|
Name |
Accession |
Description |
Interval |
E-value |
| katE |
PRK11249 |
hydroperoxidase II; Provisional |
1-750 |
0e+00 |
|
hydroperoxidase II; Provisional
Pssm-ID: 236886 [Multi-domain] Cd Length: 752 Bit Score: 1610.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 1 MSHNEKSPHQSPVHDTRESQPGLDSLAPSDDSHRPTPEPTPPGAQPTAPGSLKAPETANDKLTALDAFRKGSENYALTTN 80
Cdd:PRK11249 1 HNEKNPHQHQSPLHDSSEAKPGMDSLAPEDGSHRPAPEPTPPGAQPTAPGSLKAPDTRNEKLNSLEAFRKGSEGYALTTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 81 QGVRIADDQNSLRAGSRGPTLLEDFILREKITHFDHERIPERIVHARGSAAHGYFQPYKDLSDITKAAFLCDPQKITPVF 160
Cdd:PRK11249 81 QGVRIADDQNSLRAGSRGPSLLEDFILREKITHFDHERIPERIVHARGSAAHGYFQPYKSLSDITKAAFLQDPGKITPVF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 161 VRFSTVQGGAGSADTVRDIRGFATKFYTEEGIFDLVGNNTPIFFIQDAHKFPDFVHAVKPEPHWAIPQGQSAHDTFWDYV 240
Cdd:PRK11249 161 VRFSTVQGPRGSADTVRDIRGFATKFYTEEGNFDLVGNNTPVFFIQDAIKFPDFVHAVKPEPHNEIPQGQSAHDTFWDYV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 241 SLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLINAQGKATFVRFHWKPLAGKASLVWDESQKLTGRDPDFHRRDLW 320
Cdd:PRK11249 241 SLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLINAEGKATFVRFHWKPVAGKASLVWDEAQKLTGRDPDFHRRDLW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 321 EAIEAGDFPEYELGLQLIAEEDEFKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAENEQAAFHPGHIVPGIDFT 400
Cdd:PRK11249 321 EAIEAGDYPEYELGVQLIPEEDEFKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFHPGHIVPGIDFT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 401 NDPLLQGRLFSYTDTQISRLGGPNFHEIPINRPTCPYHNFQRDGMHRMDIDTNPANYEPNSINDNWPRETPPAPKRGGFE 480
Cdd:PRK11249 401 NDPLLQGRLFSYTDTQISRLGGPNFHEIPINRPTCPYHNFQRDGMHRMTIDTGPANYEPNSINGNWPRETPPAPKRGGFE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 481 SYQERVDGNKIRERSPSFGEYYSHPRLFWLSQTPIEQQHIIDAFSFELGKVARAYIRERVVDQLAHIDVTLAEGVAHNLG 560
Cdd:PRK11249 481 SYQERVEGNKVRERSPSFGDYYSQPRLFWLSQTPIEQRHIIDAFSFELGKVVRPYIRERVVDQLAHIDLTLAQAVAENLG 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 561 FALTHEQTQIAPPPDVNGLKKDPALSLYAVPDGDVKGRVVAILLNDKVNAADLLTILQALKAKGVHAKLLYSRMGEVTAD 640
Cdd:PRK11249 561 IPLTDEQLNITPPPDVNGLKKDPALSLYAIPDGDIKGRKVAILLNDGVDAADLLAILKALKAKGVHAKLLYPRMGEVTAD 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 641 DGSTLTIAATFAGAPSLTVDAVIVPCG--NIADIESCGDARYYLLEAYKHLKPIALAGDARRFKALLNIDSQGEEGLAEA 718
Cdd:PRK11249 641 DGTVLPIAATFAGAPSLTFDAVIVPGGkaNIADLADNGDARYYLLEAYKHLKPIALAGDARKLKAALKLPDQGEEGLVEA 720
|
730 740 750
....*....|....*....|....*....|..
gi 1539623229 719 DNVDHHFMDTLLTLMAAHRVWSRAGKINAIPA 750
Cdd:PRK11249 721 DSADGSFMDELLTAMAAHRVWSREPKADAIPA 752
|
|
| KatE |
COG0753 |
Catalase [Inorganic ion transport and metabolism]; |
77-563 |
0e+00 |
|
Catalase [Inorganic ion transport and metabolism];
Pssm-ID: 440516 [Multi-domain] Cd Length: 489 Bit Score: 941.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 77 LTTNQGVRIADDQNSLRAGSRGPTLLEDFILREKITHFDHERIPERIVHARGSAAHGYFQPYKDLSDITKAAFLCDPQKI 156
Cdd:COG0753 11 LTTNQGAPVADNQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFEVTEDISKYTKAKFFQEPGKK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 157 TPVFVRFSTVQGGAGSADTVRDIRGFATKFYTEEGIFDLVGNNTPIFFIQDAHKFPDFVHAVKPEPHWAIPQgqsaHDTF 236
Cdd:COG0753 91 TPVFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHAQKRDPDTNLPQ----HDTF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 237 WDYVSLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLINAQGKATFVRFHWKPLAGKASLVWDESQKLTGRDPDFHR 316
Cdd:COG0753 167 WDFWSLSPESLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAEGERFWVKFHWKPKQGIHSLTWDEAQKIAGKDPDFHR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 317 RDLWEAIEAGDFPEYELGLQLIAEEDEFKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAENEQAAFHPGHIVPG 396
Cdd:COG0753 247 RDLYEAIERGDFPEWELGVQVMPEEDADKFDFDPLDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAETEQAAFSPGNLVPG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 397 IDFTNDPLLQGRLFSYTDTQISRLgGPNFHEIPINRPTCPYHNFQRDGMHRMDIDTNPANYEPNSINDnwPRETPpapkr 476
Cdd:COG0753 327 IDFSPDKMLQGRLFSYADTQRYRL-GPNFHQLPVNRPKCPVHNYQRDGAMRYDINGGRVNYEPNSLGG--PREDP----- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 477 gGFESYQERVDGNKIRERSPSfGEYYSHPRLFWLSQTPIEQQHIIDAFSFELGKVARAYIRERVVDQLAHIDVTLAEGVA 556
Cdd:COG0753 399 -GFKEPPLKVDGDKVRYRSES-DDHFSQAGLLYRSMSDEEKQHLIDNIAFELGKVESEEIRERMVAHFYNVDPELGARVA 476
|
....*..
