|
Name |
Accession |
Description |
Interval |
E-value |
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
257-939 |
0e+00 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 924.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 257 IKKTKTVCTYCGVGCSFEVWTKDREILKVQPSHDSPANKIATCVKGKFSWGHINSDQRLTKPLVRKNGEFHEVEWDEALN 336
Cdd:COG3383 4 MKKVKTVCPYCGVGCGIDLEVKDGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVNSPDRLTTPLIRRGGEFREVSWDEALD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 337 VIADNFTSIKEKYGPDALSFISSSKATNEESYLMQKLARQVIGTNNVDNCSRYCQAPATKGLFRTVGHGGDSGSIEDLEK 416
Cdd:COG3383 84 LVAERLREIQAEHGPDAVAFYGSGQLTNEENYLLQKLARGVLGTNNIDNNARLCMASAVAGLKQSFGSDAPPNSYDDIEE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 417 AAMSVLIGTNTAEAHPVIASRMKRAQKlFGQKIHVFDIRKHEMAERADRFYQPKPGTDLAWLSAVTKYIIDHDLHDKAFI 496
Cdd:COG3383 164 ADVILVIGSNPAEAHPVLARRIKKAKK-NGAKLIVVDPRRTETARLADLHLQIKPGTDLALLNGLLHVIIEEGLVDEDFI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 497 DEWVDDFDEYYKSLETFTMAFAEEATGIPKSELIKFAEECAKAESVVICWAMGITQQDIGSDSSTAISNLLLVTGNYRRP 576
Cdd:COG3383 243 AERTEGFEELKASVAKYTPERVAEITGVPAEDIREAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 577 GTGAYPLRGHNNVQGCSDMGSMPDKITGYQSIEADDIRAKFEKEYGVK-LNPKAGKDNHEMVEGIHDGEVHSLYLYGEDT 655
Cdd:COG3383 323 GTGPFPLTGQNNVQGGRDMGALPNVLPGYRDVTDPEHRAKVADAWGVPpLPDKPGLTAVEMFDAIADGEIKALWIIGENP 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 656 GIVDSNINFVQAAFEKLDFMVVQDEFLTFTATYADVVLPASPSLEKDGTFTNTERRIQRLYQALEPLGDSKPDWKIFQAI 735
Cdd:COG3383 403 AVSDPDANHVREALEKLEFLVVQDIFLTETAEYADVVLPAASWAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIAEL 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 736 ANKLGFDWNYKHPSEIMDEVARLTPLYAGVSYDRLEGFNSLQWPV-QPDGTDEPILYLEGFNFDNGKAKLFPLSFDN-YF 813
Cdd:COG3383 483 ARRLGYGFDYDSPEEVFDEIARLTPDYSGISYERLEALGGVQWPCpSEDHPGTPRLFTGRFPTPDGKARFVPVEYRPpAE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 814 KQDEIYDIHVNNGRLLEHFHEGNMTYQTPMIKYKVPRAFVEISPELAEDRGIHEGAEVKLISETGEAVLQVHVTDRVKGK 893
Cdd:COG3383 563 LPDEEYPLVLTTGRLLDQWHTGTRTRRSPRLNKHAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGEVVLRARVTDRVRPG 642
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 686208005 894 EIYIPlnndaMENGDlGAINLLTNSDVDQYTDTPSYKRTSCRLEVI 939
Cdd:COG3383 643 TVFMP-----FHWGE-GAANALTNDALDPVSKQPEYKACAVRVEKV 682
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
262-936 |
0e+00 |
|
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate dehydrogenase alpha chains found mainly archaea but also in alpha and gamma proteobacteria and a small number of gram positive bacteria. The alpha chain contains domains for molybdopterin dinucleotide binding and molybdopterin oxidoreductase (pfam01568 and pfam00384, respectively). The holo-enzyme also contains beta and gamma subunits. The enzyme catalyzes the oxidation of formate (produced from pyruvate during anaerobic growth) to carbon dioxide with the concomitant release of two electrons and two protons. The enzyme's purpose is to allow growth on formate in some circumstances and, in the case of FdhH in gamma proteobacteria, to pass electrons to hydrogenase (by which process acid is neutralized). This model is well-defined, with only a single fragmentary sequence falling between trusted and noise. The alpha subunit of a version of nitrate reductase is closely related.
Pssm-ID: 130652 [Multi-domain] Cd Length: 671 Bit Score: 815.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 262 TVCTYCGVGCSFEVWTKDREILKVQPSHDSPANKIATCVKGKFSWGHINSDQRLTKPLVRKNGEFHEVEWDEALNVIADN 341
Cdd:TIGR01591 1 TVCPYCGVGCSLNLVVKDGKIVRVEPYQGHKANRGHLCVKGYFAWEFINSKDRLTTPLIREGDKFREVSWDEAISYIAEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 342 FTSIKEKYGPDALSFISSSKATNEESYLMQKLARQVIGTNNVDNCSRYCQAPATKGLFRTVGHGGDSGSIEDLEKAAMSV 421
Cdd:TIGR01591 81 LKEIKEKYGPDSIGFIGSSRGTNEENYLLQKLARAVIGTNNVDNCARVCHGPSVAGLKQTVGIGAMSNTISEIENADLIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 422 LIGTNTAEAHPVIASRMKRAQKLfGQKIHVFDIRKHEMAERADRFYQPKPGTDLAWLSAVTKYIIDHDLHDKAFIDEWVD 501
Cdd:TIGR01591 161 IIGYNPAESHPVVAQYLKNAKRN-GAKIIVIDPRKTETAKIADLHIPLKPGTDIALLNAMANVIIEEGLYDKAFIEKRTE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 502 DFDEYYKSLETFTMAFAEEATGIPKSELIKFAEECAKAESVVICWAMGITQQDIGSDSSTAISNLLLVTGNYRRPGTGAY 581
Cdd:TIGR01591 240 GFEEFREIVKGYTPEYVEDITGVPADLIREAARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGKPGGGVN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 582 PLRGHNNVQGCSDMGSMPDKITGYQSIEADDIRAKFEKEYG-VKLNPKAGKDNHEMVEGIHDGEVHSLYLYGEDTGIVDS 660
Cdd:TIGR01591 320 PLRGQNNVQGACDMGALPDFLPGYQPVSDEEVREKFAKAWGvVKLPAEPGLRIPEMIDAAADGDVKALYIMGEDPLQSDP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 661 NINFVQAAFEKLDFMVVQDEFLTFTATYADVVLPASPSLEKDGTFTNTERRIQRLYQALEPLGDSKPDWKIFQAIANKLG 740
Cdd:TIGR01591 400 NTSKVRKALEKLELLVVQDIFMTETAKYADVVLPAAAWLEKEGTFTNAERRIQRFFKAVEPKGESKPDWEIIQELANALG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 741 FDWNYKHPSEIMDEVARLTPLYAGVSYDRLEGFNSLQWPVQP-DGTDEPILYLEGFNFDNGKAKLFPLSF-DNYFKQDEI 818
Cdd:TIGR01591 480 LDWNYNHPQEIMDEIRELTPLFAGLTYERLDELGSLQWPCNDsDASPTSYLYKDKFATPDGKAKFIPLEWvAPIEEPDDE 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 819 YDIHVNNGRLLEHFHEGNMTYQTPMIKYKVPRAFVEISPELAEDRGIHEGAEVKLISETGEAVLQVHVTDRVKGKEIYIP 898
Cdd:TIGR01591 560 YPLILTTGRVLTHYNVGEMTRRVAGLRRLSPEPYVEINTEDAKKLGIKDGDLVKVKSRRGEITLRAKVSDRVNKGAIYIT 639
|
650 660 670
....*....|....*....|....*....|....*...
