|
Name |
Accession |
Description |
Interval |
E-value |
| katE |
PRK11249 |
hydroperoxidase II; Provisional |
8-684 |
0e+00 |
|
hydroperoxidase II; Provisional
Pssm-ID: 236886 [Multi-domain] Cd Length: 752 Bit Score: 1114.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 8 RVNEHSKDEQLEQYRADNSGKKMTTNQGLRVSEDEHSLKAGVRGPTLMEDFHFREKMTHFDHERIPERVVHARGFGVHGF 87
Cdd:PRK11249 55 PDTRNEKLNSLEAFRKGSEGYALTTNQGVRIADDQNSLRAGSRGPSLLEDFILREKITHFDHERIPERIVHARGSAAHGY 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 88 FQVYEPMTEYTRAKFLQDPSVKTPVFVRFSTVAGSKGSADTVRDARGFATKFYTEEGNYDLVGNNIPVFFIQDAIKFPDL 167
Cdd:PRK11249 135 FQPYKSLSDITKAAFLQDPGKITPVFVRFSTVQGPRGSADTVRDIRGFATKFYTEEGNFDLVGNNTPVFFIQDAIKFPDF 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 168 VHAFKPEPHNEMPQAATAHDTFWDFVANNPESAHMVMWTMSDRGIPRSYRMMEGFGVHTFRFVNEQGKARFVKFHWKPVL 247
Cdd:PRK11249 215 VHAVKPEPHNEIPQGQSAHDTFWDYVSLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLINAEGKATFVRFHWKPVA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 248 GVHSLVWDEAQKIAGKDPDFHRRDLWETIENGGKVEYELGVQMIDEEDEFKFDFDILDPTKLWPEELVPVKIIGKMTLIR 327
Cdd:PRK11249 295 GKASLVWDEAQKLTGRDPDFHRRDLWEAIEAGDYPEYELGVQLIPEEDEFKFDFDLLDPTKLIPEELVPVQRVGKMVLNR 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 328 NQDNVFAETEQIAFHPGNVVPGIDFTNDPLLQGRLFSYTDTQLIRLGGPNFHEIPINRPVCPFHNNQYDGYHRMTINKGP 407
Cdd:PRK11249 375 NPDNFFAETEQVAFHPGHIVPGIDFTNDPLLQGRLFSYTDTQISRLGGPNFHEIPINRPTCPYHNFQRDGMHRMTIDTGP 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 408 VAYHKNSLQNNDP--SPATAEEGGYVHYQEKVEGKKIRQRSDSFNDYYSQAKLFWNSMSPVEKQHIISAFCFEVGKVKSK 485
Cdd:PRK11249 455 ANYEPNSINGNWPreTPPAPKRGGFESYQERVEGNKVRERSPSFGDYYSQPRLFWLSQTPIEQRHIIDAFSFELGKVVRP 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 486 DVQRQVVDVFSNVDADLAEEIAKGVGVATPAK--RKASKEILT----SPALSQ-ARTVKTASTRKVAVLAGNGFHEKELQ 558
Cdd:PRK11249 535 YIRERVVDQLAHIDLTLAQAVAENLGIPLTDEqlNITPPPDVNglkkDPALSLyAIPDGDIKGRKVAILLNDGVDAADLL 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 559 TVLEALKQEGITVDIISQNLGYMTSGSGQQLEASGTFLTVDSVLYDAVYAAGGPE----LKDNKQAMAFIREAYNHYKAI 634
Cdd:PRK11249 615 AILKALKAKGVHAKLLYPRMGEVTADDGTVLPIAATFAGAPSLTFDAVIVPGGKAniadLADNGDARYYLLEAYKHLKPI 694
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1717936743 635 GAANEGIDLL-QSSVGTTEGPGIVTAKDEPDytAFSKAFIDAVAAHRHWDR 684
Cdd:PRK11249 695 ALAGDARKLKaALKLPDQGEEGLVEADSADG--SFMDELLTAMAAHRVWSR 743
|
|
| KatE |
COG0753 |
Catalase [Inorganic ion transport and metabolism]; |
23-520 |
0e+00 |
|
Catalase [Inorganic ion transport and metabolism];
Pssm-ID: 440516 [Multi-domain] Cd Length: 489 Bit Score: 977.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 23 ADNSGKKMTTNQGLRVSEDEHSLKAGVRGPTLMEDFHFREKMTHFDHERIPERVVHARGFGVHGFFQVYEPMTEYTRAKF 102
Cdd:COG0753 4 ADDEGKTLTTNQGAPVADNQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFEVTEDISKYTKAKF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 103 LQDPSVKTPVFVRFSTVAGSKGSADTVRDARGFATKFYTEEGNYDLVGNNIPVFFIQDAIKFPDLVHAFKPEPHNEMPQa 182
Cdd:COG0753 84 FQEPGKKTPVFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHAQKRDPDTNLPQ- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 183 ataHDTFWDFVANNPESAHMVMWTMSDRGIPRSYRMMEGFGVHTFRFVNEQGKARFVKFHWKPVLGVHSLVWDEAQKIAG 262
Cdd:COG0753 163 ---HDTFWDFWSLSPESLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAEGERFWVKFHWKPKQGIHSLTWDEAQKIAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 263 KDPDFHRRDLWETIENGGKVEYELGVQMIDEEDEFKFDFDILDPTKLWPEELVPVKIIGKMTLIRNQDNVFAETEQIAFH 342
Cdd:COG0753 240 KDPDFHRRDLYEAIERGDFPEWELGVQVMPEEDADKFDFDPLDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAETEQAAFS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 343 PGNVVPGIDFTNDPLLQGRLFSYTDTQLIRLgGPNFHEIPINRPVCPFHNNQYDGYHRMTINKGPVAYHKNSLqnNDPsp 422
Cdd:COG0753 320 PGNLVPGIDFSPDKMLQGRLFSYADTQRYRL-GPNFHQLPVNRPKCPVHNYQRDGAMRYDINGGRVNYEPNSL--GGP-- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 423 atAEEGGYVHYQEKVEGKKIRQRSDSfNDYYSQAKLFWNSMSPVEKQHIISAFCFEVGKVKSKDVQRQVVDVFSNVDADL 502
Cdd:COG0753 395 --REDPGFKEPPLKVDGDKVRYRSES-DDHFSQAGLLYRSMSDEEKQHLIDNIAFELGKVESEEIRERMVAHFYNVDPEL 471
|
490
....*....|....*...
