|
Name |
Accession |
Description |
Interval |
E-value |
| catalase_fungal |
cd08157 |
Fungal catalases similar to yeast catalases A and T; Catalase is a ubiquitous enzyme found in ... |
60-513 |
0e+00 |
|
Fungal catalases similar to yeast catalases A and T; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes, which is involved in the protection of cells from the toxic effects of peroxides. It catalyzes the conversion of hydrogen peroxide to water and molecular oxygen. Catalases also utilize hydrogen peroxide to oxidize various substrates such as alcohol or phenols. This family of fungal catalases has a relatively small subunit size, and binds a protoheme IX (heme b) group buried deep inside the structure. Fungal catalases also bind NADPH as a second redox-active cofactor. They form tetramers; in eukaryotic cells, catalases are typically located in peroxisomes. Saccharomyces cerevisiae catalase T is found in the cytoplasm, though.
Pssm-ID: 163713 [Multi-domain] Cd Length: 451 Bit Score: 800.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 60 LQDFHLVDLLSHFDRERIPERVVHAKGGGAHGYYQTTDPLDDLCLADIFQA-GKKCPISVRFSTVGGESGSHDCARDPRG 138
Cdd:cd08157 1 LQDFHLIDTLAHFDRERIPERVVHAKGAGAYGEFEVTDDISDITSADMLQGvGKKTPCLVRFSTVGGEKGSADTVRDPRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 139 FSVKFRTEEGNWDMVANNTPVFFLRDPAKFPHFIHTQKRDPQSHLThadDSTMFWDYLSQNPESVHQVMILMGDRGIPDG 218
Cdd:cd08157 81 FAVKFYTEEGNWDWVFNNTPVFFIRDPIKFPHFIHSQKRDPQTNLK---DSTMFWDYLSQNPESIHQVMILFSDRGTPAS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 219 WRKMHGYAGHTLKLVNKKGDWVYAQMHMKSKQGTDFITQEDSANYS---PDYAQKDLYQAIEKGDYPGWDVEFQTMTPKE 295
Cdd:cd08157 158 YRSMNGYSGHTYKWVNPDGSFKYVQFHLKSDQGPKFLTGEEAARLAgsnPDYATKDLFEAIERGDYPSWTVYVQVMTPEQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 296 AEDLwetqKINVFDLTHVWPQKQFPRRKVGEFFLNENVKNYFAEIEQIAFNPAHMPPGIEPSADPVLQSRLFSYPDTHRH 375
Cdd:cd08157 238 AEKL----RFNIFDLTKVWPHKDFPLRPVGKLTLNENPKNYFAEIEQAAFSPSHMVPGIEPSADPVLQARLFSYPDAHRH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 376 RIGVNYQQLPVNAPRVpYRIANF-QRDGAMAYL-NQGSRPAYLSSIQPNQFRKRTVNLDKTHGHFVGDAVTFLSEIRPED 453
Cdd:cd08157 314 RLGPNYQQLPVNRPKT-SPVYNPyQRDGPMSVNgNYGGDPNYVSSILPPTYFKKRVDADGHHENWVGEVVAFLTEITDED 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 454 FNAPRALWERVWDDGARERFINNVSGHMSNCtKEEIIKRQIAIFREVSNDLATRLEKATG 513
Cdd:cd08157 393 FVQPRALWEVVGKPGQQERFVKNVAGHLSGA-PPEIRKRVYEIFARVNPDLGKRIEKATE 451
|
|
| Catalase |
pfam00199 |
Catalase; |
37-424 |
0e+00 |
|
Catalase;
Pssm-ID: 459708 Cd Length: 383 Bit Score: 716.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 37 TSNGVPIAHPYEAQRVGDNGPLLLQDFHLVDLLSHFDRERIPERVVHAKGGGAHGYYQTTDPLDDLCLADIFQ-AGKKCP 115
Cdd:pfam00199 2 TSNGAPVPDNQNSLTAGPRGPLLLQDFHLIEKLAHFDRERIPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSeVGKKTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 116 ISVRFSTVGGESGSHDCARDPRGFSVKFRTEEGNWDMVANNTPVFFLRDPAKFPHFIHTQKRDPQSHLthaDDSTMFWDY 195
Cdd:pfam00199 82 VFVRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHSQKRDPQTNL---PDPAMFWDF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 196 LSQNPESVHQVMILMGDRGIPDGWRKMHGYAGHTLKLVNKKGDWVYAQMHMKSKQGTDFITQEDS---ANYSPDYAQKDL 272
Cdd:pfam00199 159 WSLNPESLHQVTWLFSDRGIPRSYRHMNGFGVHTFKLVNADGERVYVKFHFKTDQGIKNLTWEEAqklAGKDPDYHTRDL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 273 YQAIEKGDYPGWDVEFQTMTPKEAEDLwetqKINVFDLTHVWPQKQFPRRKVGEFFLNENVKNYFAEIEQIAFNPAHMPP 352
