|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15061 |
PRK15061 |
catalase/peroxidase; |
11-726 |
0e+00 |
|
catalase/peroxidase;
Pssm-ID: 237891 [Multi-domain] Cd Length: 726 Bit Score: 1406.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 11 ASAGKCPFHqggvdHSAGAGTGSKDWWPKQLRIDLLNQHSNRSNPLGEDFDYRKEFSKLDYSALKGDLKALLTDSQPWWP 90
Cdd:PRK15061 1 SSAGKCPVM-----HGAGGGTSNRDWWPNQLNLDILHQHSSKSNPMGEDFDYAEEFKKLDLEALKKDLKALMTDSQDWWP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 91 ADWGSYAGLFIRMAWHGAGTYRSVDGRGGAGRGQQRFAPLNSWPDNVSLDKARRLLWPVKQKYGQKISWADLFILAGNVA 170
Cdd:PRK15061 76 ADYGHYGPLFIRMAWHSAGTYRIGDGRGGAGGGQQRFAPLNSWPDNVNLDKARRLLWPIKQKYGNKISWADLMILAGNVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 171 LENSGFRTFGFGAGREDVWEPDLDVNWGDEKAWLTH---RDPEALAKRPLAATEMGLIYVNPEGPNASGEPLSAAAAIRA 247
Cdd:PRK15061 156 LESMGFKTFGFAGGREDVWEPEEDVYWGPEKEWLGGderYSGERDLENPLAAVQMGLIYVNPEGPNGNPDPLAAARDIRE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 248 TFGNMGMNDEETVALIAGGHTLGKTHGAGEATHVGTDPEASPIEAQGLGWASTHGTGIGADAITSGLEVIWSQTPTQWSN 327
Cdd:PRK15061 236 TFARMAMNDEETVALIAGGHTFGKTHGAGDASHVGPEPEAAPIEEQGLGWKNSYGSGKGADTITSGLEGAWTTTPTQWDN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 328 YFFENLFKYEWVQTRSPAGAIQFEAVD--APEIMPDPFDPSKKRKPTMLVTDLTLRFDPEFEKISRRFLNDPQAFNEAFA 405
Cdd:PRK15061 316 GYFENLFGYEWELTKSPAGAWQWVPKDgaAEDTVPDAHDPSKKHAPTMLTTDLALRFDPEYEKISRRFLENPEEFADAFA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 406 RAWFKLTHRDMGPKARYIGPEVPKEDLIWQDPLPqPVFHP--TQEDIESLKAEIAASGLSVSELVSVAWASASTFRGGDK 483
Cdd:PRK15061 396 RAWFKLTHRDMGPKSRYLGPEVPKEDLIWQDPVP-AVDHEliDDADIAALKAKILASGLSVSELVSTAWASASTFRGSDK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 484 RGGANGARLALAPQRDWDVNAAA--VRALPALEAIQRTTN-------KASLADIIVLAGVVGVEQAAKAAGVYVNVPFTP 554
Cdd:PRK15061 475 RGGANGARIRLAPQKDWEVNEPAqlAKVLAVLEGIQAEFNaaqsggkKVSLADLIVLGGNAAVEQAAKAAGHDVTVPFTP 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 555 GRVDARQDQTDIEMFNLLEPVADGFRNYRAQVDVSTTESLLIDKAQQLTLTAPELTVLIGGLRVLGANFDGSKNGVFTNR 634
Cdd:PRK15061 555 GRTDATQEQTDVESFAVLEPKADGFRNYLKKGYSVSPEELLVDKAQLLTLTAPEMTVLVGGLRVLGANYGGSKHGVFTDR 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 635 EGVLSNDFFVNLLDMNTQWKATDDSNELFAGSDRASGEVKYTATRADLVFGSNAVLRALAEVYASSDAHEKFVRDFVAAW 714
Cdd:PRK15061 635 PGVLTNDFFVNLLDMGTEWKPTDEDEEVYEGRDRKTGEVKWTATRVDLVFGSNSQLRALAEVYASDDAKEKFVRDFVAAW 714
|
730
....*....|..
gi 489958739 715 ARVMDLDRFDVK 726
Cdd:PRK15061 715 TKVMNLDRFDLA 726
|
|
| KatG |
COG0376 |
Catalase (peroxidase I) [Inorganic ion transport and metabolism]; |
10-726 |
0e+00 |
|
Catalase (peroxidase I) [Inorganic ion transport and metabolism];
Pssm-ID: 440145 [Multi-domain] Cd Length: 731 Bit Score: 1376.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 10 AASAGKCPFHQGGVDHSAGAGTGSKDWWPKQLRIDLLNQHSNRSNPLGEDFDYRKEFSKLDYSALKGDLKALLTDSQPWW 89
Cdd:COG0376 1 MSAEGKCPFMHGAAAAAAGGGTSNRDWWPNQLNLSILHQHSPKSNPMGEDFDYAEAFKKLDLDAVKKDLKALMTDSQDWW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 90 PADWGSYAGLFIRMAWHGAGTYRSVDGRGGAGRGQQRFAPLNSWPDNVSLDKARRLLWPVKQKYGQKISWADLFILAGNV 169
Cdd:COG0376 81 PADYGHYGPLFIRMAWHSAGTYRIGDGRGGAGGGQQRFAPLNSWPDNANLDKARRLLWPIKQKYGNKISWADLMILAGNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 170 ALENSGFRTFGFGAGREDVWEPDLDVNWGDEKAWLT---HRDPEALAKrPLAATEMGLIYVNPEGPNASGEPLSAAAAIR 246
Cdd:COG0376 161 ALESMGFKTFGFAGGREDVWEPEEDVYWGPETEWLGderYSGDRELEN-PLAAVQMGLIYVNPEGPNGNPDPLAAARDIR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 247 ATFGNMGMNDEETVALIAGGHTLGKTHGAGEATHVGTDPEASPIEAQGLGWASTHGTGIGADAITSGLEVIWSQTPTQWS 326
Cdd:COG0376 240 ETFGRMAMNDEETVALIAGGHTFGKTHGAGDAEHVGPEPEAAPIEEQGLGWKNSFGSGKGEDTITSGLEGAWTPTPTQWD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 327 NYFFENLFKYEWVQTRSPAGAIQFEAVD--APEIMPDPFDPSKKRKPTMLVTDLTLRFDPEFEKISRRFLNDPQAFNEAF 404
Cdd:COG0376 320 NGYFDNLFGYEWELTKSPAGAHQWVPKDgaAADTVPDAHDPSKRHAPMMLTTDLALRFDPAYEKISRRFLENPEEFADAF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 405 ARAWFKLTHRDMGPKARYIGPEVPKEDLIWQDPLPqPVFHPT--QEDIESLKAEIAASGLSVSELVSVAWASASTFRGGD 482
Cdd:COG0376 400 ARAWFKLTHRDMGPKSRYLGPEVPAEELIWQDPIP-AVDHELidDADIAALKAKILASGLSVSELVSTAWASASTFRGSD 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 483 KRGGANGARLALAPQRDWDVNAAA--VRALPALEAIQRTTNKA-------SLADIIVLAGVVGVEQAAKAAGVYVNVPFT 553
Cdd:COG0376 479 KRGGANGARIRLAPQKDWEVNEPEqlAKVLAVLEGIQKDFNAAqsggkkvSLADLIVLGGCAAVEKAAKDAGHDVTVPFT 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 554 PGRVDARQDQTDIEMFNLLEPVADGFRNYRAQVDVSTTESLLIDKAQQLTLTAPELTVLIGGLRVLGANFDGSKNGVFTN 633
Cdd:COG0376 559 PGRTDATQEQTDVESFAVLEPKADGFRNYLKKGYSVSAEELLVDKAQLLTLTAPEMTVLVGGLRVLGANYGGSKHGVFTD 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 634 REGVLSNDFFVNLLDMNTQWKATDDSNELFAGSDRASGEVKYTATRADLVFGSNAVLRALAEVYASSDAHEKFVRDFVAA 713
Cdd:COG0376 639 RPGTLTNDFFVNLLDMGTEWKPSSDDEGLFEGRDRKTGEVKWTATRVDLVFGSNSELRALAEVYASDDAKEKFVKDFVAA 718
|
730
....*....|...
