|
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 ... |
47-502 |
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: 828.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 47 LQDYNLIDSLAHFNRENIPQRNPHAHGSGAFGYFEVTDDITDICGSAMFSKIGKRTKCLTRFSTVGGDKGSADTVRDPRG 126
Cdd:cd08157 1 LQDFHLIDTLAHFDRERIPERVVHAKGAGAYGEFEVTDDISDITSADMLQGVGKKTPCLVRFSTVGGEKGSADTVRDPRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 127 FATKFYTEEGNLDWVYNNTPVFFIRDPSKFPHFIHTQKRNPQTNLRDADMFWDFLTTpeNQVAIHQVMILFSDRGTPANY 206
Cdd:cd08157 81 FAVKFYTEEGNWDWVFNNTPVFFIRDPIKFPHFIHSQKRDPQTNLKDSTMFWDYLSQ--NPESIHQVMILFSDRGTPASY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 207 RSMHGYSGHTYKWSNKNGDWHYVQVHIKTDQGIKNLTIEEATKIAGSNPDYCQQDLFEAIQNGNYPSWTVYIQTMTERDA 286
Cdd:cd08157 159 RSMNGYSGHTYKWVNPDGSFKYVQFHLKSDQGPKFLTGEEAARLAGSNPDYATKDLFEAIERGDYPSWTVYVQVMTPEQA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 287 KKLPFSVFDLTKVWPQGQFPLRRVGKIVLNENPLNFFAQVEQAAFAPSTTVPYQEASADPVLQARLFSYADAHRYRLGPN 366
Cdd:cd08157 239 EKLRFNIFDLTKVWPHKDFPLRPVGKLTLNENPKNYFAEIEQAAFSPSHMVPGIEPSADPVLQARLFSYPDAHRHRLGPN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 367 FHQIPVNCPYASKFFNPAIRDGPMNVNGNFGSEPTYLANDKSYTYIQQDRPIQQHQEVWNGpaIPYHWATSPGDVDFVQA 446
Cdd:cd08157 319 YQQLPVNRPKTSPVYNPYQRDGPMSVNGNYGGDPNYVSSILPPTYFKKRVDADGHHENWVG--EVVAFLTEITDEDFVQP 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 6320462 447 RNLYRVLGkQPGQQKNLAYNIGIHVEGACPQIQQRVYDMFARVDKGLSEAIKKVAE 502
Cdd:cd08157 397 RALWEVVG-KPGQQERFVKNVAGHLSGAPPEIRKRVYEIFARVNPDLGKRIEKATE 451
|
|
| Catalase |
pfam00199 |
Catalase; |
23-405 |
0e+00 |
|
Catalase;
Pssm-ID: 459708 Cd Length: 383 Bit Score: 739.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 23 TNSTGNPINEPFVTQRIGEHGPLLLQDYNLIDSLAHFNRENIPQRNPHAHGSGAFGYFEVTDDITDICGSAMFSKIGKRT 102
Cdd:pfam00199 1 TTSNGAPVPDNQNSLTAGPRGPLLLQDFHLIEKLAHFDRERIPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSEVGKKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 103 KCLTRFSTVGGDKGSADTVRDPRGFATKFYTEEGNLDWVYNNTPVFFIRDPSKFPHFIHTQKRNPQTNLRDADMFWDFLT 182
Cdd:pfam00199 81 PVFVRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHSQKRDPQTNLPDPAMFWDFWS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 183 -TPEnqvAIHQVMILFSDRGTPANYRSMHGYSGHTYKWSNKNGDWHYVQVHIKTDQGIKNLTIEEATKIAGSNPDYCQQD 261
Cdd:pfam00199 161 lNPE---SLHQVTWLFSDRGIPRSYRHMNGFGVHTFKLVNADGERVYVKFHFKTDQGIKNLTWEEAQKLAGKDPDYHTRD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 262 LFEAIQNGNYPSWTVYIQTMTERDAKKLPFSVFDLTKVWPQGQFPLRRVGKIVLNENPLNFFAQVEQAAFAPSTTVPYQE 341
Cdd:pfam00199 238 LYEAIERGDYPSWTLYVQVMTEEDAEKFRFNPFDLTKVWPHKDYPLIEVGKMVLNRNPDNYFAEVEQAAFSPSNLVPGIE 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6320462 342 ASADPVLQARLFSYADAHRYRLGPNFHQIPVNCPYASkfFNPAIRDGPMNVNGNFGSEPTYLAN 405
Cdd:pfam00199 318 PSPDPMLQGRLFSYPDTQRYRLGPNYQQLPVNRPPCP--VHNYQRDGAMRFDINQGSRPNYEPN 379
|
|
| Catalase |
smart01060 |
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ... |
27-402 |
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: 685.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 27 GNPINEPFVTQRIGEHGPLLLQDYNLIDSLAHFNRENIPQRNPHAHGSGAFGYFEVTDDITDICGSAMFSKIGKRTKCLT 106
Cdd:smart01060 2 GAPVADNQNSLTAGPRGPVLLQDFHLIEKLAHFDRERIPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQKVGKKTPVFV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 107 RFSTVGGDKGSADTVRDPRGFATKFYTEEGNLDWVYNNTPVFFIRDPSKFPHFIHTQKRNPQTNLRDADMFWDFLT-TPE 185
Cdd:smart01060 82 RFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHAQKRDPRTNLPDHDMFWDFWSlNPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 186 nqvAIHQVMILFSDRGTPANYRSMHGYSGHTYKWSNKNGDWHYVQVHIKTDQGIKNLTIEEATKIAGSNPDYCQQDLFEA 265
Cdd:smart01060 162 ---SLHQVTWLMSDRGIPASYRHMNGFGVHTFKLVNAEGERFYVKFHFKPDQGIKNLTWEEAAKLAGKDPDYHRRDLYEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 266 IQNGNYPSWTVYIQTMTERDAKKLPFSVFDLTKVWPQGQFPLRRVGKIVLNENPLNFFAQVEQAAFAPSTTVPYQEASAD 345
