|
Name |
Accession |
Description |
Interval |
E-value |
| KatE |
COG0753 |
Catalase [Inorganic ion transport and metabolism]; |
4-494 |
0e+00 |
|
Catalase [Inorganic ion transport and metabolism];
Pssm-ID: 440516 [Multi-domain] Cd Length: 489 Bit Score: 806.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 4 QKTTPHATGSTRQNGAPAVSDRQSLTVGSEGPIVLHDTHLLETHQHFNR*NIPERRPHAKGSGAFGEFEVTEDVSKYTKA 83
Cdd:COG0753 2 QYADDEGKTLTTNQGAPVADNQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFEVTEDISKYTKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 84 LVFQ-PGTKTETLLRFSTVAGELGSPDTWRDVRGFALRFYTEEGNYDLVGNNTPIFFLRDP*KFTHFIRSQKRLPDSGLR 162
Cdd:COG0753 82 KFFQePGKKTPVFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHAQKRDPDTNLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 163 DAT*QWDFWTNNPESAHQVTYL*GPRGLPRTWREMNGYGSHTYLWVNAQGEKHWVKYHFISQQGVHNLSNDEATKIAGEN 242
Cdd:COG0753 162 QHDTFWDFWSLSPESLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAEGERFWVKFHWKPKQGIHSLTWDEAQKIAGKD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 243 ADFHRQDLFESIAKGDHPKWDLYIQAIPYEEGKTYRFNPFDLTKTISQKDYPRIKVGTLTLNRNPENHFAQIESAAFSPS 322
Cdd:COG0753 242 PDFHRRDLYEAIERGDFPEWELGVQVMPEEDADKFDFDPLDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAETEQAAFSPG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 323 NTVPGIGLSPDRMLLGRAFAYHDAQLYRVGAHVNQLPVNRPKNAVHNYAFEGQ*WYDHTGDRSTYVPNSNGDSWSDEtGP 402
Cdd:COG0753 322 NLVPGIDFSPDKMLQGRLFSYADTQRYRLGPNFHQLPVNRPKCPVHNYQRDGAMRYDINGGRVNYEPNSLGGPREDP-GF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 403 VDDGWEADGTLTREAQalrADDDDFGQAGTLVReVFSDQERDDFVETVAGALKGV-RQDVQARAFEYWKNVDATIGQRIE 481
Cdd:COG0753 401 KEPPLKVDGDKVRYRS---ESDDHFSQAGLLYR-SMSDEEKQHLIDNIAFELGKVeSEEIRERMVAHFYNVDPELGARVA 476
|
490
....*....|...
gi 20663751 482 DEVKRHEGDGIPG 494
Cdd:COG0753 477 EALGLDLPEAKAL 489
|
|
| catalase_clade_3 |
cd08156 |
Clade 3 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
54-484 |
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: 736.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 54 NIPERRPHAKGSGAFGEFEVTEDVSKYTKALVFQP-GTKTETLLRFSTVAGELGSPDTWRDVRGFALRFYTEEGNYDLVG 132
Cdd:cd08156 1 RIPERVVHAKGAGAFGTFEVTHDITKYTKAKIFSEvGKKTPVFVRFSTVAGERGSADTERDPRGFALKFYTEEGNWDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 133 NNTPIFFLRDP*KFTHFIRSQKRLPDSGLRDAT*QWDFWTNNPESAHQVTYL*GPRGLPRTWREMNGYGSHTYLWVNAQG 212
Cdd:cd08156 81 NNTPVFFIRDPIKFPDFIHTQKRNPQTNLKDPDMFWDFWSLSPESLHQVTILFSDRGIPDGYRHMNGYGSHTFSLVNAKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 213 EKHWVKYHFISQQGVHNLSNDEATKIAGENADFHRQDLFESIAKGDHPKWDLYIQAIPYEEGKTYRFNPFDLTKTISQKD 292
Cdd:cd08156 161 ERFWVKFHFKTDQGIKNLTNEEAAELAGEDPDYAQRDLFEAIERGDFPSWTLYVQVMPEEDAEKYRFNPFDLTKVWPHKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 293 YPRIKVGTLTLNRNPENHFAQIESAAFSPSNTVPGIGLSPDRMLLGRAFAYHDAQLYRVGAHVNQLPVNRPKNAVHNYAF 372
Cdd:cd08156 241 YPLIEVGKLELNRNPENYFAEVEQAAFSPSNLVPGIGFSPDKMLQGRLFSYADAHRYRLGVNYHQLPVNRPKCPVNNYQR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 373 EGQ*WYDH-TGDRSTYVPNSNGDSWSDETgPVDDGWEADGTLTREAQalRADDDDFGQAGTLVREVfSDQERDDFVETVA 451
Cdd:cd08156 321 DGAMRVDGnGGGAPNYEPNSFGGPPEDPE-YAEPPLPVSGDADRYNY--RDDDDDYTQAGDLYRLV-SEDERERLVENIA 396
|
410 420 430
....*....|....*....|....*....|...