gi 1539623229 557 HNLGFAL 563
Cdd:COG0753 477 EALGLDL 483
|
|
| catalase_clade_2 |
cd08155 |
Clade 2 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
115-559 |
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: 934.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 115 DHERIPERIVHARGSAAHGYFQPYKDLSDITKAAFLCDPQKITPVFVRFSTVQGGAGSADTVRDIRGFATKFYTEEGIFD 194
Cdd:cd08155 1 DHERIPERVVHARGSGAHGYFQVYESLSQYTKAKFLQDPGKKTPVFVRFSTVAGSRGSADTVRDVRGFAVKFYTEEGNYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 195 LVGNNTPIFFIQDAHKFPDFVHAVKPEPHWAIPQGQSAHDTFWDYVSLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTF 274
Cdd:cd08155 81 LVGNNIPVFFIQDAIKFPDLIHAVKPEPHNEMPQAQSAHDTFWDFVSLQPESAHMVMWAMSDRAIPRSYRMMEGFGVHTF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 275 RLINAQGKATFVRFHWKPLAGKASLVWDESQKLTGRDPDFHRRDLWEAIEAGDFPEYELGLQLIAEEDEFKFDFDLLDPT 354
Cdd:cd08155 161 RLVNAQGKSTFVKFHWKPVLGVHSLVWDEAQKIAGKDPDFHRRDLWEAIESGDYPEWELGVQLIDEEDEFKFDFDILDPT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 355 KLIPEELVPVQRVGKMVLNRNPDNFFAENEQAAFHPGHIVPGIDFTNDPLLQGRLFSYTDTQISRLGGPNFHEIPINRPT 434
Cdd:cd08155 241 KLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFCPANVVPGIDFSNDPLLQGRLFSYLDTQLSRLGGPNFHELPINRPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 435 CPYHNFQRDGMHRMDIDTNPANYEPNSINDNWPRETPPApkRGGFESYQERVDGNKIRERSPSFGEYYSHPRLFWLSQTP 514
Cdd:cd08155 321 CPVHNNQRDGHMRMTINKGRVNYFPNSLGAGPPRAASPA--EGGFVHYPEKVEGPKIRIRSESFADHYSQARLFWNSMSP 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1539623229 515 IEQQHIIDAFSFELGKVARAYIRERVVDQLAHIDVTLAEGVAHNL 559
Cdd:cd08155 399 VEKEHIISAFTFELSKVETPEIRERVVDHLANIDEDLAKKVAKGL 443
|
|
| Catalase |
pfam00199 |
Catalase; |
78-463 |
0e+00 |
|
Catalase;
Pssm-ID: 459708 Cd Length: 383 Bit Score: 751.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 78 TTNQGVRIADDQNSLRAGSRGPTLLEDFILREKITHFDHERIPERIVHARGSAAHGYFQPYKDLSDITKAAFLCDPQKIT 157
Cdd:pfam00199 1 TTSNGAPVPDNQNSLTAGPRGPLLLQDFHLIEKLAHFDRERIPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSEVGKKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 158 PVFVRFSTVQGGAGSADTVRDIRGFATKFYTEEGIFDLVGNNTPIFFIQDAHKFPDFVHAVKPEPHWAIPQgqsaHDTFW 237
Cdd:pfam00199 81 PVFVRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHSQKRDPQTNLPD----PAMFW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 238 DYVSLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLINAQGKATFVRFHWKPLAGKASLVWDESQKLTGRDPDFHRR 317
Cdd:pfam00199 157 DFWSLNPESLHQVTWLFSDRGIPRSYRHMNGFGVHTFKLVNADGERVYVKFHFKTDQGIKNLTWEEAQKLAGKDPDYHTR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 318 DLWEAIEAGDFPEYELGLQLIAEEDEFKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAENEQAAFHPGHIVPGI 397
Cdd:pfam00199 237 DLYEAIERGDYPSWTLYVQVMTEEDAEKFRFNPFDLTKVWPHKDYPLIEVGKMVLNRNPDNYFAEVEQAAFSPSNLVPGI 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1539623229 398 DFTNDPLLQGRLFSYTDTQISRLgGPNFHEIPINRPTCPYHNFQRDGMHRMDIDTNPA-NYEPNSIN 463
Cdd:pfam00199 317 EPSPDPMLQGRLFSYPDTQRYRL-GPNYQQLPVNRPPCPVHNYQRDGAMRFDINQGSRpNYEPNSFG 382
|
|
| Catalase |
smart01060 |
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ... |
81-457 |
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: 724.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 81 QGVRIADDQNSLRAGSRGPTLLEDFILREKITHFDHERIPERIVHARGSAAHGYFQPYKDLSDITKAAFLCDPQKITPVF 160
Cdd:smart01060 1 QGAPVADNQNSLTAGPRGPVLLQDFHLIEKLAHFDRERIPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQKVGKKTPVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 161 VRFSTVQGGAGSADTVRDIRGFATKFYTEEGIFDLVGNNTPIFFIQDAHKFPDFVHAVKPEPHWAIPQgqsaHDTFWDYV 240
