|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15061 |
PRK15061 |
catalase/peroxidase; |
11-725 |
0e+00 |
|
catalase/peroxidase;
Pssm-ID: 237891 [Multi-domain] Cd Length: 726 Bit Score: 1433.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 11 TATGKCPFHQGghdqsAGAGTTTRDWWPNQLRVDLLNQHSNRSNPLGEDFDYRKEFSKLDYYGLKKDLKALLTESQPWWP 90
Cdd:PRK15061 1 SSAGKCPVMHG-----AGGGTSNRDWWPNQLNLDILHQHSSKSNPMGEDFDYAEEFKKLDLEALKKDLKALMTDSQDWWP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 91 ADWGSYAGLFIRMAWHGAGTYRSIDGRGGAGRGQQRFAPLNSWPDNVSLDKARRLLWPIKQKYGQKISWADLFILAGNVA 170
Cdd:PRK15061 76 ADYGHYGPLFIRMAWHSAGTYRIGDGRGGAGGGQQRFAPLNSWPDNVNLDKARRLLWPIKQKYGNKISWADLMILAGNVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 171 LENSGFRTFGFGAGREDVWEPDLDVNWGDEKAWLT--HRH-PEALAKAPLGATEMGLIYVNPEGPDHSGEPLSAAAAIRA 247
Cdd:PRK15061 156 LESMGFKTFGFAGGREDVWEPEEDVYWGPEKEWLGgdERYsGERDLENPLAAVQMGLIYVNPEGPNGNPDPLAAARDIRE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 248 TFGNMGMNDEETVALIAGGHTLGKTHGAGPTSNVGPDPEAAPIEEQGLGWASTYGSGVGADAITSGLEVVWTQTPTQWSN 327
Cdd:PRK15061 236 TFARMAMNDEETVALIAGGHTFGKTHGAGDASHVGPEPEAAPIEEQGLGWKNSYGSGKGADTITSGLEGAWTTTPTQWDN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 328 YFFENLFKYEWVQTRSPAGAIQFEAVD--APEIIPDPFDPSKKRKPTMLVTDLTLRFDPEFEKISRRFLNDPQAFNEAFA 405
Cdd:PRK15061 316 GYFENLFGYEWELTKSPAGAWQWVPKDgaAEDTVPDAHDPSKKHAPTMLTTDLALRFDPEYEKISRRFLENPEEFADAFA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 406 RAWFKLTHRDMGPKSRYIGPEVPKEDLIWQDPLPQPIYN-PTEQDIIDLKFAIADSGLSVSELVSVAWASASTFRGGDKR 484
Cdd:PRK15061 396 RAWFKLTHRDMGPKSRYLGPEVPKEDLIWQDPVPAVDHElIDDADIAALKAKILASGLSVSELVSTAWASASTFRGSDKR 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 485 GGANGARLALMPQRDWDVNAAA--VRALPVLEKIQKE-------SGKASLADIIVLAGVVGVEKAASAAGLSIHVPFAPG 555
Cdd:PRK15061 476 GGANGARIRLAPQKDWEVNEPAqlAKVLAVLEGIQAEfnaaqsgGKKVSLADLIVLGGNAAVEQAAKAAGHDVTVPFTPG 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 556 RVDARQDQTDIEMFELLEPIADGFRNYRARLDVSTTESLLIDKAQQLTLTAPEMTALVGGMRVLGANFDGSKNGVFTDRV 635
Cdd:PRK15061 556 RTDATQEQTDVESFAVLEPKADGFRNYLKKGYSVSPEELLVDKAQLLTLTAPEMTVLVGGLRVLGANYGGSKHGVFTDRP 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 636 GVLSNDFFVNLLDMRYEWKATDESKELFEGRDRETGEVKYTASRADLVFGSNSVLRAVAEVYASSDAHEKFVKDFVAAWV 715
Cdd:PRK15061 636 GVLTNDFFVNLLDMGTEWKPTDEDEEVYEGRDRKTGEVKWTATRVDLVFGSNSQLRALAEVYASDDAKEKFVRDFVAAWT 715
|
730
....*....|
gi 1617235220 716 KVMNLDRFDL 725
Cdd:PRK15061 716 KVMNLDRFDL 725
|
|
| KatG |
COG0376 |
Catalase (peroxidase I) [Inorganic ion transport and metabolism]; |
10-725 |
0e+00 |
|
Catalase (peroxidase I) [Inorganic ion transport and metabolism];
Pssm-ID: 440145 [Multi-domain] Cd Length: 731 Bit Score: 1402.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 10 TTATGKCPFHQGGHDQSAGAGTTTRDWWPNQLRVDLLNQHSNRSNPLGEDFDYRKEFSKLDYYGLKKDLKALLTESQPWW 89
Cdd:COG0376 1 MSAEGKCPFMHGAAAAAAGGGTSNRDWWPNQLNLSILHQHSPKSNPMGEDFDYAEAFKKLDLDAVKKDLKALMTDSQDWW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 90 PADWGSYAGLFIRMAWHGAGTYRSIDGRGGAGRGQQRFAPLNSWPDNVSLDKARRLLWPIKQKYGQKISWADLFILAGNV 169
Cdd:COG0376 81 PADYGHYGPLFIRMAWHSAGTYRIGDGRGGAGGGQQRFAPLNSWPDNANLDKARRLLWPIKQKYGNKISWADLMILAGNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 170 ALENSGFRTFGFGAGREDVWEPDLDVNWGDEKAWLT-HRHPE--ALAKaPLGATEMGLIYVNPEGPDHSGEPLSAAAAIR 246
Cdd:COG0376 161 ALESMGFKTFGFAGGREDVWEPEEDVYWGPETEWLGdERYSGdrELEN-PLAAVQMGLIYVNPEGPNGNPDPLAAARDIR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 247 ATFGNMGMNDEETVALIAGGHTLGKTHGAGPTSNVGPDPEAAPIEEQGLGWASTYGSGVGADAITSGLEVVWTQTPTQWS 326
Cdd:COG0376 240 ETFGRMAMNDEETVALIAGGHTFGKTHGAGDAEHVGPEPEAAPIEEQGLGWKNSFGSGKGEDTITSGLEGAWTPTPTQWD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 327 NYFFENLFKYEWVQTRSPAGAIQFEAVD--APEIIPDPFDPSKKRKPTMLVTDLTLRFDPEFEKISRRFLNDPQAFNEAF 404
Cdd:COG0376 320 NGYFDNLFGYEWELTKSPAGAHQWVPKDgaAADTVPDAHDPSKRHAPMMLTTDLALRFDPAYEKISRRFLENPEEFADAF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 405 ARAWFKLTHRDMGPKSRYIGPEVPKEDLIWQDPLPQPIYNP-TEQDIIDLKFAIADSGLSVSELVSVAWASASTFRGGDK 483
Cdd:COG0376 400 ARAWFKLTHRDMGPKSRYLGPEVPAEELIWQDPIPAVDHELiDDADIAALKAKILASGLSVSELVSTAWASASTFRGSDK 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 484 RGGANGARLALMPQRDWDVNAAA--VRALPVLEKIQKE-----SG--KASLADIIVLAGVVGVEKAASAAGLSIHVPFAP 554
Cdd:COG0376 480 RGGANGARIRLAPQKDWEVNEPEqlAKVLAVLEGIQKDfnaaqSGgkKVSLADLIVLGGCAAVEKAAKDAGHDVTVPFTP 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 555 GRVDARQDQTDIEMFELLEPIADGFRNY-RARLDVSTTEsLLIDKAQQLTLTAPEMTALVGGMRVLGANFDGSKNGVFTD 633
Cdd:COG0376 560 GRTDATQEQTDVESFAVLEPKADGFRNYlKKGYSVSAEE-LLVDKAQLLTLTAPEMTVLVGGLRVLGANYGGSKHGVFTD 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 634 RVGVLSNDFFVNLLDMRYEWKATDESKELFEGRDRETGEVKYTASRADLVFGSNSVLRAVAEVYASSDAHEKFVKDFVAA 713
Cdd:COG0376 639 RPGTLTNDFFVNLLDMGTEWKPSSDDEGLFEGRDRKTGEVKWTATRVDLVFGSNSELRALAEVYASDDAKEKFVKDFVAA 718
|
730
....*....|..