Cdd:pfam00199 239 YEAIERGDYPSWTLYVQVMTEEDAEKF----RFNPFDLTKVWPHKDYPLIEVGKMVLNRNPDNYFAEVEQAAFSPSNLVP 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12407459 353 GIEPSADPVLQSRLFSYPDTHRHRIGVNYQQLPVNAPRVPYriANFQRDGAMAYL-NQGSRPAYlssiQPNQF 424
Cdd:pfam00199 315 GIEPSPDPMLQGRLFSYPDTQRYRLGPNYQQLPVNRPPCPV--HNYQRDGAMRFDiNQGSRPNY----EPNSF 381
|
|
| KatE |
COG0753 |
Catalase [Inorganic ion transport and metabolism]; |
25-515 |
0e+00 |
|
Catalase [Inorganic ion transport and metabolism];
Pssm-ID: 440516 [Multi-domain] Cd Length: 489 Bit Score: 657.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 25 DRNASAEDTVYCTSNGVPIAHPYEAQRVGDNGPLLLQDFHLVDLLSHFDRERIPERVVHAKGGGAHGYYQTTDPLDDLCL 104
Cdd:COG0753 1 GQYADDEGKTLTTNQGAPVADNQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFEVTEDISKYTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 105 ADIFQ-AGKKCPISVRFSTVGGESGSHDCARDPRGFSVKFRTEEGNWDMVANNTPVFFLRDPAKFPHFIHTQKRDPQSHL 183
Cdd:COG0753 81 AKFFQePGKKTPVFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHAQKRDPDTNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 184 thaDDSTMFWDYLSQNPESVHQVMILMGDRGIPDGWRKMHGYAGHTLKLVNKKGDWVYAQMHMKSKQGTDFITQEDSANY 263
Cdd:COG0753 161 ---PQHDTFWDFWSLSPESLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAEGERFWVKFHWKPKQGIHSLTWDEAQKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 264 S---PDYAQKDLYQAIEKGDYPGWDVEFQTMTPKEAEDLwetqKINVFDLTHVWPQKQFPRRKVGEFFLNENVKNYFAEI 340
Cdd:COG0753 238 AgkdPDFHRRDLYEAIERGDFPEWELGVQVMPEEDADKF----DFDPLDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAET 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 341 EQIAFNPAHMPPGIEPSADPVLQSRLFSYPDTHRHRIGVNYQQLPVNAPRVPyrIANFQRDGAMAYLNQGSRPAYlssiQ 420
Cdd:COG0753 314 EQAAFSPGNLVPGIDFSPDKMLQGRLFSYADTQRYRLGPNFHQLPVNRPKCP--VHNYQRDGAMRYDINGGRVNY----E 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 421 PNQF-RKRTVNLDKTHGHFV-GDAVTFLSEiRPEDFNAPRALWeRVWDDGARERFINNVSGHMSNCTKEEIIKRQIAIFR 498
Cdd:COG0753 388 PNSLgGPREDPGFKEPPLKVdGDKVRYRSE-SDDHFSQAGLLY-RSMSDEEKQHLIDNIAFELGKVESEEIRERMVAHFY 465
|
490
....*....|....*..
gi 12407459 499 EVSNDLATRLEKATGVE 515
Cdd:COG0753 466 NVDPELGARVAEALGLD 482
|
|
| Catalase |
smart01060 |
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ... |
39-415 |
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: 644.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 39 NGVPIAHPYEAQRVGDNGPLLLQDFHLVDLLSHFDRERIPERVVHAKGGGAHGYYQTTDPLDDLCLADIFQ-AGKKCPIS 117
Cdd:smart01060 1 QGAPVADNQNSLTAGPRGPVLLQDFHLIEKLAHFDRERIPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQkVGKKTPVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 118 VRFSTVGGESGSHDCARDPRGFSVKFRTEEGNWDMVANNTPVFFLRDPAKFPHFIHTQKRDPQSHLThadDSTMFWDYLS 197
Cdd:smart01060 81 VRFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHAQKRDPRTNLP---DHDMFWDFWS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 198 QNPESVHQVMILMGDRGIPDGWRKMHGYAGHTLKLVNKKGDWVYAQMHMKSKQGTDFITQEDSANYS---PDYAQKDLYQ 274
Cdd:smart01060 158 LNPESLHQVTWLMSDRGIPASYRHMNGFGVHTFKLVNAEGERFYVKFHFKPDQGIKNLTWEEAAKLAgkdPDYHRRDLYE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 275 AIEKGDYPGWDVEFQTMTPKEAEDLwetqKINVFDLTHVWPQKQFPRRKVGEFFLNENVKNYFAEIEQIAFNPAHMPPGI 354
Cdd:smart01060 238 AIERGDYPEWTLYVQVMPEEDAEKF----RFDPFDLTKVWPHKDYPLIEVGKMTLNRNPDNYFAEVEQAAFSPSNLVPGI 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12407459 355 EPSADPVLQSRLFSYPDTHRHRIGVNYQQLPVNAPRVPYriANFQRDGAMAYL-NQGSRPAY 415
Cdd:smart01060 314 EFSPDKMLQGRLFSYPDTQRYRLGPNYHQLPVNRPRCPV--HNYQRDGAMRVDgNQGGDPNY 373
|
|
| PLN02609 |
PLN02609 |
catalase |
26-510 |
1.66e-170 |
|
catalase
