|
Name |
Accession |
Description |
Interval |
E-value |
| katE |
PRK11249 |
hydroperoxidase II; Provisional |
43-706 |
0e+00 |
|
hydroperoxidase II; Provisional
Pssm-ID: 236886 [Multi-domain] Cd Length: 752 Bit Score: 780.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 43 LSQFYLNDTDAFMTTDVGGPIED-QNSLTAGDRGPTLLEDFIFRQKIQRFDHERVPERAVHARGTGAHGVFTSYGDFSNI 121
Cdd:PRK11249 65 LEAFRKGSEGYALTTNQGVRIADdQNSLRAGSRGPSLLEDFILREKITHFDHERIPERIVHARGSAAHGYFQPYKSLSDI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 122 TAASFLGKEGKETPVFVRFSTVAGSRGSSDLSRDVHGFATRFYTDEGNFDIVGNNIPVFFIQDAILFPDLIHAVKPRGDN 201
Cdd:PRK11249 145 TKAAFLQDPGKITPVFVRFSTVQGPRGSADTVRDIRGFATKFYTEEGNFDLVGNNTPVFFIQDAIKFPDFVHAVKPEPHN 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 202 EIPQAATAHDSAWDFFSQQPSALHTLFWAMSGHGIPRSFRHVDGFGVHTFRFVTDDGATKLVKFHWTSLQGRASMVWEEA 281
Cdd:PRK11249 225 EIPQGQSAHDTFWDYVSLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLINAEGKATFVRFHWKPVAGKASLVWDEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 282 QQTSGKNPDYMRQDLFEAIEAGRYPEWELGVQIMDEEDQLRFGFDLLDPTKIVPEELVPITKLGKMQLNRNPRNYFAETE 361
Cdd:PRK11249 305 QKLTGRDPDFHRRDLWEAIEAGDYPEYELGVQLIPEEDEFKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAETE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 362 QVMFQPGHIVRGVDFTEDPLLQGRIFSYLDTQLNRHGGPNFEQLPINQPRVPVHNNNRDGAGQMFIPLNPHAYSPKTPTN 441
Cdd:PRK11249 385 QVAFHPGHIVPGIDFTNDPLLQGRLFSYTDTQISRLGGPNFHEIPINRPTCPYHNFQRDGMHRMTIDTGPANYEPNSING 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 442 ESPKQ---ANQtvGKGFFTAPERkVSGKLIRAVSPTFEDVWSQPRLFYNSLIPAEQQFIIDAIRFENANVKSPIVKNNVV 518
Cdd:PRK11249 465 NWPREtppAPK--RGGFESYQER-VEGNKVRERSPSFGDYYSQPRLFWLSQTPIEQRHIIDAFSFELGKVVRPYIRERVV 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 519 IQLNRVDNDLARRVARAIG---------------VNEPEPDPKFYHNNKTanvgtfGGKLKkldGLKVGFFAsvqhASSL 583
Cdd:PRK11249 542 DQLAHIDLTLAQAVAENLGipltdeqlnitpppdVNGLKKDPALSLYAIP------DGDIK---GRKVAILL----NDGV 608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 584 DAAS--ALRASLSKAGVDVVVVAERLA-----DG----VDQTYSTSDAIQFDAIIIAAGAETLFSLSSftggsanttagt 652
Cdd:PRK11249 609 DAADllAILKALKAKGVHAKLLYPRMGevtadDGtvlpIAATFAGAPSLTFDAVIVPGGKANIADLAD------------ 676
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 121712100 653 tslypTGRPLQILIDGFRFGKTVGALGSGTAALRNAGITTSRDGVVVAQSADDG 706
Cdd:PRK11249 677 -----NGDARYYLLEAYKHLKPIALAGDARKLKAALKLPDQGEEGLVEADSADG 725
|
|
| KatE |
COG0753 |
Catalase [Inorganic ion transport and metabolism]; |
47-546 |
0e+00 |
|
Catalase [Inorganic ion transport and metabolism];
Pssm-ID: 440516 [Multi-domain] Cd Length: 489 Bit Score: 777.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 47 YLNDTDAFMTTDVGGPIED-QNSLTAGDRGPTLLEDFIFRQKIQRFDHERVPERAVHARGTGAHGVFTSYGDFSNITAAS 125
Cdd:COG0753 3 YADDEGKTLTTNQGAPVADnQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFEVTEDISKYTKAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 126 FLGKEGKETPVFVRFSTVAGSRGSSDLSRDVHGFATRFYTDEGNFDIVGNNIPVFFIQDAILFPDLIHAVKPRGDNEIPQ 205
Cdd:COG0753 83 FFQEPGKKTPVFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHAQKRDPDTNLPQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 206 aataHDSAWDFFSQQPSALHTLFWAMSGHGIPRSFRHVDGFGVHTFRFVTDDGATKLVKFHWTSLQGRASMVWEEAQQTS 285
Cdd:COG0753 163 ----HDTFWDFWSLSPESLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAEGERFWVKFHWKPKQGIHSLTWDEAQKIA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 286 GKNPDYMRQDLFEAIEAGRYPEWELGVQIMDEEDQLRFGFDLLDPTKIVPEELVPITKLGKMQLNRNPRNYFAETEQVMF 365
Cdd:COG0753 239 GKDPDFHRRDLYEAIERGDFPEWELGVQVMPEEDADKFDFDPLDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAETEQAAF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 366 QPGHIVRGVDFTEDPLLQGRIFSYLDTQLNRHgGPNFEQLPINQPRVPVHNNNRDGAGQMFIPLNPHAYSPKtpTNESPK 445
Cdd:COG0753 319 SPGNLVPGIDFSPDKMLQGRLFSYADTQRYRL-GPNFHQLPVNRPKCPVHNYQRDGAMRYDINGGRVNYEPN--SLGGPR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 446 QANQtvgkgfFTAPERKVSGKLIRAVSPTfEDVWSQPRLFYNSLIPAEQQFIIDAIRFENANVKSPIVKNNVVIQLNRVD 525
Cdd:COG0753 396 EDPG------FKEPPLKVDGDKVRYRSES-DDHFSQAGLLYRSMSDEEKQHLIDNIAFELGKVESEEIRERMVAHFYNVD 468
|
490 500
....*....|....*....|.
gi 121712100 526 NDLARRVARAIGVNEPEPDPK 546
Cdd:COG0753 469 PELGARVAEALGLDLPEAKAL 489
|
|
| catalase_clade_2 |
cd08155 |
Clade 2 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
92-536 |
0e+00 |
|
Clade 2 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes, which is involved in the protection of cells from the toxic effects of peroxides. It catalyzes the conversion of hydrogen peroxide to water and molecular oxygen. Catalases also utilize hydrogen peroxide to oxidize various substrates such as alcohol or phenols. Clade 2 catalases are mostly found in bacteria and fungi; they have a large subunit size of 75 to 84 kDa, and bind a heme d group buried deep inside the structure. They appear to form tetramers. In eukaryotic cells, catalases are located in peroxisomes.
