|
Name |
Accession |
Description |
Interval |
E-value |
| catalase_clade_3 |
cd08156 |
Clade 3 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
65-494 |
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: 890.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 65 RIPERVVHAKGAGAFGYFEVTHDITKYSKAKVFEHIGKKTPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVG 144
Cdd:cd08156 1 RIPERVVHAKGAGAFGTFEVTHDITKYTKAKIFSEVGKKTPVFVRFSTVAGERGSADTERDPRGFALKFYTEEGNWDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 145 NNTPIFFIRDPILFPSFIHSQKRNPQTHLKDPDMVWDFWSLRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNANG 224
Cdd:cd08156 81 NNTPVFFIRDPIKFPDFIHTQKRNPQTNLKDPDMFWDFWSLSPESLHQVTILFSDRGIPDGYRHMNGYGSHTFSLVNAKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 225 EAVYCKFHYKTDQGIKNLSVEDAARLSQEDPDYGIRDLFNAIATGKYPSWTFYIQVMTFNQAETFPFNPFDLTKVWPHKD 304
Cdd:cd08156 161 ERFWVKFHFKTDQGIKNLTNEEAAELAGEDPDYAQRDLFEAIERGDFPSWTLYVQVMPEEDAEKYRFNPFDLTKVWPHKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 305 YPLIPVGKLVLNRNPVNYFAEVEQIAFDPSNMPPGIEASPDKMLQGRLFAYPDTHRHRLGPNYLHIPVNCPYrARVANYQ 384
Cdd:cd08156 241 YPLIEVGKLELNRNPENYFAEVEQAAFSPSNLVPGIGFSPDKMLQGRLFSYADAHRYRLGVNYHQLPVNRPK-CPVNNYQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 385 RDGPMCMQDNQGGAPNYYPNSFGAPEQQPSALEHSIQYSGEVRRFNTA-NDDNVTQVRAFYVNVlNEEQRKRLCENIAGH 463
Cdd:cd08156 320 RDGAMRVDGNGGGAPNYEPNSFGGPPEDPEYAEPPLPVSGDADRYNYRdDDDDYTQAGDLYRLV-SEDERERLVENIAGH 398
|
410 420 430
....*....|....*....|....*....|.
1DGB_C 464 LKDAQIFIQKKAVKNFTEVHPDYGSHIQALL 494
Cdd:cd08156 399 LKGAPEFIQERQVAHFYKADPDYGERVAKAL 429
|
|
| KatE |
COG0753 |
Catalase [Inorganic ion transport and metabolism]; |
14-494 |
0e+00 |
|
Catalase [Inorganic ion transport and metabolism];
Pssm-ID: 440516 [Multi-domain] Cd Length: 489 Bit Score: 845.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 14 EQRAAQKADVLTTGAGNPVGDKLNVITVGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITKYSK 93
Cdd:COG0753 1 GQYADDEGKTLTTNQGAPVADNQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFEVTEDISKYTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 94 AKVFEHIGKKTPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDPILFPSFIHSQKRNPQTHL 173
Cdd:COG0753 81 AKFFQEPGKKTPVFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHAQKRDPDTNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 174 KDPDMVWDFWSLRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKNLSVEDAARLSQE 253
Cdd:COG0753 161 PQHDTFWDFWSLSPESLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAEGERFWVKFHWKPKQGIHSLTWDEAQKIAGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 254 DPDYGIRDLFNAIATGKYPSWTFYIQVMTFNQAETFPFNPFDLTKVWPHKDYPLIPVGKLVLNRNPVNYFAEVEQIAFDP 333
Cdd:COG0753 241 DPDFHRRDLYEAIERGDFPEWELGVQVMPEEDADKFDFDPLDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAETEQAAFSP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 334 SNMPPGIEASPDKMLQGRLFAYPDTHRHRLGPNYLHIPVNCPyRARVANYQRDGPMCMqDNQGGAPNYYPNSFGAPEQQP 413
Cdd:COG0753 321 GNLVPGIDFSPDKMLQGRLFSYADTQRYRLGPNFHQLPVNRP-KCPVHNYQRDGAMRY-DINGGRVNYEPNSLGGPREDP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 414 SALEHSIQYSGEVRRFNTANDDNVTQVRAFYvNVLNEEQRKRLCENIAGHLKDAQI-FIQKKAVKNFTEVHPDYGSHIQA 492
Cdd:COG0753 399 GFKEPPLKVDGDKVRYRSESDDHFSQAGLLY-RSMSDEEKQHLIDNIAFELGKVESeEIRERMVAHFYNVDPELGARVAE 477
|
..
