALESMGFK-TFGFAGGREDVWEPDEDV 168
|
|
| plant_peroxidase_like_1 |
cd08201 |
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ... |
207-262 |
4.66e-05 |
|
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: 45.54 E-value: 4.66e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2279600791 207 GPNGEPDLEGSAKNIRESFGQMAMNDEETVALIAGGHTFGKVHGADDPD-EHVGSEP 262
Cdd:cd08201 133 GQAGVPEPQTDLGTTTESFRRQGFSTSEMIALVACGHTLGGVHSEDFPEiVPPGSVP 189
|
|
| PLN02364 |
PLN02364 |
L-ascorbate peroxidase 1 |
447-641 |
3.50e-04 |
|
L-ascorbate peroxidase 1
Pssm-ID: 166005 Cd Length: 250 Bit Score: 42.76 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 447 LVKTAWASASTYRDSDKRGGANGArLRLEPQKSWEMNepAELESVLSTLEEIREEFNgsrsddvRVSLADLIVLGGnaaV 526
Cdd:PLN02364 36 MVRLAWHSAGTFDCQSRTGGPFGT-MRFDAEQAHGAN--SGIHIALRLLDPIREQFP-------TISFADFHQLAG---V 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279600791 527 EQAAADAGYDvtIPFEPGRTDATQEQTdvesfEALKPNADGFRNYLGDDLERQpeellvdkaelLNLTANEMtVMVGGMR 606
Cdd:PLN02364 103 VAVEVTGGPD--IPFHPGREDKPQPPP-----EGRLPDATKGCDHLRDVFAKQ-----------MGLSDKDI-VALSGAH 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 2279600791 607 ALGANYQDSD--LGVFTDQPETLTNDFFVNLLDMDYE 641
Cdd:PLN02364 164 TLGRCHKDRSgfEGAWTSNPLIFDNSYFKELLSGEKE 200
|
|
| |