Pssm-ID: 163711 Cd Length: 443 Bit Score: 694.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 92 DHERVPERAVHARGTGAHGVFTSYGDFSNITAASFLGKEGKETPVFVRFSTVAGSRGSSDLSRDVHGFATRFYTDEGNFD 171
Cdd:cd08155 1 DHERIPERVVHARGSGAHGYFQVYESLSQYTKAKFLQDPGKKTPVFVRFSTVAGSRGSADTVRDVRGFAVKFYTEEGNYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 172 IVGNNIPVFFIQDAILFPDLIHAVKPRGDNEIPQAATAHDSAWDFFSQQPSALHTLFWAMSGHGIPRSFRHVDGFGVHTF 251
Cdd:cd08155 81 LVGNNIPVFFIQDAIKFPDLIHAVKPEPHNEMPQAQSAHDTFWDFVSLQPESAHMVMWAMSDRAIPRSYRMMEGFGVHTF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 252 RFVTDDGATKLVKFHWTSLQGRASMVWEEAQQTSGKNPDYMRQDLFEAIEAGRYPEWELGVQIMDEEDQLRFGFDLLDPT 331
Cdd:cd08155 161 RLVNAQGKSTFVKFHWKPVLGVHSLVWDEAQKIAGKDPDFHRRDLWEAIESGDYPEWELGVQLIDEEDEFKFDFDILDPT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 332 KIVPEELVPITKLGKMQLNRNPRNYFAETEQVMFQPGHIVRGVDFTEDPLLQGRIFSYLDTQLNRHGGPNFEQLPINQPR 411
Cdd:cd08155 241 KLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFCPANVVPGIDFSNDPLLQGRLFSYLDTQLSRLGGPNFHELPINRPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 412 VPVHNNNRDGAGQMFIPLNPHAYSPKTPTNESPKQANQTVGkGFFTAPErKVSGKLIRAVSPTFEDVWSQPRLFYNSLIP 491
Cdd:cd08155 321 CPVHNNQRDGHMRMTINKGRVNYFPNSLGAGPPRAASPAEG-GFVHYPE-KVEGPKIRIRSESFADHYSQARLFWNSMSP 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 121712100 492 AEQQFIIDAIRFENANVKSPIVKNNVVIQLNRVDNDLARRVARAI 536
Cdd:cd08155 399 VEKEHIISAFTFELSKVETPEIRERVVDHLANIDEDLAKKVAKGL 443
|
|
| Catalase |
pfam00199 |
Catalase; |
56-436 |
0e+00 |
|
Catalase;
Pssm-ID: 459708 Cd Length: 383 Bit Score: 679.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 56 TTDVGGPIED-QNSLTAGDRGPTLLEDFIFRQKIQRFDHERVPERAVHARGTGAHGVFTSYGDFSNITAASFLGKEGKET 134
Cdd:pfam00199 1 TTSNGAPVPDnQNSLTAGPRGPLLLQDFHLIEKLAHFDRERIPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSEVGKKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 135 PVFVRFSTVAGSRGSSDLSRDVHGFATRFYTDEGNFDIVGNNIPVFFIQDAILFPDLIHAVKPRGDNEIPQAATAhdsaW 214
Cdd:pfam00199 81 PVFVRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHSQKRDPQTNLPDPAMF----W 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 215 DFFSQQPSALHTLFWAMSGHGIPRSFRHVDGFGVHTFRFVTDDGATKLVKFHWTSLQGRASMVWEEAQQTSGKNPDYMRQ 294
Cdd:pfam00199 157 DFWSLNPESLHQVTWLFSDRGIPRSYRHMNGFGVHTFKLVNADGERVYVKFHFKTDQGIKNLTWEEAQKLAGKDPDYHTR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 295 DLFEAIEAGRYPEWELGVQIMDEEDQLRFGFDLLDPTKIVPEELVPITKLGKMQLNRNPRNYFAETEQVMFQPGHIVRGV 374
Cdd:pfam00199 237 DLYEAIERGDYPSWTLYVQVMTEEDAEKFRFNPFDLTKVWPHKDYPLIEVGKMVLNRNPDNYFAEVEQAAFSPSNLVPGI 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 121712100 375 DFTEDPLLQGRIFSYLDTQLNRHgGPNFEQLPINQPRVPVHNNNRDGAGQMFIPLNPHA-YSP 436
Cdd:pfam00199 317 EPSPDPMLQGRLFSYPDTQRYRL-GPNYQQLPVNRPPCPVHNYQRDGAMRFDINQGSRPnYEP 378
|
|
| Catalase |
smart01060 |
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ... |
60-434 |
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: 654.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 60 GGPIED-QNSLTAGDRGPTLLEDFIFRQKIQRFDHERVPERAVHARGTGAHGVFTSYGDFSNITAASFLGKEGKETPVFV 138
Cdd:smart01060 2 GAPVADnQNSLTAGPRGPVLLQDFHLIEKLAHFDRERIPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQKVGKKTPVFV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 139 RFSTVAGSRGSSDLSRDVHGFATRFYTDEGNFDIVGNNIPVFFIQDAILFPDLIHAVKPRGDNEIPQaataHDSAWDFFS 218
Cdd:smart01060 82 RFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHAQKRDPRTNLPD----HDMFWDFWS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 219 QQPSALHTLFWAMSGHGIPRSFRHVDGFGVHTFRFVTDDGATKLVKFHWTSLQGRASMVWEEAQQTSGKNPDYMRQDLFE 298
Cdd:smart01060 158 LNPESLHQVTWLMSDRGIPASYRHMNGFGVHTFKLVNAEGERFYVKFHFKPDQGIKNLTWEEAAKLAGKDPDYHRRDLYE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 299 AIEAGRYPEWELGVQIMDEEDQLRFGFDLLDPTKIVPEELVPITKLGKMQLNRNPRNYFAETEQVMFQPGHIVRGVDFTE 378
Cdd:smart01060 238 AIERGDYPEWTLYVQVMPEEDAEKFRFDPFDLTKVWPHKDYPLIEVGKMTLNRNPDNYFAEVEQAAFSPSNLVPGIEFSP 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 121712100 379 DPLLQGRIFSYLDTQLNRHgGPNFEQLPINQPRVPVHNNNRDGAGQMFIPLNPHAY 434
Cdd:smart01060 318 DKMLQGRLFSYPDTQRYRL-GPNYHQLPVNRPRCPVHNYQRDGAMRVDGNQGGDPN 372
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| katE |
PRK11249 |
hydroperoxidase II; Provisional |
43-706 |
0e+00 |
|
hydroperoxidase II; Provisional
Pssm-ID: 236886 [Multi-domain] Cd Length: 752 Bit Score: 780.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 43 LSQFYLNDTDAFMTTDVGGPIED-QNSLTAGDRGPTLLEDFIFRQKIQRFDHERVPERAVHARGTGAHGVFTSYGDFSNI 121