gi 20663751 452 GALKGVRQDVQARAFEYWKNVDATIGQRIEDEV 484
Cdd:cd08156 397 GHLKGAPEFIQERQVAHFYKADPDYGERVAKAL 429
|
|
| Catalase |
pfam00199 |
Catalase; |
14-393 |
0e+00 |
|
Catalase;
Pssm-ID: 459708 Cd Length: 383 Bit Score: 702.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 14 TRQNGAPAVSDRQSLTVGSEGPIVLHDTHLLETHQHFNR*NIPERRPHAKGSGAFGEFEVTEDVSKYTKALVFQ-PGTKT 92
Cdd:pfam00199 1 TTSNGAPVPDNQNSLTAGPRGPLLLQDFHLIEKLAHFDRERIPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSeVGKKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 93 ETLLRFSTVAGELGSPDTWRDVRGFALRFYTEEGNYDLVGNNTPIFFLRDP*KFTHFIRSQKRLPDSGLRDAT*QWDFWT 172
Cdd:pfam00199 81 PVFVRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHSQKRDPQTNLPDPAMFWDFWS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 173 NNPESAHQVTYL*GPRGLPRTWREMNGYGSHTYLWVNAQGEKHWVKYHFISQQGVHNLSNDEATKIAGENADFHRQDLFE 252
Cdd:pfam00199 161 LNPESLHQVTWLFSDRGIPRSYRHMNGFGVHTFKLVNADGERVYVKFHFKTDQGIKNLTWEEAQKLAGKDPDYHTRDLYE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 253 SIAKGDHPKWDLYIQAIPYEEGKTYRFNPFDLTKTISQKDYPRIKVGTLTLNRNPENHFAQIESAAFSPSNTVPGIGLSP 332
Cdd:pfam00199 241 AIERGDYPSWTLYVQVMTEEDAEKFRFNPFDLTKVWPHKDYPLIEVGKMVLNRNPDNYFAEVEQAAFSPSNLVPGIEPSP 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20663751 333 DRMLLGRAFAYHDAQLYRVGAHVNQLPVNRPKNAVHNYAFEGQ*WYD-HTGDRSTYVPNSNG 393
Cdd:pfam00199 321 DPMLQGRLFSYPDTQRYRLGPNYQQLPVNRPPCPVHNYQRDGAMRFDiNQGSRPNYEPNSFG 382
|
|
| Catalase |
smart01060 |
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ... |
17-387 |
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: 662.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 17 NGAPAVSDRQSLTVGSEGPIVLHDTHLLETHQHFNR*NIPERRPHAKGSGAFGEFEVTEDVSKYTKALVFQ-PGTKTETL 95
Cdd:smart01060 1 QGAPVADNQNSLTAGPRGPVLLQDFHLIEKLAHFDRERIPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQkVGKKTPVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 96 LRFSTVAGELGSPDTWRDVRGFALRFYTEEGNYDLVGNNTPIFFLRDP*KFTHFIRSQKRLPDSGLRDAT*QWDFWTNNP 175
Cdd:smart01060 81 VRFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHAQKRDPRTNLPDHDMFWDFWSLNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 176 ESAHQVTYL*GPRGLPRTWREMNGYGSHTYLWVNAQGEKHWVKYHFISQQGVHNLSNDEATKIAGENADFHRQDLFESIA 255
Cdd:smart01060 161 ESLHQVTWLMSDRGIPASYRHMNGFGVHTFKLVNAEGERFYVKFHFKPDQGIKNLTWEEAAKLAGKDPDYHRRDLYEAIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 256 KGDHPKWDLYIQAIPYEEGKTYRFNPFDLTKTISQKDYPRIKVGTLTLNRNPENHFAQIESAAFSPSNTVPGIGLSPDRM 335
Cdd:smart01060 241 RGDYPEWTLYVQVMPEEDAEKFRFDPFDLTKVWPHKDYPLIEVGKMTLNRNPDNYFAEVEQAAFSPSNLVPGIEFSPDKM 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 20663751 336 LLGRAFAYHDAQLYRVGAHVNQLPVNRPKNAVHNYAFEGQ*WYD-HTGDRSTY 387
Cdd:smart01060 321 LQGRLFSYPDTQRYRLGPNYHQLPVNRPRCPVHNYQRDGAMRVDgNQGGDPNY 373
|
|
| PLN02609 |
PLN02609 |
catalase |
14-481 |
2.45e-170 |
|
catalase
Pssm-ID: 215328 [Multi-domain] Cd Length: 492 Bit Score: 489.64 E-value: 2.45e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 14 TRQNGAPAVSDRQSLTVGSEGPIVLHDTHLLETHQHFNR*NIPERRPHAKGSGAFGEFEVTEDVSKYTKALVFQ-PGTKT 92
Cdd:PLN02609 18 TTNSGAPVWNNNSSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDISNLTCADFLRaPGVQT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 93 ETLLRFSTVAGELGSPDTWRDVRGFALRFYTEEGNYDLVGNNTPIFFLRDP*KFTHFIRSQKRLPDSGLRDAT*QWDFWT 172
Cdd:PLN02609 98 PVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDMVGNNFPVFFIRDGMKFPDMVHALKPNPKTHIQEPWRILDFLS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 173 NNPESAHQVTYL*GPRGLPRTWREMNGYGSHTYLWVNAQGEKHWVKYHFISQQGVHNLSNDEATKIAGENADFHRQDLFE 252
Cdd:PLN02609 178 HHPESLHMFTFLFDDRGIPQDYRHMEGFGVHTYKLINKAGKAHYVKFHWKPTCGVKNLLDEEAVRVGGSNHSHATQDLYD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 253 SIAKGDHPKWDLYIQAIPYEEGKTYRFNPFDLTKTISQKDYPRIKVGTLTLNRNPENHFAQIESAAFSPSNTVPGIGLSP 332
