|
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: 860.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 65 RIPERVVHAKGGGAFGYFEVTHDITKYCKAKPFEFVGKKTPVGIRFSTVGGESGSADSARDPRGFAVKFYTEDGNWDVVG 144
Cdd:cd08156 1 RIPERVVHAKGAGAFGTFEVTHDITKYTKAKIFSEVGKKTPVFVRFSTVAGERGSADTERDPRGFALKFYTEEGNWDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 145 NNTPIFFIRDPMLFPNFIHTQKRNPQTHLKDPDMFWDFISLRPETTHQVSFLFSDRGTPNGFRKMNGYGSHTFKMVNKEG 224
Cdd:cd08156 81 NNTPVFFIRDPIKFPDFIHTQKRNPQTNLKDPDMFWDFWSLSPESLHQVTILFSDRGIPDGYRHMNGYGSHTFSLVNAKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 225 KPVYCKFHFKTDQGIKNLMADQAAELSKNDPDYAIRDLFNAISEGDFPSWSLFIQVMTFEEAEKFKYNPFDLTKVWPQGE 304
Cdd:cd08156 161 ERFWVKFHFKTDQGIKNLTNEEAAELAGEDPDYAQRDLFEAIERGDFPSWTLYVQVMPEEDAEKYRFNPFDLTKVWPHKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 305 YPLIPVGRMVLNRNPKNYFAEVEQIAFSPAHMIPGIEASPDKMLQGRLFSYSDTHRHRLGSNYLQLAVNCPFnTKAKNYQ 384
Cdd:cd08156 241 YPLIEVGKLELNRNPENYFAEVEQAAFSPSNLVPGIGFSPDKMLQGRLFSYADAHRYRLGVNYHQLPVNRPK-CPVNNYQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 385 RDGPQCVGDNQGNAPNYFPNSFSGPQDNKQFLESPFSITGDVQRYETG-DEDNFSQVTVFWNKVlKPEERQRLVENIAGH 463
Cdd:cd08156 320 RDGAMRVDGNGGGAPNYEPNSFGGPPEDPEYAEPPLPVSGDADRYNYRdDDDDYTQAGDLYRLV-SEDERERLVENIAGH 398
|
410 420 430
....*....|....*....|....*....|.
gi 1768460843 464 LKNAQEFIQRRTVHNFTQVHPDFGGGIQKLL 494
Cdd:cd08156 399 LKGAPEFIQERQVAHFYKADPDYGERVAKAL 429
|
|
| KatE |
COG0753 |
Catalase [Inorganic ion transport and metabolism]; |
17-495 |
0e+00 |
|
Catalase [Inorganic ion transport and metabolism];
Pssm-ID: 440516 [Multi-domain] Cd Length: 489 Bit Score: 828.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 17 AQSKADVLTTGTGAPVGTKTATLTAGPRGPVLIQDFTFTDEMAHFNRERIPERVVHAKGGGAFGYFEVTHDITKYCKAKP 96
Cdd:COG0753 4 ADDEGKTLTTNQGAPVADNQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFEVTEDISKYTKAKF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 97 FEFVGKKTPVGIRFSTVGGESGSADSARDPRGFAVKFYTEDGNWDVVGNNTPIFFIRDPMLFPNFIHTQKRNPQTHLKDP 176
Cdd:COG0753 84 FQEPGKKTPVFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHAQKRDPDTNLPQH 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 177 DMFWDFISLRPETTHQVSFLFSDRGTPNGFRKMNGYGSHTFKMVNKEGKPVYCKFHFKTDQGIKNLMADQAAELSKNDPD 256
Cdd:COG0753 164 DTFWDFWSLSPESLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAEGERFWVKFHWKPKQGIHSLTWDEAQKIAGKDPD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 257 YAIRDLFNAISEGDFPSWSLFIQVMTFEEAEKFKYNPFDLTKVWPQGEYPLIPVGRMVLNRNPKNYFAEVEQIAFSPAHM 336
Cdd:COG0753 244 FHRRDLYEAIERGDFPEWELGVQVMPEEDADKFDFDPLDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAETEQAAFSPGNL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 337 IPGIEASPDKMLQGRLFSYSDTHRHRLGSNYLQLAVN---CPFNtkakNYQRDGPQCVGDNQGnAPNYFPNSFSGPQDNK 413
Cdd:COG0753 324 VPGIDFSPDKMLQGRLFSYADTQRYRLGPNFHQLPVNrpkCPVH----NYQRDGAMRYDINGG-RVNYEPNSLGGPREDP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 414 QFLESPFSITGDVQRYETGDEDNFSQVTVFWNkVLKPEERQRLVENIAGHLKNAQ-EFIQRRTVHNFTQVHPDFGGGIQK 492
Cdd:COG0753 399 GFKEPPLKVDGDKVRYRSESDDHFSQAGLLYR-SMSDEEKQHLIDNIAFELGKVEsEEIRERMVAHFYNVDPELGARVAE 477
|
...