Cdd:PRK11249 65 LEAFRKGSEGYALTTNQGVRIADdQNSLRAGSRGPSLLEDFILREKITHFDHERIPERIVHARGSAAHGYFQPYKSLSDI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 122 TAASFLGKEGKETPVFVRFSTVAGSRGSSDLSRDVHGFATRFYTDEGNFDIVGNNIPVFFIQDAILFPDLIHAVKPRGDN 201
Cdd:PRK11249 145 TKAAFLQDPGKITPVFVRFSTVQGPRGSADTVRDIRGFATKFYTEEGNFDLVGNNTPVFFIQDAIKFPDFVHAVKPEPHN 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 202 EIPQAATAHDSAWDFFSQQPSALHTLFWAMSGHGIPRSFRHVDGFGVHTFRFVTDDGATKLVKFHWTSLQGRASMVWEEA 281
Cdd:PRK11249 225 EIPQGQSAHDTFWDYVSLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLINAEGKATFVRFHWKPVAGKASLVWDEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 282 QQTSGKNPDYMRQDLFEAIEAGRYPEWELGVQIMDEEDQLRFGFDLLDPTKIVPEELVPITKLGKMQLNRNPRNYFAETE 361
Cdd:PRK11249 305 QKLTGRDPDFHRRDLWEAIEAGDYPEYELGVQLIPEEDEFKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAETE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 362 QVMFQPGHIVRGVDFTEDPLLQGRIFSYLDTQLNRHGGPNFEQLPINQPRVPVHNNNRDGAGQMFIPLNPHAYSPKTPTN 441
Cdd:PRK11249 385 QVAFHPGHIVPGIDFTNDPLLQGRLFSYTDTQISRLGGPNFHEIPINRPTCPYHNFQRDGMHRMTIDTGPANYEPNSING 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 442 ESPKQ---ANQtvGKGFFTAPERkVSGKLIRAVSPTFEDVWSQPRLFYNSLIPAEQQFIIDAIRFENANVKSPIVKNNVV 518
Cdd:PRK11249 465 NWPREtppAPK--RGGFESYQER-VEGNKVRERSPSFGDYYSQPRLFWLSQTPIEQRHIIDAFSFELGKVVRPYIRERVV 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 519 IQLNRVDNDLARRVARAIG---------------VNEPEPDPKFYHNNKTanvgtfGGKLKkldGLKVGFFAsvqhASSL 583
Cdd:PRK11249 542 DQLAHIDLTLAQAVAENLGipltdeqlnitpppdVNGLKKDPALSLYAIP------DGDIK---GRKVAILL----NDGV 608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 584 DAAS--ALRASLSKAGVDVVVVAERLA-----DG----VDQTYSTSDAIQFDAIIIAAGAETLFSLSSftggsanttagt 652
Cdd:PRK11249 609 DAADllAILKALKAKGVHAKLLYPRMGevtadDGtvlpIAATFAGAPSLTFDAVIVPGGKANIADLAD------------ 676
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 121712100 653 tslypTGRPLQILIDGFRFGKTVGALGSGTAALRNAGITTSRDGVVVAQSADDG 706
Cdd:PRK11249 677 -----NGDARYYLLEAYKHLKPIALAGDARKLKAALKLPDQGEEGLVEADSADG 725
|
|
| KatE |
COG0753 |
Catalase [Inorganic ion transport and metabolism]; |
47-546 |
0e+00 |
|
Catalase [Inorganic ion transport and metabolism];
Pssm-ID: 440516 [Multi-domain] Cd Length: 489 Bit Score: 777.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 47 YLNDTDAFMTTDVGGPIED-QNSLTAGDRGPTLLEDFIFRQKIQRFDHERVPERAVHARGTGAHGVFTSYGDFSNITAAS 125
Cdd:COG0753 3 YADDEGKTLTTNQGAPVADnQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFEVTEDISKYTKAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 126 FLGKEGKETPVFVRFSTVAGSRGSSDLSRDVHGFATRFYTDEGNFDIVGNNIPVFFIQDAILFPDLIHAVKPRGDNEIPQ 205
Cdd:COG0753 83 FFQEPGKKTPVFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHAQKRDPDTNLPQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 206 aataHDSAWDFFSQQPSALHTLFWAMSGHGIPRSFRHVDGFGVHTFRFVTDDGATKLVKFHWTSLQGRASMVWEEAQQTS 285
Cdd:COG0753 163 ----HDTFWDFWSLSPESLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAEGERFWVKFHWKPKQGIHSLTWDEAQKIA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 286 GKNPDYMRQDLFEAIEAGRYPEWELGVQIMDEEDQLRFGFDLLDPTKIVPEELVPITKLGKMQLNRNPRNYFAETEQVMF 365
Cdd:COG0753 239 GKDPDFHRRDLYEAIERGDFPEWELGVQVMPEEDADKFDFDPLDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAETEQAAF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 366 QPGHIVRGVDFTEDPLLQGRIFSYLDTQLNRHgGPNFEQLPINQPRVPVHNNNRDGAGQMFIPLNPHAYSPKtpTNESPK 445
Cdd:COG0753 319 SPGNLVPGIDFSPDKMLQGRLFSYADTQRYRL-GPNFHQLPVNRPKCPVHNYQRDGAMRYDINGGRVNYEPN--SLGGPR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 446 QANQtvgkgfFTAPERKVSGKLIRAVSPTfEDVWSQPRLFYNSLIPAEQQFIIDAIRFENANVKSPIVKNNVVIQLNRVD 525
Cdd:COG0753 396 EDPG------FKEPPLKVDGDKVRYRSES-DDHFSQAGLLYRSMSDEEKQHLIDNIAFELGKVESEEIRERMVAHFYNVD 468
|
490 500
....*....|....*....|.
gi 121712100 526 NDLARRVARAIGVNEPEPDPK 546
Cdd:COG0753 469 PELGARVAEALGLDLPEAKAL 489
|
|
| catalase_clade_2 |
cd08155 |
Clade 2 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
92-536 |
0e+00 |
|
Clade 2 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes, which is involved in the protection of cells from the toxic effects of peroxides. It catalyzes the conversion of hydrogen peroxide to water and molecular oxygen. Catalases also utilize hydrogen peroxide to oxidize various substrates such as alcohol or phenols. Clade 2 catalases are mostly found in bacteria and fungi; they have a large subunit size of 75 to 84 kDa, and bind a heme d group buried deep inside the structure. They appear to form tetramers. In eukaryotic cells, catalases are located in peroxisomes.