Cdd:PLN02609 258 SIAAGNYPEWKLFIQTMDPEDEDKFDFDPLDVTKTWPEDILPLQPVGRLVLNRNIDNFFAENEQLAFCPAIVVPGIYYSD 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 333 DRMLLGRAFAYHDAQLYRVGAHVNQLPVNRPKNAVHNYAFEGQ*WYDHTGDRSTYVPNSNGDSWSDETGPVDDGWEAdgt 412
Cdd:PLN02609 338 DKLLQTRIFAYADTQRHRLGPNYLQLPVNAPKCAHHNNHHEGFMNFMHRDEEVNYFPSRFDPVRHAERVPIPHPPLS--- 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20663751 413 lTREAQALRADDDDFGQAGTLVREvFSDQERDDFVETVAGALKGVRQDVQARAF--EYWKNVDATIGQRIE 481
Cdd:PLN02609 415 -GRREKCKIEKENNFKQPGERYRS-WSPDRQERFIKRWVDALSDPRVTHEIRSIwiSYWSQCDKSLGQKLA 483
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| KatE |
COG0753 |
Catalase [Inorganic ion transport and metabolism]; |
4-494 |
0e+00 |
|
Catalase [Inorganic ion transport and metabolism];
Pssm-ID: 440516 [Multi-domain] Cd Length: 489 Bit Score: 806.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 4 QKTTPHATGSTRQNGAPAVSDRQSLTVGSEGPIVLHDTHLLETHQHFNR*NIPERRPHAKGSGAFGEFEVTEDVSKYTKA 83
Cdd:COG0753 2 QYADDEGKTLTTNQGAPVADNQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFEVTEDISKYTKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 84 LVFQ-PGTKTETLLRFSTVAGELGSPDTWRDVRGFALRFYTEEGNYDLVGNNTPIFFLRDP*KFTHFIRSQKRLPDSGLR 162
Cdd:COG0753 82 KFFQePGKKTPVFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHAQKRDPDTNLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 163 DAT*QWDFWTNNPESAHQVTYL*GPRGLPRTWREMNGYGSHTYLWVNAQGEKHWVKYHFISQQGVHNLSNDEATKIAGEN 242
Cdd:COG0753 162 QHDTFWDFWSLSPESLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAEGERFWVKFHWKPKQGIHSLTWDEAQKIAGKD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 243 ADFHRQDLFESIAKGDHPKWDLYIQAIPYEEGKTYRFNPFDLTKTISQKDYPRIKVGTLTLNRNPENHFAQIESAAFSPS 322
Cdd:COG0753 242 PDFHRRDLYEAIERGDFPEWELGVQVMPEEDADKFDFDPLDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAETEQAAFSPG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 323 NTVPGIGLSPDRMLLGRAFAYHDAQLYRVGAHVNQLPVNRPKNAVHNYAFEGQ*WYDHTGDRSTYVPNSNGDSWSDEtGP 402
Cdd:COG0753 322 NLVPGIDFSPDKMLQGRLFSYADTQRYRLGPNFHQLPVNRPKCPVHNYQRDGAMRYDINGGRVNYEPNSLGGPREDP-GF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 403 VDDGWEADGTLTREAQalrADDDDFGQAGTLVReVFSDQERDDFVETVAGALKGV-RQDVQARAFEYWKNVDATIGQRIE 481
Cdd:COG0753 401 KEPPLKVDGDKVRYRS---ESDDHFSQAGLLYR-SMSDEEKQHLIDNIAFELGKVeSEEIRERMVAHFYNVDPELGARVA 476
|
490
....*....|...
gi 20663751 482 DEVKRHEGDGIPG 494
Cdd:COG0753 477 EALGLDLPEAKAL 489
|
|
| catalase_clade_3 |
cd08156 |
Clade 3 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
54-484 |
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: 736.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 54 NIPERRPHAKGSGAFGEFEVTEDVSKYTKALVFQP-GTKTETLLRFSTVAGELGSPDTWRDVRGFALRFYTEEGNYDLVG 132
Cdd:cd08156 1 RIPERVVHAKGAGAFGTFEVTHDITKYTKAKIFSEvGKKTPVFVRFSTVAGERGSADTERDPRGFALKFYTEEGNWDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 133 NNTPIFFLRDP*KFTHFIRSQKRLPDSGLRDAT*QWDFWTNNPESAHQVTYL*GPRGLPRTWREMNGYGSHTYLWVNAQG 212
Cdd:cd08156 81 NNTPVFFIRDPIKFPDFIHTQKRNPQTNLKDPDMFWDFWSLSPESLHQVTILFSDRGIPDGYRHMNGYGSHTFSLVNAKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 213 EKHWVKYHFISQQGVHNLSNDEATKIAGENADFHRQDLFESIAKGDHPKWDLYIQAIPYEEGKTYRFNPFDLTKTISQKD 292
Cdd:cd08156 161 ERFWVKFHFKTDQGIKNLTNEEAAELAGEDPDYAQRDLFEAIERGDFPSWTLYVQVMPEEDAEKYRFNPFDLTKVWPHKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 293 YPRIKVGTLTLNRNPENHFAQIESAAFSPSNTVPGIGLSPDRMLLGRAFAYHDAQLYRVGAHVNQLPVNRPKNAVHNYAF 372
Cdd:cd08156 241 YPLIEVGKLELNRNPENYFAEVEQAAFSPSNLVPGIGFSPDKMLQGRLFSYADAHRYRLGVNYHQLPVNRPKCPVNNYQR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 373 EGQ*WYDH-TGDRSTYVPNSNGDSWSDETgPVDDGWEADGTLTREAQalRADDDDFGQAGTLVREVfSDQERDDFVETVA 451
Cdd:cd08156 321 DGAMRVDGnGGGAPNYEPNSFGGPPEDPE-YAEPPLPVSGDADRYNY--RDDDDDYTQAGDLYRLV-SEDERERLVENIA 396
|
410 420 430
....*....|....*....|....*....|...
