|
Name |
Accession |
Description |
Interval |
E-value |
| KatE |
COG0753 |
Catalase [Inorganic ion transport and metabolism]; |
2-481 |
0e+00 |
|
Catalase [Inorganic ion transport and metabolism];
Pssm-ID: 440516 [Multi-domain] Cd Length: 489 Bit Score: 881.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 2 SDDVRKPTTTDAGIPVASDEHSLTVGPDGPIVLHDHYLIEQMANFNRERIPERQPHAKGSGAFGHFEVTEDVSQFTKAAL 81
Cdd:COG0753 4 ADDEGKTLTTNQGAPVADNQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFEVTEDISKYTKAKF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 82 FQ-PGVKTDVVMRFSTVAGERGSPDTWRDPRGFSIKFYTSEGNYDMVGNNTPVFFIRDPMKFQHFIRSQKRRADNNLRDN 160
Cdd:COG0753 84 FQePGKKTPVFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHAQKRDPDTNLPQH 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 161 DMQWDFWTLSPESAHQVTWLMGDRGIPKSWRHMNGYSSHTYMWVNAQGEKFWVKYHFKTDQGIEFLAQEDADTLAGQDGD 240
Cdd:COG0753 164 DTFWDFWSLSPESLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAEGERFWVKFHWKPKQGIHSLTWDEAQKIAGKDPD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 241 YHTRDLFEAIKAGNSPSWTLHMQIMPFADAETYRYNPFDLTKVWPHGDYPLIKVGKLVLDHNPTDNFAQIEQVAFEPNNL 320
Cdd:COG0753 244 FHRRDLYEAIERGDFPEWELGVQVMPEEDADKFDFDPLDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAETEQAAFSPGNL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 321 VPGIGLSPDKMLMGRIFAYADAHRARLGVNYKQIPVNAPKSPVNSYSKDGAMRID-LASDPVYAPNSKGGPAADGERypT 399
Cdd:COG0753 324 VPGIDFSPDKMLQGRLFSYADTQRYRLGPNFHQLPVNRPKCPVHNYQRDGAMRYDiNGGRVNYEPNSLGGPREDPGF--K 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 400 DSTWGSQGNLVRSAYtlrADDDDYSQANDLVNkVMDDAARDRLVNNVTGHLLKGVEEPVLSRAFEYWRNIDRATGDRIAA 479
Cdd:COG0753 402 EPPLKVDGDKVRYRS---ESDDHFSQAGLLYR-SMSDEEKQHLIDNIAFELGKVESEEIRERMVAHFYNVDPELGARVAE 477
|
..
gi 490273731 480 RV 481
Cdd:COG0753 478 AL 479
|
|
| catalase_clade_3 |
cd08156 |
Clade 3 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
50-481 |
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: 777.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 50 RIPERQPHAKGSGAFGHFEVTEDVSQFTKAALFQP-GVKTDVVMRFSTVAGERGSPDTWRDPRGFSIKFYTSEGNYDMVG 128
Cdd:cd08156 1 RIPERVVHAKGAGAFGTFEVTHDITKYTKAKIFSEvGKKTPVFVRFSTVAGERGSADTERDPRGFALKFYTEEGNWDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 129 NNTPVFFIRDPMKFQHFIRSQKRRADNNLRDNDMQWDFWTLSPESAHQVTWLMGDRGIPKSWRHMNGYSSHTYMWVNAQG 208
Cdd:cd08156 81 NNTPVFFIRDPIKFPDFIHTQKRNPQTNLKDPDMFWDFWSLSPESLHQVTILFSDRGIPDGYRHMNGYGSHTFSLVNAKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 209 EKFWVKYHFKTDQGIEFLAQEDADTLAGQDGDYHTRDLFEAIKAGNSPSWTLHMQIMPFADAETYRYNPFDLTKVWPHGD 288
Cdd:cd08156 161 ERFWVKFHFKTDQGIKNLTNEEAAELAGEDPDYAQRDLFEAIERGDFPSWTLYVQVMPEEDAEKYRFNPFDLTKVWPHKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 289 YPLIKVGKLVLDHNPTDNFAQIEQVAFEPNNLVPGIGLSPDKMLMGRIFAYADAHRARLGVNYKQIPVNAPKSPVNSYSK 368
Cdd:cd08156 241 YPLIEVGKLELNRNPENYFAEVEQAAFSPSNLVPGIGFSPDKMLQGRLFSYADAHRYRLGVNYHQLPVNRPKCPVNNYQR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 369 DGAMRIDLA--SDPVYAPNSKGGPAADgeRYPTDSTWGSQGNLVRSAYtlRADDDDYSQANDLVNKvMDDAARDRLVNNV 446
Cdd:cd08156 321 DGAMRVDGNggGAPNYEPNSFGGPPED--PEYAEPPLPVSGDADRYNY--RDDDDDYTQAGDLYRL-VSEDERERLVENI 395
|
410 420 430
....*....|....*....|....*....|....*
gi 490273731 447 TGHlLKGVEEPVLSRAFEYWRNIDRATGDRIAARV 481
Cdd:cd08156 396 AGH-LKGAPEFIQERQVAHFYKADPDYGERVAKAL 429
|
|
| Catalase |
pfam00199 |
Catalase; |
10-389 |
0e+00 |
|
Catalase;
Pssm-ID: 459708 Cd Length: 383 Bit Score: 765.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 10 TTDAGIPVASDEHSLTVGPDGPIVLHDHYLIEQMANFNRERIPERQPHAKGSGAFGHFEVTEDVSQFTKAALFQ-PGVKT 88
Cdd:pfam00199 1 TTSNGAPVPDNQNSLTAGPRGPLLLQDFHLIEKLAHFDRERIPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSeVGKKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 89 DVVMRFSTVAGERGSPDTWRDPRGFSIKFYTSEGNYDMVGNNTPVFFIRDPMKFQHFIRSQKRRADNNLRDNDMQWDFWT 168
