|
Name |
Accession |
Description |
Interval |
E-value |
| KatE |
COG0753 |
Catalase [Inorganic ion transport and metabolism]; |
5-489 |
0e+00 |
|
Catalase [Inorganic ion transport and metabolism];
Pssm-ID: 440516 [Multi-domain] Cd Length: 489 Bit Score: 928.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 5 NSSKVLTTGFGIPVGDDQNSLTAGNRGPVLMQDVHLLDKLSHFDHERIPERVVHAKGAGAGGYFEVTADVTKYTKAKFLS 84
Cdd:COG0753 6 DEGKTLTTNQGAPVADNQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFEVTEDISKYTKAKFFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 85 EIGKRTEVFVRFSTVGGEKGSADSARDPRGFAVKFYTEDGNYDLVGNNTPVFFIRDPLKFPDFIHTQKRNPATNCKDPDM 164
Cdd:COG0753 86 EPGKKTPVFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHAQKRDPDTNLPQHDT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 165 FWDFLSLTPESIHQVTILFSDRGTPATYRNMNGYSSHTYKWYNEKGEYFWVQYHFKTDQGIKNLTLEEAEKIGGSDPDHA 244
Cdd:COG0753 166 FWDFWSLSPESLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAEGERFWVKFHWKPKQGIHSLTWDEAQKIAGKDPDFH 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 245 TRDLYEAIKKGDYPSWTLEMQIMTPEQAEDYRFDIRDITKVWPHGDFPTMKIGKLVLNRNPTNYFAEVEQAAFSPANLVP 324
Cdd:COG0753 246 RRDLYEAIERGDFPEWELGVQVMPEEDADKFDFDPLDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAETEQAAFSPGNLVP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 325 GIGISPDKMLQGRVFSYHDTHIHRLGPNYNLIPVNAPKySPENSYQRDGFMRVDANGGSgPNYWPNSFGGPSPDSVYLEP 404
Cdd:COG0753 326 GIDFSPDKMLQGRLFSYADTQRYRLGPNFHQLPVNRPK-CPVHNYQRDGAMRYDINGGR-VNYEPNSLGGPREDPGFKEP 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 405 PFGVSGLAARtlYTHP-NDDFVQAGNLYRdVMTDYDRENLVGNIVSHLSAAQ-KRIQLRQTALFFKADRDYGSRVAKGLE 482
Cdd:COG0753 404 PLKVDGDKVR--YRSEsDDHFSQAGLLYR-SMSDEEKQHLIDNIAFELGKVEsEEIRERMVAHFYNVDPELGARVAEALG 480
|
....*..
gi 9972755 483 LDIKEVE 489
Cdd:COG0753 481 LDLPEAK 487
|
|
| catalase_clade_3 |
cd08156 |
Clade 3 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
51-481 |
0e+00 |
|
Clade 3 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes, which is involved in the protection of cells from the toxic effects of peroxides. It catalyzes the conversion of hydrogen peroxide to water and molecular oxygen. Catalases also utilize hydrogen peroxide to oxidize various substrates such as alcohol or phenols. Clade 3 catalases are the most abundant subfamily and are found in all three kingdoms of life; they have a relatively small subunit size of 43 to 75 kDa, and bind a protoheme IX (heme b) group buried deep inside the structure. Clade 3 catalases also bind NADPH as a second redox-active cofactor. They form tetramers, and in eukaryotic cells, catalases are located in peroxisomes.
Pssm-ID: 163712 [Multi-domain] Cd Length: 429 Bit Score: 865.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 51 RIPERVVHAKGAGAGGYFEVTADVTKYTKAKFLSEIGKRTEVFVRFSTVGGEKGSADSARDPRGFAVKFYTEDGNYDLVG 130
Cdd:cd08156 1 RIPERVVHAKGAGAFGTFEVTHDITKYTKAKIFSEVGKKTPVFVRFSTVAGERGSADTERDPRGFALKFYTEEGNWDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 131 NNTPVFFIRDPLKFPDFIHTQKRNPATNCKDPDMFWDFLSLTPESIHQVTILFSDRGTPATYRNMNGYSSHTYKWYNEKG 210
Cdd:cd08156 81 NNTPVFFIRDPIKFPDFIHTQKRNPQTNLKDPDMFWDFWSLSPESLHQVTILFSDRGIPDGYRHMNGYGSHTFSLVNAKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 211 EYFWVQYHFKTDQGIKNLTLEEAEKIGGSDPDHATRDLYEAIKKGDYPSWTLEMQIMTPEQAEDYRFDIRDITKVWPHGD 290
Cdd:cd08156 161 ERFWVKFHFKTDQGIKNLTNEEAAELAGEDPDYAQRDLFEAIERGDFPSWTLYVQVMPEEDAEKYRFNPFDLTKVWPHKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 291 FPTMKIGKLVLNRNPTNYFAEVEQAAFSPANLVPGIGISPDKMLQGRVFSYHDTHIHRLGPNYNLIPVNAPKySPENSYQ 370
Cdd:cd08156 241 YPLIEVGKLELNRNPENYFAEVEQAAFSPSNLVPGIGFSPDKMLQGRLFSYADAHRYRLGVNYHQLPVNRPK-CPVNNYQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 371 RDGFMRVDANGGSGPNYWPNSFGGPSPDSVYLEPPFGVSGLAARTLYTHPNDDFVQAGNLYRDvMTDYDRENLVGNIVSH 450
Cdd:cd08156 320 RDGAMRVDGNGGGAPNYEPNSFGGPPEDPEYAEPPLPVSGDADRYNYRDDDDDYTQAGDLYRL-VSEDERERLVENIAGH 398
|
410 420 430
....*....|....*....|....*....|.