1DGB_C 493 LL 494
Cdd:COG0753 478 AL 479
|
|
| Catalase |
pfam00199 |
Catalase; |
25-407 |
0e+00 |
|
Catalase;
Pssm-ID: 459708 Cd Length: 383 Bit Score: 822.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 25 TTGAGNPVGDKLNVITVGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITKYSKAKVFEHIGKKT 104
Cdd:pfam00199 1 TTSNGAPVPDNQNSLTAGPRGPLLLQDFHLIEKLAHFDRERIPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSEVGKKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 105 PIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDPILFPSFIHSQKRNPQTHLKDPDMVWDFWS 184
Cdd:pfam00199 81 PVFVRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHSQKRDPQTNLPDPAMFWDFWS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 185 LRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKNLSVEDAARLSQEDPDYGIRDLFN 264
Cdd:pfam00199 161 LNPESLHQVTWLFSDRGIPRSYRHMNGFGVHTFKLVNADGERVYVKFHFKTDQGIKNLTWEEAQKLAGKDPDYHTRDLYE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 265 AIATGKYPSWTFYIQVMTFNQAETFPFNPFDLTKVWPHKDYPLIPVGKLVLNRNPVNYFAEVEQIAFDPSNMPPGIEASP 344
Cdd:pfam00199 241 AIERGDYPSWTLYVQVMTEEDAEKFRFNPFDLTKVWPHKDYPLIEVGKMVLNRNPDNYFAEVEQAAFSPSNLVPGIEPSP 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
1DGB_C 345 DKMLQGRLFAYPDTHRHRLGPNYLHIPVNCPyRARVANYQRDGPMCMQDNQGGAPNYYPNSFG 407
Cdd:pfam00199 321 DPMLQGRLFSYPDTQRYRLGPNYQQLPVNRP-PCPVHNYQRDGAMRFDINQGSRPNYEPNSFG 382
|
|
| Catalase |
smart01060 |
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ... |
28-401 |
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: 784.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 28 AGNPVGDKLNVITVGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITKYSKAKVFEHIGKKTPIA 107
Cdd:smart01060 1 QGAPVADNQNSLTAGPRGPVLLQDFHLIEKLAHFDRERIPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQKVGKKTPVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 108 VRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDPILFPSFIHSQKRNPQTHLKDPDMVWDFWSLRP 187
Cdd:smart01060 81 VRFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHAQKRDPRTNLPDHDMFWDFWSLNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 188 ESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKNLSVEDAARLSQEDPDYGIRDLFNAIA 267
Cdd:smart01060 161 ESLHQVTWLMSDRGIPASYRHMNGFGVHTFKLVNAEGERFYVKFHFKPDQGIKNLTWEEAAKLAGKDPDYHRRDLYEAIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 268 TGKYPSWTFYIQVMTFNQAETFPFNPFDLTKVWPHKDYPLIPVGKLVLNRNPVNYFAEVEQIAFDPSNMPPGIEASPDKM 347
Cdd:smart01060 241 RGDYPEWTLYVQVMPEEDAEKFRFDPFDLTKVWPHKDYPLIEVGKMTLNRNPDNYFAEVEQAAFSPSNLVPGIEFSPDKM 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
1DGB_C 348 LQGRLFAYPDTHRHRLGPNYLHIPVNCPyRARVANYQRDGPMCMQDNQGGAPNY 401
Cdd:smart01060 321 LQGRLFSYPDTQRYRLGPNYHQLPVNRP-RCPVHNYQRDGAMRVDGNQGGDPNY 373
|
|
| PLN02609 |
PLN02609 |
catalase |
25-494 |
0e+00 |
|
catalase
Pssm-ID: 215328 [Multi-domain] Cd Length: 492 Bit Score: 608.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 25 TTGAGNPVGDKLNVITVGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITKYSKAKVFEHIGKKT 104
Cdd:PLN02609 18 TTNSGAPVWNNNSSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDISNLTCADFLRAPGVQT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 105 PIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDPILFPSFIHSQKRNPQTHLKDPDMVWDFWS 184
Cdd:PLN02609 98 PVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDMVGNNFPVFFIRDGMKFPDMVHALKPNPKTHIQEPWRILDFLS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 185 LRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKNLSVEDAARLSQEDPDYGIRDLFN 264
Cdd:PLN02609 178 HHPESLHMFTFLFDDRGIPQDYRHMEGFGVHTYKLINKAGKAHYVKFHWKPTCGVKNLLDEEAVRVGGSNHSHATQDLYD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 265 AIATGKYPSWTFYIQVMTFNQAETFPFNPFDLTKVWPHKDYPLIPVGKLVLNRNPVNYFAEVEQIAFDPSNMPPGIEASP 344