gi 1717936743 503 AEEIAKGVGVATPAKRKA 520
Cdd:COG0753 472 GARVAEALGLDLPEAKAL 489
|
|
| catalase_clade_2 |
cd08155 |
Clade 2 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
68-510 |
0e+00 |
|
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: 967.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 68 DHERIPERVVHARGFGVHGFFQVYEPMTEYTRAKFLQDPSVKTPVFVRFSTVAGSKGSADTVRDARGFATKFYTEEGNYD 147
Cdd:cd08155 1 DHERIPERVVHARGSGAHGYFQVYESLSQYTKAKFLQDPGKKTPVFVRFSTVAGSRGSADTVRDVRGFAVKFYTEEGNYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 148 LVGNNIPVFFIQDAIKFPDLVHAFKPEPHNEMPQAATAHDTFWDFVANNPESAHMVMWTMSDRGIPRSYRMMEGFGVHTF 227
Cdd:cd08155 81 LVGNNIPVFFIQDAIKFPDLIHAVKPEPHNEMPQAQSAHDTFWDFVSLQPESAHMVMWAMSDRAIPRSYRMMEGFGVHTF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 228 RFVNEQGKARFVKFHWKPVLGVHSLVWDEAQKIAGKDPDFHRRDLWETIENGGKVEYELGVQMIDEEDEFKFDFDILDPT 307
Cdd:cd08155 161 RLVNAQGKSTFVKFHWKPVLGVHSLVWDEAQKIAGKDPDFHRRDLWEAIESGDYPEWELGVQLIDEEDEFKFDFDILDPT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 308 KLWPEELVPVKIIGKMTLIRNQDNVFAETEQIAFHPGNVVPGIDFTNDPLLQGRLFSYTDTQLIRLGGPNFHEIPINRPV 387
Cdd:cd08155 241 KLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFCPANVVPGIDFSNDPLLQGRLFSYLDTQLSRLGGPNFHELPINRPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 388 CPFHNNQYDGYHRMTINKGPVAYHKNSLQNNDPSPATAEEGGYVHYQEKVEGKKIRQRSDSFNDYYSQAKLFWNSMSPVE 467
Cdd:cd08155 321 CPVHNNQRDGHMRMTINKGRVNYFPNSLGAGPPRAASPAEGGFVHYPEKVEGPKIRIRSESFADHYSQARLFWNSMSPVE 400
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1717936743 468 KQHIISAFCFEVGKVKSKDVQRQVVDVFSNVDADLAEEIAKGV 510
Cdd:cd08155 401 KEHIISAFTFELSKVETPEIRERVVDHLANIDEDLAKKVAKGL 443
|
|
| Catalase |
pfam00199 |
Catalase; |
31-417 |
0e+00 |
|
Catalase;
Pssm-ID: 459708 Cd Length: 383 Bit Score: 763.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 31 TTNQGLRVSEDEHSLKAGVRGPTLMEDFHFREKMTHFDHERIPERVVHARGFGVHGFFQVYEPMTEYTRAKFLQDPSVKT 110
Cdd:pfam00199 1 TTSNGAPVPDNQNSLTAGPRGPLLLQDFHLIEKLAHFDRERIPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSEVGKKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 111 PVFVRFSTVAGSKGSADTVRDARGFATKFYTEEGNYDLVGNNIPVFFIQDAIKFPDLVHAFKPEPHNEMPQAatahDTFW 190
Cdd:pfam00199 81 PVFVRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHSQKRDPQTNLPDP----AMFW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 191 DFVANNPESAHMVMWTMSDRGIPRSYRMMEGFGVHTFRFVNEQGKARFVKFHWKPVLGVHSLVWDEAQKIAGKDPDFHRR 270
Cdd:pfam00199 157 DFWSLNPESLHQVTWLFSDRGIPRSYRHMNGFGVHTFKLVNADGERVYVKFHFKTDQGIKNLTWEEAQKLAGKDPDYHTR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 271 DLWETIENGGKVEYELGVQMIDEEDEFKFDFDILDPTKLWPEELVPVKIIGKMTLIRNQDNVFAETEQIAFHPGNVVPGI 350
Cdd:pfam00199 237 DLYEAIERGDYPSWTLYVQVMTEEDAEKFRFNPFDLTKVWPHKDYPLIEVGKMVLNRNPDNYFAEVEQAAFSPSNLVPGI 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717936743 351 DFTNDPLLQGRLFSYTDTQLIRLgGPNFHEIPINRPVCPFHNNQYDGYHRMTINKGP-VAYHKNSLQN 417
Cdd:pfam00199 317 EPSPDPMLQGRLFSYPDTQRYRL-GPNYQQLPVNRPPCPVHNYQRDGAMRFDINQGSrPNYEPNSFGG 383
|
|
| Catalase |
smart01060 |
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ... |
34-410 |
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: 738.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 34 QGLRVSEDEHSLKAGVRGPTLMEDFHFREKMTHFDHERIPERVVHARGFGVHGFFQVYEPMTEYTRAKFLQDPSVKTPVF 113
Cdd:smart01060 1 QGAPVADNQNSLTAGPRGPVLLQDFHLIEKLAHFDRERIPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQKVGKKTPVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 114 VRFSTVAGSKGSADTVRDARGFATKFYTEEGNYDLVGNNIPVFFIQDAIKFPDLVHAFKPEPHNEMPQaataHDTFWDFV 193
Cdd:smart01060 81 VRFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHAQKRDPRTNLPD----HDMFWDFW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 194 ANNPESAHMVMWTMSDRGIPRSYRMMEGFGVHTFRFVNEQGKARFVKFHWKPVLGVHSLVWDEAQKIAGKDPDFHRRDLW 273