Pssm-ID: 163711 Cd Length: 443 Bit Score: 694.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 92 DHERVPERAVHARGTGAHGVFTSYGDFSNITAASFLGKEGKETPVFVRFSTVAGSRGSSDLSRDVHGFATRFYTDEGNFD 171
Cdd:cd08155 1 DHERIPERVVHARGSGAHGYFQVYESLSQYTKAKFLQDPGKKTPVFVRFSTVAGSRGSADTVRDVRGFAVKFYTEEGNYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 172 IVGNNIPVFFIQDAILFPDLIHAVKPRGDNEIPQAATAHDSAWDFFSQQPSALHTLFWAMSGHGIPRSFRHVDGFGVHTF 251
Cdd:cd08155 81 LVGNNIPVFFIQDAIKFPDLIHAVKPEPHNEMPQAQSAHDTFWDFVSLQPESAHMVMWAMSDRAIPRSYRMMEGFGVHTF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 252 RFVTDDGATKLVKFHWTSLQGRASMVWEEAQQTSGKNPDYMRQDLFEAIEAGRYPEWELGVQIMDEEDQLRFGFDLLDPT 331
Cdd:cd08155 161 RLVNAQGKSTFVKFHWKPVLGVHSLVWDEAQKIAGKDPDFHRRDLWEAIESGDYPEWELGVQLIDEEDEFKFDFDILDPT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 332 KIVPEELVPITKLGKMQLNRNPRNYFAETEQVMFQPGHIVRGVDFTEDPLLQGRIFSYLDTQLNRHGGPNFEQLPINQPR 411
Cdd:cd08155 241 KLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFCPANVVPGIDFSNDPLLQGRLFSYLDTQLSRLGGPNFHELPINRPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 412 VPVHNNNRDGAGQMFIPLNPHAYSPKTPTNESPKQANQTVGkGFFTAPErKVSGKLIRAVSPTFEDVWSQPRLFYNSLIP 491
Cdd:cd08155 321 CPVHNNQRDGHMRMTINKGRVNYFPNSLGAGPPRAASPAEG-GFVHYPE-KVEGPKIRIRSESFADHYSQARLFWNSMSP 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 121712100 492 AEQQFIIDAIRFENANVKSPIVKNNVVIQLNRVDNDLARRVARAI 536
Cdd:cd08155 399 VEKEHIISAFTFELSKVETPEIRERVVDHLANIDEDLAKKVAKGL 443
|
|
| Catalase |
pfam00199 |
Catalase; |
56-436 |
0e+00 |
|
Catalase;
Pssm-ID: 459708 Cd Length: 383 Bit Score: 679.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 56 TTDVGGPIED-QNSLTAGDRGPTLLEDFIFRQKIQRFDHERVPERAVHARGTGAHGVFTSYGDFSNITAASFLGKEGKET 134
Cdd:pfam00199 1 TTSNGAPVPDnQNSLTAGPRGPLLLQDFHLIEKLAHFDRERIPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSEVGKKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 135 PVFVRFSTVAGSRGSSDLSRDVHGFATRFYTDEGNFDIVGNNIPVFFIQDAILFPDLIHAVKPRGDNEIPQAATAhdsaW 214
Cdd:pfam00199 81 PVFVRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHSQKRDPQTNLPDPAMF----W 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 215 DFFSQQPSALHTLFWAMSGHGIPRSFRHVDGFGVHTFRFVTDDGATKLVKFHWTSLQGRASMVWEEAQQTSGKNPDYMRQ 294
Cdd:pfam00199 157 DFWSLNPESLHQVTWLFSDRGIPRSYRHMNGFGVHTFKLVNADGERVYVKFHFKTDQGIKNLTWEEAQKLAGKDPDYHTR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 295 DLFEAIEAGRYPEWELGVQIMDEEDQLRFGFDLLDPTKIVPEELVPITKLGKMQLNRNPRNYFAETEQVMFQPGHIVRGV 374
Cdd:pfam00199 237 DLYEAIERGDYPSWTLYVQVMTEEDAEKFRFNPFDLTKVWPHKDYPLIEVGKMVLNRNPDNYFAEVEQAAFSPSNLVPGI 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 121712100 375 DFTEDPLLQGRIFSYLDTQLNRHgGPNFEQLPINQPRVPVHNNNRDGAGQMFIPLNPHA-YSP 436
Cdd:pfam00199 317 EPSPDPMLQGRLFSYPDTQRYRL-GPNYQQLPVNRPPCPVHNYQRDGAMRFDINQGSRPnYEP 378
|
|
| Catalase |
smart01060 |
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ... |
60-434 |
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: 654.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 60 GGPIED-QNSLTAGDRGPTLLEDFIFRQKIQRFDHERVPERAVHARGTGAHGVFTSYGDFSNITAASFLGKEGKETPVFV 138
Cdd:smart01060 2 GAPVADnQNSLTAGPRGPVLLQDFHLIEKLAHFDRERIPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQKVGKKTPVFV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 139 RFSTVAGSRGSSDLSRDVHGFATRFYTDEGNFDIVGNNIPVFFIQDAILFPDLIHAVKPRGDNEIPQaataHDSAWDFFS 218
Cdd:smart01060 82 RFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHAQKRDPRTNLPD----HDMFWDFWS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 219 QQPSALHTLFWAMSGHGIPRSFRHVDGFGVHTFRFVTDDGATKLVKFHWTSLQGRASMVWEEAQQTSGKNPDYMRQDLFE 298