gi 9972755 451 LSAAQKRIQLRQTALFFKADRDYGSRVAKGL 481
Cdd:cd08156 399 LKGAPEFIQERQVAHFYKADPDYGERVAKAL 429
|
|
| Catalase |
pfam00199 |
Catalase; |
11-394 |
0e+00 |
|
Catalase;
Pssm-ID: 459708 Cd Length: 383 Bit Score: 843.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 11 TTGFGIPVGDDQNSLTAGNRGPVLMQDVHLLDKLSHFDHERIPERVVHAKGAGAGGYFEVTADVTKYTKAKFLSEIGKRT 90
Cdd:pfam00199 1 TTSNGAPVPDNQNSLTAGPRGPLLLQDFHLIEKLAHFDRERIPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSEVGKKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 91 EVFVRFSTVGGEKGSADSARDPRGFAVKFYTEDGNYDLVGNNTPVFFIRDPLKFPDFIHTQKRNPATNCKDPDMFWDFLS 170
Cdd:pfam00199 81 PVFVRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHSQKRDPQTNLPDPAMFWDFWS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 171 LTPESIHQVTILFSDRGTPATYRNMNGYSSHTYKWYNEKGEYFWVQYHFKTDQGIKNLTLEEAEKIGGSDPDHATRDLYE 250
Cdd:pfam00199 161 LNPESLHQVTWLFSDRGIPRSYRHMNGFGVHTFKLVNADGERVYVKFHFKTDQGIKNLTWEEAQKLAGKDPDYHTRDLYE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 251 AIKKGDYPSWTLEMQIMTPEQAEDYRFDIRDITKVWPHGDFPTMKIGKLVLNRNPTNYFAEVEQAAFSPANLVPGIGISP 330
Cdd:pfam00199 241 AIERGDYPSWTLYVQVMTEEDAEKFRFNPFDLTKVWPHKDYPLIEVGKMVLNRNPDNYFAEVEQAAFSPSNLVPGIEPSP 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9972755 331 DKMLQGRVFSYHDTHIHRLGPNYNLIPVNAPKYsPENSYQRDGFMRVDANGGSGPNYWPNSFGG 394
Cdd:pfam00199 321 DPMLQGRLFSYPDTQRYRLGPNYQQLPVNRPPC-PVHNYQRDGAMRFDINQGSRPNYEPNSFGG 383
|
|
| Catalase |
smart01060 |
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ... |
14-387 |
0e+00 |
|
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water and molecular oxygen, serving to protect cells from its toxic effects; Hydrogen peroxide is produced as a consequence of oxidative cellular metabolism and can be converted to the highly reactive hydroxyl radical via transition metals, this radical being able to damage a wide variety of molecules within a cell, leading to oxidative stress and cell death. Catalases act to neutralise hydrogen peroxide toxicity, and are produced by all aerobic organisms ranging from bacteria to man. Most catalases are mono-functional, haem-containing enzymes, although there are also bifunctional haem-containing peroxidase/catalases that are closely related to plant peroxidases, and non-haem, manganese-containing catalases that are found in bacteria.
Pssm-ID: 215003 Cd Length: 373 Bit Score: 782.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 14 FGIPVGDDQNSLTAGNRGPVLMQDVHLLDKLSHFDHERIPERVVHAKGAGAGGYFEVTADVTKYTKAKFLSEIGKRTEVF 93
Cdd:smart01060 1 QGAPVADNQNSLTAGPRGPVLLQDFHLIEKLAHFDRERIPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQKVGKKTPVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 94 VRFSTVGGEKGSADSARDPRGFAVKFYTEDGNYDLVGNNTPVFFIRDPLKFPDFIHTQKRNPATNCKDPDMFWDFLSLTP 173
Cdd:smart01060 81 VRFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHAQKRDPRTNLPDHDMFWDFWSLNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 174 ESIHQVTILFSDRGTPATYRNMNGYSSHTYKWYNEKGEYFWVQYHFKTDQGIKNLTLEEAEKIGGSDPDHATRDLYEAIK 253
Cdd:smart01060 161 ESLHQVTWLMSDRGIPASYRHMNGFGVHTFKLVNAEGERFYVKFHFKPDQGIKNLTWEEAAKLAGKDPDYHRRDLYEAIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 254 KGDYPSWTLEMQIMTPEQAEDYRFDIRDITKVWPHGDFPTMKIGKLVLNRNPTNYFAEVEQAAFSPANLVPGIGISPDKM 333
Cdd:smart01060 241 RGDYPEWTLYVQVMPEEDAEKFRFDPFDLTKVWPHKDYPLIEVGKMTLNRNPDNYFAEVEQAAFSPSNLVPGIEFSPDKM 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 9972755 334 LQGRVFSYHDTHIHRLGPNYNLIPVNAPKySPENSYQRDGFMRVDANGGSGPNY 387
Cdd:smart01060 321 LQGRLFSYPDTQRYRLGPNYHQLPVNRPR-CPVHNYQRDGAMRVDGNQGGDPNY 373
|
|
| PLN02609 |
PLN02609 |
catalase |
7-483 |
0e+00 |
|
catalase
Pssm-ID: 215328 [Multi-domain] Cd Length: 492 Bit Score: 638.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 7 SKVLTTGFGIPVGDDQNSLTAGNRGPVLMQDVHLLDKLSHFDHERIPERVVHAKGAGAGGYFEVTADVTKYTKAKFLSEI 86
Cdd:PLN02609 14 SPFFTTNSGAPVWNNNSSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDISNLTCADFLRAP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 87 GKRTEVFVRFSTVGGEKGSADSARDPRGFAVKFYTEDGNYDLVGNNTPVFFIRDPLKFPDFIHTQKRNPATNCKDPDMFW 166
Cdd:PLN02609 94 GVQTPVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDMVGNNFPVFFIRDGMKFPDMVHALKPNPKTHIQEPWRIL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 167 DFLSLTPESIHQVTILFSDRGTPATYRNMNGYSSHTYKWYNEKGEYFWVQYHFKTDQGIKNLTLEEAEKIGGSDPDHATR 246
Cdd:PLN02609 174 DFLSHHPESLHMFTFLFDDRGIPQDYRHMEGFGVHTYKLINKAGKAHYVKFHWKPTCGVKNLLDEEAVRVGGSNHSHATQ 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 247 DLYEAIKKGDYPSWTLEMQIMTPEQAEDYRFDIRDITKVWPHGDFPTMKIGKLVLNRNPTNYFAEVEQAAFSPANLVPGI 326