Cdd:smart01060 157 SLNPESLHQVTWLMSDRGIPASYRHMNGFGVHTFKLVNAEGERFYVKFHFKPDQGIKNLTWEEAAKLAGKDPDYHRRDLY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 274 ETIENGGKVEYELGVQMIDEEDEFKFDFDILDPTKLWPEELVPVKIIGKMTLIRNQDNVFAETEQIAFHPGNVVPGIDFT 353
Cdd:smart01060 237 EAIERGDYPEWTLYVQVMPEEDAEKFRFDPFDLTKVWPHKDYPLIEVGKMTLNRNPDNYFAEVEQAAFSPSNLVPGIEFS 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1717936743 354 NDPLLQGRLFSYTDTQLIRLgGPNFHEIPINRPVCPFHNNQYDGYHRMTINKGPVAY 410
Cdd:smart01060 317 PDKMLQGRLFSYPDTQRYRL-GPNYHQLPVNRPRCPVHNYQRDGAMRVDGNQGGDPN 372
|
|
| catalase |
cd00328 |
Catalase heme-binding enzyme; Catalase is a ubiquitous enzyme found in both prokaryotes and ... |
71-510 |
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: 619.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 71 RIPERVVHARGFGVHGFFQVYEPMTEYTRAKFLQDPSVKTPVFVRFSTVAGSKGSADTVRDARGFATKFYTEEGNYDLVG 150
Cdd:cd00328 1 RIPERVVHARGAGAFGYFTAYGDWSDISAAAFFSAIGKKTPVFVRFSTVVGGAGSADTVRDPHGFATKFYTEEGNFDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 151 NNIPVFFIQDAIKFPDLVHAFKPEPHNEMPQaataHDTFWDFVANNPESAHMVMWTMSDRGIPRSYRMMEGFGVHTFRFV 230
Cdd:cd00328 81 NNTPIFFIRDAIKFPDFIHAQKPNPQTALPD----ADRFWDFLSLRPESLHQVSFLFSDRGIPAAYRHMNGYGSHTFKLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 231 NEQGKARFVKFHWKPVLGVHSLVWDEAQKIAGKDPDFHRRDLWETIENGGKVEYELGVQMIDEEDEFKFDFDILDPTKLW 310
Cdd:cd00328 157 NANGKVHYVKFHWKTDQGIANLVWEEAARLAGEDPDYHRQDLFEAIEAGDYPSWELYIQVMTFNDAEKFPFNPLDPTKVW 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 311 PEELVPVKIIGKMTLIRNQDNVFAETEQIAFHPGNVVPGIDFTNDPLLQGRLFSYTDTQLIRLgGPNFHEIPINRPVCPF 390
Cdd:cd00328 237 PEELVPLIVVGKLVLNRNPLNFFAEVEQAAFDPGHIVPGVEFSEDPLLQGRLFSYADTQLYRL-GPNFQQLPVNRPYAPV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 391 HNNQYDGYHRMTINKGPVAYHKNSLqnNDPSPATAEEGGYVHYQEKVEGKKIRQRSDSFNDYYSQAKLFWNSMSPVEKQH 470
Cdd:cd00328 316 HNNQRDGAGNMNDNTGVPNYEPNAK--DVRYPAQGAPKFDRGHFSHWKSGVNREASTTNDDNFTQARLFYRSLTPGQQKR 393
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1717936743 471 IISAFCFEVGKVKSKDVQRQVVDVFSNVDADLAEEIAKGV 510
Cdd:cd00328 394 LVDAFRFELADAVSPQIQQRVLDQFAKVDAAAAKRVAKAL 433
|
|
| catalase_clade_1 |
cd08154 |
Clade 1 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
30-510 |
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: 617.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 30 MTTNQGLRVSEDEHSLKAGVRGPTLMEDFHFREKMTHFDHERIPERVVHARGFGVHGFFQVYEPMTEYTRAKFLQDPSVK 109
Cdd:cd08154 2 LTTNQGAPVGDNQNSQTVGPRGPVLLEDYHLIEKLAHFDRERIPERVVHARGAGAHGYFEAYGDISDYTRASFLQEPGKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 110 TPVFVRFSTVAGSKGSADTVRDARGFATKFYTEEGNYDLVGNNIPVFFIQDAIKFPDLVHAFKPEPHNEMPQAatahDTF 189
Cdd:cd08154 82 TPVFVRFSTVIHGKGSPETLRDPRGFAVKFYTEEGNWDLVGNNLPVFFIRDAIKFPDMIHALKPSPVTNIQDP----NRI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 190 WDFVANNPESAHMVMWTMSDRGIPRSYRMMEGFGVHTFRFVNEQGKARFVKFHWKPVLGVHSLVWDEAQKIAGKDPDFHR 269
Cdd:cd08154 158 FDFFSHVPESTHMLTFLYSDWGTPASYRHMDGSGVHTYKWVNAEGKVVYVKYHWKPKQGVKNLTAEEAAEVQGKNFNHAT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 270 RDLWETIENGGKVEYELGVQMIDEEDEFKFDFDILDPTKLWPEELVPVKIIGKMTLIRNQDNVFAETEQIAFHPGNVVPG 349
Cdd:cd08154 238 QDLYDAIAAGNYPEWELYVQIMDPKDLDKLDFDPLDDTKIWPEDQFPLKPVGKMTLNKNPDNFFAEVEQVAFSPGNLVPG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 350 IDFTNDPLLQGRLFSYTDTQLIRLgGPNFHEIPINRPVCPFHNNQYDGYHRMTINKGPVAYHKNSLqnndpsPATAEEGG 429
Cdd:cd08154 318 IEPSDDKMLQGRLFSYSDTQRYRL-GPNYLQLPINAPKAAVHNNQRDGQMNYGHDTSDVNYEPSRL------DGLPEAPK 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 430 YVHYQEKVEGKKIRQRSDSFNDyYSQAKLFWNSMSPVEKQHIISAFcfevgKVKSKDVQRQVVDV----FSNVDADLAEE 505
Cdd:cd08154 391 YPYSQPPLSGTTQQAPIAKTNN-FKQAGERYRSFSEEEQENLIKNL-----VVDLSDVNEEIKLRmlsyFSQADPDYGER 464