gi 686208005 899 LNNdamengDLGAINLLTNSDVDQYTDTPSYKRTSCRL 936
Cdd:TIGR01591 640 MHF------WDGAVNNLTTDDLDPISGTPEYKYTAVRI 671
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
261-808 |
0e+00 |
|
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. Members of the MopB_Formate-Dh-H CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239154 [Multi-domain] Cd Length: 512 Bit Score: 772.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 261 KTVCTYCGVGCSFEVWTKDREILKVQPSHDSPANKIATCVKGKFSWGHINSDQRLTKPLVRKNGEFHEVEWDEALNVIAD 340
Cdd:cd02753 1 KTVCPYCGVGCGLELWVKDNKIVGVEPVKGHPVNRGKLCVKGRFGFDFVNSKDRLTKPLIRKNGKFVEASWDEALSLVAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 341 NFTSIKEKYGPDALSFISSSKATNEESYLMQKLARQVIGTNNVDNCSRYCQAPATKGLFRTVGHGGDSGSIEDLEKAAMS 420
Cdd:cd02753 81 RLKEIKDKYGPDAIAFFGSAKCTNEENYLFQKLARAVGGTNNVDHCARLCHSPTVAGLAETLGSGAMTNSIADIEEADVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 421 VLIGTNTAEAHPVIASRMKRAqKLFGQKIHVFDIRKHEMAERADRFYQPKPGTDLAWLSAVTKYIIDHDLHDKAFIDEWV 500
Cdd:cd02753 161 LVIGSNTTEAHPVIARRIKRA-KRNGAKLIVADPRRTELARFADLHLQLRPGTDVALLNAMAHVIIEEGLYDEEFIEERT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 501 DDFDEYYKSLETFTMAFAEEATGIPKSELIKFAEECAKAESVVICWAMGITQQDIGSDSSTAISNLLLVTGNYRRPGTGA 580
Cdd:cd02753 240 EGFEELKEIVEKYTPEYAERITGVPAEDIREAARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGTGV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 581 YPLRGHNNVQGCSDMGSMPDKITGYqsieaddirakfekeygvklnpkagkdnhemvegihdgeVHSLYLYGEDTGIVDS 660
Cdd:cd02753 320 NPLRGQNNVQGACDMGALPNVLPGY---------------------------------------VKALYIMGENPALSDP 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 661 NINFVQAAFEKLDFMVVQDEFLTFTATYADVVLPASPSLEKDGTFTNTERRIQRLYQALEPLGDSKPDWKIFQAIANKLG 740
Cdd:cd02753 361 NTNHVRKALESLEFLVVQDIFLTETAELADVVLPAASFAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIQELANRLG 440
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 686208005 741 FDWNYKHPSEIMDEVARLTPLYAGVSYDRLEGFNSLQWPVQP-DGTDEPILYLEGFNFDNGKAKLFPLS 808
Cdd:cd02753 441 YPGFYSHPEEIFDEIARLTPQYAGISYERLERPGGLQWPCPDeDHPGTPILHTERFATPDGKARFMPVE 509
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
257-937 |
1.02e-172 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 519.40 E-value: 1.02e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 257 IKKTKTVCTYCGVGCSFEVWTKDREILKVQPSHDSPANKIATCVKGKFSWGHINSDQRLTKPLVRKN----GEFHEVEWD 332
Cdd:COG0243 21 TKTVKTTCPGCGVGCGLGVKVEDGRVVRVRGDPDHPVNRGRLCAKGAALDERLYSPDRLTYPMKRVGprgsGKFERISWD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 333 EALNVIADNFTSIKEKYGPDALSFISSS----KATNEESYLMQKLARQvIGTNNVDNCSRYCQAPATKGLFRTVGHGGDS 408
Cdd:COG0243 101 EALDLIAEKLKAIIDEYGPEAVAFYTSGgsagRLSNEAAYLAQRFARA-LGTNNLDDNSRLCHESAVAGLPRTFGSDKGT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 409 GSIEDLEKAAMSVLIGTNTAEAHPVIASRMKRAQKLFGQKIHVFDIRKHEMAERADRFYQPKPGTDLAWLSAVTKYIIDH 488
Cdd:COG0243 180 VSYEDLEHADLIVLWGSNPAENHPRLLRRLREAAKKRGAKIVVIDPRRTETAAIADEWLPIRPGTDAALLLALAHVLIEE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 489 DLHDKAFIDEWVDDFDEYYKSLETFTMAFAEEATGIPKSELIKFAEECAKAESVVICWAMGITQQDIGSDSSTAISNLLL 568
Cdd:COG0243 260 GLYDRDFLARHTVGFDELAAYVAAYTPEWAAEITGVPAEDIRELAREFATAKPAVILWGMGLQQHSNGTQTVRAIANLAL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 569 VTGNYRRPGTGAYPLRGhnnvqgcsdmgsmpdkitgyqsieaddirakfekeygvklnpkagkdnHEMVEGiHDGEVHSL 648
Cdd:COG0243 340 LTGNIGKPGGGPFSLTG------------------------------------------------EAILDG-KPYPIKAL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 649 YLYGEDTGIVDSNINFVQAAFEKLDFMVVQDEFLTFTATYADVVLPASPSLEKDGTFTNTE-RRIQRLYQALEPLGDSKP 727
Cdd:COG0243 371 WVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARYADIVLPATTWLERDDIVTNSEdRRVHLSRPAVEPPGEARS 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 728 DWKIFQAIANKLG----FDWNyKHPSEIMDEVARLTPlYAGVSYDRLEGFNSLQWPVQPDGtdepiLYLE--GFNFDNGK 801
Cdd:COG0243 451 DWEIFAELAKRLGfeeaFPWG-RTEEDYLRELLEATR-GRGITFEELREKGPVQLPVPPEP-----AFRNdgPFPTPSGK 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 802 AKLFPLS------------FDNYFKQDEIYDIHVNNGRLLEHFHegNMTYQTPMIKYKVPRAFVEISPELAEDRGIHEGA 869
Cdd:COG0243 524 AEFYSETlalpplpryappYEGAEPLDAEYPLRLITGRSRDQWH--STTYNNPRLREIGPRPVVEINPEDAAALGIKDGD 601
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 686208005 870 EVKLISETGEAVLQVHVTDRVKGKEIYIP-LNNDAMENGDLGAINLLTNSDVDQYTDTPSYKRTSCRLE 937
Cdd:COG0243 602 LVRVESDRGEVLARAKVTEGIRPGVVFAPhGWWYEPADDKGGNVNVLTPDATDPLSGTPAFKSVPVRVE 670
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
261-807 |
1.40e-167 |
|
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. Members of the MopB_Nitrate-R-NapA CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239155 [Multi-domain] Cd Length: 565 Bit Score: 502.14 E-value: 1.40e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 261 KTVCTYCGVGCSFEVWTKDREILKVQPSHDSPANKIATCVKGKFSWGHINSDQRLTKPLVRKNG-EFHEVEWDEALNVIA 339
Cdd:cd02754 1 KTTCPYCGVGCGVEIGVKDGKVVAVRGDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLLRRNGgELVPVSWDEALDLIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 340 DNFTSIKEKYGPDALSFISSSKATNEESYLMQKLARQVIGTNNVDNCSRYCQAPATKGLFRTVGHGGDSGSIEDLEKAAM 419
Cdd:cd02754 81 ERFKAIQAEYGPDSVAFYGSGQLLTEEYYAANKLAKGGLGTNNIDTNSRLCMASAVAGYKRSFGADGPPGSYDDIEHADC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 420 SVLIGTNTAEAHPVIASRM-KRAQKLFGQKIHVFDIRKHEMAERADRFYQPKPGTDLAWLSAVTKYIIDHDLHDKAFIDE 498
Cdd:cd02754 161 FFLIGSNMAECHPILFRRLlDRKKANPGAKIIVVDPRRTRTADIADLHLPIRPGTDLALLNGLLHVLIEEGLIDRDFIDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 499 WVDDFDEYYKSLETFTMAFAEEATGIPKSELIKFAEECAKAESVVICWAMGITQQDIGSDSSTAISNLLLVTGNYRRPGT 578
Cdd:cd02754 241 HTEGFEELKAFVADYTPEKVAEITGVPEADIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGRPGS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 579 GAYPLRGHNNVQGCSDMGSMPDKITGYQSIEADDIRAKFEKEYGV---KLNPKAGKDNHEMVEGIHDGEVHSLYLYGEDT 655
Cdd:cd02754 321 GPFSLTGQPNAMGGREVGGLANLLPGHRSVNNPEHRAEVAKFWGVpegTIPPKPGLHAVEMFEAIEDGEIKALWVMCTNP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 656 GIVDSNINFVQAAFEKLDFMVVQDEFL-TFTATYADVVLPASPSLEKDGTFTNTERRIQRLYQALEPLGDSKPDWKIFQA 734
Cdd:cd02754 401 AVSLPNANRVREALERLEFVVVQDAFAdTETAEYADLVLPAASWGEKEGTMTNSERRVSLLRAAVEPPGEARPDWWILAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 735 IANKLGFD--WNYKHPSEIMDEVARLTPL----YAGVSYDRLEGfNSLQWPVQPDGTDEPILYLEGFNFDN--GKAKLFP 806
Cdd:cd02754 481 VARRLGFGelFPYTSPEEVFEEYRRLSRGrgadLSGLSYERLRD-GGVQWPCPDGPPEGTRRLFEDGRFPTpdGRARFVA 559
|
.
gi 686208005 807 L 807
Cdd:cd02754 560 V 560
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
261-739 |
8.52e-125 |
|
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site.
