|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05290 |
PRK05290 |
hybrid cluster protein; Provisional |
1-452 |
0e+00 |
|
hybrid cluster protein; Provisional
Pssm-ID: 235391 Cd Length: 546 Bit Score: 776.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 1 MFCIQCEQTIQTpavKGCsFAQGMCGKTSEVSDLQDVLVYTLQGVSFWAARALEFNIINDEINQWAPRACFSTLTNVNFD 80
Cdd:PRK05290 1 MFCYQCEQTARG---NGC-TAQGVCGKTAETADLQDLLIYALKGLSAYALKARELGIIDHEVDRFVPEALFTTLTNVNFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 81 PERILELTSQAATYKALLKDQVMSAATLADEVvlnvPNVANFELPNSAEEILAFAPQVAVNRGKDqVHEDVIGLRLLCLY 160
Cdd:PRK05290 77 DERIVGYIKEAIALREALKAKLAADGNAPEDL----PDAALWLPADDLEELLAQAAEVGVLADAT-ENEDIRSLRELLLY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 161 GLKGAAAYMEHARVLEQTNNDIFAEYHEIMAWLGTDPEDLGELLDCSMRIDLMNYKVMEMLDHGETATFGHPEPTTVNVK 240
Cdd:PRK05290 152 GLKGMAAYAEHARVLGQTDEEIYAFYHKALAALGDDPLDVDELLALVLECGKMNVKVMALLDKANTETYGHPEPTKVNIG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 241 PVKGKCILVSGHDLHDLEKILQQTEGKGINVYTNGEMLPEHGYPELKKYSHLVGNYGSAWQNQQKEFANFPGAIVMTSNC 320
Cdd:PRK05290 232 VRKGPGILVSGHDLKDLEELLEQTEGTGINVYTHGEMLPAHGYPELKKYPHLVGNYGSAWQNQQKEFASFPGPILMTTNC 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 321 LLNPNvGQYADRLFTRSIVGWPGVAHLEGD---DFSQVVECALAQEGFQHDEIEHNITVGFGRNALMNAAPAVIDQVKQG 397
Cdd:PRK05290 312 IIPPK-GSYKDRIFTTGIVGWPGVKHIEGDgkkDFSPVIEKALELPGFPPDEIEHEITVGFAHNAVLAVADKVIDAVKSG 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 501077508 398 NIKHFFLVGGCDGDKAERSYYTDFTAEAPEDTLILTLACGKYRFNKNTFGDINGI 452
Cdd:PRK05290 391 AIRHFFLMGGCDGAKPGRNYYTEFAEKLPKDTVILTLGCGKYRFNKLDLGDIGGI 445
|
|
| hybrid_clust |
TIGR01703 |
hydroxylamine reductase; This model represents a family of proteins containing an unusual ... |
1-452 |
0e+00 |
|
hydroxylamine reductase; This model represents a family of proteins containing an unusual 4Fe-2S-2O hydrid cluster. Earlier reports had proposed a 6Fe-6S prismane cluster. This subfamily is heterogeneous with respect to the presence or absence of a region of about 100 amino acids not far from the N-terminus of the protein. Members have been described as monomeric. The general function is unknown, although members from E. coli and several other species have hydroxylamine reductase activity. Members are found in various bacteria, in Archaea, and in several parasitic eukaryotes: Giardia intestinalis, Trichomonas vaginalis, and Entamoeba histolytica. [Cellular processes, Detoxification, Energy metabolism, Amino acids and amines]
Pssm-ID: 130764 Cd Length: 522 Bit Score: 565.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 1 MFCIQCEQTIQTpavKGCSfAQGMCGKTSEVSDLQDVLVYTLQGVSFWAARALEFNIINdEINQWAPRACFSTLTNVNFD 80
Cdd:TIGR01703 1 MFCYQCEQTARG---TGCT-VRGVCGKDPETANLQDLLVYVLKGISLWALQARKLGIDS-EIDSFIPRALFSTLTNVNFD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 81 PERILELTSQAATYKALLKDQvmsaatladevvlnvpnvaNFELPNSAEEILAFAPqvavNRGKDQVHEDVIGLRLLCLY 160
Cdd:TIGR01703 76 EDRIVEYIEDAIKLREKLKKK-------------------CRLADSNSLLIQSFAL----NGDKSHVNDDVNSLRDLLLY 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 161 GLKGAAAYMEHARVLEQTNNDIFAEYHEIMAWLGTDPEDLGELLDCSMRIDLMNYKVMEMLDHGETATFGHPEPTTVNVK 240
Cdd:TIGR01703 133 GIKGIAAYLYHARELGYDDEEIYAFLEEALASTLTNVFDADELIDLALEVGKMNLEAMKLLDKANTETYGLPEPTEVNIG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 241 PVKGKCILVSGHDLHDLEKILQQTEGKGINVYTNGEMLPEHGYPELKKYSHLVGNYGSAWQNQQKEFANFPGAIVMTSNC 320
Cdd:TIGR01703 213 TTEGKAILVSGHDLKDLEELLEQTEGTGINVYTHGEMLPAHGYPELKKYPHLAGNYGGAWQDQQREFAEFPGPILMTSNC 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 321 LLNPNVgQYADRLFTRSIVGWPGVAHLEGDDFSQVVECALAQEGFQHDEIEHNITVGFGRNALMNAAPAVIDQVKQGNIK 400
Cdd:TIGR01703 293 IIPPRK-SYKDRIFTTGIVGWPGVKHIENYDFSPVIEKALELPGFPKELEEGTITTGFGHHTILALADKIVELVKEGKIR 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 501077508 401 HFFLVGGCDGDKAERSYYTDFTAEAPEDTLILTLACGKYRFNKNTFGDINGI 452
Cdd:TIGR01703 372 HFFLVGGCDGPNPERNYYTEFARKLPKDAIILTLACGKYRFNKLDLGDIEGI 423
|
|
| HCP |
cd01914 |
Hybrid cluster protein (HCP), formerly known as prismane, is thought to play a role in ... |
1-452 |
2.75e-170 |
|
Hybrid cluster protein (HCP), formerly known as prismane, is thought to play a role in nitrogen metabolism but its specific function is unknown. HCP has three structural domains, an N-terminal alpha-helical domain, and two similar domains comprising a central beta-sheet flanked by alpha-helices. HCP contains two iron-sulfur clusters, one of which is a [Fe4-S4] cubane cluster similar to that of carbon monoxide dehydrogenase (CODH). The second cluster, referred to as the hybrid cluster, is a hybrid [Fe4-S2-O2] center located at the interface of the three domains. Although the hybrid cluster is buried within the protein, it is accessible through a large hydrophobic cavity.