Cdd:PLN02609 254 DLYDSIAAGNYPEWKLFIQTMDPEDEDKFDFDPLDVTKTWPEDILPLQPVGRLVLNRNIDNFFAENEQLAFCPAIVVPGI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 327 GISPDKMLQGRVFSYHDTHIHRLGPNYNLIPVNAPKYSPENsYQRDGFMRVDANgGSGPNYWPNSFGG-PSPDSVYLEPP 405
Cdd:PLN02609 334 YYSDDKLLQTRIFAYADTQRHRLGPNYLQLPVNAPKCAHHN-NHHEGFMNFMHR-DEEVNYFPSRFDPvRHAERVPIPHP 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 406 FgVSGLAARTLYTHPNdDFVQAGNLYRDvMTDYDRENLVGNIVSHLSAAQKRIQLRQT--ALFFKADRDYGSRVAKGLEL 483
Cdd:PLN02609 412 P-LSGRREKCKIEKEN-NFKQPGERYRS-WSPDRQERFIKRWVDALSDPRVTHEIRSIwiSYWSQCDKSLGQKLASRLNV 488
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| KatE |
COG0753 |
Catalase [Inorganic ion transport and metabolism]; |
5-489 |
0e+00 |
|
Catalase [Inorganic ion transport and metabolism];
Pssm-ID: 440516 [Multi-domain] Cd Length: 489 Bit Score: 928.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 5 NSSKVLTTGFGIPVGDDQNSLTAGNRGPVLMQDVHLLDKLSHFDHERIPERVVHAKGAGAGGYFEVTADVTKYTKAKFLS 84
Cdd:COG0753 6 DEGKTLTTNQGAPVADNQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFEVTEDISKYTKAKFFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 85 EIGKRTEVFVRFSTVGGEKGSADSARDPRGFAVKFYTEDGNYDLVGNNTPVFFIRDPLKFPDFIHTQKRNPATNCKDPDM 164
Cdd:COG0753 86 EPGKKTPVFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHAQKRDPDTNLPQHDT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 165 FWDFLSLTPESIHQVTILFSDRGTPATYRNMNGYSSHTYKWYNEKGEYFWVQYHFKTDQGIKNLTLEEAEKIGGSDPDHA 244
Cdd:COG0753 166 FWDFWSLSPESLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAEGERFWVKFHWKPKQGIHSLTWDEAQKIAGKDPDFH 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 245 TRDLYEAIKKGDYPSWTLEMQIMTPEQAEDYRFDIRDITKVWPHGDFPTMKIGKLVLNRNPTNYFAEVEQAAFSPANLVP 324
Cdd:COG0753 246 RRDLYEAIERGDFPEWELGVQVMPEEDADKFDFDPLDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAETEQAAFSPGNLVP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 325 GIGISPDKMLQGRVFSYHDTHIHRLGPNYNLIPVNAPKySPENSYQRDGFMRVDANGGSgPNYWPNSFGGPSPDSVYLEP 404
Cdd:COG0753 326 GIDFSPDKMLQGRLFSYADTQRYRLGPNFHQLPVNRPK-CPVHNYQRDGAMRYDINGGR-VNYEPNSLGGPREDPGFKEP 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 405 PFGVSGLAARtlYTHP-NDDFVQAGNLYRdVMTDYDRENLVGNIVSHLSAAQ-KRIQLRQTALFFKADRDYGSRVAKGLE 482
Cdd:COG0753 404 PLKVDGDKVR--YRSEsDDHFSQAGLLYR-SMSDEEKQHLIDNIAFELGKVEsEEIRERMVAHFYNVDPELGARVAEALG 480
|
....*..
gi 9972755 483 LDIKEVE 489
Cdd:COG0753 481 LDLPEAK 487
|
|
| catalase_clade_3 |
cd08156 |
Clade 3 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
51-481 |
0e+00 |
|
Clade 3 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes, which is involved in the protection of cells from the toxic effects of peroxides. It catalyzes the conversion of hydrogen peroxide to water and molecular oxygen. Catalases also utilize hydrogen peroxide to oxidize various substrates such as alcohol or phenols. Clade 3 catalases are the most abundant subfamily and are found in all three kingdoms of life; they have a relatively small subunit size of 43 to 75 kDa, and bind a protoheme IX (heme b) group buried deep inside the structure. Clade 3 catalases also bind NADPH as a second redox-active cofactor. They form tetramers, and in eukaryotic cells, catalases are located in peroxisomes.
Pssm-ID: 163712 [Multi-domain] Cd Length: 429 Bit Score: 865.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 51 RIPERVVHAKGAGAGGYFEVTADVTKYTKAKFLSEIGKRTEVFVRFSTVGGEKGSADSARDPRGFAVKFYTEDGNYDLVG 130
Cdd:cd08156 1 RIPERVVHAKGAGAFGTFEVTHDITKYTKAKIFSEVGKKTPVFVRFSTVAGERGSADTERDPRGFALKFYTEEGNWDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 131 NNTPVFFIRDPLKFPDFIHTQKRNPATNCKDPDMFWDFLSLTPESIHQVTILFSDRGTPATYRNMNGYSSHTYKWYNEKG 210
Cdd:cd08156 81 NNTPVFFIRDPIKFPDFIHTQKRNPQTNLKDPDMFWDFWSLSPESLHQVTILFSDRGIPDGYRHMNGYGSHTFSLVNAKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 211 EYFWVQYHFKTDQGIKNLTLEEAEKIGGSDPDHATRDLYEAIKKGDYPSWTLEMQIMTPEQAEDYRFDIRDITKVWPHGD 290
Cdd:cd08156 161 ERFWVKFHFKTDQGIKNLTNEEAAELAGEDPDYAQRDLFEAIERGDFPSWTLYVQVMPEEDAEKYRFNPFDLTKVWPHKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 291 FPTMKIGKLVLNRNPTNYFAEVEQAAFSPANLVPGIGISPDKMLQGRVFSYHDTHIHRLGPNYNLIPVNAPKySPENSYQ 370
Cdd:cd08156 241 YPLIEVGKLELNRNPENYFAEVEQAAFSPSNLVPGIGFSPDKMLQGRLFSYADAHRYRLGVNYHQLPVNRPK-CPVNNYQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 371 RDGFMRVDANGGSGPNYWPNSFGGPSPDSVYLEPPFGVSGLAARTLYTHPNDDFVQAGNLYRDvMTDYDRENLVGNIVSH 450
Cdd:cd08156 320 RDGAMRVDGNGGGAPNYEPNSFGGPPEDPEYAEPPLPVSGDADRYNYRDDDDDYTQAGDLYRL-VSEDERERLVENIAGH 398
|
410 420 430
....*....|....*....|....*....|.