Cdd:smart01060 158 LNPESLHQVTWLMSDRGIPASYRHMNGFGVHTFKLVNAEGERFYVKFHFKPDQGIKNLTWEEAAKLAGKDPDYHRRDLYE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 299 AIEAGRYPEWELGVQIMDEEDQLRFGFDLLDPTKIVPEELVPITKLGKMQLNRNPRNYFAETEQVMFQPGHIVRGVDFTE 378
Cdd:smart01060 238 AIERGDYPEWTLYVQVMPEEDAEKFRFDPFDLTKVWPHKDYPLIEVGKMTLNRNPDNYFAEVEQAAFSPSNLVPGIEFSP 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 121712100 379 DPLLQGRIFSYLDTQLNRHgGPNFEQLPINQPRVPVHNNNRDGAGQMFIPLNPHAY 434
Cdd:smart01060 318 DKMLQGRLFSYPDTQRYRL-GPNYHQLPVNRPRCPVHNYQRDGAMRVDGNQGGDPN 372
|
|
| catalase |
cd00328 |
Catalase heme-binding enzyme; Catalase is a ubiquitous enzyme found in both prokaryotes and ... |
95-536 |
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: 644.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 95 RVPERAVHARGTGAHGVFTSYGDFSNITAASFLGKEGKETPVFVRFSTVAGSRGSSDLSRDVHGFATRFYTDEGNFDIVG 174
Cdd:cd00328 1 RIPERVVHARGAGAFGYFTAYGDWSDISAAAFFSAIGKKTPVFVRFSTVVGGAGSADTVRDPHGFATKFYTEEGNFDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 175 NNIPVFFIQDAILFPDLIHAVKPRGDNEIPQaataHDSAWDFFSQQPSALHTLFWAMSGHGIPRSFRHVDGFGVHTFRFV 254
Cdd:cd00328 81 NNTPIFFIRDAIKFPDFIHAQKPNPQTALPD----ADRFWDFLSLRPESLHQVSFLFSDRGIPAAYRHMNGYGSHTFKLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 255 TDDGATKLVKFHWTSLQGRASMVWEEAQQTSGKNPDYMRQDLFEAIEAGRYPEWELGVQIMDEEDQLRFGFDLLDPTKIV 334
Cdd:cd00328 157 NANGKVHYVKFHWKTDQGIANLVWEEAARLAGEDPDYHRQDLFEAIEAGDYPSWELYIQVMTFNDAEKFPFNPLDPTKVW 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 335 PEELVPITKLGKMQLNRNPRNYFAETEQVMFQPGHIVRGVDFTEDPLLQGRIFSYLDTQLNRHgGPNFEQLPINQPRVPV 414
Cdd:cd00328 237 PEELVPLIVVGKLVLNRNPLNFFAEVEQAAFDPGHIVPGVEFSEDPLLQGRLFSYADTQLYRL-GPNFQQLPVNRPYAPV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 415 HNNNRDGAGQMFIPLNPHAYSPKTPTNESPKQANQTVGKGFFtapeRKVSGKLIRAVSPTFEDVWSQPRLFYNSLIPAEQ 494
Cdd:cd00328 316 HNNQRDGAGNMNDNTGVPNYEPNAKDVRYPAQGAPKFDRGHF----SHWKSGVNREASTTNDDNFTQARLFYRSLTPGQQ 391
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 121712100 495 QFIIDAIRFENANVKSPIVKNNVVIQLNRVDNDLARRVARAI 536
Cdd:cd00328 392 KRLVDAFRFELADAVSPQIQQRVLDQFAKVDAAAAKRVAKAL 433
|
|
| catalase_clade_1 |
cd08154 |
Clade 1 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
54-536 |
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: 568.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 54 FMTTDVGGPIED-QNSLTAGDRGPTLLEDFIFRQKIQRFDHERVPERAVHARGTGAHGVFTSYGDFSNITAASFLGKEGK 132
Cdd:cd08154 1 TLTTNQGAPVGDnQNSQTVGPRGPVLLEDYHLIEKLAHFDRERIPERVVHARGAGAHGYFEAYGDISDYTRASFLQEPGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 133 ETPVFVRFSTVAGSRGSSDLSRDVHGFATRFYTDEGNFDIVGNNIPVFFIQDAILFPDLIHAVKPRGDNEIPQAatahDS 212
Cdd:cd08154 81 KTPVFVRFSTVIHGKGSPETLRDPRGFAVKFYTEEGNWDLVGNNLPVFFIRDAIKFPDMIHALKPSPVTNIQDP----NR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 213 AWDFFSQQPSALHTLFWAMSGHGIPRSFRHVDGFGVHTFRFVTDDGATKLVKFHWTSLQGRASMVWEEAQQTSGKNPDYM 292
Cdd:cd08154 157 IFDFFSHVPESTHMLTFLYSDWGTPASYRHMDGSGVHTYKWVNAEGKVVYVKYHWKPKQGVKNLTAEEAAEVQGKNFNHA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 293 RQDLFEAIEAGRYPEWELGVQIMDEEDQLRFGFDLLDPTKIVPEELVPITKLGKMQLNRNPRNYFAETEQVMFQPGHIVR 372
Cdd:cd08154 237 TQDLYDAIAAGNYPEWELYVQIMDPKDLDKLDFDPLDDTKIWPEDQFPLKPVGKMTLNKNPDNFFAEVEQVAFSPGNLVP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 373 GVDFTEDPLLQGRIFSYLDTQLNRHgGPNFEQLPINQPRVPVHNNNRDGAGQMFIPLNPHAYSPKT--PTNESPKqanqt 450
Cdd:cd08154 317 GIEPSDDKMLQGRLFSYSDTQRYRL-GPNYLQLPINAPKAAVHNNQRDGQMNYGHDTSDVNYEPSRldGLPEAPK----- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 451 vgkgfFTAPERKVSGKLIRAVSPTfEDVWSQPRLFYNSLIPAEQQFIIDAIRFENANVKSPIvKNNVVIQLNRVDNDLAR 530
Cdd:cd08154 391 -----YPYSQPPLSGTTQQAPIAK-TNNFKQAGERYRSFSEEEQENLIKNLVVDLSDVNEEI-KLRMLSYFSQADPDYGE 463
|
....*.