Pssm-ID: 215328 [Multi-domain] Cd Length: 492 Bit Score: 492.33 E-value: 1.66e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 26 RNASAEDTVYCTSN-GVPIAHPYEAQRVGDNGPLLLQDFHLVDLLSHFDRERIPERVVHAKGGGAHGYYQTTDPLDDLCL 104
Cdd:PLN02609 7 RPSSAYNSPFFTTNsGAPVWNNNSSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDISNLTC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 105 ADIFQA-GKKCPISVRFSTVGGESGSHDCARDPRGFSVKFRTEEGNWDMVANNTPVFFLRDPAKFPHFIHTQKRDPQshl 183
Cdd:PLN02609 87 ADFLRApGVQTPVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDMVGNNFPVFFIRDGMKFPDMVHALKPNPK--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 184 THADDSTMFWDYLSQNPESVHQVMILMGDRGIPDGWRKMHGYAGHTLKLVNKKGDWVYAQMHMKSKQGTDFITQEDS--- 260
Cdd:PLN02609 164 THIQEPWRILDFLSHHPESLHMFTFLFDDRGIPQDYRHMEGFGVHTYKLINKAGKAHYVKFHWKPTCGVKNLLDEEAvrv 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 261 ANYSPDYAQKDLYQAIEKGDYPGWDVEFQTMTPKEAEDLwetqKINVFDLTHVWPQKQFPRRKVGEFFLNENVKNYFAEI 340
Cdd:PLN02609 244 GGSNHSHATQDLYDSIAAGNYPEWKLFIQTMDPEDEDKF----DFDPLDVTKTWPEDILPLQPVGRLVLNRNIDNFFAEN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 341 EQIAFNPAHMPPGIEPSADPVLQSRLFSYPDTHRHRIGVNYQQLPVNAPRVPYRiaNFQRDGAMAYLNQGSRPAYLssiq 420
Cdd:PLN02609 320 EQLAFCPAIVVPGIYYSDDKLLQTRIFAYADTQRHRLGPNYLQLPVNAPKCAHH--NNHHEGFMNFMHRDEEVNYF---- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 421 PNQFRkrtvnlDKTHGHFVGDAVTFLSEIRP-------EDFNAPRALWeRVWDDGARERFINNVSGHMSNcTKEEIIKRQ 493
Cdd:PLN02609 394 PSRFD------PVRHAERVPIPHPPLSGRREkckiekeNNFKQPGERY-RSWSPDRQERFIKRWVDALSD-PRVTHEIRS 465
|
490
....*....|....*....
gi 12407459 494 IAI--FREVSNDLATRLEK 510
Cdd:PLN02609 466 IWIsyWSQCDKSLGQKLAS 484
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| catalase_fungal |
cd08157 |
Fungal catalases similar to yeast catalases A and T; Catalase is a ubiquitous enzyme found in ... |
60-513 |
0e+00 |
|
Fungal catalases similar to yeast catalases A and T; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes, which is involved in the protection of cells from the toxic effects of peroxides. It catalyzes the conversion of hydrogen peroxide to water and molecular oxygen. Catalases also utilize hydrogen peroxide to oxidize various substrates such as alcohol or phenols. This family of fungal catalases has a relatively small subunit size, and binds a protoheme IX (heme b) group buried deep inside the structure. Fungal catalases also bind NADPH as a second redox-active cofactor. They form tetramers; in eukaryotic cells, catalases are typically located in peroxisomes. Saccharomyces cerevisiae catalase T is found in the cytoplasm, though.
Pssm-ID: 163713 [Multi-domain] Cd Length: 451 Bit Score: 800.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 60 LQDFHLVDLLSHFDRERIPERVVHAKGGGAHGYYQTTDPLDDLCLADIFQA-GKKCPISVRFSTVGGESGSHDCARDPRG 138
Cdd:cd08157 1 LQDFHLIDTLAHFDRERIPERVVHAKGAGAYGEFEVTDDISDITSADMLQGvGKKTPCLVRFSTVGGEKGSADTVRDPRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 139 FSVKFRTEEGNWDMVANNTPVFFLRDPAKFPHFIHTQKRDPQSHLThadDSTMFWDYLSQNPESVHQVMILMGDRGIPDG 218
Cdd:cd08157 81 FAVKFYTEEGNWDWVFNNTPVFFIRDPIKFPHFIHSQKRDPQTNLK---DSTMFWDYLSQNPESIHQVMILFSDRGTPAS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 219 WRKMHGYAGHTLKLVNKKGDWVYAQMHMKSKQGTDFITQEDSANYS---PDYAQKDLYQAIEKGDYPGWDVEFQTMTPKE 295
Cdd:cd08157 158 YRSMNGYSGHTYKWVNPDGSFKYVQFHLKSDQGPKFLTGEEAARLAgsnPDYATKDLFEAIERGDYPSWTVYVQVMTPEQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 296 AEDLwetqKINVFDLTHVWPQKQFPRRKVGEFFLNENVKNYFAEIEQIAFNPAHMPPGIEPSADPVLQSRLFSYPDTHRH 375