gi 9972755 451 LSAAQKRIQLRQTALFFKADRDYGSRVAKGL 481
Cdd:cd08156 399 LKGAPEFIQERQVAHFYKADPDYGERVAKAL 429
|
|
| Catalase |
pfam00199 |
Catalase; |
11-394 |
0e+00 |
|
Catalase;
Pssm-ID: 459708 Cd Length: 383 Bit Score: 843.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 11 TTGFGIPVGDDQNSLTAGNRGPVLMQDVHLLDKLSHFDHERIPERVVHAKGAGAGGYFEVTADVTKYTKAKFLSEIGKRT 90
Cdd:pfam00199 1 TTSNGAPVPDNQNSLTAGPRGPLLLQDFHLIEKLAHFDRERIPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSEVGKKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 91 EVFVRFSTVGGEKGSADSARDPRGFAVKFYTEDGNYDLVGNNTPVFFIRDPLKFPDFIHTQKRNPATNCKDPDMFWDFLS 170
Cdd:pfam00199 81 PVFVRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHSQKRDPQTNLPDPAMFWDFWS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 171 LTPESIHQVTILFSDRGTPATYRNMNGYSSHTYKWYNEKGEYFWVQYHFKTDQGIKNLTLEEAEKIGGSDPDHATRDLYE 250
Cdd:pfam00199 161 LNPESLHQVTWLFSDRGIPRSYRHMNGFGVHTFKLVNADGERVYVKFHFKTDQGIKNLTWEEAQKLAGKDPDYHTRDLYE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 251 AIKKGDYPSWTLEMQIMTPEQAEDYRFDIRDITKVWPHGDFPTMKIGKLVLNRNPTNYFAEVEQAAFSPANLVPGIGISP 330
Cdd:pfam00199 241 AIERGDYPSWTLYVQVMTEEDAEKFRFNPFDLTKVWPHKDYPLIEVGKMVLNRNPDNYFAEVEQAAFSPSNLVPGIEPSP 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9972755 331 DKMLQGRVFSYHDTHIHRLGPNYNLIPVNAPKYsPENSYQRDGFMRVDANGGSGPNYWPNSFGG 394
Cdd:pfam00199 321 DPMLQGRLFSYPDTQRYRLGPNYQQLPVNRPPC-PVHNYQRDGAMRFDINQGSRPNYEPNSFGG 383
|
|
| Catalase |
smart01060 |
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ... |
14-387 |
0e+00 |
|
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water and molecular oxygen, serving to protect cells from its toxic effects; Hydrogen peroxide is produced as a consequence of oxidative cellular metabolism and can be converted to the highly reactive hydroxyl radical via transition metals, this radical being able to damage a wide variety of molecules within a cell, leading to oxidative stress and cell death. Catalases act to neutralise hydrogen peroxide toxicity, and are produced by all aerobic organisms ranging from bacteria to man. Most catalases are mono-functional, haem-containing enzymes, although there are also bifunctional haem-containing peroxidase/catalases that are closely related to plant peroxidases, and non-haem, manganese-containing catalases that are found in bacteria.
Pssm-ID: 215003 Cd Length: 373 Bit Score: 782.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 14 FGIPVGDDQNSLTAGNRGPVLMQDVHLLDKLSHFDHERIPERVVHAKGAGAGGYFEVTADVTKYTKAKFLSEIGKRTEVF 93
Cdd:smart01060 1 QGAPVADNQNSLTAGPRGPVLLQDFHLIEKLAHFDRERIPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQKVGKKTPVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 94 VRFSTVGGEKGSADSARDPRGFAVKFYTEDGNYDLVGNNTPVFFIRDPLKFPDFIHTQKRNPATNCKDPDMFWDFLSLTP 173
Cdd:smart01060 81 VRFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHAQKRDPRTNLPDHDMFWDFWSLNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 174 ESIHQVTILFSDRGTPATYRNMNGYSSHTYKWYNEKGEYFWVQYHFKTDQGIKNLTLEEAEKIGGSDPDHATRDLYEAIK 253
Cdd:smart01060 161 ESLHQVTWLMSDRGIPASYRHMNGFGVHTFKLVNAEGERFYVKFHFKPDQGIKNLTWEEAAKLAGKDPDYHRRDLYEAIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 254 KGDYPSWTLEMQIMTPEQAEDYRFDIRDITKVWPHGDFPTMKIGKLVLNRNPTNYFAEVEQAAFSPANLVPGIGISPDKM 333
Cdd:smart01060 241 RGDYPEWTLYVQVMPEEDAEKFRFDPFDLTKVWPHKDYPLIEVGKMTLNRNPDNYFAEVEQAAFSPSNLVPGIEFSPDKM 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 9972755 334 LQGRVFSYHDTHIHRLGPNYNLIPVNAPKySPENSYQRDGFMRVDANGGSGPNY 387
Cdd:smart01060 321 LQGRLFSYPDTQRYRLGPNYHQLPVNRPR-CPVHNYQRDGAMRVDGNQGGDPNY 373
|
|
| catalase_fungal |
cd08157 |
Fungal catalases similar to yeast catalases A and T; Catalase is a ubiquitous enzyme found in ... |
35-482 |
0e+00 |
|
Fungal catalases similar to yeast catalases A and T; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes, which is involved in the protection of cells from the toxic effects of peroxides. It catalyzes the conversion of hydrogen peroxide to water and molecular oxygen. Catalases also utilize hydrogen peroxide to oxidize various substrates such as alcohol or phenols. This family of fungal catalases has a relatively small subunit size, and binds a protoheme IX (heme b) group buried deep inside the structure. Fungal catalases also bind NADPH as a second redox-active cofactor. They form tetramers; in eukaryotic cells, catalases are typically located in peroxisomes. Saccharomyces cerevisiae catalase T is found in the cytoplasm, though.