|
....*
gi 1717936743 506 IAKGV 510
Cdd:cd08154 465 VAEGL 469
|
|
| PLN02609 |
PLN02609 |
catalase |
19-512 |
0e+00 |
|
catalase
Pssm-ID: 215328 [Multi-domain] Cd Length: 492 Bit Score: 534.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 19 EQYRADNSG--KKMTTNQGLRVSEDEHSLKAGVRGPTLMEDFHFREKMTHFDHERIPERVVHARGFGVHGFFQVYEPMTE 96
Cdd:PLN02609 4 YKYRPSSAYnsPFFTTNSGAPVWNNNSSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDISN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 97 YTRAKFLQDPSVKTPVFVRFSTVAGSKGSADTVRDARGFATKFYTEEGNYDLVGNNIPVFFIQDAIKFPDLVHAFKPEPH 176
Cdd:PLN02609 84 LTCADFLRAPGVQTPVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDMVGNNFPVFFIRDGMKFPDMVHALKPNPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 177 NEMPQAatahDTFWDFVANNPESAHMVMWTMSDRGIPRSYRMMEGFGVHTFRFVNEQGKARFVKFHWKPVLGVHSLVWDE 256
Cdd:PLN02609 164 THIQEP----WRILDFLSHHPESLHMFTFLFDDRGIPQDYRHMEGFGVHTYKLINKAGKAHYVKFHWKPTCGVKNLLDEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 257 AQKIAGKDPDFHRRDLWETIENGGKVEYELGVQMIDEEDEFKFDFDILDPTKLWPEELVPVKIIGKMTLIRNQDNVFAET 336
Cdd:PLN02609 240 AVRVGGSNHSHATQDLYDSIAAGNYPEWKLFIQTMDPEDEDKFDFDPLDVTKTWPEDILPLQPVGRLVLNRNIDNFFAEN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 337 EQIAFHPGNVVPGIDFTNDPLLQGRLFSYTDTQLIRLgGPNFHEIPINRPVCPFHNNQYDGYHRMTINKGPVAYHKNS-- 414
Cdd:PLN02609 320 EQLAFCPAIVVPGIYYSDDKLLQTRIFAYADTQRHRL-GPNYLQLPVNAPKCAHHNNHHEGFMNFMHRDEEVNYFPSRfd 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 415 -LQNNDPSPATAeeggyVHYQEKVEGKKIRQRSDsfndyYSQAKLFWNSMSPVEKQHIISAFCFEVGKVKSKDVQRQV-V 492
Cdd:PLN02609 399 pVRHAERVPIPH-----PPLSGRREKCKIEKENN-----FKQPGERYRSWSPDRQERFIKRWVDALSDPRVTHEIRSIwI 468
|
490 500
....*....|....*....|
gi 1717936743 493 DVFSNVDADLAEEIAKGVGV 512
Cdd:PLN02609 469 SYWSQCDKSLGQKLASRLNV 488
|
|
| catalase_clade_3 |
cd08156 |
Clade 3 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
71-510 |
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: 527.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 71 RIPERVVHARGFGVHGFFQVYEPMTEYTRAKFLQDPSVKTPVFVRFSTVAGSKGSADTVRDARGFATKFYTEEGNYDLVG 150
Cdd:cd08156 1 RIPERVVHAKGAGAFGTFEVTHDITKYTKAKIFSEVGKKTPVFVRFSTVAGERGSADTERDPRGFALKFYTEEGNWDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 151 NNIPVFFIQDAIKFPDLVHAFKPEPHNEMPQaataHDTFWDFVANNPESAHMVMWTMSDRGIPRSYRMMEGFGVHTFRFV 230
Cdd:cd08156 81 NNTPVFFIRDPIKFPDFIHTQKRNPQTNLKD----PDMFWDFWSLSPESLHQVTILFSDRGIPDGYRHMNGYGSHTFSLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 231 NEQGKARFVKFHWKPVLGVHSLVWDEAQKIAGKDPDFHRRDLWETIENGGKVEYELGVQMIDEEDEFKFDFDILDPTKLW 310
Cdd:cd08156 157 NAKGERFWVKFHFKTDQGIKNLTNEEAAELAGEDPDYAQRDLFEAIERGDFPSWTLYVQVMPEEDAEKYRFNPFDLTKVW 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 311 PEELVPVKIIGKMTLIRNQDNVFAETEQIAFHPGNVVPGIDFTNDPLLQGRLFSYTDTQLIRLgGPNFHEIPINRPVCPF 390
Cdd:cd08156 237 PHKDYPLIEVGKLELNRNPENYFAEVEQAAFSPSNLVPGIGFSPDKMLQGRLFSYADAHRYRL-GVNYHQLPVNRPKCPV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 391 HNNQYDGYHRMTINKGPVA-YHKNSLQNNDPSPATAEEGgyvhyqEKVEGKKIRQRSDSFNDYYSQAKLFWNSMSPVEKQ 469
Cdd:cd08156 316 NNYQRDGAMRVDGNGGGAPnYEPNSFGGPPEDPEYAEPP------LPVSGDADRYNYRDDDDDYTQAGDLYRLVSEDERE 389
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1717936743 470 HIISAFCFEVGKVKsKDVQRQVVDVFSNVDADLAEEIAKGV 510
Cdd:cd08156 390 RLVENIAGHLKGAP-EFIQERQVAHFYKADPDYGERVAKAL 429
|
|
| catalase_fungal |
cd08157 |
Fungal catalases similar to yeast catalases A and T; Catalase is a ubiquitous enzyme found in ... |
55-511 |
4.43e-165 |
|
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: 481.46 E-value: 4.43e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 55 MEDFHFREKMTHFDHERIPERVVHARGFGVHGFFQVYEPMTEYTRAKFLQDPSVKTPVFVRFSTVAGSKGSADTVRDARG 134