Cdd:PLN02609 258 SIAAGNYPEWKLFIQTMDPEDEDKFDFDPLDVTKTWPEDILPLQPVGRLVLNRNIDNFFAENEQLAFCPAIVVPGIYYSD 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 345 DKMLQGRLFAYPDTHRHRLGPNYLHIPVNCPyRARVANYQRDGPMCMQDNqGGAPNYYPNSFG-APEQQPSALEHSIqYS 423
Cdd:PLN02609 338 DKLLQTRIFAYADTQRHRLGPNYLQLPVNAP-KCAHHNNHHEGFMNFMHR-DEEVNYFPSRFDpVRHAERVPIPHPP-LS 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1DGB_C 424 GEVRRFNTANDDNVTQVRAFYvNVLNEEQRKRLCENIAGHLKDAQIFIQKKA--VKNFTEVHPDYGSHIQALL 494
Cdd:PLN02609 415 GRREKCKIEKENNFKQPGERY-RSWSPDRQERFIKRWVDALSDPRVTHEIRSiwISYWSQCDKSLGQKLASRL 486
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| catalase_clade_3 |
cd08156 |
Clade 3 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
65-494 |
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: 890.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 65 RIPERVVHAKGAGAFGYFEVTHDITKYSKAKVFEHIGKKTPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVG 144
Cdd:cd08156 1 RIPERVVHAKGAGAFGTFEVTHDITKYTKAKIFSEVGKKTPVFVRFSTVAGERGSADTERDPRGFALKFYTEEGNWDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 145 NNTPIFFIRDPILFPSFIHSQKRNPQTHLKDPDMVWDFWSLRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNANG 224
Cdd:cd08156 81 NNTPVFFIRDPIKFPDFIHTQKRNPQTNLKDPDMFWDFWSLSPESLHQVTILFSDRGIPDGYRHMNGYGSHTFSLVNAKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 225 EAVYCKFHYKTDQGIKNLSVEDAARLSQEDPDYGIRDLFNAIATGKYPSWTFYIQVMTFNQAETFPFNPFDLTKVWPHKD 304
Cdd:cd08156 161 ERFWVKFHFKTDQGIKNLTNEEAAELAGEDPDYAQRDLFEAIERGDFPSWTLYVQVMPEEDAEKYRFNPFDLTKVWPHKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 305 YPLIPVGKLVLNRNPVNYFAEVEQIAFDPSNMPPGIEASPDKMLQGRLFAYPDTHRHRLGPNYLHIPVNCPYrARVANYQ 384
Cdd:cd08156 241 YPLIEVGKLELNRNPENYFAEVEQAAFSPSNLVPGIGFSPDKMLQGRLFSYADAHRYRLGVNYHQLPVNRPK-CPVNNYQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 385 RDGPMCMQDNQGGAPNYYPNSFGAPEQQPSALEHSIQYSGEVRRFNTA-NDDNVTQVRAFYVNVlNEEQRKRLCENIAGH 463
Cdd:cd08156 320 RDGAMRVDGNGGGAPNYEPNSFGGPPEDPEYAEPPLPVSGDADRYNYRdDDDDYTQAGDLYRLV-SEDERERLVENIAGH 398
|
410 420 430
....*....|....*....|....*....|.
1DGB_C 464 LKDAQIFIQKKAVKNFTEVHPDYGSHIQALL 494
Cdd:cd08156 399 LKGAPEFIQERQVAHFYKADPDYGERVAKAL 429
|
|
| KatE |
COG0753 |
Catalase [Inorganic ion transport and metabolism]; |
14-494 |
0e+00 |
|
Catalase [Inorganic ion transport and metabolism];
Pssm-ID: 440516 [Multi-domain] Cd Length: 489 Bit Score: 845.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 14 EQRAAQKADVLTTGAGNPVGDKLNVITVGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITKYSK 93
Cdd:COG0753 1 GQYADDEGKTLTTNQGAPVADNQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFEVTEDISKYTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 94 AKVFEHIGKKTPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDPILFPSFIHSQKRNPQTHL 173
Cdd:COG0753 81 AKFFQEPGKKTPVFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHAQKRDPDTNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 174 KDPDMVWDFWSLRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKNLSVEDAARLSQE 253
Cdd:COG0753 161 PQHDTFWDFWSLSPESLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAEGERFWVKFHWKPKQGIHSLTWDEAQKIAGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 254 DPDYGIRDLFNAIATGKYPSWTFYIQVMTFNQAETFPFNPFDLTKVWPHKDYPLIPVGKLVLNRNPVNYFAEVEQIAFDP 333
Cdd:COG0753 241 DPDFHRRDLYEAIERGDFPEWELGVQVMPEEDADKFDFDPLDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAETEQAAFSP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 334 SNMPPGIEASPDKMLQGRLFAYPDTHRHRLGPNYLHIPVNCPyRARVANYQRDGPMCMqDNQGGAPNYYPNSFGAPEQQP 413
Cdd:COG0753 321 GNLVPGIDFSPDKMLQGRLFSYADTQRYRLGPNFHQLPVNRP-KCPVHNYQRDGAMRY-DINGGRVNYEPNSLGGPREDP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 414 SALEHSIQYSGEVRRFNTANDDNVTQVRAFYvNVLNEEQRKRLCENIAGHLKDAQI-FIQKKAVKNFTEVHPDYGSHIQA 492
Cdd:COG0753 399 GFKEPPLKVDGDKVRYRSESDDHFSQAGLLY-RSMSDEEKQHLIDNIAFELGKVESeEIRERMVAHFYNVDPELGARVAE 477
|
..