Pssm-ID: 163713 [Multi-domain] Cd Length: 451 Bit Score: 684.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 35 MQDVHLLDKLSHFDHERIPERVVHAKGAGAGGYFEVTADVTKYTKAKFLSEIGKRTEVFVRFSTVGGEKGSADSARDPRG 114
Cdd:cd08157 1 LQDFHLIDTLAHFDRERIPERVVHAKGAGAYGEFEVTDDISDITSADMLQGVGKKTPCLVRFSTVGGEKGSADTVRDPRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 115 FAVKFYTEDGNYDLVGNNTPVFFIRDPLKFPDFIHTQKRNPATNCKDPDMFWDFLSLTPESIHQVTILFSDRGTPATYRN 194
Cdd:cd08157 81 FAVKFYTEEGNWDWVFNNTPVFFIRDPIKFPHFIHSQKRDPQTNLKDSTMFWDYLSQNPESIHQVMILFSDRGTPASYRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 195 MNGYSSHTYKWYNEKGEYFWVQYHFKTDQGIKNLTLEEAEKIGGSDPDHATRDLYEAIKKGDYPSWTLEMQIMTPEQAED 274
Cdd:cd08157 161 MNGYSGHTYKWVNPDGSFKYVQFHLKSDQGPKFLTGEEAARLAGSNPDYATKDLFEAIERGDYPSWTVYVQVMTPEQAEK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 275 YRFDIRDITKVWPHGDFPTMKIGKLVLNRNPTNYFAEVEQAAFSPANLVPGIGISPDKMLQGRVFSYHDTHIHRLGPNYN 354
Cdd:cd08157 241 LRFNIFDLTKVWPHKDFPLRPVGKLTLNENPKNYFAEIEQAAFSPSHMVPGIEPSADPVLQARLFSYPDAHRHRLGPNYQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 355 LIPVNAPKYSPE-NSYQRDGFMRVDANGGSGPNY----WPNSFGGPSPDSVYLEPPFgvSGLAARTLYTHPNDDFVQAGN 429
Cdd:cd08157 321 QLPVNRPKTSPVyNPYQRDGPMSVNGNYGGDPNYvssiLPPTYFKKRVDADGHHENW--VGEVVAFLTEITDEDFVQPRA 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 9972755 430 LYRDVMTDYDRENLVGNIVSHLSAAQKRIQLRQTALFFKADRDYGSRVAKGLE 482
Cdd:cd08157 399 LWEVVGKPGQQERFVKNVAGHLSGAPPEIRKRVYEIFARVNPDLGKRIEKATE 451
|
|
| catalase_clade_1 |
cd08154 |
Clade 1 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
10-481 |
0e+00 |
|
Clade 1 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes, which is involved in the protection of cells from the toxic effects of peroxides. It catalyzes the conversion of hydrogen peroxide to water and molecular oxygen. Catalases also utilize hydrogen peroxide to oxidize various substrates such as alcohol or phenols. Clade 1 catalases are found in bacteria, algae, and plants; they have a relatively small subunit size of 55 to 69 kDa, and bind a protoheme IX (heme b) group buried deep inside the structure. They appear to form tetramers. In eukaryotic cells, catalases are located in peroxisomes.
Pssm-ID: 163710 [Multi-domain] Cd Length: 469 Bit Score: 684.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 10 LTTGFGIPVGDDQNSLTAGNRGPVLMQDVHLLDKLSHFDHERIPERVVHAKGAGAGGYFEVTADVTKYTKAKFLSEIGKR 89
Cdd:cd08154 2 LTTNQGAPVGDNQNSQTVGPRGPVLLEDYHLIEKLAHFDRERIPERVVHARGAGAHGYFEAYGDISDYTRASFLQEPGKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 90 TEVFVRFSTVGGEKGSADSARDPRGFAVKFYTEDGNYDLVGNNTPVFFIRDPLKFPDFIHTQKRNPATNCKDPDMFWDFL 169
Cdd:cd08154 82 TPVFVRFSTVIHGKGSPETLRDPRGFAVKFYTEEGNWDLVGNNLPVFFIRDAIKFPDMIHALKPSPVTNIQDPNRIFDFF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 170 SLTPESIHQVTILFSDRGTPATYRNMNGYSSHTYKWYNEKGEYFWVQYHFKTDQGIKNLTLEEAEKIGGSDPDHATRDLY 249
Cdd:cd08154 162 SHVPESTHMLTFLYSDWGTPASYRHMDGSGVHTYKWVNAEGKVVYVKYHWKPKQGVKNLTAEEAAEVQGKNFNHATQDLY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 250 EAIKKGDYPSWTLEMQIMTPEQAEDYRFDIRDITKVWPHGDFPTMKIGKLVLNRNPTNYFAEVEQAAFSPANLVPGIGIS 329
Cdd:cd08154 242 DAIAAGNYPEWELYVQIMDPKDLDKLDFDPLDDTKIWPEDQFPLKPVGKMTLNKNPDNFFAEVEQVAFSPGNLVPGIEPS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 330 PDKMLQGRVFSYHDTHIHRLGPNYNLIPVNAPKYSPENsYQRDGFMRVdANGGSGPNYWPNSFGGPSPDSVYLEPPFGVS 409
Cdd:cd08154 322 DDKMLQGRLFSYSDTQRYRLGPNYLQLPINAPKAAVHN-NQRDGQMNY-GHDTSDVNYEPSRLDGLPEAPKYPYSQPPLS 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9972755 410 GLAARTLYTHPNdDFVQAGNLYRDvMTDYDRENLVGNIVSHLSAAQKRIQLRQTALFFKADRDYGSRVAKGL 481
Cdd:cd08154 400 GTTQQAPIAKTN-NFKQAGERYRS-FSEEEQENLIKNLVVDLSDVNEEIKLRMLSYFSQADPDYGERVAEGL 469
|
|
| PLN02609 |
PLN02609 |
catalase |
7-483 |
0e+00 |
|
catalase
Pssm-ID: 215328 [Multi-domain] Cd Length: 492 Bit Score: 638.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 7 SKVLTTGFGIPVGDDQNSLTAGNRGPVLMQDVHLLDKLSHFDHERIPERVVHAKGAGAGGYFEVTADVTKYTKAKFLSEI 86
Cdd:PLN02609 14 SPFFTTNSGAPVWNNNSSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDISNLTCADFLRAP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 87 GKRTEVFVRFSTVGGEKGSADSARDPRGFAVKFYTEDGNYDLVGNNTPVFFIRDPLKFPDFIHTQKRNPATNCKDPDMFW 166
Cdd:PLN02609 94 GVQTPVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDMVGNNFPVFFIRDGMKFPDMVHALKPNPKTHIQEPWRIL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 167 DFLSLTPESIHQVTILFSDRGTPATYRNMNGYSSHTYKWYNEKGEYFWVQYHFKTDQGIKNLTLEEAEKIGGSDPDHATR 246
Cdd:PLN02609 174 DFLSHHPESLHMFTFLFDDRGIPQDYRHMEGFGVHTYKLINKAGKAHYVKFHWKPTCGVKNLLDEEAVRVGGSNHSHATQ 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 247 DLYEAIKKGDYPSWTLEMQIMTPEQAEDYRFDIRDITKVWPHGDFPTMKIGKLVLNRNPTNYFAEVEQAAFSPANLVPGI 326
Cdd:PLN02609 254 DLYDSIAAGNYPEWKLFIQTMDPEDEDKFDFDPLDVTKTWPEDILPLQPVGRLVLNRNIDNFFAENEQLAFCPAIVVPGI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 327 GISPDKMLQGRVFSYHDTHIHRLGPNYNLIPVNAPKYSPENsYQRDGFMRVDANgGSGPNYWPNSFGG-PSPDSVYLEPP 405
Cdd:PLN02609 334 YYSDDKLLQTRIFAYADTQRHRLGPNYLQLPVNAPKCAHHN-NHHEGFMNFMHR-DEEVNYFPSRFDPvRHAERVPIPHP 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 406 FgVSGLAARTLYTHPNdDFVQAGNLYRDvMTDYDRENLVGNIVSHLSAAQKRIQLRQT--ALFFKADRDYGSRVAKGLEL 483
Cdd:PLN02609 412 P-LSGRREKCKIEKEN-NFKQPGERYRS-WSPDRQERFIKRWVDALSDPRVTHEIRSIwiSYWSQCDKSLGQKLASRLNV 488
|
|
| catalase |
cd00328 |
Catalase heme-binding enzyme; Catalase is a ubiquitous enzyme found in both prokaryotes and ... |
51-481 |
0e+00 |
|
Catalase heme-binding enzyme; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes, which is involved in the protection of cells from the toxic effects of peroxides. It catalyzes the conversion of hydrogen peroxide to water and molecular oxygen. Catalases also utilize hydrogen peroxide to oxidize various substrates such as alcohol or phenols. Most catalases exist as tetramers of 65KD subunits containing a protoheme IX group buried deep inside the structure. In eukaryotic cells, catalases are located in peroxisomes.