Cdd:smart01060 239 IERGDYPEWTLYVQVMPEEDAEKFRFDPFDLTKVWPHKDYPLIEVGKMTLNRNPDNYFAEVEQAAFSPSNLVPGIEFSPD 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 6320462 346 PVLQARLFSYADAHRYRLGPNFHQIPVNCPYASkfFNPAIRDGPMNVNGNFGSEPTY 402
Cdd:smart01060 319 KMLQGRLFSYPDTQRYRLGPNYHQLPVNRPRCP--VHNYQRDGAMRVDGNQGGDPNY 373
|
|
| KatE |
COG0753 |
Catalase [Inorganic ion transport and metabolism]; |
18-503 |
0e+00 |
|
Catalase [Inorganic ion transport and metabolism];
Pssm-ID: 440516 [Multi-domain] Cd Length: 489 Bit Score: 676.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 18 EDRVVTNSTGNPINEPFVTQRIGEHGPLLLQDYNLIDSLAHFNRENIPQRNPHAHGSGAFGYFEVTDDITDICGSAMFSK 97
Cdd:COG0753 7 EGKTLTTNQGAPVADNQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFEVTEDISKYTKAKFFQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 98 IGKRTKCLTRFSTVGGDKGSADTVRDPRGFATKFYTEEGNLDWVYNNTPVFFIRDPSKFPHFIHTQKRNPQTNLRDADMF 177
Cdd:COG0753 87 PGKKTPVFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHAQKRDPDTNLPQHDTF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 178 WDFLT-TPEnqvAIHQVMILFSDRGTPANYRSMHGYSGHTYKWSNKNGDWHYVQVHIKTDQGIKNLTIEEATKIAGSNPD 256
Cdd:COG0753 167 WDFWSlSPE---SLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAEGERFWVKFHWKPKQGIHSLTWDEAQKIAGKDPD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 257 YCQQDLFEAIQNGNYPSWTVYIQTMTERDAKKLPFSVFDLTKVWPQGQFPLRRVGKIVLNENPLNFFAQVEQAAFAPSTT 336
Cdd:COG0753 244 FHRRDLYEAIERGDFPEWELGVQVMPEEDADKFDFDPLDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAETEQAAFSPGNL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 337 VPYQEASADPVLQARLFSYADAHRYRLGPNFHQIPVNCPYASkfFNPAIRDGPMNVNGNfGSEPTYLANdkSYTYIQQDR 416
Cdd:COG0753 324 VPGIDFSPDKMLQGRLFSYADTQRYRLGPNFHQLPVNRPKCP--VHNYQRDGAMRYDIN-GGRVNYEPN--SLGGPREDP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 417 PIQQHQEVWNGPAIpyhWATSPGDVDFVQARNLYRVLGkqPGQQKNLAYNIGIHVEGA-CPQIQQRVYDMFARVDKGLSE 495
Cdd:COG0753 399 GFKEPPLKVDGDKV---RYRSESDDHFSQAGLLYRSMS--DEEKQHLIDNIAFELGKVeSEEIRERMVAHFYNVDPELGA 473
|
....*...
gi 6320462 496 aikKVAEA 503
Cdd:COG0753 474 ---RVAEA 478
|
|
| PLN02609 |
PLN02609 |
catalase |
23-504 |
1.22e-174 |
|
catalase
Pssm-ID: 215328 [Multi-domain] Cd Length: 492 Bit Score: 500.81 E-value: 1.22e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 23 TNSTGNPINEPFVTQRIGEHGPLLLQDYNLIDSLAHFNRENIPQRNPHAHGSGAFGYFEVTDDITDICGSAMFSKIGKRT 102
Cdd:PLN02609 18 TTNSGAPVWNNNSSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDISNLTCADFLRAPGVQT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 103 KCLTRFSTVGGDKGSADTVRDPRGFATKFYTEEGNLDWVYNNTPVFFIRDPSKFPHFIHTQKRNPQTNLRDADMFWDFLT 182
Cdd:PLN02609 98 PVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDMVGNNFPVFFIRDGMKFPDMVHALKPNPKTHIQEPWRILDFLS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 183 -TPEnqvAIHQVMILFSDRGTPANYRSMHGYSGHTYKWSNKNGDWHYVQVHIKTDQGIKNLTIEEATKIAGSNPDYCQQD 261
Cdd:PLN02609 178 hHPE---SLHMFTFLFDDRGIPQDYRHMEGFGVHTYKLINKAGKAHYVKFHWKPTCGVKNLLDEEAVRVGGSNHSHATQD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 262 LFEAIQNGNYPSWTVYIQTMTERDAKKLPFSVFDLTKVWPQGQFPLRRVGKIVLNENPLNFFAQVEQAAFAPSTTVPYQE 341
Cdd:PLN02609 255 LYDSIAAGNYPEWKLFIQTMDPEDEDKFDFDPLDVTKTWPEDILPLQPVGRLVLNRNIDNFFAENEQLAFCPAIVVPGIY 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 342 ASADPVLQARLFSYADAHRYRLGPNFHQIPVNCPYASKFFNPaiRDGPMNVNGNfGSEPTYLANdkSYTYIQQDRPIQQH 421
Cdd:PLN02609 335 YSDDKLLQTRIFAYADTQRHRLGPNYLQLPVNAPKCAHHNNH--HEGFMNFMHR-DEEVNYFPS--RFDPVRHAERVPIP 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 422 QEVWNGPAIPYHWATSPgdvDFVQARNLYRVLgkQPGQQKNLAYNIGIHVEGACPQIQQRVYDM--FARVDKGLSEAIKK 499
Cdd:PLN02609 410 HPPLSGRREKCKIEKEN---NFKQPGERYRSW--SPDRQERFIKRWVDALSDPRVTHEIRSIWIsyWSQCDKSLGQKLAS 484