gi 1768460843 493 LLN 495
Cdd:COG0753 478 ALG 480
|
|
| Catalase |
pfam00199 |
Catalase; |
25-408 |
0e+00 |
|
Catalase;
Pssm-ID: 459708 Cd Length: 383 Bit Score: 801.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 25 TTGTGAPVGTKTATLTAGPRGPVLIQDFTFTDEMAHFNRERIPERVVHAKGGGAFGYFEVTHDITKYCKAKPFEFVGKKT 104
Cdd:pfam00199 1 TTSNGAPVPDNQNSLTAGPRGPLLLQDFHLIEKLAHFDRERIPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSEVGKKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 105 PVGIRFSTVGGESGSADSARDPRGFAVKFYTEDGNWDVVGNNTPIFFIRDPMLFPNFIHTQKRNPQTHLKDPDMFWDFIS 184
Cdd:pfam00199 81 PVFVRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHSQKRDPQTNLPDPAMFWDFWS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 185 LRPETTHQVSFLFSDRGTPNGFRKMNGYGSHTFKMVNKEGKPVYCKFHFKTDQGIKNLMADQAAELSKNDPDYAIRDLFN 264
Cdd:pfam00199 161 LNPESLHQVTWLFSDRGIPRSYRHMNGFGVHTFKLVNADGERVYVKFHFKTDQGIKNLTWEEAQKLAGKDPDYHTRDLYE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 265 AISEGDFPSWSLFIQVMTFEEAEKFKYNPFDLTKVWPQGEYPLIPVGRMVLNRNPKNYFAEVEQIAFSPAHMIPGIEASP 344
Cdd:pfam00199 241 AIERGDYPSWTLYVQVMTEEDAEKFRFNPFDLTKVWPHKDYPLIEVGKMVLNRNPDNYFAEVEQAAFSPSNLVPGIEPSP 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1768460843 345 DKMLQGRLFSYSDTHRHRLGSNYLQLAVNCPfNTKAKNYQRDGPQCVGDNQGNAPNYFPNSFSG 408
Cdd:pfam00199 321 DPMLQGRLFSYPDTQRYRLGPNYQQLPVNRP-PCPVHNYQRDGAMRFDINQGSRPNYEPNSFGG 383
|
|
| Catalase |
smart01060 |
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ... |
29-401 |
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: 741.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 29 GAPVGTKTATLTAGPRGPVLIQDFTFTDEMAHFNRERIPERVVHAKGGGAFGYFEVTHDITKYCKAKPFEFVGKKTPVGI 108
Cdd:smart01060 2 GAPVADNQNSLTAGPRGPVLLQDFHLIEKLAHFDRERIPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQKVGKKTPVFV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 109 RFSTVGGESGSADSARDPRGFAVKFYTEDGNWDVVGNNTPIFFIRDPMLFPNFIHTQKRNPQTHLKDPDMFWDFISLRPE 188
Cdd:smart01060 82 RFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHAQKRDPRTNLPDHDMFWDFWSLNPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 189 TTHQVSFLFSDRGTPNGFRKMNGYGSHTFKMVNKEGKPVYCKFHFKTDQGIKNLMADQAAELSKNDPDYAIRDLFNAISE 268
Cdd:smart01060 162 SLHQVTWLMSDRGIPASYRHMNGFGVHTFKLVNAEGERFYVKFHFKPDQGIKNLTWEEAAKLAGKDPDYHRRDLYEAIER 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 269 GDFPSWSLFIQVMTFEEAEKFKYNPFDLTKVWPQGEYPLIPVGRMVLNRNPKNYFAEVEQIAFSPAHMIPGIEASPDKML 348
Cdd:smart01060 242 GDYPEWTLYVQVMPEEDAEKFRFDPFDLTKVWPHKDYPLIEVGKMTLNRNPDNYFAEVEQAAFSPSNLVPGIEFSPDKML 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1768460843 349 QGRLFSYSDTHRHRLGSNYLQLAVNCPFNtKAKNYQRDGPQCVGDNQGNAPNY 401
Cdd:smart01060 322 QGRLFSYPDTQRYRLGPNYHQLPVNRPRC-PVHNYQRDGAMRVDGNQGGDPNY 373
|
|
| PLN02609 |
PLN02609 |
catalase |
25-499 |
0e+00 |
|
catalase
Pssm-ID: 215328 [Multi-domain] Cd Length: 492 Bit Score: 620.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 25 TTGTGAPVGTKTATLTAGPRGPVLIQDFTFTDEMAHFNRERIPERVVHAKGGGAFGYFEVTHDITKYCKAKPFEFVGKKT 104
Cdd:PLN02609 18 TTNSGAPVWNNNSSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDISNLTCADFLRAPGVQT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 105 PVGIRFSTVGGESGSADSARDPRGFAVKFYTEDGNWDVVGNNTPIFFIRDPMLFPNFIHTQKRNPQTHLKDPDMFWDFIS 184
Cdd:PLN02609 98 PVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDMVGNNFPVFFIRDGMKFPDMVHALKPNPKTHIQEPWRILDFLS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 185 LRPETTHQVSFLFSDRGTPNGFRKMNGYGSHTFKMVNKEGKPVYCKFHFKTDQGIKNLMADQAAELSKNDPDYAIRDLFN 264
Cdd:PLN02609 178 HHPESLHMFTFLFDDRGIPQDYRHMEGFGVHTYKLINKAGKAHYVKFHWKPTCGVKNLLDEEAVRVGGSNHSHATQDLYD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 265 AISEGDFPSWSLFIQVMTFEEAEKFKYNPFDLTKVWPQGEYPLIPVGRMVLNRNPKNYFAEVEQIAFSPAHMIPGIEASP 344