gi 20663751 452 GALKGVRQDVQARAFEYWKNVDATIGQRIEDEV 484
Cdd:cd08156 397 GHLKGAPEFIQERQVAHFYKADPDYGERVAKAL 429
|
|
| Catalase |
pfam00199 |
Catalase; |
14-393 |
0e+00 |
|
Catalase;
Pssm-ID: 459708 Cd Length: 383 Bit Score: 702.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 14 TRQNGAPAVSDRQSLTVGSEGPIVLHDTHLLETHQHFNR*NIPERRPHAKGSGAFGEFEVTEDVSKYTKALVFQ-PGTKT 92
Cdd:pfam00199 1 TTSNGAPVPDNQNSLTAGPRGPLLLQDFHLIEKLAHFDRERIPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSeVGKKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 93 ETLLRFSTVAGELGSPDTWRDVRGFALRFYTEEGNYDLVGNNTPIFFLRDP*KFTHFIRSQKRLPDSGLRDAT*QWDFWT 172
Cdd:pfam00199 81 PVFVRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHSQKRDPQTNLPDPAMFWDFWS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 173 NNPESAHQVTYL*GPRGLPRTWREMNGYGSHTYLWVNAQGEKHWVKYHFISQQGVHNLSNDEATKIAGENADFHRQDLFE 252
Cdd:pfam00199 161 LNPESLHQVTWLFSDRGIPRSYRHMNGFGVHTFKLVNADGERVYVKFHFKTDQGIKNLTWEEAQKLAGKDPDYHTRDLYE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 253 SIAKGDHPKWDLYIQAIPYEEGKTYRFNPFDLTKTISQKDYPRIKVGTLTLNRNPENHFAQIESAAFSPSNTVPGIGLSP 332
Cdd:pfam00199 241 AIERGDYPSWTLYVQVMTEEDAEKFRFNPFDLTKVWPHKDYPLIEVGKMVLNRNPDNYFAEVEQAAFSPSNLVPGIEPSP 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20663751 333 DRMLLGRAFAYHDAQLYRVGAHVNQLPVNRPKNAVHNYAFEGQ*WYD-HTGDRSTYVPNSNG 393
Cdd:pfam00199 321 DPMLQGRLFSYPDTQRYRLGPNYQQLPVNRPPCPVHNYQRDGAMRFDiNQGSRPNYEPNSFG 382
|
|
| Catalase |
smart01060 |
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ... |
17-387 |
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: 662.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 17 NGAPAVSDRQSLTVGSEGPIVLHDTHLLETHQHFNR*NIPERRPHAKGSGAFGEFEVTEDVSKYTKALVFQ-PGTKTETL 95
Cdd:smart01060 1 QGAPVADNQNSLTAGPRGPVLLQDFHLIEKLAHFDRERIPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQkVGKKTPVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 96 LRFSTVAGELGSPDTWRDVRGFALRFYTEEGNYDLVGNNTPIFFLRDP*KFTHFIRSQKRLPDSGLRDAT*QWDFWTNNP 175
Cdd:smart01060 81 VRFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHAQKRDPRTNLPDHDMFWDFWSLNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 176 ESAHQVTYL*GPRGLPRTWREMNGYGSHTYLWVNAQGEKHWVKYHFISQQGVHNLSNDEATKIAGENADFHRQDLFESIA 255
Cdd:smart01060 161 ESLHQVTWLMSDRGIPASYRHMNGFGVHTFKLVNAEGERFYVKFHFKPDQGIKNLTWEEAAKLAGKDPDYHRRDLYEAIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 256 KGDHPKWDLYIQAIPYEEGKTYRFNPFDLTKTISQKDYPRIKVGTLTLNRNPENHFAQIESAAFSPSNTVPGIGLSPDRM 335
Cdd:smart01060 241 RGDYPEWTLYVQVMPEEDAEKFRFDPFDLTKVWPHKDYPLIEVGKMTLNRNPDNYFAEVEQAAFSPSNLVPGIEFSPDKM 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 20663751 336 LLGRAFAYHDAQLYRVGAHVNQLPVNRPKNAVHNYAFEGQ*WYD-HTGDRSTY 387
Cdd:smart01060 321 LQGRLFSYPDTQRYRLGPNYHQLPVNRPRCPVHNYQRDGAMRVDgNQGGDPNY 373
|
|
| catalase_fungal |
cd08157 |
Fungal catalases similar to yeast catalases A and T; Catalase is a ubiquitous enzyme found in ... |
38-482 |
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: 544.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 38 LHDTHLLETHQHFNR*NIPERRPHAKGSGAFGEFEVTEDVSKYTKALVFQ-PGTKTETLLRFSTVAGELGSPDTWRDVRG 116
Cdd:cd08157 1 LQDFHLIDTLAHFDRERIPERVVHAKGAGAYGEFEVTDDISDITSADMLQgVGKKTPCLVRFSTVGGEKGSADTVRDPRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 117 FALRFYTEEGNYDLVGNNTPIFFLRDP*KFTHFIRSQKRLPDSGLRDAT*QWDFWTNNPESAHQVTYL*GPRGLPRTWRE 196
Cdd:cd08157 81 FAVKFYTEEGNWDWVFNNTPVFFIRDPIKFPHFIHSQKRDPQTNLKDSTMFWDYLSQNPESIHQVMILFSDRGTPASYRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 197 MNGYGSHTYLWVNAQGEKHWVKYHFISQQGVHNLSNDEATKIAGENADFHRQDLFESIAKGDHPKWDLYIQAIPYEEGKT 276