|
....*
gi 6320462 500 VAEAK 504
Cdd:PLN02609 485 RLNVK 489
|
|
| |
|
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 ... |
47-502 |
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: 828.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 47 LQDYNLIDSLAHFNRENIPQRNPHAHGSGAFGYFEVTDDITDICGSAMFSKIGKRTKCLTRFSTVGGDKGSADTVRDPRG 126
Cdd:cd08157 1 LQDFHLIDTLAHFDRERIPERVVHAKGAGAYGEFEVTDDISDITSADMLQGVGKKTPCLVRFSTVGGEKGSADTVRDPRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 127 FATKFYTEEGNLDWVYNNTPVFFIRDPSKFPHFIHTQKRNPQTNLRDADMFWDFLTTpeNQVAIHQVMILFSDRGTPANY 206
Cdd:cd08157 81 FAVKFYTEEGNWDWVFNNTPVFFIRDPIKFPHFIHSQKRDPQTNLKDSTMFWDYLSQ--NPESIHQVMILFSDRGTPASY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 207 RSMHGYSGHTYKWSNKNGDWHYVQVHIKTDQGIKNLTIEEATKIAGSNPDYCQQDLFEAIQNGNYPSWTVYIQTMTERDA 286
Cdd:cd08157 159 RSMNGYSGHTYKWVNPDGSFKYVQFHLKSDQGPKFLTGEEAARLAGSNPDYATKDLFEAIERGDYPSWTVYVQVMTPEQA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 287 KKLPFSVFDLTKVWPQGQFPLRRVGKIVLNENPLNFFAQVEQAAFAPSTTVPYQEASADPVLQARLFSYADAHRYRLGPN 366
Cdd:cd08157 239 EKLRFNIFDLTKVWPHKDFPLRPVGKLTLNENPKNYFAEIEQAAFSPSHMVPGIEPSADPVLQARLFSYPDAHRHRLGPN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 367 FHQIPVNCPYASKFFNPAIRDGPMNVNGNFGSEPTYLANDKSYTYIQQDRPIQQHQEVWNGpaIPYHWATSPGDVDFVQA 446
Cdd:cd08157 319 YQQLPVNRPKTSPVYNPYQRDGPMSVNGNYGGDPNYVSSILPPTYFKKRVDADGHHENWVG--EVVAFLTEITDEDFVQP 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 6320462 447 RNLYRVLGkQPGQQKNLAYNIGIHVEGACPQIQQRVYDMFARVDKGLSEAIKKVAE 502
Cdd:cd08157 397 RALWEVVG-KPGQQERFVKNVAGHLSGAPPEIRKRVYEIFARVNPDLGKRIEKATE 451
|
|
| Catalase |
pfam00199 |
Catalase; |
23-405 |
0e+00 |
|
Catalase;
Pssm-ID: 459708 Cd Length: 383 Bit Score: 739.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 23 TNSTGNPINEPFVTQRIGEHGPLLLQDYNLIDSLAHFNRENIPQRNPHAHGSGAFGYFEVTDDITDICGSAMFSKIGKRT 102
Cdd:pfam00199 1 TTSNGAPVPDNQNSLTAGPRGPLLLQDFHLIEKLAHFDRERIPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSEVGKKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 103 KCLTRFSTVGGDKGSADTVRDPRGFATKFYTEEGNLDWVYNNTPVFFIRDPSKFPHFIHTQKRNPQTNLRDADMFWDFLT 182
Cdd:pfam00199 81 PVFVRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHSQKRDPQTNLPDPAMFWDFWS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 183 -TPEnqvAIHQVMILFSDRGTPANYRSMHGYSGHTYKWSNKNGDWHYVQVHIKTDQGIKNLTIEEATKIAGSNPDYCQQD 261
Cdd:pfam00199 161 lNPE---SLHQVTWLFSDRGIPRSYRHMNGFGVHTFKLVNADGERVYVKFHFKTDQGIKNLTWEEAQKLAGKDPDYHTRD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 262 LFEAIQNGNYPSWTVYIQTMTERDAKKLPFSVFDLTKVWPQGQFPLRRVGKIVLNENPLNFFAQVEQAAFAPSTTVPYQE 341
Cdd:pfam00199 238 LYEAIERGDYPSWTLYVQVMTEEDAEKFRFNPFDLTKVWPHKDYPLIEVGKMVLNRNPDNYFAEVEQAAFSPSNLVPGIE 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6320462 342 ASADPVLQARLFSYADAHRYRLGPNFHQIPVNCPYASkfFNPAIRDGPMNVNGNFGSEPTYLAN 405
Cdd:pfam00199 318 PSPDPMLQGRLFSYPDTQRYRLGPNYQQLPVNRPPCP--VHNYQRDGAMRFDINQGSRPNYEPN 379
|
|
| catalase |
cd00328 |
Catalase heme-binding enzyme; Catalase is a ubiquitous enzyme found in both prokaryotes and ... |
63-501 |
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: 711.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 63 NIPQRNPHAHGSGAFGYFEVTDDITDICGSAMFSKIGKRTKCLTRFSTVGGDKGSADTVRDPRGFATKFYTEEGNLDWVY 142
Cdd:cd00328 1 RIPERVVHARGAGAFGYFTAYGDWSDISAAAFFSAIGKKTPVFVRFSTVVGGAGSADTVRDPHGFATKFYTEEGNFDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 143 NNTPVFFIRDPSKFPHFIHTQKRNPQTNLRDADMFWDFLTTpeNQVAIHQVMILFSDRGTPANYRSMHGYSGHTYKWSNK 222
Cdd:cd00328 81 NNTPIFFIRDAIKFPDFIHAQKPNPQTALPDADRFWDFLSL--RPESLHQVSFLFSDRGIPAAYRHMNGYGSHTFKLVNA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 223 NGDWHYVQVHIKTDQGIKNLTIEEATKIAGSNPDYCQQDLFEAIQNGNYPSWTVYIQTMTERDAKKLPFSVFDLTKVWPQ 302