Cdd:PLN02609 258 SIAAGNYPEWKLFIQTMDPEDEDKFDFDPLDVTKTWPEDILPLQPVGRLVLNRNIDNFFAENEQLAFCPAIVVPGIYYSD 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 345 DKMLQGRLFSYSDTHRHRLGSNYLQLAVNCPFNtKAKNYQRDGPQCVGDNqGNAPNYFPNSFSGPQDNKQFLESPFSITG 424
Cdd:PLN02609 338 DKLLQTRIFAYADTQRHRLGPNYLQLPVNAPKC-AHHNNHHEGFMNFMHR-DEEVNYFPSRFDPVRHAERVPIPHPPLSG 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1768460843 425 DVQRYETGDEDNFSQVTVFWnKVLKPEERQRLVENIAGHLKNAQEFIQRRT--VHNFTQVHPDFGGGIQKLLNSYKK 499
Cdd:PLN02609 416 RREKCKIEKENNFKQPGERY-RSWSPDRQERFIKRWVDALSDPRVTHEIRSiwISYWSQCDKSLGQKLASRLNVKPS 491
|
|
| |
|
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: 860.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 65 RIPERVVHAKGGGAFGYFEVTHDITKYCKAKPFEFVGKKTPVGIRFSTVGGESGSADSARDPRGFAVKFYTEDGNWDVVG 144
Cdd:cd08156 1 RIPERVVHAKGAGAFGTFEVTHDITKYTKAKIFSEVGKKTPVFVRFSTVAGERGSADTERDPRGFALKFYTEEGNWDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 145 NNTPIFFIRDPMLFPNFIHTQKRNPQTHLKDPDMFWDFISLRPETTHQVSFLFSDRGTPNGFRKMNGYGSHTFKMVNKEG 224
Cdd:cd08156 81 NNTPVFFIRDPIKFPDFIHTQKRNPQTNLKDPDMFWDFWSLSPESLHQVTILFSDRGIPDGYRHMNGYGSHTFSLVNAKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 225 KPVYCKFHFKTDQGIKNLMADQAAELSKNDPDYAIRDLFNAISEGDFPSWSLFIQVMTFEEAEKFKYNPFDLTKVWPQGE 304
Cdd:cd08156 161 ERFWVKFHFKTDQGIKNLTNEEAAELAGEDPDYAQRDLFEAIERGDFPSWTLYVQVMPEEDAEKYRFNPFDLTKVWPHKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 305 YPLIPVGRMVLNRNPKNYFAEVEQIAFSPAHMIPGIEASPDKMLQGRLFSYSDTHRHRLGSNYLQLAVNCPFnTKAKNYQ 384
Cdd:cd08156 241 YPLIEVGKLELNRNPENYFAEVEQAAFSPSNLVPGIGFSPDKMLQGRLFSYADAHRYRLGVNYHQLPVNRPK-CPVNNYQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 385 RDGPQCVGDNQGNAPNYFPNSFSGPQDNKQFLESPFSITGDVQRYETG-DEDNFSQVTVFWNKVlKPEERQRLVENIAGH 463
Cdd:cd08156 320 RDGAMRVDGNGGGAPNYEPNSFGGPPEDPEYAEPPLPVSGDADRYNYRdDDDDYTQAGDLYRLV-SEDERERLVENIAGH 398
|
410 420 430
....*....|....*....|....*....|.
gi 1768460843 464 LKNAQEFIQRRTVHNFTQVHPDFGGGIQKLL 494
Cdd:cd08156 399 LKGAPEFIQERQVAHFYKADPDYGERVAKAL 429
|
|
| KatE |
COG0753 |
Catalase [Inorganic ion transport and metabolism]; |
17-495 |
0e+00 |
|
Catalase [Inorganic ion transport and metabolism];
Pssm-ID: 440516 [Multi-domain] Cd Length: 489 Bit Score: 828.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 17 AQSKADVLTTGTGAPVGTKTATLTAGPRGPVLIQDFTFTDEMAHFNRERIPERVVHAKGGGAFGYFEVTHDITKYCKAKP 96
Cdd:COG0753 4 ADDEGKTLTTNQGAPVADNQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFEVTEDISKYTKAKF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 97 FEFVGKKTPVGIRFSTVGGESGSADSARDPRGFAVKFYTEDGNWDVVGNNTPIFFIRDPMLFPNFIHTQKRNPQTHLKDP 176
Cdd:COG0753 84 FQEPGKKTPVFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHAQKRDPDTNLPQH 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 177 DMFWDFISLRPETTHQVSFLFSDRGTPNGFRKMNGYGSHTFKMVNKEGKPVYCKFHFKTDQGIKNLMADQAAELSKNDPD 256
Cdd:COG0753 164 DTFWDFWSLSPESLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAEGERFWVKFHWKPKQGIHSLTWDEAQKIAGKDPD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 257 YAIRDLFNAISEGDFPSWSLFIQVMTFEEAEKFKYNPFDLTKVWPQGEYPLIPVGRMVLNRNPKNYFAEVEQIAFSPAHM 336
Cdd:COG0753 244 FHRRDLYEAIERGDFPEWELGVQVMPEEDADKFDFDPLDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAETEQAAFSPGNL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 337 IPGIEASPDKMLQGRLFSYSDTHRHRLGSNYLQLAVN---CPFNtkakNYQRDGPQCVGDNQGnAPNYFPNSFSGPQDNK 413
Cdd:COG0753 324 VPGIDFSPDKMLQGRLFSYADTQRYRLGPNFHQLPVNrpkCPVH----NYQRDGAMRYDINGG-RVNYEPNSLGGPREDP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 414 QFLESPFSITGDVQRYETGDEDNFSQVTVFWNkVLKPEERQRLVENIAGHLKNAQ-EFIQRRTVHNFTQVHPDFGGGIQK 492
Cdd:COG0753 399 GFKEPPLKVDGDKVRYRSESDDHFSQAGLLYR-SMSDEEKQHLIDNIAFELGKVEsEEIRERMVAHFYNVDPELGARVAE 477
|
...