gi 121712100 531 RVARAI 536
Cdd:cd08154 464 RVAEGL 469
|
|
| PLN02609 |
PLN02609 |
catalase |
54-538 |
7.93e-161 |
|
catalase
Pssm-ID: 215328 [Multi-domain] Cd Length: 492 Bit Score: 473.84 E-value: 7.93e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 54 FMTTDVGGPIEDQN-SLTAGDRGPTLLEDFIFRQKIQRFDHERVPERAVHARGTGAHGVFTSYGDFSNITAASFLGKEGK 132
Cdd:PLN02609 16 FFTTNSGAPVWNNNsSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDISNLTCADFLRAPGV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 133 ETPVFVRFSTVAGSRGSSDLSRDVHGFATRFYTDEGNFDIVGNNIPVFFIQDAILFPDLIHAVKPRGDNEIPQAatahDS 212
Cdd:PLN02609 96 QTPVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDMVGNNFPVFFIRDGMKFPDMVHALKPNPKTHIQEP----WR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 213 AWDFFSQQPSALHTLFWAMSGHGIPRSFRHVDGFGVHTFRFVTDDGATKLVKFHWTSLQGRASMVWEEAQQTSGKNPDYM 292
Cdd:PLN02609 172 ILDFLSHHPESLHMFTFLFDDRGIPQDYRHMEGFGVHTYKLINKAGKAHYVKFHWKPTCGVKNLLDEEAVRVGGSNHSHA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 293 RQDLFEAIEAGRYPEWELGVQIMDEEDQLRFGFDLLDPTKIVPEELVPITKLGKMQLNRNPRNYFAETEQVMFQPGHIVR 372
Cdd:PLN02609 252 TQDLYDSIAAGNYPEWKLFIQTMDPEDEDKFDFDPLDVTKTWPEDILPLQPVGRLVLNRNIDNFFAENEQLAFCPAIVVP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 373 GVDFTEDPLLQGRIFSYLDTQlnRHG-GPNFEQLPINQPRVPVHNNNRDGAGQM-------------FIPLnPHAysPKT 438
Cdd:PLN02609 332 GIYYSDDKLLQTRIFAYADTQ--RHRlGPNYLQLPVNAPKCAHHNNHHEGFMNFmhrdeevnyfpsrFDPV-RHA--ERV 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 439 PTnespkqanqtvgkgfftaPERKVSGKLIRAVSPTfEDVWSQPRLFYNSLIPAEQ-QFI---IDAIRfeNANVkSPIVK 514
Cdd:PLN02609 407 PI------------------PHPPLSGRREKCKIEK-ENNFKQPGERYRSWSPDRQeRFIkrwVDALS--DPRV-THEIR 464
|
490 500
....*....|....*....|....
gi 121712100 515 NNVVIQLNRVDNDLARRVARAIGV 538
Cdd:PLN02609 465 SIWISYWSQCDKSLGQKLASRLNV 488
|
|
| catalase_clade_3 |
cd08156 |
Clade 3 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
95-536 |
2.14e-157 |
|
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: 462.39 E-value: 2.14e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 95 RVPERAVHARGTGAHGVFTSYGDFSNITAASFLGKEGKETPVFVRFSTVAGSRGSSDLSRDVHGFATRFYTDEGNFDIVG 174
Cdd:cd08156 1 RIPERVVHAKGAGAFGTFEVTHDITKYTKAKIFSEVGKKTPVFVRFSTVAGERGSADTERDPRGFALKFYTEEGNWDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 175 NNIPVFFIQDAILFPDLIHAVKPRGDNEIPQaataHDSAWDFFSQQPSALHTLFWAMSGHGIPRSFRHVDGFGVHTFRFV 254
Cdd:cd08156 81 NNTPVFFIRDPIKFPDFIHTQKRNPQTNLKD----PDMFWDFWSLSPESLHQVTILFSDRGIPDGYRHMNGYGSHTFSLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 255 TDDGATKLVKFHWTSLQGRASMVWEEAQQTSGKNPDYMRQDLFEAIEAGRYPEWELGVQIMDEEDQLRFGFDLLDPTKIV 334
Cdd:cd08156 157 NAKGERFWVKFHFKTDQGIKNLTNEEAAELAGEDPDYAQRDLFEAIERGDFPSWTLYVQVMPEEDAEKYRFNPFDLTKVW 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 335 PEELVPITKLGKMQLNRNPRNYFAETEQVMFQPGHIVRGVDFTEDPLLQGRIFSYLDTQLNRHgGPNFEQLPINQPRVPV 414
Cdd:cd08156 237 PHKDYPLIEVGKLELNRNPENYFAEVEQAAFSPSNLVPGIGFSPDKMLQGRLFSYADAHRYRL-GVNYHQLPVNRPKCPV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 415 HNNNRDGAGQMFIPLNPHA-YSPKTpTNESPKQANqtvgkgfFTAPERKVSGKLIRAVSPTFEDVWSQPRLFYNSLIPAE 493
Cdd:cd08156 316 NNYQRDGAMRVDGNGGGAPnYEPNS-FGGPPEDPE-------YAEPPLPVSGDADRYNYRDDDDDYTQAGDLYRLVSEDE 387
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 121712100 494 QQFIIDAIRFENANVKSPIVKNNVViQLNRVDNDLARRVARAI 536
Cdd:cd08156 388 RERLVENIAGHLKGAPEFIQERQVA-HFYKADPDYGERVAKAL 429
|
|
| catalase_fungal |
cd08157 |
Fungal catalases similar to yeast catalases A and T; Catalase is a ubiquitous enzyme found in ... |
79-537 |
8.28e-147 |
|
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: 436.01 E-value: 8.28e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 79 LEDFIFRQKIQRFDHERVPERAVHARGTGAHGVFTSYGDFSNITAASFLGKEGKETPVFVRFSTVAGSRGSSDLSRDVHG 158
Cdd:cd08157 1 LQDFHLIDTLAHFDRERIPERVVHAKGAGAYGEFEVTDDISDITSADMLQGVGKKTPCLVRFSTVGGEKGSADTVRDPRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 159 FATRFYTDEGNFDIVGNNIPVFFIQDAILFPDLIHAVKPRgdneiPQAATAHDSA-WDFFSQQPSALHTLFWAMSGHGIP 237
Cdd:cd08157 81 FAVKFYTEEGNWDWVFNNTPVFFIRDPIKFPHFIHSQKRD-----PQTNLKDSTMfWDYLSQNPESIHQVMILFSDRGTP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 238 RSFRHVDGFGVHTFRFVTDDGATKLVKFHWTSLQGRASMVWEEAQQTSGKNPDYMRQDLFEAIEAGRYPEWELGVQIMDE 317