Cdd:cd08157 238 AEKL----RFNIFDLTKVWPHKDFPLRPVGKLTLNENPKNYFAEIEQAAFSPSHMVPGIEPSADPVLQARLFSYPDAHRH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 376 RIGVNYQQLPVNAPRVpYRIANF-QRDGAMAYL-NQGSRPAYLSSIQPNQFRKRTVNLDKTHGHFVGDAVTFLSEIRPED 453
Cdd:cd08157 314 RLGPNYQQLPVNRPKT-SPVYNPyQRDGPMSVNgNYGGDPNYVSSILPPTYFKKRVDADGHHENWVGEVVAFLTEITDED 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 454 FNAPRALWERVWDDGARERFINNVSGHMSNCtKEEIIKRQIAIFREVSNDLATRLEKATG 513
Cdd:cd08157 393 FVQPRALWEVVGKPGQQERFVKNVAGHLSGA-PPEIRKRVYEIFARVNPDLGKRIEKATE 451
|
|
| Catalase |
pfam00199 |
Catalase; |
37-424 |
0e+00 |
|
Catalase;
Pssm-ID: 459708 Cd Length: 383 Bit Score: 716.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 37 TSNGVPIAHPYEAQRVGDNGPLLLQDFHLVDLLSHFDRERIPERVVHAKGGGAHGYYQTTDPLDDLCLADIFQ-AGKKCP 115
Cdd:pfam00199 2 TSNGAPVPDNQNSLTAGPRGPLLLQDFHLIEKLAHFDRERIPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSeVGKKTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 116 ISVRFSTVGGESGSHDCARDPRGFSVKFRTEEGNWDMVANNTPVFFLRDPAKFPHFIHTQKRDPQSHLthaDDSTMFWDY 195
Cdd:pfam00199 82 VFVRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHSQKRDPQTNL---PDPAMFWDF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 196 LSQNPESVHQVMILMGDRGIPDGWRKMHGYAGHTLKLVNKKGDWVYAQMHMKSKQGTDFITQEDS---ANYSPDYAQKDL 272
Cdd:pfam00199 159 WSLNPESLHQVTWLFSDRGIPRSYRHMNGFGVHTFKLVNADGERVYVKFHFKTDQGIKNLTWEEAqklAGKDPDYHTRDL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 273 YQAIEKGDYPGWDVEFQTMTPKEAEDLwetqKINVFDLTHVWPQKQFPRRKVGEFFLNENVKNYFAEIEQIAFNPAHMPP 352
Cdd:pfam00199 239 YEAIERGDYPSWTLYVQVMTEEDAEKF----RFNPFDLTKVWPHKDYPLIEVGKMVLNRNPDNYFAEVEQAAFSPSNLVP 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12407459 353 GIEPSADPVLQSRLFSYPDTHRHRIGVNYQQLPVNAPRVPYriANFQRDGAMAYL-NQGSRPAYlssiQPNQF 424
Cdd:pfam00199 315 GIEPSPDPMLQGRLFSYPDTQRYRLGPNYQQLPVNRPPCPV--HNYQRDGAMRFDiNQGSRPNY----EPNSF 381
|
|
| KatE |
COG0753 |
Catalase [Inorganic ion transport and metabolism]; |
25-515 |
0e+00 |
|
Catalase [Inorganic ion transport and metabolism];
Pssm-ID: 440516 [Multi-domain] Cd Length: 489 Bit Score: 657.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 25 DRNASAEDTVYCTSNGVPIAHPYEAQRVGDNGPLLLQDFHLVDLLSHFDRERIPERVVHAKGGGAHGYYQTTDPLDDLCL 104
Cdd:COG0753 1 GQYADDEGKTLTTNQGAPVADNQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFEVTEDISKYTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 105 ADIFQ-AGKKCPISVRFSTVGGESGSHDCARDPRGFSVKFRTEEGNWDMVANNTPVFFLRDPAKFPHFIHTQKRDPQSHL 183
Cdd:COG0753 81 AKFFQePGKKTPVFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHAQKRDPDTNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 184 thaDDSTMFWDYLSQNPESVHQVMILMGDRGIPDGWRKMHGYAGHTLKLVNKKGDWVYAQMHMKSKQGTDFITQEDSANY 263
Cdd:COG0753 161 ---PQHDTFWDFWSLSPESLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAEGERFWVKFHWKPKQGIHSLTWDEAQKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 264 S---PDYAQKDLYQAIEKGDYPGWDVEFQTMTPKEAEDLwetqKINVFDLTHVWPQKQFPRRKVGEFFLNENVKNYFAEI 340
Cdd:COG0753 238 AgkdPDFHRRDLYEAIERGDFPEWELGVQVMPEEDADKF----DFDPLDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAET 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 341 EQIAFNPAHMPPGIEPSADPVLQSRLFSYPDTHRHRIGVNYQQLPVNAPRVPyrIANFQRDGAMAYLNQGSRPAYlssiQ 420
Cdd:COG0753 314 EQAAFSPGNLVPGIDFSPDKMLQGRLFSYADTQRYRLGPNFHQLPVNRPKCP--VHNYQRDGAMRYDINGGRVNY----E 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 421 PNQF-RKRTVNLDKTHGHFV-GDAVTFLSEiRPEDFNAPRALWeRVWDDGARERFINNVSGHMSNCTKEEIIKRQIAIFR 498
Cdd:COG0753 388 PNSLgGPREDPGFKEPPLKVdGDKVRYRSE-SDDHFSQAGLLY-RSMSDEEKQHLIDNIAFELGKVESEEIRERMVAHFY 465
|
490
....*....|....*..