Pssm-ID: 163705 [Multi-domain] Cd Length: 433 Bit Score: 582.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 51 RIPERVVHAKGAGAGGYFEVTADVTKYTKAKFLSEIGKRTEVFVRFSTVGGEKGSADSARDPRGFAVKFYTEDGNYDLVG 130
Cdd:cd00328 1 RIPERVVHARGAGAFGYFTAYGDWSDISAAAFFSAIGKKTPVFVRFSTVVGGAGSADTVRDPHGFATKFYTEEGNFDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 131 NNTPVFFIRDPLKFPDFIHTQKRNPATNCKDPDMFWDFLSLTPESIHQVTILFSDRGTPATYRNMNGYSSHTYKWYNEKG 210
Cdd:cd00328 81 NNTPIFFIRDAIKFPDFIHAQKPNPQTALPDADRFWDFLSLRPESLHQVSFLFSDRGIPAAYRHMNGYGSHTFKLVNANG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 211 EYFWVQYHFKTDQGIKNLTLEEAEKIGGSDPDHATRDLYEAIKKGDYPSWTLEMQIMTPEQAEDYRFDIRDITKVWPHGD 290
Cdd:cd00328 161 KVHYVKFHWKTDQGIANLVWEEAARLAGEDPDYHRQDLFEAIEAGDYPSWELYIQVMTFNDAEKFPFNPLDPTKVWPEEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 291 FPTMKIGKLVLNRNPTNYFAEVEQAAFSPANLVPGIGISPDKMLQGRVFSYHDTHIHRLGPNYNLIPVNAPkYSPENSYQ 370
Cdd:cd00328 241 VPLIVVGKLVLNRNPLNFFAEVEQAAFDPGHIVPGVEFSEDPLLQGRLFSYADTQLYRLGPNFQQLPVNRP-YAPVHNNQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 371 RDGFMRVDANGGsGPNYWPNSFGGPSPDSVYLEPPFG----VSGLAARTLYTHPNDDFVQAGNLYRdVMTDYDRENLVGN 446
Cdd:cd00328 320 RDGAGNMNDNTG-VPNYEPNAKDVRYPAQGAPKFDRGhfshWKSGVNREASTTNDDNFTQARLFYR-SLTPGQQKRLVDA 397
|
410 420 430
....*....|....*....|....*....|....*.
gi 9972755 447 IVSHLS-AAQKRIQLRQTALFFKADRDYGSRVAKGL 481
Cdd:cd00328 398 FRFELAdAVSPQIQQRVLDQFAKVDAAAAKRVAKAL 433
|
|
| katE |
PRK11249 |
hydroperoxidase II; Provisional |
10-484 |
1.93e-178 |
|
hydroperoxidase II; Provisional
Pssm-ID: 236886 [Multi-domain] Cd Length: 752 Bit Score: 519.60 E-value: 1.93e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 10 LTTGFGIPVGDDQNSLTAGNRGPVLMQDVHLLDKLSHFDHERIPERVVHAKGAGAGGYFEVTADVTKYTKAKFLSEIGKR 89
Cdd:PRK11249 77 LTTNQGVRIADDQNSLRAGSRGPSLLEDFILREKITHFDHERIPERIVHARGSAAHGYFQPYKSLSDITKAAFLQDPGKI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 90 TEVFVRFSTVGGEKGSADSARDPRGFAVKFYTEDGNYDLVGNNTPVFFIRDPLKFPDFIHTQKRNP----ATNCKDPDMF 165
Cdd:PRK11249 157 TPVFVRFSTVQGPRGSADTVRDIRGFATKFYTEEGNFDLVGNNTPVFFIQDAIKFPDFVHAVKPEPhneiPQGQSAHDTF 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 166 WDFLSLTPESIHQVTILFSDRGTPATYRNMNGYSSHTYKWYNEKGEYFWVQYHFKTDQGIKNLTLEEAEKIGGSDPDHAT 245
Cdd:PRK11249 237 WDYVSLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLINAEGKATFVRFHWKPVAGKASLVWDEAQKLTGRDPDFHR 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 246 RDLYEAIKKGDYPSWTLEMQIMTPEQAEDYRFDIRDITKVWPHGDFPTMKIGKLVLNRNPTNYFAEVEQAAFSPANLVPG 325
Cdd:PRK11249 317 RDLWEAIEAGDYPEYELGVQLIPEEDEFKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFHPGHIVPG 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 326 IGISPDKMLQGRVFSYHDTHIHRL-GPNYNLIPVNAPkYSPENSYQRDGFMRVDANGGSGpNYWPNSFGG-------PSP 397
Cdd:PRK11249 397 IDFTNDPLLQGRLFSYTDTQISRLgGPNFHEIPINRP-TCPYHNFQRDGMHRMTIDTGPA-NYEPNSINGnwpretpPAP 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 398 D----SVYLEPpfgVSGLAARTLYTHPNDDFVQAgNLYRDVMTDYDRENLVGNIVSHLSAAQKR-IQLRQTALFFKADRD 472
Cdd:PRK11249 475 KrggfESYQER---VEGNKVRERSPSFGDYYSQP-RLFWLSQTPIEQRHIIDAFSFELGKVVRPyIRERVVDQLAHIDLT 550
|
490
....*....|..
gi 9972755 473 YGSRVAKGLELD 484
Cdd:PRK11249 551 LAQAVAENLGIP 562
|
|
| catalase_clade_2 |
cd08155 |
Clade 2 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
48-481 |
5.19e-174 |
|
Clade 2 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes, which is involved in the protection of cells from the toxic effects of peroxides. It catalyzes the conversion of hydrogen peroxide to water and molecular oxygen. Catalases also utilize hydrogen peroxide to oxidize various substrates such as alcohol or phenols. Clade 2 catalases are mostly found in bacteria and fungi; they have a large subunit size of 75 to 84 kDa, and bind a heme d group buried deep inside the structure. They appear to form tetramers. In eukaryotic cells, catalases are located in peroxisomes.