Pssm-ID: 238895 Cd Length: 423 Bit Score: 486.78 E-value: 2.75e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 1 MFCIQCEQTIQtpaVKGCSFAqGMCGKTSEVSDLQDvlvytlqgvsfwaaralefniindeinqwapracfstltnvnfd 80
Cdd:cd01914 1 MFCYQCEQTAK---GTGCTVR-GVCGKDPEVANLQD-------------------------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 81 perileltsqaatykallkdqvmsaatladevvlnvpnvanfelpnsaeeilafapqvavnrgkdqvhedviglrllclY 160
Cdd:cd01914 33 -------------------------------------------------------------------------------Y 33
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 161 GLKGAAAYMEHARVLEQTNNDIFAEYHEIMAWLGTDPEDLGELLDCSMRIDLMNYKVMEMLDHGETATFGHPEPTTVNVK 240
Cdd:cd01914 34 GLKGIAAYAEHARVLGYDDEEIYAFIEKALASLLDNPLDADELLALALETGRMNLKVMELLDKANTETYGHPEPTEVNIG 113
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 241 PVKGKCILVSGHDLHDLEKILQQTEGKGINVYTNGEMLPEHGYPELKKYSHLVGNYGSAWQNQQKEFANFPGAIVMTSNC 320
Cdd:cd01914 114 VRAGKGILVSGHDLKDLEELLEQTEGTGVDVYTHGEMLPAHGYPELKKYPHLVGNYGGAWQNQQKEFARFPGPILMTTNC 193
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 321 LLNPNvGQYADRLFTRSIVGWPGVAHLEGDDFSQVVECALAQEGFQHDEIEHNITVGFGRNALMNAAPAVIDQVKQGNIK 400
Cdd:cd01914 194 IIPPR-ESYKDRIFTTGIVGWPGVKHIEGKDFSEVIEKAKELPGFPEEEESGTITTGFAHNQVLAVADKVVEAVKSGKIR 272
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 501077508 401 HFFLVGGCDGDKAERSYYTDFTAEAPEDTLILTLACGKYRFNKNTFGDINGI 452
Cdd:cd01914 273 HFFVVGGCDGRHKGRNYYTEFAEKLPKDTVILTLGCGKYRFNKLDLGDIGGI 324
|
|
| Prismane |
pfam03063 |
Prismane/CO dehydrogenase family; This family includes both hybrid-cluster proteins and the ... |
1-456 |
9.75e-151 |
|
Prismane/CO dehydrogenase family; This family includes both hybrid-cluster proteins and the beta chain of carbon monoxide dehydrogenase. The hybrid-cluster proteins contain two Fe/S centres - a [4Fe-4S] cubane cluster, and a hybrid [4Fe-2S-2O] cluster. The physiological role of this protein is as yet unknown, although a role in nitrate/nitrite respiration has been suggested. The prismane protein from Escherichia coli was shown to contain hydroxylamine reductase activity (NH2OH + 2e + 2 H+ -> NH3 + H2O). This activity is rather low. Hydroxylamine reductase activity was also found in CO-dehydrogenase in which the active site Ni was replaced by Fe. The CO dehydrogenase contains a Ni-3Fe-2S-3O centre.
Pssm-ID: 460790 [Multi-domain] Cd Length: 539 Bit Score: 441.20 E-value: 9.75e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 1 MFCIQCEQTiqtpavkGCS---FAQGMCGKTSEVSDLQDVLVYTLQGVSFWAARALEFNIINDEinqwaprACFSTLTNV 77
Cdd:pfam03063 1 MFCRQCEMG-------PCRitpKPRGVCGKTADTIVARNLLRYVAAGAAAHSDHARELGLTLKE-------ALFGTLTNY 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 78 NFDPERILELTSQAATYKALLKDqvmsaatladevvlnvpnvanfelpnsAEEILAFAPQVAVNRGKDQvHEDVIGLRLL 157
Cdd:pfam03063 67 NIDDERKLKRIAEALGIRTELKD---------------------------IEELAAEVADVGLEDFYGK-NEDIRSLREL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 158 CLYGLKGAAAymEHARVLEQTNNDIFAEYHEIMAWLGTDPEDLgelLDCSMRIDLMNYKVMEMLDHGETATFGHPEP--T 235
Cdd:pfam03063 119 APYGRKGLWA--EHAIVPGGIDREVFEFMHRTLTGLDSDPLDL---LLLALRCGLADLGGMELLDEANDILFGTPEPvlT 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 236 TVNVKPVK--GKCILVSGHDLHDLEKILQQTEGKGINVYTNGEMLPEHGYPELK-KYSHLVGNYGSAWQNQQKEFANFPG 312
Cdd:pfam03063 194 EVNLGVLDkdYVNILVSGHDPKDLEMLLEQTEGTGINVYAHGEMLPGHCCPGLKlKYRHGVGNYGNAWQQELAEFTGFPD 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 313 AIVMTSNCLLNP--NVGQ-YADRLFTRSIVGW-PGVAHLEGD------DFSQVVECALAQEGFQHDEIEH------NITV 376
Cdd:pfam03063 274 AIVVDTNCIMPPlaSVAScYHTRLITTSPVGKiPGATHIEFDeekadkDASEIIEKAIEAFKFREIEKVEipgekvGGVA 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 377 GFG----RNALMNAAPAVIDQVKQGNIKHFFLVGGCDGDKAERSYYTDFTAE-APEDTLILTLACGKYRFNKNTFGDI-- 449
Cdd:pfam03063 354 GFSteaiHEAVLGSADPLIDAIKSGAIRGFVLVVGCDNAKPGRDYYTELAKElIPKDILVLTTGCAKYRFNKLGLGDIea 433
|
490
....*....|....*..