Cdd:smart01060 81 VRFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHAQKRDPRTNLPD----HDMFWDFW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 241 SLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLINAQGKATFVRFHWKPLAGKASLVWDESQKLTGRDPDFHRRDLW 320
Cdd:smart01060 157 SLNPESLHQVTWLMSDRGIPASYRHMNGFGVHTFKLVNAEGERFYVKFHFKPDQGIKNLTWEEAAKLAGKDPDYHRRDLY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 321 EAIEAGDFPEYELGLQLIAEEDEFKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAENEQAAFHPGHIVPGIDFT 400
Cdd:smart01060 237 EAIERGDYPEWTLYVQVMPEEDAEKFRFDPFDLTKVWPHKDYPLIEVGKMTLNRNPDNYFAEVEQAAFSPSNLVPGIEFS 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1539623229 401 NDPLLQGRLFSYTDTQISRLgGPNFHEIPINRPTCPYHNFQRDGMHRMD-IDTNPANY 457
Cdd:smart01060 317 PDKMLQGRLFSYPDTQRYRL-GPNYHQLPVNRPRCPVHNYQRDGAMRVDgNQGGDPNY 373
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| katE |
PRK11249 |
hydroperoxidase II; Provisional |
1-750 |
0e+00 |
|
hydroperoxidase II; Provisional
Pssm-ID: 236886 [Multi-domain] Cd Length: 752 Bit Score: 1610.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 1 MSHNEKSPHQSPVHDTRESQPGLDSLAPSDDSHRPTPEPTPPGAQPTAPGSLKAPETANDKLTALDAFRKGSENYALTTN 80
Cdd:PRK11249 1 HNEKNPHQHQSPLHDSSEAKPGMDSLAPEDGSHRPAPEPTPPGAQPTAPGSLKAPDTRNEKLNSLEAFRKGSEGYALTTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 81 QGVRIADDQNSLRAGSRGPTLLEDFILREKITHFDHERIPERIVHARGSAAHGYFQPYKDLSDITKAAFLCDPQKITPVF 160
Cdd:PRK11249 81 QGVRIADDQNSLRAGSRGPSLLEDFILREKITHFDHERIPERIVHARGSAAHGYFQPYKSLSDITKAAFLQDPGKITPVF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 161 VRFSTVQGGAGSADTVRDIRGFATKFYTEEGIFDLVGNNTPIFFIQDAHKFPDFVHAVKPEPHWAIPQGQSAHDTFWDYV 240
Cdd:PRK11249 161 VRFSTVQGPRGSADTVRDIRGFATKFYTEEGNFDLVGNNTPVFFIQDAIKFPDFVHAVKPEPHNEIPQGQSAHDTFWDYV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 241 SLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLINAQGKATFVRFHWKPLAGKASLVWDESQKLTGRDPDFHRRDLW 320
Cdd:PRK11249 241 SLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLINAEGKATFVRFHWKPVAGKASLVWDEAQKLTGRDPDFHRRDLW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 321 EAIEAGDFPEYELGLQLIAEEDEFKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAENEQAAFHPGHIVPGIDFT 400
Cdd:PRK11249 321 EAIEAGDYPEYELGVQLIPEEDEFKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFHPGHIVPGIDFT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 401 NDPLLQGRLFSYTDTQISRLGGPNFHEIPINRPTCPYHNFQRDGMHRMDIDTNPANYEPNSINDNWPRETPPAPKRGGFE 480
Cdd:PRK11249 401 NDPLLQGRLFSYTDTQISRLGGPNFHEIPINRPTCPYHNFQRDGMHRMTIDTGPANYEPNSINGNWPRETPPAPKRGGFE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 481 SYQERVDGNKIRERSPSFGEYYSHPRLFWLSQTPIEQQHIIDAFSFELGKVARAYIRERVVDQLAHIDVTLAEGVAHNLG 560
Cdd:PRK11249 481 SYQERVEGNKVRERSPSFGDYYSQPRLFWLSQTPIEQRHIIDAFSFELGKVVRPYIRERVVDQLAHIDLTLAQAVAENLG 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 561 FALTHEQTQIAPPPDVNGLKKDPALSLYAVPDGDVKGRVVAILLNDKVNAADLLTILQALKAKGVHAKLLYSRMGEVTAD 640
Cdd:PRK11249 561 IPLTDEQLNITPPPDVNGLKKDPALSLYAIPDGDIKGRKVAILLNDGVDAADLLAILKALKAKGVHAKLLYPRMGEVTAD 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 641 DGSTLTIAATFAGAPSLTVDAVIVPCG--NIADIESCGDARYYLLEAYKHLKPIALAGDARRFKALLNIDSQGEEGLAEA 718
Cdd:PRK11249 641 DGTVLPIAATFAGAPSLTFDAVIVPGGkaNIADLADNGDARYYLLEAYKHLKPIALAGDARKLKAALKLPDQGEEGLVEA 720
|
730 740 750
....*....|....*....|....*....|..