gi 489958739 714 WARVMDLDRFDVK 726
Cdd:COG0376 719 WTKVMNLDRFDLA 731
|
|
| cat_per_HPI |
TIGR00198 |
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ... |
18-725 |
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: 1238.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 18 FHQGGVDHSAGAGTGSKDWWPKQLRIDLLNQHSNRSNPLGEDFDYRKEFSKLDYSALKGDLKALLTDSQPWWPADWGSYA 97
Cdd:TIGR00198 1 ASQGGVMHGANTTGQTGDWWPNALNLDILHQHDRKTNPMGEDFDYAEEFQQLDLAAVKQDLKHLMTDSQSWWPADWGHYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 98 GLFIRMAWHGAGTYRSVDGRGGAGRGQQRFAPLNSWPDNVSLDKARRLLWPVKQKYGQKISWADLFILAGNVALENSGFR 177
Cdd:TIGR00198 81 GLFIRMAWHAAGTYRIADGRGGAATGNQRFAPLNSWPDNVNLDKARRLLWPIKKKYGNKLSWADLIILAGTVAYESMGLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 178 TFGFGAGREDVWEPDLDVNWGDEKAWLTH-RDPEALAKRPLAATEMGLIYVNPEGPNASGEPLSAAAAIRATFGNMGMND 256
Cdd:TIGR00198 161 VFGFAGGREDIWEPDKDIYWGAEKEWLTSsREDRESLENPLAATEMGLIYVNPEGPDGHPDPLCTAQDIRTTFARMGMND 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 257 EETVALIAGGHTLGKTHGAGEATHVGTDPEASPIEAQGLGWASTHGTGIGADAITSGLEVIWSQTPTQWSNYFFENLFKY 336
Cdd:TIGR00198 241 EETVALIAGGHTVGKCHGAGPAELIGPDPEGAPIEEQGLGWHNQYGKGVGRDTMTSGLEVAWTTTPTQWDNGYFYMLFNY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 337 EWVQTRSPAGAIQFEAVDAPEIMPDPFDPSKKRKPTMLVTDLTLRFDPEFEKISRRFLNDPQAFNEAFARAWFKLTHRDM 416
Cdd:TIGR00198 321 EWELKKSPAGAWQWEAVDAPEIIPDVEDPNKKHNPIMLDADLALRFDPEFRKISRRFLREPDYFAEAFAKAWFKLTHRDM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 417 GPKARYIGPEVPKEDLIWQDPLPQPVFHPTQEDIESLKAEIAASGLSVSELVSVAWASASTFRGGDKRGGANGARLALAP 496
Cdd:TIGR00198 401 GPKSRYIGPDVPQEDLIWQDPLPPVDYTLSEGDIKELKQQILASGLSVSELVCTAWASASTFRSSDYRGGANGARIRLEP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 497 QRDWDVN--AAAVRALPALEAIQRTTN--KASLADIIVLAGVVGVEQAAKAAGVYVNVPFTPGRVDARQDQTDIEMFNLL 572
Cdd:TIGR00198 481 QKNWPVNepTRLAKVLAVLEKIQAEFAkgPVSLADLIVLGGGAAVEKAALDAGISVNVPFLPGRVDATQAMTDAESFTPL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 573 EPVADGFRNYRAQVDVSTTESLLIDKAQQLTLTAPELTVLIGGLRVLGANFDGSKNGVFTNREGVLSNDFFVNLLDMNTQ 652
Cdd:TIGR00198 561 EPIADGFRNYLKRDYAVTPEELLLDKAQLLTLTAPEMTVLIGGMRVLGANHGGSKHGVFTDRVGVLSNDFFVNLLDMAYE 640
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489958739 653 WKATDDSNELFAGSDRASGEVKYTATRADLVFGSNAVLRALAEVYASSDAHEKFVRDFVAAWARVMDLDRFDV 725
Cdd:TIGR00198 641 WRAADNNRYLFEGGDRQTGEVKWTATRVDLVFGSNSILRAVAEVYAQDDAREKFVKDFVAAWTKVMNLDRFDL 713
|
|
| catalase_peroxidase_1 |
cd00649 |
N-terminal catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ... |
28-432 |
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: 722.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 28 GAGTGSKDWWPKQLRIDLLNQHSNRSNPLGEDFDYRKEFSKLDYSALKGDLKALLTDSQPWWPADWGSYAGLFIRMAWHG 107
Cdd:cd00649 1 GGGTSNQDWWPNRLNLKILHQHSPKSNPMGEDFNYAEEFKKLDLEALKEDLKALMTDSQDWWPADYGHYGPLFIRMAWHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 108 AGTYRSVDGRGGAGRGQQRFAPLNSWPDNVSLDKARRLLWPVKQKYGQKISWADLFILAGNVALENSGFRTFGFGAGRED 187
Cdd:cd00649 81 AGTYRIADGRGGAGTGQQRFAPLNSWPDNVNLDKARRLLWPIKQKYGNKISWADLMILAGNVALESMGFKTFGFAGGRED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 188 VWEPDLDVNWGDEKAWLT---HRDPEALaKRPLAATEMGLIYVNPEGPNASGEPLSAAAAIRATFGNMGMNDEETVALIA 264
Cdd:cd00649 161 VWEPDEDVYWGPEKEWLAdkrYSGDRDL-ENPLAAVQMGLIYVNPEGPDGNPDPLAAAKDIRETFARMAMNDEETVALIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 265 GGHTLGKTHGAGEATHVGTDPEASPIEAQGLGWASTHGTGIGADAITSGLEVIWSQTPTQWSNYFFENLFKYEWVQTRSP 344