gi 501077508 450 -----NGI-----CGSC 456
Cdd:pfam03063 434 aelagDGLppvldMGQC 450
|
|
| Hcp |
COG1151 |
Hydroxylamine reductase (hybrid-cluster protein) [Energy production and conversion]; |
1-454 |
4.12e-120 |
|
Hydroxylamine reductase (hybrid-cluster protein) [Energy production and conversion];
Pssm-ID: 440765 Cd Length: 613 Bit Score: 365.29 E-value: 4.12e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 1 MFCIQCEQTiqtpavkGCSF----AQGMCGKTSEVSDLQDVLVYTLQGVSFWAARALE-------------FNIINDEIN 63
Cdd:COG1151 38 MCCRQCEQG-------PCRItpktPRGVCGKTADTIVARNLLRYVAKGAAAHADHAREvaltlkaaaegadYEIKDEEKL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 64 QWAPRACFSTltnvnfdpERILELTSQAATYKALLKDQVMSAAtladevvlnvPNVANFelpnsaeeILAFAPQvavnrg 143
Cdd:COG1151 111 RFVAEALGIT--------TEGKDLIEIALELADALLEDFGKAG----------GEPATW--------LEAKAPE------ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 144 kdqvhEDVIGLRLLclyglkgaaaymeharvlEQTNNDIFAEYHEIMAWLGTD-PEDLGELLDCSMRIDLMNYKVMEMLD 222
Cdd:COG1151 159 -----ERIESWREL------------------GIEPRGIDREIVEALARTHTGvDLDPVNLLLLALRTGLADWGGMALLD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 223 HGETATFGHPEPTTVNVKPV----KGKCILVSGHDLH----------DLEKILQQTEGKGINVY----TNGEMLPEHGYP 284
Cdd:COG1151 216 EANDILFGTPEPTEVEVNLGvlkeDGVNILVHGHDPKlseaiveaarDLEELAKQTGAKGINVYgiccTGGEMLPRHGYP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 285 ElKKYSHLVGNYGSAwqnqqkEFANFPGAI---VMTSNCLLnPNVGQYA-----DRLFTRSIVGWPGVAHLEGD------ 350
Cdd:COG1151 296 E-KKYVHLAGNYGSA------EFAIFTGAIdamVVDTNCIM-PPLASVAecyytDRITTTGVVGIPGAEHIEFDeegale 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 351 DFSQVVECALAQEGFQHDE------IEHNITVGFGRNALMNA---APAVIDQVKQGNIKHFFLVGGCDGDKAER--SYYT 419
Cdd:COG1151 368 DASEIIEKAIENFKPREDEkvyipqEKGEIVVGFSHEAVLAAlgsADPLIDAIKSGKIRGFVLVVGCDGRKPGRdyNYYT 447
|
490 500 510
....*....|....*....|....*....|....*..
gi 501077508 420 DFTAEAPEDTLILTLACGKYRFNKNTFGDINGI--CG 454
Cdd:COG1151 448 LFKELIPNDVLVLTTGCAKYRLNKLGLGDIEAAelAG 484
|
|
| PRK10684 |
PRK10684 |
HCP oxidoreductase, NADH-dependent; Provisional |
451-496 |
3.16e-13 |
|
HCP oxidoreductase, NADH-dependent; Provisional
Pssm-ID: 236735 [Multi-domain] Cd Length: 332 Bit Score: 70.51 E-value: 3.16e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 501077508 451 GICGSCKCKVRKGSVSSTSLETLTPEEIEQGYVLACSSTIESDLEV 496
Cdd:PRK10684 286 GVCGCCKTKVVSGEYTVSSTMTLTPAEIAQGYVLACSCHPQGDLVL 331
|
|
| Fdx |
COG0633 |
Ferredoxin [Energy production and conversion]; |
419-498 |
9.87e-13 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440398 [Multi-domain] Cd Length: 87 Bit Score: 63.71 E-value: 9.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 419 TDFTAEAPEDTLILTLA----------CGkyrfnkntfgdiNGICGSCKCKVRKGSVSSTSLETLTPEEIEQGYVLACSS 488
Cdd:COG0633 9 EGHTVEVPAGESLLEAAlragidlpysCR------------SGACGTCHVRVLEGEVDHREEDALSDEERAAGSRLACQA 76
|
90
....*....|
gi 501077508 489 TIESDLEVQI 498
Cdd:COG0633 77 RPTSDLVVEL 86
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
419-497 |
3.33e-11 |
|
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.
Pssm-ID: 238126 [Multi-domain] Cd Length: 84 Bit Score: 59.33 E-value: 3.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 419 TDFTAEAPEDTLILTLA----------CGkyrfnkntfgdiNGICGSCKCKVRKGSVSSTSLETLTPEEIEQGYVLACSS 488
Cdd:cd00207 8 SGVEVEVPEGETLLDAAreagidipysCR------------AGACGTCKVEVVEGEVDQSDPSLLDEEEAEGGYVLACQT 75
|
....*....