gi 12407459 499 EVSNDLATRLEKATGVE 515
Cdd:COG0753 466 NVDPELGARVAEALGLD 482
|
|
| Catalase |
smart01060 |
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ... |
39-415 |
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: 644.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 39 NGVPIAHPYEAQRVGDNGPLLLQDFHLVDLLSHFDRERIPERVVHAKGGGAHGYYQTTDPLDDLCLADIFQ-AGKKCPIS 117
Cdd:smart01060 1 QGAPVADNQNSLTAGPRGPVLLQDFHLIEKLAHFDRERIPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQkVGKKTPVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 118 VRFSTVGGESGSHDCARDPRGFSVKFRTEEGNWDMVANNTPVFFLRDPAKFPHFIHTQKRDPQSHLThadDSTMFWDYLS 197
Cdd:smart01060 81 VRFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHAQKRDPRTNLP---DHDMFWDFWS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 198 QNPESVHQVMILMGDRGIPDGWRKMHGYAGHTLKLVNKKGDWVYAQMHMKSKQGTDFITQEDSANYS---PDYAQKDLYQ 274
Cdd:smart01060 158 LNPESLHQVTWLMSDRGIPASYRHMNGFGVHTFKLVNAEGERFYVKFHFKPDQGIKNLTWEEAAKLAgkdPDYHRRDLYE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 275 AIEKGDYPGWDVEFQTMTPKEAEDLwetqKINVFDLTHVWPQKQFPRRKVGEFFLNENVKNYFAEIEQIAFNPAHMPPGI 354
Cdd:smart01060 238 AIERGDYPEWTLYVQVMPEEDAEKF----RFDPFDLTKVWPHKDYPLIEVGKMTLNRNPDNYFAEVEQAAFSPSNLVPGI 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12407459 355 EPSADPVLQSRLFSYPDTHRHRIGVNYQQLPVNAPRVPYriANFQRDGAMAYL-NQGSRPAY 415
Cdd:smart01060 314 EFSPDKMLQGRLFSYPDTQRYRLGPNYHQLPVNRPRCPV--HNYQRDGAMRVDgNQGGDPNY 373
|
|
| catalase_clade_3 |
cd08156 |
Clade 3 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
76-511 |
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: 603.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 76 RIPERVVHAKGGGAHGYYQTTDPLDDLCLADIFQ-AGKKCPISVRFSTVGGESGSHDCARDPRGFSVKFRTEEGNWDMVA 154
Cdd:cd08156 1 RIPERVVHAKGAGAFGTFEVTHDITKYTKAKIFSeVGKKTPVFVRFSTVAGERGSADTERDPRGFALKFYTEEGNWDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 155 NNTPVFFLRDPAKFPHFIHTQKRDPQSHLThadDSTMFWDYLSQNPESVHQVMILMGDRGIPDGWRKMHGYAGHTLKLVN 234
Cdd:cd08156 81 NNTPVFFIRDPIKFPDFIHTQKRNPQTNLK---DPDMFWDFWSLSPESLHQVTILFSDRGIPDGYRHMNGYGSHTFSLVN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 235 KKGDWVYAQMHMKSKQGTDFITQEDSANYS---PDYAQKDLYQAIEKGDYPGWDVEFQTMTPKEAEdlweTQKINVFDLT 311
Cdd:cd08156 158 AKGERFWVKFHFKTDQGIKNLTNEEAAELAgedPDYAQRDLFEAIERGDFPSWTLYVQVMPEEDAE----KYRFNPFDLT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 312 HVWPQKQFPRRKVGEFFLNENVKNYFAEIEQIAFNPAHMPPGIEPSADPVLQSRLFSYPDTHRHRIGVNYQQLPVNAPRV 391
Cdd:cd08156 234 KVWPHKDYPLIEVGKLELNRNPENYFAEVEQAAFSPSNLVPGIGFSPDKMLQGRLFSYADAHRYRLGVNYHQLPVNRPKC 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 392 PYRiaNFQRDGAMAYL-NQGSRPAYlssiQPNQFRKRTVNLDKTHGHFV--GDAVTFLSEIRPEDFNAPRALWERVwDDG 468
Cdd:cd08156 314 PVN--NYQRDGAMRVDgNGGGAPNY----EPNSFGGPPEDPEYAEPPLPvsGDADRYNYRDDDDDYTQAGDLYRLV-SED 386
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 12407459 469 ARERFINNVSGHMSNCtKEEIIKRQIAIFREVSNDLATRLEKA 511
Cdd:cd08156 387 ERERLVENIAGHLKGA-PEFIQERQVAHFYKADPDYGERVAKA 428
|
|
| catalase_clade_1 |
cd08154 |
Clade 1 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
37-512 |
5.95e-172 |
|
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: 495.28 E-value: 5.95e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 37 TSNGVPIAHPYEAQRVGDNGPLLLQDFHLVDLLSHFDRERIPERVVHAKGGGAHGYYQTTDPLDDLCLADIFQA-GKKCP 115
Cdd:cd08154 4 TNQGAPVGDNQNSQTVGPRGPVLLEDYHLIEKLAHFDRERIPERVVHARGAGAHGYFEAYGDISDYTRASFLQEpGKKTP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 116 ISVRFSTVGGESGSHDCARDPRGFSVKFRTEEGNWDMVANNTPVFFLRDPAKFPHFIHTQKRDPQSHLthaDDSTMFWDY 195
Cdd:cd08154 84 VFVRFSTVIHGKGSPETLRDPRGFAVKFYTEEGNWDLVGNNLPVFFIRDAIKFPDMIHALKPSPVTNI---QDPNRIFDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 196 LSQNPESVHQVMILMGDRGIPDGWRKMHGYAGHTLKLVNKKGDWVYAQMHMKSKQGTDFITQEDSANYS---PDYAQKDL 272
Cdd:cd08154 161 FSHVPESTHMLTFLYSDWGTPASYRHMDGSGVHTYKWVNAEGKVVYVKYHWKPKQGVKNLTAEEAAEVQgknFNHATQDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 273 YQAIEKGDYPGWDVEFQTMTPKEAEDLwetqKINVFDLTHVWPQKQFPRRKVGEFFLNENVKNYFAEIEQIAFNPAHMPP 352
Cdd:cd08154 241 YDAIAAGNYPEWELYVQIMDPKDLDKL----DFDPLDDTKIWPEDQFPLKPVGKMTLNKNPDNFFAEVEQVAFSPGNLVP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 353 GIEPSADPVLQSRLFSYPDTHRHRIGVNYQQLPVNAPRVPyrIANFQRDGAMAYLNQGSRPAYlssiQPNQFRK-RTVNL 431
Cdd:cd08154 317 GIEPSDDKMLQGRLFSYSDTQRYRLGPNYLQLPINAPKAA--VHNNQRDGQMNYGHDTSDVNY----EPSRLDGlPEAPK 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 432 DKTHGHFVGDAVTFLSEIRPEDFNAPRALWeRVWDDGARERFINNVSGHMSNCTkEEIIKRQIAIFREVSNDLATRLEKA 511
Cdd:cd08154 391 YPYSQPPLSGTTQQAPIAKTNNFKQAGERY-RSFSEEEQENLIKNLVVDLSDVN-EEIKLRMLSYFSQADPDYGERVAEG 468
|
.
