|
Name |
Accession |
Description |
Interval |
E-value |
| KatE |
COG0753 |
Catalase [Inorganic ion transport and metabolism]; |
2-479 |
0e+00 |
|
Catalase [Inorganic ion transport and metabolism];
Pssm-ID: 440516 [Multi-domain] Cd Length: 489 Bit Score: 915.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 2 TDKTLHSTNGAPVVDNNNSLTAGPRGPVLMQDIWLMEKLAHFDRERIPERVVHAKGSGAYGTFTVTHDISAFSKADLFNA 81
Cdd:COG0753 7 EGKTLTTNQGAPVADNQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFEVTEDISKYTKAKFFQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 82 IGKQTPVFLRFSTVAGEKGAADAERDVRGFALKFYTEQGNWDLVGNNTPVFFIRDPLKFPDFIHTQKRDPRTNLRSATAA 161
Cdd:COG0753 87 PGKKTPVFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHAQKRDPDTNLPQHDTF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 162 WDFWSRHPESLHQVTILFSDRGIPKSLREMNGYGSHTFSFINDANERFWVKFHFKTEQGHSFYTDEEAANVVGQDRETSQ 241
Cdd:COG0753 167 WDFWSLSPESLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAEGERFWVKFHWKPKQGIHSLTWDEAQKIAGKDPDFHR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 242 ADLYNAIERGDFPRWKVYVQVMPEADAQTYRIHPFDLTKVWPHSDYPLIPVGVLELNQNPDNYFAHVEQAAFTPANVVPG 321
Cdd:COG0753 247 RDLYEAIERGDFPEWELGVQVMPEEDADKFDFDPLDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAETEQAAFSPGNLVPG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 322 IGFSPDRMLQGRLFSYGDTQRYRLGVNHGLLPVNAPRCPFHHGaHRDGAMRSDSNGGaSPNYQPNRFGTQQPSEQH-EPA 400
Cdd:COG0753 327 IDFSPDKMLQGRLFSYADTQRYRLGPNFHQLPVNRPKCPVHNY-QRDGAMRYDINGG-RVNYEPNSLGGPREDPGFkEPP 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544709564 401 LSLEGAALHYDFRdyDSDYYSQPGKLFRIMDEGQRSRLAANMARSLINVEDDAIVVAQLRHLEQADPEYAKRVELALAA 479
Cdd:COG0753 405 LKVDGDKVRYRSE--SDDHFSQAGLLYRSMSDEEKQHLIDNIAFELGKVESEEIRERMVAHFYNVDPELGARVAEALGL 481
|
|
| catalase_clade_3 |
cd08156 |
Clade 3 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
47-477 |
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: 817.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 47 RIPERVVHAKGSGAYGTFTVTHDISAFSKADLFNAIGKQTPVFLRFSTVAGEKGAADAERDVRGFALKFYTEQGNWDLVG 126
Cdd:cd08156 1 RIPERVVHAKGAGAFGTFEVTHDITKYTKAKIFSEVGKKTPVFVRFSTVAGERGSADTERDPRGFALKFYTEEGNWDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 127 NNTPVFFIRDPLKFPDFIHTQKRDPRTNLRSATAAWDFWSRHPESLHQVTILFSDRGIPKSLREMNGYGSHTFSFINDAN 206
Cdd:cd08156 81 NNTPVFFIRDPIKFPDFIHTQKRNPQTNLKDPDMFWDFWSLSPESLHQVTILFSDRGIPDGYRHMNGYGSHTFSLVNAKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 207 ERFWVKFHFKTEQGHSFYTDEEAANVVGQDRETSQADLYNAIERGDFPRWKVYVQVMPEADAQTYRIHPFDLTKVWPHSD 286
Cdd:cd08156 161 ERFWVKFHFKTDQGIKNLTNEEAAELAGEDPDYAQRDLFEAIERGDFPSWTLYVQVMPEEDAEKYRFNPFDLTKVWPHKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 287 YPLIPVGVLELNQNPDNYFAHVEQAAFTPANVVPGIGFSPDRMLQGRLFSYGDTQRYRLGVNHGLLPVNAPRCPFHHGaH 366
Cdd:cd08156 241 YPLIEVGKLELNRNPENYFAEVEQAAFSPSNLVPGIGFSPDKMLQGRLFSYADAHRYRLGVNYHQLPVNRPKCPVNNY-Q 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 367 RDGAMRSDSNGGASPNYQPNRF-GTQQPSEQHEPALSLEGAALHYDFRDyDSDYYSQPGKLFRIMDEGQRSRLAANMARS 445
Cdd:cd08156 320 RDGAMRVDGNGGGAPNYEPNSFgGPPEDPEYAEPPLPVSGDADRYNYRD-DDDDYTQAGDLYRLVSEDERERLVENIAGH 398
|
410 420 430
....*....|....*....|....*....|..