gi 501077508 489 TIESDLEVQ 497
Cdd:cd00207 76 RVTDGLVIE 84
|
|
| Fer2 |
pfam00111 |
2Fe-2S iron-sulfur cluster binding domain; |
419-491 |
8.21e-04 |
|
2Fe-2S iron-sulfur cluster binding domain;
Pssm-ID: 395061 [Multi-domain] Cd Length: 77 Bit Score: 38.27 E-value: 8.21e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501077508 419 TDFTAEAPEDTLILTLACgkyrfnKNTFGDI-----NGICGSCKCKVRKGSVSSTSLETLTPEEIEQGYVLACSSTIE 491
Cdd:pfam00111 6 KGVTIEVPDGETTLLDAA------EEAGIDIpyscrGGGCGTCAVKVLEGEDQSDQSFLEDDELAAGYVVLACQTYPK 77
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05290 |
PRK05290 |
hybrid cluster protein; Provisional |
1-452 |
0e+00 |
|
hybrid cluster protein; Provisional
Pssm-ID: 235391 Cd Length: 546 Bit Score: 776.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 1 MFCIQCEQTIQTpavKGCsFAQGMCGKTSEVSDLQDVLVYTLQGVSFWAARALEFNIINDEINQWAPRACFSTLTNVNFD 80
Cdd:PRK05290 1 MFCYQCEQTARG---NGC-TAQGVCGKTAETADLQDLLIYALKGLSAYALKARELGIIDHEVDRFVPEALFTTLTNVNFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 81 PERILELTSQAATYKALLKDQVMSAATLADEVvlnvPNVANFELPNSAEEILAFAPQVAVNRGKDqVHEDVIGLRLLCLY 160
Cdd:PRK05290 77 DERIVGYIKEAIALREALKAKLAADGNAPEDL----PDAALWLPADDLEELLAQAAEVGVLADAT-ENEDIRSLRELLLY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 161 GLKGAAAYMEHARVLEQTNNDIFAEYHEIMAWLGTDPEDLGELLDCSMRIDLMNYKVMEMLDHGETATFGHPEPTTVNVK 240
Cdd:PRK05290 152 GLKGMAAYAEHARVLGQTDEEIYAFYHKALAALGDDPLDVDELLALVLECGKMNVKVMALLDKANTETYGHPEPTKVNIG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 241 PVKGKCILVSGHDLHDLEKILQQTEGKGINVYTNGEMLPEHGYPELKKYSHLVGNYGSAWQNQQKEFANFPGAIVMTSNC 320
Cdd:PRK05290 232 VRKGPGILVSGHDLKDLEELLEQTEGTGINVYTHGEMLPAHGYPELKKYPHLVGNYGSAWQNQQKEFASFPGPILMTTNC 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 321 LLNPNvGQYADRLFTRSIVGWPGVAHLEGD---DFSQVVECALAQEGFQHDEIEHNITVGFGRNALMNAAPAVIDQVKQG 397
Cdd:PRK05290 312 IIPPK-GSYKDRIFTTGIVGWPGVKHIEGDgkkDFSPVIEKALELPGFPPDEIEHEITVGFAHNAVLAVADKVIDAVKSG 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 501077508 398 NIKHFFLVGGCDGDKAERSYYTDFTAEAPEDTLILTLACGKYRFNKNTFGDINGI 452
Cdd:PRK05290 391 AIRHFFLMGGCDGAKPGRNYYTEFAEKLPKDTVILTLGCGKYRFNKLDLGDIGGI 445
|
|
| hybrid_clust |
TIGR01703 |
hydroxylamine reductase; This model represents a family of proteins containing an unusual ... |
1-452 |
0e+00 |
|
hydroxylamine reductase; This model represents a family of proteins containing an unusual 4Fe-2S-2O hydrid cluster. Earlier reports had proposed a 6Fe-6S prismane cluster. This subfamily is heterogeneous with respect to the presence or absence of a region of about 100 amino acids not far from the N-terminus of the protein. Members have been described as monomeric. The general function is unknown, although members from E. coli and several other species have hydroxylamine reductase activity. Members are found in various bacteria, in Archaea, and in several parasitic eukaryotes: Giardia intestinalis, Trichomonas vaginalis, and Entamoeba histolytica. [Cellular processes, Detoxification, Energy metabolism, Amino acids and amines]
Pssm-ID: 130764 Cd Length: 522 Bit Score: 565.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 1 MFCIQCEQTIQTpavKGCSfAQGMCGKTSEVSDLQDVLVYTLQGVSFWAARALEFNIINdEINQWAPRACFSTLTNVNFD 80
Cdd:TIGR01703 1 MFCYQCEQTARG---TGCT-VRGVCGKDPETANLQDLLVYVLKGISLWALQARKLGIDS-EIDSFIPRALFSTLTNVNFD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 81 PERILELTSQAATYKALLKDQvmsaatladevvlnvpnvaNFELPNSAEEILAFAPqvavNRGKDQVHEDVIGLRLLCLY 160
Cdd:TIGR01703 76 EDRIVEYIEDAIKLREKLKKK-------------------CRLADSNSLLIQSFAL----NGDKSHVNDDVNSLRDLLLY 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 161 GLKGAAAYMEHARVLEQTNNDIFAEYHEIMAWLGTDPEDLGELLDCSMRIDLMNYKVMEMLDHGETATFGHPEPTTVNVK 240
Cdd:TIGR01703 133 GIKGIAAYLYHARELGYDDEEIYAFLEEALASTLTNVFDADELIDLALEVGKMNLEAMKLLDKANTETYGLPEPTEVNIG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 241 PVKGKCILVSGHDLHDLEKILQQTEGKGINVYTNGEMLPEHGYPELKKYSHLVGNYGSAWQNQQKEFANFPGAIVMTSNC 320
Cdd:TIGR01703 213 TTEGKAILVSGHDLKDLEELLEQTEGTGINVYTHGEMLPAHGYPELKKYPHLAGNYGGAWQDQQREFAEFPGPILMTSNC 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 321 LLNPNVgQYADRLFTRSIVGWPGVAHLEGDDFSQVVECALAQEGFQHDEIEHNITVGFGRNALMNAAPAVIDQVKQGNIK 400
Cdd:TIGR01703 293 IIPPRK-SYKDRIFTTGIVGWPGVKHIENYDFSPVIEKALELPGFPKELEEGTITTGFGHHTILALADKIVELVKEGKIR 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 501077508 401 HFFLVGGCDGDKAERSYYTDFTAEAPEDTLILTLACGKYRFNKNTFGDINGI 452
Cdd:TIGR01703 372 HFFLVGGCDGPNPERNYYTEFARKLPKDAIILTLACGKYRFNKLDLGDIEGI 423
|
|
| HCP |
cd01914 |
Hybrid cluster protein (HCP), formerly known as prismane, is thought to play a role in ... |
1-452 |
2.75e-170 |
|
Hybrid cluster protein (HCP), formerly known as prismane, is thought to play a role in nitrogen metabolism but its specific function is unknown. HCP has three structural domains, an N-terminal alpha-helical domain, and two similar domains comprising a central beta-sheet flanked by alpha-helices. HCP contains two iron-sulfur clusters, one of which is a [Fe4-S4] cubane cluster similar to that of carbon monoxide dehydrogenase (CODH). The second cluster, referred to as the hybrid cluster, is a hybrid [Fe4-S2-O2] center located at the interface of the three domains. Although the hybrid cluster is buried within the protein, it is accessible through a large hydrophobic cavity.