gi 1617235220 714 WVKVMNLDRFDL 725
Cdd:COG0376 719 WTKVMNLDRFDL 730
|
|
| cat_per_HPI |
TIGR00198 |
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ... |
18-726 |
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: 1344.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 18 FHQGGHDQSAGAGTTTRDWWPNQLRVDLLNQHSNRSNPLGEDFDYRKEFSKLDYYGLKKDLKALLTESQPWWPADWGSYA 97
Cdd:TIGR00198 1 ASQGGVMHGANTTGQTGDWWPNALNLDILHQHDRKTNPMGEDFDYAEEFQQLDLAAVKQDLKHLMTDSQSWWPADWGHYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 98 GLFIRMAWHGAGTYRSIDGRGGAGRGQQRFAPLNSWPDNVSLDKARRLLWPIKQKYGQKISWADLFILAGNVALENSGFR 177
Cdd:TIGR00198 81 GLFIRMAWHAAGTYRIADGRGGAATGNQRFAPLNSWPDNVNLDKARRLLWPIKKKYGNKLSWADLIILAGTVAYESMGLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 178 TFGFGAGREDVWEPDLDVNWGDEKAWLTH-RHPEALAKAPLGATEMGLIYVNPEGPDHSGEPLSAAAAIRATFGNMGMND 256
Cdd:TIGR00198 161 VFGFAGGREDIWEPDKDIYWGAEKEWLTSsREDRESLENPLAATEMGLIYVNPEGPDGHPDPLCTAQDIRTTFARMGMND 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 257 EETVALIAGGHTLGKTHGAGPTSNVGPDPEAAPIEEQGLGWASTYGSGVGADAITSGLEVVWTQTPTQWSNYFFENLFKY 336
Cdd:TIGR00198 241 EETVALIAGGHTVGKCHGAGPAELIGPDPEGAPIEEQGLGWHNQYGKGVGRDTMTSGLEVAWTTTPTQWDNGYFYMLFNY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 337 EWVQTRSPAGAIQFEAVDAPEIIPDPFDPSKKRKPTMLVTDLTLRFDPEFEKISRRFLNDPQAFNEAFARAWFKLTHRDM 416
Cdd:TIGR00198 321 EWELKKSPAGAWQWEAVDAPEIIPDVEDPNKKHNPIMLDADLALRFDPEFRKISRRFLREPDYFAEAFAKAWFKLTHRDM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 417 GPKSRYIGPEVPKEDLIWQDPLPQPIYNPTEQDIIDLKFAIADSGLSVSELVSVAWASASTFRGGDKRGGANGARLALMP 496
Cdd:TIGR00198 401 GPKSRYIGPDVPQEDLIWQDPLPPVDYTLSEGDIKELKQQILASGLSVSELVCTAWASASTFRSSDYRGGANGARIRLEP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 497 QRDWDVN--AAAVRALPVLEKIQKES--GKASLADIIVLAGVVGVEKAASAAGLSIHVPFAPGRVDARQDQTDIEMFELL 572
Cdd:TIGR00198 481 QKNWPVNepTRLAKVLAVLEKIQAEFakGPVSLADLIVLGGGAAVEKAALDAGISVNVPFLPGRVDATQAMTDAESFTPL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 573 EPIADGFRNYRARLDVSTTESLLIDKAQQLTLTAPEMTALVGGMRVLGANFDGSKNGVFTDRVGVLSNDFFVNLLDMRYE 652
Cdd:TIGR00198 561 EPIADGFRNYLKRDYAVTPEELLLDKAQLLTLTAPEMTVLIGGMRVLGANHGGSKHGVFTDRVGVLSNDFFVNLLDMAYE 640
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1617235220 653 WKATDESKELFEGRDRETGEVKYTASRADLVFGSNSVLRAVAEVYASSDAHEKFVKDFVAAWVKVMNLDRFDLL 726
Cdd:TIGR00198 641 WRAADNNRYLFEGGDRQTGEVKWTATRVDLVFGSNSILRAVAEVYAQDDAREKFVKDFVAAWTKVMNLDRFDLP 714
|
|
| 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: 733.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 28 GAGTTTRDWWPNQLRVDLLNQHSNRSNPLGEDFDYRKEFSKLDYYGLKKDLKALLTESQPWWPADWGSYAGLFIRMAWHG 107
Cdd:cd00649 1 GGGTSNQDWWPNRLNLKILHQHSPKSNPMGEDFNYAEEFKKLDLEALKEDLKALMTDSQDWWPADYGHYGPLFIRMAWHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 108 AGTYRSIDGRGGAGRGQQRFAPLNSWPDNVSLDKARRLLWPIKQKYGQKISWADLFILAGNVALENSGFRTFGFGAGRED 187
Cdd:cd00649 81 AGTYRIADGRGGAGTGQQRFAPLNSWPDNVNLDKARRLLWPIKQKYGNKISWADLMILAGNVALESMGFKTFGFAGGRED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 188 VWEPDLDVNWGDEKAWLT---HRHPEALAKaPLGATEMGLIYVNPEGPDHSGEPLSAAAAIRATFGNMGMNDEETVALIA 264
Cdd:cd00649 161 VWEPDEDVYWGPEKEWLAdkrYSGDRDLEN-PLAAVQMGLIYVNPEGPDGNPDPLAAAKDIRETFARMAMNDEETVALIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 265 GGHTLGKTHGAGPTSNVGPDPEAAPIEEQGLGWASTYGSGVGADAITSGLEVVWTQTPTQWSNYFFENLFKYEWVQTRSP 344
Cdd:cd00649 240 GGHTFGKTHGAGPASHVGPEPEAAPIEQQGLGWKNSYGTGKGKDTITSGLEGAWTPTPTKWDNNYLKNLFGYEWELTKSP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 345 AGAIQFEAVDA--PEIIPDPFDPSKKRKPTMLVTDLTLRFDPEFEKISRRFLNDPQAFNEAFARAWFKLTHRDMGPKSRY 422
Cdd:cd00649 320 AGAWQWVPKNAagENTVPDAHDPSKKHAPMMLTTDLALRFDPEYEKISRRFLENPDEFADAFAKAWFKLTHRDMGPKSRY 399
|
410
....*....|
gi 1617235220 423 IGPEVPKEDL 432
Cdd:cd00649 400 LGPEVPEEDL 409
|
|
| peroxidase |
pfam00141 |
Peroxidase; |
89-273 |
2.85e-32 |
|
Peroxidase;