gi 544709564 446 LINVEDDaIVVAQLRHLEQADPEYAKRVELAL 477
Cdd:cd08156 399 LKGAPEF-IQERQVAHFYKADPDYGERVAKAL 429
|
|
| Catalase |
pfam00199 |
Catalase; |
8-389 |
0e+00 |
|
Catalase;
Pssm-ID: 459708 Cd Length: 383 Bit Score: 799.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 8 STNGAPVVDNNNSLTAGPRGPVLMQDIWLMEKLAHFDRERIPERVVHAKGSGAYGTFTVTHDISAFSKADLFNAIGKQTP 87
Cdd:pfam00199 2 TSNGAPVPDNQNSLTAGPRGPLLLQDFHLIEKLAHFDRERIPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSEVGKKTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 88 VFLRFSTVAGEKGAADAERDVRGFALKFYTEQGNWDLVGNNTPVFFIRDPLKFPDFIHTQKRDPRTNLRSATAAWDFWSR 167
Cdd:pfam00199 82 VFVRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHSQKRDPQTNLPDPAMFWDFWSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 168 HPESLHQVTILFSDRGIPKSLREMNGYGSHTFSFINDANERFWVKFHFKTEQGHSFYTDEEAANVVGQDRETSQADLYNA 247
Cdd:pfam00199 162 NPESLHQVTWLFSDRGIPRSYRHMNGFGVHTFKLVNADGERVYVKFHFKTDQGIKNLTWEEAQKLAGKDPDYHTRDLYEA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 248 IERGDFPRWKVYVQVMPEADAQTYRIHPFDLTKVWPHSDYPLIPVGVLELNQNPDNYFAHVEQAAFTPANVVPGIGFSPD 327
Cdd:pfam00199 242 IERGDYPSWTLYVQVMTEEDAEKFRFNPFDLTKVWPHKDYPLIEVGKMVLNRNPDNYFAEVEQAAFSPSNLVPGIEPSPD 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544709564 328 RMLQGRLFSYGDTQRYRLGVNHGLLPVNAPRCPFHHgAHRDGAMRSDSNGGASPNYQPNRFG 389
Cdd:pfam00199 322 PMLQGRLFSYPDTQRYRLGPNYQQLPVNRPPCPVHN-YQRDGAMRFDINQGSRPNYEPNSFG 382
|
|
| Catalase |
smart01060 |
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ... |
10-383 |
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: 765.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 10 NGAPVVDNNNSLTAGPRGPVLMQDIWLMEKLAHFDRERIPERVVHAKGSGAYGTFTVTHDISAFSKADLFNAIGKQTPVF 89
Cdd:smart01060 1 QGAPVADNQNSLTAGPRGPVLLQDFHLIEKLAHFDRERIPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQKVGKKTPVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 90 LRFSTVAGEKGAADAERDVRGFALKFYTEQGNWDLVGNNTPVFFIRDPLKFPDFIHTQKRDPRTNLRSATAAWDFWSRHP 169
Cdd:smart01060 81 VRFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHAQKRDPRTNLPDHDMFWDFWSLNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 170 ESLHQVTILFSDRGIPKSLREMNGYGSHTFSFINDANERFWVKFHFKTEQGHSFYTDEEAANVVGQDRETSQADLYNAIE 249
Cdd:smart01060 161 ESLHQVTWLMSDRGIPASYRHMNGFGVHTFKLVNAEGERFYVKFHFKPDQGIKNLTWEEAAKLAGKDPDYHRRDLYEAIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 250 RGDFPRWKVYVQVMPEADAQTYRIHPFDLTKVWPHSDYPLIPVGVLELNQNPDNYFAHVEQAAFTPANVVPGIGFSPDRM 329
Cdd:smart01060 241 RGDYPEWTLYVQVMPEEDAEKFRFDPFDLTKVWPHKDYPLIEVGKMTLNRNPDNYFAEVEQAAFSPSNLVPGIEFSPDKM 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 544709564 330 LQGRLFSYGDTQRYRLGVNHGLLPVNAPRCPFHHGaHRDGAMRSDSNGGASPNY 383
Cdd:smart01060 321 LQGRLFSYPDTQRYRLGPNYHQLPVNRPRCPVHNY-QRDGAMRVDGNQGGDPNY 373
|
|
| PLN02609 |
PLN02609 |
catalase |
7-478 |
0e+00 |
|
catalase
Pssm-ID: 215328 [Multi-domain] Cd Length: 492 Bit Score: 592.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 7 HSTN-GAPVVDNNNSLTAGPRGPVLMQDIWLMEKLAHFDRERIPERVVHAKGSGAYGTFTVTHDISAFSKADLFNAIGKQ 85
Cdd:PLN02609 17 FTTNsGAPVWNNNSSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDISNLTCADFLRAPGVQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 86 TPVFLRFSTVAGEKGAADAERDVRGFALKFYTEQGNWDLVGNNTPVFFIRDPLKFPDFIHTQKRDPRTNLRSATAAWDFW 165
Cdd:PLN02609 97 TPVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDMVGNNFPVFFIRDGMKFPDMVHALKPNPKTHIQEPWRILDFL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 166 SRHPESLHQVTILFSDRGIPKSLREMNGYGSHTFSFINDANERFWVKFHFKTEQGHSFYTDEEAANVVGQDRETSQADLY 245
Cdd:PLN02609 177 SHHPESLHMFTFLFDDRGIPQDYRHMEGFGVHTYKLINKAGKAHYVKFHWKPTCGVKNLLDEEAVRVGGSNHSHATQDLY 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 246 NAIERGDFPRWKVYVQVMPEADAQTYRIHPFDLTKVWPHSDYPLIPVGVLELNQNPDNYFAHVEQAAFTPANVVPGIGFS 325