Pssm-ID: 238895 Cd Length: 423 Bit Score: 486.78 E-value: 2.75e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 1 MFCIQCEQTIQtpaVKGCSFAqGMCGKTSEVSDLQDvlvytlqgvsfwaaralefniindeinqwapracfstltnvnfd 80
Cdd:cd01914 1 MFCYQCEQTAK---GTGCTVR-GVCGKDPEVANLQD-------------------------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 81 perileltsqaatykallkdqvmsaatladevvlnvpnvanfelpnsaeeilafapqvavnrgkdqvhedviglrllclY 160
Cdd:cd01914 33 -------------------------------------------------------------------------------Y 33
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 161 GLKGAAAYMEHARVLEQTNNDIFAEYHEIMAWLGTDPEDLGELLDCSMRIDLMNYKVMEMLDHGETATFGHPEPTTVNVK 240
Cdd:cd01914 34 GLKGIAAYAEHARVLGYDDEEIYAFIEKALASLLDNPLDADELLALALETGRMNLKVMELLDKANTETYGHPEPTEVNIG 113
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 241 PVKGKCILVSGHDLHDLEKILQQTEGKGINVYTNGEMLPEHGYPELKKYSHLVGNYGSAWQNQQKEFANFPGAIVMTSNC 320
Cdd:cd01914 114 VRAGKGILVSGHDLKDLEELLEQTEGTGVDVYTHGEMLPAHGYPELKKYPHLVGNYGGAWQNQQKEFARFPGPILMTTNC 193
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 321 LLNPNvGQYADRLFTRSIVGWPGVAHLEGDDFSQVVECALAQEGFQHDEIEHNITVGFGRNALMNAAPAVIDQVKQGNIK 400
Cdd:cd01914 194 IIPPR-ESYKDRIFTTGIVGWPGVKHIEGKDFSEVIEKAKELPGFPEEEESGTITTGFAHNQVLAVADKVVEAVKSGKIR 272
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 501077508 401 HFFLVGGCDGDKAERSYYTDFTAEAPEDTLILTLACGKYRFNKNTFGDINGI 452
Cdd:cd01914 273 HFFVVGGCDGRHKGRNYYTEFAEKLPKDTVILTLGCGKYRFNKLDLGDIGGI 324
|
|
| Prismane |
pfam03063 |
Prismane/CO dehydrogenase family; This family includes both hybrid-cluster proteins and the ... |
1-456 |
9.75e-151 |
|
Prismane/CO dehydrogenase family; This family includes both hybrid-cluster proteins and the beta chain of carbon monoxide dehydrogenase. The hybrid-cluster proteins contain two Fe/S centres - a [4Fe-4S] cubane cluster, and a hybrid [4Fe-2S-2O] cluster. The physiological role of this protein is as yet unknown, although a role in nitrate/nitrite respiration has been suggested. The prismane protein from Escherichia coli was shown to contain hydroxylamine reductase activity (NH2OH + 2e + 2 H+ -> NH3 + H2O). This activity is rather low. Hydroxylamine reductase activity was also found in CO-dehydrogenase in which the active site Ni was replaced by Fe. The CO dehydrogenase contains a Ni-3Fe-2S-3O centre.
Pssm-ID: 460790 [Multi-domain] Cd Length: 539 Bit Score: 441.20 E-value: 9.75e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 1 MFCIQCEQTiqtpavkGCS---FAQGMCGKTSEVSDLQDVLVYTLQGVSFWAARALEFNIINDEinqwaprACFSTLTNV 77
Cdd:pfam03063 1 MFCRQCEMG-------PCRitpKPRGVCGKTADTIVARNLLRYVAAGAAAHSDHARELGLTLKE-------ALFGTLTNY 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 78 NFDPERILELTSQAATYKALLKDqvmsaatladevvlnvpnvanfelpnsAEEILAFAPQVAVNRGKDQvHEDVIGLRLL 157
Cdd:pfam03063 67 NIDDERKLKRIAEALGIRTELKD---------------------------IEELAAEVADVGLEDFYGK-NEDIRSLREL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 158 CLYGLKGAAAymEHARVLEQTNNDIFAEYHEIMAWLGTDPEDLgelLDCSMRIDLMNYKVMEMLDHGETATFGHPEP--T 235
Cdd:pfam03063 119 APYGRKGLWA--EHAIVPGGIDREVFEFMHRTLTGLDSDPLDL---LLLALRCGLADLGGMELLDEANDILFGTPEPvlT 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 236 TVNVKPVK--GKCILVSGHDLHDLEKILQQTEGKGINVYTNGEMLPEHGYPELK-KYSHLVGNYGSAWQNQQKEFANFPG 312
Cdd:pfam03063 194 EVNLGVLDkdYVNILVSGHDPKDLEMLLEQTEGTGINVYAHGEMLPGHCCPGLKlKYRHGVGNYGNAWQQELAEFTGFPD 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 313 AIVMTSNCLLNP--NVGQ-YADRLFTRSIVGW-PGVAHLEGD------DFSQVVECALAQEGFQHDEIEH------NITV 376
Cdd:pfam03063 274 AIVVDTNCIMPPlaSVAScYHTRLITTSPVGKiPGATHIEFDeekadkDASEIIEKAIEAFKFREIEKVEipgekvGGVA 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 377 GFG----RNALMNAAPAVIDQVKQGNIKHFFLVGGCDGDKAERSYYTDFTAE-APEDTLILTLACGKYRFNKNTFGDI-- 449
Cdd:pfam03063 354 GFSteaiHEAVLGSADPLIDAIKSGAIRGFVLVVGCDNAKPGRDYYTELAKElIPKDILVLTTGCAKYRFNKLGLGDIea 433
|
490
....*....|....*..