gi 1539623229 719 DNVDHHFMDTLLTLMAAHRVWSRAGKINAIPA 750
Cdd:PRK11249 721 DSADGSFMDELLTAMAAHRVWSREPKADAIPA 752
|
|
| KatE |
COG0753 |
Catalase [Inorganic ion transport and metabolism]; |
77-563 |
0e+00 |
|
Catalase [Inorganic ion transport and metabolism];
Pssm-ID: 440516 [Multi-domain] Cd Length: 489 Bit Score: 941.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 77 LTTNQGVRIADDQNSLRAGSRGPTLLEDFILREKITHFDHERIPERIVHARGSAAHGYFQPYKDLSDITKAAFLCDPQKI 156
Cdd:COG0753 11 LTTNQGAPVADNQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFEVTEDISKYTKAKFFQEPGKK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 157 TPVFVRFSTVQGGAGSADTVRDIRGFATKFYTEEGIFDLVGNNTPIFFIQDAHKFPDFVHAVKPEPHWAIPQgqsaHDTF 236
Cdd:COG0753 91 TPVFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHAQKRDPDTNLPQ----HDTF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 237 WDYVSLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLINAQGKATFVRFHWKPLAGKASLVWDESQKLTGRDPDFHR 316
Cdd:COG0753 167 WDFWSLSPESLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAEGERFWVKFHWKPKQGIHSLTWDEAQKIAGKDPDFHR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 317 RDLWEAIEAGDFPEYELGLQLIAEEDEFKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAENEQAAFHPGHIVPG 396
Cdd:COG0753 247 RDLYEAIERGDFPEWELGVQVMPEEDADKFDFDPLDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAETEQAAFSPGNLVPG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 397 IDFTNDPLLQGRLFSYTDTQISRLgGPNFHEIPINRPTCPYHNFQRDGMHRMDIDTNPANYEPNSINDnwPRETPpapkr 476
Cdd:COG0753 327 IDFSPDKMLQGRLFSYADTQRYRL-GPNFHQLPVNRPKCPVHNYQRDGAMRYDINGGRVNYEPNSLGG--PREDP----- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 477 gGFESYQERVDGNKIRERSPSfGEYYSHPRLFWLSQTPIEQQHIIDAFSFELGKVARAYIRERVVDQLAHIDVTLAEGVA 556
Cdd:COG0753 399 -GFKEPPLKVDGDKVRYRSES-DDHFSQAGLLYRSMSDEEKQHLIDNIAFELGKVESEEIRERMVAHFYNVDPELGARVA 476
|
....*..
gi 1539623229 557 HNLGFAL 563
Cdd:COG0753 477 EALGLDL 483
|
|
| catalase_clade_2 |
cd08155 |
Clade 2 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
115-559 |
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: 934.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 115 DHERIPERIVHARGSAAHGYFQPYKDLSDITKAAFLCDPQKITPVFVRFSTVQGGAGSADTVRDIRGFATKFYTEEGIFD 194
Cdd:cd08155 1 DHERIPERVVHARGSGAHGYFQVYESLSQYTKAKFLQDPGKKTPVFVRFSTVAGSRGSADTVRDVRGFAVKFYTEEGNYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 195 LVGNNTPIFFIQDAHKFPDFVHAVKPEPHWAIPQGQSAHDTFWDYVSLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTF 274
Cdd:cd08155 81 LVGNNIPVFFIQDAIKFPDLIHAVKPEPHNEMPQAQSAHDTFWDFVSLQPESAHMVMWAMSDRAIPRSYRMMEGFGVHTF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 275 RLINAQGKATFVRFHWKPLAGKASLVWDESQKLTGRDPDFHRRDLWEAIEAGDFPEYELGLQLIAEEDEFKFDFDLLDPT 354
Cdd:cd08155 161 RLVNAQGKSTFVKFHWKPVLGVHSLVWDEAQKIAGKDPDFHRRDLWEAIESGDYPEWELGVQLIDEEDEFKFDFDILDPT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 355 KLIPEELVPVQRVGKMVLNRNPDNFFAENEQAAFHPGHIVPGIDFTNDPLLQGRLFSYTDTQISRLGGPNFHEIPINRPT 434
Cdd:cd08155 241 KLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFCPANVVPGIDFSNDPLLQGRLFSYLDTQLSRLGGPNFHELPINRPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 435 CPYHNFQRDGMHRMDIDTNPANYEPNSINDNWPRETPPApkRGGFESYQERVDGNKIRERSPSFGEYYSHPRLFWLSQTP 514
Cdd:cd08155 321 CPVHNNQRDGHMRMTINKGRVNYFPNSLGAGPPRAASPA--EGGFVHYPEKVEGPKIRIRSESFADHYSQARLFWNSMSP 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1539623229 515 IEQQHIIDAFSFELGKVARAYIRERVVDQLAHIDVTLAEGVAHNL 559
Cdd:cd08155 399 VEKEHIISAFTFELSKVETPEIRERVVDHLANIDEDLAKKVAKGL 443
|
|
| Catalase |
pfam00199 |
Catalase; |
78-463 |
0e+00 |
|
Catalase;
Pssm-ID: 459708 Cd Length: 383 Bit Score: 751.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 78 TTNQGVRIADDQNSLRAGSRGPTLLEDFILREKITHFDHERIPERIVHARGSAAHGYFQPYKDLSDITKAAFLCDPQKIT 157
Cdd:pfam00199 1 TTSNGAPVPDNQNSLTAGPRGPLLLQDFHLIEKLAHFDRERIPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSEVGKKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 158 PVFVRFSTVQGGAGSADTVRDIRGFATKFYTEEGIFDLVGNNTPIFFIQDAHKFPDFVHAVKPEPHWAIPQgqsaHDTFW 237
Cdd:pfam00199 81 PVFVRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHSQKRDPQTNLPD----PAMFW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 238 DYVSLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLINAQGKATFVRFHWKPLAGKASLVWDESQKLTGRDPDFHRR 317