Cdd:PLN02609 257 DSIAAGNYPEWKLFIQTMDPEDEDKFDFDPLDVTKTWPEDILPLQPVGRLVLNRNIDNFFAENEQLAFCPAIVVPGIYYS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 326 PDRMLQGRLFSYGDTQRYRLGVNHGLLPVNAPRCPfHHGAHRDGAMRSDSNgGASPNYQPNRFGTQQPSEQH-EPALSLE 404
Cdd:PLN02609 337 DDKLLQTRIFAYADTQRHRLGPNYLQLPVNAPKCA-HHNNHHEGFMNFMHR-DEEVNYFPSRFDPVRHAERVpIPHPPLS 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544709564 405 GAALHYDFRDYDSdyYSQPGKLFRIMDEGQRSRLAANMARSLinveDDAIVVAQLR-----HLEQADPEYAKRVELALA 478
Cdd:PLN02609 415 GRREKCKIEKENN--FKQPGERYRSWSPDRQERFIKRWVDAL----SDPRVTHEIRsiwisYWSQCDKSLGQKLASRLN 487
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| KatE |
COG0753 |
Catalase [Inorganic ion transport and metabolism]; |
2-479 |
0e+00 |
|
Catalase [Inorganic ion transport and metabolism];
Pssm-ID: 440516 [Multi-domain] Cd Length: 489 Bit Score: 915.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 2 TDKTLHSTNGAPVVDNNNSLTAGPRGPVLMQDIWLMEKLAHFDRERIPERVVHAKGSGAYGTFTVTHDISAFSKADLFNA 81
Cdd:COG0753 7 EGKTLTTNQGAPVADNQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFEVTEDISKYTKAKFFQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 82 IGKQTPVFLRFSTVAGEKGAADAERDVRGFALKFYTEQGNWDLVGNNTPVFFIRDPLKFPDFIHTQKRDPRTNLRSATAA 161
Cdd:COG0753 87 PGKKTPVFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHAQKRDPDTNLPQHDTF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 162 WDFWSRHPESLHQVTILFSDRGIPKSLREMNGYGSHTFSFINDANERFWVKFHFKTEQGHSFYTDEEAANVVGQDRETSQ 241
Cdd:COG0753 167 WDFWSLSPESLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAEGERFWVKFHWKPKQGIHSLTWDEAQKIAGKDPDFHR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 242 ADLYNAIERGDFPRWKVYVQVMPEADAQTYRIHPFDLTKVWPHSDYPLIPVGVLELNQNPDNYFAHVEQAAFTPANVVPG 321
Cdd:COG0753 247 RDLYEAIERGDFPEWELGVQVMPEEDADKFDFDPLDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAETEQAAFSPGNLVPG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 322 IGFSPDRMLQGRLFSYGDTQRYRLGVNHGLLPVNAPRCPFHHGaHRDGAMRSDSNGGaSPNYQPNRFGTQQPSEQH-EPA 400
Cdd:COG0753 327 IDFSPDKMLQGRLFSYADTQRYRLGPNFHQLPVNRPKCPVHNY-QRDGAMRYDINGG-RVNYEPNSLGGPREDPGFkEPP 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544709564 401 LSLEGAALHYDFRdyDSDYYSQPGKLFRIMDEGQRSRLAANMARSLINVEDDAIVVAQLRHLEQADPEYAKRVELALAA 479
Cdd:COG0753 405 LKVDGDKVRYRSE--SDDHFSQAGLLYRSMSDEEKQHLIDNIAFELGKVESEEIRERMVAHFYNVDPELGARVAEALGL 481
|
|
| catalase_clade_3 |
cd08156 |
Clade 3 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
47-477 |
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: 817.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 47 RIPERVVHAKGSGAYGTFTVTHDISAFSKADLFNAIGKQTPVFLRFSTVAGEKGAADAERDVRGFALKFYTEQGNWDLVG 126
Cdd:cd08156 1 RIPERVVHAKGAGAFGTFEVTHDITKYTKAKIFSEVGKKTPVFVRFSTVAGERGSADTERDPRGFALKFYTEEGNWDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 127 NNTPVFFIRDPLKFPDFIHTQKRDPRTNLRSATAAWDFWSRHPESLHQVTILFSDRGIPKSLREMNGYGSHTFSFINDAN 206
Cdd:cd08156 81 NNTPVFFIRDPIKFPDFIHTQKRNPQTNLKDPDMFWDFWSLSPESLHQVTILFSDRGIPDGYRHMNGYGSHTFSLVNAKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 207 ERFWVKFHFKTEQGHSFYTDEEAANVVGQDRETSQADLYNAIERGDFPRWKVYVQVMPEADAQTYRIHPFDLTKVWPHSD 286
Cdd:cd08156 161 ERFWVKFHFKTDQGIKNLTNEEAAELAGEDPDYAQRDLFEAIERGDFPSWTLYVQVMPEEDAEKYRFNPFDLTKVWPHKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 287 YPLIPVGVLELNQNPDNYFAHVEQAAFTPANVVPGIGFSPDRMLQGRLFSYGDTQRYRLGVNHGLLPVNAPRCPFHHGaH 366
Cdd:cd08156 241 YPLIEVGKLELNRNPENYFAEVEQAAFSPSNLVPGIGFSPDKMLQGRLFSYADAHRYRLGVNYHQLPVNRPKCPVNNY-Q 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 367 RDGAMRSDSNGGASPNYQPNRF-GTQQPSEQHEPALSLEGAALHYDFRDyDSDYYSQPGKLFRIMDEGQRSRLAANMARS 445
Cdd:cd08156 320 RDGAMRVDGNGGGAPNYEPNSFgGPPEDPEYAEPPLPVSGDADRYNYRD-DDDDYTQAGDLYRLVSEDERERLVENIAGH 398
|
410 420 430
....*....|....*....|....*....|..