gi 501077508 450 -----NGI-----CGSC 456
Cdd:pfam03063 434 aelagDGLppvldMGQC 450
|
|
| PRK12310 |
PRK12310 |
hydroxylamine reductase; Provisional |
1-451 |
7.63e-129 |
|
hydroxylamine reductase; Provisional
Pssm-ID: 183427 Cd Length: 433 Bit Score: 381.57 E-value: 7.63e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 1 MFCIQCEQTiqtpAVKGCSFAqGMCGKTSEVSDLQDVLVYTLQGVSFWAARALEFNIINDEINQWAPRACFSTLTNVNFD 80
Cdd:PRK12310 5 MFCYQCEQT----ATGGCTVM-GVCGKDETLASLQDTLIFGLKGIAAYRYHARELGYTDPEVDAFLAEALYSTLTNVNFD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 81 PERILELtsqaatykallkdqvmsaatladevvlnvpnvanfelpnsaeeilafapqvavnrgkdqvhedviglrllcly 160
Cdd:PRK12310 80 LQEHIDL------------------------------------------------------------------------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 161 glkgaaaymeharvleqtnndifaeyheimawlgtdpedlgeLLDCSMridlMNYKVMEMLDHGETATFGHPEPTTVNVK 240
Cdd:PRK12310 87 ------------------------------------------ALKVGK----ANLKVMELLDKAHTETFGEPEPVEVTQG 120
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 241 PVKGKCILVSGHDLHDLEKILQQTEGKGINVYTNGEMLPEHGYPELKKYSHLVGNYGSAWQNQQKEFANFPGAIVMTSNC 320
Cdd:PRK12310 121 TVEGKAILVTGHNLKALEELLKQTEGKGINVYTHSEMLPAHGYPELKKYKHLKGNIGKAWYDQRKLFEKFPGAILGTTNC 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 321 LLNPNvGQYADRLFTRSIVGWPGVAHLEGDDFSQVVECALAQEGFQHDEIEhNITVGFGRNALMNAAPAVIDQVKQGNIK 400
Cdd:PRK12310 201 VMPPK-GSYADRMFTYGIAGLEGVQHIENDDFTPLIEKALELPELEMESDE-TLVTGFHHTTVLSLAPKIIEAVKEGKIR 278
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 501077508 401 HFFLVGGCDGDKAERSYYTDFTAEAPEDTLILTLACGKYRFNKNTFGDING 451
Cdd:PRK12310 279 RFFVIAGCDAPGKGREYYRELATSLPKDTVILTLSCGKFRFNDLDYGTIEG 329
|
|
| Hcp |
COG1151 |
Hydroxylamine reductase (hybrid-cluster protein) [Energy production and conversion]; |
1-454 |
4.12e-120 |
|
Hydroxylamine reductase (hybrid-cluster protein) [Energy production and conversion];
Pssm-ID: 440765 Cd Length: 613 Bit Score: 365.29 E-value: 4.12e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 1 MFCIQCEQTiqtpavkGCSF----AQGMCGKTSEVSDLQDVLVYTLQGVSFWAARALE-------------FNIINDEIN 63
Cdd:COG1151 38 MCCRQCEQG-------PCRItpktPRGVCGKTADTIVARNLLRYVAKGAAAHADHAREvaltlkaaaegadYEIKDEEKL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 64 QWAPRACFSTltnvnfdpERILELTSQAATYKALLKDQVMSAAtladevvlnvPNVANFelpnsaeeILAFAPQvavnrg 143
Cdd:COG1151 111 RFVAEALGIT--------TEGKDLIEIALELADALLEDFGKAG----------GEPATW--------LEAKAPE------ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 144 kdqvhEDVIGLRLLclyglkgaaaymeharvlEQTNNDIFAEYHEIMAWLGTD-PEDLGELLDCSMRIDLMNYKVMEMLD 222
Cdd:COG1151 159 -----ERIESWREL------------------GIEPRGIDREIVEALARTHTGvDLDPVNLLLLALRTGLADWGGMALLD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 223 HGETATFGHPEPTTVNVKPV----KGKCILVSGHDLH----------DLEKILQQTEGKGINVY----TNGEMLPEHGYP 284
Cdd:COG1151 216 EANDILFGTPEPTEVEVNLGvlkeDGVNILVHGHDPKlseaiveaarDLEELAKQTGAKGINVYgiccTGGEMLPRHGYP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 285 ElKKYSHLVGNYGSAwqnqqkEFANFPGAI---VMTSNCLLnPNVGQYA-----DRLFTRSIVGWPGVAHLEGD------ 350
Cdd:COG1151 296 E-KKYVHLAGNYGSA------EFAIFTGAIdamVVDTNCIM-PPLASVAecyytDRITTTGVVGIPGAEHIEFDeegale 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 351 DFSQVVECALAQEGFQHDE------IEHNITVGFGRNALMNA---APAVIDQVKQGNIKHFFLVGGCDGDKAER--SYYT 419
Cdd:COG1151 368 DASEIIEKAIENFKPREDEkvyipqEKGEIVVGFSHEAVLAAlgsADPLIDAIKSGKIRGFVLVVGCDGRKPGRdyNYYT 447
|
490 500 510
....*....|....*....|....*....|....*..