Cdd:pfam00199 81 PVFVRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHSQKRDPQTNLPDPAMFWDFWS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 169 LSPESAHQVTWLMGDRGIPKSWRHMNGYSSHTYMWVNAQGEKFWVKYHFKTDQGIEFLAQEDADTLAGQDGDYHTRDLFE 248
Cdd:pfam00199 161 LNPESLHQVTWLFSDRGIPRSYRHMNGFGVHTFKLVNADGERVYVKFHFKTDQGIKNLTWEEAQKLAGKDPDYHTRDLYE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 249 AIKAGNSPSWTLHMQIMPFADAETYRYNPFDLTKVWPHGDYPLIKVGKLVLDHNPTDNFAQIEQVAFEPNNLVPGIGLSP 328
Cdd:pfam00199 241 AIERGDYPSWTLYVQVMTEEDAEKFRFNPFDLTKVWPHKDYPLIEVGKMVLNRNPDNYFAEVEQAAFSPSNLVPGIEPSP 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490273731 329 DKMLMGRIFAYADAHRARLGVNYKQIPVNAPKSPVNSYSKDGAMR--IDLASDPVYAPNSKGG 389
Cdd:pfam00199 321 DPMLQGRLFSYPDTQRYRLGPNYQQLPVNRPPCPVHNYQRDGAMRfdINQGSRPNYEPNSFGG 383
|
|
| Catalase |
smart01060 |
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ... |
13-382 |
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: 732.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 13 AGIPVASDEHSLTVGPDGPIVLHDHYLIEQMANFNRERIPERQPHAKGSGAFGHFEVTEDVSQFTKAALFQ-PGVKTDVV 91
Cdd:smart01060 1 QGAPVADNQNSLTAGPRGPVLLQDFHLIEKLAHFDRERIPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQkVGKKTPVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 92 MRFSTVAGERGSPDTWRDPRGFSIKFYTSEGNYDMVGNNTPVFFIRDPMKFQHFIRSQKRRADNNLRDNDMQWDFWTLSP 171
Cdd:smart01060 81 VRFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHAQKRDPRTNLPDHDMFWDFWSLNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 172 ESAHQVTWLMGDRGIPKSWRHMNGYSSHTYMWVNAQGEKFWVKYHFKTDQGIEFLAQEDADTLAGQDGDYHTRDLFEAIK 251
Cdd:smart01060 161 ESLHQVTWLMSDRGIPASYRHMNGFGVHTFKLVNAEGERFYVKFHFKPDQGIKNLTWEEAAKLAGKDPDYHRRDLYEAIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 252 AGNSPSWTLHMQIMPFADAETYRYNPFDLTKVWPHGDYPLIKVGKLVLDHNPTDNFAQIEQVAFEPNNLVPGIGLSPDKM 331
Cdd:smart01060 241 RGDYPEWTLYVQVMPEEDAEKFRFDPFDLTKVWPHKDYPLIEVGKMTLNRNPDNYFAEVEQAAFSPSNLVPGIEFSPDKM 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 490273731 332 LMGRIFAYADAHRARLGVNYKQIPVNAPKSPVNSYSKDGAMRID--LASDPVY 382
Cdd:smart01060 321 LQGRLFSYPDTQRYRLGPNYHQLPVNRPRCPVHNYQRDGAMRVDgnQGGDPNY 373
|
|
| PLN02609 |
PLN02609 |
catalase |
2-487 |
0e+00 |
|
catalase
Pssm-ID: 215328 [Multi-domain] Cd Length: 492 Bit Score: 544.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 2 SDDVRKPTTTDAGIPVASDEHSLTVGPDGPIVLHDHYLIEQMANFNRERIPERQPHAKGSGAFGHFEVTEDVSQFTKAAL 81
Cdd:PLN02609 10 SAYNSPFFTTNSGAPVWNNNSSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDISNLTCADF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 82 FQ-PGVKTDVVMRFSTVAGERGSPDTWRDPRGFSIKFYTSEGNYDMVGNNTPVFFIRDPMKFQHFIRSQKRRADNNLRDN 160
Cdd:PLN02609 90 LRaPGVQTPVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDMVGNNFPVFFIRDGMKFPDMVHALKPNPKTHIQEP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 161 DMQWDFWTLSPESAHQVTWLMGDRGIPKSWRHMNGYSSHTYMWVNAQGEKFWVKYHFKTDQGIEFLAQEDADTLAGQDGD 240
Cdd:PLN02609 170 WRILDFLSHHPESLHMFTFLFDDRGIPQDYRHMEGFGVHTYKLINKAGKAHYVKFHWKPTCGVKNLLDEEAVRVGGSNHS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 241 YHTRDLFEAIKAGNSPSWTLHMQIMPFADAETYRYNPFDLTKVWPHGDYPLIKVGKLVLDHNPTDNFAQIEQVAFEPNNL 320
Cdd:PLN02609 250 HATQDLYDSIAAGNYPEWKLFIQTMDPEDEDKFDFDPLDVTKTWPEDILPLQPVGRLVLNRNIDNFFAENEQLAFCPAIV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 321 VPGIGLSPDKMLMGRIFAYADAHRARLGVNYKQIPVNAPKSPVNSYSKDGAMRI-DLASDPVYAPNSKgGPAADGERYPT 399
Cdd:PLN02609 330 VPGIYYSDDKLLQTRIFAYADTQRHRLGPNYLQLPVNAPKCAHHNNHHEGFMNFmHRDEEVNYFPSRF-DPVRHAERVPI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 400 DSTWGSQgnlvRSAYTLRADDDDYSQANDLVnKVMDDAARDRLVNNVTGHLLKGVEEPVL-SRAFEYWRNIDRATGDRIA 478
Cdd:PLN02609 409 PHPPLSG----RREKCKIEKENNFKQPGERY-RSWSPDRQERFIKRWVDALSDPRVTHEIrSIWISYWSQCDKSLGQKLA 483
|
....*....