1DGB_C 493 LL 494
Cdd:COG0753 478 AL 479
|
|
| Catalase |
pfam00199 |
Catalase; |
25-407 |
0e+00 |
|
Catalase;
Pssm-ID: 459708 Cd Length: 383 Bit Score: 822.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 25 TTGAGNPVGDKLNVITVGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITKYSKAKVFEHIGKKT 104
Cdd:pfam00199 1 TTSNGAPVPDNQNSLTAGPRGPLLLQDFHLIEKLAHFDRERIPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSEVGKKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 105 PIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDPILFPSFIHSQKRNPQTHLKDPDMVWDFWS 184
Cdd:pfam00199 81 PVFVRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHSQKRDPQTNLPDPAMFWDFWS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 185 LRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKNLSVEDAARLSQEDPDYGIRDLFN 264
Cdd:pfam00199 161 LNPESLHQVTWLFSDRGIPRSYRHMNGFGVHTFKLVNADGERVYVKFHFKTDQGIKNLTWEEAQKLAGKDPDYHTRDLYE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 265 AIATGKYPSWTFYIQVMTFNQAETFPFNPFDLTKVWPHKDYPLIPVGKLVLNRNPVNYFAEVEQIAFDPSNMPPGIEASP 344
Cdd:pfam00199 241 AIERGDYPSWTLYVQVMTEEDAEKFRFNPFDLTKVWPHKDYPLIEVGKMVLNRNPDNYFAEVEQAAFSPSNLVPGIEPSP 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
1DGB_C 345 DKMLQGRLFAYPDTHRHRLGPNYLHIPVNCPyRARVANYQRDGPMCMQDNQGGAPNYYPNSFG 407
Cdd:pfam00199 321 DPMLQGRLFSYPDTQRYRLGPNYQQLPVNRP-PCPVHNYQRDGAMRFDINQGSRPNYEPNSFG 382
|
|
| Catalase |
smart01060 |
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ... |
28-401 |
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: 784.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 28 AGNPVGDKLNVITVGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITKYSKAKVFEHIGKKTPIA 107
Cdd:smart01060 1 QGAPVADNQNSLTAGPRGPVLLQDFHLIEKLAHFDRERIPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQKVGKKTPVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 108 VRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDPILFPSFIHSQKRNPQTHLKDPDMVWDFWSLRP 187
Cdd:smart01060 81 VRFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHAQKRDPRTNLPDHDMFWDFWSLNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 188 ESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKNLSVEDAARLSQEDPDYGIRDLFNAIA 267
Cdd:smart01060 161 ESLHQVTWLMSDRGIPASYRHMNGFGVHTFKLVNAEGERFYVKFHFKPDQGIKNLTWEEAAKLAGKDPDYHRRDLYEAIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 268 TGKYPSWTFYIQVMTFNQAETFPFNPFDLTKVWPHKDYPLIPVGKLVLNRNPVNYFAEVEQIAFDPSNMPPGIEASPDKM 347
Cdd:smart01060 241 RGDYPEWTLYVQVMPEEDAEKFRFDPFDLTKVWPHKDYPLIEVGKMTLNRNPDNYFAEVEQAAFSPSNLVPGIEFSPDKM 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
1DGB_C 348 LQGRLFAYPDTHRHRLGPNYLHIPVNCPyRARVANYQRDGPMCMQDNQGGAPNY 401
Cdd:smart01060 321 LQGRLFSYPDTQRYRLGPNYHQLPVNRP-RCPVHNYQRDGAMRVDGNQGGDPNY 373
|
|
| catalase |
cd00328 |
Catalase heme-binding enzyme; Catalase is a ubiquitous enzyme found in both prokaryotes and ... |
65-494 |
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: 728.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 65 RIPERVVHAKGAGAFGYFEVTHDITKYSKAKVFEHIGKKTPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVG 144
Cdd:cd00328 1 RIPERVVHARGAGAFGYFTAYGDWSDISAAAFFSAIGKKTPVFVRFSTVVGGAGSADTVRDPHGFATKFYTEEGNFDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 145 NNTPIFFIRDPILFPSFIHSQKRNPQTHLKDPDMVWDFWSLRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNANG 224
Cdd:cd00328 81 NNTPIFFIRDAIKFPDFIHAQKPNPQTALPDADRFWDFLSLRPESLHQVSFLFSDRGIPAAYRHMNGYGSHTFKLVNANG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 225 EAVYCKFHYKTDQGIKNLSVEDAARLSQEDPDYGIRDLFNAIATGKYPSWTFYIQVMTFNQAETFPFNPFDLTKVWPHKD 304
Cdd:cd00328 161 KVHYVKFHWKTDQGIANLVWEEAARLAGEDPDYHRQDLFEAIEAGDYPSWELYIQVMTFNDAEKFPFNPLDPTKVWPEEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 305 YPLIPVGKLVLNRNPVNYFAEVEQIAFDPSNMPPGIEASPDKMLQGRLFAYPDTHRHRLGPNYLHIPVNCPYrARVANYQ 384
Cdd:cd00328 241 VPLIVVGKLVLNRNPLNFFAEVEQAAFDPGHIVPGVEFSEDPLLQGRLFSYADTQLYRLGPNFQQLPVNRPY-APVHNNQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 385 RDGPMCMQDNQGGaPNYYPNSFGAPEQQPSALEHSIQ-----YSGEVRRFNTANDDNVTQVRAFYVNvLNEEQRKRLCEN 459
Cdd:cd00328 320 RDGAGNMNDNTGV-PNYEPNAKDVRYPAQGAPKFDRGhfshwKSGVNREASTTNDDNFTQARLFYRS-LTPGQQKRLVDA 397
|
410 420 430
....*....|....*....|....*....|....*.