Pssm-ID: 425483 [Multi-domain] Cd Length: 187 Bit Score: 123.44 E-value: 2.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 89 WPADWGSYAGLFIRMAWHGAGT---YRSIdgrggagrGQQRFAPLNSWPDNVSLDKARRLLWPIKQKY----GQKISWAD 161
Cdd:pfam00141 8 AFKADPTMGPSLLRLHFHDCFVggcDGSV--------LLDGFKPEKDAPPNLGLRKGFEVIDDIKAKLeaacPGVVSCAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 162 LFILAGNVALENSGFRTFGFGAGREDVWEPDLDvnwgdekawlthrhpealakaplgatemgliYVNPEGPDhsgePLSA 241
Cdd:pfam00141 80 ILALAARDAVELAGGPSWPVPLGRRDGTVSSAV-------------------------------EANSNLPA----PTDS 124
|
170 180 190
....*....|....*....|....*....|..
gi 1617235220 242 AAAIRATFGNMGMNDEETVALiAGGHTLGKTH 273
Cdd:pfam00141 125 LDQLRDRFARKGLTAEDLVAL-SGAHTIGRAH 155
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15061 |
PRK15061 |
catalase/peroxidase; |
11-725 |
0e+00 |
|
catalase/peroxidase;
Pssm-ID: 237891 [Multi-domain] Cd Length: 726 Bit Score: 1433.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 11 TATGKCPFHQGghdqsAGAGTTTRDWWPNQLRVDLLNQHSNRSNPLGEDFDYRKEFSKLDYYGLKKDLKALLTESQPWWP 90
Cdd:PRK15061 1 SSAGKCPVMHG-----AGGGTSNRDWWPNQLNLDILHQHSSKSNPMGEDFDYAEEFKKLDLEALKKDLKALMTDSQDWWP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 91 ADWGSYAGLFIRMAWHGAGTYRSIDGRGGAGRGQQRFAPLNSWPDNVSLDKARRLLWPIKQKYGQKISWADLFILAGNVA 170
Cdd:PRK15061 76 ADYGHYGPLFIRMAWHSAGTYRIGDGRGGAGGGQQRFAPLNSWPDNVNLDKARRLLWPIKQKYGNKISWADLMILAGNVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 171 LENSGFRTFGFGAGREDVWEPDLDVNWGDEKAWLT--HRH-PEALAKAPLGATEMGLIYVNPEGPDHSGEPLSAAAAIRA 247
Cdd:PRK15061 156 LESMGFKTFGFAGGREDVWEPEEDVYWGPEKEWLGgdERYsGERDLENPLAAVQMGLIYVNPEGPNGNPDPLAAARDIRE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 248 TFGNMGMNDEETVALIAGGHTLGKTHGAGPTSNVGPDPEAAPIEEQGLGWASTYGSGVGADAITSGLEVVWTQTPTQWSN 327
Cdd:PRK15061 236 TFARMAMNDEETVALIAGGHTFGKTHGAGDASHVGPEPEAAPIEEQGLGWKNSYGSGKGADTITSGLEGAWTTTPTQWDN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 328 YFFENLFKYEWVQTRSPAGAIQFEAVD--APEIIPDPFDPSKKRKPTMLVTDLTLRFDPEFEKISRRFLNDPQAFNEAFA 405
Cdd:PRK15061 316 GYFENLFGYEWELTKSPAGAWQWVPKDgaAEDTVPDAHDPSKKHAPTMLTTDLALRFDPEYEKISRRFLENPEEFADAFA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 406 RAWFKLTHRDMGPKSRYIGPEVPKEDLIWQDPLPQPIYN-PTEQDIIDLKFAIADSGLSVSELVSVAWASASTFRGGDKR 484
Cdd:PRK15061 396 RAWFKLTHRDMGPKSRYLGPEVPKEDLIWQDPVPAVDHElIDDADIAALKAKILASGLSVSELVSTAWASASTFRGSDKR 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 485 GGANGARLALMPQRDWDVNAAA--VRALPVLEKIQKE-------SGKASLADIIVLAGVVGVEKAASAAGLSIHVPFAPG 555
Cdd:PRK15061 476 GGANGARIRLAPQKDWEVNEPAqlAKVLAVLEGIQAEfnaaqsgGKKVSLADLIVLGGNAAVEQAAKAAGHDVTVPFTPG 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 556 RVDARQDQTDIEMFELLEPIADGFRNYRARLDVSTTESLLIDKAQQLTLTAPEMTALVGGMRVLGANFDGSKNGVFTDRV 635
Cdd:PRK15061 556 RTDATQEQTDVESFAVLEPKADGFRNYLKKGYSVSPEELLVDKAQLLTLTAPEMTVLVGGLRVLGANYGGSKHGVFTDRP 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 636 GVLSNDFFVNLLDMRYEWKATDESKELFEGRDRETGEVKYTASRADLVFGSNSVLRAVAEVYASSDAHEKFVKDFVAAWV 715
Cdd:PRK15061 636 GVLTNDFFVNLLDMGTEWKPTDEDEEVYEGRDRKTGEVKWTATRVDLVFGSNSQLRALAEVYASDDAKEKFVRDFVAAWT 715
|
730
....*....|
gi 1617235220 716 KVMNLDRFDL 725
Cdd:PRK15061 716 KVMNLDRFDL 725
|
|
| KatG |
COG0376 |
Catalase (peroxidase I) [Inorganic ion transport and metabolism]; |
10-725 |
0e+00 |
|
Catalase (peroxidase I) [Inorganic ion transport and metabolism];
Pssm-ID: 440145 [Multi-domain] Cd Length: 731 Bit Score: 1402.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 10 TTATGKCPFHQGGHDQSAGAGTTTRDWWPNQLRVDLLNQHSNRSNPLGEDFDYRKEFSKLDYYGLKKDLKALLTESQPWW 89
Cdd:COG0376 1 MSAEGKCPFMHGAAAAAAGGGTSNRDWWPNQLNLSILHQHSPKSNPMGEDFDYAEAFKKLDLDAVKKDLKALMTDSQDWW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 90 PADWGSYAGLFIRMAWHGAGTYRSIDGRGGAGRGQQRFAPLNSWPDNVSLDKARRLLWPIKQKYGQKISWADLFILAGNV 169