Cdd:cd00649 240 GGHTFGKTHGAGPASHVGPEPEAAPIEQQGLGWKNSYGTGKGKDTITSGLEGAWTPTPTKWDNNYLKNLFGYEWELTKSP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 345 AGAIQFEAVDA--PEIMPDPFDPSKKRKPTMLVTDLTLRFDPEFEKISRRFLNDPQAFNEAFARAWFKLTHRDMGPKARY 422
Cdd:cd00649 320 AGAWQWVPKNAagENTVPDAHDPSKKHAPMMLTTDLALRFDPEYEKISRRFLENPDEFADAFAKAWFKLTHRDMGPKSRY 399
|
410
....*....|
gi 489958739 423 IGPEVPKEDL 432
Cdd:cd00649 400 LGPEVPEEDL 409
|
|
| peroxidase |
pfam00141 |
Peroxidase; |
89-273 |
6.56e-31 |
|
Peroxidase;
Pssm-ID: 425483 [Multi-domain] Cd Length: 187 Bit Score: 119.59 E-value: 6.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 89 WPADWGSYAGLFIRMAWHGAGT---YRSVdgrggagrGQQRFAPLNSWPDNVSLDKARRLLWPVKQKY----GQKISWAD 161
Cdd:pfam00141 8 AFKADPTMGPSLLRLHFHDCFVggcDGSV--------LLDGFKPEKDAPPNLGLRKGFEVIDDIKAKLeaacPGVVSCAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 162 LFILAGNVALENSGFRTFGFGAGREDVWEPDLDvnwgdekawlthrdpealakrplaatemgliYVNPEGPnasgEPLSA 241
Cdd:pfam00141 80 ILALAARDAVELAGGPSWPVPLGRRDGTVSSAV-------------------------------EANSNLP----APTDS 124
|
170 180 190
....*....|....*....|....*....|..
gi 489958739 242 AAAIRATFGNMGMNDEETVALiAGGHTLGKTH 273
Cdd:pfam00141 125 LDQLRDRFARKGLTAEDLVAL-SGAHTIGRAH 155
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15061 |
PRK15061 |
catalase/peroxidase; |
11-726 |
0e+00 |
|
catalase/peroxidase;
Pssm-ID: 237891 [Multi-domain] Cd Length: 726 Bit Score: 1406.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 11 ASAGKCPFHqggvdHSAGAGTGSKDWWPKQLRIDLLNQHSNRSNPLGEDFDYRKEFSKLDYSALKGDLKALLTDSQPWWP 90
Cdd:PRK15061 1 SSAGKCPVM-----HGAGGGTSNRDWWPNQLNLDILHQHSSKSNPMGEDFDYAEEFKKLDLEALKKDLKALMTDSQDWWP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 91 ADWGSYAGLFIRMAWHGAGTYRSVDGRGGAGRGQQRFAPLNSWPDNVSLDKARRLLWPVKQKYGQKISWADLFILAGNVA 170
Cdd:PRK15061 76 ADYGHYGPLFIRMAWHSAGTYRIGDGRGGAGGGQQRFAPLNSWPDNVNLDKARRLLWPIKQKYGNKISWADLMILAGNVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 171 LENSGFRTFGFGAGREDVWEPDLDVNWGDEKAWLTH---RDPEALAKRPLAATEMGLIYVNPEGPNASGEPLSAAAAIRA 247
Cdd:PRK15061 156 LESMGFKTFGFAGGREDVWEPEEDVYWGPEKEWLGGderYSGERDLENPLAAVQMGLIYVNPEGPNGNPDPLAAARDIRE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 248 TFGNMGMNDEETVALIAGGHTLGKTHGAGEATHVGTDPEASPIEAQGLGWASTHGTGIGADAITSGLEVIWSQTPTQWSN 327
Cdd:PRK15061 236 TFARMAMNDEETVALIAGGHTFGKTHGAGDASHVGPEPEAAPIEEQGLGWKNSYGSGKGADTITSGLEGAWTTTPTQWDN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 328 YFFENLFKYEWVQTRSPAGAIQFEAVD--APEIMPDPFDPSKKRKPTMLVTDLTLRFDPEFEKISRRFLNDPQAFNEAFA 405
Cdd:PRK15061 316 GYFENLFGYEWELTKSPAGAWQWVPKDgaAEDTVPDAHDPSKKHAPTMLTTDLALRFDPEYEKISRRFLENPEEFADAFA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 406 RAWFKLTHRDMGPKARYIGPEVPKEDLIWQDPLPqPVFHP--TQEDIESLKAEIAASGLSVSELVSVAWASASTFRGGDK 483
Cdd:PRK15061 396 RAWFKLTHRDMGPKSRYLGPEVPKEDLIWQDPVP-AVDHEliDDADIAALKAKILASGLSVSELVSTAWASASTFRGSDK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 484 RGGANGARLALAPQRDWDVNAAA--VRALPALEAIQRTTN-------KASLADIIVLAGVVGVEQAAKAAGVYVNVPFTP 554
Cdd:PRK15061 475 RGGANGARIRLAPQKDWEVNEPAqlAKVLAVLEGIQAEFNaaqsggkKVSLADLIVLGGNAAVEQAAKAAGHDVTVPFTP 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 555 GRVDARQDQTDIEMFNLLEPVADGFRNYRAQVDVSTTESLLIDKAQQLTLTAPELTVLIGGLRVLGANFDGSKNGVFTNR 634
Cdd:PRK15061 555 GRTDATQEQTDVESFAVLEPKADGFRNYLKKGYSVSPEELLVDKAQLLTLTAPEMTVLVGGLRVLGANYGGSKHGVFTDR 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 635 EGVLSNDFFVNLLDMNTQWKATDDSNELFAGSDRASGEVKYTATRADLVFGSNAVLRALAEVYASSDAHEKFVRDFVAAW 714
Cdd:PRK15061 635 PGVLTNDFFVNLLDMGTEWKPTDEDEEVYEGRDRKTGEVKWTATRVDLVFGSNSQLRALAEVYASDDAKEKFVRDFVAAW 714
|
730
....*....|..