gi 544709564 446 LINVEDDaIVVAQLRHLEQADPEYAKRVELAL 477
Cdd:cd08156 399 LKGAPEF-IQERQVAHFYKADPDYGERVAKAL 429
|
|
| Catalase |
pfam00199 |
Catalase; |
8-389 |
0e+00 |
|
Catalase;
Pssm-ID: 459708 Cd Length: 383 Bit Score: 799.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 8 STNGAPVVDNNNSLTAGPRGPVLMQDIWLMEKLAHFDRERIPERVVHAKGSGAYGTFTVTHDISAFSKADLFNAIGKQTP 87
Cdd:pfam00199 2 TSNGAPVPDNQNSLTAGPRGPLLLQDFHLIEKLAHFDRERIPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSEVGKKTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 88 VFLRFSTVAGEKGAADAERDVRGFALKFYTEQGNWDLVGNNTPVFFIRDPLKFPDFIHTQKRDPRTNLRSATAAWDFWSR 167
Cdd:pfam00199 82 VFVRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHSQKRDPQTNLPDPAMFWDFWSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 168 HPESLHQVTILFSDRGIPKSLREMNGYGSHTFSFINDANERFWVKFHFKTEQGHSFYTDEEAANVVGQDRETSQADLYNA 247
Cdd:pfam00199 162 NPESLHQVTWLFSDRGIPRSYRHMNGFGVHTFKLVNADGERVYVKFHFKTDQGIKNLTWEEAQKLAGKDPDYHTRDLYEA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 248 IERGDFPRWKVYVQVMPEADAQTYRIHPFDLTKVWPHSDYPLIPVGVLELNQNPDNYFAHVEQAAFTPANVVPGIGFSPD 327
Cdd:pfam00199 242 IERGDYPSWTLYVQVMTEEDAEKFRFNPFDLTKVWPHKDYPLIEVGKMVLNRNPDNYFAEVEQAAFSPSNLVPGIEPSPD 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544709564 328 RMLQGRLFSYGDTQRYRLGVNHGLLPVNAPRCPFHHgAHRDGAMRSDSNGGASPNYQPNRFG 389
Cdd:pfam00199 322 PMLQGRLFSYPDTQRYRLGPNYQQLPVNRPPCPVHN-YQRDGAMRFDINQGSRPNYEPNSFG 382
|
|
| Catalase |
smart01060 |
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ... |
10-383 |
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: 765.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 10 NGAPVVDNNNSLTAGPRGPVLMQDIWLMEKLAHFDRERIPERVVHAKGSGAYGTFTVTHDISAFSKADLFNAIGKQTPVF 89
Cdd:smart01060 1 QGAPVADNQNSLTAGPRGPVLLQDFHLIEKLAHFDRERIPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQKVGKKTPVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 90 LRFSTVAGEKGAADAERDVRGFALKFYTEQGNWDLVGNNTPVFFIRDPLKFPDFIHTQKRDPRTNLRSATAAWDFWSRHP 169
Cdd:smart01060 81 VRFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHAQKRDPRTNLPDHDMFWDFWSLNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 170 ESLHQVTILFSDRGIPKSLREMNGYGSHTFSFINDANERFWVKFHFKTEQGHSFYTDEEAANVVGQDRETSQADLYNAIE 249
Cdd:smart01060 161 ESLHQVTWLMSDRGIPASYRHMNGFGVHTFKLVNAEGERFYVKFHFKPDQGIKNLTWEEAAKLAGKDPDYHRRDLYEAIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 250 RGDFPRWKVYVQVMPEADAQTYRIHPFDLTKVWPHSDYPLIPVGVLELNQNPDNYFAHVEQAAFTPANVVPGIGFSPDRM 329
Cdd:smart01060 241 RGDYPEWTLYVQVMPEEDAEKFRFDPFDLTKVWPHKDYPLIEVGKMTLNRNPDNYFAEVEQAAFSPSNLVPGIEFSPDKM 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 544709564 330 LQGRLFSYGDTQRYRLGVNHGLLPVNAPRCPFHHGaHRDGAMRSDSNGGASPNY 383
Cdd:smart01060 321 LQGRLFSYPDTQRYRLGPNYHQLPVNRPRCPVHNY-QRDGAMRVDGNQGGDPNY 373
|
|
| catalase_clade_1 |
cd08154 |
Clade 1 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
5-477 |
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: 616.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 5 TLHSTNGAPVVDNNNSLTAGPRGPVLMQDIWLMEKLAHFDRERIPERVVHAKGSGAYGTFTVTHDISAFSKADLFNAIGK 84
Cdd:cd08154 1 TLTTNQGAPVGDNQNSQTVGPRGPVLLEDYHLIEKLAHFDRERIPERVVHARGAGAHGYFEAYGDISDYTRASFLQEPGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 85 QTPVFLRFSTVAGEKGAADAERDVRGFALKFYTEQGNWDLVGNNTPVFFIRDPLKFPDFIHTQKRDPRTNLRSATAAWDF 164
Cdd:cd08154 81 KTPVFVRFSTVIHGKGSPETLRDPRGFAVKFYTEEGNWDLVGNNLPVFFIRDAIKFPDMIHALKPSPVTNIQDPNRIFDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 165 WSRHPESLHQVTILFSDRGIPKSLREMNGYGSHTFSFINDANERFWVKFHFKTEQGHSFYTDEEAANVVGQDRETSQADL 244