Cdd:COG0376 81 PADYGHYGPLFIRMAWHSAGTYRIGDGRGGAGGGQQRFAPLNSWPDNANLDKARRLLWPIKQKYGNKISWADLMILAGNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 170 ALENSGFRTFGFGAGREDVWEPDLDVNWGDEKAWLT-HRHPE--ALAKaPLGATEMGLIYVNPEGPDHSGEPLSAAAAIR 246
Cdd:COG0376 161 ALESMGFKTFGFAGGREDVWEPEEDVYWGPETEWLGdERYSGdrELEN-PLAAVQMGLIYVNPEGPNGNPDPLAAARDIR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 247 ATFGNMGMNDEETVALIAGGHTLGKTHGAGPTSNVGPDPEAAPIEEQGLGWASTYGSGVGADAITSGLEVVWTQTPTQWS 326
Cdd:COG0376 240 ETFGRMAMNDEETVALIAGGHTFGKTHGAGDAEHVGPEPEAAPIEEQGLGWKNSFGSGKGEDTITSGLEGAWTPTPTQWD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 327 NYFFENLFKYEWVQTRSPAGAIQFEAVD--APEIIPDPFDPSKKRKPTMLVTDLTLRFDPEFEKISRRFLNDPQAFNEAF 404
Cdd:COG0376 320 NGYFDNLFGYEWELTKSPAGAHQWVPKDgaAADTVPDAHDPSKRHAPMMLTTDLALRFDPAYEKISRRFLENPEEFADAF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 405 ARAWFKLTHRDMGPKSRYIGPEVPKEDLIWQDPLPQPIYNP-TEQDIIDLKFAIADSGLSVSELVSVAWASASTFRGGDK 483
Cdd:COG0376 400 ARAWFKLTHRDMGPKSRYLGPEVPAEELIWQDPIPAVDHELiDDADIAALKAKILASGLSVSELVSTAWASASTFRGSDK 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 484 RGGANGARLALMPQRDWDVNAAA--VRALPVLEKIQKE-----SG--KASLADIIVLAGVVGVEKAASAAGLSIHVPFAP 554
Cdd:COG0376 480 RGGANGARIRLAPQKDWEVNEPEqlAKVLAVLEGIQKDfnaaqSGgkKVSLADLIVLGGCAAVEKAAKDAGHDVTVPFTP 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 555 GRVDARQDQTDIEMFELLEPIADGFRNY-RARLDVSTTEsLLIDKAQQLTLTAPEMTALVGGMRVLGANFDGSKNGVFTD 633
Cdd:COG0376 560 GRTDATQEQTDVESFAVLEPKADGFRNYlKKGYSVSAEE-LLVDKAQLLTLTAPEMTVLVGGLRVLGANYGGSKHGVFTD 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 634 RVGVLSNDFFVNLLDMRYEWKATDESKELFEGRDRETGEVKYTASRADLVFGSNSVLRAVAEVYASSDAHEKFVKDFVAA 713
Cdd:COG0376 639 RPGTLTNDFFVNLLDMGTEWKPSSDDEGLFEGRDRKTGEVKWTATRVDLVFGSNSELRALAEVYASDDAKEKFVKDFVAA 718
|
730
....*....|..
gi 1617235220 714 WVKVMNLDRFDL 725
Cdd:COG0376 719 WTKVMNLDRFDL 730
|
|
| cat_per_HPI |
TIGR00198 |
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ... |
18-726 |
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: 1344.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 18 FHQGGHDQSAGAGTTTRDWWPNQLRVDLLNQHSNRSNPLGEDFDYRKEFSKLDYYGLKKDLKALLTESQPWWPADWGSYA 97
Cdd:TIGR00198 1 ASQGGVMHGANTTGQTGDWWPNALNLDILHQHDRKTNPMGEDFDYAEEFQQLDLAAVKQDLKHLMTDSQSWWPADWGHYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 98 GLFIRMAWHGAGTYRSIDGRGGAGRGQQRFAPLNSWPDNVSLDKARRLLWPIKQKYGQKISWADLFILAGNVALENSGFR 177
Cdd:TIGR00198 81 GLFIRMAWHAAGTYRIADGRGGAATGNQRFAPLNSWPDNVNLDKARRLLWPIKKKYGNKLSWADLIILAGTVAYESMGLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 178 TFGFGAGREDVWEPDLDVNWGDEKAWLTH-RHPEALAKAPLGATEMGLIYVNPEGPDHSGEPLSAAAAIRATFGNMGMND 256
Cdd:TIGR00198 161 VFGFAGGREDIWEPDKDIYWGAEKEWLTSsREDRESLENPLAATEMGLIYVNPEGPDGHPDPLCTAQDIRTTFARMGMND 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 257 EETVALIAGGHTLGKTHGAGPTSNVGPDPEAAPIEEQGLGWASTYGSGVGADAITSGLEVVWTQTPTQWSNYFFENLFKY 336
Cdd:TIGR00198 241 EETVALIAGGHTVGKCHGAGPAELIGPDPEGAPIEEQGLGWHNQYGKGVGRDTMTSGLEVAWTTTPTQWDNGYFYMLFNY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 337 EWVQTRSPAGAIQFEAVDAPEIIPDPFDPSKKRKPTMLVTDLTLRFDPEFEKISRRFLNDPQAFNEAFARAWFKLTHRDM 416
Cdd:TIGR00198 321 EWELKKSPAGAWQWEAVDAPEIIPDVEDPNKKHNPIMLDADLALRFDPEFRKISRRFLREPDYFAEAFAKAWFKLTHRDM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 417 GPKSRYIGPEVPKEDLIWQDPLPQPIYNPTEQDIIDLKFAIADSGLSVSELVSVAWASASTFRGGDKRGGANGARLALMP 496
Cdd:TIGR00198 401 GPKSRYIGPDVPQEDLIWQDPLPPVDYTLSEGDIKELKQQILASGLSVSELVCTAWASASTFRSSDYRGGANGARIRLEP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 497 QRDWDVN--AAAVRALPVLEKIQKES--GKASLADIIVLAGVVGVEKAASAAGLSIHVPFAPGRVDARQDQTDIEMFELL 572
Cdd:TIGR00198 481 QKNWPVNepTRLAKVLAVLEKIQAEFakGPVSLADLIVLGGGAAVEKAALDAGISVNVPFLPGRVDATQAMTDAESFTPL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 573 EPIADGFRNYRARLDVSTTESLLIDKAQQLTLTAPEMTALVGGMRVLGANFDGSKNGVFTDRVGVLSNDFFVNLLDMRYE 652