gi 489958739 715 ARVMDLDRFDVK 726
Cdd:PRK15061 715 TKVMNLDRFDLA 726
|
|
| KatG |
COG0376 |
Catalase (peroxidase I) [Inorganic ion transport and metabolism]; |
10-726 |
0e+00 |
|
Catalase (peroxidase I) [Inorganic ion transport and metabolism];
Pssm-ID: 440145 [Multi-domain] Cd Length: 731 Bit Score: 1376.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 10 AASAGKCPFHQGGVDHSAGAGTGSKDWWPKQLRIDLLNQHSNRSNPLGEDFDYRKEFSKLDYSALKGDLKALLTDSQPWW 89
Cdd:COG0376 1 MSAEGKCPFMHGAAAAAAGGGTSNRDWWPNQLNLSILHQHSPKSNPMGEDFDYAEAFKKLDLDAVKKDLKALMTDSQDWW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 90 PADWGSYAGLFIRMAWHGAGTYRSVDGRGGAGRGQQRFAPLNSWPDNVSLDKARRLLWPVKQKYGQKISWADLFILAGNV 169
Cdd:COG0376 81 PADYGHYGPLFIRMAWHSAGTYRIGDGRGGAGGGQQRFAPLNSWPDNANLDKARRLLWPIKQKYGNKISWADLMILAGNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 170 ALENSGFRTFGFGAGREDVWEPDLDVNWGDEKAWLT---HRDPEALAKrPLAATEMGLIYVNPEGPNASGEPLSAAAAIR 246
Cdd:COG0376 161 ALESMGFKTFGFAGGREDVWEPEEDVYWGPETEWLGderYSGDRELEN-PLAAVQMGLIYVNPEGPNGNPDPLAAARDIR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 247 ATFGNMGMNDEETVALIAGGHTLGKTHGAGEATHVGTDPEASPIEAQGLGWASTHGTGIGADAITSGLEVIWSQTPTQWS 326
Cdd:COG0376 240 ETFGRMAMNDEETVALIAGGHTFGKTHGAGDAEHVGPEPEAAPIEEQGLGWKNSFGSGKGEDTITSGLEGAWTPTPTQWD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 327 NYFFENLFKYEWVQTRSPAGAIQFEAVD--APEIMPDPFDPSKKRKPTMLVTDLTLRFDPEFEKISRRFLNDPQAFNEAF 404
Cdd:COG0376 320 NGYFDNLFGYEWELTKSPAGAHQWVPKDgaAADTVPDAHDPSKRHAPMMLTTDLALRFDPAYEKISRRFLENPEEFADAF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 405 ARAWFKLTHRDMGPKARYIGPEVPKEDLIWQDPLPqPVFHPT--QEDIESLKAEIAASGLSVSELVSVAWASASTFRGGD 482
Cdd:COG0376 400 ARAWFKLTHRDMGPKSRYLGPEVPAEELIWQDPIP-AVDHELidDADIAALKAKILASGLSVSELVSTAWASASTFRGSD 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 483 KRGGANGARLALAPQRDWDVNAAA--VRALPALEAIQRTTNKA-------SLADIIVLAGVVGVEQAAKAAGVYVNVPFT 553
Cdd:COG0376 479 KRGGANGARIRLAPQKDWEVNEPEqlAKVLAVLEGIQKDFNAAqsggkkvSLADLIVLGGCAAVEKAAKDAGHDVTVPFT 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 554 PGRVDARQDQTDIEMFNLLEPVADGFRNYRAQVDVSTTESLLIDKAQQLTLTAPELTVLIGGLRVLGANFDGSKNGVFTN 633
Cdd:COG0376 559 PGRTDATQEQTDVESFAVLEPKADGFRNYLKKGYSVSAEELLVDKAQLLTLTAPEMTVLVGGLRVLGANYGGSKHGVFTD 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 634 REGVLSNDFFVNLLDMNTQWKATDDSNELFAGSDRASGEVKYTATRADLVFGSNAVLRALAEVYASSDAHEKFVRDFVAA 713
Cdd:COG0376 639 RPGTLTNDFFVNLLDMGTEWKPSSDDEGLFEGRDRKTGEVKWTATRVDLVFGSNSELRALAEVYASDDAKEKFVKDFVAA 718
|
730
....*....|...
gi 489958739 714 WARVMDLDRFDVK 726
Cdd:COG0376 719 WTKVMNLDRFDLA 731
|
|
| cat_per_HPI |
TIGR00198 |
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ... |
18-725 |
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: 1238.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 18 FHQGGVDHSAGAGTGSKDWWPKQLRIDLLNQHSNRSNPLGEDFDYRKEFSKLDYSALKGDLKALLTDSQPWWPADWGSYA 97
Cdd:TIGR00198 1 ASQGGVMHGANTTGQTGDWWPNALNLDILHQHDRKTNPMGEDFDYAEEFQQLDLAAVKQDLKHLMTDSQSWWPADWGHYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 98 GLFIRMAWHGAGTYRSVDGRGGAGRGQQRFAPLNSWPDNVSLDKARRLLWPVKQKYGQKISWADLFILAGNVALENSGFR 177
Cdd:TIGR00198 81 GLFIRMAWHAAGTYRIADGRGGAATGNQRFAPLNSWPDNVNLDKARRLLWPIKKKYGNKLSWADLIILAGTVAYESMGLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 178 TFGFGAGREDVWEPDLDVNWGDEKAWLTH-RDPEALAKRPLAATEMGLIYVNPEGPNASGEPLSAAAAIRATFGNMGMND 256
Cdd:TIGR00198 161 VFGFAGGREDIWEPDKDIYWGAEKEWLTSsREDRESLENPLAATEMGLIYVNPEGPDGHPDPLCTAQDIRTTFARMGMND 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 257 EETVALIAGGHTLGKTHGAGEATHVGTDPEASPIEAQGLGWASTHGTGIGADAITSGLEVIWSQTPTQWSNYFFENLFKY 336
Cdd:TIGR00198 241 EETVALIAGGHTVGKCHGAGPAELIGPDPEGAPIEEQGLGWHNQYGKGVGRDTMTSGLEVAWTTTPTQWDNGYFYMLFNY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 337 EWVQTRSPAGAIQFEAVDAPEIMPDPFDPSKKRKPTMLVTDLTLRFDPEFEKISRRFLNDPQAFNEAFARAWFKLTHRDM 416
Cdd:TIGR00198 321 EWELKKSPAGAWQWEAVDAPEIIPDVEDPNKKHNPIMLDADLALRFDPEFRKISRRFLREPDYFAEAFAKAWFKLTHRDM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 417 GPKARYIGPEVPKEDLIWQDPLPQPVFHPTQEDIESLKAEIAASGLSVSELVSVAWASASTFRGGDKRGGANGARLALAP 496
Cdd:TIGR00198 401 GPKSRYIGPDVPQEDLIWQDPLPPVDYTLSEGDIKELKQQILASGLSVSELVCTAWASASTFRSSDYRGGANGARIRLEP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 497 QRDWDVN--AAAVRALPALEAIQRTTN--KASLADIIVLAGVVGVEQAAKAAGVYVNVPFTPGRVDARQDQTDIEMFNLL 572