Cdd:cd08154 161 FSHVPESTHMLTFLYSDWGTPASYRHMDGSGVHTYKWVNAEGKVVYVKYHWKPKQGVKNLTAEEAAEVQGKNFNHATQDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 245 YNAIERGDFPRWKVYVQVMPEADAQTYRIHPFDLTKVWPHSDYPLIPVGVLELNQNPDNYFAHVEQAAFTPANVVPGIGF 324
Cdd:cd08154 241 YDAIAAGNYPEWELYVQIMDPKDLDKLDFDPLDDTKIWPEDQFPLKPVGKMTLNKNPDNFFAEVEQVAFSPGNLVPGIEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 325 SPDRMLQGRLFSYGDTQRYRLGVNHGLLPVNAPRCPfHHGAHRDGAMRSdSNGGASPNYQPNRFGTQQPSEQH-EPALSL 403
Cdd:cd08154 321 SDDKMLQGRLFSYSDTQRYRLGPNYLQLPINAPKAA-VHNNQRDGQMNY-GHDTSDVNYEPSRLDGLPEAPKYpYSQPPL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544709564 404 EGAALHYdfRDYDSDYYSQPGKLFRIMDEGQRSRLAANMARSLINVEDDaIVVAQLRHLEQADPEYAKRVELAL 477
Cdd:cd08154 399 SGTTQQA--PIAKTNNFKQAGERYRSFSEEEQENLIKNLVVDLSDVNEE-IKLRMLSYFSQADPDYGERVAEGL 469
|
|
| PLN02609 |
PLN02609 |
catalase |
7-478 |
0e+00 |
|
catalase
Pssm-ID: 215328 [Multi-domain] Cd Length: 492 Bit Score: 592.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 7 HSTN-GAPVVDNNNSLTAGPRGPVLMQDIWLMEKLAHFDRERIPERVVHAKGSGAYGTFTVTHDISAFSKADLFNAIGKQ 85
Cdd:PLN02609 17 FTTNsGAPVWNNNSSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDISNLTCADFLRAPGVQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 86 TPVFLRFSTVAGEKGAADAERDVRGFALKFYTEQGNWDLVGNNTPVFFIRDPLKFPDFIHTQKRDPRTNLRSATAAWDFW 165
Cdd:PLN02609 97 TPVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDMVGNNFPVFFIRDGMKFPDMVHALKPNPKTHIQEPWRILDFL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 166 SRHPESLHQVTILFSDRGIPKSLREMNGYGSHTFSFINDANERFWVKFHFKTEQGHSFYTDEEAANVVGQDRETSQADLY 245
Cdd:PLN02609 177 SHHPESLHMFTFLFDDRGIPQDYRHMEGFGVHTYKLINKAGKAHYVKFHWKPTCGVKNLLDEEAVRVGGSNHSHATQDLY 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 246 NAIERGDFPRWKVYVQVMPEADAQTYRIHPFDLTKVWPHSDYPLIPVGVLELNQNPDNYFAHVEQAAFTPANVVPGIGFS 325
Cdd:PLN02609 257 DSIAAGNYPEWKLFIQTMDPEDEDKFDFDPLDVTKTWPEDILPLQPVGRLVLNRNIDNFFAENEQLAFCPAIVVPGIYYS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 326 PDRMLQGRLFSYGDTQRYRLGVNHGLLPVNAPRCPfHHGAHRDGAMRSDSNgGASPNYQPNRFGTQQPSEQH-EPALSLE 404
Cdd:PLN02609 337 DDKLLQTRIFAYADTQRHRLGPNYLQLPVNAPKCA-HHNNHHEGFMNFMHR-DEEVNYFPSRFDPVRHAERVpIPHPPLS 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544709564 405 GAALHYDFRDYDSdyYSQPGKLFRIMDEGQRSRLAANMARSLinveDDAIVVAQLR-----HLEQADPEYAKRVELALA 478
Cdd:PLN02609 415 GRREKCKIEKENN--FKQPGERYRSWSPDRQERFIKRWVDAL----SDPRVTHEIRsiwisYWSQCDKSLGQKLASRLN 487
|
|
| catalase_fungal |
cd08157 |
Fungal catalases similar to yeast catalases A and T; Catalase is a ubiquitous enzyme found in ... |
31-478 |
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: 588.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 31 MQDIWLMEKLAHFDRERIPERVVHAKGSGAYGTFTVTHDISAFSKADLFNAIGKQTPVFLRFSTVAGEKGAADAERDVRG 110
Cdd:cd08157 1 LQDFHLIDTLAHFDRERIPERVVHAKGAGAYGEFEVTDDISDITSADMLQGVGKKTPCLVRFSTVGGEKGSADTVRDPRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 111 FALKFYTEQGNWDLVGNNTPVFFIRDPLKFPDFIHTQKRDPRTNLRSATAAWDFWSRHPESLHQVTILFSDRGIPKSLRE 190
Cdd:cd08157 81 FAVKFYTEEGNWDWVFNNTPVFFIRDPIKFPHFIHSQKRDPQTNLKDSTMFWDYLSQNPESIHQVMILFSDRGTPASYRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 191 MNGYGSHTFSFINDANERFWVKFHFKTEQGHSFYTDEEAANVVGQDRETSQADLYNAIERGDFPRWKVYVQVMPEADAQT 270
Cdd:cd08157 161 MNGYSGHTYKWVNPDGSFKYVQFHLKSDQGPKFLTGEEAARLAGSNPDYATKDLFEAIERGDYPSWTVYVQVMTPEQAEK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 271 YRIHPFDLTKVWPHSDYPLIPVGVLELNQNPDNYFAHVEQAAFTPANVVPGIGFSPDRMLQGRLFSYGDTQRYRLGVNHG 350