Pssm-ID: 163711 Cd Length: 443 Bit Score: 497.28 E-value: 5.19e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 48 DHERIPERVVHAKGAGAGGYFEVTADVTKYTKAKFLSEIGKRTEVFVRFSTVGGEKGSADSARDPRGFAVKFYTEDGNYD 127
Cdd:cd08155 1 DHERIPERVVHARGSGAHGYFQVYESLSQYTKAKFLQDPGKKTPVFVRFSTVAGSRGSADTVRDVRGFAVKFYTEEGNYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 128 LVGNNTPVFFIRDPLKFPDFIHTQKRNP----ATNCKDPDMFWDFLSLTPESIHQVTILFSDRGTPATYRNMNGYSSHTY 203
Cdd:cd08155 81 LVGNNIPVFFIQDAIKFPDLIHAVKPEPhnemPQAQSAHDTFWDFVSLQPESAHMVMWAMSDRAIPRSYRMMEGFGVHTF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 204 KWYNEKGEYFWVQYHFKTDQGIKNLTLEEAEKIGGSDPDHATRDLYEAIKKGDYPSWTLEMQIMTPEQAEDYRFDIRDIT 283
Cdd:cd08155 161 RLVNAQGKSTFVKFHWKPVLGVHSLVWDEAQKIAGKDPDFHRRDLWEAIESGDYPEWELGVQLIDEEDEFKFDFDILDPT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 284 KVWPHGDFPTMKIGKLVLNRNPTNYFAEVEQAAFSPANLVPGIGISPDKMLQGRVFSYHDTHIHRLG-PNYNLIPVNAPK 362
Cdd:cd08155 241 KLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFCPANVVPGIDFSNDPLLQGRLFSYLDTQLSRLGgPNFHELPINRPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 363 ySPENSYQRDGFMRVDANGGsGPNYWPNSFGGPSPDSV------YLEPPFGVSGLAARTLYTHPNDDFVQAgNLYRDVMT 436
Cdd:cd08155 321 -CPVHNNQRDGHMRMTINKG-RVNYFPNSLGAGPPRAAspaeggFVHYPEKVEGPKIRIRSESFADHYSQA-RLFWNSMS 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 9972755 437 DYDRENLVGNIVSHLSAAQ-KRIQLRQTALFFKADRDYGSRVAKGL 481
Cdd:cd08155 398 PVEKEHIISAFTFELSKVEtPEIRERVVDHLANIDEDLAKKVAKGL 443
|
|
| catalase_like |
cd08150 |
Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found ... |
53-349 |
2.67e-68 |
|
Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes involved in the protection of cells from the toxic effects of peroxides. It catalyses the conversion of hydrogen peroxide to water and molecular oxygen. Several other related protein families share the catalase fold and bind to heme, but do not necessarily have catalase activity.
Pssm-ID: 163706 Cd Length: 283 Bit Score: 220.51 E-value: 2.67e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 53 PERVVHAKGAGAGGYFEVTADVTKYTKAKFLSEiGKRTEVFVRFSTVggeKGSADSARDPRGFAVKFYTEDGN--YDLVG 130
Cdd:cd08150 1 GLRGQHFQGTCAFGTFEVLADLKERLRVGLFAE-GKVYPAYIRFSNG---AGIDDTKPDIRGFAIKFTGVADAgtLDFVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 131 NNTPVFFIRDPLKFPDFIHTQKRnPATNCKDPDMFWDFLSLTPESIHQVtiLFSDRGTPATYRNMNGYSSHTYKWYNEKG 210
Cdd:cd08150 77 NNTPVFFIRNTSDYEDFVAEFAR-SARGEPPLDFIAWYVEKRPEDLPNL--LGARSQVPDSYAAARYFSQVTFAFINGAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 211 EYFWVQYHFKTDQGIKNLTLEEAEkigGSDPDHATRDLYEAIKKGdYPSWTLEMQIMTPEQAedyrFDIRDITKVWPHgD 290
Cdd:cd08150 154 KYRVVRSKDNPVDGIPSLEDHELE---ARPPDYLREELTERLQRG-PVVYDFRIQLNDDTDA----TTIDNPTILWPT-E 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9972755 291 FPTMKIGKLVLNRNPTNyfAEVEQAAFSPANLVPGIGISPDK--MLQGRVFSYHDTHIHRL 349
Cdd:cd08150 225 HPVEAVAKITIPPPTFT--AAQEAFAFNPFTPWHGLLETNDLgpILEVRRRVYTSSQGLRH 283
|
|
| srpA_like |
cd08153 |
Catalase-like heme-binding proteins similar to the uncharacterized srpA; Catalase is a ... |
55-349 |
1.19e-42 |
|
Catalase-like heme-binding proteins similar to the uncharacterized srpA; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes involved in the protection of cells from the toxic effects of peroxides. It catalyses the conversion of hydrogen peroxide to water and molecular oxygen. Several other related protein families share the catalase fold and bind to heme, but do not necessarily have catalase activity. This family contains uncharacterized proteins similar to the Synechococcus elongatus PCC 7942 periplasmic protein srpA, of mostly bacterial origin. The plasmid-encoded srpA is regulated by sulfate, but does not seem to function in its uptake or metabolism.