Cdd:pfam00199 157 DFWSLNPESLHQVTWLFSDRGIPRSYRHMNGFGVHTFKLVNADGERVYVKFHFKTDQGIKNLTWEEAQKLAGKDPDYHTR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 318 DLWEAIEAGDFPEYELGLQLIAEEDEFKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAENEQAAFHPGHIVPGI 397
Cdd:pfam00199 237 DLYEAIERGDYPSWTLYVQVMTEEDAEKFRFNPFDLTKVWPHKDYPLIEVGKMVLNRNPDNYFAEVEQAAFSPSNLVPGI 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1539623229 398 DFTNDPLLQGRLFSYTDTQISRLgGPNFHEIPINRPTCPYHNFQRDGMHRMDIDTNPA-NYEPNSIN 463
Cdd:pfam00199 317 EPSPDPMLQGRLFSYPDTQRYRL-GPNYQQLPVNRPPCPVHNYQRDGAMRFDINQGSRpNYEPNSFG 382
|
|
| Catalase |
smart01060 |
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ... |
81-457 |
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: 724.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 81 QGVRIADDQNSLRAGSRGPTLLEDFILREKITHFDHERIPERIVHARGSAAHGYFQPYKDLSDITKAAFLCDPQKITPVF 160
Cdd:smart01060 1 QGAPVADNQNSLTAGPRGPVLLQDFHLIEKLAHFDRERIPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQKVGKKTPVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 161 VRFSTVQGGAGSADTVRDIRGFATKFYTEEGIFDLVGNNTPIFFIQDAHKFPDFVHAVKPEPHWAIPQgqsaHDTFWDYV 240
Cdd:smart01060 81 VRFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHAQKRDPRTNLPD----HDMFWDFW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 241 SLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLINAQGKATFVRFHWKPLAGKASLVWDESQKLTGRDPDFHRRDLW 320
Cdd:smart01060 157 SLNPESLHQVTWLMSDRGIPASYRHMNGFGVHTFKLVNAEGERFYVKFHFKPDQGIKNLTWEEAAKLAGKDPDYHRRDLY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 321 EAIEAGDFPEYELGLQLIAEEDEFKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAENEQAAFHPGHIVPGIDFT 400
Cdd:smart01060 237 EAIERGDYPEWTLYVQVMPEEDAEKFRFDPFDLTKVWPHKDYPLIEVGKMTLNRNPDNYFAEVEQAAFSPSNLVPGIEFS 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1539623229 401 NDPLLQGRLFSYTDTQISRLgGPNFHEIPINRPTCPYHNFQRDGMHRMD-IDTNPANY 457
Cdd:smart01060 317 PDKMLQGRLFSYPDTQRYRL-GPNYHQLPVNRPRCPVHNYQRDGAMRVDgNQGGDPNY 373
|
|
| catalase |
cd00328 |
Catalase heme-binding enzyme; Catalase is a ubiquitous enzyme found in both prokaryotes and ... |
118-559 |
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: 721.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 118 RIPERIVHARGSAAHGYFQPYKDLSDITKAAFLCDPQKITPVFVRFSTVQGGAGSADTVRDIRGFATKFYTEEGIFDLVG 197
Cdd:cd00328 1 RIPERVVHARGAGAFGYFTAYGDWSDISAAAFFSAIGKKTPVFVRFSTVVGGAGSADTVRDPHGFATKFYTEEGNFDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 198 NNTPIFFIQDAHKFPDFVHAVKPEPHWAIPQgqsaHDTFWDYVSLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLI 277
Cdd:cd00328 81 NNTPIFFIRDAIKFPDFIHAQKPNPQTALPD----ADRFWDFLSLRPESLHQVSFLFSDRGIPAAYRHMNGYGSHTFKLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 278 NAQGKATFVRFHWKPLAGKASLVWDESQKLTGRDPDFHRRDLWEAIEAGDFPEYELGLQLIAEEDEFKFDFDLLDPTKLI 357
Cdd:cd00328 157 NANGKVHYVKFHWKTDQGIANLVWEEAARLAGEDPDYHRQDLFEAIEAGDYPSWELYIQVMTFNDAEKFPFNPLDPTKVW 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 358 PEELVPVQRVGKMVLNRNPDNFFAENEQAAFHPGHIVPGIDFTNDPLLQGRLFSYTDTQISRLgGPNFHEIPINRPTCPY 437
Cdd:cd00328 237 PEELVPLIVVGKLVLNRNPLNFFAEVEQAAFDPGHIVPGVEFSEDPLLQGRLFSYADTQLYRL-GPNFQQLPVNRPYAPV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 438 HNFQRDGMHRMDIDTNPANYEPNSINDNWPRETPPAPKRGGFesyqERVDGNKIRERSPSFGEYYSHPRLFWLSQTPIEQ 517
Cdd:cd00328 316 HNNQRDGAGNMNDNTGVPNYEPNAKDVRYPAQGAPKFDRGHF----SHWKSGVNREASTTNDDNFTQARLFYRSLTPGQQ 391
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1539623229 518 QHIIDAFSFELGKVARAYIRERVVDQLAHIDVTLAEGVAHNL 559
Cdd:cd00328 392 KRLVDAFRFELADAVSPQIQQRVLDQFAKVDAAAAKRVAKAL 433
|
|
| catalase_clade_1 |
cd08154 |
Clade 1 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
76-556 |
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: 587.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 76 ALTTNQGVRIADDQNSLRAGSRGPTLLEDFILREKITHFDHERIPERIVHARGSAAHGYFQPYKDLSDITKAAFLCDPQK 155
Cdd:cd08154 1 TLTTNQGAPVGDNQNSQTVGPRGPVLLEDYHLIEKLAHFDRERIPERVVHARGAGAHGYFEAYGDISDYTRASFLQEPGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 156 ITPVFVRFSTVQGGAGSADTVRDIRGFATKFYTEEGIFDLVGNNTPIFFIQDAHKFPDFVHAVKPEPHWAIPQGQSahdt 235