gi 1768460843 493 LLN 495
Cdd:COG0753 478 ALG 480
|
|
| Catalase |
pfam00199 |
Catalase; |
25-408 |
0e+00 |
|
Catalase;
Pssm-ID: 459708 Cd Length: 383 Bit Score: 801.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 25 TTGTGAPVGTKTATLTAGPRGPVLIQDFTFTDEMAHFNRERIPERVVHAKGGGAFGYFEVTHDITKYCKAKPFEFVGKKT 104
Cdd:pfam00199 1 TTSNGAPVPDNQNSLTAGPRGPLLLQDFHLIEKLAHFDRERIPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSEVGKKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 105 PVGIRFSTVGGESGSADSARDPRGFAVKFYTEDGNWDVVGNNTPIFFIRDPMLFPNFIHTQKRNPQTHLKDPDMFWDFIS 184
Cdd:pfam00199 81 PVFVRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHSQKRDPQTNLPDPAMFWDFWS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 185 LRPETTHQVSFLFSDRGTPNGFRKMNGYGSHTFKMVNKEGKPVYCKFHFKTDQGIKNLMADQAAELSKNDPDYAIRDLFN 264
Cdd:pfam00199 161 LNPESLHQVTWLFSDRGIPRSYRHMNGFGVHTFKLVNADGERVYVKFHFKTDQGIKNLTWEEAQKLAGKDPDYHTRDLYE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 265 AISEGDFPSWSLFIQVMTFEEAEKFKYNPFDLTKVWPQGEYPLIPVGRMVLNRNPKNYFAEVEQIAFSPAHMIPGIEASP 344
Cdd:pfam00199 241 AIERGDYPSWTLYVQVMTEEDAEKFRFNPFDLTKVWPHKDYPLIEVGKMVLNRNPDNYFAEVEQAAFSPSNLVPGIEPSP 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1768460843 345 DKMLQGRLFSYSDTHRHRLGSNYLQLAVNCPfNTKAKNYQRDGPQCVGDNQGNAPNYFPNSFSG 408
Cdd:pfam00199 321 DPMLQGRLFSYPDTQRYRLGPNYQQLPVNRP-PCPVHNYQRDGAMRFDINQGSRPNYEPNSFGG 383
|
|
| Catalase |
smart01060 |
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ... |
29-401 |
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: 741.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 29 GAPVGTKTATLTAGPRGPVLIQDFTFTDEMAHFNRERIPERVVHAKGGGAFGYFEVTHDITKYCKAKPFEFVGKKTPVGI 108
Cdd:smart01060 2 GAPVADNQNSLTAGPRGPVLLQDFHLIEKLAHFDRERIPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQKVGKKTPVFV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 109 RFSTVGGESGSADSARDPRGFAVKFYTEDGNWDVVGNNTPIFFIRDPMLFPNFIHTQKRNPQTHLKDPDMFWDFISLRPE 188
Cdd:smart01060 82 RFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHAQKRDPRTNLPDHDMFWDFWSLNPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 189 TTHQVSFLFSDRGTPNGFRKMNGYGSHTFKMVNKEGKPVYCKFHFKTDQGIKNLMADQAAELSKNDPDYAIRDLFNAISE 268
Cdd:smart01060 162 SLHQVTWLMSDRGIPASYRHMNGFGVHTFKLVNAEGERFYVKFHFKPDQGIKNLTWEEAAKLAGKDPDYHRRDLYEAIER 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 269 GDFPSWSLFIQVMTFEEAEKFKYNPFDLTKVWPQGEYPLIPVGRMVLNRNPKNYFAEVEQIAFSPAHMIPGIEASPDKML 348
Cdd:smart01060 242 GDYPEWTLYVQVMPEEDAEKFRFDPFDLTKVWPHKDYPLIEVGKMTLNRNPDNYFAEVEQAAFSPSNLVPGIEFSPDKML 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1768460843 349 QGRLFSYSDTHRHRLGSNYLQLAVNCPFNtKAKNYQRDGPQCVGDNQGNAPNY 401
Cdd:smart01060 322 QGRLFSYPDTQRYRLGPNYHQLPVNRPRC-PVHNYQRDGAMRVDGNQGGDPNY 373
|
|
| 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: 676.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 50 QDFTFTDEMAHFNRERIPERVVHAKGGGAFGYFEVTHDITKYCKAKPFEFVGKKTPVGIRFSTVGGESGSADSARDPRGF 129
Cdd:cd08157 2 QDFHLIDTLAHFDRERIPERVVHAKGAGAYGEFEVTDDISDITSADMLQGVGKKTPCLVRFSTVGGEKGSADTVRDPRGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 130 AVKFYTEDGNWDVVGNNTPIFFIRDPMLFPNFIHTQKRNPQTHLKDPDMFWDFISLRPETTHQVSFLFSDRGTPNGFRKM 209
Cdd:cd08157 82 AVKFYTEEGNWDWVFNNTPVFFIRDPIKFPHFIHSQKRDPQTNLKDSTMFWDYLSQNPESIHQVMILFSDRGTPASYRSM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 210 NGYGSHTFKMVNKEGKPVYCKFHFKTDQGIKNLMADQAAELSKNDPDYAIRDLFNAISEGDFPSWSLFIQVMTFEEAEKF 289