Cdd:cd08157 1 LQDFHLIDTLAHFDRERIPERVVHAKGAGAYGEFEVTDDISDITSADMLQGVGKKTPCLVRFSTVGGEKGSADTVRDPRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 135 FATKFYTEEGNYDLVGNNIPVFFIQDAIKFPDLVHAFKPEPHNEMPQAatahDTFWDFVANNPESAHMVMWTMSDRGIPR 214
Cdd:cd08157 81 FAVKFYTEEGNWDWVFNNTPVFFIRDPIKFPHFIHSQKRDPQTNLKDS----TMFWDYLSQNPESIHQVMILFSDRGTPA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 215 SYRMMEGFGVHTFRFVNEQGKARFVKFHWKPVLGVHSLVWDEAQKIAGKDPDFHRRDLWETIENGGKVEYELGVQMIDEE 294
Cdd:cd08157 157 SYRSMNGYSGHTYKWVNPDGSFKYVQFHLKSDQGPKFLTGEEAARLAGSNPDYATKDLFEAIERGDYPSWTVYVQVMTPE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 295 DEFKFDFDILDPTKLWPEELVPVKIIGKMTLIRNQDNVFAETEQIAFHPGNVVPGIDFTNDPLLQGRLFSYTDTQLIRLg 374
Cdd:cd08157 237 QAEKLRFNIFDLTKVWPHKDFPLRPVGKLTLNENPKNYFAEIEQAAFSPSHMVPGIEPSADPVLQARLFSYPDAHRHRL- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 375 GPNFHEIPINRPV-CPFHN-NQYDGYHRMTINKGPVAYHKNSLQNNDPSPATAEEGGyvHYQEKVEGKKIRQRSDSFNDY 452
Cdd:cd08157 316 GPNYQQLPVNRPKtSPVYNpYQRDGPMSVNGNYGGDPNYVSSILPPTYFKKRVDADG--HHENWVGEVVAFLTEITDEDF 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 453 YsQAKLFW-NSMSPVEKQHIISAFCFEVGKVkSKDVQRQVVDVFSNVDADLAEEIAKGVG 511
Cdd:cd08157 394 V-QPRALWeVVGKPGQQERFVKNVAGHLSGA-PPEIRKRVYEIFARVNPDLGKRIEKATE 451
|
|
| catalase_like |
cd08150 |
Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found ... |
73-373 |
1.50e-98 |
|
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: 304.10 E-value: 1.50e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 73 PERVVHARGFGVHGFFQVYEPMTEYTRAKFLQDPSVkTPVFVRFSTVagsKGSADTVRDARGFATKFYTE--EGNYDLVG 150
Cdd:cd08150 1 GLRGQHFQGTCAFGTFEVLADLKERLRVGLFAEGKV-YPAYIRFSNG---AGIDDTKPDIRGFAIKFTGVadAGTLDFVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 151 NNIPVFFIQDAIKFPDLVHAFKPEPHNEMPqaataHDTFWDFVANNPESAHMVMWTMSdrGIPRSYRMMEGFGVHTFRFV 230
Cdd:cd08150 77 NNTPVFFIRNTSDYEDFVAEFARSARGEPP-----LDFIAWYVEKRPEDLPNLLGARS--QVPDSYAAARYFSQVTFAFI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 231 NEQGKARFVKFHWKPVLGVHSLVWDEAQkiaGKDPDFHRRDLWETIENgGKVEYELGVQMIDEEDefkfDFDILDPTKLW 310
Cdd:cd08150 150 NGAGKYRVVRSKDNPVDGIPSLEDHELE---ARPPDYLREELTERLQR-GPVVYDFRIQLNDDTD----ATTIDNPTILW 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717936743 311 PEElVPVKIIGKMTLIRNQDNvfAETEQIAFHPGNVVPGIDFTND--PLLQGRLFSYTDTQLIRL 373
Cdd:cd08150 222 PTE-HPVEAVAKITIPPPTFT--AAQEAFAFNPFTPWHGLLETNDlgPILEVRRRVYTSSQGLRH 283
|
|
| GATase1_catalase |
cd03132 |
Type 1 glutamine amidotransferase (GATase1)-like domain found in at the C-terminal of several ... |
541-680 |
4.36e-48 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain found in at the C-terminal of several large catalases; Type 1 glutamine amidotransferase (GATase1)-like domain found in at the C-terminal of several large catalases. Catalase catalyzes the dismutation of hydrogen peroxide (H2O2) to water and oxygen. This group includes the large catalases: Neurospora crassa Catalase-1 and Catalase-3 and, Escherichia coli HP-II. This GATase1-like domain has an essential role in HP-II catalase activity. However, it lacks enzymatic activity and the catalytic triad typical of GATase1 domains. Catalase-1 and -3 are homotetrameric, HP-II is homohexameric. It has been proposed that this domain may facilitate the folding and oligomerization process. The interface between this GATase1-like domain of HP-II and the core of the subunit forms part of a channel which provides access to the deeply buried catalase active sites of HPII. Catalase-1 is associated with non-growing cells; Catalase-3 is associated with growing conditions. HP-II is produced in stationary phase. Catalase-1 is induced by ethanol and heat shock. Catalase-3 is induced under stress conditions such a hydrogen peroxide, paraquat, cadmium, heat shock, uric acid and nitrate treatment.