Cdd:cd00328 159 NGKVHYVKFHWKTDQGIANLVWEEAARLAGEDPDYHRQDLFEAIEAGDYPSWELYIQVMTFNDAEKFPFNPLDPTKVWPE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 303 GQFPLRRVGKIVLNENPLNFFAQVEQAAFAPSTTVPYQEASADPVLQARLFSYADAHRYRLGPNFHQIPVNCPYAskFFN 382
Cdd:cd00328 239 ELVPLIVVGKLVLNRNPLNFFAEVEQAAFDPGHIVPGVEFSEDPLLQGRLFSYADTQLYRLGPNFQQLPVNRPYA--PVH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 383 PAIRDGPMNVNGNFGsEPTYLANDKSYTYIQQDRPIQQHQEVWNGPAIPYHWATSPGDVDFVQARNLYRVLgkQPGQQKN 462
Cdd:cd00328 317 NNQRDGAGNMNDNTG-VPNYEPNAKDVRYPAQGAPKFDRGHFSHWKSGVNREASTTNDDNFTQARLFYRSL--TPGQQKR 393
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 6320462 463 LAYNIGIHVEGA-CPQIQQRVYDMFARVDKGLSEAIKKVA 501
Cdd:cd00328 394 LVDAFRFELADAvSPQIQQRVLDQFAKVDAAAAKRVAKAL 433
|
|
| Catalase |
smart01060 |
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ... |
27-402 |
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: 685.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 27 GNPINEPFVTQRIGEHGPLLLQDYNLIDSLAHFNRENIPQRNPHAHGSGAFGYFEVTDDITDICGSAMFSKIGKRTKCLT 106
Cdd:smart01060 2 GAPVADNQNSLTAGPRGPVLLQDFHLIEKLAHFDRERIPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQKVGKKTPVFV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 107 RFSTVGGDKGSADTVRDPRGFATKFYTEEGNLDWVYNNTPVFFIRDPSKFPHFIHTQKRNPQTNLRDADMFWDFLT-TPE 185
Cdd:smart01060 82 RFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHAQKRDPRTNLPDHDMFWDFWSlNPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 186 nqvAIHQVMILFSDRGTPANYRSMHGYSGHTYKWSNKNGDWHYVQVHIKTDQGIKNLTIEEATKIAGSNPDYCQQDLFEA 265
Cdd:smart01060 162 ---SLHQVTWLMSDRGIPASYRHMNGFGVHTFKLVNAEGERFYVKFHFKPDQGIKNLTWEEAAKLAGKDPDYHRRDLYEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 266 IQNGNYPSWTVYIQTMTERDAKKLPFSVFDLTKVWPQGQFPLRRVGKIVLNENPLNFFAQVEQAAFAPSTTVPYQEASAD 345
Cdd:smart01060 239 IERGDYPEWTLYVQVMPEEDAEKFRFDPFDLTKVWPHKDYPLIEVGKMTLNRNPDNYFAEVEQAAFSPSNLVPGIEFSPD 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 6320462 346 PVLQARLFSYADAHRYRLGPNFHQIPVNCPYASkfFNPAIRDGPMNVNGNFGSEPTY 402
Cdd:smart01060 319 KMLQGRLFSYPDTQRYRLGPNYHQLPVNRPRCP--VHNYQRDGAMRVDGNQGGDPNY 373
|
|
| KatE |
COG0753 |
Catalase [Inorganic ion transport and metabolism]; |
18-503 |
0e+00 |
|
Catalase [Inorganic ion transport and metabolism];
Pssm-ID: 440516 [Multi-domain] Cd Length: 489 Bit Score: 676.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 18 EDRVVTNSTGNPINEPFVTQRIGEHGPLLLQDYNLIDSLAHFNRENIPQRNPHAHGSGAFGYFEVTDDITDICGSAMFSK 97
Cdd:COG0753 7 EGKTLTTNQGAPVADNQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFEVTEDISKYTKAKFFQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 98 IGKRTKCLTRFSTVGGDKGSADTVRDPRGFATKFYTEEGNLDWVYNNTPVFFIRDPSKFPHFIHTQKRNPQTNLRDADMF 177
Cdd:COG0753 87 PGKKTPVFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHAQKRDPDTNLPQHDTF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 178 WDFLT-TPEnqvAIHQVMILFSDRGTPANYRSMHGYSGHTYKWSNKNGDWHYVQVHIKTDQGIKNLTIEEATKIAGSNPD 256
Cdd:COG0753 167 WDFWSlSPE---SLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAEGERFWVKFHWKPKQGIHSLTWDEAQKIAGKDPD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 257 YCQQDLFEAIQNGNYPSWTVYIQTMTERDAKKLPFSVFDLTKVWPQGQFPLRRVGKIVLNENPLNFFAQVEQAAFAPSTT 336
Cdd:COG0753 244 FHRRDLYEAIERGDFPEWELGVQVMPEEDADKFDFDPLDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAETEQAAFSPGNL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 337 VPYQEASADPVLQARLFSYADAHRYRLGPNFHQIPVNCPYASkfFNPAIRDGPMNVNGNfGSEPTYLANdkSYTYIQQDR 416
Cdd:COG0753 324 VPGIDFSPDKMLQGRLFSYADTQRYRLGPNFHQLPVNRPKCP--VHNYQRDGAMRYDIN-GGRVNYEPN--SLGGPREDP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 417 PIQQHQEVWNGPAIpyhWATSPGDVDFVQARNLYRVLGkqPGQQKNLAYNIGIHVEGA-CPQIQQRVYDMFARVDKGLSE 495
Cdd:COG0753 399 GFKEPPLKVDGDKV---RYRSESDDHFSQAGLLYRSMS--DEEKQHLIDNIAFELGKVeSEEIRERMVAHFYNVDPELGA 473
|
....*...