gi 490273731 479 ARvLQERAK 487
Cdd:PLN02609 484 SR-LNVKPS 491
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| KatE |
COG0753 |
Catalase [Inorganic ion transport and metabolism]; |
2-481 |
0e+00 |
|
Catalase [Inorganic ion transport and metabolism];
Pssm-ID: 440516 [Multi-domain] Cd Length: 489 Bit Score: 881.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 2 SDDVRKPTTTDAGIPVASDEHSLTVGPDGPIVLHDHYLIEQMANFNRERIPERQPHAKGSGAFGHFEVTEDVSQFTKAAL 81
Cdd:COG0753 4 ADDEGKTLTTNQGAPVADNQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFEVTEDISKYTKAKF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 82 FQ-PGVKTDVVMRFSTVAGERGSPDTWRDPRGFSIKFYTSEGNYDMVGNNTPVFFIRDPMKFQHFIRSQKRRADNNLRDN 160
Cdd:COG0753 84 FQePGKKTPVFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHAQKRDPDTNLPQH 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 161 DMQWDFWTLSPESAHQVTWLMGDRGIPKSWRHMNGYSSHTYMWVNAQGEKFWVKYHFKTDQGIEFLAQEDADTLAGQDGD 240
Cdd:COG0753 164 DTFWDFWSLSPESLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAEGERFWVKFHWKPKQGIHSLTWDEAQKIAGKDPD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 241 YHTRDLFEAIKAGNSPSWTLHMQIMPFADAETYRYNPFDLTKVWPHGDYPLIKVGKLVLDHNPTDNFAQIEQVAFEPNNL 320
Cdd:COG0753 244 FHRRDLYEAIERGDFPEWELGVQVMPEEDADKFDFDPLDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAETEQAAFSPGNL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 321 VPGIGLSPDKMLMGRIFAYADAHRARLGVNYKQIPVNAPKSPVNSYSKDGAMRID-LASDPVYAPNSKGGPAADGERypT 399
Cdd:COG0753 324 VPGIDFSPDKMLQGRLFSYADTQRYRLGPNFHQLPVNRPKCPVHNYQRDGAMRYDiNGGRVNYEPNSLGGPREDPGF--K 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 400 DSTWGSQGNLVRSAYtlrADDDDYSQANDLVNkVMDDAARDRLVNNVTGHLLKGVEEPVLSRAFEYWRNIDRATGDRIAA 479
Cdd:COG0753 402 EPPLKVDGDKVRYRS---ESDDHFSQAGLLYR-SMSDEEKQHLIDNIAFELGKVESEEIRERMVAHFYNVDPELGARVAE 477
|
..
gi 490273731 480 RV 481
Cdd:COG0753 478 AL 479
|
|
| catalase_clade_3 |
cd08156 |
Clade 3 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
50-481 |
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: 777.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 50 RIPERQPHAKGSGAFGHFEVTEDVSQFTKAALFQP-GVKTDVVMRFSTVAGERGSPDTWRDPRGFSIKFYTSEGNYDMVG 128
Cdd:cd08156 1 RIPERVVHAKGAGAFGTFEVTHDITKYTKAKIFSEvGKKTPVFVRFSTVAGERGSADTERDPRGFALKFYTEEGNWDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 129 NNTPVFFIRDPMKFQHFIRSQKRRADNNLRDNDMQWDFWTLSPESAHQVTWLMGDRGIPKSWRHMNGYSSHTYMWVNAQG 208
Cdd:cd08156 81 NNTPVFFIRDPIKFPDFIHTQKRNPQTNLKDPDMFWDFWSLSPESLHQVTILFSDRGIPDGYRHMNGYGSHTFSLVNAKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 209 EKFWVKYHFKTDQGIEFLAQEDADTLAGQDGDYHTRDLFEAIKAGNSPSWTLHMQIMPFADAETYRYNPFDLTKVWPHGD 288
Cdd:cd08156 161 ERFWVKFHFKTDQGIKNLTNEEAAELAGEDPDYAQRDLFEAIERGDFPSWTLYVQVMPEEDAEKYRFNPFDLTKVWPHKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 289 YPLIKVGKLVLDHNPTDNFAQIEQVAFEPNNLVPGIGLSPDKMLMGRIFAYADAHRARLGVNYKQIPVNAPKSPVNSYSK 368
Cdd:cd08156 241 YPLIEVGKLELNRNPENYFAEVEQAAFSPSNLVPGIGFSPDKMLQGRLFSYADAHRYRLGVNYHQLPVNRPKCPVNNYQR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 369 DGAMRIDLA--SDPVYAPNSKGGPAADgeRYPTDSTWGSQGNLVRSAYtlRADDDDYSQANDLVNKvMDDAARDRLVNNV 446
Cdd:cd08156 321 DGAMRVDGNggGAPNYEPNSFGGPPED--PEYAEPPLPVSGDADRYNY--RDDDDDYTQAGDLYRL-VSEDERERLVENI 395
|
410 420 430
....*....|....*....|....*....|....*
gi 490273731 447 TGHlLKGVEEPVLSRAFEYWRNIDRATGDRIAARV 481
Cdd:cd08156 396 AGH-LKGAPEFIQERQVAHFYKADPDYGERVAKAL 429
|
|
| Catalase |
pfam00199 |
Catalase; |
10-389 |
0e+00 |
|
Catalase;
Pssm-ID: 459708 Cd Length: 383 Bit Score: 765.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 10 TTDAGIPVASDEHSLTVGPDGPIVLHDHYLIEQMANFNRERIPERQPHAKGSGAFGHFEVTEDVSQFTKAALFQ-PGVKT 88