Pssm-ID: 238218 [Multi-domain] Cd Length: 374 Bit Score: 383.99 E-value: 8.52e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 261 KTVCTYCGVGCSFEVWTKDREILKVQPSHDSPANKIATCVKGKFSWGHINSDQRLTKPLVRKN--GEFHEVEWDEALNVI 338
Cdd:cd00368 1 PSVCPFCGVGCGILVYVKDGKVVRIEGDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGgrGKFVPISWDEALDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 339 ADNFTSIKEKYGPDALSFISSSKATNEESYLMQKLARqVIGTNNVDNCSRYCQAPATKGLfRTVGHGGDSGSIEDLEKAA 418
Cdd:cd00368 81 AEKLKEIREKYGPDAIAFYGGGGASNEEAYLLQKLLR-ALGSNNVDSHARLCHASAVAAL-KAFGGGAPTNTLADIENAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 419 MSVLIGTNTAEAHPVIASRMKRAqKLFGQKIHVFDIRKHEMAERADRFYQPKPGTDLAWLSAvtkyiidhdlhdkafidE 498
Cdd:cd00368 159 LILLWGSNPAETHPVLAARLRRA-KKRGAKLIVIDPRRTETAAKADEWLPIRPGTDAALALA-----------------E 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 499 WvddfdeyyksletftmafAEEATGIPKSELIKFAEECAKAESVVICWAMGITQQDIGSDSSTAISNLLLVTGNYRRPGT 578
Cdd:cd00368 221 W------------------AAEITGVPAETIRALAREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 579 GAYPlrGHNNVQgcsdmgSMPDkitgyqsieaddirakfekeygvklnpkagkdnhemvegihdgevhslylygedtgiv 658
Cdd:cd00368 283 GLGP--GGNPLV------SAPD---------------------------------------------------------- 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 659 dsnINFVQAAFEKLDFMVVQDEFLTFTATYADVVLPASPSLEKDGTFTNTERRIQRLYQALEPLGDSKPDWKIFQAIANK 738
Cdd:cd00368 297 ---ANRVRAALKKLDFVVVIDIFMTETAAYADVVLPAATYLEKEGTYTNTEGRVQLFRQAVEPPGEARSDWEILRELAKR 373
|
.
gi 686208005 739 L 739
Cdd:cd00368 374 L 374
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
261-777 |
5.08e-94 |
|
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. Members of the MopB_Formate-Dh-Na-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239153 [Multi-domain] Cd Length: 649 Bit Score: 311.64 E-value: 5.08e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 261 KTVCTYCGVGCSFEVWTKDREILKVQPSHDSPANKIATCVKGKFSWGHINSDQRLTKPLVRKNG--EFHEVEWDEALNVI 338
Cdd:cd02752 1 RTICPYCSVGCGLIAYVQNGVWVHQEGDPDHPVNRGSLCPKGAALRDFVHSPKRLKYPMYRAPGsgKWEEISWDEALDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 339 ADNFTSIKEK------------YGPDALSFISSSKATNEESYLMQKLARqVIGTNNVDNCSRYCQAPATKGLFRTVGHGG 406
Cdd:cd02752 81 ARKMKDIRDAsfveknaagvvvNRPDSIAFLGSAKLSNEECYLIRKFAR-ALGTNNLDHQARIUHSPTVAGLANTFGRGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 407 DSGSIEDLEKAAMSVLIGTNTAEAHPVIASRMKRAQKLFGQKIHVFDIRKHEMAERADRFYQPKPGTDLAWLSAVTKYII 486
Cdd:cd02752 160 MTNSWNDIKNADVILVMGGNPAEAHPVSFKWILEAKEKNGAKLIVVDPRFTRTAAKADLYVPIRSGTDIAFLGGMINYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 487 DHDLhdkafidEWVddfdeyyksletftmafaEEATGIPKSELIKFAEECAK----AESVVICWAMGITQQDIGSDSSTA 562
Cdd:cd02752 240 RYTP-------EEV------------------EDICGVPKEDFLKVAEMFAAtgrpDKPGTILYAMGWTQHTVGSQNIRA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 563 ISNLLLVTGNYRRPGTGAYPLRGHNNVQGCSDMGSMPDKITGYqsieaddirakfekeYGvKLNPKAGKdnhemvegihd 642
Cdd:cd02752 295 MCILQLLLGNIGVAGGGVNALRGHSNVQGATDLGLLSHNLPGY---------------LG-GQNPNSSF----------- 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 643 gevhslylygedtgivdSNINFVQAAFEKLDFMVVQDEFLTFTATYAD-------------VVLPASPSLEKDGTFTNTE 709
Cdd:cd02752 348 -----------------PNANKVRRALDKLDWLVVIDPFPTETAAFWKnpgmdpksiqtevFLLPAACQYEKEGSITNSG 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 710 RRIQRLYQALEPLGDSKPDWKIFQAIANKLGF--------------DWNYKH-----PSEIMDEVAR--LTPLYAGVSYD 768
Cdd:cd02752 411 RWLQWRYKVVEPPGEAKSDGDILVELAKRLGFlyekeggafpepitKWNYGYgdeptPEEIAREINGgaLTDGYTGQSPE 490
|
570
....*....|....*.
gi 686208005 769 RL-------EGFNSLQ 777
Cdd:cd02752 491 RLkahgqnvHTFDTLR 506
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
314-804 |
2.54e-77 |
|
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239168 [Multi-domain] Cd Length: 574 Bit Score: 264.17 E-value: 2.54e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 314 RLTKPLVRKNGEFH--EVEWDEALNVIADNFTSIKekygPDALSFISSSKATNEESYLMQKLARqVIGTNNVDNCSRYCQ 391
Cdd:cd02767 64 RLTYPMRYDAGSDHyrPISWDEAFAEIAARLRALD----PDRAAFYTSGRASNEAAYLYQLFAR-AYGTNNLPDCSNMCH 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 392 APATKGLFRTVGHGGDSGSIEDLEKAAMSVLIGTNTAEAHPVIASRMKRAQKLfGQKIHVFDIRKHEMAER--------- 462
Cdd:cd02767 139 EPSSVGLKKSIGVGKGTVSLEDFEHTDLIFFIGQNPGTNHPRMLHYLREAKKR-GGKIIVINPLREPGLERfanpqnpes 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 463 --------ADRFYQPKPGTDLAWLSAVTKYIIDHDLH-----DKAFIDEWVDDFDEYYKSLETFTMAFAEEATGIPKSEL 529
Cdd:cd02767 218 mltggtkiADEYFQVRIGGDIALLNGMAKHLIERDDEpgnvlDHDFIAEHTSGFEEYVAALRALSWDEIERASGLSREEI 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 530 IKFAEECAKAESVVICWAMGITQQDIGSDSSTAISNLLLVTGNYRRPGTGAYPLRGHNNVQGCSDMGsmpdkITgyqSIE 609
Cdd:cd02767 298 EAFAAMYAKSERVVFVWGMGITQHAHGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQGDRTMG-----IT---EKP 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 610 ADDIRAKFEKEYGVKLNPKAGKDNHEMVEGIHDGEVHSLYLYGEDTGIVDSNINFVQAAFEKLDFMVVQDEFLTFTATY- 688
Cdd:cd02767 370 FPEFLDALEEVFGFTPPRDPGLDTVEAIEAALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLTVHVATKLNRSHLVh 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 689 --ADVVLPASPSLEKDGTFTN---------------------TERRIQR-----LYQALEP-LGDSKPDWKIFqaiankl 739
Cdd:cd02767 450 geEALILPCLGRTEIDMQAGGaqavtvedsmsmthtsrgrlkPASRVLLseeaiVAGIAGArLGEAKPEWEIL------- 522
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 686208005 740 gfdwnykhpseiMDEVARLTPLYAGVSYDRLEGFNS--LQWP--VQPDGTDEPIlylegFNFDNGKAKL 804
Cdd:cd02767 523 ------------VEDYDRIRDEIAAVIYEGFADFNQrgDQPGgfHLPNGARERK-----FNTPSGKAQF 574
|
|
| Fdhalpha-like |
TIGR01701 |
oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of ... |
314-937 |
6.08e-75 |
|
oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of oxidoreductase alpha subunits most closely related to a group of formate dehydrogenases including the E. coli FdhH protein (TIGR01591). These alpha subunits contain a molybdopterin cofactor and generally associate with two other subunits which contain iron-sulfur clusters and cytochromes. The particular subunits with which this enzyme interacts and the substrate which is reduced is unknown at this time. In Ralstonia, the gene is associated with the cbb operon, but is not essential for CO2 fixation.