1DGB_C 460 IAGHLKDA-QIFIQKKAVKNFTEVHPDYGSHIQALL 494
Cdd:cd00328 398 FRFELADAvSPQIQQRVLDQFAKVDAAAAKRVAKAL 433
|
|
| catalase_fungal |
cd08157 |
Fungal catalases similar to yeast catalases A and T; Catalase is a ubiquitous enzyme found in ... |
50-492 |
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: 687.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 50 QDVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITKYSKAKVFEHIGKKTPIAVRFSTVAGESGSADTVRDPRGF 129
Cdd:cd08157 2 QDFHLIDTLAHFDRERIPERVVHAKGAGAYGEFEVTDDISDITSADMLQGVGKKTPCLVRFSTVGGEKGSADTVRDPRGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 130 AVKFYTEDGNWDLVGNNTPIFFIRDPILFPSFIHSQKRNPQTHLKDPDMVWDFWSLRPESLHQVSFLFSDRGIPDGHRHM 209
Cdd:cd08157 82 AVKFYTEEGNWDWVFNNTPVFFIRDPIKFPHFIHSQKRDPQTNLKDSTMFWDYLSQNPESIHQVMILFSDRGTPASYRSM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 210 NGYGSHTFKLVNANGEAVYCKFHYKTDQGIKNLSVEDAARLSQEDPDYGIRDLFNAIATGKYPSWTFYIQVMTFNQAETF 289
Cdd:cd08157 162 NGYSGHTYKWVNPDGSFKYVQFHLKSDQGPKFLTGEEAARLAGSNPDYATKDLFEAIERGDYPSWTVYVQVMTPEQAEKL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 290 PFNPFDLTKVWPHKDYPLIPVGKLVLNRNPVNYFAEVEQIAFDPSNMPPGIEASPDKMLQGRLFAYPDTHRHRLGPNYLH 369
Cdd:cd08157 242 RFNIFDLTKVWPHKDFPLRPVGKLTLNENPKNYFAEIEQAAFSPSHMVPGIEPSADPVLQARLFSYPDAHRHRLGPNYQQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 370 IPVNCPYRARVAN-YQRDGPMCMQDNQGGAPNyYPNSFGAP---EQQPSALEHSIQYSGEVRRFNTA-NDDNVTQVRAFY 444
Cdd:cd08157 322 LPVNRPKTSPVYNpYQRDGPMSVNGNYGGDPN-YVSSILPPtyfKKRVDADGHHENWVGEVVAFLTEiTDEDFVQPRALW 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
1DGB_C 445 VNVLNEEQRKRLCENIAGHLKDAQIFIQKKAVKNFTEVHPDYGSHIQA 492
Cdd:cd08157 401 EVVGKPGQQERFVKNVAGHLSGAPPEIRKRVYEIFARVNPDLGKRIEK 448
|
|
| catalase_clade_1 |
cd08154 |
Clade 1 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
24-494 |
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: 628.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 24 LTTGAGNPVGDKLNVITVGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITKYSKAKVFEHIGKK 103
Cdd:cd08154 2 LTTNQGAPVGDNQNSQTVGPRGPVLLEDYHLIEKLAHFDRERIPERVVHARGAGAHGYFEAYGDISDYTRASFLQEPGKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 104 TPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDPILFPSFIHSQKRNPQTHLKDPDMVWDFW 183
Cdd:cd08154 82 TPVFVRFSTVIHGKGSPETLRDPRGFAVKFYTEEGNWDLVGNNLPVFFIRDAIKFPDMIHALKPSPVTNIQDPNRIFDFF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 184 SLRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKNLSVEDAARLSQEDPDYGIRDLF 263
Cdd:cd08154 162 SHVPESTHMLTFLYSDWGTPASYRHMDGSGVHTYKWVNAEGKVVYVKYHWKPKQGVKNLTAEEAAEVQGKNFNHATQDLY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 264 NAIATGKYPSWTFYIQVMTFNQAETFPFNPFDLTKVWPHKDYPLIPVGKLVLNRNPVNYFAEVEQIAFDPSNMPPGIEAS 343
Cdd:cd08154 242 DAIAAGNYPEWELYVQIMDPKDLDKLDFDPLDDTKIWPEDQFPLKPVGKMTLNKNPDNFFAEVEQVAFSPGNLVPGIEPS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 344 PDKMLQGRLFAYPDTHRHRLGPNYLHIPVNCPyRARVANYQRDGPMCMQdNQGGAPNYYPNSFGAPEQQPSALEHSIQYS 423
Cdd:cd08154 322 DDKMLQGRLFSYSDTQRYRLGPNYLQLPINAP-KAAVHNNQRDGQMNYG-HDTSDVNYEPSRLDGLPEAPKYPYSQPPLS 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1DGB_C 424 GEVRRFNTANDDNVTQVRAFYVNvLNEEQRKRLCENIAGHLKDAQIFIQKKAVKNFTEVHPDYGSHIQALL 494
Cdd:cd08154 400 GTTQQAPIAKTNNFKQAGERYRS-FSEEEQENLIKNLVVDLSDVNEEIKLRMLSYFSQADPDYGERVAEGL 469