Cdd:TIGR00198 561 EPIADGFRNYLKRDYAVTPEELLLDKAQLLTLTAPEMTVLIGGMRVLGANHGGSKHGVFTDRVGVLSNDFFVNLLDMAYE 640
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1617235220 653 WKATDESKELFEGRDRETGEVKYTASRADLVFGSNSVLRAVAEVYASSDAHEKFVKDFVAAWVKVMNLDRFDLL 726
Cdd:TIGR00198 641 WRAADNNRYLFEGGDRQTGEVKWTATRVDLVFGSNSILRAVAEVYAQDDAREKFVKDFVAAWTKVMNLDRFDLP 714
|
|
| 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: 733.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 28 GAGTTTRDWWPNQLRVDLLNQHSNRSNPLGEDFDYRKEFSKLDYYGLKKDLKALLTESQPWWPADWGSYAGLFIRMAWHG 107
Cdd:cd00649 1 GGGTSNQDWWPNRLNLKILHQHSPKSNPMGEDFNYAEEFKKLDLEALKEDLKALMTDSQDWWPADYGHYGPLFIRMAWHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 108 AGTYRSIDGRGGAGRGQQRFAPLNSWPDNVSLDKARRLLWPIKQKYGQKISWADLFILAGNVALENSGFRTFGFGAGRED 187
Cdd:cd00649 81 AGTYRIADGRGGAGTGQQRFAPLNSWPDNVNLDKARRLLWPIKQKYGNKISWADLMILAGNVALESMGFKTFGFAGGRED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 188 VWEPDLDVNWGDEKAWLT---HRHPEALAKaPLGATEMGLIYVNPEGPDHSGEPLSAAAAIRATFGNMGMNDEETVALIA 264
Cdd:cd00649 161 VWEPDEDVYWGPEKEWLAdkrYSGDRDLEN-PLAAVQMGLIYVNPEGPDGNPDPLAAAKDIRETFARMAMNDEETVALIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 265 GGHTLGKTHGAGPTSNVGPDPEAAPIEEQGLGWASTYGSGVGADAITSGLEVVWTQTPTQWSNYFFENLFKYEWVQTRSP 344
Cdd:cd00649 240 GGHTFGKTHGAGPASHVGPEPEAAPIEQQGLGWKNSYGTGKGKDTITSGLEGAWTPTPTKWDNNYLKNLFGYEWELTKSP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 345 AGAIQFEAVDA--PEIIPDPFDPSKKRKPTMLVTDLTLRFDPEFEKISRRFLNDPQAFNEAFARAWFKLTHRDMGPKSRY 422
Cdd:cd00649 320 AGAWQWVPKNAagENTVPDAHDPSKKHAPMMLTTDLALRFDPEYEKISRRFLENPDEFADAFAKAWFKLTHRDMGPKSRY 399
|
410
....*....|
gi 1617235220 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 |
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: 529.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 436 DPLPQPIY-NPTEQDIIDLKFAIADSGLSVSELVSVAWASASTFRGGDKRGGANGARLALMPQRDWDVN--AAAVRALPV 512
Cdd:cd08200 1 DPIPAVDYeLIDDADIAALKAKILASGLTVSELVSTAWASASTFRNSDKRGGANGARIRLAPQKDWEVNepEELAKVLAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 513 LEKIQKESG-------KASLADIIVLAGVVGVEKAASAAGLSIHVPFAPGRVDARQDQTDIEMFELLEPIADGFRNYRAR 585
Cdd:cd08200 81 LEGIQKEFNesqsggkKVSLADLIVLGGCAAVEKAAKDAGVDIKVPFTPGRTDATQEQTDVESFEVLEPKADGFRNYLKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 586 LDVSTTESLLIDKAQQLTLTAPEMTALVGGMRVLGANFDGSKNGVFTDRVGVLSNDFFVNLLDMRYEWKATDESKELFEG 665
Cdd:cd08200 161 GYRVPPEEMLVDKAQLLTLTAPEMTVLVGGLRVLGANYGGSKHGVFTDRPGVLTNDFFVNLLDMSTEWKPADEDDGLFEG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1617235220 666 RDRETGEVKYTASRADLVFGSNSVLRAVAEVYASSDAHEKFVKDFVAAWVKVMNLDR 722
Cdd:cd08200 241 RDRKTGEVKWTATRVDLVFGSNSELRAVAEVYASDDAQEKFVKDFVAAWTKVMNLDR 297
|
|
| plant_peroxidase_like |
cd00314 |
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ... |
91-413 |
4.94e-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: 167.33 E-value: 4.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 91 ADWGSYAGLFIRMAWHGAGTYRSIDGRGGAGRGQQRFAPLNSWPDNVSLDKARRLLWPIKQKYG--QKISWADLFILAGN 168
Cdd:cd00314 12 TQAGALAGSLLRLAFHDAGTYDIADGKGGGADGSIRFEPELDRPENGGLDKALRALEPIKSAYDggNPVSRADLIALAGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 169 VALENS--GFRTFGFGAGREDvwepdldvnwgdekawlthrhpealakaplgATEMGLIYVNPEGPDhsGEPLSAAAAIR 246
Cdd:cd00314 92 VAVESTfgGGPLIPFRFGRLD-------------------------------ATEPDLGVPDPEGLL--PNETSSATELR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 247 ATFGNMGMNDEETVALIAGGHTL-GKTHGagptsnvgpdpeaapieeqglgwastygsgvgaDAITSGLEVVWTQTPTQW 325
Cdd:cd00314 139 DKFKRMGLSPSELVALSAGAHTLgGKNHG---------------------------------DLLNYEGSGLWTSTPFTF 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 326 SNYFFENLFKYEWvqtrspagaiqfeavdapEIIPDPFDPSKKRKPTMLVTDLTLRFDPEFEKISRRFLNDPQAFNEAFA 405
Cdd:cd00314 186 DNAYFKNLLDMNW------------------EWRVGSPDPDGVKGPGLLPSDYALLSDSETRALVERYASDQEKFFEDFA 247
|
....*...