Cdd:cd08157 241 LRFNIFDLTKVWPHKDFPLRPVGKLTLNENPKNYFAEIEQAAFSPSHMVPGIEPSADPVLQARLFSYPDAHRHRLGPNYQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 351 LLPVNAPR-CPFHHGAHRDGAMRSDSNGGASPNY----QPNRFGTQQPSE-QHEPALSLEGAALHYDFRDYDsdyYSQPG 424
Cdd:cd08157 321 QLPVNRPKtSPVYNPYQRDGPMSVNGNYGGDPNYvssiLPPTYFKKRVDAdGHHENWVGEVVAFLTEITDED---FVQPR 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 544709564 425 KL-FRIMDEGQRSRLAANMARSLINVEDDaIVVAQLRHLEQADPEYAKRVELALA 478
Cdd:cd08157 398 ALwEVVGKPGQQERFVKNVAGHLSGAPPE-IRKRVYEIFARVNPDLGKRIEKATE 451
|
|
| catalase |
cd00328 |
Catalase heme-binding enzyme; Catalase is a ubiquitous enzyme found in both prokaryotes and ... |
47-477 |
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: 517.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 47 RIPERVVHAKGSGAYGTFTVTHDISAFSKADLFNAIGKQTPVFLRFSTVAGEKGAADAERDVRGFALKFYTEQGNWDLVG 126
Cdd:cd00328 1 RIPERVVHARGAGAFGYFTAYGDWSDISAAAFFSAIGKKTPVFVRFSTVVGGAGSADTVRDPHGFATKFYTEEGNFDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 127 NNTPVFFIRDPLKFPDFIHTQKRDPRTNLRSATAAWDFWSRHPESLHQVTILFSDRGIPKSLREMNGYGSHTFSFINDAN 206
Cdd:cd00328 81 NNTPIFFIRDAIKFPDFIHAQKPNPQTALPDADRFWDFLSLRPESLHQVSFLFSDRGIPAAYRHMNGYGSHTFKLVNANG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 207 ERFWVKFHFKTEQGHSFYTDEEAANVVGQDRETSQADLYNAIERGDFPRWKVYVQVMPEADAQTYRIHPFDLTKVWPHSD 286
Cdd:cd00328 161 KVHYVKFHWKTDQGIANLVWEEAARLAGEDPDYHRQDLFEAIEAGDYPSWELYIQVMTFNDAEKFPFNPLDPTKVWPEEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 287 YPLIPVGVLELNQNPDNYFAHVEQAAFTPANVVPGIGFSPDRMLQGRLFSYGDTQRYRLGVNHGLLPVNAPRCPFHHGaH 366
Cdd:cd00328 241 VPLIVVGKLVLNRNPLNFFAEVEQAAFDPGHIVPGVEFSEDPLLQGRLFSYADTQLYRLGPNFQQLPVNRPYAPVHNN-Q 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 367 RDGAMRSDSNGGAsPNYQPNRFGTQQPSE-----QHEPALSLEGAALHYdFRDYDSDYYSQPGKLFRIMDEGQRSRLAAN 441
Cdd:cd00328 320 RDGAGNMNDNTGV-PNYEPNAKDVRYPAQgapkfDRGHFSHWKSGVNRE-ASTTNDDNFTQARLFYRSLTPGQQKRLVDA 397
|
410 420 430
....*....|....*....|....*....|....*.
gi 544709564 442 MARSLINVEDDAIVVAQLRHLEQADPEYAKRVELAL 477
Cdd:cd00328 398 FRFELADAVSPQIQQRVLDQFAKVDAAAAKRVAKAL 433
|
|
| catalase_clade_2 |
cd08155 |
Clade 2 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
44-477 |
2.94e-160 |
|
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: 461.07 E-value: 2.94e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 44 DRERIPERVVHAKGSGAYGTFTVTHDISAFSKADLFNAIGKQTPVFLRFSTVAGEKGAADAERDVRGFALKFYTEQGNWD 123
Cdd:cd08155 1 DHERIPERVVHARGSGAHGYFQVYESLSQYTKAKFLQDPGKKTPVFVRFSTVAGSRGSADTVRDVRGFAVKFYTEEGNYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 124 LVGNNTPVFFIRDPLKFPDFIHTQKRDPRTNLRSATAA----WDFWSRHPESLHQVTILFSDRGIPKSLREMNGYGSHTF 199
Cdd:cd08155 81 LVGNNIPVFFIQDAIKFPDLIHAVKPEPHNEMPQAQSAhdtfWDFVSLQPESAHMVMWAMSDRAIPRSYRMMEGFGVHTF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 200 SFINDANERFWVKFHFKTEQG-HSFYTDeEAANVVGQDRETSQADLYNAIERGDFPRWKVYVQVMPEADAQTYRIHPFDL 278
Cdd:cd08155 161 RLVNAQGKSTFVKFHWKPVLGvHSLVWD-EAQKIAGKDPDFHRRDLWEAIESGDYPEWELGVQLIDEEDEFKFDFDILDP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 279 TKVWPHSDYPLIPVGVLELNQNPDNYFAHVEQAAFTPANVVPGIGFSPDRMLQGRLFSYGDTQRYRLG-VNHGLLPVNAP 357
Cdd:cd08155 240 TKLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFCPANVVPGIDFSNDPLLQGRLFSYLDTQLSRLGgPNFHELPINRP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 358 RCPFHHGaHRDGAMRSDSNGGASpNYQPNRFGTQQPseqhEPALSLEGAALHYDFR----------DYDSDYYSQPGKLF 427