gi 501077508 420 DFTAEAPEDTLILTLACGKYRFNKNTFGDINGI--CG 454
Cdd:COG1151 448 LFKELIPNDVLVLTTGCAKYRLNKLGLGDIEAAelAG 484
|
|
| PRK05274 |
PRK05274 |
2-keto-3-deoxygluconate permease; Provisional |
49-476 |
5.23e-74 |
|
2-keto-3-deoxygluconate permease; Provisional
Pssm-ID: 235384 Cd Length: 326 Bit Score: 236.72 E-value: 5.23e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 49 AARALEFNIINDEINQWAPRA-CFSTLTNVNFDpERILELtsqaatykallkdqvMSAATLADEVVLNVPNVANfELPNS 127
Cdd:PRK05274 14 GGMMLVPLLLGALINTFAPGAlYFGSFTNALFK-TGAVPI---------------LAVFLFCMGASINLRATGT-VLKKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 128 AEEILAFapqVAVNRGKDQVHEDVIGLRLLCLyGLKGAAAYMEHARVLEQTNNDIfaeYHEIMAWLGTDPEDLGELLDCS 207
Cdd:PRK05274 77 GTLLLTK---FAVAALVGVIAGKFIGEEGIRL-GGFAGLSTLAIIAAMDNTNGGL---YAALMGQYGTKEDAGAFVLMSL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 208 MRIDLMNYKVmemLDHGETATFGHPEPTTVNvkpvkgkCILVSGHDLHDLEKILQQTEGKGINVytngeMLPEHGYPelk 287
Cdd:PRK05274 150 EDGPFMTMLA---LGAAGLASFPPPALVGAV-------LPLLVGFILGNLDPELRQFLGKAVPV-----LIPFFAFA--- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 288 kyshlvgnYGSAWQNQQKEFANFPGAIVMTSNCLLNPNVGQYADRLFTrsivGWPGVAHLEGDDFSQVVECALAqegfQH 367
Cdd:PRK05274 212 --------LGNGIDLGTIITAGLSGILLGVAVVAVTGIPLYLADRLIG----GGNGVAGAAAGSTAGNAVATPA----AV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 368 DEIEHNItVGFGRNALMNAAPAVIdqvkqgnikhfflvggcdgdkaersyytdftaeapedtliltlacgkyrfnkntfg 447
Cdd:PRK05274 276 AAADPSF-APFAPAATAQVAAAVI-------------------------------------------------------- 298
|
410 420
....*....|....*....|....*....
gi 501077508 448 dINGICGSCKCKVRKGSVSSTSLETLTPE 476
Cdd:PRK05274 299 -VTAILAPILTAWWSKRVGKRAAETETPE 326
|
|
| PRK10684 |
PRK10684 |
HCP oxidoreductase, NADH-dependent; Provisional |
451-496 |
3.16e-13 |
|
HCP oxidoreductase, NADH-dependent; Provisional
Pssm-ID: 236735 [Multi-domain] Cd Length: 332 Bit Score: 70.51 E-value: 3.16e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 501077508 451 GICGSCKCKVRKGSVSSTSLETLTPEEIEQGYVLACSSTIESDLEV 496
Cdd:PRK10684 286 GVCGCCKTKVVSGEYTVSSTMTLTPAEIAQGYVLACSCHPQGDLVL 331
|
|
| Fdx |
COG0633 |
Ferredoxin [Energy production and conversion]; |
419-498 |
9.87e-13 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440398 [Multi-domain] Cd Length: 87 Bit Score: 63.71 E-value: 9.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 419 TDFTAEAPEDTLILTLA----------CGkyrfnkntfgdiNGICGSCKCKVRKGSVSSTSLETLTPEEIEQGYVLACSS 488
Cdd:COG0633 9 EGHTVEVPAGESLLEAAlragidlpysCR------------SGACGTCHVRVLEGEVDHREEDALSDEERAAGSRLACQA 76
|
90
....*....|
gi 501077508 489 TIESDLEVQI 498
Cdd:COG0633 77 RPTSDLVVEL 86
|
|
| COG3894 |
COG3894 |
Uncharacterized 2Fe-2S and 4Fe-4S clusters-containing protein, contains DUF4445 domain ... |
422-498 |
6.61e-12 |
|
Uncharacterized 2Fe-2S and 4Fe-4S clusters-containing protein, contains DUF4445 domain [Function unknown];
Pssm-ID: 443101 [Multi-domain] Cd Length: 621 Bit Score: 67.91 E-value: 6.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 422 TAEAPEDTLILTLA----------CGKyrfnkntfgdiNGICGSCKCKVRKGSVSS-TSLET--LTPEEIEQGYVLACSS 488
Cdd:COG3894 14 RVEVEAGTTLLDAAreagvdidapCGG-----------RGTCGKCKVKVEEGEFSPvTEEERrlLSPEELAEGYRLACQA 82
|
90
....*....|
gi 501077508 489 TIESDLEVQI 498
Cdd:COG3894 83 RVLGDLVVEV 92
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
419-497 |
3.33e-11 |
|
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.
Pssm-ID: 238126 [Multi-domain] Cd Length: 84 Bit Score: 59.33 E-value: 3.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 419 TDFTAEAPEDTLILTLA----------CGkyrfnkntfgdiNGICGSCKCKVRKGSVSSTSLETLTPEEIEQGYVLACSS 488
Cdd:cd00207 8 SGVEVEVPEGETLLDAAreagidipysCR------------AGACGTCKVEVVEGEVDQSDPSLLDEEEAEGGYVLACQT 75
|
....*....