Cdd:cd08154 81 KTPVFVRFSTVIHGKGSPETLRDPRGFAVKFYTEEGNWDLVGNNLPVFFIRDAIKFPDMIHALKPSPVTNIQDPNR---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 236 FWDYVSLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLINAQGKATFVRFHWKPLAGKASLVWDESQKLTGRDPDFH 315
Cdd:cd08154 157 IFDFFSHVPESTHMLTFLYSDWGTPASYRHMDGSGVHTYKWVNAEGKVVYVKYHWKPKQGVKNLTAEEAAEVQGKNFNHA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 316 RRDLWEAIEAGDFPEYELGLQLIAEEDEFKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAENEQAAFHPGHIVP 395
Cdd:cd08154 237 TQDLYDAIAAGNYPEWELYVQIMDPKDLDKLDFDPLDDTKIWPEDQFPLKPVGKMTLNKNPDNFFAEVEQVAFSPGNLVP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 396 GIDFTNDPLLQGRLFSYTDTQISRLgGPNFHEIPINRPTCPYHNFQRDGMHRMDIDTNPANYEPNSINdnwprETPPAPK 475
Cdd:cd08154 317 GIEPSDDKMLQGRLFSYSDTQRYRL-GPNYLQLPINAPKAAVHNNQRDGQMNYGHDTSDVNYEPSRLD-----GLPEAPK 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 476 rggFESYQERVDGNKIRERSPSfGEYYSHPRLFWLSQTPIEQQHIIDAFSFELGKVaRAYIRERVVDQLAHIDVTLAEGV 555
Cdd:cd08154 391 ---YPYSQPPLSGTTQQAPIAK-TNNFKQAGERYRSFSEEEQENLIKNLVVDLSDV-NEEIKLRMLSYFSQADPDYGERV 465
|
.
gi 1539623229 556 A 556
Cdd:cd08154 466 A 466
|
|
| catalase_clade_3 |
cd08156 |
Clade 3 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
118-556 |
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: 523.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 118 RIPERIVHARGSAAHGYFQPYKDLSDITKAAFLCDPQKITPVFVRFSTVQGGAGSADTVRDIRGFATKFYTEEGIFDLVG 197
Cdd:cd08156 1 RIPERVVHAKGAGAFGTFEVTHDITKYTKAKIFSEVGKKTPVFVRFSTVAGERGSADTERDPRGFALKFYTEEGNWDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 198 NNTPIFFIQDAHKFPDFVHAVKPEPHwaipQGQSAHDTFWDYVSLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLI 277
Cdd:cd08156 81 NNTPVFFIRDPIKFPDFIHTQKRNPQ----TNLKDPDMFWDFWSLSPESLHQVTILFSDRGIPDGYRHMNGYGSHTFSLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 278 NAQGKATFVRFHWKPLAGKASLVWDESQKLTGRDPDFHRRDLWEAIEAGDFPEYELGLQLIAEEDEFKFDFDLLDPTKLI 357
Cdd:cd08156 157 NAKGERFWVKFHFKTDQGIKNLTNEEAAELAGEDPDYAQRDLFEAIERGDFPSWTLYVQVMPEEDAEKYRFNPFDLTKVW 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 358 PEELVPVQRVGKMVLNRNPDNFFAENEQAAFHPGHIVPGIDFTNDPLLQGRLFSYTDTQISRLgGPNFHEIPINRPTCPY 437
Cdd:cd08156 237 PHKDYPLIEVGKLELNRNPENYFAEVEQAAFSPSNLVPGIGFSPDKMLQGRLFSYADAHRYRL-GVNYHQLPVNRPKCPV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 438 HNFQRDGMHRMDIDTNPA-NYEPNSINDNWPRETPPAPKrggfesyqERVDGNKIRERSPSFGEYYSHPRLFWLSQTPIE 516
Cdd:cd08156 316 NNYQRDGAMRVDGNGGGApNYEPNSFGGPPEDPEYAEPP--------LPVSGDADRYNYRDDDDDYTQAGDLYRLVSEDE 387
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1539623229 517 QQHIIDAFSFELGKvARAYIRERVVDQLAHIDVTLAEGVA 556
Cdd:cd08156 388 RERLVENIAGHLKG-APEFIQERQVAHFYKADPDYGERVA 426
|
|
| PLN02609 |
PLN02609 |
catalase |
78-560 |
2.18e-178 |
|
catalase
Pssm-ID: 215328 [Multi-domain] Cd Length: 492 Bit Score: 519.30 E-value: 2.18e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 78 TTNQGVRIADDQNSLRAGSRGPTLLEDFILREKITHFDHERIPERIVHARGSAAHGYFQPYKDLSDITKAAFLCDPQKIT 157
Cdd:PLN02609 18 TTNSGAPVWNNNSSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDISNLTCADFLRAPGVQT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 158 PVFVRFSTVQGGAGSADTVRDIRGFATKFYTEEGIFDLVGNNTPIFFIQDAHKFPDFVHAVKPEPHWAIPQgqsaHDTFW 237
Cdd:PLN02609 98 PVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDMVGNNFPVFFIRDGMKFPDMVHALKPNPKTHIQE----PWRIL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 238 DYVSLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLINAQGKATFVRFHWKPLAGKASLVWDESQKLTGRDPDFHRR 317
Cdd:PLN02609 174 DFLSHHPESLHMFTFLFDDRGIPQDYRHMEGFGVHTYKLINKAGKAHYVKFHWKPTCGVKNLLDEEAVRVGGSNHSHATQ 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 318 DLWEAIEAGDFPEYELGLQLIAEEDEFKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAENEQAAFHPGHIVPGI 397
Cdd:PLN02609 254 DLYDSIAAGNYPEWKLFIQTMDPEDEDKFDFDPLDVTKTWPEDILPLQPVGRLVLNRNIDNFFAENEQLAFCPAIVVPGI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 398 DFTNDPLLQGRLFSYTDTQISRLgGPNFHEIPINRPTCPYHNFQRDG-MHRMDIDTNPaNYEPNSIND---NWPRETPPA 473
Cdd:PLN02609 334 YYSDDKLLQTRIFAYADTQRHRL-GPNYLQLPVNAPKCAHHNNHHEGfMNFMHRDEEV-NYFPSRFDPvrhAERVPIPHP 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 474 PKRGGFESYQERVDGNkirerspsfgeyYSHPRLFWLSQTPIEQQHIIDAFSFELGKVARAY-IRERVVDQLAHIDVTLA 552
Cdd:PLN02609 412 PLSGRREKCKIEKENN------------FKQPGERYRSWSPDRQERFIKRWVDALSDPRVTHeIRSIWISYWSQCDKSLG 479
|
....*...