Cdd:cd08155 320 VCPVHNN-QRDGHMRMTINKGRV-NYFPNSLGAGPP----RAASPAEGGFVHYPEKvegpkirirsESFADHYSQARLFW 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 544709564 428 RIMDEGQRSRLAANMARSLINVEDDAIVVAQLRHLEQADPEYAKRVELAL 477
Cdd:cd08155 394 NSMSPVEKEHIISAFTFELSKVETPEIRERVVDHLANIDEDLAKKVAKGL 443
|
|
| katE |
PRK11249 |
hydroperoxidase II; Provisional |
2-473 |
5.07e-159 |
|
hydroperoxidase II; Provisional
Pssm-ID: 236886 [Multi-domain] Cd Length: 752 Bit Score: 469.14 E-value: 5.07e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 2 TDKTLHSTNGAPVVDNNNSLTAGPRGPVLMQDIWLMEKLAHFDRERIPERVVHAKGSGAYGTFTVTHDISAFSKADLFNA 81
Cdd:PRK11249 73 EGYALTTNQGVRIADDQNSLRAGSRGPSLLEDFILREKITHFDHERIPERIVHARGSAAHGYFQPYKSLSDITKAAFLQD 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 82 IGKQTPVFLRFSTVAGEKGAADAERDVRGFALKFYTEQGNWDLVGNNTPVFFIRDPLKFPDFIHTQKRDPRTNLRSATAA 161
Cdd:PRK11249 153 PGKITPVFVRFSTVQGPRGSADTVRDIRGFATKFYTEEGNFDLVGNNTPVFFIQDAIKFPDFVHAVKPEPHNEIPQGQSA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 162 ----WDFWSRHPESLHQVTILFSDRGIPKSLREMNGYGSHTFSFINDANERFWVKFHFKTEQG-HSFYTDeEAANVVGQD 236
Cdd:PRK11249 233 hdtfWDYVSLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLINAEGKATFVRFHWKPVAGkASLVWD-EAQKLTGRD 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 237 RETSQADLYNAIERGDFPRWKVYVQVMPEADAQTYRIHPFDLTKVWPHSDYPLIPVGVLELNQNPDNYFAHVEQAAFTPA 316
Cdd:PRK11249 312 PDFHRRDLWEAIEAGDYPEYELGVQLIPEEDEFKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFHPG 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 317 NVVPGIGFSPDRMLQGRLFSYGDTQRYRL-GVNHGLLPVNAPRCPFHHGaHRDGAMRSDSNGGASpNYQPNRFGTQQPSE 395
Cdd:PRK11249 392 HIVPGIDFTNDPLLQGRLFSYTDTQISRLgGPNFHEIPINRPTCPYHNF-QRDGMHRMTIDTGPA-NYEPNSINGNWPRE 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 396 QhEPALSLEGaalhydFRDYD---------------SDYYSQPGKLFRIMDEGQRSRLAANMARSLINVEDDAIVVAQLR 460
Cdd:PRK11249 470 T-PPAPKRGG------FESYQervegnkvrerspsfGDYYSQPRLFWLSQTPIEQRHIIDAFSFELGKVVRPYIRERVVD 542
|
490
....*....|...
gi 544709564 461 HLEQADPEYAKRV 473
Cdd:PRK11249 543 QLAHIDLTLAQAV 555
|
|
| catalase_like |
cd08150 |
Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found ... |
49-345 |
2.98e-59 |
|
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: 196.63 E-value: 2.98e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 49 PERVVHAKGSGAYGTFTVTHDISAFSKADLFNAiGKQTPVFLRFSTVageKGAADAERDVRGFALKFYTEQGN--WDLVG 126
Cdd:cd08150 1 GLRGQHFQGTCAFGTFEVLADLKERLRVGLFAE-GKVYPAYIRFSNG---AGIDDTKPDIRGFAIKFTGVADAgtLDFVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 127 NNTPVFFIRDPLKFPDFIHTQKRDPRTNLRSATaAWDFWSRHPESLHQVtiLFSDRGIPKSLREMNGYGSHTFSFINDAN 206
Cdd:cd08150 77 NNTPVFFIRNTSDYEDFVAEFARSARGEPPLDF-IAWYVEKRPEDLPNL--LGARSQVPDSYAAARYFSQVTFAFINGAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 207 ERFWVKFHFKTEQGHSFYTDEEAAnvvGQDRETSQADLYNAIERGdFPRWKVYVQVMPEADAQTYrihpFDLTKVWPhSD 286
Cdd:cd08150 154 KYRVVRSKDNPVDGIPSLEDHELE---ARPPDYLREELTERLQRG-PVVYDFRIQLNDDTDATTI----DNPTILWP-TE 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544709564 287 YPLIPVGVLELNQNPDNyfAHVEQAAFTPANVVPGIGFSPDR--MLQGRLFSYGDTQRYRL 345
Cdd:cd08150 225 HPVEAVAKITIPPPTFT--AAQEAFAFNPFTPWHGLLETNDLgpILEVRRRVYTSSQGLRH 283
|
|
| srpA_like |
cd08153 |
Catalase-like heme-binding proteins similar to the uncharacterized srpA; Catalase is a ... |
51-333 |
1.02e-39 |
|
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: 145.07 E-value: 1.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 51 RVVHAKGSGAYGTFTVTHDISAFSKADLFNaiGKQTPVFLRFSTVAGEKGAADAERDVRGFALKFYTEQGN-WDLVGNNT 129