Cdd:TIGR00198 481 QKNWPVNepTRLAKVLAVLEKIQAEFAkgPVSLADLIVLGGGAAVEKAALDAGISVNVPFLPGRVDATQAMTDAESFTPL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 573 EPVADGFRNYRAQVDVSTTESLLIDKAQQLTLTAPELTVLIGGLRVLGANFDGSKNGVFTNREGVLSNDFFVNLLDMNTQ 652
Cdd:TIGR00198 561 EPIADGFRNYLKRDYAVTPEELLLDKAQLLTLTAPEMTVLIGGMRVLGANHGGSKHGVFTDRVGVLSNDFFVNLLDMAYE 640
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489958739 653 WKATDDSNELFAGSDRASGEVKYTATRADLVFGSNAVLRALAEVYASSDAHEKFVRDFVAAWARVMDLDRFDV 725
Cdd:TIGR00198 641 WRAADNNRYLFEGGDRQTGEVKWTATRVDLVFGSNSILRAVAEVYAQDDAREKFVKDFVAAWTKVMNLDRFDL 713
|
|
| catalase_peroxidase_1 |
cd00649 |
N-terminal catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ... |
28-432 |
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: 722.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 28 GAGTGSKDWWPKQLRIDLLNQHSNRSNPLGEDFDYRKEFSKLDYSALKGDLKALLTDSQPWWPADWGSYAGLFIRMAWHG 107
Cdd:cd00649 1 GGGTSNQDWWPNRLNLKILHQHSPKSNPMGEDFNYAEEFKKLDLEALKEDLKALMTDSQDWWPADYGHYGPLFIRMAWHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 108 AGTYRSVDGRGGAGRGQQRFAPLNSWPDNVSLDKARRLLWPVKQKYGQKISWADLFILAGNVALENSGFRTFGFGAGRED 187
Cdd:cd00649 81 AGTYRIADGRGGAGTGQQRFAPLNSWPDNVNLDKARRLLWPIKQKYGNKISWADLMILAGNVALESMGFKTFGFAGGRED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 188 VWEPDLDVNWGDEKAWLT---HRDPEALaKRPLAATEMGLIYVNPEGPNASGEPLSAAAAIRATFGNMGMNDEETVALIA 264
Cdd:cd00649 161 VWEPDEDVYWGPEKEWLAdkrYSGDRDL-ENPLAAVQMGLIYVNPEGPDGNPDPLAAAKDIRETFARMAMNDEETVALIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 265 GGHTLGKTHGAGEATHVGTDPEASPIEAQGLGWASTHGTGIGADAITSGLEVIWSQTPTQWSNYFFENLFKYEWVQTRSP 344
Cdd:cd00649 240 GGHTFGKTHGAGPASHVGPEPEAAPIEQQGLGWKNSYGTGKGKDTITSGLEGAWTPTPTKWDNNYLKNLFGYEWELTKSP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 345 AGAIQFEAVDA--PEIMPDPFDPSKKRKPTMLVTDLTLRFDPEFEKISRRFLNDPQAFNEAFARAWFKLTHRDMGPKARY 422
Cdd:cd00649 320 AGAWQWVPKNAagENTVPDAHDPSKKHAPMMLTTDLALRFDPEYEKISRRFLENPDEFADAFAKAWFKLTHRDMGPKSRY 399
|
410
....*....|
gi 489958739 423 IGPEVPKEDL 432
Cdd:cd00649 400 LGPEVPEEDL 409
|
|
| catalase_peroxidase_2 |
cd08200 |
C-terminal non-catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ... |
436-722 |
1.20e-177 |
|
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: 508.69 E-value: 1.20e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 436 DPLPqPVFHP--TQEDIESLKAEIAASGLSVSELVSVAWASASTFRGGDKRGGANGARLALAPQRDWDVN--AAAVRALP 511
Cdd:cd08200 1 DPIP-AVDYEliDDADIAALKAKILASGLTVSELVSTAWASASTFRNSDKRGGANGARIRLAPQKDWEVNepEELAKVLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 512 ALEAIQRTTN-------KASLADIIVLAGVVGVEQAAKAAGVYVNVPFTPGRVDARQDQTDIEMFNLLEPVADGFRNYRA 584
Cdd:cd08200 80 VLEGIQKEFNesqsggkKVSLADLIVLGGCAAVEKAAKDAGVDIKVPFTPGRTDATQEQTDVESFEVLEPKADGFRNYLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 585 QVDVSTTESLLIDKAQQLTLTAPELTVLIGGLRVLGANFDGSKNGVFTNREGVLSNDFFVNLLDMNTQWKATDDSNELFA 664
Cdd:cd08200 160 KGYRVPPEEMLVDKAQLLTLTAPEMTVLVGGLRVLGANYGGSKHGVFTDRPGVLTNDFFVNLLDMSTEWKPADEDDGLFE 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 489958739 665 GSDRASGEVKYTATRADLVFGSNAVLRALAEVYASSDAHEKFVRDFVAAWARVMDLDR 722
Cdd:cd08200 240 GRDRKTGEVKWTATRVDLVFGSNSELRAVAEVYASDDAQEKFVKDFVAAWTKVMNLDR 297
|
|
| plant_peroxidase_like |
cd00314 |
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ... |
91-413 |
7.23e-46 |
|
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: 164.25 E-value: 7.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 91 ADWGSYAGLFIRMAWHGAGTYRSVDGRGGAGRGQQRFAPLNSWPDNVSLDKARRLLWPVKQKYG--QKISWADLFILAGN 168
Cdd:cd00314 12 TQAGALAGSLLRLAFHDAGTYDIADGKGGGADGSIRFEPELDRPENGGLDKALRALEPIKSAYDggNPVSRADLIALAGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 169 VALENS--GFRTFGFGAGREDvwepdldvnwgdekawlthrdpealakrplaATEMGLIYVNPEGPNasGEPLSAAAAIR 246
Cdd:cd00314 92 VAVESTfgGGPLIPFRFGRLD-------------------------------ATEPDLGVPDPEGLL--PNETSSATELR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 247 ATFGNMGMNDEETVALIAGGHTL-GKTHGageathvgtdpeaspieaqglgwasthgtgigaDAITSGLEVIWSQTPTQW 325
Cdd:cd00314 139 DKFKRMGLSPSELVALSAGAHTLgGKNHG---------------------------------DLLNYEGSGLWTSTPFTF 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 326 SNYFFENLFKYEWvqtrspagaiqfeavdapEIMPDPFDPSKKRKPTMLVTDLTLRFDPEFEKISRRFLNDPQAFNEAFA 405
Cdd:cd00314 186 DNAYFKNLLDMNW------------------EWRVGSPDPDGVKGPGLLPSDYALLSDSETRALVERYASDQEKFFEDFA 247
|
....*...