Pssm-ID: 153226 Cd Length: 142 Bit Score: 165.51 E-value: 4.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 541 TRKVAVLAGNGFHEKELQTVLEALKQEGITVDIISQNLGYMTSGSGQQLEASGTFLTVDSVLYDAVYAAGGPE----LKD 616
Cdd:cd03132 1 GRKVGILVADGVDAAELSALKAALKAAGANVKVVAPTLGGVVDSDGKTLEVDQTYAGAPSVLFDAVVVPGGAEaafaLAP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717936743 617 NKQAMAFIREAYNHYKAIGAANEGIDLLQSSVGTTEGPGIVTAKDEPDytAFSKAFIDAVAAHR 680
Cdd:cd03132 81 SGRALHFVTEAFKHGKPIGAVGEGSDLLEAAGIPLEDPGVVTADDVKD--VFTDRFIDALALHR 142
|
|
| srpA_like |
cd08153 |
Catalase-like heme-binding proteins similar to the uncharacterized srpA; Catalase is a ... |
75-361 |
1.76e-41 |
|
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: 152.77 E-value: 1.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 75 RVVHARGFGVHGFFQVYEPMTEYTRAKFLQDPSVktPVFVRFSTVAGSKGSADTVRDARGFATKFYTEEGN-YDLVGNNI 153
Cdd:cd08153 15 RRNHAKGICVSGTFTPSGAAASLSRAPLFSGGSV--PVTGRFSLGGGNPKAPDDAANPRGMALKFRLPDGEqWRMVMNSF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 154 PVFFIQDAIKFPDLVHAFKPE----PHnemPQAATAhdtfwdFVANNPESAHMVMWTMSdRGIPRSYRMMEGFGVHTFRF 229
Cdd:cd08153 93 PVFPVRTPEEFLALLKAIAPDatgkPD---PAKLKA------FLAAHPEAAAFLAWIKT-APPPASFANTTYYGVNAFYF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 230 VNEQGKARFVKFHWKPVLGVHSLVWDEAQKiagKDPDFHRRDLWETIENgGKVEYELGVQMIDEEDefkfdfDILDPTKL 309
Cdd:cd08153 163 TNANGKRQPVRWRFVPEDGVKYLSDEEAAK---LGPDFLFDELAQRLAQ-GPVRWDLVLQLAEPGD------PTDDPTKP 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1717936743 310 WPEELvpvKII--GKMTLIRNQDNVFAETEQIAFHPGNVVPGIDFTNDPLLQGR 361
Cdd:cd08153 233 WPADR---KEVdaGTLTITKVAPDQGGACRDINFDPLVLPDGIEPSDDPLLAAR 283
|
|
| Catalase-rel |
pfam06628 |
Catalase-related immune-responsive; This family represents a small conserved region within ... |
446-510 |
5.11e-26 |
|
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: 101.29 E-value: 5.11e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717936743 446 SDSFNDYYSQAKLFWNSMSPVEKQHIISAFCFEVGKVKSKDVQRQVVDVFSNVDADLAEEIAKGV 510
Cdd:pfam06628 1 SIDFDDHFSQAGLFYRSMSEEERQRLVDNIAFELSKVTDPEIQERMVAHFYKVDPDLGQRVAEAL 65
|
|
| Catalase_C |
pfam18011 |
C-terminal domain found in long catalases; This domain is found at the C-terminus of a variety ... |
541-684 |
7.47e-23 |
|
C-terminal domain found in long catalases; This domain is found at the C-terminus of a variety of large catalase enzymes from bacteria. Structurally it is related to class I glutamine amidotransferase domains. The precise molecular function of this domain is uncertain.
Pssm-ID: 436209 Cd Length: 150 Bit Score: 95.03 E-value: 7.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 541 TRKVAVLAGNGFHE--KELQTVLEALKQEGITVDIIsqnlgymtsGSGQQLEASGTFLTVDSVLYDAVY-AAGGPELKDN 617
Cdd:pfam18011 2 GLTVGILASNDSDAslAQAKALAAALAAAGVDVLVV---------AETLADGVNRTYSTADATLFDAIVvADGAEGLFSA 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717936743 618 KQAMA-----------FIREAYNHYKAIGAANEGIDLLQSSVGTTEGPGIVTAKDEPDytAFSKAFIDAVAAHRHWDR 684
Cdd:pfam18011 73 KATAAsslypagrplqILLDAYRHGKPIGALGSGSSALSGAGISAEGPGVYVGDSADD--ALVEDVEEGLATFRFWDR 148
|
|
| YajL |
COG0693 |
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ... |
541-636 |
4.86e-13 |
|
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins and nucleic acids) [Defense mechanisms];
Pssm-ID: 440457 [Multi-domain] Cd Length: 170 Bit Score: 67.44 E-value: 4.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 541 TRKVAVLAGNGFHEKELQTVLEALKQEGITVDIISQNLG-YMTSGSGQQLEASGTFLTVDSVLYDAVYAAGGPE----LK 615
Cdd:COG0693 2 MKKVLILLTDGFEDEELTVPYDALREAGAEVDVASPEGGpPVTSKHGITVTADKTLDDVDPDDYDALVLPGGHGapddLR 81
|
90 100
....*....|....*....|.