gi 6320462 496 aikKVAEA 503
Cdd:COG0753 474 ---RVAEA 478
|
|
| catalase_clade_3 |
cd08156 |
Clade 3 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
63-499 |
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: 651.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 63 NIPQRNPHAHGSGAFGYFEVTDDITDICGSAMFSKIGKRTKCLTRFSTVGGDKGSADTVRDPRGFATKFYTEEGNLDWVY 142
Cdd:cd08156 1 RIPERVVHAKGAGAFGTFEVTHDITKYTKAKIFSEVGKKTPVFVRFSTVAGERGSADTERDPRGFALKFYTEEGNWDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 143 NNTPVFFIRDPSKFPHFIHTQKRNPQTNLRDADMFWDFLT-TPEnqvAIHQVMILFSDRGTPANYRSMHGYSGHTYKWSN 221
Cdd:cd08156 81 NNTPVFFIRDPIKFPDFIHTQKRNPQTNLKDPDMFWDFWSlSPE---SLHQVTILFSDRGIPDGYRHMNGYGSHTFSLVN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 222 KNGDWHYVQVHIKTDQGIKNLTIEEATKIAGSNPDYCQQDLFEAIQNGNYPSWTVYIQTMTERDAKKLPFSVFDLTKVWP 301
Cdd:cd08156 158 AKGERFWVKFHFKTDQGIKNLTNEEAAELAGEDPDYAQRDLFEAIERGDFPSWTLYVQVMPEEDAEKYRFNPFDLTKVWP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 302 QGQFPLRRVGKIVLNENPLNFFAQVEQAAFAPSTTVPYQEASADPVLQARLFSYADAHRYRLGPNFHQIPVNCPYASkfF 381
Cdd:cd08156 238 HKDYPLIEVGKLELNRNPENYFAEVEQAAFSPSNLVPGIGFSPDKMLQGRLFSYADAHRYRLGVNYHQLPVNRPKCP--V 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 382 NPAIRDGPMNVNGNFGSEPTYLANdkSYTYIQQDRPIQQHQEVWNGPAipYHWATSPGDVDFVQARNLYRVLgkQPGQQK 461
Cdd:cd08156 316 NNYQRDGAMRVDGNGGGAPNYEPN--SFGGPPEDPEYAEPPLPVSGDA--DRYNYRDDDDDYTQAGDLYRLV--SEDERE 389
|
410 420 430
....*....|....*....|....*....|....*...
gi 6320462 462 NLAYNIGIHVEGACPQIQQRVYDMFARVDKGLSEAIKK 499
Cdd:cd08156 390 RLVENIAGHLKGAPEFIQERQVAHFYKADPDYGERVAK 427
|
|
| PLN02609 |
PLN02609 |
catalase |
23-504 |
1.22e-174 |
|
catalase
Pssm-ID: 215328 [Multi-domain] Cd Length: 492 Bit Score: 500.81 E-value: 1.22e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 23 TNSTGNPINEPFVTQRIGEHGPLLLQDYNLIDSLAHFNRENIPQRNPHAHGSGAFGYFEVTDDITDICGSAMFSKIGKRT 102
Cdd:PLN02609 18 TTNSGAPVWNNNSSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDISNLTCADFLRAPGVQT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 103 KCLTRFSTVGGDKGSADTVRDPRGFATKFYTEEGNLDWVYNNTPVFFIRDPSKFPHFIHTQKRNPQTNLRDADMFWDFLT 182
Cdd:PLN02609 98 PVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDMVGNNFPVFFIRDGMKFPDMVHALKPNPKTHIQEPWRILDFLS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 183 -TPEnqvAIHQVMILFSDRGTPANYRSMHGYSGHTYKWSNKNGDWHYVQVHIKTDQGIKNLTIEEATKIAGSNPDYCQQD 261
Cdd:PLN02609 178 hHPE---SLHMFTFLFDDRGIPQDYRHMEGFGVHTYKLINKAGKAHYVKFHWKPTCGVKNLLDEEAVRVGGSNHSHATQD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 262 LFEAIQNGNYPSWTVYIQTMTERDAKKLPFSVFDLTKVWPQGQFPLRRVGKIVLNENPLNFFAQVEQAAFAPSTTVPYQE 341
Cdd:PLN02609 255 LYDSIAAGNYPEWKLFIQTMDPEDEDKFDFDPLDVTKTWPEDILPLQPVGRLVLNRNIDNFFAENEQLAFCPAIVVPGIY 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 342 ASADPVLQARLFSYADAHRYRLGPNFHQIPVNCPYASKFFNPaiRDGPMNVNGNfGSEPTYLANdkSYTYIQQDRPIQQH 421
Cdd:PLN02609 335 YSDDKLLQTRIFAYADTQRHRLGPNYLQLPVNAPKCAHHNNH--HEGFMNFMHR-DEEVNYFPS--RFDPVRHAERVPIP 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 422 QEVWNGPAIPYHWATSPgdvDFVQARNLYRVLgkQPGQQKNLAYNIGIHVEGACPQIQQRVYDM--FARVDKGLSEAIKK 499
Cdd:PLN02609 410 HPPLSGRREKCKIEKEN---NFKQPGERYRSW--SPDRQERFIKRWVDALSDPRVTHEIRSIWIsyWSQCDKSLGQKLAS 484
|
....*
gi 6320462 500 VAEAK 504
Cdd:PLN02609 485 RLNVK 489
|
|
| catalase_clade_1 |
cd08154 |
Clade 1 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
23-503 |