Pssm-ID: 273765 [Multi-domain] Cd Length: 743 Bit Score: 262.05 E-value: 6.08e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 314 RLTKPLVRKNGE--FHEVEWDEALNVIADNFTSikekYGPDALSFISSSKATNEESYLMQKLARQvIGTNNVDNCSRYCQ 391
Cdd:TIGR01701 99 RLTYPLSLRPGSdhYTPISWDDAYQEIAAKLNS----LDPKQVAFYTSGRTSNEAAYLYQLFARS-LGSNNLPDCSNMCH 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 392 APATKGLFRTVGHGGDSGSIEDLEKAAMSVLIGTNTAEAHPVIASRMKRAQKLfGQKIHVFDIRKHEMAER--------- 462
Cdd:TIGR01701 174 EPSSVALKRSIGIGKGSVNLEDFEHTDCLVFIGSNAGTNHPRMLKYLYAAKKR-GAKIIAINPLRERGLERfwipqipes 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 463 ---------ADRFYQPKPGTDLAWLSAVTKYIIDHD------LHDKAFIDEWVDDFDEYYKSLETFTMAFAEEATGIPKS 527
Cdd:TIGR01701 253 mltgggtqiSSEYYQVRIGGDIALFNGVMKLLIEAEdaqpgsLIDHEFIANHTNGFDELRRHVLQLNWNDIERSSGLSQE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 528 ELIKFAEECAKAESVVICWAMGITQQDIGSDSSTAISNLLLVTGNYRRPGTGAYPLRGHNNVQGCSDMGsmpdkITGYQS 607
Cdd:TIGR01701 333 EILEFAKLLANSRRVVFCWAMGLTQHAHGVDNISQVANLALLRGNIGKPGAGVCPIRGHSNVQGDRTMG-----ITEKPE 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 608 IEaddIRAKFEKEYGVKLNPKAGKDNHEMVEGIHDGEVHSLYLYGEDTGIVDSNINFVQAAFEKLDFMVVQDEFLTFT-- 685
Cdd:TIGR01701 408 EE---FLARLSQIYGFTPPDWPGDTTVAMIEAILTGKVRAFICLGGNFLEAMPDTAAIERALRQLDLRVHVATKLNRShv 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 686 -ATYADVVLPASPSLEKDG--------TFTNTERRIQRLYQALEPLGDS-KPDWKIFQAIANKL----GFDWNY--KHPS 749
Cdd:TIGR01701 485 lAKEEALILPVLGRYEQDGqgtgkqavSVESSMRMVHFSRGILKPRGAElRSEWAIIAEIAKALlpetPVAWEIlvDTYD 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 750 EIMDEVARLTPLYAGVSY--DRLEGFnslQWPVQPdgTDEPIlylegFNFDNGKAKLFP---LSFDnyFKQDEIYDIHVN 824
Cdd:TIGR01701 565 QIRDAIAATNPGYDDINHrkRRPDGF---QLPGAA--LCERK-----FPTPDGKANFIViplPEFR--VPTGHEFELVLV 632
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 825 NGRLLEHFHEGNMTYQTPMIKYKVPRAFVEISPELAEDRGIHEGAEVKLISETGEAVLQvhvtdRVKGKEIY---IPLNN 901
Cdd:TIGR01701 633 TLRSHDQFNTTIYGEDDRYRGVDGHRRVVFMNETDIKKLGLRNGERVDVYNQYGDGQKR-----KFDNLRIVfydTPTGN 707
|
650 660 670
....*....|....*....|....*....|....*.
gi 686208005 902 DAMENGDlgAINLLTNSDVDQYTDTPSYKRTSCRLE 937
Cdd:TIGR01701 708 AAAYYPE--ANPLLPLDHHDPQSKTPEYKTIPVRLE 741
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
241-879 |
3.97e-72 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 255.59 E-value: 3.97e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 241 PLFAISDSEAEMRKERIKKTKTVCTYCGVGCSFEVWTKDREILKVQPSHDSPANKIATCVKGKFSWGHINSDQRLTKPLV 320
Cdd:PRK13532 24 SLPAVANAVVGSAQTAIKWDKAPCRFCGTGCGVLVGTKDGRVVATQGDPDAPVNRGLNCIKGYFLSKIMYGKDRLTQPLL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 321 R-------KNGEFHEVEWDEALNVIADNF-TSIKEKyGPDALSFISSSKATNEESYLMQKLARQVIGTNNVDNCSRYCQA 392
Cdd:PRK13532 104 RmkdgkydKEGEFTPVSWDQAFDVMAEKFkKALKEK-GPTAVGMFGSGQWTIWEGYAASKLMKAGFRSNNIDPNARHCMA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 393 PATKGLFRTVGHGGDSGSIEDLEKAAMSVLIGTNTAEAHPVIASRM--KRAQKLfGQKIHVFDIRKHEMAERADRFYQPK 470
Cdd:PRK13532 183 SAVVGFMRTFGIDEPMGCYDDIEAADAFVLWGSNMAEMHPILWSRVtdRRLSNP-DVKVAVLSTFEHRSFELADNGIIFT 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 471 PGTDLAWLSAVTKYIIDHDLHDKAFIDE----------------------------------WVDDFDEYYKSLETFTMA 516
Cdd:PRK13532 262 PQTDLAILNYIANYIIQNNAVNWDFVNKhtnfrkgatdigyglrpthplekaaknpgtagksEPISFEEFKKFVAPYTLE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 517 FAEEATGIPKSELIKFAEECA-KAESVVICWAMGITQQDIGSDSSTAISNLLLVTGNYRRPGTGAYPLRGHNNVQGC--- 592
Cdd:PRK13532 342 KTAKMSGVPKEQLEQLAKLYAdPNRKVVSFWTMGFNQHTRGVWANNLVYNIHLLTGKISTPGNGPFSLTGQPSACGTare 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 593 ---------SDMGSMPDKitgyqsieaddIRAKFEKEYGV---KLNPKAGKDNHEMVEGIHDGEVHSLYlygedtgiVDS 660
Cdd:PRK13532 422 vgtfshrlpADMVVTNPK-----------HREIAEKIWKLpegTIPPKPGYHAVAQDRMLKDGKLNAYW--------VMC 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 661 NiNFVQA----------AFEKLD-FMVVQDEFLTFTATYADVVLPASPSLEKDGTFTNTERRIQRLYQALEPLGDSKPD- 728
Cdd:PRK13532 483 N-NNMQAgpnineerlpGWRNPDnFIVVSDPYPTVSALAADLILPTAMWVEKEGAYGNAERRTQFWRQQVKAPGEAKSDl 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 729 WKIFQ--------------------AIANKLGFDWNYKH------------PSEIMDEVAR--------LTPLYAG---- 764
Cdd:PRK13532 562 WQLVEfskrfkteevwpeellakkpEYRGKTLYDVLFANgqvdkfplselaEGYLNDEAKHfgfyvqkgLFEEYASfgrg 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 765 -----VSYDRLEGFNSLQWPVQpDGTDEPILYLEGF--------------NFDnGKAKLFPLSF-DNYFKQDEIYDIHVN 824
Cdd:PRK13532 642 hghdlAPFDTYHKVRGLRWPVV-DGKETLWRYREGYdpyvkagegfkfygKPD-GKAVIFALPYePPAESPDEEYDLWLS 719
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 686208005 825 NGRLLEHFHEGNMTYQTPMIKYKVPRAFVEISPELAEDRGIHEGAEVKLISETGE 879
Cdd:PRK13532 720 TGRVLEHWHTGSMTRRVPELYRAFPEAVCFMHPEDAKARGLRRGDEVKVVSRRGE 774
|
|
| MopB_NDH-1_NuoG2-N7 |
cd02771 |
MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of ... |
261-765 |
8.59e-71 |
|
MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1) found in various bacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Unique to this group, compared to the other prokaryotic and eukaryotic groups in this domain protein family (NADH-Q-OR-NuoG2), is an N-terminal [4Fe-4S] cluster (N7/N1c) present in the second domain. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239172 [Multi-domain] Cd Length: 472 Bit Score: 243.06 E-value: 8.59e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 261 KTVCTYCGVGCSFEVWTKDREILKVQPSHDSPANKIATCVKGKFSWGHINSDQRLTKPLVRKNGEFHEVEWDEALNVIAD 340
Cdd:cd02771 1 PSICHHCSVGCNISLGERYGELRRVENRYNGAVNHYFLCDRGRFGYGYVNSRDRLTQPLIRRGGTLVPVSWNEALDVAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 341 NFTSIKEKYGPdalsfISSSKATNEESYLMQKLARQVIGTNNVDNCSRYCQAPATKGLfrtvghGGDSGSIEDLEKAAMS 420
Cdd:cd02771 81 RLKEAKDKVGG-----IGSPRASNESNYALQKLVGAVLGTNNVDHRARRLIAEILRNG------PIYIPSLRDIESADAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 421 VLIGTNTAEAHPVIASRMKRAQKLFGQKIhVFDIRKHEMAERADRFYQPKPGTDLAWLSAVTKYIIDHDlHDKAFIDewV 500
Cdd:cd02771 150 LVLGEDLTQTAPRIALALRQAARRKAVEL-AALSGIPKWQDAAVRNIAQGAKSPLFIVNALATRLDDIA-AESIRAS--P 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 501 DDFDEYYKSLETFTMAFAEEATGIPKSELIK-FAEECAKAESVVICWamGITQQDIGSDSSTAisNLLLVTGNyRRPGTG 579
Cdd:cd02771 226 GGQARLGAALARAVDASAAGVSGLAPKEKAArIAARLTGAKKPLIVS--GTLSGSLELIKAAA--NLAKALKR-RGENAG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 580 AYPLRGHNNVQGCSDMGSMPDkitgyqsieaddirakfekeygvklnpKAGKDNHEMVEGIHDGEVHSLYLYGEDTGIVD 659
Cdd:cd02771 301 LTLAVEEGNSPGLLLLGGHVT---------------------------EPGLDLDGALAALEDGSADALIVLGNDLYRSA 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 660 SNINfVQAAFEKLDFMVVQDEFLTFTATYADVVLPASPSLEKDGTFTNTERRIQRLYQAL-EPLGDSKPDWKIFQAIANK 738
Cdd:cd02771 354 PERR-VEAALDAAEFVVVLDHFLTETAERADVVLPAASFAEKSGTFVNYEGRAQRFFKAYdDPAGDARSDWRWLHALAAK 432
|
490 500 510
....*....|....*....|....*....|..
gi 686208005 739 LG-----FDWnykhpsEIMDEVARLTPLYAGV 765
Cdd:cd02771 433 LGgklvpSDA------AILDEIIALVPGKAPV 458
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
262-806 |
2.01e-67 |
|
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239167 [Multi-domain] Cd Length: 501 Bit Score: 234.45 E-value: 2.01e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 262 TVCTY-CGVGCSFEVWTKDREILKVQPSHDSPANKIATCVKGKFSWGHINSDQRLTKPLVR---KNGEFHEVEWDEALNV 337
Cdd:cd02766 2 SVCPLdCPDTCSLLVTVEDGRIVRVEGDPAHPYTRGFICAKGARYVERVYSPDRLLTPLKRvgrKGGQWERISWDEALDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 338 IADNFTSIKEKYGPDALSFISSS-----KATNEESYLMQKL-ARQVIGTnnvdncsrYCQAPATKGLFRTVGhGGDSGSI 411
Cdd:cd02766 82 IAAKLKEIKAEYGPESILPYSYAgtmglLQRAARGRFFHALgASELRGT--------ICSGAGIEAQKYDFG-ASLGNDP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 412 EDLEKAAMSVLIGTNTAEAHPVIASRMKRAQKLfGQKIHVFDIRKHEMAERADRFYQPKPGTDLAWLSAVTKYIIDHDLH 491
Cdd:cd02766 153 EDMVNADLIVIWGINPAATNIHLMRIIQEARKR-GAKVVVIDPYRTATAARADLHIQIRPGTDGALALGVAKVLFREGLY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 492 DKAFIDEWVDDFDEYYKSLETFTMAFAEEATGIPKSELIKFAEECAKAESVVICWAMGITQQDIGSDSSTAISNLLLVTG 571
Cdd:cd02766 232 DRDFLARHTEGFEELKAHLETYTPEWAAEITGVSAEEIEELARLYGEAKPPSIRLGYGMQRYRNGGQNVRAIDALPALTG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 572 NYRRPGTGAYplrghnnvqgcsdmgsmpdkitgyqsieaddirakfekeYGVKLNPkagkdnhemvegihdgeVHSLYLY 651
Cdd:cd02766 312 NIGVPGGGAF---------------------------------------YSNSGPP-----------------VKALWVY 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 652 GEDTGIVDSNINFV-QAAFEKLDFMVVQDEFLTFTATYADVVLPASPSLEKD---GTFTNTerRIQRLYQALEPLGDSKP 727
Cdd:cd02766 336 NSNPVAQAPDSNKVrKGLAREDLFVVVHDQFMTDTARYADIVLPATTFLEHEdvyASYWHY--YLQYNEPAIPPPGEARS 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 728 DWKIFQAIANKLGFDWNYKHPS--EIMDEVARLTPLY-AGVSYDRLEGFNSLQWPVQPdgtdepiLYLEGFNFDNGKAKL 804
Cdd:cd02766 414 NTEIFRELAKRLGFGEPPFEESdeEWLDQALDGTGLPlEGIDLERLLGPRKAGFPLVA-------WEDRGFPTPSGKFEF 486
|
..
gi 686208005 805 FP 806
Cdd:cd02766 487 YS 488
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
314-738 |
1.47e-66 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 227.67 E-value: 1.47e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 314 RLTKPLVRKN-GEFHEVEWDEALNVIADNFTSIKEKYGPD--ALSFISSSKATNEESYLMQKLARQVIGTN--NVDNCSR 388
Cdd:pfam00384 1 RLKYPMVRRGdGKFVRVSWDEALDLIAKKLKRIIKKYGPDaiAINGGSGGLTDVESLYALKKLLNRLGSKNgnTEDHNGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 389 YCQAPATKGLFRTVGHGGDSGSIEDLEKAAMSVLIGTNTAEAHPVIASRMKRAQKLFGQKIHVFDIRKHemAERADRFYQ 468
Cdd:pfam00384 81 LCTAAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRKAALKGKAKVIVIGPRLD--LTYADEHLG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 469 PKPGTDLAWLSAVTKYIIDHDLHDKAFidewvddfdeyyksletftmafaeeatgipkselikfaeecakAESVVICWAM 548
Cdd:pfam00384 159 IKPGTDLALALAGAHVFIKELKKDKDF-------------------------------------------APKPIIIVGA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 549 GITQQDIGSDSSTAISNLLLVTGNYRRPGTGAYPLrghNNVQGC-SDMGsmpdkitgyqsieADDIraKFEKEYGVKlnp 627
Cdd:pfam00384 196 GVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGL---NILQGAaSPVG-------------ALDL--GLVPGIKSV--- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 628 kagkdnhEMVEGIHDGEVHSLYLYGEDTGIVDSNINFVQAAFEKLDFMVVQDEFL-TFTATYADVVLPASPSLEKDGTFT 706
Cdd:pfam00384 255 -------EMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFVVYDGHHgDKTAKYADVILPAAAYTEKNGTYV 327
|
410 420 430
....*....|....*....|....*....|..