gi 12407459 512 T 512
Cdd:cd08154 469 L 469
|
|
| PLN02609 |
PLN02609 |
catalase |
26-510 |
1.66e-170 |
|
catalase
Pssm-ID: 215328 [Multi-domain] Cd Length: 492 Bit Score: 492.33 E-value: 1.66e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 26 RNASAEDTVYCTSN-GVPIAHPYEAQRVGDNGPLLLQDFHLVDLLSHFDRERIPERVVHAKGGGAHGYYQTTDPLDDLCL 104
Cdd:PLN02609 7 RPSSAYNSPFFTTNsGAPVWNNNSSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDISNLTC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 105 ADIFQA-GKKCPISVRFSTVGGESGSHDCARDPRGFSVKFRTEEGNWDMVANNTPVFFLRDPAKFPHFIHTQKRDPQshl 183
Cdd:PLN02609 87 ADFLRApGVQTPVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDMVGNNFPVFFIRDGMKFPDMVHALKPNPK--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 184 THADDSTMFWDYLSQNPESVHQVMILMGDRGIPDGWRKMHGYAGHTLKLVNKKGDWVYAQMHMKSKQGTDFITQEDS--- 260
Cdd:PLN02609 164 THIQEPWRILDFLSHHPESLHMFTFLFDDRGIPQDYRHMEGFGVHTYKLINKAGKAHYVKFHWKPTCGVKNLLDEEAvrv 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 261 ANYSPDYAQKDLYQAIEKGDYPGWDVEFQTMTPKEAEDLwetqKINVFDLTHVWPQKQFPRRKVGEFFLNENVKNYFAEI 340
Cdd:PLN02609 244 GGSNHSHATQDLYDSIAAGNYPEWKLFIQTMDPEDEDKF----DFDPLDVTKTWPEDILPLQPVGRLVLNRNIDNFFAEN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 341 EQIAFNPAHMPPGIEPSADPVLQSRLFSYPDTHRHRIGVNYQQLPVNAPRVPYRiaNFQRDGAMAYLNQGSRPAYLssiq 420
Cdd:PLN02609 320 EQLAFCPAIVVPGIYYSDDKLLQTRIFAYADTQRHRLGPNYLQLPVNAPKCAHH--NNHHEGFMNFMHRDEEVNYF---- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 421 PNQFRkrtvnlDKTHGHFVGDAVTFLSEIRP-------EDFNAPRALWeRVWDDGARERFINNVSGHMSNcTKEEIIKRQ 493
Cdd:PLN02609 394 PSRFD------PVRHAERVPIPHPPLSGRREkckiekeNNFKQPGERY-RSWSPDRQERFIKRWVDALSD-PRVTHEIRS 465
|
490
....*....|....*....
gi 12407459 494 IAI--FREVSNDLATRLEK 510
Cdd:PLN02609 466 IWIsyWSQCDKSLGQKLAS 484
|
|
| catalase |
cd00328 |
Catalase heme-binding enzyme; Catalase is a ubiquitous enzyme found in both prokaryotes and ... |
76-511 |
5.43e-167 |
|
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: 481.19 E-value: 5.43e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 76 RIPERVVHAKGGGAHGYYQTTDPLDDLCLADIFQA-GKKCPISVRFSTVGGESGSHDCARDPRGFSVKFRTEEGNWDMVA 154
Cdd:cd00328 1 RIPERVVHARGAGAFGYFTAYGDWSDISAAAFFSAiGKKTPVFVRFSTVVGGAGSADTVRDPHGFATKFYTEEGNFDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 155 NNTPVFFLRDPAKFPHFIHTQKRDPQSHLTHADdstMFWDYLSQNPESVHQVMILMGDRGIPDGWRKMHGYAGHTLKLVN 234
Cdd:cd00328 81 NNTPIFFIRDAIKFPDFIHAQKPNPQTALPDAD---RFWDFLSLRPESLHQVSFLFSDRGIPAAYRHMNGYGSHTFKLVN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 235 KKGDWVYAQMHMKSKQGTDFITQEDSANYS---PDYAQKDLYQAIEKGDYPGWDVEFQTMTPKEAEdlweTQKINVFDLT 311
Cdd:cd00328 158 ANGKVHYVKFHWKTDQGIANLVWEEAARLAgedPDYHRQDLFEAIEAGDYPSWELYIQVMTFNDAE----KFPFNPLDPT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 312 HVWPQKQFPRRKVGEFFLNENVKNYFAEIEQIAFNPAHMPPGIEPSADPVLQSRLFSYPDTHRHRIGVNYQQLPVNAPRV 391
Cdd:cd00328 234 KVWPEELVPLIVVGKLVLNRNPLNFFAEVEQAAFDPGHIVPGVEFSEDPLLQGRLFSYADTQLYRLGPNFQQLPVNRPYA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 392 PYriANFQRDGAMAYLNQGSRPAYL-SSIQPNQFRKRTVNLDKTHG-HFVGDAVTFLSEIRPEDFNAPRALWeRVWDDGA 469
Cdd:cd00328 314 PV--HNNQRDGAGNMNDNTGVPNYEpNAKDVRYPAQGAPKFDRGHFsHWKSGVNREASTTNDDNFTQARLFY-RSLTPGQ 390