Cdd:cd08157 161 MNGYSGHTYKWVNPDGSFKYVQFHLKSDQGPKFLTGEEAARLAGSNPDYATKDLFEAIERGDYPSWTVYVQVMTPEQAEK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 277 YRFNPFDLTKTISQKDYPRIKVGTLTLNRNPENHFAQIESAAFSPSNTVPGIGLSPDRMLLGRAFAYHDAQLYRVGAHVN 356
Cdd:cd08157 241 LRFNIFDLTKVWPHKDFPLRPVGKLTLNENPKNYFAEIEQAAFSPSHMVPGIEPSADPVLQARLFSYPDAHRHRLGPNYQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 357 QLPVNRPKNA-VHN-YAFEG-Q*WYDHTGDRSTYVPNSNGDSWSDETGPVdDGWEADGTLTREAQALRADDDDFGQAGTL 433
Cdd:cd08157 321 QLPVNRPKTSpVYNpYQRDGpMSVNGNYGGDPNYVSSILPPTYFKKRVDA-DGHHENWVGEVVAFLTEITDEDFVQPRAL 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 20663751 434 VREVFSDQERDDFVETVAGALKGVRQDVQARAFEYWKNVDATIGQRIED 482
Cdd:cd08157 400 WEVVGKPGQQERFVKNVAGHLSGAPPEIRKRVYEIFARVNPDLGKRIEK 448
|
|
| catalase_clade_1 |
cd08154 |
Clade 1 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
14-480 |
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: 538.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 14 TRQNGAPAVSDRQSLTVGSEGPIVLHDTHLLETHQHFNR*NIPERRPHAKGSGAFGEFEVTEDVSKYTKALVFQ-PGTKT 92
Cdd:cd08154 3 TTNQGAPVGDNQNSQTVGPRGPVLLEDYHLIEKLAHFDRERIPERVVHARGAGAHGYFEAYGDISDYTRASFLQePGKKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 93 ETLLRFSTVAGELGSPDTWRDVRGFALRFYTEEGNYDLVGNNTPIFFLRDP*KFTHFIRSQKRLPDSGLRDAT*QWDFWT 172
Cdd:cd08154 83 PVFVRFSTVIHGKGSPETLRDPRGFAVKFYTEEGNWDLVGNNLPVFFIRDAIKFPDMIHALKPSPVTNIQDPNRIFDFFS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 173 NNPESAHQVTYL*GPRGLPRTWREMNGYGSHTYLWVNAQGEKHWVKYHFISQQGVHNLSNDEATKIAGENADFHRQDLFE 252
Cdd:cd08154 163 HVPESTHMLTFLYSDWGTPASYRHMDGSGVHTYKWVNAEGKVVYVKYHWKPKQGVKNLTAEEAAEVQGKNFNHATQDLYD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 253 SIAKGDHPKWDLYIQAIPYEEGKTYRFNPFDLTKTISQKDYPRIKVGTLTLNRNPENHFAQIESAAFSPSNTVPGIGLSP 332
Cdd:cd08154 243 AIAAGNYPEWELYVQIMDPKDLDKLDFDPLDDTKIWPEDQFPLKPVGKMTLNKNPDNFFAEVEQVAFSPGNLVPGIEPSD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 333 DRMLLGRAFAYHDAQLYRVGAHVNQLPVNRPKNAVHNYAFEGQ*WYDHTGDRSTYVPNSNGDSWSDETGPvDDGWEADGT 412
Cdd:cd08154 323 DKMLQGRLFSYSDTQRYRLGPNYLQLPINAPKAAVHNNQRDGQMNYGHDTSDVNYEPSRLDGLPEAPKYP-YSQPPLSGT 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20663751 413 LTreaQALRADDDDFGQAGTLVREvFSDQERDDFVETVAGALKGVRQDVQARAFEYWKNVDATIGQRI 480
Cdd:cd08154 402 TQ---QAPIAKTNNFKQAGERYRS-FSEEEQENLIKNLVVDLSDVNEEIKLRMLSYFSQADPDYGERV 465
|
|
| PLN02609 |
PLN02609 |
catalase |
14-481 |
2.45e-170 |
|
catalase
Pssm-ID: 215328 [Multi-domain] Cd Length: 492 Bit Score: 489.64 E-value: 2.45e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 14 TRQNGAPAVSDRQSLTVGSEGPIVLHDTHLLETHQHFNR*NIPERRPHAKGSGAFGEFEVTEDVSKYTKALVFQ-PGTKT 92
Cdd:PLN02609 18 TTNSGAPVWNNNSSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDISNLTCADFLRaPGVQT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 93 ETLLRFSTVAGELGSPDTWRDVRGFALRFYTEEGNYDLVGNNTPIFFLRDP*KFTHFIRSQKRLPDSGLRDAT*QWDFWT 172
Cdd:PLN02609 98 PVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDMVGNNFPVFFIRDGMKFPDMVHALKPNPKTHIQEPWRILDFLS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 173 NNPESAHQVTYL*GPRGLPRTWREMNGYGSHTYLWVNAQGEKHWVKYHFISQQGVHNLSNDEATKIAGENADFHRQDLFE 252
Cdd:PLN02609 178 HHPESLHMFTFLFDDRGIPQDYRHMEGFGVHTYKLINKAGKAHYVKFHWKPTCGVKNLLDEEAVRVGGSNHSHATQDLYD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 253 SIAKGDHPKWDLYIQAIPYEEGKTYRFNPFDLTKTISQKDYPRIKVGTLTLNRNPENHFAQIESAAFSPSNTVPGIGLSP 332
Cdd:PLN02609 258 SIAAGNYPEWKLFIQTMDPEDEDKFDFDPLDVTKTWPEDILPLQPVGRLVLNRNIDNFFAENEQLAFCPAIVVPGIYYSD 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 333 DRMLLGRAFAYHDAQLYRVGAHVNQLPVNRPKNAVHNYAFEGQ*WYDHTGDRSTYVPNSNGDSWSDETGPVDDGWEAdgt 412