gi 686208005 707 NTERRIQRLYQALEPLGDSKPDWKIFQAIANK 738
Cdd:pfam00384 328 NTEGRVQSTKQAVPPPGEAREDWKILRALSEV 359
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
262-749 |
3.40e-63 |
|
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and other related proteins. Thiosulfate reductase catalyzes the cleavage of sulfur-sulfur bonds in thiosulfate. Polysulfide reductase is a membrane-bound enzyme that catalyzes the reduction of polysulfide using either hydrogen or formate as the electron donor. Members of the MopB_Thiosulfate-R-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239156 [Multi-domain] Cd Length: 454 Bit Score: 221.40 E-value: 3.40e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 262 TVCTYCGVGCSFEVWTKDREILKVQPSHDSPANKIATCVKGKFSWGHINSDQRLTKPLVR--KNGE--FHEVEWDEALNV 337
Cdd:cd02755 3 SICEMCSSRCGILARVEDGRVVKIDGNPLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRvgERGEgkFREASWDEALQY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 338 IADNFTSIKEKYGPDALSFisSSKATNEESYLmQKLArQVIGTNNVDNCSRYCQAPATKGLFRTVGHGGDSGSIeDLEKA 417
Cdd:cd02755 83 IASKLKEIKEQHGPESVLF--GGHGGCYSPFF-KHFA-AAFGSPNIFSHESTCLASKNLAWKLVIDSFGGEVNP-DFENA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 418 AMSVLIGTNTAEA-HPVIASRMKRAQKLfGQKIHVFDIRKHEMAERADRFYQPKPGTDLAWLSAVTKYIIDHDLHDKAFI 496
Cdd:cd02755 158 RYIILFGRNLAEAiIVVDARRLMKALEN-GAKVVVVDPRFSELASKADEWIPIKPGTDLAFVLALIHVLISENLYDAAFV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 497 DEWVDDFDEYYKSLETFTMAFAEEATGIPKSELIKFAEECAKAESVVIC---WAMGITQQDIGSDSSTAISNLLLvtGNY 573
Cdd:cd02755 237 EKYTNGFELLKAHVKPYTPEWAAQITDIPADTIRRIAREFAAAAPHAVVdpgWRGTFYSNSFQTRRAIAIINALL--GNI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 574 RRPG-------TGAYPLRGHnNVQGCSDMGSMPDkitgyqsieaddiRAKFEKeygvklnpkagkdnhemvegihdgevh 646
Cdd:cd02755 315 DKRGglyyagsAKPYPIKAL-FIYRTNPFHSMPD-------------RARLIK--------------------------- 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 647 slylygedtgivdsninfvqaAFEKLDFMVVQDEFLTFTATYADVVLPASPSLEKDGTFT----NTERRIQRlYQALEPL 722
Cdd:cd02755 354 ---------------------ALKNLDLVVAIDILPSDTALYADVILPEATYLERDEPFSdkggPAPAVATR-QRAIEPL 411
|
490 500
....*....|....*....|....*..
gi 686208005 723 GDSKPDWKIFQAIANKLGFdwnYKHPS 749
Cdd:cd02755 412 YDTRPGWDILKELARRLGL---FGTPS 435
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
261-739 |
3.76e-61 |
|
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone oxidoreductase (NADH-Q-OR)/respiratory complex I/NADH dehydrogenase-1 (NDH-1). The NADH-Q-OR is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The atomic structure of complex I is not known and the mechanisms of electron transfer and proton pumping are not established. The nad11 gene codes for the largest (75-kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Escherichia coli, this subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The nad11 gene is nuclear-encoded in animals, plants, and fungi, but is still encoded in the mitochondrial genome of some protists. The Nad11/NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain family belongs to the molybdopterin_binding (MopB) superfamily of proteins. Bacterial type II NADH-quinone oxidoreductases and NQR-type sodium-motive NADH-quinone oxidoreductases are not homologs of this domain family.
Pssm-ID: 239169 [Multi-domain] Cd Length: 386 Bit Score: 213.30 E-value: 3.76e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 261 KTVCTYCGVGCSFEVWTKDREILKVQPSHDSPANKIATCVKGKFSWGHINSDQRLTKPLVRKNGEFHEVEWDEALNVIAD 340
Cdd:cd02768 1 ESIDVHDALGSNIRVDVRGGEVMRILPRENEAINEEWISDKGRFGYDGLNSRQRLTQPLIKKGGKLVPVSWEEALKTVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 341 NFTSIKekygPDALSFISSSKATNEESYLMQKLARQViGTNNVDNCSRYCQAPATKGLFRTVGHGgdsGSIEDLEKAAMS 420
Cdd:cd02768 81 GLKAVK----GDKIGGIAGPRADLESLFLLKKLLNKL-GSNNIDHRLRQSDLPADNRLRGNYLFN---TSIAEIEEADAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 421 VLIGTNTAEAHPVIASRMKRAqkLFGQKIHVFDIrkhemaeradrfyqpkpGTDLAWLSAVTKYIIDHdlhdkafIDEWV 500
Cdd:cd02768 153 LLIGSNLRKEAPLLNARLRKA--VKKKGAKIAVI-----------------GPKDTDLIADLTYPVSP-------LGASL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 501 DdfdeyyksletftmAFAEEATGipkSELIKFAEECAKAESVVICWAMGITQQDIGSDSStAISNLLLVtgnyrrPGTGA 580
Cdd:cd02768 207 A--------------TLLDIAEG---KHLKPFAKSLKKAKKPLIILGSSALRKDGAAILK-ALANLAAK------LGTGA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 581 yplRGHNNVQGCSDMGSmpdkitgyqSIEADDIRAKFEKEYGVKLnpkagkdnhemvegihdgevhSLYLYGEDtGIVDS 660
Cdd:cd02768 263 ---GLWNGLNVLNSVGA---------RLGGAGLDAGLALLEPGKA---------------------KLLLLGED-ELDRS 308
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 686208005 661 NINFVQaAFEKLDFMVVQDEFLTFTATYADVVLPASPSLEKDGTFTNTERRIQRLYQALEPLGDSKPDWKIFQAIANKL 739
Cdd:cd02768 309 NPPAAV-ALAAADAFVVYQGHHGDTGAQADVILPAAAFTEKSGTYVNTEGRVQRFKKAVSPPGDAREDWKILRALSNLL 386
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
261-798 |
6.59e-61 |
|
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239160 [Multi-domain] Cd Length: 477 Bit Score: 215.63 E-value: 6.59e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 261 KTVCTYCGVGCSFEVWTKDREILKVQPSHDSPANKIATCVKGKFSWGHINSDQRLTKPLVRKN----GEFHEVEWDEALN 336
Cdd:cd02759 1 KGTCPGCHSGCGVLVYVKDGKLVKVEGDPNHPTNKGRLCMRGLAAPEIVYHPDRLLYPLKRVGergeNKWERISWDEALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 337 VIADNFTSIKEKYGPDALSFIS-SSKATNEESYLMQKLARQVIGTNNVDNCSRYCQAPATKGLFRTVGHGGDSGSIeDLE 415
Cdd:cd02759 81 EIAEKLAEIKAEYGPESIATAVgTGRGTMWQDSLFWIRFVRLFGSPNLFLSGESCYWPRDMAHALTTGFGLGYDEP-DWE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 416 KAAMSVLIGTNTAEAHPV-IASRMKRAQKLfGQKIHVFDIRKHEMAERADRFYQPKPGTDLAWLSAVTKYIIDHDLHDKA 494
Cdd:cd02759 160 NPECIVLWGKNPLNSNLDlQGHWLVAAMKR-GAKLIVVDPRLTWLAARADLWLPIRPGTDAALALGMLNVIINEGLYDKD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 495 FIDEWVDDFDEYYKSLETFTMAFAEEATGIPKSELIKFAEECAKAESVVICWAMGITQQDIGSDSSTAISNLLLVTGNYR 574