gi 1717936743 616 DNKQAMAFIREAYNHYKAIGA 636
Cdd:COG0693 82 EDPDVVALVREFYEAGKPVAA 102
|
|
| y4iL_like |
cd08152 |
Catalase-like heme-binding proteins similar to the uncharacterized y4iL; Catalase is a ... |
75-341 |
1.29e-11 |
|
Catalase-like heme-binding proteins similar to the uncharacterized y4iL; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes involved in the protection of cells from the toxic effects of peroxides. It catalyses the conversion of hydrogen peroxide to water and molecular oxygen. Several other related protein families share the catalase fold and bind to heme, but do not necessarily have catalase activity. This family contains uncharacterized proteins similar to Rhizobium sp. NGR234 y4iL, of mostly bacterial origin.
Pssm-ID: 163708 Cd Length: 305 Bit Score: 66.13 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 75 RVVHARGFG-VHGFFQVYEPMTEYTRAKFLQDPsvKT-PVFVRFSTVAGsKGSADTVRDARGFATKFY----------TE 142
Cdd:cd08152 5 RDAHAKSHGcLKAEFTVLDDLPPELAQGLFAEP--GTyPAVIRFSNAPG-DILDDSVPDPRGMAIKVLgvpgekllpeED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 143 EGNYDLVGNNIPVFFIQDAIKF-------------PDLVHAFKPEP---HNEMPQAATAHDTFWDFVANNPES-AHMVMW 205
Cdd:cd08152 82 ATTQDFVLVNHPVFFARDAKDYlallkllarttslPDGAKAALSAPlrgALRVLEAAGGESPTLKLGGHPPAHpLGETYW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 206 TMSdrgiprSYRmmegFGVHtfrfvneqgkarFVKFHWKPVlGVHSLVWDEAQKIAGKDPDFHRRDLWETIeNGGKVEYE 285
Cdd:cd08152 162 SQA------PYR----FGDY------------VAKYSVVPA-SPALPALTGKELDLTDDPDALREALADFL-AENDAEFE 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1717936743 286 LGVQMIDEEDEFKfdfdILDPTKLWPEELVPVKIIGKMTLIRnQDnVFAETEQIAF 341
Cdd:cd08152 218 FRIQLCTDLEKMP----IEDASVEWPEALSPFVPVATITIPP-QD-FDSPARQRAF 267
|
|
| GATase1_PfpI_like |
cd03134 |
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ... |
543-636 |
3.72e-09 |
|
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus; A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus. This group includes proteins similar to PfpI from P. furiosus. and PH1704 from Pyrococcus horikoshii. These enzymes are ATP-independent intracellular proteases and may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For PH1704, it is believed that this Cys together with a different His in one monomer and Glu (from an adjacent monomer) forms a different catalytic triad from the typical GATase1domain. PfpI is homooligomeric. Protease activity is only found for oligomeric forms of PH1704.
Pssm-ID: 153228 [Multi-domain] Cd Length: 165 Bit Score: 56.40 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 543 KVAVLAGNGFHEKELQTVLEALKQEGITVDIISQNLGYMTSG--SGQQLEASGTFLTVDSVLYDAVYAAGG--PE-LKDN 617
Cdd:cd03134 1 KVAILAADGFEDVELTYPLYRLREAGAEVVVAGPEAGGEIQGkhGYDTVTVDLTIADVDADDYDALVIPGGtnPDkLRRD 80
|
90
....*....|....*....
gi 1717936743 618 KQAMAFIREAYNHYKAIGA 636
Cdd:cd03134 81 PDAVAFVRAFAEAGKPVAA 99
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
544-636 |
1.56e-08 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153210 [Multi-domain] Cd Length: 115 Bit Score: 52.99 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 544 VAVLAGNGFHEKELQTVLEALKQEGITVDIISQNLGYMTSGsgqqleasgtfltVDSVLYDAVYAAGGP----ELKDNKQ 619
Cdd:cd01653 1 VAVLLFPGFEELELASPLDALREAGAEVDVVSPDGGPVESD-------------VDLDDYDGLILPGGPgtpdDLARDEA 67
|
90
....*....|....*..
gi 1717936743 620 AMAFIREAYNHYKAIGA 636
Cdd:cd01653 68 LLALLREAAAAGKPILG 84
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
544-636 |
6.97e-08 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.
Pssm-ID: 153222 [Multi-domain] Cd Length: 92 Bit Score: 50.66 E-value: 6.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 544 VAVLAGNGFHEKELQTVLEALKQEGITVDIISQNLGYMTSGsgqqleasgtfltVDSVLYDAVYAAGGP----ELKDNKQ 619
Cdd:cd03128 1 VAVLLFGGSEELELASPLDALREAGAEVDVVSPDGGPVESD-------------VDLDDYDGLILPGGPgtpdDLAWDEA 67
|
90
....*....|....*..