Cdd:PLN02609 338 DKLLQTRIFAYADTQRHRLGPNYLQLPVNAPKCAHHNNHHEGFMNFMHRDEEVNYFPSRFDPVRHAERVPIPHPPLS--- 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20663751 413 lTREAQALRADDDDFGQAGTLVREvFSDQERDDFVETVAGALKGVRQDVQARAF--EYWKNVDATIGQRIE 481
Cdd:PLN02609 415 -GRREKCKIEKENNFKQPGERYRS-WSPDRQERFIKRWVDALSDPRVTHEIRSIwiSYWSQCDKSLGQKLA 483
|
|
| catalase |
cd00328 |
Catalase heme-binding enzyme; Catalase is a ubiquitous enzyme found in both prokaryotes and ... |
54-480 |
3.12e-164 |
|
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: 471.95 E-value: 3.12e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 54 NIPERRPHAKGSGAFGEFEVTEDVSKYTKALVFQ-PGTKTETLLRFSTVAGELGSPDTWRDVRGFALRFYTEEGNYDLVG 132
Cdd:cd00328 1 RIPERVVHARGAGAFGYFTAYGDWSDISAAAFFSaIGKKTPVFVRFSTVVGGAGSADTVRDPHGFATKFYTEEGNFDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 133 NNTPIFFLRDP*KFTHFIRSQKRLPDSGLRDAT*QWDFWTNNPESAHQVTYL*GPRGLPRTWREMNGYGSHTYLWVNAQG 212
Cdd:cd00328 81 NNTPIFFIRDAIKFPDFIHAQKPNPQTALPDADRFWDFLSLRPESLHQVSFLFSDRGIPAAYRHMNGYGSHTFKLVNANG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 213 EKHWVKYHFISQQGVHNLSNDEATKIAGENADFHRQDLFESIAKGDHPKWDLYIQAIPYEEGKTYRFNPFDLTKTISQKD 292
Cdd:cd00328 161 KVHYVKFHWKTDQGIANLVWEEAARLAGEDPDYHRQDLFEAIEAGDYPSWELYIQVMTFNDAEKFPFNPLDPTKVWPEEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 293 YPRIKVGTLTLNRNPENHFAQIESAAFSPSNTVPGIGLSPDRMLLGRAFAYHDAQLYRVGAHVNQLPVNRPKNAVHNYAF 372
Cdd:cd00328 241 VPLIVVGKLVLNRNPLNFFAEVEQAAFDPGHIVPGVEFSEDPLLQGRLFSYADTQLYRLGPNFQQLPVNRPYAPVHNNQR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 373 EGQ*WYDHTGDRSTYVPNSNGDSWSDETGPVDD---GWEADGTLTREAQAlrADDDDFGQAGTLVReVFSDQERDDFVET 449
Cdd:cd00328 321 DGAGNMNDNTGVPNYEPNAKDVRYPAQGAPKFDrghFSHWKSGVNREAST--TNDDNFTQARLFYR-SLTPGQQKRLVDA 397
|
410 420 430
....*....|....*....|....*....|..
gi 20663751 450 VAGALKGVRQ-DVQARAFEYWKNVDATIGQRI 480
Cdd:cd00328 398 FRFELADAVSpQIQQRVLDQFAKVDAAAAKRV 429
|
|
| catalase_clade_2 |
cd08155 |
Clade 2 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
55-480 |
2.23e-138 |
|
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: 406.37 E-value: 2.23e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 55 IPERRPHAKGSGAFGEFEVTEDVSKYTKALVFQ-PGTKTETLLRFSTVAGELGSPDTWRDVRGFALRFYTEEGNYDLVGN 133
Cdd:cd08155 5 IPERVVHARGSGAHGYFQVYESLSQYTKAKFLQdPGKKTPVFVRFSTVAGSRGSADTVRDVRGFAVKFYTEEGNYDLVGN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 134 NTPIFFLRDP*KFTHFIRSQKRLPDSGLRDAT*Q----WDFWTNNPESAHQVTYL*GPRGLPRTWREMNGYGSHTYLWVN 209
Cdd:cd08155 85 NIPVFFIQDAIKFPDLIHAVKPEPHNEMPQAQSAhdtfWDFVSLQPESAHMVMWAMSDRAIPRSYRMMEGFGVHTFRLVN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 210 AQGEKHWVKYHFISQQGVHNLSNDEATKIAGENADFHRQDLFESIAKGDHPKWDLYIQAIPYEEGKTYRFNPFDLTKTIS 289
Cdd:cd08155 165 AQGKSTFVKFHWKPVLGVHSLVWDEAQKIAGKDPDFHRRDLWEAIESGDYPEWELGVQLIDEEDEFKFDFDILDPTKLIP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 290 QKDYPRIKVGTLTLNRNPENHFAQIESAAFSPSNTVPGIGLSPDRMLLGRAFAYHDAQLYRVG-AHVNQLPVNRPKNAVH 368
Cdd:cd08155 245 EELVPVQRVGKMVLNRNPDNFFAETEQVAFCPANVVPGIDFSNDPLLQGRLFSYLDTQLSRLGgPNFHELPINRPVCPVH 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 369 NYAFEGQ*WYDHTGDRSTYVPNSNGDSWSDETGPVDDGWE-----ADGTLTREaqalRAD--DDDFGQAgTLVREVFSDQ 441
Cdd:cd08155 325 NNQRDGHMRMTINKGRVNYFPNSLGAGPPRAASPAEGGFVhypekVEGPKIRI----RSEsfADHYSQA-RLFWNSMSPV 399
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 20663751 442 ERDDFVETVAGAL-KGVRQDVQARAFEYWKNVDATIGQRI 480
Cdd:cd08155 400 EKEHIISAFTFELsKVETPEIRERVVDHLANIDEDLAKKV 439