Cdd:cd02759 239 FVENWCYGFEELAERVQEYTPEKVAEITGVPAEKIRKAARLYATAKPACIQWGLAIDQQKNGTQTSRAIAILRAITGNLD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 575 RPGT---GAYPLRGHnNVQGCSDMGSMPDkitgyqsiEADdirakfekeygvklnpkagkdnhemvegihdgevhslyly 651
Cdd:cd02759 319 VPGGnllIPYPVKML-IVFGTNPLASYAD--------TAP---------------------------------------- 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 652 gedtgivdsninfVQAAFEKLDFMVVQDEFLTFTATYADVVLPASPSLEKDGTFTNTERRI--QRLYQALEPLGDSKPDW 729
Cdd:cd02759 350 -------------VLEALKALDFIVVVDLFMTPTAMLADIVLPVAMSLERPGLRGGFEAENfvQLRQKAVEPYGEAKSDY 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 686208005 730 KIFQAIANKLGFD-WNYKHPSEIMDEvarltplyagvsYDRLEGFNSlqwpvqPDGTDEpiLY---LEGFNFD 798
Cdd:cd02759 417 EIVLELGKRLGPEeAEYYKYEKGLLR------------PDGQPGFNT------PTGKVE--LYstmLEELGYD 469
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
7-348 |
2.00e-57 |
|
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440657 [Multi-domain] Cd Length: 453 Bit Score: 205.07 E-value: 2.00e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 7 VTLDGKDYLVEPGTNLLEFIKSQDTFVPSICYNESMGPIQTCDTCTVEIDG--KIERSCSTVIDRPMTVNTVNNDVKDAQ 84
Cdd:COG1034 4 ITIDGKEVEVPKGTTVLQAAEKAGIEIPRFCYHPKLSIAGACRMCLVEVEGapKPVASCATPVTDGMVVKTDSPKVKKAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 85 KEALDRILEKHMLYCTVCDyNNGDCEihntmdawgLQHQTYEY--KEKPYE--------KDYGPFYRYDPNQCILCGRCV 154
Cdd:COG1034 84 KGVMEFLLINHPLDCPICD-QGGECD---------LQDQAMEYgvDESRYEeekrtvpkKDLGPLILLDMNRCILCTRCV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 155 EACQDI-EVNEtIRIDWDREHPRVIWDNDVPINessCVSCGQCATVCPcnammeVnmegnaGYMTDTepgslaamiDLTK 233
Cdd:COG1034 154 RFCDEIaGDPE-LGVIGRGEHSEIGTYLGKPLD---SEFSGNCIDVCP------V------GALTSK---------PFRF 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 234 KAepgygplfaisdseaemRKERIKKTKTVCTYCGVGCSFEVWTKDREILKVQPSHDSPANKIATCVKGKFSWGHINSDQ 313
Cdd:COG1034 209 KA-----------------RPWELKKTPSICPHCSVGCNIRVDVRGGKVYRVLPRENEAVNEEWLCDKGRFGYDGLNSPD 271
|
330 340 350
....*....|....*....|....*....|....*
gi 686208005 314 RLTKPLVRKNGEFHEVEWDEALNVIADNFTSIKEK 348
Cdd:COG1034 272 RLTRPLVRKDGELVEASWEEALAAAAEGLKALKKA 306
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
261-739 |
1.09e-55 |
|
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239163 [Multi-domain] Cd Length: 539 Bit Score: 202.24 E-value: 1.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 261 KTVCTYCGVGCSFEVWTKDREILKVQPSHDSPANKIATCVKGKfSWGHI-NSDQRLTKPLVRKNGEFHEVEWDEALNVIA 339
Cdd:cd02762 1 KRACILCEANCGLVVTVEDGRVASIRGDPDDPLSKGYICPKAA-ALGDYqNDPDRLRTPMRRRGGSFEEIDWDEAFDEIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 340 DNFTSIKEKYGPDALSFISSSKATNEES---YLMQKLArqVIGTNNVDNCSRYCQAPATKGLFRTVGHGGdSGSIEDLEK 416
Cdd:cd02762 80 ERLRAIRARHGGDAVGVYGGNPQAHTHAggaYSPALLK--ALGTSNYFSAATADQKPGHFWSGLMFGHPG-LHPVPDIDR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 417 AAMSVLIGTNTAEAH------PVIASRMKRAQKLfGQKIHVFDIRKHEMAERADRFYQPKPGTDLAWLSAVTKYIIDHDL 490
Cdd:cd02762 157 TDYLLILGANPLQSNgslrtaPDRVLRLKAAKDR-GGSLVVIDPRRTETAKLADEHLFVRPGTDAWLLAAMLAVLLAEGL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 491 HDKAFIDEWVDDFDEYYKSLETFTMAFAEEATGIPKSELIKFAEECAKAESVVICWAMGITQQDIGSDSSTAISNLLLVT 570
Cdd:cd02762 236 TDRRFLAEHCDGLDEVRAALAEFTPEAYAPRCGVPAETIRRLAREFAAAPSAAVYGRLGVQTQLFGTLCSWLVKLLNLLT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 571 GNYRRPGtgayplrGHNNVQGCSDMGSMPDKITGYQSIEADDIRAKFE--KEYGVKLNPkagkdnhEMVEGIHDGEVHSL 648
Cdd:cd02762 316 GNLDRPG-------GAMFTTPALDLVGQTSGRTIGRGEWRSRVSGLPEiaGELPVNVLA-------EEILTDGPGRIRAM 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 649 YLYGEDTGIVDSNINFVQAAFEKLDFMVVQDEFLTFTATYADVVLPASPSLEKD-GTFTNTE--RRIQRLYQAL-EPLGD 724
Cdd:cd02762 382 IVVAGNPVLSAPDGARLEAALGGLEFMVSVDVYMTETTRHADYILPPASQLEKPhATFFNLEfpRNAFRYRRPLfPPPPG 461
|
490
....*....|....*
gi 686208005 725 SKPDWKIFQAIANKL 739
Cdd:cd02762 462 TLPEWEILARLVEAL 476
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
222-879 |
4.33e-53 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 199.12 E-value: 4.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 222 PGSLAAMIDltkkaepgyGPLfaisdseaemrKERIKKTKTVCTYCGVGCSFEVWTKDREILKVQPSHDSPANKIATCVK 301
Cdd:PRK15488 26 PGALAANEI---------AQL-----------KGKTKLTPSICEMCSTRCPIEARVVNGKNVFIQGNPKAKSFGTKVCAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 302 GKFSWGHINSDQRLTKPLVRK----NGEFHEVEWDEALNVIADNFTSIKEKYGPDALSFISSSKATneeSYLMQKLArQV 377
Cdd:PRK15488 86 GGSGHSLLYDPQRIVKPLKRVgergEGKWQEISWDEAYQEIAAKLNAIKQQHGPESVAFSSKSGSL---SSHLFHLA-TA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 378 IGTNNVDNCSRYCqaPATKGLFRTVGHGGDSGsiEDLEKAAMSVLIGTNTAEAHPVIASR-MKRAQKLFGQKIHVFDIRK 456
Cdd:PRK15488 162 FGSPNTFTHASTC--PAGYAIAAKVMFGGKLK--RDLANSKYIINFGHNLYEGINMSDTRgLMTAQMEKGAKLVVFEPRF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 457 HEMAERADRFYQPKPGTDLAWLSAVTKYIIDHDLHDKAFIDEWVDDFDEYYKSLETFTMAFAEEATGIPKSELIKFAEEC 536
Cdd:PRK15488 238 SVVASKADEWHAIRPGTDLAVVLALCHVLIEENLYDKAFVERYTSGFEELAASVKEYTPEWAEAISDVPADDIRRIAREL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 537 AK-AESVVICWA--MGITQQDIgsDSSTAI--SNLLLvtGNYRRPGtGAYPLRG---HNNVQGCSDMGSMPD-KITGYQS 607
Cdd:PRK15488 318 AAaAPHAIVDFGhrATFTPEEF--DMRRAIfaANVLL--GNIERKG-GLYFGKNasvYNKLAGEKVAPTLAKpGVKGMPK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 608 IEA---DDIRAKFekeygvklnpKAGKDNHEMVEGIHDGEVHSL-YlygEDTGIVDSNINFVQA---------AFEKLDF 674
Cdd:PRK15488 393 PTAkriDLVGEQF----------KYIAAGGGVVQSIIDATLTQKpY---QIKGWVMSRHNPMQTvtdradvvkALKKLDL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 675 MVVQDEFLTFTATYADVVLPASPSLEKDGTFTNTERRIQRLY---QALEPLGDSKPDWKIFQAIANKLGFDWNYkhPSEI 751
Cdd:PRK15488 460 VVVCDVYLSESAAYADVVLPESTYLERDEEISDKSGKNPAYAlrqRVVEPIGDTKPSWQIFKELGEKMGLGQYY--PWQD 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 752 MDE-----VARLTPLYAGVsydRLEGFnsLQW-----------------------PVQPDGTDEPILYLEGFnfdNGKAK 803