Cdd:pfam00199 1 TTSNGAPVPDNQNSLTAGPRGPLLLQDFHLIEKLAHFDRERIPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSeVGKKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 89 DVVMRFSTVAGERGSPDTWRDPRGFSIKFYTSEGNYDMVGNNTPVFFIRDPMKFQHFIRSQKRRADNNLRDNDMQWDFWT 168
Cdd:pfam00199 81 PVFVRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHSQKRDPQTNLPDPAMFWDFWS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 169 LSPESAHQVTWLMGDRGIPKSWRHMNGYSSHTYMWVNAQGEKFWVKYHFKTDQGIEFLAQEDADTLAGQDGDYHTRDLFE 248
Cdd:pfam00199 161 LNPESLHQVTWLFSDRGIPRSYRHMNGFGVHTFKLVNADGERVYVKFHFKTDQGIKNLTWEEAQKLAGKDPDYHTRDLYE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 249 AIKAGNSPSWTLHMQIMPFADAETYRYNPFDLTKVWPHGDYPLIKVGKLVLDHNPTDNFAQIEQVAFEPNNLVPGIGLSP 328
Cdd:pfam00199 241 AIERGDYPSWTLYVQVMTEEDAEKFRFNPFDLTKVWPHKDYPLIEVGKMVLNRNPDNYFAEVEQAAFSPSNLVPGIEPSP 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490273731 329 DKMLMGRIFAYADAHRARLGVNYKQIPVNAPKSPVNSYSKDGAMR--IDLASDPVYAPNSKGG 389
Cdd:pfam00199 321 DPMLQGRLFSYPDTQRYRLGPNYQQLPVNRPPCPVHNYQRDGAMRfdINQGSRPNYEPNSFGG 383
|
|
| Catalase |
smart01060 |
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ... |
13-382 |
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: 732.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 13 AGIPVASDEHSLTVGPDGPIVLHDHYLIEQMANFNRERIPERQPHAKGSGAFGHFEVTEDVSQFTKAALFQ-PGVKTDVV 91
Cdd:smart01060 1 QGAPVADNQNSLTAGPRGPVLLQDFHLIEKLAHFDRERIPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQkVGKKTPVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 92 MRFSTVAGERGSPDTWRDPRGFSIKFYTSEGNYDMVGNNTPVFFIRDPMKFQHFIRSQKRRADNNLRDNDMQWDFWTLSP 171
Cdd:smart01060 81 VRFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHAQKRDPRTNLPDHDMFWDFWSLNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 172 ESAHQVTWLMGDRGIPKSWRHMNGYSSHTYMWVNAQGEKFWVKYHFKTDQGIEFLAQEDADTLAGQDGDYHTRDLFEAIK 251
Cdd:smart01060 161 ESLHQVTWLMSDRGIPASYRHMNGFGVHTFKLVNAEGERFYVKFHFKPDQGIKNLTWEEAAKLAGKDPDYHRRDLYEAIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 252 AGNSPSWTLHMQIMPFADAETYRYNPFDLTKVWPHGDYPLIKVGKLVLDHNPTDNFAQIEQVAFEPNNLVPGIGLSPDKM 331
Cdd:smart01060 241 RGDYPEWTLYVQVMPEEDAEKFRFDPFDLTKVWPHKDYPLIEVGKMTLNRNPDNYFAEVEQAAFSPSNLVPGIEFSPDKM 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 490273731 332 LMGRIFAYADAHRARLGVNYKQIPVNAPKSPVNSYSKDGAMRID--LASDPVY 382
Cdd:smart01060 321 LQGRLFSYPDTQRYRLGPNYHQLPVNRPRCPVHNYQRDGAMRVDgnQGGDPNY 373
|
|
| catalase_fungal |
cd08157 |
Fungal catalases similar to yeast catalases A and T; Catalase is a ubiquitous enzyme found in ... |
34-481 |
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: 570.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 34 LHDHYLIEQMANFNRERIPERQPHAKGSGAFGHFEVTEDVSQFTKAALFQ-PGVKTDVVMRFSTVAGERGSPDTWRDPRG 112
Cdd:cd08157 1 LQDFHLIDTLAHFDRERIPERVVHAKGAGAYGEFEVTDDISDITSADMLQgVGKKTPCLVRFSTVGGEKGSADTVRDPRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 113 FSIKFYTSEGNYDMVGNNTPVFFIRDPMKFQHFIRSQKRRADNNLRDNDMQWDFWTLSPESAHQVTWLMGDRGIPKSWRH 192
Cdd:cd08157 81 FAVKFYTEEGNWDWVFNNTPVFFIRDPIKFPHFIHSQKRDPQTNLKDSTMFWDYLSQNPESIHQVMILFSDRGTPASYRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 193 MNGYSSHTYMWVNAQGEKFWVKYHFKTDQGIEFLAQEDADTLAGQDGDYHTRDLFEAIKAGNSPSWTLHMQIMPFADAET 272
Cdd:cd08157 161 MNGYSGHTYKWVNPDGSFKYVQFHLKSDQGPKFLTGEEAARLAGSNPDYATKDLFEAIERGDYPSWTVYVQVMTPEQAEK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 273 YRYNPFDLTKVWPHGDYPLIKVGKLVLDHNPTDNFAQIEQVAFEPNNLVPGIGLSPDKMLMGRIFAYADAHRARLGVNYK 352