|
|
| katE |
PRK11249 |
hydroperoxidase II; Provisional |
9-480 |
7.24e-128 |
|
hydroperoxidase II; Provisional
Pssm-ID: 236886 [Multi-domain] Cd Length: 752 Bit Score: 389.79 E-value: 7.24e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 9 HATGST-RQNGAPAVSDRQ-SLTVGSEGPIVLHDTHLLETHQHFNR*NIPERRPHAKGSGAFGEFEVTEDVSKYTKALVF 86
Cdd:PRK11249 71 GSEGYAlTTNQGVRIADDQnSLRAGSRGPSLLEDFILREKITHFDHERIPERIVHARGSAAHGYFQPYKSLSDITKAAFL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 87 Q-PGTKTETLLRFSTVAGELGSPDTWRDVRGFALRFYTEEGNYDLVGNNTPIFFLRDP*KFTHFIRSQK-----RLPDSG 160
Cdd:PRK11249 151 QdPGKITPVFVRFSTVQGPRGSADTVRDIRGFATKFYTEEGNFDLVGNNTPVFFIQDAIKFPDFVHAVKpephnEIPQGQ 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 161 LRDAT*qWDFWTNNPESAHQVTYL*GPRGLPRTWREMNGYGSHTYLWVNAQGEKHWVKYHFISQQGVHNLSNDEATKIAG 240
Cdd:PRK11249 231 SAHDTF-WDYVSLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLINAEGKATFVRFHWKPVAGKASLVWDEAQKLTG 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 241 ENADFHRQDLFESIAKGDHPKWDLYIQAIPYEEGKTYRFNPFDLTKTISQKDYPRIKVGTLTLNRNPENHFAQIESAAFS 320
Cdd:PRK11249 310 RDPDFHRRDLWEAIEAGDYPEYELGVQLIPEEDEFKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFH 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 321 PSNTVPGIGLSPDRMLLGRAFAYHDAQLYRV-GAHVNQLPVNRPKNAVHNYAFEGQ*WYD-HTGdRSTYVPNSNGDSWSD 398
Cdd:PRK11249 390 PGHIVPGIDFTNDPLLQGRLFSYTDTQISRLgGPNFHEIPINRPTCPYHNFQRDGMHRMTiDTG-PANYEPNSINGNWPR 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 399 ET--GPVDDGWEA-----DGTLTREaqalRADD--DDFGQAgTLVREVFSDQERDDFVETVAGAL-KGVRQDVQARAFEY 468
Cdd:PRK11249 469 ETppAPKRGGFESyqervEGNKVRE----RSPSfgDYYSQP-RLFWLSQTPIEQRHIIDAFSFELgKVVRPYIRERVVDQ 543
|
490
....*....|..
gi 20663751 469 WKNVDATIGQRI 480
Cdd:PRK11249 544 LAHIDLTLAQAV 555
|
|
| catalase_like |
cd08150 |
Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found ... |
56-350 |
4.22e-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: 180.83 E-value: 4.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 56 PERRPHAKGSGAFGEFEVTEDVSKYTKALVFQPGTKTETLLRFSTVAgelGSPDTWRDVRGFALRFYTE--EGNYDLVGN 133
Cdd:cd08150 1 GLRGQHFQGTCAFGTFEVLADLKERLRVGLFAEGKVYPAYIRFSNGA---GIDDTKPDIRGFAIKFTGVadAGTLDFVLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 134 NTPIFFLRDP*KFTHFIRSQKRlPDSGLRDAT*QWDFWTNNPESAHQVTYL*gpRGLPRTWREMNGYGSHTYLWVNAQGE 213
Cdd:cd08150 78 NTPVFFIRNTSDYEDFVAEFAR-SARGEPPLDFIAWYVEKRPEDLPNLLGAR--SQVPDSYAAARYFSQVTFAFINGAGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 214 KHWVKYHFISQQGVHNLSNDEATkiaGENADFHRQDLFESIAKGDhPKWDLYIQAIPyEEGKTYRFNPfdlTKTISqKDY 293
Cdd:cd08150 155 YRVVRSKDNPVDGIPSLEDHELE---ARPPDYLREELTERLQRGP-VVYDFRIQLND-DTDATTIDNP---TILWP-TEH 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 20663751 294 PRIKVGTLTLNRNPENhfAQIESAAFSPSNTVPGIGLSPDR--MLLGRAFAYHDAQLYR 350
Cdd:cd08150 226 PVEAVAKITIPPPTFT--AAQEAFAFNPFTPWHGLLETNDLgpILEVRRRVYTSSQGLR 282
|
|
| srpA_like |
cd08153 |
Catalase-like heme-binding proteins similar to the uncharacterized srpA; Catalase is a ... |
58-344 |
4.44e-43 |
|
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: 154.70 E-value: 4.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 58 RRPHAKGSGAFGEFEVTEDVSKYTKALVFQPGTkTETLLRFSTVAGELGSPDTWRDVRGFALRFYTEEGN-YDLVGNNTP 136
Cdd:cd08153 15 RRNHAKGICVSGTFTPSGAAASLSRAPLFSGGS-VPVTGRFSLGGGNPKAPDDAANPRGMALKFRLPDGEqWRMVMNSFP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 137 IFFLRDP*KFTHFIrsQKRLPDS-GLRDAT*QWDFWTNNPESAHQVTYL*GPRGLPRTWREMNGYGSHTYLWVNAQGEKH 215