|
|
| PLN02609 |
PLN02609 |
catalase |
25-494 |
0e+00 |
|
catalase
Pssm-ID: 215328 [Multi-domain] Cd Length: 492 Bit Score: 608.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 25 TTGAGNPVGDKLNVITVGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITKYSKAKVFEHIGKKT 104
Cdd:PLN02609 18 TTNSGAPVWNNNSSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDISNLTCADFLRAPGVQT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 105 PIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDPILFPSFIHSQKRNPQTHLKDPDMVWDFWS 184
Cdd:PLN02609 98 PVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDMVGNNFPVFFIRDGMKFPDMVHALKPNPKTHIQEPWRILDFLS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 185 LRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKNLSVEDAARLSQEDPDYGIRDLFN 264
Cdd:PLN02609 178 HHPESLHMFTFLFDDRGIPQDYRHMEGFGVHTYKLINKAGKAHYVKFHWKPTCGVKNLLDEEAVRVGGSNHSHATQDLYD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 265 AIATGKYPSWTFYIQVMTFNQAETFPFNPFDLTKVWPHKDYPLIPVGKLVLNRNPVNYFAEVEQIAFDPSNMPPGIEASP 344
Cdd:PLN02609 258 SIAAGNYPEWKLFIQTMDPEDEDKFDFDPLDVTKTWPEDILPLQPVGRLVLNRNIDNFFAENEQLAFCPAIVVPGIYYSD 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 345 DKMLQGRLFAYPDTHRHRLGPNYLHIPVNCPyRARVANYQRDGPMCMQDNqGGAPNYYPNSFG-APEQQPSALEHSIqYS 423
Cdd:PLN02609 338 DKLLQTRIFAYADTQRHRLGPNYLQLPVNAP-KCAHHNNHHEGFMNFMHR-DEEVNYFPSRFDpVRHAERVPIPHPP-LS 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1DGB_C 424 GEVRRFNTANDDNVTQVRAFYvNVLNEEQRKRLCENIAGHLKDAQIFIQKKA--VKNFTEVHPDYGSHIQALL 494
Cdd:PLN02609 415 GRREKCKIEKENNFKQPGERY-RSWSPDRQERFIKRWVDALSDPRVTHEIRSiwISYWSQCDKSLGQKLASRL 486
|
|
| catalase_clade_2 |
cd08155 |
Clade 2 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
62-490 |
4.24e-161 |
|
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: 464.15 E-value: 4.24e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 62 DRERIPERVVHAKGAGAFGYFEVTHDITKYSKAKVFEHIGKKTPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWD 141
Cdd:cd08155 1 DHERIPERVVHARGSGAHGYFQVYESLSQYTKAKFLQDPGKKTPVFVRFSTVAGSRGSADTVRDVRGFAVKFYTEEGNYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 142 LVGNNTPIFFIRDPILFPSFIHSQKrnPQTHLKDP------DMVWDFWSLRPESLHQVSFLFSDRGIPDGHRHMNGYGSH 215
Cdd:cd08155 81 LVGNNIPVFFIQDAIKFPDLIHAVK--PEPHNEMPqaqsahDTFWDFVSLQPESAHMVMWAMSDRAIPRSYRMMEGFGVH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 216 TFKLVNANGEAVYCKFHYKTDQGIKNLSVEDAARLSQEDPDYGIRDLFNAIATGKYPSWTFYIQVMTFNQAETFPFNPFD 295
Cdd:cd08155 159 TFRLVNAQGKSTFVKFHWKPVLGVHSLVWDEAQKIAGKDPDFHRRDLWEAIESGDYPEWELGVQLIDEEDEFKFDFDILD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 296 LTKVWPHKDYPLIPVGKLVLNRNPVNYFAEVEQIAFDPSNMPPGIEASPDKMLQGRLFAYPDTHRHRLG-PNYLHIPVNC 374
Cdd:cd08155 239 PTKLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFCPANVVPGIDFSNDPLLQGRLFSYLDTQLSRLGgPNFHELPINR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 375 PyRARVANYQRDGPMCMQDNQGGApNYYPNSFGA--PEQQPSALEHSIQYSGEV-----RRFNTANDDNVTQVRAFYVNV 447
Cdd:cd08155 319 P-VCPVHNNQRDGHMRMTINKGRV-NYFPNSLGAgpPRAASPAEGGFVHYPEKVegpkiRIRSESFADHYSQARLFWNSM 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
1DGB_C 448 LNEEQRkrlceniagHLKDAQIF---------IQKKAVKNFTEVHPDYGSHI 490
Cdd:cd08155 397 SPVEKE---------HIISAFTFelskvetpeIRERVVDHLANIDEDLAKKV 439