gi 1539623229 553 EGVAHNLG 560
Cdd:PLN02609 480 QKLASRLN 487
|
|
| catalase_fungal |
cd08157 |
Fungal catalases similar to yeast catalases A and T; Catalase is a ubiquitous enzyme found in ... |
102-560 |
1.74e-158 |
|
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: 466.82 E-value: 1.74e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 102 LEDFILREKITHFDHERIPERIVHARGSAAHGYFQPYKDLSDITKAAFLCDPQKITPVFVRFSTVQGGAGSADTVRDIRG 181
Cdd:cd08157 1 LQDFHLIDTLAHFDRERIPERVVHAKGAGAYGEFEVTDDISDITSADMLQGVGKKTPCLVRFSTVGGEKGSADTVRDPRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 182 FATKFYTEEGIFDLVGNNTPIFFIQDAHKFPDFVHAVKPEPHWAIPQGqsahDTFWDYVSLQPETLHNVMWAMSDRGIPR 261
Cdd:cd08157 81 FAVKFYTEEGNWDWVFNNTPVFFIRDPIKFPHFIHSQKRDPQTNLKDS----TMFWDYLSQNPESIHQVMILFSDRGTPA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 262 SYRTMEGFGIHTFRLINAQGKATFVRFHWKPLAGKASLVWDESQKLTGRDPDFHRRDLWEAIEAGDFPEYELGLQLIAEE 341
Cdd:cd08157 157 SYRSMNGYSGHTYKWVNPDGSFKYVQFHLKSDQGPKFLTGEEAARLAGSNPDYATKDLFEAIERGDYPSWTVYVQVMTPE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 342 DEFKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAENEQAAFHPGHIVPGIDFTNDPLLQGRLFSYTDTQISRLg 421
Cdd:cd08157 237 QAEKLRFNIFDLTKVWPHKDFPLRPVGKLTLNENPKNYFAEIEQAAFSPSHMVPGIEPSADPVLQARLFSYPDAHRHRL- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 422 GPNFHEIPINRP-TCPYHNF-QRDGMHRMDidtnpANYEPNSindNWPRETPPA---PKRGGFESYQERVDGNKIRERSP 496
Cdd:cd08157 316 GPNYQQLPVNRPkTSPVYNPyQRDGPMSVN-----GNYGGDP---NYVSSILPPtyfKKRVDADGHHENWVGEVVAFLTE 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1539623229 497 SFGEYYSHPRLFW-LSQTPIEQQHIIDAFSFELGKVaRAYIRERVVDQLAHIDVTLAEGVAHNLG 560
Cdd:cd08157 388 ITDEDFVQPRALWeVVGKPGQQERFVKNVAGHLSGA-PPEIRKRVYEIFARVNPDLGKRIEKATE 451
|
|
| catalase_like |
cd08150 |
Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found ... |
120-420 |
1.77e-117 |
|
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: 354.94 E-value: 1.77e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 120 PERIVHARGSAAHGYFQPYKDL--SDITKAAFlcdPQKITPVFVRFSTVQGgagSADTVRDIRGFATKFYTE--EGIFDL 195
Cdd:cd08150 1 GLRGQHFQGTCAFGTFEVLADLkeRLRVGLFA---EGKVYPAYIRFSNGAG---IDDTKPDIRGFAIKFTGVadAGTLDF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 196 VGNNTPIFFIQDAHKFPDFVHAVKPEPhwaipQGQSAHDTFWDYVSLQPETLHNVMWAMSdrGIPRSYRTMEGFGIHTFR 275
Cdd:cd08150 75 VLNNTPVFFIRNTSDYEDFVAEFARSA-----RGEPPLDFIAWYVEKRPEDLPNLLGARS--QVPDSYAAARYFSQVTFA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 276 LINAQGKATFVRFHWKPLAGKASLVWdesQKLTGRDPDFHRRDLWEAIEAGdFPEYELGLQLIAEEDefkfDFDLLDPTK 355
Cdd:cd08150 148 FINGAGKYRVVRSKDNPVDGIPSLED---HELEARPPDYLREELTERLQRG-PVVYDFRIQLNDDTD----ATTIDNPTI 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1539623229 356 LIPEElVPVQRVGKMVLNRNPDNffAENEQAAFHPGHIVPGIDFTND--PLLQGRLFSYTDTQISRL 420
Cdd:cd08150 220 LWPTE-HPVEAVAKITIPPPTFT--AAQEAFAFNPFTPWHGLLETNDlgPILEVRRRVYTSSQGLRH 283
|
|
| srpA_like |
cd08153 |
Catalase-like heme-binding proteins similar to the uncharacterized srpA; Catalase is a ... |
122-408 |
4.92e-38 |
|
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: 143.53 E-value: 4.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 122 RIVHARGSAAHGYFQPYKDLSDITKAAFLcdPQKITPVFVRFSTVQGGAGSADTVRDIRGFATKFYTEEGIF-DLVGNNT 200
Cdd:cd08153 15 RRNHAKGICVSGTFTPSGAAASLSRAPLF--SGGSVPVTGRFSLGGGNPKAPDDAANPRGMALKFRLPDGEQwRMVMNSF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 201 PIFFIQDAHKFPDFVHAVKPephwaIPQGQSAHDTFWDYVSLQPETLHNVMWAMSdRGIPRSYRTMEGFGIHTFRLINAQ 280