Cdd:cd08157 241 LRFNIFDLTKVWPHKDFPLRPVGKLTLNENPKNYFAEIEQAAFSPSHMVPGIEPSADPVLQARLFSYPDAHRHRLGPNYQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 353 QIPVNAPK-SPV-NSYSKDGAMRID--LASDPVYAPNSKggPAADGERYPTDSTWGSQGNLVRSAYTLRADDDDYSQAND 428
Cdd:cd08157 321 QLPVNRPKtSPVyNPYQRDGPMSVNgnYGGDPNYVSSIL--PPTYFKKRVDADGHHENWVGEVVAFLTEITDEDFVQPRA 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 490273731 429 LVNKVMDDAARDRLVNNVTGHlLKGVEEPVLSRAFEYWRNIDRATGDRIAARV 481
Cdd:cd08157 399 LWEVVGKPGQQERFVKNVAGH-LSGAPPEIRKRVYEIFARVNPDLGKRIEKAT 450
|
|
| 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: 545.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 10 TTDAGIPVASDEHSLTVGPDGPIVLHDHYLIEQMANFNRERIPERQPHAKGSGAFGHFEVTEDVSQFTKAALFQ-PGVKT 88
Cdd:cd08154 3 TTNQGAPVGDNQNSQTVGPRGPVLLEDYHLIEKLAHFDRERIPERVVHARGAGAHGYFEAYGDISDYTRASFLQePGKKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 89 DVVMRFSTVAGERGSPDTWRDPRGFSIKFYTSEGNYDMVGNNTPVFFIRDPMKFQHFIRSQKRRADNNLRDNDMQWDFWT 168
Cdd:cd08154 83 PVFVRFSTVIHGKGSPETLRDPRGFAVKFYTEEGNWDLVGNNLPVFFIRDAIKFPDMIHALKPSPVTNIQDPNRIFDFFS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 169 LSPESAHQVTWLMGDRGIPKSWRHMNGYSSHTYMWVNAQGEKFWVKYHFKTDQGIEFLAQEDADTLAGQDGDYHTRDLFE 248
Cdd:cd08154 163 HVPESTHMLTFLYSDWGTPASYRHMDGSGVHTYKWVNAEGKVVYVKYHWKPKQGVKNLTAEEAAEVQGKNFNHATQDLYD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 249 AIKAGNSPSWTLHMQIMPFADAETYRYNPFDLTKVWPHGDYPLIKVGKLVLDHNPTDNFAQIEQVAFEPNNLVPGIGLSP 328
Cdd:cd08154 243 AIAAGNYPEWELYVQIMDPKDLDKLDFDPLDDTKIWPEDQFPLKPVGKMTLNKNPDNFFAEVEQVAFSPGNLVPGIEPSD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 329 DKMLMGRIFAYADAHRARLGVNYKQIPVNAPKSPVNSYSKDGAMRIDLASDPV-YAPNSKGGPAADgERYPtDSTWGSQG 407
Cdd:cd08154 323 DKMLQGRLFSYSDTQRYRLGPNYLQLPINAPKAAVHNNQRDGQMNYGHDTSDVnYEPSRLDGLPEA-PKYP-YSQPPLSG 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490273731 408 NLVRSAYtlrADDDDYSQANDLvNKVMDDAARDRLVNNVTGhLLKGVEEPVLSRAFEYWRNIDRATGDRIAARV 481
Cdd:cd08154 401 TTQQAPI---AKTNNFKQAGER-YRSFSEEEQENLIKNLVV-DLSDVNEEIKLRMLSYFSQADPDYGERVAEGL 469
|
|
| PLN02609 |
PLN02609 |
catalase |
2-487 |
0e+00 |
|
catalase
Pssm-ID: 215328 [Multi-domain] Cd Length: 492 Bit Score: 544.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 2 SDDVRKPTTTDAGIPVASDEHSLTVGPDGPIVLHDHYLIEQMANFNRERIPERQPHAKGSGAFGHFEVTEDVSQFTKAAL 81
Cdd:PLN02609 10 SAYNSPFFTTNSGAPVWNNNSSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDISNLTCADF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 82 FQ-PGVKTDVVMRFSTVAGERGSPDTWRDPRGFSIKFYTSEGNYDMVGNNTPVFFIRDPMKFQHFIRSQKRRADNNLRDN 160
Cdd:PLN02609 90 LRaPGVQTPVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDMVGNNFPVFFIRDGMKFPDMVHALKPNPKTHIQEP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 161 DMQWDFWTLSPESAHQVTWLMGDRGIPKSWRHMNGYSSHTYMWVNAQGEKFWVKYHFKTDQGIEFLAQEDADTLAGQDGD 240
Cdd:PLN02609 170 WRILDFLSHHPESLHMFTFLFDDRGIPQDYRHMEGFGVHTYKLINKAGKAHYVKFHWKPTCGVKNLLDEEAVRVGGSNHS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 241 YHTRDLFEAIKAGNSPSWTLHMQIMPFADAETYRYNPFDLTKVWPHGDYPLIKVGKLVLDHNPTDNFAQIEQVAFEPNNL 320
Cdd:PLN02609 250 HATQDLYDSIAAGNYPEWKLFIQTMDPEDEDKFDFDPLDVTKTWPEDILPLQPVGRLVLNRNIDNFFAENEQLAFCPAIV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 321 VPGIGLSPDKMLMGRIFAYADAHRARLGVNYKQIPVNAPKSPVNSYSKDGAMRI-DLASDPVYAPNSKgGPAADGERYPT 399
Cdd:PLN02609 330 VPGIYYSDDKLLQTRIFAYADTQRHRLGPNYLQLPVNAPKCAHHNNHHEGFMNFmHRDEEVNYFPSRF-DPVRHAERVPI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 400 DSTWGSQgnlvRSAYTLRADDDDYSQANDLVnKVMDDAARDRLVNNVTGHLLKGVEEPVL-SRAFEYWRNIDRATGDRIA 478
Cdd:PLN02609 409 PHPPLSG----RREKCKIEKENNFKQPGERY-RSWSPDRQERFIKRWVDALSDPRVTHEIrSIWISYWSQCDKSLGQKLA 483
|
....*....