|
|
| katE |
PRK11249 |
hydroperoxidase II; Provisional |
1-415 |
1.22e-155 |
|
hydroperoxidase II; Provisional
Pssm-ID: 236886 [Multi-domain] Cd Length: 752 Bit Score: 461.05 E-value: 1.22e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 1 SRDPASDQMQHWKEQRAAQKADVLTTGAGNPVGDKLNVITVGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFG 80
Cdd:PRK11249 54 APDTRNEKLNSLEAFRKGSEGYALTTNQGVRIADDQNSLRAGSRGPSLLEDFILREKITHFDHERIPERIVHARGSAAHG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 81 YFEVTHDITKYSKAKVFEHIGKKTPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDPILFPS 160
Cdd:PRK11249 134 YFQPYKSLSDITKAAFLQDPGKITPVFVRFSTVQGPRGSADTVRDIRGFATKFYTEEGNFDLVGNNTPVFFIQDAIKFPD 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 161 FIHSQKrnPQTHLKDP------DMVWDFWSLRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYK 234
Cdd:PRK11249 214 FVHAVK--PEPHNEIPqgqsahDTFWDYVSLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLINAEGKATFVRFHWK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 235 TDQGIKNLSVEDAARLSQEDPDYGIRDLFNAIATGKYPSWTFYIQVMTFNQAETFPFNPFDLTKVWPHKDYPLIPVGKLV 314
Cdd:PRK11249 292 PVAGKASLVWDEAQKLTGRDPDFHRRDLWEAIEAGDYPEYELGVQLIPEEDEFKFDFDLLDPTKLIPEELVPVQRVGKMV 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 315 LNRNPVNYFAEVEQIAFDPSNMPPGIEASPDKMLQGRLFAYPDTHRHRL-GPNYLHIPVN---CPYrarvANYQRDGPMC 390
Cdd:PRK11249 372 LNRNPDNFFAETEQVAFHPGHIVPGIDFTNDPLLQGRLFSYTDTQISRLgGPNFHEIPINrptCPY----HNFQRDGMHR 447
|
410 420
....*....|....*....|....*..
1DGB_C 391 MQDNQGGApNYYPNSF--GAPEQQPSA 415
Cdd:PRK11249 448 MTIDTGPA-NYEPNSIngNWPRETPPA 473
|
|
| catalase_like |
cd08150 |
Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found ... |
67-363 |
1.49e-64 |
|
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: 210.88 E-value: 1.49e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 67 PERVVHAKGAGAFGYFEVTHDITKYSKAKVFEHiGKKTPIAVRFSTVAGesgSADTVRDPRGFAVKFYTEDGN--WDLVG 144
Cdd:cd08150 1 GLRGQHFQGTCAFGTFEVLADLKERLRVGLFAE-GKVYPAYIRFSNGAG---IDDTKPDIRGFAIKFTGVADAgtLDFVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 145 NNTPIFFIRDPILFPSFIHSQKRNPQTHlKDPDMVWDFWSLRPESLHQVSFLFSdrGIPDGHRHMNGYGSHTFKLVNANG 224
Cdd:cd08150 77 NNTPVFFIRNTSDYEDFVAEFARSARGE-PPLDFIAWYVEKRPEDLPNLLGARS--QVPDSYAAARYFSQVTFAFINGAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 225 EAVYCKFHYKTDQGIKNLSvedAARLSQEDPDYGIRDLFNAIATGkYPSWTFYIQVmtfNQAETfPFNPFDLTKVWPhKD 304
Cdd:cd08150 154 KYRVVRSKDNPVDGIPSLE---DHELEARPPDYLREELTERLQRG-PVVYDFRIQL---NDDTD-ATTIDNPTILWP-TE 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
1DGB_C 305 YPLIPVGKLVLNRNPVNyfAEVEQIAFDPSNMPPGIEASPDK--MLQGRLFAYPDTHRHRL 363
Cdd:cd08150 225 HPVEAVAKITIPPPTFT--AAQEAFAFNPFTPWHGLLETNDLgpILEVRRRVYTSSQGLRH 283
|
|
| srpA_like |
cd08153 |
Catalase-like heme-binding proteins similar to the uncharacterized srpA; Catalase is a ... |
69-363 |
7.97e-45 |
|
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: 158.93 E-value: 7.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 69 RVVHAKGAGAFGYFEVTHDITKYSKAKVFEhiGKKTPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGN-WDLVGNNT 147
Cdd:cd08153 15 RRNHAKGICVSGTFTPSGAAASLSRAPLFS--GGSVPVTGRFSLGGGNPKAPDDAANPRGMALKFRLPDGEqWRMVMNSF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 148 PIFFIRDPILFPSFIhsQKRNPQTHLK-DPDMVWDFWSLRPESLHQVSFLFSdRGIPDGHRHMNGYGSHTFKLVNANGEA 226