Cdd:cd08157 156 ASYRSMNGYSGHTYKWVNPDGSFKYVQFHLKSDQGPKFLTGEEAARLAGSNPDYATKDLFEAIERGDYPSWTVYVQVMTP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 318 EDQLRFGFDLLDPTKIVPEELVPITKLGKMQLNRNPRNYFAETEQVMFQPGHIVRGVDFTEDPLLQGRIFSYLDTQlnRH 397
Cdd:cd08157 236 EQAEKLRFNIFDLTKVWPHKDFPLRPVGKLTLNENPKNYFAEIEQAAFSPSHMVPGIEPSADPVLQARLFSYPDAH--RH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 398 G-GPNFEQLPINQPRV-PVHN-NNRDGAGQMFIPLNPHAyspkTPTNESPKQANQTVGKGFFTAPERKVSGKLIRAVSPT 474
Cdd:cd08157 314 RlGPNYQQLPVNRPKTsPVYNpYQRDGPMSVNGNYGGDP----NYVSSILPPTYFKKRVDADGHHENWVGEVVAFLTEIT 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 121712100 475 FEDvWSQPRLFYNSLIPAEQQ--FIID-AIRFENAnvkSPIVKNNVVIQLNRVDNDLARRVARAIG 537
Cdd:cd08157 390 DED-FVQPRALWEVVGKPGQQerFVKNvAGHLSGA---PPEIRKRVYEIFARVNPDLGKRIEKATE 451
|
|
| catalase_like |
cd08150 |
Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found ... |
97-397 |
8.26e-77 |
|
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: 248.63 E-value: 8.26e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 97 PERAVHARGTGAHGVFTSYGDFSNITAASFLGkEGKETPVFVRFSTVAGSrgsSDLSRDVHGFATRFYT--DEGNFDIVG 174
Cdd:cd08150 1 GLRGQHFQGTCAFGTFEVLADLKERLRVGLFA-EGKVYPAYIRFSNGAGI---DDTKPDIRGFAIKFTGvaDAGTLDFVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 175 NNIPVFFIQDAILFPDLIHAVKPRgdneiPQAATAHDSAWDFFSQQPSALHTLFWAMSGhgIPRSFRHVDGFGVHTFRFV 254
Cdd:cd08150 77 NNTPVFFIRNTSDYEDFVAEFARS-----ARGEPPLDFIAWYVEKRPEDLPNLLGARSQ--VPDSYAAARYFSQVTFAFI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 255 TDDGATKLVKFHWTSLQGRASMVWEEAQqtsGKNPDYMRQDLFEAIEAGrYPEWELGVQIMDEEDQlrfgFDLLDPTKIV 334
Cdd:cd08150 150 NGAGKYRVVRSKDNPVDGIPSLEDHELE---ARPPDYLREELTERLQRG-PVVYDFRIQLNDDTDA----TTIDNPTILW 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 121712100 335 PEElVPITKLGKMQLNRNPRNyfAETEQVMFQPGHIVRGVDFTED--PLLQGRIFSYLDTQLNRH 397
Cdd:cd08150 222 PTE-HPVEAVAKITIPPPTFT--AAQEAFAFNPFTPWHGLLETNDlgPILEVRRRVYTSSQGLRH 283
|
|
| Catalase_C |
pfam18011 |
C-terminal domain found in long catalases; This domain is found at the C-terminus of a variety ... |
567-725 |
9.22e-64 |
|
C-terminal domain found in long catalases; This domain is found at the C-terminus of a variety of large catalase enzymes from bacteria. Structurally it is related to class I glutamine amidotransferase domains. The precise molecular function of this domain is uncertain.
Pssm-ID: 436209 Cd Length: 150 Bit Score: 209.05 E-value: 9.22e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 567 DGLKVGFFASVQHASSLDAASALRASLSKAGVDVVVVAERLADGVDQTYSTSDAIQFDAIIIAAGAETLFSLSSftggsa 646
Cdd:pfam18011 1 DGLTVGILASNDSDASLAQAKALAAALAAAGVDVLVVAETLADGVNRTYSTADATLFDAIVVADGAEGLFSAKA------ 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 121712100 647 nttAGTTSLYPTGRPLQILIDGFRFGKTVGALGSGTAALRNAGITTSRDGVVVAQSADDGFVEHIKDGLSTFKFVDRFA 725
Cdd:pfam18011 75 ---TAASSLYPAGRPLQILLDAYRHGKPIGALGSGSSALSGAGISAEGPGVYVGDSADDALVEDVEEGLATFRFWDRFP 150
|
|
| GATase1_catalase |
cd03132 |
Type 1 glutamine amidotransferase (GATase1)-like domain found in at the C-terminal of several ... |
568-728 |
8.13e-36 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain found in at the C-terminal of several large catalases; Type 1 glutamine amidotransferase (GATase1)-like domain found in at the C-terminal of several large catalases. Catalase catalyzes the dismutation of hydrogen peroxide (H2O2) to water and oxygen. This group includes the large catalases: Neurospora crassa Catalase-1 and Catalase-3 and, Escherichia coli HP-II. This GATase1-like domain has an essential role in HP-II catalase activity. However, it lacks enzymatic activity and the catalytic triad typical of GATase1 domains. Catalase-1 and -3 are homotetrameric, HP-II is homohexameric. It has been proposed that this domain may facilitate the folding and oligomerization process. The interface between this GATase1-like domain of HP-II and the core of the subunit forms part of a channel which provides access to the deeply buried catalase active sites of HPII. Catalase-1 is associated with non-growing cells; Catalase-3 is associated with growing conditions. HP-II is produced in stationary phase. Catalase-1 is induced by ethanol and heat shock. Catalase-3 is induced under stress conditions such a hydrogen peroxide, paraquat, cadmium, heat shock, uric acid and nitrate treatment.