gi 490273731 479 ARvLQERAK 487
Cdd:PLN02609 484 SR-LNVKPS 491
|
|
| catalase |
cd00328 |
Catalase heme-binding enzyme; Catalase is a ubiquitous enzyme found in both prokaryotes and ... |
50-479 |
1.64e-180 |
|
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: 512.78 E-value: 1.64e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 50 RIPERQPHAKGSGAFGHFEVTEDVSQFTKAALFQ-PGVKTDVVMRFSTVAGERGSPDTWRDPRGFSIKFYTSEGNYDMVG 128
Cdd:cd00328 1 RIPERVVHARGAGAFGYFTAYGDWSDISAAAFFSaIGKKTPVFVRFSTVVGGAGSADTVRDPHGFATKFYTEEGNFDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 129 NNTPVFFIRDPMKFQHFIRSQKRRADNNLRDNDMQWDFWTLSPESAHQVTWLMGDRGIPKSWRHMNGYSSHTYMWVNAQG 208
Cdd:cd00328 81 NNTPIFFIRDAIKFPDFIHAQKPNPQTALPDADRFWDFLSLRPESLHQVSFLFSDRGIPAAYRHMNGYGSHTFKLVNANG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 209 EKFWVKYHFKTDQGIEFLAQEDADTLAGQDGDYHTRDLFEAIKAGNSPSWTLHMQIMPFADAETYRYNPFDLTKVWPHGD 288
Cdd:cd00328 161 KVHYVKFHWKTDQGIANLVWEEAARLAGEDPDYHRQDLFEAIEAGDYPSWELYIQVMTFNDAEKFPFNPLDPTKVWPEEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 289 YPLIKVGKLVLDHNPTDNFAQIEQVAFEPNNLVPGIGLSPDKMLMGRIFAYADAHRARLGVNYKQIPVNAPKSPVNSYSK 368
Cdd:cd00328 241 VPLIVVGKLVLNRNPLNFFAEVEQAAFDPGHIVPGVEFSEDPLLQGRLFSYADTQLYRLGPNFQQLPVNRPYAPVHNNQR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 369 DGAMR-IDLASDPVYAPNSKG-GPAADGERYPT-DSTWGSQGNLVRSAYTlrADDDDYSQANDLVNkVMDDAARDRLVNN 445
Cdd:cd00328 321 DGAGNmNDNTGVPNYEPNAKDvRYPAQGAPKFDrGHFSHWKSGVNREAST--TNDDNFTQARLFYR-SLTPGQQKRLVDA 397
|
410 420 430
....*....|....*....|....*....|....
gi 490273731 446 VTGHLLKGVEEPVLSRAFEYWRNIDRATGDRIAA 479
Cdd:cd00328 398 FRFELADAVSPQIQQRVLDQFAKVDAAAAKRVAK 431
|
|
| catalase_clade_2 |
cd08155 |
Clade 2 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
49-481 |
3.60e-144 |
|
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: 420.62 E-value: 3.60e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 49 ERIPERQPHAKGSGAFGHFEVTEDVSQFTKAALFQ-PGVKTDVVMRFSTVAGERGSPDTWRDPRGFSIKFYTSEGNYDMV 127
Cdd:cd08155 3 ERIPERVVHARGSGAHGYFQVYESLSQYTKAKFLQdPGKKTPVFVRFSTVAGSRGSADTVRDVRGFAVKFYTEEGNYDLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 128 GNNTPVFFIRDPMKFQHFIRSQKRRADNNLRD----NDMQWDFWTLSPESAHQVTWLMGDRGIPKSWRHMNGYSSHTYMW 203
Cdd:cd08155 83 GNNIPVFFIQDAIKFPDLIHAVKPEPHNEMPQaqsaHDTFWDFVSLQPESAHMVMWAMSDRAIPRSYRMMEGFGVHTFRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 204 VNAQGEKFWVKYHFKTDQGIEFLAQEDADTLAGQDGDYHTRDLFEAIKAGNSPSWTLHMQIMPFADAETYRYNPFDLTKV 283
Cdd:cd08155 163 VNAQGKSTFVKFHWKPVLGVHSLVWDEAQKIAGKDPDFHRRDLWEAIESGDYPEWELGVQLIDEEDEFKFDFDILDPTKL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 284 WPHGDYPLIKVGKLVLDHNPTDNFAQIEQVAFEPNNLVPGIGLSPDKMLMGRIFAYADAHRARLG-VNYKQIPVNAPKSP 362
Cdd:cd08155 243 IPEELVPVQRVGKMVLNRNPDNFFAETEQVAFCPANVVPGIDFSNDPLLQGRLFSYLDTQLSRLGgPNFHELPINRPVCP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 363 VNSYSKDGAMRIDLASDPV-YAPNSKGgpaaDGERYPTDSTWGS--------QGNLVRSaytlRAD--DDDYSQANDLVN 431
Cdd:cd08155 323 VHNNQRDGHMRMTINKGRVnYFPNSLG----AGPPRAASPAEGGfvhypekvEGPKIRI----RSEsfADHYSQARLFWN 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 490273731 432 KvMDDAARDRLVNNVTGHLLKgVEEPVL-SRAFEYWRNIDRATGDRIAARV 481
Cdd:cd08155 395 S-MSPVEKEHIISAFTFELSK-VETPEIrERVVDHLANIDEDLAKKVAKGL 443
|
|
| katE |
PRK11249 |
hydroperoxidase II; Provisional |
8-481 |
8.09e-137 |
|