Cdd:cd08157 162 NGYSGHTYKWVNPDGSFKYVQFHLKSDQGPKFLTGEEAARLAGSNPDYATKDLFEAIERGDYPSWTVYVQVMTPEQAEKL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 290 KYNPFDLTKVWPQGEYPLIPVGRMVLNRNPKNYFAEVEQIAFSPAHMIPGIEASPDKMLQGRLFSYSDTHRHRLGSNYLQ 369
Cdd:cd08157 242 RFNIFDLTKVWPHKDFPLRPVGKLTLNENPKNYFAEIEQAAFSPSHMVPGIEPSADPVLQARLFSYPDAHRHRLGPNYQQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 370 LAVNCPFNTKAKN-YQRDGPQCVGDNQGNAPNYfPNSFSGPQDNKQFLESPFSIT---GDVQRY--ETGDEDnFSQVTVF 443
Cdd:cd08157 322 LPVNRPKTSPVYNpYQRDGPMSVNGNYGGDPNY-VSSILPPTYFKKRVDADGHHEnwvGEVVAFltEITDED-FVQPRAL 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1768460843 444 WNKVLKPEERQRLVENIAGHLKNAQEFIQRRTVHNFTQVHPDFGGGIQK 492
Cdd:cd08157 400 WEVVGKPGQQERFVKNVAGHLSGAPPEIRKRVYEIFARVNPDLGKRIEK 448
|
|
| catalase_clade_1 |
cd08154 |
Clade 1 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
24-487 |
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: 630.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 24 LTTGTGAPVGTKTATLTAGPRGPVLIQDFTFTDEMAHFNRERIPERVVHAKGGGAFGYFEVTHDITKYCKAKPFEFVGKK 103
Cdd:cd08154 2 LTTNQGAPVGDNQNSQTVGPRGPVLLEDYHLIEKLAHFDRERIPERVVHARGAGAHGYFEAYGDISDYTRASFLQEPGKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 104 TPVGIRFSTVGGESGSADSARDPRGFAVKFYTEDGNWDVVGNNTPIFFIRDPMLFPNFIHTQKRNPQTHLKDPDMFWDFI 183
Cdd:cd08154 82 TPVFVRFSTVIHGKGSPETLRDPRGFAVKFYTEEGNWDLVGNNLPVFFIRDAIKFPDMIHALKPSPVTNIQDPNRIFDFF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 184 SLRPETTHQVSFLFSDRGTPNGFRKMNGYGSHTFKMVNKEGKPVYCKFHFKTDQGIKNLMADQAAELSKNDPDYAIRDLF 263
Cdd:cd08154 162 SHVPESTHMLTFLYSDWGTPASYRHMDGSGVHTYKWVNAEGKVVYVKYHWKPKQGVKNLTAEEAAEVQGKNFNHATQDLY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 264 NAISEGDFPSWSLFIQVMTFEEAEKFKYNPFDLTKVWPQGEYPLIPVGRMVLNRNPKNYFAEVEQIAFSPAHMIPGIEAS 343
Cdd:cd08154 242 DAIAAGNYPEWELYVQIMDPKDLDKLDFDPLDDTKIWPEDQFPLKPVGKMTLNKNPDNFFAEVEQVAFSPGNLVPGIEPS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 344 PDKMLQGRLFSYSDTHRHRLGSNYLQLAVNCPFNTKAkNYQRDGPQCVGdNQGNAPNYFPNSFSGPQDNKQFLESPFSIT 423
Cdd:cd08154 322 DDKMLQGRLFSYSDTQRYRLGPNYLQLPINAPKAAVH-NNQRDGQMNYG-HDTSDVNYEPSRLDGLPEAPKYPYSQPPLS 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1768460843 424 GDVQRYETGDEDNFSQVTVFWnKVLKPEERQRLVENIAGHLKNAQEFIQRRTVHNFTQVHPDFG 487
Cdd:cd08154 400 GTTQQAPIAKTNNFKQAGERY-RSFSEEEQENLIKNLVVDLSDVNEEIKLRMLSYFSQADPDYG 462
|
|
| PLN02609 |
PLN02609 |
catalase |
25-499 |
0e+00 |
|
catalase
Pssm-ID: 215328 [Multi-domain] Cd Length: 492 Bit Score: 620.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 25 TTGTGAPVGTKTATLTAGPRGPVLIQDFTFTDEMAHFNRERIPERVVHAKGGGAFGYFEVTHDITKYCKAKPFEFVGKKT 104
Cdd:PLN02609 18 TTNSGAPVWNNNSSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDISNLTCADFLRAPGVQT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 105 PVGIRFSTVGGESGSADSARDPRGFAVKFYTEDGNWDVVGNNTPIFFIRDPMLFPNFIHTQKRNPQTHLKDPDMFWDFIS 184
Cdd:PLN02609 98 PVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDMVGNNFPVFFIRDGMKFPDMVHALKPNPKTHIQEPWRILDFLS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 185 LRPETTHQVSFLFSDRGTPNGFRKMNGYGSHTFKMVNKEGKPVYCKFHFKTDQGIKNLMADQAAELSKNDPDYAIRDLFN 264
Cdd:PLN02609 178 HHPESLHMFTFLFDDRGIPQDYRHMEGFGVHTYKLINKAGKAHYVKFHWKPTCGVKNLLDEEAVRVGGSNHSHATQDLYD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 265 AISEGDFPSWSLFIQVMTFEEAEKFKYNPFDLTKVWPQGEYPLIPVGRMVLNRNPKNYFAEVEQIAFSPAHMIPGIEASP 344
Cdd:PLN02609 258 SIAAGNYPEWKLFIQTMDPEDEDKFDFDPLDVTKTWPEDILPLQPVGRLVLNRNIDNFFAENEQLAFCPAIVVPGIYYSD 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 345 DKMLQGRLFSYSDTHRHRLGSNYLQLAVNCPFNtKAKNYQRDGPQCVGDNqGNAPNYFPNSFSGPQDNKQFLESPFSITG 424