gi 1617235220 406 RAWFKLTH 413
Cdd:cd00314 248 KAWIKMVN 255
|
|
| plant_peroxidase_like |
cd00314 |
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ... |
457-719 |
2.86e-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: 156.93 E-value: 2.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 457 IADSGLSVSELVSVAWASASTFRGGDKRGGANGARLALMPQRDWDVNAAAVRALPVLEKIQKE---SGKASLADIIVLAG 533
Cdd:cd00314 11 ITQAGALAGSLLRLAFHDAGTYDIADGKGGGADGSIRFEPELDRPENGGLDKALRALEPIKSAydgGNPVSRADLIALAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 534 VVGVEkaaSAAGLSIHVPFAPGRVDArqdqtdiemFELLEPIADGFRNYRARLDVSTTeslLIDKAQQLTLTAPEMTALV 613
Cdd:cd00314 91 AVAVE---STFGGGPLIPFRFGRLDA---------TEPDLGVPDPEGLLPNETSSATE---LRDKFKRMGLSPSELVALS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 614 GGMRVL-----GANFDGSKNGVFTDRVGVLSNDFFVNLLDMRYEWKAtdeskelfeGRDRETGEVKYTASRADLVFGSNS 688
Cdd:cd00314 156 AGAHTLggknhGDLLNYEGSGLWTSTPFTFDNAYFKNLLDMNWEWRV---------GSPDPDGVKGPGLLPSDYALLSDS 226
|
250 260 270
....*....|....*....|....*....|.
gi 1617235220 689 VLRAVAEVYASSDahEKFVKDFVAAWVKVMN 719
Cdd:cd00314 227 ETRALVERYASDQ--EKFFEDFAKAWIKMVN 255
|
|
| ascorbate_peroxidase |
cd00691 |
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ... |
70-412 |
2.02e-33 |
|
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: 128.86 E-value: 2.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 70 DYYGLKKDLKALLTEsqpwwpadwGSYAGLFIRMAWHGAGTYR----------SIdgrggagrgqqRFAPLNSWPDNVSL 139
Cdd:cd00691 12 DLEAARNDIAKLIDD---------KNCAPILVRLAWHDSGTYDketktggsngTI-----------RFDPELNHGANAGL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 140 DKARRLLWPIKQKYgQKISWADLFILAGNVALENSGFRTFGFGAGREDVWEPDldvnwgdekawlthrhpealakaplga 219
Cdd:cd00691 72 DIARKLLEPIKKKY-PDISYADLWQLAGVVAIEEMGGPKIPFRPGRVDASDPE--------------------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 220 temgliYVNPEG--PDHSGeplsAAAAIRATFGNMGMNDEETVALIaGGHTLGKTHgagptsnvgpdPEAapieeqglgw 297
Cdd:cd00691 124 ------ECPPEGrlPDASK----GADHLRDVFYRMGFNDQEIVALS-GAHTLGRCH-----------KER---------- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 298 astygsgvgadaitSGLEVVWTQTPTQWSNYFFENLFKYEWVqtrspagaiqfeaVDAPEIIpdpfdpskkrkptMLVTD 377
Cdd:cd00691 172 --------------SGYDGPWTKNPLKFDNSYFKELLEEDWK-------------LPTPGLL-------------MLPTD 211
|
330 340 350
....*....|....*....|....*....|....*
gi 1617235220 378 LTLRFDPEFEKISRRFLNDPQAFNEAFARAWFKLT 412
Cdd:cd00691 212 KALLEDPKFRPYVELYAKDQDAFFKDYAEAHKKLS 246
|
|
| peroxidase |
pfam00141 |
Peroxidase; |
89-273 |
2.85e-32 |
|
Peroxidase;
Pssm-ID: 425483 [Multi-domain] Cd Length: 187 Bit Score: 123.44 E-value: 2.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 89 WPADWGSYAGLFIRMAWHGAGT---YRSIdgrggagrGQQRFAPLNSWPDNVSLDKARRLLWPIKQKY----GQKISWAD 161
Cdd:pfam00141 8 AFKADPTMGPSLLRLHFHDCFVggcDGSV--------LLDGFKPEKDAPPNLGLRKGFEVIDDIKAKLeaacPGVVSCAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 162 LFILAGNVALENSGFRTFGFGAGREDVWEPDLDvnwgdekawlthrhpealakaplgatemgliYVNPEGPDhsgePLSA 241
Cdd:pfam00141 80 ILALAARDAVELAGGPSWPVPLGRRDGTVSSAV-------------------------------EANSNLPA----PTDS 124
|
170 180 190
....*....|....*....|....*....|..
gi 1617235220 242 AAAIRATFGNMGMNDEETVALiAGGHTLGKTH 273
Cdd:pfam00141 125 LDQLRDRFARKGLTAEDLVAL-SGAHTIGRAH 155
|
|
| peroxidase |
pfam00141 |
Peroxidase; |
485-700 |
1.40e-22 |
|
Peroxidase;
Pssm-ID: 425483 [Multi-domain] Cd Length: 187 Bit Score: 95.71 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 485 GGANGARL--ALMPQRDWDVNAAAVRALPVLEKIQKESGKA-----SLADIIVLAGVVGVEKaasAAGLSIhvPFAPGRV 557
Cdd:pfam00141 30 GGCDGSVLldGFKPEKDAPPNLGLRKGFEVIDDIKAKLEAAcpgvvSCADILALAARDAVEL---AGGPSW--PVPLGRR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 558 DARQDQTDiEMFELLePiadgfrnyRARLDVSTteslLIDKAQQLTLTAPEMTALvGGMRVLGANfdgskngvftdrvgv 637
Cdd:pfam00141 105 DGTVSSAV-EANSNL-P--------APTDSLDQ----LRDRFARKGLTAEDLVAL-SGAHTIGRA--------------- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1617235220 638 lsndfFVNLLDMRyewkatdeskelfegrdretgevkyTASRADLVFGSNSVLRAVAEVYASS 700
Cdd:pfam00141 155 -----HKNLLDGR-------------------------GLLTSDQALLSDPRTRALVERYAAD 187
|
|
| PLN02608 |
PLN02608 |
L-ascorbate peroxidase |
59-420 |
1.35e-14 |
|
L-ascorbate peroxidase
Pssm-ID: 178218 [Multi-domain] Cd Length: 289 Bit Score: 74.80 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 59 DFDYRKEFSKLdyyglKKDLKALLTESqpwwpadwgSYAGLFIRMAWHGAGTYrSIDGRGGAGRGQQRFAPLNSWPDNVS 138
Cdd:PLN02608 7 DAEYLKEIEKA-----RRDLRALIASK---------NCAPIMLRLAWHDAGTY-DAKTKTGGPNGSIRNEEEYSHGANNG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 139 LDKARRLLWPIKQKYgQKISWADLFILAGNVALENSGFRTFGFGAGRED-VWEPDldvnwgdekawlTHRHPEAlakapl 217
Cdd:PLN02608 72 LKIAIDLCEPVKAKH-PKITYADLYQLAGVVAVEVTGGPTIDFVPGRKDsNACPE------------EGRLPDA------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 218 gatemgliyvnPEGPDHsgeplsaaaaIRATFGNMGMNDEETVALiAGGHTLGKTHgagptsnvgpdPEaapieeqglgw 297