Cdd:cd08153 15 RRNHAKGICVSGTFTPSGAAASLSRAPLFS--GGSVPVTGRFSLGGGNPKAPDDAANPRGMALKFRLPDGEqWRMVMNSF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 130 PVFFIRDPLKFPDFIHTQKRDPRTNLRSATAAWdFWSRHPESLHQVTILFSdRGIPKSLREMNGYGSHTFSFINDANERF 209
Cdd:cd08153 93 PVFPVRTPEEFLALLKAIAPDATGKPDPAKLKA-FLAAHPEAAAFLAWIKT-APPPASFANTTYYGVNAFYFTNANGKRQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 210 WVKFHFKTEQGHSFYTDEEAANvvgQDRETSQADLYNAIERGdfP-RWKVYVQVMPEADAQTyrihpfDLTKVWPhSDYP 288
Cdd:cd08153 171 PVRWRFVPEDGVKYLSDEEAAK---LGPDFLFDELAQRLAQG--PvRWDLVLQLAEPGDPTD------DPTKPWP-ADRK 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 544709564 289 LIPVGVLELNQNPDNYFAHVEQAAFTPANVVPGIGFSPDRMLQGR 333
Cdd:cd08153 239 EVDAGTLTITKVAPDQGGACRDINFDPLVLPDGIEPSDDPLLAAR 283
|
|
| Catalase-rel |
pfam06628 |
Catalase-related immune-responsive; This family represents a small conserved region within ... |
418-477 |
1.79e-17 |
|
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: 76.25 E-value: 1.79e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 418 DYYSQPGKLFRIMDEGQRSRLAANMARSLINVEDDAIVVAQLRHLEQADPEYAKRVELAL 477
Cdd:pfam06628 6 DHFSQAGLFYRSMSEEERQRLVDNIAFELSKVTDPEIQERMVAHFYKVDPDLGQRVAEAL 65
|
|
| AOS |
cd08151 |
Allene oxide synthase; Allene oxide synthase converts a fatty acid hydroperoxide to an allene ... |
51-326 |
3.04e-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: 58.20 E-value: 3.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 51 RVVHAKGSGAYGTFTVTHDiSAFSKADLFNAiGKQTPVFLRFSTVAGEKGaaDAERDVRGFALKFYT----EQGNWDLVG 126
Cdd:cd08151 28 RGTHTIGVGAKGVLTVLAE-SDFPEHAFFTA-GKRFPVILRHANIVGGDD--DASLDGRGAALRFLNagddDAGPLDLVM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 127 NNTPVFFIRDPLKFPDFIHT-----QKRDPRTNLRSATAAWdfwsrhpESLhqvtilfsdRGIPKSLREMNGYGSHTFSF 201
Cdd:cd08151 104 NTGESFGFWTAASFADFAGAglpfrEKAAKLRGPLARYAVW-------ASL---------RRAPDSYTDLHYYSQICYEF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 202 INDANERFWVKFHF-------KTEQGHSFYTDEEAANVVGQDRETSQADLYNAIeRGDFP--------RWKVYVQVMPEA 266
Cdd:cd08151 168 VALDGKSRYARFRLlppdadtEWDLGEDVLETIFQRPRLYLPRLPGDTRPKDYL-RNEFRqrlqspgvRYRLQIQLREVS 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544709564 267 DAQTYRIhpFDLTKVWPHSDYPLIPVGVLELNQN-PDNYfahVEQAAFTPANVVPGIGFSP 326
Cdd:cd08151 247 DDATAVA--LDCCRPWDEDEHPWLDLAVVRLGAPlPNDE---LEKLAFNPGNTPESLGLPL 302
|
|
| y4iL_like |
cd08152 |
Catalase-like heme-binding proteins similar to the uncharacterized y4iL; Catalase is a ... |
51-320 |
1.42e-08 |
|
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: 56.12 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 51 RVVHAKGSGAY-GTFTVTHDISAFSKADLFnAIGKQTPVFLRFSTVAGEkGAADAERDVRGFALKFY----------TEQ 119
Cdd:cd08152 5 RDAHAKSHGCLkAEFTVLDDLPPELAQGLF-AEPGTYPAVIRFSNAPGD-ILDDSVPDPRGMAIKVLgvpgekllpeEDA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 120 GNWDLVGNNTPVFFIRDPLKFPDFIHTQKRDPRTNLRSATAAWDFWSRHpeslhqVTILFSDRGIPKSLREMNGYGSHTF 199
Cdd:cd08152 83 TTQDFVLVNHPVFFARDAKDYLALLKLLARTTSLPDGAKAALSAPLRGA------LRVLEAAGGESPTLKLGGHPPAHPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 200 SfindanERFW-----------VKFHFKTEQGHSF-YTDEEAANVVGQD--RETsqadLYNAIERGDFpRWKVYVQVMPE 265
Cdd:cd08152 157 G------ETYWsqapyrfgdyvAKYSVVPASPALPaLTGKELDLTDDPDalREA----LADFLAENDA-EFEFRIQLCTD 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 544709564 266 ADAQtyrihPF-DLTKVWPHSDYPLIPVGVLELNQ----NPDNYFAHVEQAAFTPANVVP 320
Cdd:cd08152 226 LEKM-----PIeDASVEWPEALSPFVPVATITIPPqdfdSPARQRAFDDNLSFNPWHGLA 280
|
|
| |