Cdd:PLN02609 338 DKLLQTRIFAYADTQRHRLGPNYLQLPVNAPKC-AHHNNHHEGFMNFMHR-DEEVNYFPSRFDPVRHAERVPIPHPPLSG 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1768460843 425 DVQRYETGDEDNFSQVTVFWnKVLKPEERQRLVENIAGHLKNAQEFIQRRT--VHNFTQVHPDFGGGIQKLLNSYKK 499
Cdd:PLN02609 416 RREKCKIEKENNFKQPGERY-RSWSPDRQERFIKRWVDALSDPRVTHEIRSiwISYWSQCDKSLGQKLASRLNVKPS 491
|
|
| 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: 611.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 65 RIPERVVHAKGGGAFGYFEVTHDITKYCKAKPFEFVGKKTPVGIRFSTVGGESGSADSARDPRGFAVKFYTEDGNWDVVG 144
Cdd:cd00328 1 RIPERVVHARGAGAFGYFTAYGDWSDISAAAFFSAIGKKTPVFVRFSTVVGGAGSADTVRDPHGFATKFYTEEGNFDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 145 NNTPIFFIRDPMLFPNFIHTQKRNPQTHLKDPDMFWDFISLRPETTHQVSFLFSDRGTPNGFRKMNGYGSHTFKMVNKEG 224
Cdd:cd00328 81 NNTPIFFIRDAIKFPDFIHAQKPNPQTALPDADRFWDFLSLRPESLHQVSFLFSDRGIPAAYRHMNGYGSHTFKLVNANG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 225 KPVYCKFHFKTDQGIKNLMADQAAELSKNDPDYAIRDLFNAISEGDFPSWSLFIQVMTFEEAEKFKYNPFDLTKVWPQGE 304
Cdd:cd00328 161 KVHYVKFHWKTDQGIANLVWEEAARLAGEDPDYHRQDLFEAIEAGDYPSWELYIQVMTFNDAEKFPFNPLDPTKVWPEEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 305 YPLIPVGRMVLNRNPKNYFAEVEQIAFSPAHMIPGIEASPDKMLQGRLFSYSDTHRHRLGSNYLQLAVNCPfNTKAKNYQ 384
Cdd:cd00328 241 VPLIVVGKLVLNRNPLNFFAEVEQAAFDPGHIVPGVEFSEDPLLQGRLFSYADTQLYRLGPNFQQLPVNRP-YAPVHNNQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 385 RDGPQCVGDNQgNAPNYFPNSFSG--PQDNKQFLESPFSIT---GDVQRYETGDEDNFSQVTVFWNkVLKPEERQRLVEN 459
Cdd:cd00328 320 RDGAGNMNDNT-GVPNYEPNAKDVryPAQGAPKFDRGHFSHwksGVNREASTTNDDNFTQARLFYR-SLTPGQQKRLVDA 397
|
410 420 430
....*....|....*....|....*....|....*.
gi 1768460843 460 IAGHLKNA-QEFIQRRTVHNFTQVHPDFGGGIQKLL 494
Cdd:cd00328 398 FRFELADAvSPQIQQRVLDQFAKVDAAAAKRVAKAL 433
|
|
| katE |
PRK11249 |
hydroperoxidase II; Provisional |
2-490 |
9.86e-162 |
|
hydroperoxidase II; Provisional
Pssm-ID: 236886 [Multi-domain] Cd Length: 752 Bit Score: 476.84 E-value: 9.86e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 2 ANRDKATNQLEEFKK-AQSKAdvLTTGTGAPVGTKTATLTAGPRGPVLIQDFTFTDEMAHFNRERIPERVVHAKGGGAFG 80
Cdd:PRK11249 56 DTRNEKLNSLEAFRKgSEGYA--LTTNQGVRIADDQNSLRAGSRGPSLLEDFILREKITHFDHERIPERIVHARGSAAHG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 81 YFEVTHDITKYCKAKPFEFVGKKTPVGIRFSTVGGESGSADSARDPRGFAVKFYTEDGNWDVVGNNTPIFFIRDPMLFPN 160
Cdd:PRK11249 134 YFQPYKSLSDITKAAFLQDPGKITPVFVRFSTVQGPRGSADTVRDIRGFATKFYTEEGNFDLVGNNTPVFFIQDAIKFPD 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 161 FIHTQKrnPQTHLKDP------DMFWDFISLRPETTHQVSFLFSDRGTPNGFRKMNGYGSHTFKMVNKEGKPVYCKFHFK 234
Cdd:PRK11249 214 FVHAVK--PEPHNEIPqgqsahDTFWDYVSLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLINAEGKATFVRFHWK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 235 TDQGIKNLMADQAAELSKNDPDYAIRDLFNAISEGDFPSWSLFIQVMTFEEAEKFKYNPFDLTKVWPQGEYPLIPVGRMV 314
Cdd:PRK11249 292 PVAGKASLVWDEAQKLTGRDPDFHRRDLWEAIEAGDYPEYELGVQLIPEEDEFKFDFDLLDPTKLIPEELVPVQRVGKMV 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 315 LNRNPKNYFAEVEQIAFSPAHMIPGIEASPDKMLQGRLFSYSDTHRHRLGS-NYLQLAVN---CPFNtkakNYQRDGPQC 390
Cdd:PRK11249 372 LNRNPDNFFAETEQVAFHPGHIVPGIDFTNDPLLQGRLFSYTDTQISRLGGpNFHEIPINrptCPYH----NFQRDGMHR 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 391 VGDNQGNApNYFPNSFSG---------PQDNKqFLESPFSITGDVQRYETGD-EDNFSQVTVFWNKvLKPEERQRLVENI 460
Cdd:PRK11249 448 MTIDTGPA-NYEPNSINGnwpretppaPKRGG-FESYQERVEGNKVRERSPSfGDYYSQPRLFWLS-QTPIEQRHIIDAF 524
|
490 500 510
....*....|....*....|....*....|.