gi 489958739 406 RAWFKLTH 413
Cdd:cd00314 248 KAWIKMVN 255
|
|
| plant_peroxidase_like |
cd00314 |
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ... |
451-718 |
1.54e-43 |
|
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: 157.70 E-value: 1.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 451 ESLKAEIAASGLSVSELVSVAWASASTFRGGDKRGGANGARLALAPQRDWDVNAAAVRALPALEAIQRTT---NKASLAD 527
Cdd:cd00314 5 AILEDLITQAGALAGSLLRLAFHDAGTYDIADGKGGGADGSIRFEPELDRPENGGLDKALRALEPIKSAYdggNPVSRAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 528 IIVLAGVVGVEQAAkaaGVYVNVPFTPGRVDArqdqtDIEMFNLLEPVADgFRNYRAQVDVstteslLIDKAQQLTLTAP 607
Cdd:cd00314 85 LIALAGAVAVESTF---GGGPLIPFRFGRLDA-----TEPDLGVPDPEGL-LPNETSSATE------LRDKFKRMGLSPS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 608 ELTVLIGGLRVL-----GANFDGSKNGVFTNREGVLSNDFFVNLLDMNTQWKatddsnelfAGSDRASGEVKYTATRADL 682
Cdd:cd00314 150 ELVALSAGAHTLggknhGDLLNYEGSGLWTSTPFTFDNAYFKNLLDMNWEWR---------VGSPDPDGVKGPGLLPSDY 220
|
250 260 270
....*....|....*....|....*....|....*.
gi 489958739 683 VFGSNAVLRALAEVYASSDahEKFVRDFVAAWARVM 718
Cdd:cd00314 221 ALLSDSETRALVERYASDQ--EKFFEDFAKAWIKMV 254
|
|
| ascorbate_peroxidase |
cd00691 |
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ... |
70-412 |
2.86e-34 |
|
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: 131.56 E-value: 2.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 70 DYSALKGDLKALLTDsqpwwpadwGSYAGLFIRMAWHGAGTYrSVDGRGGAGRGQQRFAPLNSWPDNVSLDKARRLLWPV 149
Cdd:cd00691 12 DLEAARNDIAKLIDD---------KNCAPILVRLAWHDSGTY-DKETKTGGSNGTIRFDPELNHGANAGLDIARKLLEPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 150 KQKYgQKISWADLFILAGNVALENSGFRTFGFGAGREDVWEPDldvnwgdekawlthrdpealakrplaatemgliYVNP 229
Cdd:cd00691 82 KKKY-PDISYADLWQLAGVVAIEEMGGPKIPFRPGRVDASDPE---------------------------------ECPP 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 230 EG--PNASGeplsAAAAIRATFGNMGMNDEETVALIaGGHTLGKTHgageathvgtdPEAspieaqglgwasthgtgiga 307
Cdd:cd00691 128 EGrlPDASK----GADHLRDVFYRMGFNDQEIVALS-GAHTLGRCH-----------KER-------------------- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 308 daitSGLEVIWSQTPTQWSNYFFENLFKYEWVqtrspagaiqfeaVDAPEIMpdpfdpskkrkptMLVTDLTLRFDPEFE 387
Cdd:cd00691 172 ----SGYDGPWTKNPLKFDNSYFKELLEEDWK-------------LPTPGLL-------------MLPTDKALLEDPKFR 221
|
330 340
....*....|....*....|....*
gi 489958739 388 KISRRFLNDPQAFNEAFARAWFKLT 412
Cdd:cd00691 222 PYVELYAKDQDAFFKDYAEAHKKLS 246
|
|
| peroxidase |
pfam00141 |
Peroxidase; |
89-273 |
6.56e-31 |
|
Peroxidase;
Pssm-ID: 425483 [Multi-domain] Cd Length: 187 Bit Score: 119.59 E-value: 6.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 89 WPADWGSYAGLFIRMAWHGAGT---YRSVdgrggagrGQQRFAPLNSWPDNVSLDKARRLLWPVKQKY----GQKISWAD 161
Cdd:pfam00141 8 AFKADPTMGPSLLRLHFHDCFVggcDGSV--------LLDGFKPEKDAPPNLGLRKGFEVIDDIKAKLeaacPGVVSCAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 162 LFILAGNVALENSGFRTFGFGAGREDVWEPDLDvnwgdekawlthrdpealakrplaatemgliYVNPEGPnasgEPLSA 241
Cdd:pfam00141 80 ILALAARDAVELAGGPSWPVPLGRRDGTVSSAV-------------------------------EANSNLP----APTDS 124
|
170 180 190
....*....|....*....|....*....|..