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 12407459 470 RERFINNVSGHMSNCTKEEIIKRQIAIFREVSNDLATRLEKA 511
Cdd:cd00328 391 QKRLVDAFRFELADAVSPQIQQRVLDQFAKVDAAAAKRVAKA 432
|
|
| catalase_clade_2 |
cd08155 |
Clade 2 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
73-511 |
8.52e-128 |
|
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: 381.72 E-value: 8.52e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 73 DRERIPERVVHAKGGGAHGYYQTTDPLDDLCLADIFQ-AGKKCPISVRFSTVGGESGSHDCARDPRGFSVKFRTEEGNWD 151
Cdd:cd08155 1 DHERIPERVVHARGSGAHGYFQVYESLSQYTKAKFLQdPGKKTPVFVRFSTVAGSRGSADTVRDVRGFAVKFYTEEGNYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 152 MVANNTPVFFLRDPAKFPHFIHTQKRDPQSHLTH---ADDStmFWDYLSQNPESVHQVMILMGDRGIPDGWRKMHGYAGH 228
Cdd:cd08155 81 LVGNNIPVFFIQDAIKFPDLIHAVKPEPHNEMPQaqsAHDT--FWDFVSLQPESAHMVMWAMSDRAIPRSYRMMEGFGVH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 229 TLKLVNKKGDWVYAQMHMKSKQGTDFITQEDS---ANYSPDYAQKDLYQAIEKGDYPGWDVEFQtMTPKEAEDLWEtqkI 305
Cdd:cd08155 159 TFRLVNAQGKSTFVKFHWKPVLGVHSLVWDEAqkiAGKDPDFHRRDLWEAIESGDYPEWELGVQ-LIDEEDEFKFD---F 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 306 NVFDLTHVWPQKQFPRRKVGEFFLNENVKNYFAEIEQIAFNPAHMPPGIEPSADPVLQSRLFSYPDTHRHRIG-VNYQQL 384
Cdd:cd08155 235 DILDPTKLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFCPANVVPGIDFSNDPLLQGRLFSYLDTQLSRLGgPNFHEL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 385 PVNAPRVPYRiaNFQRDGAMAYLNQGSRPAYlssiQPNQFRK-RTVNLDKTHGHFV-------GDAVTFLSEIRPEDFNA 456
Cdd:cd08155 315 PINRPVCPVH--NNQRDGHMRMTINKGRVNY----FPNSLGAgPPRAASPAEGGFVhypekveGPKIRIRSESFADHYSQ 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 12407459 457 PRALWERVwDDGARERFINNVSGHMSNCTKEEIIKRQIAIFREVSNDLATRLEKA 511
Cdd:cd08155 389 ARLFWNSM-SPVEKEHIISAFTFELSKVETPEIRERVVDHLANIDEDLAKKVAKG 442
|
|
| katE |
PRK11249 |
hydroperoxidase II; Provisional |
3-402 |
2.69e-124 |
|
hydroperoxidase II; Provisional
Pssm-ID: 236886 [Multi-domain] Cd Length: 752 Bit Score: 382.86 E-value: 2.69e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 3 PSATAHSADGRTTGDIHRDYNDDRnASAEDTVYCTSNGVPIAHPYEAQRVGDNGPLLLQDFHLVDLLSHFDRERIPERVV 82
Cdd:PRK11249 46 PTAPGSLKAPDTRNEKLNSLEAFR-KGSEGYALTTNQGVRIADDQNSLRAGSRGPSLLEDFILREKITHFDHERIPERIV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 83 HAKGGGAHGYYQTTDPLDDLCLADIFQ-AGKKCPISVRFSTVGGESGSHDCARDPRGFSVKFRTEEGNWDMVANNTPVFF 161
Cdd:PRK11249 125 HARGSAAHGYFQPYKSLSDITKAAFLQdPGKITPVFVRFSTVQGPRGSADTVRDIRGFATKFYTEEGNFDLVGNNTPVFF 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 162 LRDPAKFPHFIHTQKRDPQSHL-THADDSTMFWDYLSQNPESVHQVMILMGDRGIPDGWRKMHGYAGHTLKLVNKKGDWV 240
Cdd:PRK11249 205 IQDAIKFPDFVHAVKPEPHNEIpQGQSAHDTFWDYVSLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLINAEGKAT 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 241 YAQMHMKSKQGTDFITQEDS---ANYSPDYAQKDLYQAIEKGDYPGWDVEFQtMTPKEAEDLWEtqkinvFDL---THVW 314
Cdd:PRK11249 285 FVRFHWKPVAGKASLVWDEAqklTGRDPDFHRRDLWEAIEAGDYPEYELGVQ-LIPEEDEFKFD------FDLldpTKLI 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 315 PQKQFPRRKVGEFFLNENVKNYFAEIEQIAFNPAHMPPGIEPSADPVLQSRLFSYPDTHRHRI-GVNYQQLPVNAPRVPY 393
Cdd:PRK11249 358 PEELVPVQRVGKMVLNRNPDNFFAETEQVAFHPGHIVPGIDFTNDPLLQGRLFSYTDTQISRLgGPNFHEIPINRPTCPY 437
|
....*....