gi 1768460843 461 AGHL-KNAQEFIQRRTVHNFTQVHPDFGGGI 490
Cdd:PRK11249 525 SFELgKVVRPYIRERVVDQLAHIDLTLAQAV 555
|
|
| catalase_clade_2 |
cd08155 |
Clade 2 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
64-494 |
1.80e-157 |
|
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: 455.29 E-value: 1.80e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 64 ERIPERVVHAKGGGAFGYFEVTHDITKYCKAKPFEFVGKKTPVGIRFSTVGGESGSADSARDPRGFAVKFYTEDGNWDVV 143
Cdd:cd08155 3 ERIPERVVHARGSGAHGYFQVYESLSQYTKAKFLQDPGKKTPVFVRFSTVAGSRGSADTVRDVRGFAVKFYTEEGNYDLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 144 GNNTPIFFIRDPMLFPNFIHTQKrnPQTHLKDP------DMFWDFISLRPETTHQVSFLFSDRGTPNGFRKMNGYGSHTF 217
Cdd:cd08155 83 GNNIPVFFIQDAIKFPDLIHAVK--PEPHNEMPqaqsahDTFWDFVSLQPESAHMVMWAMSDRAIPRSYRMMEGFGVHTF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 218 KMVNKEGKPVYCKFHFKTDQGIKNLMADQAAELSKNDPDYAIRDLFNAISEGDFPSWSLFIQVMTFEEAEKFKYNPFDLT 297
Cdd:cd08155 161 RLVNAQGKSTFVKFHWKPVLGVHSLVWDEAQKIAGKDPDFHRRDLWEAIESGDYPEWELGVQLIDEEDEFKFDFDILDPT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 298 KVWPQGEYPLIPVGRMVLNRNPKNYFAEVEQIAFSPAHMIPGIEASPDKMLQGRLFSYSDTHRHRLGS-NYLQLAVN--- 373
Cdd:cd08155 241 KLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFCPANVVPGIDFSNDPLLQGRLFSYLDTQLSRLGGpNFHELPINrpv 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 374 CPFNtkakNYQRDGPQCVGDNQGNApNYFPNSFSG------PQDNKQFLESPFSITGDVQRYETGD-EDNFSQVTVFWNK 446
Cdd:cd08155 321 CPVH----NNQRDGHMRMTINKGRV-NYFPNSLGAgppraaSPAEGGFVHYPEKVEGPKIRIRSESfADHYSQARLFWNS 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1768460843 447 vLKPEERQRLVENIAGHL-KNAQEFIQRRTVHNFTQVHPDFGGGIQKLL 494
Cdd:cd08155 396 -MSPVEKEHIISAFTFELsKVETPEIRERVVDHLANIDEDLAKKVAKGL 443
|
|
| catalase_like |
cd08150 |
Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found ... |
67-363 |
1.56e-66 |
|
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: 216.27 E-value: 1.56e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 67 PERVVHAKGGGAFGYFEVTHDITKYCKAKPFeFVGKKTPVGIRFSTVGGesgSADSARDPRGFAVKFYTEDGN--WDVVG 144
Cdd:cd08150 1 GLRGQHFQGTCAFGTFEVLADLKERLRVGLF-AEGKVYPAYIRFSNGAG---IDDTKPDIRGFAIKFTGVADAgtLDFVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 145 NNTPIFFIRDPMLFPNFIHTQKRNPQTHlKDPDMFWDFISLRPETTHQVSFLFSdrGTPNGFRKMNGYGSHTFKMVNKEG 224
Cdd:cd08150 77 NNTPVFFIRNTSDYEDFVAEFARSARGE-PPLDFIAWYVEKRPEDLPNLLGARS--QVPDSYAAARYFSQVTFAFINGAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 225 KPVYCKFHFKTDQGIKNLmadQAAELSKNDPDYAIRDLFNAISEGdFPSWSLFIQVMTfEEAEKFKYNPfdlTKVWPQgE 304
Cdd:cd08150 154 KYRVVRSKDNPVDGIPSL---EDHELEARPPDYLREELTERLQRG-PVVYDFRIQLND-DTDATTIDNP---TILWPT-E 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1768460843 305 YPLIPVGRMVLNRNPKNyfAEVEQIAFSPAHMIPGIEASPDK--MLQGRLFSYSDTHRHRL 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 |
2.22e-37 |
|
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: 139.29 E-value: 2.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 69 RVVHAKGGGAFGYFEVTHDITKYCKAKPFEfvGKKTPVGIRFSTVGGESGSADSARDPRGFAVKFYTEDGN-WDVVGNNT 147
Cdd:cd08153 15 RRNHAKGICVSGTFTPSGAAASLSRAPLFS--GGSVPVTGRFSLGGGNPKAPDDAANPRGMALKFRLPDGEqWRMVMNSF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 148 PIFFIRDPMLFPNFIhtQKRNPQTHLK-DPDMFWDFISLRPETTHQVSFLFSdRGTPNGFRKMNGYGSHTFKMVNKEGKP 226
Cdd:cd08153 93 PVFPVRTPEEFLALL--KAIAPDATGKpDPAKLKAFLAAHPEAAAFLAWIKT-APPPASFANTTYYGVNAFYFTNANGKR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 227 VYCKFHFKTDQGIKNLMADQAAelsKNDPDYAIRDLFNAISEGdfP-SWSLFIQVMTFEEAEKfkynpfDLTKVWPqGEY 305
Cdd:cd08153 170 QPVRWRFVPEDGVKYLSDEEAA---KLGPDFLFDELAQRLAQG--PvRWDLVLQLAEPGDPTD------DPTKPWP-ADR 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1768460843 306 PLIPVGRMVLNRNPKNYFAEVEQIAFSPAHMIPGIEASPDKMLQGRLFSYSDTHRHRL 363
Cdd:cd08153 238 KEVDAGTLTITKVAPDQGGACRDINFDPLVLPDGIEPSDDPLLAARSAAYAVSFSRRQ 295
|
|
| Catalase-rel |
pfam06628 |
Catalase-related immune-responsive; This family represents a small conserved region within ... |
434-494 |
9.87e-19 |
|
Catalase-related immune-responsive; This family represents a small conserved region within catalase enzymes (EC:1.11.1.6). All members also contain the Catalase family, pfam00199 domain. Catalase decomposes hydrogen peroxide into water and oxygen, serving to protect cells from its toxic effects. This domain carries the immune-responsive amphipathic octa-peptide that is recognized by T cells.