hydroperoxidase II; Provisional
Pssm-ID: 236886 [Multi-domain] Cd Length: 752 Bit Score: 412.13 E-value: 8.09e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 8 PTTTDAGIPVASDEHSLTVGPDGPIVLHDHYLIEQMANFNRERIPERQPHAKGSGAFGHFEVTEDVSQFTKAALFQ-PGV 86
Cdd:PRK11249 76 ALTTNQGVRIADDQNSLRAGSRGPSLLEDFILREKITHFDHERIPERIVHARGSAAHGYFQPYKSLSDITKAAFLQdPGK 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 87 KTDVVMRFSTVAGERGSPDTWRDPRGFSIKFYTSEGNYDMVGNNTPVFFIRDPMKFQHFIRSQKRRADNNL----RDNDM 162
Cdd:PRK11249 156 ITPVFVRFSTVQGPRGSADTVRDIRGFATKFYTEEGNFDLVGNNTPVFFIQDAIKFPDFVHAVKPEPHNEIpqgqSAHDT 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 163 QWDFWTLSPESAHQVTWLMGDRGIPKSWRHMNGYSSHTYMWVNAQGEKFWVKYHFKTDQGIEFLAQEDADTLAGQDGDYH 242
Cdd:PRK11249 236 FWDYVSLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLINAEGKATFVRFHWKPVAGKASLVWDEAQKLTGRDPDFH 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 243 TRDLFEAIKAGNSPSWTLHMQIMPFADAETYRYNPFDLTKVWPHGDYPLIKVGKLVLDHNPTDNFAQIEQVAFEPNNLVP 322
Cdd:PRK11249 316 RRDLWEAIEAGDYPEYELGVQLIPEEDEFKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFHPGHIVP 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 323 GIGLSPDKMLMGRIFAYADAHRARL-GVNYKQIPVNAPKSPVNSYSKDGAMRIDLASDPV-YAPNSKGG-------PAAD 393
Cdd:PRK11249 396 GIDFTNDPLLQGRLFSYTDTQISRLgGPNFHEIPINRPTCPYHNFQRDGMHRMTIDTGPAnYEPNSINGnwpretpPAPK 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 394 G---ERYPTDstwgSQGNLVRsaytLRADD--DDYSQANdLVNKVMDDAARDRLVNNVTGHLLKGVEEPVLSRAFEYWRN 468
Cdd:PRK11249 476 RggfESYQER----VEGNKVR----ERSPSfgDYYSQPR-LFWLSQTPIEQRHIIDAFSFELGKVVRPYIRERVVDQLAH 546
|
490
....*....|...
gi 490273731 469 IDRATGDRIAARV 481
Cdd:PRK11249 547 IDLTLAQAVAENL 559
|
|
| catalase_like |
cd08150 |
Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found ... |
52-347 |
3.60e-57 |
|
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: 191.23 E-value: 3.60e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 52 PERQPHAKGSGAFGHFEVTEDVSQFTKAALFQPGVKTDVVMRFSTVAgerGSPDTWRDPRGFSIKFYT--SEGNYDMVGN 129
Cdd:cd08150 1 GLRGQHFQGTCAFGTFEVLADLKERLRVGLFAEGKVYPAYIRFSNGA---GIDDTKPDIRGFAIKFTGvaDAGTLDFVLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 130 NTPVFFIRDPMKFQHFIRSQKRRADNNlRDNDMQWDFWTLSPESAHQVTWLMgdRGIPKSWRHMNGYSSHTYMWVNAQGE 209
Cdd:cd08150 78 NTPVFFIRNTSDYEDFVAEFARSARGE-PPLDFIAWYVEKRPEDLPNLLGAR--SQVPDSYAAARYFSQVTFAFINGAGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 210 KFWVKYHFKTDQGIeflAQEDADTLAGQDGDYHTRDLFEAIKAGnSPSWTLHMQIMPFADAETYrynpFDLTKVWPHgDY 289
Cdd:cd08150 155 YRVVRSKDNPVDGI---PSLEDHELEARPPDYLREELTERLQRG-PVVYDFRIQLNDDTDATTI----DNPTILWPT-EH 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 290 PLIKVGKLVLDhNPTDNFAQiEQVAFEPNNLVPGIGLSPDK--MLMGRIFAYADAHRARL 347
Cdd:cd08150 226 PVEAVAKITIP-PPTFTAAQ-EAFAFNPFTPWHGLLETNDLgpILEVRRRVYTSSQGLRH 283
|
|
| srpA_like |
cd08153 |
Catalase-like heme-binding proteins similar to the uncharacterized srpA; Catalase is a ... |
54-347 |
1.44e-44 |
|
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: 158.16 E-value: 1.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 54 RQPHAKGSGAFGHFEVTEDVSQFTKAALFQPGVkTDVVMRFSTVAGERGSPDTWRDPRGFSIKFYTSEGN-YDMVGNNTP 132
Cdd:cd08153 15 RRNHAKGICVSGTFTPSGAAASLSRAPLFSGGS-VPVTGRFSLGGGNPKAPDDAANPRGMALKFRLPDGEqWRMVMNSFP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 133 VFFIRDPMKFQHFIrsQKRRADNNLrDND---MQWdFWTLSPESAHQVTWLmGDRGIPKSWRHMNGYSSHTYMWVNAQGE 209