gi 501077508 489 TIESDLEVQ 497
Cdd:cd00207 76 RVTDGLVIE 84
|
|
| PRK07609 |
PRK07609 |
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated |
450-498 |
2.78e-07 |
|
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
Pssm-ID: 181058 [Multi-domain] Cd Length: 339 Bit Score: 52.57 E-value: 2.78e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 501077508 450 NGICGSCKCKVRKGSVSST--SLETLTPEEIEQGYVLACSSTIESDLEVQI 498
Cdd:PRK07609 39 NGACGSCKGRLLEGEVEQGphQASALSGEERAAGEALTCCAKPLSDLVLEA 89
|
|
| HCP_like |
cd00587 |
The HCP family of iron-sulfur proteins includes hybrid cluster protein (HCP), acetyl-CoA ... |
390-454 |
3.34e-06 |
|
The HCP family of iron-sulfur proteins includes hybrid cluster protein (HCP), acetyl-CoA synthase (ACS), and carbon monoxide dehydrogenase (CODH), all of which contain [Fe4-S4] metal clusters at their active sites. These proteins have a conserved alpha-beta rossman fold domain. HCP, formerly known as prismane, is thought to play a role in nitrogen metabolism but its specific function is unknown. Acetyl-CoA synthase (ACS), is found in acetogenic and methanogenic organisms and is responsible for the synthesis and breakdown of acetyl-CoA. ACS forms a heterotetramer with carbon monoxide dehydrogenase (CODH) consisting of two ACS and two CODH subunits. CODH reduces carbon dioxide to carbon monoxide and ACS then synthesizes acetyl-CoA from carbon monoxide and CoA.
Pssm-ID: 238330 [Multi-domain] Cd Length: 258 Bit Score: 48.36 E-value: 3.34e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501077508 390 VIDQVKQGNIKHFFLVGGCDGDKAERSYYTDFTAEAPE-DTLILTLACGKYRFNKNTFGDINGICG 454
Cdd:cd00587 85 VGIAVVDGTIPGVALIVGCNNDKKQDKAYADIAKELMKrGVMVLATGCAAEALLKLGLEDGAGILG 150
|
|
| CODH |
cd01915 |
Carbon monoxide dehydrogenase (CODH) is found in acetogenic and methanogenic organisms and is ... |
229-437 |
9.62e-05 |
|
Carbon monoxide dehydrogenase (CODH) is found in acetogenic and methanogenic organisms and is responsible for the synthesis and breakdown of acetyl-CoA, respectively. CODH has two types of metal clusters, a cubane [Fe4-S4] center (B-cluster) similar to that of hybrid cluster protein (HCP) and a Ni-Fe-S center (C-cluster) where carbon monoxide oxidation occurs. Bifunctional CODH forms a heterotetramer with acetyl-CoA synthase (ACS) consisting of two CODH and two ACS subunits while monofunctional CODH forms a homodimer. Bifunctional CODH reduces carbon dioxide to carbon monoxide and ACS then synthesizes acetyl-CoA from carbon monoxide, CoA, and a methyl group donated by another protein (CoFeSP), while monofunctional CODH oxidizes carbon monoxide to carbon dioxide. CODH and ACS each have a metal cluster referred to as the C- and A-clusters, respectively.
Pssm-ID: 238896 Cd Length: 613 Bit Score: 44.95 E-value: 9.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 229 FGHPEPTTV--NVKPVKGKC--ILVSGHDLHDLEKILQQTE------------GKGINVY----TNGEMLPEHGYPelkk 288
Cdd:cd01915 225 FGTPKPVVSeaNLGVLDPDYvnIAVHGHNPVLSEAIVEAARelelqeeakaagAKGINVVgiccTGNELLMRHGVP---- 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 289 yshLVGNYGSAwqnqqkEFANFPGAI---VMTSNCLLnPNVGQYADRLFTR-----SIVGWPGVAHLegdDFS--QVVEC 358
Cdd:cd01915 301 ---LAGNWLSQ------ELAIATGAVdamVVDVQCIM-PSLPQYAECFHTKlittsDVAKIPGAEHI---DFDpeEADES 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501077508 359 A-----LAQEGFQH--------DEIEHNITVGFGRNALMNA-----APaVIDQVKQGNIKHFFLVGGCDGDKAER-SYYT 419
Cdd:cd01915 368 AkeiirMAIEAFKRrkkskvyiPQHKSKAVVGFSTEAILDAlggslKP-LIDAIASGNIKGVVGIVGCNNLKVQQdSSHV 446
|
250
....*....|....*....
gi 501077508 420 DFTAE-APEDTLILTLACG 437
Cdd:cd01915 447 TLAKElIKRNVLVLATGCG 465
|
|
| PLN03136 |
PLN03136 |
Ferredoxin; Provisional |
451-497 |
7.56e-04 |
|
Ferredoxin; Provisional
Pssm-ID: 178681 [Multi-domain] Cd Length: 148 Bit Score: 40.12 E-value: 7.56e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 501077508 451 GICGSCKCKVRKGSVSSTSLETLTPEEIEQGYVLACSSTIESDLEVQ 497
Cdd:PLN03136 94 GSCSSCAGKVVSGSIDQSDQSFLDDEQISEGYVLTCVAYPTSDVVIE 140
|
|
| Fer2 |
pfam00111 |
2Fe-2S iron-sulfur cluster binding domain; |
419-491 |
8.21e-04 |
|
2Fe-2S iron-sulfur cluster binding domain;
Pssm-ID: 395061 [Multi-domain] Cd Length: 77 Bit Score: 38.27 E-value: 8.21e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501077508 419 TDFTAEAPEDTLILTLACgkyrfnKNTFGDI-----NGICGSCKCKVRKGSVSSTSLETLTPEEIEQGYVLACSSTIE 491
Cdd:pfam00111 6 KGVTIEVPDGETTLLDAA------EEAGIDIpyscrGGGCGTCAVKVLEGEDQSDQSFLEDDELAAGYVVLACQTYPK 77
|
|
| petF |
CHL00134 |
ferredoxin; Validated |
451-497 |
9.64e-03 |
|
ferredoxin; Validated
Pssm-ID: 177056 [Multi-domain] Cd Length: 99 Bit Score: 35.85 E-value: 9.64e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 501077508 451 GICGSCKCKVRKGSVSSTSLETLTPEEIEQGYVLACSSTIESDLEVQ 497
Cdd:CHL00134 45 GACSTCAGKVTEGTVDQSDQSFLDDDQLEAGFVLTCVAYPTSDCTIL 91
|
|
| |