3.20e-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: 494.12 E-value: 3.20e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 23 TNSTGNPINEPFVTQRIGEHGPLLLQDYNLIDSLAHFNRENIPQRNPHAHGSGAFGYFEVTDDITDICGSAMFSKIGKRT 102
Cdd:cd08154 3 TTNQGAPVGDNQNSQTVGPRGPVLLEDYHLIEKLAHFDRERIPERVVHARGAGAHGYFEAYGDISDYTRASFLQEPGKKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 103 KCLTRFSTVGGDKGSADTVRDPRGFATKFYTEEGNLDWVYNNTPVFFIRDPSKFPHFIHTQKRNPQTNLRDADMFWDFLT 182
Cdd:cd08154 83 PVFVRFSTVIHGKGSPETLRDPRGFAVKFYTEEGNWDLVGNNLPVFFIRDAIKFPDMIHALKPSPVTNIQDPNRIFDFFS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 183 -TPEnqvAIHQVMILFSDRGTPANYRSMHGYSGHTYKWSNKNGDWHYVQVHIKTDQGIKNLTIEEATKIAGSNPDYCQQD 261
Cdd:cd08154 163 hVPE---STHMLTFLYSDWGTPASYRHMDGSGVHTYKWVNAEGKVVYVKYHWKPKQGVKNLTAEEAAEVQGKNFNHATQD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 262 LFEAIQNGNYPSWTVYIQTMTERDAKKLPFSVFDLTKVWPQGQFPLRRVGKIVLNENPLNFFAQVEQAAFAPSTTVPYQE 341
Cdd:cd08154 240 LYDAIAAGNYPEWELYVQIMDPKDLDKLDFDPLDDTKIWPEDQFPLKPVGKMTLNKNPDNFFAEVEQVAFSPGNLVPGIE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 342 ASADPVLQARLFSYADAHRYRLGPNFHQIPVNCPYASKFFNpaIRDGPMNvngnfgseptylandksytYIQQDRPIQ-- 419
Cdd:cd08154 320 PSDDKMLQGRLFSYSDTQRYRLGPNYLQLPINAPKAAVHNN--QRDGQMN-------------------YGHDTSDVNye 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 420 --QHQEVWNGPAIPYHWATSPGDV---------DFVQARNLYRVLgkQPGQQKNLAYNIGIHVEGACPQIQQRVYDMFAR 488
Cdd:cd08154 379 psRLDGLPEAPKYPYSQPPLSGTTqqapiaktnNFKQAGERYRSF--SEEEQENLIKNLVVDLSDVNEEIKLRMLSYFSQ 456
|
490
....*....|....*
gi 6320462 489 VDKGLseaIKKVAEA 503
Cdd:cd08154 457 ADPDY---GERVAEG 468
|
|
| catalase_clade_2 |
cd08155 |
Clade 2 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
62-499 |
1.85e-131 |
|
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: 389.04 E-value: 1.85e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 62 ENIPQRNPHAHGSGAFGYFEVTDDITDICGSAMFSKIGKRTKCLTRFSTVGGDKGSADTVRDPRGFATKFYTEEGNLDWV 141
Cdd:cd08155 3 ERIPERVVHARGSGAHGYFQVYESLSQYTKAKFLQDPGKKTPVFVRFSTVAGSRGSADTVRDVRGFAVKFYTEEGNYDLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 142 YNNTPVFFIRDPSKFPHFIHTQKRNPQTNLRDA----DMFWDFLT-TPEnqvAIHQVMILFSDRGTPANYRSMHGYSGHT 216
Cdd:cd08155 83 GNNIPVFFIQDAIKFPDLIHAVKPEPHNEMPQAqsahDTFWDFVSlQPE---SAHMVMWAMSDRAIPRSYRMMEGFGVHT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 217 YKWSNKNGDWHYVQVHIKTDQGIKNLTIEEATKIAGSNPDYCQQDLFEAIQNGNYPSWTVYIQTMTERDAKKLPFSVFDL 296
Cdd:cd08155 160 FRLVNAQGKSTFVKFHWKPVLGVHSLVWDEAQKIAGKDPDFHRRDLWEAIESGDYPEWELGVQLIDEEDEFKFDFDILDP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 297 TKVWPQGQFPLRRVGKIVLNENPLNFFAQVEQAAFAPSTTVPYQEASADPVLQARLFSYADAHRYRLG-PNFHQIPVN-- 373
Cdd:cd08155 240 TKLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFCPANVVPGIDFSNDPLLQGRLFSYLDTQLSRLGgPNFHELPINrp 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 374 -CPYASkfFNpaiRDGPMNVNGNFGS---EPTYLANDKSYTYIQQDRPIQQHQEVWNGPAIpYHWATSPGDvDFVQARNL 449
Cdd:cd08155 320 vCPVHN--NQ---RDGHMRMTINKGRvnyFPNSLGAGPPRAASPAEGGFVHYPEKVEGPKI-RIRSESFAD-HYSQARLF 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 6320462 450 YRVLGKQPGQ--QKNLAYNIGiHVEGacPQIQQRVYDMFARVDKGLSEAIKK 499
Cdd:cd08155 393 WNSMSPVEKEhiISAFTFELS-KVET--PEIRERVVDHLANIDEDLAKKVAK 441
|
|
| katE |
PRK11249 |
hydroperoxidase II; Provisional |
36-502 |
3.58e-128 |
|
hydroperoxidase II; Provisional
Pssm-ID: 236886 [Multi-domain] Cd Length: 752 Bit Score: 390.94 E-value: 3.58e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 36 TQRIGEHGPLLLQDYNLIDSLAHFNRENIPQRNPHAHGSGAFGYFEVTDDITDICGSAMFSKIGKRTKCLTRFSTVGGDK 115