Cdd:cd08153 94 VFPVRTPEEFLALL--KAIAPDATG-KPDpakLKA-FLAAHPEAAAFLAWI-KTAPPPASFANTTYYGVNAFYFTNANGK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 210 KFWVKYHFKTDQGIEFLAQEDADTLagqDGDYHTRDLFEAIKAGNSpSWTLHMQIMPFADAETyrynpfDLTKVWPhGDY 289
Cdd:cd08153 169 RQPVRWRFVPEDGVKYLSDEEAAKL---GPDFLFDELAQRLAQGPV-RWDLVLQLAEPGDPTD------DPTKPWP-ADR 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 490273731 290 PLIKVGKLVLDHNPTDNFAQIEQVAFEPNNLVPGIGLSPDKMLMGRIFAYADAHRARL 347
Cdd:cd08153 238 KEVDAGTLTITKVAPDQGGACRDINFDPLVLPDGIEPSDDPLLAARSAAYAVSFSRRQ 295
|
|
| Catalase-rel |
pfam06628 |
Catalase-related immune-responsive; This family represents a small conserved region within ... |
420-481 |
1.23e-16 |
|
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: 73.94 E-value: 1.23e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490273731 420 DDDYSQANDLVNkVMDDAARDRLVNNVTGHLLKGVEEPVLSRAFEYWRNIDRATGDRIAARV 481
Cdd:pfam06628 5 DDHFSQAGLFYR-SMSEEERQRLVDNIAFELSKVTDPEIQERMVAHFYKVDPDLGQRVAEAL 65
|
|
| y4iL_like |
cd08152 |
Catalase-like heme-binding proteins similar to the uncharacterized y4iL; Catalase is a ... |
54-315 |
1.25e-11 |
|
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: 65.36 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 54 RQPHAKGSGAF-GHFEVTEDVSQFTKAALFQPGVKTDVVMRFSTVAGERgSPDTWRDPRGFSIKFYTSEG---------- 122
Cdd:cd08152 5 RDAHAKSHGCLkAEFTVLDDLPPELAQGLFAEPGTYPAVIRFSNAPGDI-LDDSVPDPRGMAIKVLGVPGekllpeedat 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 123 NYDMVGNNTPVFFIRDPmkfQHFIRSQKRRAdnNLRDNDMQWDFWTLSPESAHQvTWLMGDRGipksWRHMNGYSSHTYm 202
Cdd:cd08152 84 TQDFVLVNHPVFFARDA---KDYLALLKLLA--RTTSLPDGAKAALSAPLRGAL-RVLEAAGG----ESPTLKLGGHPP- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 203 wVNAQGEKFW-----------VKYHFKTdqgieflAQEDADTLAGQDGDYHTRD--LFEAIK---AGNSPSWTLHMQI-- 264
Cdd:cd08152 153 -AHPLGETYWsqapyrfgdyvAKYSVVP-------ASPALPALTGKELDLTDDPdaLREALAdflAENDAEFEFRIQLct 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 490273731 265 ----MPFADAetyrynpfdlTKVWPHGDYPLIKVGKLVLdhNPTDNFAQIEQVAF 315
Cdd:cd08152 225 dlekMPIEDA----------SVEWPEALSPFVPVATITI--PPQDFDSPARQRAF 267
|
|
| AOS |
cd08151 |
Allene oxide synthase; Allene oxide synthase converts a fatty acid hydroperoxide to an allene ... |
54-328 |
1.61e-09 |
|
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: 59.36 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 54 RQPHAKGSGAFGHFEVTEDvSQFTKAALFQPGVKTDVVMRFSTVAGERGspDTWRDPRGFSIKFYTS----EGNYDMVGN 129
Cdd:cd08151 28 RGTHTIGVGAKGVLTVLAE-SDFPEHAFFTAGKRFPVILRHANIVGGDD--DASLDGRGAALRFLNAgdddAGPLDLVMN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 130 NTPVFFIRDPMKFQHFIRSQkrradnnlrdNDMQWDFWTLSPESAHQVTWlMGDRGIPKSWRHMNGYSSHTYMWVNAQGE 209
Cdd:cd08151 105 TGESFGFWTAASFADFAGAG----------LPFREKAAKLRGPLARYAVW-ASLRRAPDSYTDLHYYSQICYEFVALDGK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273731 210 KFWVKYHF-KTDQGIEFLAQEDADTLAGQDGDYHT-------------RDLFEAIKAGNSPSWTLHMQIMPFADAETYry 275
Cdd:cd08151 174 SRYARFRLlPPDADTEWDLGEDVLETIFQRPRLYLprlpgdtrpkdylRNEFRQRLQSPGVRYRLQIQLREVSDDATA-- 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 490273731 276 NPFDLTKVWPHGDYPLIKVGKLVLDHN-PTDnfaQIEQVAFEPNNLVPGIGLSP 328
Cdd:cd08151 252 VALDCCRPWDEDEHPWLDLAVVRLGAPlPND---ELEKLAFNPGNTPESLGLPL 302
|
|
| |