Pssm-ID: 461967 [Multi-domain] Cd Length: 65 Bit Score: 80.10 E-value: 9.87e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1768460843 434 EDNFSQVTVFWNkVLKPEERQRLVENIAGHLKNAQ-EFIQRRTVHNFTQVHPDFGGGIQKLL 494
Cdd:pfam06628 5 DDHFSQAGLFYR-SMSEEERQRLVDNIAFELSKVTdPEIQERMVAHFYKVDPDLGQRVAEAL 65
|
|
| y4iL_like |
cd08152 |
Catalase-like heme-binding proteins similar to the uncharacterized y4iL; Catalase is a ... |
69-338 |
1.21e-10 |
|
Catalase-like heme-binding proteins similar to the uncharacterized y4iL; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes involved in the protection of cells from the toxic effects of peroxides. It catalyses the conversion of hydrogen peroxide to water and molecular oxygen. Several other related protein families share the catalase fold and bind to heme, but do not necessarily have catalase activity. This family contains uncharacterized proteins similar to Rhizobium sp. NGR234 y4iL, of mostly bacterial origin.
Pssm-ID: 163708 Cd Length: 305 Bit Score: 62.66 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 69 RVVHAKG-GGAFGYFEVTHDITKYCK----AKPFEFvgkktPVGIRFSTVGGEsGSADSARDPRGFAVKFY--------- 134
Cdd:cd08152 5 RDAHAKShGCLKAEFTVLDDLPPELAqglfAEPGTY-----PAVIRFSNAPGD-ILDDSVPDPRGMAIKVLgvpgekllp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 135 -TEDGNWDVVGNNTPIFFIRDP-------MLF------PNFIHTQKRNPQT-HLKDPDMFWDFISLRPETTHQVSFLFSD 199
Cdd:cd08152 79 eEDATTQDFVLVNHPVFFARDAkdylallKLLarttslPDGAKAALSAPLRgALRVLEAAGGESPTLKLGGHPPAHPLGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 200 R---GTPngFRkmngYGSHtfkmvnkegkpvYCKFHFKTDQgiKNLMADQAAELSKNDPDYAIRD-LFNAISEGDFpSWS 275
Cdd:cd08152 159 TywsQAP--YR----FGDY------------VAKYSVVPAS--PALPALTGKELDLTDDPDALREaLADFLAENDA-EFE 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 276 LFIQVMTFEEA---EkfkynpfDLTKVWPQGEYPLIPVGRMVLNR----NPKNYFAEVEQIAFSPAHMIP 338
Cdd:cd08152 218 FRIQLCTDLEKmpiE-------DASVEWPEALSPFVPVATITIPPqdfdSPARQRAFDDNLSFNPWHGLA 280
|
|
| AOS |
cd08151 |
Allene oxide synthase; Allene oxide synthase converts a fatty acid hydroperoxide to an allene ... |
69-335 |
4.04e-08 |
|
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: 55.12 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 69 RVVHAKGGGAFGYFEVTHDItKYCKAKPFEfVGKKTPVGIRFSTVggeSGSADSAR-DPRGFAVKFYT----EDGNWDVV 143
Cdd:cd08151 28 RGTHTIGVGAKGVLTVLAES-DFPEHAFFT-AGKRFPVILRHANI---VGGDDDASlDGRGAALRFLNagddDAGPLDLV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 144 GNNTPIFFIRDPMLFPNFIhtqkRNPQTHLKDPDMFWDFisLRPETTHQvsflfSDRGTPNGFRKMNGYGSHTFKMVNKE 223
Cdd:cd08151 103 MNTGESFGFWTAASFADFA----GAGLPFREKAAKLRGP--LARYAVWA-----SLRRAPDSYTDLHYYSQICYEFVALD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768460843 224 GKPVYCKFHF-KTDQGIKNLMADQAAELSKNDPDYAIRDLFNAISEGDF-----------PSWSLFIQVMTFEEAEKFKY 291
Cdd:cd08151 172 GKSRYARFRLlPPDADTEWDLGEDVLETIFQRPRLYLPRLPGDTRPKDYlrnefrqrlqsPGVRYRLQIQLREVSDDATA 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1768460843 292 NPFDLTKVWPQGEYPLIPVGRMVLNRNPKNyfAEVEQIAFSPAH 335
Cdd:cd08151 252 VALDCCRPWDEDEHPWLDLAVVRLGAPLPN--DELEKLAFNPGN 293
|
|
| |