gi 489958739 242 AAAIRATFGNMGMNDEETVALiAGGHTLGKTH 273
Cdd:pfam00141 125 LDQLRDRFARKGLTAEDLVAL-SGAHTIGRAH 155
|
|
| peroxidase |
pfam00141 |
Peroxidase; |
485-700 |
8.87e-22 |
|
Peroxidase;
Pssm-ID: 425483 [Multi-domain] Cd Length: 187 Bit Score: 93.40 E-value: 8.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 485 GGANGARL--ALAPQRDWDVNAAAVRALPALEAIQRTTNKA-----SLADIIVLAGVVGVEqaaKAAGVYVNVPftPGRV 557
Cdd:pfam00141 30 GGCDGSVLldGFKPEKDAPPNLGLRKGFEVIDDIKAKLEAAcpgvvSCADILALAARDAVE---LAGGPSWPVP--LGRR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 558 DARQDQTDiEMFNLLePVADGfrnyraqvDVSTteslLIDKAQQLTLTAPELTVLIGGlRVLGANfdgskngvftnregv 637
Cdd:pfam00141 105 DGTVSSAV-EANSNL-PAPTD--------SLDQ----LRDRFARKGLTAEDLVALSGA-HTIGRA--------------- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489958739 638 lsndfFVNLLDmntqwkatddsnelfagsdrasgevKYTATRADLVFGSNAVLRALAEVYASS 700
Cdd:pfam00141 155 -----HKNLLD-------------------------GRGLLTSDQALLSDPRTRALVERYAAD 187
|
|
| PLN02608 |
PLN02608 |
L-ascorbate peroxidase |
59-412 |
1.98e-13 |
|
L-ascorbate peroxidase
Pssm-ID: 178218 [Multi-domain] Cd Length: 289 Bit Score: 71.33 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 59 DFDYRKEFSKLdysalKGDLKALLTDSqpwwpadwgSYAGLFIRMAWHGAGTYrSVDGRGGAGRGQQRFAPLNSWPDNVS 138
Cdd:PLN02608 7 DAEYLKEIEKA-----RRDLRALIASK---------NCAPIMLRLAWHDAGTY-DAKTKTGGPNGSIRNEEEYSHGANNG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 139 LDKARRLLWPVKQKYgQKISWADLFILAGNVALENSGFRTFGFGAGREDvwepdldvnwgdekawlthrdpealakrPLA 218
Cdd:PLN02608 72 LKIAIDLCEPVKAKH-PKITYADLYQLAGVVAVEVTGGPTIDFVPGRKD----------------------------SNA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 219 ATEMGLIyvnpegPNASgeplSAAAAIRATFGNMGMNDEETVALiAGGHTLGKTHgageathvgtdPEaspieaqglgwa 298
Cdd:PLN02608 123 CPEEGRL------PDAK----KGAKHLRDVFYRMGLSDKDIVAL-SGGHTLGRAH-----------PE------------ 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 299 sthgtgigadaiTSGLEVIWSQTPTQWSNYFFENLFKYEwvqtrsPAGAIQfeavdapeimpdpfdpskkrkptmLVTDL 378
Cdd:PLN02608 169 ------------RSGFDGPWTKEPLKFDNSYFVELLKGE------SEGLLK------------------------LPTDK 206
|
330 340 350
....*....|....*....|....*....|....
gi 489958739 379 TLRFDPEFEKISRRFLNDPQAFNEAFARAWFKLT 412
Cdd:PLN02608 207 ALLEDPEFRPYVELYAKDEDAFFRDYAESHKKLS 240
|
|
| ascorbate_peroxidase |
cd00691 |
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ... |
446-720 |
2.92e-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: 70.31 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 446 TQEDIESLKAEIAASglsVSE------LVSVAWASASTFRGGDKRGGANGArLALAPQRDWDVNAAAVRALPALEAIQRT 519
Cdd:cd00691 9 AAKDLEAARNDIAKL---IDDkncapiLVRLAWHDSGTYDKETKTGGSNGT-IRFDPELNHGANAGLDIARKLLEPIKKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 520 TNKASLADIIVLAGVVGVEQAAKAAgvyvnVPFTPGRVDARQDQTDIEMFNLlePVADGFRNYraqvdvstteslLIDKA 599
Cdd:cd00691 85 YPDISYADLWQLAGVVAIEEMGGPK-----IPFRPGRVDASDPEECPPEGRL--PDASKGADH------------LRDVF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 600 QQLTLTAPELTVLIGGlRVLG---ANFDGsKNGVFTNREGVLSNDFFVNLLDMNTQWKatddSNELfagsdrasgevkyt 676
Cdd:cd00691 146 YRMGFNDQEIVALSGA-HTLGrchKERSG-YDGPWTKNPLKFDNSYFKELLEEDWKLP----TPGL-------------- 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 489958739 677 atradLVFGSNAVL------RALAEVYASSDahEKFVRDFVAAWARVMDL 720
Cdd:cd00691 206 -----LMLPTDKALledpkfRPYVELYAKDQ--DAFFKDYAEAHKKLSEL 248
|
|
| PLN02879 |
PLN02879 |
L-ascorbate peroxidase |
97-412 |
2.35e-12 |
|
L-ascorbate peroxidase
Pssm-ID: 178467 [Multi-domain] Cd Length: 251 Bit Score: 67.78 E-value: 2.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 97 AGLFIRMAWHGAGTYrSVDGRGGAGRGQQRFAPLNSWPDNVSLDKARRLLWPVKQKYgQKISWADLFILAGNVALENSGF 176
Cdd:PLN02879 34 APIVLRLAWHSAGTF-DVKTKTGGPFGTIRHPQELAHDANNGLDIAVRLLDPIKELF-PILSYADFYQLAGVVAVEITGG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 177 RTFGFGAGREDVWEPDldvnwgdekawlthrdpealakrplaatemgliyvnPEG--PNASgeplSAAAAIRATFGNMGM 254
Cdd:PLN02879 112 PEIPFHPGRLDKVEPP------------------------------------PEGrlPQAT----KGVDHLRDVFGRMGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 255 NDEETVALiAGGHTLGKTHGAgeathvgtdpeaspieaqglgwasthgtgigadaiTSGLEVIWSQTPTQWSNYFFENLF 334
Cdd:PLN02879 152 NDKDIVAL-SGGHTLGRCHKE-----------------------------------RSGFEGAWTPNPLIFDNSYFKEIL 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489958739 335 KYEwvqtrsPAGAIQfeavdapeimpdpfdpskkrkptmLVTDLTLRFDPEFEKISRRFLNDPQAFNEAFARAWFKLT 412
Cdd:PLN02879 196 SGE------KEGLLQ------------------------LPTDKALLDDPLFLPFVEKYAADEDAFFEDYTEAHLKLS 243
|
|
| PLN02364 |
PLN02364 |
L-ascorbate peroxidase 1 |
97-412 |
1.91e-09 |
|
L-ascorbate peroxidase 1
Pssm-ID: 166005 Cd Length: 250 Bit Score: 58.94 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 97 AGLFIRMAWHGAGTYrSVDGRGGAGRGQQRFAPLNSWPDNVSLDKARRLLWPVKQKYgQKISWADLFILAGNVALENSGF 176
Cdd:PLN02364 33 APIMVRLAWHSAGTF-DCQSRTGGPFGTMRFDAEQAHGANSGIHIALRLLDPIREQF-PTISFADFHQLAGVVAVEVTGG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 177 RTFGFGAGREDVWEPDldvnwgdekawlthrdpealakrplaatemgliyvnPEG--PNASgeplSAAAAIRATFG-NMG 253
Cdd:PLN02364 111 PDIPFHPGREDKPQPP------------------------------------PEGrlPDAT----KGCDHLRDVFAkQMG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 254 MNDEETVALiAGGHTLGKTHGAgeathvgtdpeaspieaqglgwasthgtgigadaiTSGLEVIWSQTPTQWSNYFFENL 333
Cdd:PLN02364 151 LSDKDIVAL-SGAHTLGRCHKD-----------------------------------RSGFEGAWTSNPLIFDNSYFKEL 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489958739 334 FKYEwvqtrsPAGAIQfeavdapeimpdpfdpskkrkptmLVTDLTLRFDPEFEKISRRFLNDPQAFNEAFARAWFKLT 412
Cdd:PLN02364 195 LSGE------KEGLLQ------------------------LVSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHMKLS 243
|
|
| catalase_peroxidase_1 |
cd00649 |
N-terminal catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ... |
471-566 |
2.74e-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: 53.46 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 471 AWASASTFRGGDKRGGANGARLALAPQRDWDVNAAAVRALPALEAI-QRTTNKASLADIIVLAGVVGVEQAA-KAAGvyv 548
Cdd:cd00649 77 AWHSAGTYRIADGRGGAGTGQQRFAPLNSWPDNVNLDKARRLLWPIkQKYGNKISWADLMILAGNVALESMGfKTFG--- 153
|
90
....*....|....*...