Cdd:cd08153 94 VFPVRTPEEFLALL--KAIAPDAtGKPDPAKLKAFLAAHPEAAAFLAWI-KTAPPPASFANTTYYGVNAFYFTNANGKRQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 216 WVKYHFISQQGVHNLSNDEAtkiAGENADFHRQDLFESIAKGdhP-KWDLYIQ-AipyeegktyrfNPFDLTKTISQ--- 290
Cdd:cd08153 171 PVRWRFVPEDGVKYLSDEEA---AKLGPDFLFDELAQRLAQG--PvRWDLVLQlA-----------EPGDPTDDPTKpwp 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 20663751 291 KDYPRIKVGTLTLNRNPENHFAQIESAAFSPSNTVPGIGLSPDRMLLGRAFAYH 344
Cdd:cd08153 235 ADRKEVDAGTLTITKVAPDQGGACRDINFDPLVLPDGIEPSDDPLLAARSAAYA 288
|
|
| Catalase-rel |
pfam06628 |
Catalase-related immune-responsive; This family represents a small conserved region within ... |
424-482 |
9.43e-16 |
|
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: 71.63 E-value: 9.43e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 424 DDDFGQAGTLVReVFSDQERDDFVETVAGALKGV-RQDVQARAFEYWKNVDATIGQRIED 482
Cdd:pfam06628 5 DDHFSQAGLFYR-SMSEEERQRLVDNIAFELSKVtDPEIQERMVAHFYKVDPDLGQRVAE 63
|
|
| y4iL_like |
cd08152 |
Catalase-like heme-binding proteins similar to the uncharacterized y4iL; Catalase is a ... |
61-326 |
8.48e-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: 59.97 E-value: 8.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 61 HAKGSGAF-GEFEVTEDVSKYTKALVFQPGTKTETLLRFSTVAGELgSPDTWRDVRGFALRFY----------TEEGNYD 129
Cdd:cd08152 8 HAKSHGCLkAEFTVLDDLPPELAQGLFAEPGTYPAVIRFSNAPGDI-LDDSVPDPRGMAIKVLgvpgekllpeEDATTQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 130 LVGNNTPIFFLRDP*KFTHFIRSQKRLPDSG--------------LRDAT*QWDFWTNNPESAHQVTYL*GPRglprtwr 195
Cdd:cd08152 87 FVLVNHPVFFARDAKDYLALLKLLARTTSLPdgakaalsaplrgaLRVLEAAGGESPTLKLGGHPPAHPLGET------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 196 emngYGSHT-YLWvnaqGEkHWVKYHFISQQGvHNLSNDEATKIAGENADFHRQDLFESIAKGDHpKWDLYIQ------A 268
Cdd:cd08152 160 ----YWSQApYRF----GD-YVAKYSVVPASP-ALPALTGKELDLTDDPDALREALADFLAENDA-EFEFRIQlctdleK 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20663751 269 IPYEegktyrfnpfDLTKTISQKDYPRIKVGTLTLNR----NPENHFAQIESAAFSPSNTVP 326
Cdd:cd08152 229 MPIE----------DASVEWPEALSPFVPVATITIPPqdfdSPARQRAFDDNLSFNPWHGLA 280
|
|
| AOS |
cd08151 |
Allene oxide synthase; Allene oxide synthase converts a fatty acid hydroperoxide to an allene ... |
58-332 |
2.46e-08 |
|
Allene oxide synthase; Allene oxide synthase converts a fatty acid hydroperoxide to an allene oxide, which is an unstable epoxide. In corals, the enzyme is part of a eiconaosid synthesis pathway that is initiated by a lipoxygenase, which generates the fatty acid hydroperoxides in the first step. The structure of allene oxide synthase closely resembles that of catalase, but allene oxide synthase does not have catalase activity.
Pssm-ID: 163707 Cd Length: 328 Bit Score: 55.51 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 58 RRP-HAKGSGAFGEFEVTEDvSKYTKALVFQPGTKTETLLRFSTVAGelGSPDTWRDVRGFALRFYT----EEGNYDLVG 132
Cdd:cd08151 27 RRGtHTIGVGAKGVLTVLAE-SDFPEHAFFTAGKRFPVILRHANIVG--GDDDASLDGRGAALRFLNagddDAGPLDLVM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 133 NNTPIFFLRDP*KFTHFIRsqkrlpdSGLRDAT*QWDFWtnnpESAHQVTYL*GPRGLPRTWREMNGYGSHTYLWVNAQG 212
Cdd:cd08151 104 NTGESFGFWTAASFADFAG-------AGLPFREKAAKLR----GPLARYAVWASLRRAPDSYTDLHYYSQICYEFVALDG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20663751 213 EKHWVKYHFI--SQQGVHNLSNDEATKIAGENADFH-------RQDLF---ESIAKGDHPKWDLYIQAIPYEEGKTYRFN 280
Cdd:cd08151 173 KSRYARFRLLppDADTEWDLGEDVLETIFQRPRLYLprlpgdtRPKDYlrnEFRQRLQSPGVRYRLQIQLREVSDDATAV 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 20663751 281 PFDLTKTISQKDYPRIKVGTLTLNRNPENHfaQIESAAFSPSNTVPGIGLSP 332
Cdd:cd08151 253 ALDCCRPWDEDEHPWLDLAVVRLGAPLPND--ELEKLAFNPGNTPESLGLPL 302
|
|
| |