Cdd:PRK11249 91 SLRAGSRGPSLLEDFILREKITHFDHERIPERIVHARGSAAHGYFQPYKSLSDITKAAFLQDPGKITPVFVRFSTVQGPR 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 116 GSADTVRDPRGFATKFYTEEGNLDWVYNNTPVFFIRDPSKFPHFIHTQKRNPQ----TNLRDADMFWDFLT-TPEnqvAI 190
Cdd:PRK11249 171 GSADTVRDIRGFATKFYTEEGNFDLVGNNTPVFFIQDAIKFPDFVHAVKPEPHneipQGQSAHDTFWDYVSlQPE---TL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 191 HQVMILFSDRGTPANYRSMHGYSGHTYKWSNKNGDWHYVQVHIKTDQGIKNLTIEEATKIAGSNPDYCQQDLFEAIQNGN 270
Cdd:PRK11249 248 HNVMWAMSDRGIPRSYRTMEGFGIHTFRLINAEGKATFVRFHWKPVAGKASLVWDEAQKLTGRDPDFHRRDLWEAIEAGD 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 271 YPSWTVYIQTMTERDAKKLPFSVFDLTKVWPQGQFPLRRVGKIVLNENPLNFFAQVEQAAFAPSTTVPYQEASADPVLQA 350
Cdd:PRK11249 328 YPEYELGVQLIPEEDEFKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFHPGHIVPGIDFTNDPLLQG 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 351 RLFSYADAHRYRL-GPNFHQIPVN---CPYASKffnpaIRDG--------------PMNVNGNFGSEPTYLANDKSYTYI 412
Cdd:PRK11249 408 RLFSYTDTQISRLgGPNFHEIPINrptCPYHNF-----QRDGmhrmtidtgpanyePNSINGNWPRETPPAPKRGGFESY 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 413 QQdrPIQQHQEVWNGPAIPYHwatspgdvdFVQARNLYRVLgkQPGQQKNL--AYNIGI-HVEGacPQIQQRVYDMFARV 489
Cdd:PRK11249 483 QE--RVEGNKVRERSPSFGDY---------YSQPRLFWLSQ--TPIEQRHIidAFSFELgKVVR--PYIRERVVDQLAHI 547
|
490
....*....|...
gi 6320462 490 DKGLSeaiKKVAE 502
Cdd:PRK11249 548 DLTLA---QAVAE 557
|
|
| catalase_like |
cd08150 |
Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found ... |
65-363 |
8.42e-52 |
|
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: 177.75 E-value: 8.42e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 65 PQRNPHAHGSGAFGYFEVTDDITDICGSAMFSKiGKRTKCLTRFSTVggdKGSADTVRDPRGFATKFYTE--EGNLDWVY 142
Cdd:cd08150 1 GLRGQHFQGTCAFGTFEVLADLKERLRVGLFAE-GKVYPAYIRFSNG---AGIDDTKPDIRGFAIKFTGVadAGTLDFVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 143 NNTPVFFIRDPSKFPHFIHTQKRNPQTNlRDADMFWDFLTT-PENqvaIHQVMilFSDRGTPANYRSMHGYSGHTYKWSN 221
Cdd:cd08150 77 NNTPVFFIRNTSDYEDFVAEFARSARGE-PPLDFIAWYVEKrPED---LPNLL--GARSQVPDSYAAARYFSQVTFAFIN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 222 KNGDWHYVQVHIKTDQGIKNLTIEEATkiaGSNPDYCQQDLFEAIQNGnYPSWTVYIQTMTERDAkklpFSVFDLTKVWP 301
Cdd:cd08150 151 GAGKYRVVRSKDNPVDGIPSLEDHELE---ARPPDYLREELTERLQRG-PVVYDFRIQLNDDTDA----TTIDNPTILWP 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6320462 302 QgQFPLRRVGKIVLNENPLNffAQVEQAAFAPSTTVPYQEASAD--PVLQARLFSYADAHRYRL 363
Cdd:cd08150 223 T-EHPVEAVAKITIPPPTFT--AAQEAFAFNPFTPWHGLLETNDlgPILEVRRRVYTSSQGLRH 283
|
|
| srpA_like |
cd08153 |
Catalase-like heme-binding proteins similar to the uncharacterized srpA; Catalase is a ... |
67-363 |
3.53e-27 |
|
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: 111.17 E-value: 3.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 67 RNpHAHGSGAFGYFEVTDDITDICGSAMFSkiGKRTKCLTRFSTVGGDKGSADTVRDPRGFATKFYTEEGNL-DWVYNNT 145
Cdd:cd08153 16 RN-HAKGICVSGTFTPSGAAASLSRAPLFS--GGSVPVTGRFSLGGGNPKAPDDAANPRGMALKFRLPDGEQwRMVMNSF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 146 PVFFIRDPSKFPHFIhtQKRNPQ-TNLRDADMFWDFLTT-PENQvaiHQVMILFSdRGTPANYRSMHGYSGHTYKWSNKN 223
Cdd:cd08153 93 PVFPVRTPEEFLALL--KAIAPDaTGKPDPAKLKAFLAAhPEAA---AFLAWIKT-APPPASFANTTYYGVNAFYFTNAN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 224 GDWHYVQVHIKTDQGIKNLTIEEATKIAgsnPDYCQQDLFEAIQNGNYpSWTVYIQTMTERDAkklpfsVFDLTKVWPQG 303