Cdd:cd08153 93 PVFPVRTPEEFLALLKAIAP-----DATGKPDPAKLKAFLAAHPEAAAFLAWIKT-APPPASFANTTYYGVNAFYFTNAN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 281 GKATFVRFHWKPLAGKASLvwdESQKLTGRDPDFHRRDLWEAIEAGdfP-EYELGLQLIAEEDefkfdfDLLDPTKLIPE 359
Cdd:cd08153 167 GKRQPVRWRFVPEDGVKYL---SDEEAAKLGPDFLFDELAQRLAQG--PvRWDLVLQLAEPGD------PTDDPTKPWPA 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1539623229 360 ELvPVQRVGKMVLNR-NPDNFFAENeQAAFHPGHIVPGIDFTNDPLLQGR 408
Cdd:cd08153 236 DR-KEVDAGTLTITKvAPDQGGACR-DINFDPLVLPDGIEPSDDPLLAAR 283
|
|
| GATase1_catalase |
cd03132 |
Type 1 glutamine amidotransferase (GATase1)-like domain found in at the C-terminal of several ... |
597-737 |
2.10e-34 |
|
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: 128.15 E-value: 2.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 597 GRVVAILLNDKVNAADLLTILQALKAKGVHAKLLYSRMGEVTADDGSTLTIAATFAGAPSLTVDAVIVPCGNiADIESC- 675
Cdd:cd03132 1 GRKVGILVADGVDAAELSALKAALKAAGANVKVVAPTLGGVVDSDGKTLEVDQTYAGAPSVLFDAVVVPGGA-EAAFALa 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1539623229 676 --GDARYYLLEAYKHLKPIALAGDARRFKALLNIdSQGEEGLAEADNVDHHFMDTLLTLMAAHR 737
Cdd:cd03132 80 psGRALHFVTEAFKHGKPIGAVGEGSDLLEAAGI-PLEDPGVVTADDVKDVFTDRFIDALALHR 142
|
|
| Catalase-rel |
pfam06628 |
Catalase-related immune-responsive; This family represents a small conserved region within ... |
495-559 |
6.08e-23 |
|
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: 92.43 E-value: 6.08e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1539623229 495 SPSFGEYYSHPRLFWLSQTPIEQQHIIDAFSFELGKVARAYIRERVVDQLAHIDVTLAEGVAHNL 559
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 ... |
596-741 |
4.44e-11 |
|
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: 61.52 E-value: 4.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 596 KGRVVAILLNDKVNA--ADLLTILQALKAKGVHAKLLysrmGEvTADDGstltIAATFAGAPSLTVDAVIVPCG--NIAD 671
Cdd:pfam18011 1 DGLTVGILASNDSDAslAQAKALAAALAAAGVDVLVV----AE-TLADG----VNRTYSTADATLFDAIVVADGaeGLFS 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1539623229 672 IESCGDARYY--------LLEAYKHLKPIALAGDARRFKALLNIDSQGEeGLAEADNVDHHFMDTLLTLMAAHRVWSR 741
Cdd:pfam18011 72 AKATAASSLYpagrplqiLLDAYRHGKPIGALGSGSSALSGAGISAEGP-GVYVGDSADDALVEDVEEGLATFRFWDR 148
|
|
| y4iL_like |
cd08152 |
Catalase-like heme-binding proteins similar to the uncharacterized y4iL; Catalase is a ... |
158-388 |
1.29e-05 |
|
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: 47.64 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 158 PVFVRFSTVQGgAGSADTVRDIRGFATKFY----------TEEGIFDLVGNNTPIFFIQDAHKFPDFVHAVK------PE 221
Cdd:cd08152 41 PAVIRFSNAPG-DILDDSVPDPRGMAIKVLgvpgekllpeEDATTQDFVLVNHPVFFARDAKDYLALLKLLArttslpDG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 222 PHWAIPQGQSAHDTFWDYVSLQPETLhnvmwamSDRGIPR------SYRTME----GFGIHTFRLINAQGKAtfvrfhwK 291
Cdd:cd08152 120 AKAALSAPLRGALRVLEAAGGESPTL-------KLGGHPPahplgeTYWSQApyrfGDYVAKYSVVPASPAL-------P 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539623229 292 PLAGKASLVWDesqkltgrDPDFHRRDLWEAIEAGDFpEYELGLQLIAEEDEFKFDfdllDPTKLIPEELVPVQRVGKmv 371
Cdd:cd08152 186 ALTGKELDLTD--------DPDALREALADFLAENDA-EFEFRIQLCTDLEKMPIE----DASVEWPEALSPFVPVAT-- 250
|
250
....*....|....*..
gi 1539623229 372 LNRNPDNFFAENEQAAF 388
Cdd:cd08152 251 ITIPPQDFDSPARQRAF 267
|
|
| |