gi 1717936743 620 AMAFIREAYNHYKAIGA 636
Cdd:cd03128 68 LLALLREAAAAGKPVLG 84
|
|
| AOS |
cd08151 |
Allene oxide synthase; Allene oxide synthase converts a fatty acid hydroperoxide to an allene ... |
75-345 |
1.28e-07 |
|
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: 53.97 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 75 RVVHARGFGVHGFFQVYEPMtEYTRAKFLQdPSVKTPVFVRFSTVAGSKGsaDTVRDARGFATKFYT----EEGNYDLVG 150
Cdd:cd08151 28 RGTHTIGVGAKGVLTVLAES-DFPEHAFFT-AGKRFPVILRHANIVGGDD--DASLDGRGAALRFLNagddDAGPLDLVM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 151 NNIPVFFIQDAIKFPDLvhafkpephneMPQAATAHDTFWDFvannpesAHMVMWTMSDRGIPR---SYRMMEGFGVHTF 227
Cdd:cd08151 104 NTGESFGFWTAASFADF-----------AGAGLPFREKAAKL-------RGPLARYAVWASLRRapdSYTDLHYYSQICY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 228 RFVNEQGKARFVKFHWKPvlGVHSLVWDEAQ---------------KIAGKD--PDFHRRDLWETIENGGkVEYELGVQM 290
Cdd:cd08151 166 EFVALDGKSRYARFRLLP--PDADTEWDLGEdvletifqrprlylpRLPGDTrpKDYLRNEFRQRLQSPG-VRYRLQIQL 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1717936743 291 IDEEDEFKFDfdILDPTKLWPEELVPVKIIGKMTLIRNQDNvfAETEQIAFHPGN 345
Cdd:cd08151 243 REVSDDATAV--ALDCCRPWDEDEHPWLDLAVVRLGAPLPN--DELEKLAFNPGN 293
|
|
| DJ-1_PfpI |
pfam01965 |
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ... |
542-636 |
2.63e-07 |
|
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in transcriptional regulators.
Pssm-ID: 396514 [Multi-domain] Cd Length: 165 Bit Score: 50.72 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 542 RKVAVLAGNGFHEKELQTVLEALKQEGITVDIISQNLGYMTSGSGQQLEASGTFLTVDSVLYDAVYAAGG---PE-LKDN 617
Cdd:pfam01965 1 KKVLVLLADGFEDIELIYPADVLRRAGIKVTVVSVDGGEVKGSRGVKVTVDASLDDVKPDDYDALVLPGGragPErLRDN 80
|
90
....*....|....*....
gi 1717936743 618 KQAMAFIREAYNHYKAIGA 636
Cdd:pfam01965 81 EKLVEFVKDFYEKGKPVAA 99
|
|
| GATase1_DJ-1 |
cd03135 |
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ... |
544-637 |
2.45e-05 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1. DJ-1 is involved in multiple physiological processes including cancer, Parkinson's disease and male fertility. It is unclear how DJ-1 functions in these. DJ-1 has been shown to possess chaperone activity. DJ-1 is preferentially expressed in the testis and moderately in other tissues; it is induced together with genes involved in oxidative stress response. The Drosophila homologue (DJ-1A) plays an essential role in oxidative stress response and neuronal maintenance. Inhibition of DJ-1A function through RNAi, results in the cellular accumulation of reactive oxygen species, organismal hypersensitivity to oxidative stress, and dysfunction and degeneration of dopaminergic and photoreceptor neurons. DJ-1 has lacks enzymatic activity and the catalytic triad of typical GATase1 domains, however it does contain the highly conserved cysteine located at the nucelophile elbow region typical of these domains. This cysteine been proposed to be a site of regulation of DJ-1 activity by oxidation. DJ-1 is a dimeric enzyme.
Pssm-ID: 153229 [Multi-domain] Cd Length: 163 Bit Score: 45.24 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 544 VAVLAGNGFHEKELQTVLEALKQEGITVDIIS-QNLGYMTSGSGQQLEASGTFLTVDSVLYDAVYAAGGP----ELKDNK 618
Cdd:cd03135 1 VLVILADGFEEIEAVTPVDVLRRAGIEVTTASlEKKLAVGSSHGIKVKADKTLSDVNLDDYDAIVIPGGLpgaqNLADNE 80
|
90 100
....*....|....*....|..
gi 1717936743 619 QAMAFIREAYNHYK---AIGAA 637
Cdd:cd03135 81 KLIKLLKEFNAKGKliaAICAA 102
|
|
| GATase1_Hsp31_like |
cd03141 |
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ... |
551-636 |
1.90e-03 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Escherichia coli Hsp31 protein; Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Escherichia coli Hsp31 protein (EcHsp31). This group includes EcHsp31 and Saccharomyces cerevisiae Ydr533c protein. EcHsp31 has chaperone activity. Ydr533c is upregulated in response to various stress conditions along with the heat shock family. EcHsp31 coordinates a metal ion using a 2-His-1-carboxylate motif present in various ions that use iron as a cofactor such as Carboxypeptidase A. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with a typical GATase1 domain, a reactive Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For EcHsp31, this Cys together with a different His and, an Asp (rather than a Glu) residue form a different catalytic triad from the typical GATase1 domain. For Ydr533c a catalytic triad forms from the conserved Cys together with a different His and Glu from that of the typical GATase1domain. Ydr533c protein and EcHsp31 are homodimers.
Pssm-ID: 153235 [Multi-domain] Cd Length: 221 Bit Score: 40.23 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936743 551 GFHEKELQTVLEALKQEGITVDIISQNLGYMT-----------------SGSGQQLEASGTFLTVDSVL---YDAVYAAG 610
Cdd:cd03141 19 GLWLEELAHPYDVFTEAGYEVDFASPKGGKVPldprsldaeddddasvfDNDEEFKKKLANTKKLSDVDpsdYDAIFIPG 98
|
90 100 110
....*....|....*....|....*....|
gi 1717936743 611 GP----ELKDNKQAMAFIREAYNHYKAIGA 636
Cdd:cd03141 99 GHgpmfDLPDNPDLQDLLREFYENGKVVAA 128
|
|
| |