gi 489958739 549 nvpFTPGRVDARQDQTDI 566
Cdd:cd00649 154 ---FAGGREDVWEPDEDV 168
|
|
| secretory_peroxidase |
cd00693 |
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ... |
238-407 |
1.02e-05 |
|
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: 47.89 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 238 PLSAAAAIRATFGNMGMNDEETVALiAGGHTLGKTHGA-------GEATHVGTDPEASPIEAQGLGWASTHGtgiGADAI 310
Cdd:cd00693 139 PFFSVSQLISLFASKGLTVTDLVAL-SGAHTIGRAHCSsfsdrlyNFSGTGDPDPTLDPAYAAQLRKKCPAG---GDDDT 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 311 TSGLEVIwsqTPTQWSNYFFENLfkyewvqtrspagaiqfeavdapeimpdpfdpsKKRKpTMLVTDLTLRFDPEFEKIS 390
Cdd:cd00693 215 LVPLDPG---TPNTFDNSYYKNL---------------------------------LAGR-GLLTSDQALLSDPRTRAIV 257
|
170
....*....|....*..
gi 489958739 391 RRFLNDPQAFNEAFARA 407
Cdd:cd00693 258 NRYAANQDAFFRDFAAA 274
|
|
| PLN02364 |
PLN02364 |
L-ascorbate peroxidase 1 |
467-720 |
6.02e-05 |
|
L-ascorbate peroxidase 1
Pssm-ID: 166005 Cd Length: 250 Bit Score: 45.46 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 467 LVSVAWASASTFRGGDKRGGANGArLALAPQRDWDVNAAAVRALPALEAIQRTTNKASLADIIVLAGVVGVEQAAKAagv 546
Cdd:PLN02364 36 MVRLAWHSAGTFDCQSRTGGPFGT-MRFDAEQAHGANSGIHIALRLLDPIREQFPTISFADFHQLAGVVAVEVTGGP--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 547 yvNVPFTPGRVDARQdqtdiemfnllePVADGfrnyRAQVDVSTTESLLIDKAQQLTLTAPELTVLIGGLRVLGANFDGS 626
Cdd:PLN02364 112 --DIPFHPGREDKPQ------------PPPEG----RLPDATKGCDHLRDVFAKQMGLSDKDIVALSGAHTLGRCHKDRS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 627 K-NGVFTNREGVLSNDFFVNLLdmntqwkatddsnelfagSDRASGEVKYTATRADLvfgSNAVLRALAEVYASSDahEK 705
Cdd:PLN02364 174 GfEGAWTSNPLIFDNSYFKELL------------------SGEKEGLLQLVSDKALL---DDPVFRPLVEKYAADE--DA 230
|
250
....*....|....*
gi 489958739 706 FVRDFVAAWARVMDL 720
Cdd:PLN02364 231 FFADYAEAHMKLSEL 245
|
|
| catalase_peroxidase_2 |
cd08200 |
C-terminal non-catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ... |
100-187 |
2.17e-03 |
|
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: 40.67 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 100 FIRMAWHGAGTYRSVDGRGGAGRGQQRFAPLNSWPDN--VSLDKARRLLWPVKQKY------GQKISWADLFILAGNVAL 171
Cdd:cd08200 33 LVSTAWASASTFRNSDKRGGANGARIRLAPQKDWEVNepEELAKVLAVLEGIQKEFnesqsgGKKVSLADLIVLGGCAAV 112
|
90 100
....*....|....*....|.
gi 489958739 172 E----NSGFR-TFGFGAGRED 187
Cdd:cd08200 113 EkaakDAGVDiKVPFTPGRTD 133
|
|
| plant_peroxidase_like_1 |
cd08201 |
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ... |
231-289 |
2.32e-03 |
|
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: 40.53 E-value: 2.32e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489958739 231 GPNASGEPLSAAAAIRATFGNMGMNDEETVALIAGGHTLGKTHGAG--EATHVGTDPEASP 289
Cdd:cd08201 133 GQAGVPEPQTDLGTTTESFRRQGFSTSEMIALVACGHTLGGVHSEDfpEIVPPGSVPDTVL 193
|
|
| PLN02879 |
PLN02879 |
L-ascorbate peroxidase |
467-558 |
6.77e-03 |
|
L-ascorbate peroxidase
Pssm-ID: 178467 [Multi-domain] Cd Length: 251 Bit Score: 38.89 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 467 LVSVAWASASTFRGGDKRGGANGArlALAPQR-DWDVNAAAVRALPALEAIQRTTNKASLADIIVLAGVVGVEQAAKAag 545
Cdd:PLN02879 37 VLRLAWHSAGTFDVKTKTGGPFGT--IRHPQElAHDANNGLDIAVRLLDPIKELFPILSYADFYQLAGVVAVEITGGP-- 112
|
90
....*....|...
gi 489958739 546 vyvNVPFTPGRVD 558
Cdd:PLN02879 113 ---EIPFHPGRLD 122
|
|
| PLN02608 |
PLN02608 |
L-ascorbate peroxidase |
470-559 |
8.38e-03 |
|
L-ascorbate peroxidase
Pssm-ID: 178218 [Multi-domain] Cd Length: 289 Bit Score: 38.98 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958739 470 VAWASASTFRGGDKRGGANGArLALAPQRDWDVNAAAVRALPALEAIQRTTNKASLADIIVLAGVVGVEQAAKAagvyvN 549
Cdd:PLN02608 37 LAWHDAGTYDAKTKTGGPNGS-IRNEEEYSHGANNGLKIAIDLCEPVKAKHPKITYADLYQLAGVVAVEVTGGP-----T 110
|
90
....*....|
gi 489958739 550 VPFTPGRVDA 559
Cdd:PLN02608 111 IDFVPGRKDS 120
|
|
| |