gi 12407459 394 riANFQRDG 402
Cdd:PRK11249 438 --HNFQRDG 444
|
|
| catalase_like |
cd08150 |
Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found ... |
78-376 |
2.19e-53 |
|
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: 183.14 E-value: 2.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 78 PERVVHAKGGGAHGYYQTTDPLDDLCLADIFQAGKKCPISVRFSTVGgesGSHDCARDPRGFSVKFRTE--EGNWDMVAN 155
Cdd:cd08150 1 GLRGQHFQGTCAFGTFEVLADLKERLRVGLFAEGKVYPAYIRFSNGA---GIDDTKPDIRGFAIKFTGVadAGTLDFVLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 156 NTPVFFLRDPAKFPHFIHTQKRDPQSHLTHAddstMFWDYLSQNPESVHQVMILMgdRGIPDGWRKMHGYAGHTLKLVNK 235
Cdd:cd08150 78 NTPVFFIRNTSDYEDFVAEFARSARGEPPLD----FIAWYVEKRPEDLPNLLGAR--SQVPDSYAAARYFSQVTFAFING 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 236 KGDWVYAQMHMKSKQGTDFITQEDSANYSPDYAQKDLYQAIEKGdYPGWDVEFQTMTPKEAEDLwetqkinvFDLTHVWP 315
Cdd:cd08150 152 AGKYRVVRSKDNPVDGIPSLEDHELEARPPDYLREELTERLQRG-PVVYDFRIQLNDDTDATTI--------DNPTILWP 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12407459 316 qKQFPRRKVGEFFLNENVKNyfAEIEQIAFNPAHMPPGIEPSAD--PVLQSRLFSYPDTHRHR 376
Cdd:cd08150 223 -TEHPVEAVAKITIPPPTFT--AAQEAFAFNPFTPWHGLLETNDlgPILEVRRRVYTSSQGLR 282
|
|
| srpA_like |
cd08153 |
Catalase-like heme-binding proteins similar to the uncharacterized srpA; Catalase is a ... |
80-376 |
7.55e-34 |
|
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: 130.43 E-value: 7.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 80 RVVHAKGGGAHGYYQTTDPLDDLCLADIFQaGKKCPISVRFSTVGGESGSHDCARDPRGFSVKFRTEEGN-WDMVANNTP 158
Cdd:cd08153 15 RRNHAKGICVSGTFTPSGAAASLSRAPLFS-GGSVPVTGRFSLGGGNPKAPDDAANPRGMALKFRLPDGEqWRMVMNSFP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 159 VFFLRDPAKFPHFIHTQKRDPqshlTHADDSTMFWDYLSQNPESVHQVMiLMGDRGIPDGWRKMHGYAGHTLKLVNKKGD 238
Cdd:cd08153 94 VFPVRTPEEFLALLKAIAPDA----TGKPDPAKLKAFLAAHPEAAAFLA-WIKTAPPPASFANTTYYGVNAFYFTNANGK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 239 WVYAQMHMKSKQGTDFITQEDSANYSPDYAQKDLYQAIEKGdyP-GWDVEFQTMTPKEAEDlwetqkinvfDLTHVWPQK 317
Cdd:cd08153 169 RQPVRWRFVPEDGVKYLSDEEAAKLGPDFLFDELAQRLAQG--PvRWDLVLQLAEPGDPTD----------DPTKPWPAD 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12407459 318 qfpRRKV--GEFFLNENVKNYFAEIEQIAFNPAHMPPGIEPSADPVLQSRLFSYPDTHRHR 376
Cdd:cd08153 237 ---RKEVdaGTLTITKVAPDQGGACRDINFDPLVLPDGIEPSDDPLLAARSAAYAVSFSRR 294
|
|
| Catalase-rel |
pfam06628 |
Catalase-related immune-responsive; This family represents a small conserved region within ... |
450-511 |
3.07e-17 |
|
Catalase-related immune-responsive; This family represents a small conserved region within catalase enzymes (EC:1.11.1.6). All members also contain the Catalase family, pfam00199 domain. Catalase decomposes hydrogen peroxide into water and oxygen, serving to protect cells from its toxic effects. This domain carries the immune-responsive amphipathic octa-peptide that is recognized by T cells.
Pssm-ID: 461967 [Multi-domain] Cd Length: 65 Bit Score: 75.86 E-value: 3.07e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12407459 450 RPEDFNAPRALWeRVWDDGARERFINNVSGHMSNCTKEEIIKRQIAIFREVSNDLATRLEKA 511
Cdd:pfam06628 4 FDDHFSQAGLFY-RSMSEEERQRLVDNIAFELSKVTDPEIQERMVAHFYKVDPDLGQRVAEA 64
|
|
| y4iL_like |
cd08152 |
Catalase-like heme-binding proteins similar to the uncharacterized y4iL; Catalase is a ... |
80-168 |
5.96e-06 |
|
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: 48.41 E-value: 5.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12407459 80 RVVHAKG-GGAHGYYQTTDPLDDLCLADIFQAGKKCPISVRFSTVGGESGShDCARDPRGFSVK----------FRTEEG 148
Cdd:cd08152 5 RDAHAKShGCLKAEFTVLDDLPPELAQGLFAEPGTYPAVIRFSNAPGDILD-DSVPDPRGMAIKvlgvpgekllPEEDAT 83
|
90 100
....*....|....*....|
gi 12407459 149 NWDMVANNTPVFFLRDPAKF 168
Cdd:cd08152 84 TQDFVLVNHPVFFARDAKDY 103
|
|
| |