Pssm-ID: 153226 Cd Length: 142 Bit Score: 132.00 E-value: 8.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 568 GLKVGFFASvqHASSLDAASALRASLSKAGVDVVVVAERLADG---------VDQTYSTSDAIQFDAIIIAAGAETLFSL 638
Cdd:cd03132 1 GRKVGILVA--DGVDAAELSALKAALKAAGANVKVVAPTLGGVvdsdgktleVDQTYAGAPSVLFDAVVVPGGAEAAFAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 639 ssftggsanttagttslYPTGRPLQILIDGFRFGKTVGALGSGTAALRNAGITTSRDGVVVAQSADDGFvehikdglsTF 718
Cdd:cd03132 79 -----------------APSGRALHFVTEAFKHGKPIGAVGEGSDLLEAAGIPLEDPGVVTADDVKDVF---------TD 132
|
170
....*....|
gi 121712100 719 KFVDRFAVDH 728
Cdd:cd03132 133 RFIDALALHR 142
|
|
| srpA_like |
cd08153 |
Catalase-like heme-binding proteins similar to the uncharacterized srpA; Catalase is a ... |
99-385 |
2.13e-35 |
|
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: 135.82 E-value: 2.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 99 RAVHARGTGAHGVFTSYGDFSNITAASFLgkEGKETPVFVRFSTVAGSRGSSDLSRDVHGFATRFYTDEGNF-DIVGNNI 177
Cdd:cd08153 15 RRNHAKGICVSGTFTPSGAAASLSRAPLF--SGGSVPVTGRFSLGGGNPKAPDDAANPRGMALKFRLPDGEQwRMVMNSF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 178 PVFFIQDAILFPDLIHAVKPRGDNEI-PQAATAhdsawdFFSQQPSALHTLFWAMSgHGIPRSFRHVDGFGVHTFRFVTD 256
Cdd:cd08153 93 PVFPVRTPEEFLALLKAIAPDATGKPdPAKLKA------FLAAHPEAAAFLAWIKT-APPPASFANTTYYGVNAFYFTNA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 257 DGATKLVKFHWTSLQGRASMvweEAQQTSGKNPDYMRQDLFEAIEAGryP-EWELGVQIMDEEDqlrfgfDLLDPTKIVP 335
Cdd:cd08153 166 NGKRQPVRWRFVPEDGVKYL---SDEEAAKLGPDFLFDELAQRLAQG--PvRWDLVLQLAEPGD------PTDDPTKPWP 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 121712100 336 EELvPITKLGKMQLNRNPRNYFAETEQVMFQPGHIVRGVDFTEDPLLQGR 385
Cdd:cd08153 235 ADR-KEVDAGTLTITKVAPDQGGACRDINFDPLVLPDGIEPSDDPLLAAR 283
|
|
| Catalase-rel |
pfam06628 |
Catalase-related immune-responsive; This family represents a small conserved region within ... |
472-536 |
3.75e-22 |
|
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: 90.12 E-value: 3.75e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 121712100 472 SPTFEDVWSQPRLFYNSLIPAEQQFIIDAIRFENANVKSPIVKNNVVIQLNRVDNDLARRVARAI 536
Cdd:pfam06628 1 SIDFDDHFSQAGLFYRSMSEEERQRLVDNIAFELSKVTDPEIQERMVAHFYKVDPDLGQRVAEAL 65
|
|
| AOS |
cd08151 |
Allene oxide synthase; Allene oxide synthase converts a fatty acid hydroperoxide to an allene ... |
99-369 |
6.50e-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: 55.12 E-value: 6.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 99 RAVHARGTGAHGVFTSYGDfSNITAASFLGKeGKETPVFVRFSTVAGSRgsSDLSRDVHGFATRFYT----DEGNFDIVG 174
Cdd:cd08151 28 RGTHTIGVGAKGVLTVLAE-SDFPEHAFFTA-GKRFPVILRHANIVGGD--DDASLDGRGAALRFLNagddDAGPLDLVM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 175 NNIPVFFIQDAILFPDLihavkprgdneIPQAATAHDSAWDFFsqqpsalHTLFWAMSGHGIPR---SFRHVDGFGVHTF 251
Cdd:cd08151 104 NTGESFGFWTAASFADF-----------AGAGLPFREKAAKLR-------GPLARYAVWASLRRapdSYTDLHYYSQICY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 252 RFVTDDGATKLVKFH---------WTSLQGRasmVWEEAQQTSGKNP---------DYMRQDLFEAIEAGRYpEWELGVQ 313
Cdd:cd08151 166 EFVALDGKSRYARFRllppdadteWDLGEDV---LETIFQRPRLYLPrlpgdtrpkDYLRNEFRQRLQSPGV-RYRLQIQ 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 121712100 314 IMDEEDQLRfgFDLLDPTKIVPEELVPITKLGKMQLNRNPRNyfAETEQVMFQPGH 369
Cdd:cd08151 242 LREVSDDAT--AVALDCCRPWDEDEHPWLDLAVVRLGAPLPN--DELEKLAFNPGN 293
|
|
| y4iL_like |
cd08152 |
Catalase-like heme-binding proteins similar to the uncharacterized y4iL; Catalase is a ... |
99-359 |
1.29e-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: 50.72 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 99 RAVHARGTGA-HGVFTSYgdfSNITA--ASFLGKEGKETPVFVRFSTVAGsRGSSDLSRDVHGFATRFY----------T 165
Cdd:cd08152 5 RDAHAKSHGClKAEFTVL---DDLPPelAQGLFAEPGTYPAVIRFSNAPG-DILDDSVPDPRGMAIKVLgvpgekllpeE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 166 DEGNFDIVGNNIPVFFIQDA-------------ILFPDLIHAVKP---RGDNEIPQAATAHDSAWDFFSQQP-SALHTLF 228
Cdd:cd08152 81 DATTQDFVLVNHPVFFARDAkdylallkllartTSLPDGAKAALSaplRGALRVLEAAGGESPTLKLGGHPPaHPLGETY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 229 WAMSghgiprSFRHVDGFGVHTFRFVTDdgatklvkfhwtslqgrASMVWEEAQQTSGKNPDYMRQDL---FEAIEAgry 305
Cdd:cd08152 161 WSQA------PYRFGDYVAKYSVVPASP-----------------ALPALTGKELDLTDDPDALREALadfLAENDA--- 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 121712100 306 pEWELGVQI-MDEEDQLrfgfdLLDPTKIVPEELVPITKLGKMQLNRNP------RNYFAE 359
Cdd:cd08152 215 -EFEFRIQLcTDLEKMP-----IEDASVEWPEALSPFVPVATITIPPQDfdsparQRAFDD 269
|
|
| PBP1_ABC_ligand_binding-like |
cd06341 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
543-640 |
1.29e-04 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in transport of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in transport of amino acids, peptides, or inorganic ions. Members of this group are sequence-similar to members of the family of ABC-type hydrophobic amino acid transporters such as leucine-isoleucine-valine binding protein (LIVBP); however their ligand specificity has not been determined experimentally.
Pssm-ID: 380564 [Multi-domain] Cd Length: 340 Bit Score: 44.61 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121712100 543 PDPKFYHNNKTANVGTFGGKLKKLDGLKVGFFASVQHASSLDAASALRASLSKAGVDVVVVAERLADGVDqtySTSDAIQ 622
Cdd:cd06341 107 MFSNFFSLGGGGSTTTYGQYAAALGGTKAAVVVTDIPAASQQLAQQLAASLRAAGVEVVGTAPYAAAAPD---YTAVAQA 183
|
90
....*....|....*...
gi 121712100 623 fdaiIIAAGAETLFSLSS 640
Cdd:cd06341 184 ----AKAAGADAVVGVLD 197
|
|
| |