Pssm-ID: 163709 Cd Length: 295 Bit Score: 153.54 E-value: 1.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 55 RVVHAKGAGAGGYFEVTADVTKYTKAKFLSeiGKRTEVFVRFSTVGGEKGSADSARDPRGFAVKFYTEDGN-YDLVGNNT 133
Cdd:cd08153 15 RRNHAKGICVSGTFTPSGAAASLSRAPLFS--GGSVPVTGRFSLGGGNPKAPDDAANPRGMALKFRLPDGEqWRMVMNSF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 134 PVFFIRDPLKFPDFIhtQKRNP-ATNCKDPDMFWDFLSLTPESIHQVTILFSdRGTPATYRNMNGYSSHTYKWYNEKGEY 212
Cdd:cd08153 93 PVFPVRTPEEFLALL--KAIAPdATGKPDPAKLKAFLAAHPEAAAFLAWIKT-APPPASFANTTYYGVNAFYFTNANGKR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 213 FWVQYHFKTDQGIKNLTLEEAEKIggsDPDHATRDLYEAIKKGdyP-SWTLEMQIMTPEQAEDyrfdirDITKVWPhGDF 291
Cdd:cd08153 170 QPVRWRFVPEDGVKYLSDEEAAKL---GPDFLFDELAQRLAQG--PvRWDLVLQLAEPGDPTD------DPTKPWP-ADR 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 9972755 292 PTMKIGKLVLNRNPTNYFAEVEQAAFSPANLVPGIGISPDKMLQGRVFSYHDTHIHRL 349
Cdd:cd08153 238 KEVDAGTLTITKVAPDQGGACRDINFDPLVLPDGIEPSDDPLLAARSAAYAVSFSRRQ 295
|
|
| Catalase-rel |
pfam06628 |
Catalase-related immune-responsive; This family represents a small conserved region within ... |
419-481 |
1.06e-19 |
|
Catalase-related immune-responsive; This family represents a small conserved region within catalase enzymes (EC:1.11.1.6). All members also contain the Catalase family, pfam00199 domain. Catalase decomposes hydrogen peroxide into water and oxygen, serving to protect cells from its toxic effects. This domain carries the immune-responsive amphipathic octa-peptide that is recognized by T cells.
Pssm-ID: 461967 [Multi-domain] Cd Length: 65 Bit Score: 82.80 E-value: 1.06e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9972755 419 HPNDDFVQAGNLYRdVMTDYDRENLVGNIVSHLSAAQ-KRIQLRQTALFFKADRDYGSRVAKGL 481
Cdd:pfam06628 3 DFDDHFSQAGLFYR-SMSEEERQRLVDNIAFELSKVTdPEIQERMVAHFYKVDPDLGQRVAEAL 65
|
|
| AOS |
cd08151 |
Allene oxide synthase; Allene oxide synthase converts a fatty acid hydroperoxide to an allene ... |
55-330 |
2.28e-11 |
|
Allene oxide synthase; Allene oxide synthase converts a fatty acid hydroperoxide to an allene oxide, which is an unstable epoxide. In corals, the enzyme is part of a eiconaosid synthesis pathway that is initiated by a lipoxygenase, which generates the fatty acid hydroperoxides in the first step. The structure of allene oxide synthase closely resembles that of catalase, but allene oxide synthase does not have catalase activity.
Pssm-ID: 163707 Cd Length: 328 Bit Score: 65.14 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 55 RVVHAKGAGAGGYFEVTADVtKYTKAKFLSEiGKRTEVFVRFSTVggeKGSADSAR-DPRGFAVKFYT----EDGNYDLV 129
Cdd:cd08151 28 RGTHTIGVGAKGVLTVLAES-DFPEHAFFTA-GKRFPVILRHANI---VGGDDDASlDGRGAALRFLNagddDAGPLDLV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 130 GNNTPVFFIRDPLKFPDFIhtqkrnpatNCKDP-----DMFWDFLSLTPesihqvtILFSDRGTPATYRNMNGYSSHTYK 204
Cdd:cd08151 103 MNTGESFGFWTAASFADFA---------GAGLPfrekaAKLRGPLARYA-------VWASLRRAPDSYTDLHYYSQICYE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 205 WYNEKGEYFWVQYHF-KTDQGIKNLTLEEAEKIGGSDPDHATRDLYEAIKKGDY-----------PSWTLEMQIMTPEQA 272
Cdd:cd08151 167 FVALDGKSRYARFRLlPPDADTEWDLGEDVLETIFQRPRLYLPRLPGDTRPKDYlrnefrqrlqsPGVRYRLQIQLREVS 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 9972755 273 EDYRFDIRDITKVWPHGDFPTMKIGKLVLNRNPTNyfAEVEQAAFSPANLVPGIGISP 330
Cdd:cd08151 247 DDATAVALDCCRPWDEDEHPWLDLAVVRLGAPLPN--DELEKLAFNPGNTPESLGLPL 302
|
|
| y4iL_like |
cd08152 |
Catalase-like heme-binding proteins similar to the uncharacterized y4iL; Catalase is a ... |
55-317 |
9.60e-10 |
|
Catalase-like heme-binding proteins similar to the uncharacterized y4iL; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes involved in the protection of cells from the toxic effects of peroxides. It catalyses the conversion of hydrogen peroxide to water and molecular oxygen. Several other related protein families share the catalase fold and bind to heme, but do not necessarily have catalase activity. This family contains uncharacterized proteins similar to Rhizobium sp. NGR234 y4iL, of mostly bacterial origin.
Pssm-ID: 163708 Cd Length: 305 Bit Score: 59.97 E-value: 9.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 55 RVVHAKGAGA-GGYFEVTADVTKYTKAKFLSEiGKRTEVFVRFSTVGGEkGSADSARDPRGFAVKFY----------TED 123
Cdd:cd08152 5 RDAHAKSHGClKAEFTVLDDLPPELAQGLFAE-PGTYPAVIRFSNAPGD-ILDDSVPDPRGMAIKVLgvpgekllpeEDA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 124 GNYDLVGNNTPVFFIRDPlkfPDFIHTQKRNPATNCKdPDMFWDFLSLTpeSIHQVTILFSDRGTPAT-------YRNMN 196
Cdd:cd08152 83 TTQDFVLVNHPVFFARDA---KDYLALLKLLARTTSL-PDGAKAALSAP--LRGALRVLEAAGGESPTlklgghpPAHPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9972755 197 GYSSHT---YKWynekGEYFwVQYHFKTDQGiKNLTLEEAEKIGGSDPDHATRDLYEAIKKGDYpSWTLEMQIMTPEQae 273
Cdd:cd08152 157 GETYWSqapYRF----GDYV-AKYSVVPASP-ALPALTGKELDLTDDPDALREALADFLAENDA-EFEFRIQLCTDLE-- 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 9972755 274 dyRFDIRDITKVWPHGDFPTMKIGKLVLNRNPTNyfAEVEQAAF 317
Cdd:cd08152 228 --KMPIEDASVEWPEALSPFVPVATITIPPQDFD--SPARQRAF 267
|
|
| |