Cdd:cd08153 167 GKRQPVRWRFVPEDGVKYLSDEEAAKLG---PDFLFDELAQRLAQGPV-RWDLVLQLAEPGDP------TDDPTKPWPAD 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6320462 304 qfplRR---VGKIVLNENPLNFFAQVEQAAFAPSTTVPYQEASADPVLQARLFSYADAHRYRL 363
Cdd:cd08153 237 ----RKevdAGTLTITKVAPDQGGACRDINFDPLVLPDGIEPSDDPLLAARSAAYAVSFSRRQ 295
|
|
| y4iL_like |
cd08152 |
Catalase-like heme-binding proteins similar to the uncharacterized y4iL; Catalase is a ... |
67-331 |
1.58e-10 |
|
Catalase-like heme-binding proteins similar to the uncharacterized y4iL; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes involved in the protection of cells from the toxic effects of peroxides. It catalyses the conversion of hydrogen peroxide to water and molecular oxygen. Several other related protein families share the catalase fold and bind to heme, but do not necessarily have catalase activity. This family contains uncharacterized proteins similar to Rhizobium sp. NGR234 y4iL, of mostly bacterial origin.
Pssm-ID: 163708 Cd Length: 305 Bit Score: 62.28 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 67 RNPHAHGSGAF-GYFEVTDDITDICGSAMFSKiGKRTKCLTRFSTVGGDkGSADTVRDPRGFATKFY----------TEE 135
Cdd:cd08152 5 RDAHAKSHGCLkAEFTVLDDLPPELAQGLFAE-PGTYPAVIRFSNAPGD-ILDDSVPDPRGMAIKVLgvpgekllpeEDA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 136 GNLDWVYNNTPVFFIRDPSKFPHFIHTQKRnpQTNLRD-ADMFWDFLTTPENQVAIHQVMILFSDRGTPANYRSMHGYSG 214
Cdd:cd08152 83 TTQDFVLVNHPVFFARDAKDYLALLKLLAR--TTSLPDgAKAALSAPLRGALRVLEAAGGESPTLKLGGHPPAHPLGETY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 215 HT---YKWsnknGDwHYVQVHIKTDQGiKNLTIEEATKIAGSNPDYCQQDLFEAIQNGNYpSWTVYIQTMTerDAKKLPf 291
Cdd:cd08152 161 WSqapYRF----GD-YVAKYSVVPASP-ALPALTGKELDLTDDPDALREALADFLAENDA-EFEFRIQLCT--DLEKMP- 230
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 6320462 292 sVFDLTKVWPQGQFPLRRVGKIVLneNPLNFFAQVEQAAF 331
Cdd:cd08152 231 -IEDASVEWPEALSPFVPVATITI--PPQDFDSPARQRAF 267
|
|
| Catalase-rel |
pfam06628 |
Catalase-related immune-responsive; This family represents a small conserved region within ... |
442-503 |
4.29e-08 |
|
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: 50.06 E-value: 4.29e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6320462 442 DFVQARNLYRVLGkqPGQQKNLAYNIGIHVEGA-CPQIQQRVYDMFARVDKGLSeaiKKVAEA 503
Cdd:pfam06628 7 HFSQAGLFYRSMS--EEERQRLVDNIAFELSKVtDPEIQERMVAHFYKVDPDLG---QRVAEA 64
|
|
| AOS |
cd08151 |
Allene oxide synthase; Allene oxide synthase converts a fatty acid hydroperoxide to an allene ... |
67-338 |
4.84e-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: 51.66 E-value: 4.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 67 RNPHAHGSGAFGYFEVTDDItDICGSAMFSKiGKRTKCLTRFSTVGGDKGsaDTVRDPRGFATKFYT----EEGNLDWVY 142
Cdd:cd08151 28 RGTHTIGVGAKGVLTVLAES-DFPEHAFFTA-GKRFPVILRHANIVGGDD--DASLDGRGAALRFLNagddDAGPLDLVM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 143 NNTPVFFIRDPSKFPHFIhtqkRNPQTNLRDADMFWDFLTtPENQVAihqvmilfSDRGTPANYRSMHGYSGHTYKWSNK 222
Cdd:cd08151 104 NTGESFGFWTAASFADFA----GAGLPFREKAAKLRGPLA-RYAVWA--------SLRRAPDSYTDLHYYSQICYEFVAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320462 223 NGDWHYVQVHI-------KTDQGIKNLTIEEATKI------AGSN--PDYCQQDLFEAIQNGNYpSWTVYIQTM-TERDA 286
Cdd:cd08151 171 DGKSRYARFRLlppdadtEWDLGEDVLETIFQRPRlylprlPGDTrpKDYLRNEFRQRLQSPGV-RYRLQIQLReVSDDA 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 6320462 287 KKlpfSVFDLTKVWPQGQFPLRRVGKIVLNENPLNffAQVEQAAFAPSTTVP 338
Cdd:cd08151 250 TA---VALDCCRPWDEDEHPWLDLAVVRLGAPLPN--DELEKLAFNPGNTPE 296
|
|
| |