Cdd:PLN02608 133 -----------KKGAKH----------LRDVFYRMGLSDKDIVAL-SGGHTLGRAH-----------PE----------- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 298 astygsgvgadaiTSGLEVVWTQTPTQWSNYFFENLFKYEwvqtrsPAGAIQfeavdapeiipdpfdpskkrkptmLVTD 377
Cdd:PLN02608 169 -------------RSGFDGPWTKEPLKFDNSYFVELLKGE------SEGLLK------------------------LPTD 205
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1617235220 378 LTLRFDPEFEKISRRFLNDPQAFNEAFARAWFKLTHRDMGPKS 420
Cdd:PLN02608 206 KALLEDPEFRPYVELYAKDEDAFFRDYAESHKKLSELGFTPPS 248
|
|
| PLN02879 |
PLN02879 |
L-ascorbate peroxidase |
51-412 |
5.01e-14 |
|
L-ascorbate peroxidase
Pssm-ID: 178467 [Multi-domain] Cd Length: 251 Bit Score: 72.40 E-value: 5.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 51 NRSNPLGEDfDYRKEFSKLdyyglKKDLKALLTESQpwwpadwgsYAGLFIRMAWHGAGTYRSIDGRGGAGRGQQRFAPL 130
Cdd:PLN02879 3 KKSYPEVKE-EYKKAVQRC-----KRKLRGLIAEKH---------CAPIVLRLAWHSAGTFDVKTKTGGPFGTIRHPQEL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 131 NSWPDNvSLDKARRLLWPIKQKYgQKISWADLFILAGNVALENSGFRTFGFGAGREDVWEPDLDvnwgdekawltHRHPE 210
Cdd:PLN02879 68 AHDANN-GLDIAVRLLDPIKELF-PILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVEPPPE-----------GRLPQ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 211 AlakaplgatemgliyvnPEGPDHsgeplsaaaaIRATFGNMGMNDEETVALiAGGHTLGKTHgagptsnvgpdpeaapi 290
Cdd:PLN02879 135 A-----------------TKGVDH----------LRDVFGRMGLNDKDIVAL-SGGHTLGRCH----------------- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 291 EEQglgwastygsgvgadaitSGLEVVWTQTPTQWSNYFFENLFKYEwvqtrsPAGAIQfeavdapeiipdpfdpskkrk 370
Cdd:PLN02879 170 KER------------------SGFEGAWTPNPLIFDNSYFKEILSGE------KEGLLQ--------------------- 204
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1617235220 371 ptmLVTDLTLRFDPEFEKISRRFLNDPQAFNEAFARAWFKLT 412
Cdd:PLN02879 205 ---LPTDKALLDDPLFLPFVEKYAADEDAFFEDYTEAHLKLS 243
|
|
| ascorbate_peroxidase |
cd00691 |
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ... |
467-720 |
9.65e-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: 68.77 E-value: 9.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 467 LVSVAWASASTFRGGDKRGGANGA-RLAlmPQRDWDVNAAAVRALPVLEKIQKESGKASLADIIVLAGVVGVEKAASAAg 545
Cdd:cd00691 33 LVRLAWHDSGTYDKETKTGGSNGTiRFD--PELNHGANAGLDIARKLLEPIKKKYPDISYADLWQLAGVVAIEEMGGPK- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 546 lsihVPFAPGRVDARQDQtdiemfellEPIADGfrnyraRL-DVSTTESLLIDKAQQLTLTAPEMTALVGGMRVLGANFD 624
Cdd:cd00691 110 ----IPFRPGRVDASDPE---------ECPPEG------RLpDASKGADHLRDVFYRMGFNDQEIVALSGAHTLGRCHKE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 625 GS-KNGVFTDRVGVLSNDFFVNLLDMRYEWK-------ATDesKELFEgrdretgevkytasraDLVFgsnsvlRAVAEV 696
Cdd:cd00691 171 RSgYDGPWTKNPLKFDNSYFKELLEEDWKLPtpgllmlPTD--KALLE----------------DPKF------RPYVEL 226
|
250 260
....*....|....*....|....
gi 1617235220 697 YASSDahEKFVKDFVAAWVKVMNL 720
Cdd:cd00691 227 YAKDQ--DAFFKDYAEAHKKLSEL 248
|
|
| PLN02364 |
PLN02364 |
L-ascorbate peroxidase 1 |
61-412 |
2.53e-11 |
|
L-ascorbate peroxidase 1
Pssm-ID: 166005 Cd Length: 250 Bit Score: 64.72 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 61 DYRKEFSKLdyyglKKDLKALLTESqpwwpadwgSYAGLFIRMAWHGAGTYrSIDGRGGAGRGQQRFAPLNSWPDNVSLD 140
Cdd:PLN02364 11 DYKKAVEKC-----RRKLRGLIAEK---------NCAPIMVRLAWHSAGTF-DCQSRTGGPFGTMRFDAEQAHGANSGIH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 141 KARRLLWPIKQKYgQKISWADLFILAGNVALENSGFRTFGFGAGREDVWEPDLDvnwgdekawltHRHPEAlakaplgat 220
Cdd:PLN02364 76 IALRLLDPIREQF-PTISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPPPE-----------GRLPDA--------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 221 emgliyvnPEGPDHsgeplsaaaaIRATFG-NMGMNDEETVALiAGGHTLGKTHGAgptsnvgpdpeaapieeqglgwas 299
Cdd:PLN02364 135 --------TKGCDH----------LRDVFAkQMGLSDKDIVAL-SGAHTLGRCHKD------------------------ 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 300 tygsgvgadaiTSGLEVVWTQTPTQWSNYFFENLFKYEwvqtrsPAGAIQfeavdapeiipdpfdpskkrkptmLVTDLT 379
Cdd:PLN02364 172 -----------RSGFEGAWTSNPLIFDNSYFKELLSGE------KEGLLQ------------------------LVSDKA 210
|
330 340 350
....*....|....*....|....*....|...
gi 1617235220 380 LRFDPEFEKISRRFLNDPQAFNEAFARAWFKLT 412
Cdd:PLN02364 211 LLDDPVFRPLVEKYAADEDAFFADYAEAHMKLS 243
|
|
| catalase_peroxidase_1 |
cd00649 |
N-terminal catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ... |
471-566 |
2.16e-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: 53.85 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 471 AWASASTFRGGDKRGGANGARLALMPQRDWDVNAAAVRALPVLEKIQKESG-KASLADIIVLAGVVGVEkaasAAGLSIh 549
Cdd:cd00649 77 AWHSAGTYRIADGRGGAGTGQQRFAPLNSWPDNVNLDKARRLLWPIKQKYGnKISWADLMILAGNVALE----SMGFKT- 151
|
90
....*....|....*..