Cdd:cd08153 93 PVFPVRTPEEFLALL--KAIAPDATGKpDPAKLKAFLAAHPEAAAFLAWIKT-APPPASFANTTYYGVNAFYFTNANGKR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 227 VYCKFHYKTDQGIKNLSVEDAArlsQEDPDYGIRDLFNAIATGKYpSWTFYIQVmtfnqAEtfPFNPF-DLTKVWPhKDY 305
Cdd:cd08153 170 QPVRWRFVPEDGVKYLSDEEAA---KLGPDFLFDELAQRLAQGPV-RWDLVLQL-----AE--PGDPTdDPTKPWP-ADR 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
1DGB_C 306 PLIPVGKLVLNRNPVNYFAEVEQIAFDPSNMPPGIEASPDKMLQGRLFAYPDTHRHRL 363
Cdd:cd08153 238 KEVDAGTLTITKVAPDQGGACRDINFDPLVLPDGIEPSDDPLLAARSAAYAVSFSRRQ 295
|
|
| Catalase-rel |
pfam06628 |
Catalase-related immune-responsive; This family represents a small conserved region within ... |
434-494 |
2.05e-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: 73.55 E-value: 2.05e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
1DGB_C 434 DDNVTQVRAFYvNVLNEEQRKRLCENIAGHLKDAQI-FIQKKAVKNFTEVHPDYGSHIQALL 494
Cdd:pfam06628 5 DDHFSQAGLFY-RSMSEEERQRLVDNIAFELSKVTDpEIQERMVAHFYKVDPDLGQRVAEAL 65
|
|
| AOS |
cd08151 |
Allene oxide synthase; Allene oxide synthase converts a fatty acid hydroperoxide to an allene ... |
69-338 |
1.81e-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: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 69 RVVHAKGAGAFGYFEVTHDItKYSKAKVFEHiGKKTPIAVRFSTVAGesGSADTVRDPRGFAVKFYT----EDGNWDLVG 144
Cdd:cd08151 28 RGTHTIGVGAKGVLTVLAES-DFPEHAFFTA-GKRFPVILRHANIVG--GDDDASLDGRGAALRFLNagddDAGPLDLVM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 145 NNTPIFFIRDPILFPSFI--------HSQKRnpqTHLKDPDMVWdfwslrpESLhqvsflfsdRGIPDGHRHMNGYGSHT 216
Cdd:cd08151 104 NTGESFGFWTAASFADFAgaglpfreKAAKL---RGPLARYAVW-------ASL---------RRAPDSYTDLHYYSQIC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 217 FKLVNANGEAVYCKFH-YKTDQGIKNLSVEDA------------ARLSQED--PDYgIRDLFNAIATGKYPSWTFYIQVM 281
Cdd:cd08151 165 YEFVALDGKSRYARFRlLPPDADTEWDLGEDVletifqrprlylPRLPGDTrpKDY-LRNEFRQRLQSPGVRYRLQIQLR 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
1DGB_C 282 TFNQAETFPFnpFDLTKVWPHKDYPLIPVGKLVLNRNPVNyfAEVEQIAFDPSNMPP 338
Cdd:cd08151 244 EVSDDATAVA--LDCCRPWDEDEHPWLDLAVVRLGAPLPN--DELEKLAFNPGNTPE 296
|
|
| y4iL_like |
cd08152 |
Catalase-like heme-binding proteins similar to the uncharacterized y4iL; Catalase is a ... |
69-332 |
7.23e-09 |
|
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: 57.27 E-value: 7.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 69 RVVHAKGAGAF-GYFEVTHDITKYSKAKVFEHiGKKTPIAVRFSTVAGEsGSADTVRDPRGFAVKFY----------TED 137
Cdd:cd08152 5 RDAHAKSHGCLkAEFTVLDDLPPELAQGLFAE-PGTYPAVIRFSNAPGD-ILDDSVPDPRGMAIKVLgvpgekllpeEDA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 138 GNWDLVGNNTPIFFIRDPILFPSFIHSQKRNPQThlkdPDMVWDFWS---LRPESLHQVSFLFSDRGIPDGH--RHMNGY 212
Cdd:cd08152 83 TTQDFVLVNHPVFFARDAKDYLALLKLLARTTSL----PDGAKAALSaplRGALRVLEAAGGESPTLKLGGHppAHPLGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DGB_C 213 GSHT---FKLvnanGEAVyCKFHYKTDQGiKNLSVEDAARLSQEDPDYgIRD-LFNAIATGKYpSWTFYIQVMTfnQAET 288
Cdd:cd08152 159 TYWSqapYRF----GDYV-AKYSVVPASP-ALPALTGKELDLTDDPDA-LREaLADFLAENDA-EFEFRIQLCT--DLEK 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....
1DGB_C 289 FPFNpfDLTKVWPHKDYPLIPVGKLVLNRNPVNyfAEVEQIAFD 332
Cdd:cd08152 229 MPIE--DASVEWPEALSPFVPVATITIPPQDFD--SPARQRAFD 268
|
|
| |