gi 1617235220 550 VPFAPGRVDARQDQTDI 566
Cdd:cd00649 152 FGFAGGREDVWEPDEDV 168
|
|
| secretory_peroxidase |
cd00693 |
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ... |
238-407 |
1.09e-06 |
|
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: 50.98 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 238 PLSAAAAIRATFGNMGMNDEETVALiAGGHTLGKTHGA-------GPTSNVGPDPEAAPIEEQGLGWAStygSGVGADAI 310
Cdd:cd00693 139 PFFSVSQLISLFASKGLTVTDLVAL-SGAHTIGRAHCSsfsdrlyNFSGTGDPDPTLDPAYAAQLRKKC---PAGGDDDT 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 311 TSGLEVVwtqTPTQWSNYFFENLfkyewvqtrspagaiqfeavdapeiipdpfdpsKKRKpTMLVTDLTLRFDPEFEKIS 390
Cdd:cd00693 215 LVPLDPG---TPNTFDNSYYKNL---------------------------------LAGR-GLLTSDQALLSDPRTRAIV 257
|
170
....*....|....*..
gi 1617235220 391 RRFLNDPQAFNEAFARA 407
Cdd:cd00693 258 NRYAANQDAFFRDFAAA 274
|
|
| PLN02364 |
PLN02364 |
L-ascorbate peroxidase 1 |
467-720 |
3.71e-06 |
|
L-ascorbate peroxidase 1
Pssm-ID: 166005 Cd Length: 250 Bit Score: 48.92 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 467 LVSVAWASASTFRGGDKRGGANGArLALMPQRDWDVNAAAVRALPVLEKIQKESGKASLADIIVLAGVVGVEKAASAagl 546
Cdd:PLN02364 36 MVRLAWHSAGTFDCQSRTGGPFGT-MRFDAEQAHGANSGIHIALRLLDPIREQFPTISFADFHQLAGVVAVEVTGGP--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 547 siHVPFAPGRVDARQdqtdiemfellePIADGfrnyraRLDVSTT--ESLLIDKAQQLTLTAPEMTALVGGMRVLGANFD 624
Cdd:PLN02364 112 --DIPFHPGREDKPQ------------PPPEG------RLPDATKgcDHLRDVFAKQMGLSDKDIVALSGAHTLGRCHKD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 625 GSK-NGVFTDRVGVLSNDFFvnlldmryewkatdesKELFEGrdRETGEVKYTASRADLvfgSNSVLRAVAEVYASSDah 703
Cdd:PLN02364 172 RSGfEGAWTSNPLIFDNSYF----------------KELLSG--EKEGLLQLVSDKALL---DDPVFRPLVEKYAADE-- 228
|
250
....*....|....*..
gi 1617235220 704 EKFVKDFVAAWVKVMNL 720
Cdd:PLN02364 229 DAFFADYAEAHMKLSEL 245
|
|
| PLN02879 |
PLN02879 |
L-ascorbate peroxidase |
467-720 |
8.24e-04 |
|
L-ascorbate peroxidase
Pssm-ID: 178467 [Multi-domain] Cd Length: 251 Bit Score: 41.97 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 467 LVSVAWASASTFRGGDKRGGANGArlALMPQR-DWDVNAAAVRALPVLEKIQKESGKASLADIIVLAGVVGVEKAASAag 545
Cdd:PLN02879 37 VLRLAWHSAGTFDVKTKTGGPFGT--IRHPQElAHDANNGLDIAVRLLDPIKELFPILSYADFYQLAGVVAVEITGGP-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 546 lsiHVPFAPGRVDArqdqtdiemfelLEPIADGfrnyraRLDVSTTE-SLLIDKAQQLTLTAPEMTALVGGMRVLGANFD 624
Cdd:PLN02879 113 ---EIPFHPGRLDK------------VEPPPEG------RLPQATKGvDHLRDVFGRMGLNDKDIVALSGGHTLGRCHKE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 625 GSK-NGVFTDRVGVLSNDFFvnlldmryewkatdesKELFEGrdRETGEVKYTASRADLvfgSNSVLRAVAEVYASSDah 703
Cdd:PLN02879 172 RSGfEGAWTPNPLIFDNSYF----------------KEILSG--EKEGLLQLPTDKALL---DDPLFLPFVEKYAADE-- 228
|
250
....*....|....*..
gi 1617235220 704 EKFVKDFVAAWVKVMNL 720
Cdd:PLN02879 229 DAFFEDYTEAHLKLSEL 245
|
|
| catalase_peroxidase_2 |
cd08200 |
C-terminal non-catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ... |
100-187 |
8.89e-04 |
|
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: 41.83 E-value: 8.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 100 FIRMAWHGAGTYRSIDGRGGAGRGQQRFAPLNSWPDN--VSLDKARRLLWPIKQKY------GQKISWADLFILAGNVAL 171
Cdd:cd08200 33 LVSTAWASASTFRNSDKRGGANGARIRLAPQKDWEVNepEELAKVLAVLEGIQKEFnesqsgGKKVSLADLIVLGGCAAV 112
|
90 100
....*....|....*....|.
gi 1617235220 172 E----NSGFR-TFGFGAGRED 187
Cdd:cd08200 113 EkaakDAGVDiKVPFTPGRTD 133
|
|
| PLN02608 |
PLN02608 |
L-ascorbate peroxidase |
470-559 |
2.39e-03 |
|
L-ascorbate peroxidase
Pssm-ID: 178218 [Multi-domain] Cd Length: 289 Bit Score: 40.52 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617235220 470 VAWASASTFRGGDKRGGANGArlaLMPQRDWD--VNAAAVRALPVLEKIQKESGKASLADIIVLAGVVGVEkaaSAAGLS 547
Cdd:PLN02608 37 LAWHDAGTYDAKTKTGGPNGS---IRNEEEYShgANNGLKIAIDLCEPVKAKHPKITYADLYQLAGVVAVE---VTGGPT 110
|
90
....*....|..
gi 1617235220 548 IHvpFAPGRVDA 559
Cdd:PLN02608 111 ID--FVPGRKDS 120
|
|
| plant_peroxidase_like_1 |
cd08201 |
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ... |
237-286 |
7.99e-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: 38.99 E-value: 7.99e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1617235220 237 EPLSAAAAIRATFGNMGMNDEETVALIAGGHTLGKTHGAGPTSNVGPDPE 286
Cdd:cd08201 139 EPQTDLGTTTESFRRQGFSTSEMIALVACGHTLGGVHSEDFPEIVPPGSV 188
|
|
| |