Cdd:PRK15488 538 METlqlyqVNGDHALLKEL---KKKGY--VSFgvplllrepkmvakfvarypnakAVDEDGTYGSQLKFKTP---SGKIE 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 804 LFP------------LSFDN--YFKQDEIYDIhvnNGRLleHFHEGNMTYQTPMIKYKVPRAFVEISPELAEDRGIHEGA 869
Cdd:PRK15488 610 LFSaklealapgygvPRYRDvaLKKEDELYFI---QGKV--AVHTNGATQNVPLLANLMSDNAVWIHPQTAGKLGIKNGD 684
|
730
....*....|
gi 686208005 870 EVKLISETGE 879
Cdd:PRK15488 685 EIRLENSVGK 694
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
819-938 |
2.94e-49 |
|
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. This CD (MopB_CT_Formate-Dh-Na-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239193 [Multi-domain] Cd Length: 122 Bit Score: 170.10 E-value: 2.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 819 YDIHVNNGRLLEHFHEGNMTYQTPMIKYKVPRAFVEISPELAEDRGIHEGAEVKLISETGEAVLQVHVTDRVKGKEIYIP 898
Cdd:cd02792 3 FPLVLTTGRLTEHFHGGNMTRNSPYLAELQPEMFVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHEVGIP 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 686208005 899 LNNDAMENGDLGAINLLTNSDVDQYTDTPSYKRTSCRLEV 938
Cdd:cd02792 83 YHWGGMGLVIGDSANTLTPYVGDPNTQTPEYKAFLVNIEK 122
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
262-742 |
1.19e-45 |
|
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase (DMSOR) of Escherichia coli and other related DMSOR-like enzymes. Unlike other DMSOR-like enzymes, this group has a predicted N-terminal iron-sulfur [4Fe-4S] cluster binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239171 [Multi-domain] Cd Length: 617 Bit Score: 174.43 E-value: 1.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 262 TVCTY-CGVGCSFEVWTKDREILKVQPSH---DSPAN-KIATCVKGKFSWGHINSDQRLTKPLVRKN----GEFHEVEWD 332
Cdd:cd02770 2 SACTVnCGGRCPLKAHVKDGVITRIETDDtgdDDPGFhQIRACLRGRSQRKRVYNPDRLKYPMKRVGkrgeGKFVRISWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 333 EALNVIADNFTSIKEKYGPDALSFISSSKATNEESYLMQKLAR--QVIG--TNNVDNCSRYCQAPATKglfRTVGHGGDS 408
Cdd:cd02770 82 EALDTIASELKRIIEKYGNEAIYVNYGTGTYGGVPAGRGAIARllNLTGgyLNYYGTYSWAQITTATP---YTYGAAASG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 409 GSIEDLEKAAMSVLIGTNTAE-----AHPVIASR-MKRAqklfGQKIHVFDIRKHE-MAERADRFYQPKPGTDLAWLSAV 481
Cdd:cd02770 159 SSLDDLKDSKLVVLFGHNPAEtrmggGGSTYYYLqAKKA----GAKFIVIDPRYTDtAVTLADEWIPIRPGTDAALVAAM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 482 TKYIIDHDLHDKAFIDEWVDDFDE-----------YYKS--LETF------TMAFAEEATGIPKSELIKFAEECAKAESV 542
Cdd:cd02770 235 AYVMITENLHDQAFLDRYCVGFDAehlpegappneSYKDyvLGTGydgtpkTPEWASEITGVPAETIRRLAREIATTKPA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 543 VICWAMGITQQDIGSDSSTAISNLLLVTGNYRRPG--TGAYPLRGHNNVQGCSdMGSMP--DKITGYQSIEADDIRAKFE 618
Cdd:cd02770 315 AILQGWGPQRHANGEQAARAIMMLAAMTGNVGIPGgnTGARPGGSAYNGAGLP-AGKNPvkTSIPCFMWTDAIERGEEMT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 619 KEYGVKLNPKAGKDNHEMvegihdgevhsLYLYGEDTGI----VDSN-INFVQAAFEKLDFMVVQDEFLTFTATYADVVL 693
Cdd:cd02770 394 ADDGGVKGADKLKSNIKM-----------IWNYAGNTLInqhsDDNNtTRALLDDESKCEFIVVIDNFMTPSARYADILL 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 686208005 694 PASPSLEK-DGTFTNTERRIQRLY---QALEPLGDSKPDWKIFQAIANKLGFD 742
Cdd:cd02770 463 PDTTELEReDIVLTSNAGMMEYLIysqKAIEPLYECKSDYEICAELAKRLGVE 515
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
261-739 |
1.11e-42 |
|
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. Members of the MopB_Nitrate-R-NarG-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239151 [Multi-domain] Cd Length: 461 Bit Score: 162.49 E-value: 1.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 261 KTVCTYCGV----GCSFEVWTKDREILKVQPSHDSPANKIAT-------CVKGK-FSWgHINSDQRLTKPLVRK----NG 324
Cdd:cd02750 2 KVVRSTHGVnctgSCSWNVYVKNGIVTREEQATDYPETPPDLpdynprgCQRGAsFSW-YLYSPDRVKYPLKRVgargEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 325 EFHEVEWDEALNVIADNFTSIKEKYGPDALSFISSSKATNEESY-LMQKLArQVIGTNNVDNCSRYCQAPAtkGLFRTVG 403
Cdd:cd02750 81 KWKRISWDEALELIADAIIDTIKKYGPDRVIGFSPIPAMSMVSYaAGSRFA-SLIGGVSLSFYDWYGDLPP--GSPQTWG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 404 HGGDSGSIEDLEKAAMSVLIGTN-----TAEAHPVIASRMKraqklfGQKIHVFDIRKHEMAERADRFYQPKPGTDLAWL 478
Cdd:cd02750 158 EQTDVPESADWYNADYIIMWGSNvpvtrTPDAHFLTEARYN------GAKVVVVSPDYSPSAKHADLWVPIKPGTDAALA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 479 SAVTKYIIDHDLHDKAFIDEWVDDfdeyykSLETFTMAFAEEATGIPKSELIKFAEECAKAESVVICWAMGITQQDIGSD 558
Cdd:cd02750 232 LAMAHVIIKEKLYDEDYLKEYTDL------PFLVYTPAWQEAITGVPRETVIRLAREFATNGRSMIIVGAGINHWYHGDL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 559 SSTAISNLLLVTGNYRRPGTGAYPLRGhnnvqgcsdmgsmpdKITGYQSIEADDIRAKfekeygvklnpkagKDNHEMve 638
Cdd:cd02750 306 CYRALILLLALTGNEGKNGGGWAHYVG---------------QPRVLFVWRGNLFGSS--------------GKGHEY-- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 639 gihdgevhslylygedtgivdsninFVQAAFEKLDFMVVQDEFLTFTATYADVVLPASPSLEK-DGTFTNTERRIQRLYQ 717
Cdd:cd02750 355 -------------------------FEDAPEGKLDLIVDLDFRMDSTALYSDIVLPAATWYEKhDLSTTDMHPFIHPFSP 409
|
490 500
....*....|....*....|..
gi 686208005 718 ALEPLGDSKPDWKIFQAIANKL 739
Cdd:cd02750 410 AVDPLWEAKSDWEIFKALAKKV 431
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
271-742 |
3.61e-42 |
|
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. Members of the MopB_DMSOR-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239152 [Multi-domain] Cd Length: 609 Bit Score: 163.94 E-value: 3.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 271 CSFEVWTKDREILKVQPSHDspaNKIATCVKGKFSWGHINSDQRLTKPLVRK--------------NGEFHEVEWDEALN 336
Cdd:cd02751 7 GPFKAHVKDGVIVRVEPDDT---DQPRPCPRGRSVRDRVYSPDRIKYPMKRVgwlgngpgsrelrgEGEFVRISWDEALD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 337 VIADNFTSIKEKYGPDALsFISSSKATneeSYLMQKLARQVIG---------TNNVDNcsrYCQAPATKGLFRTVGHGGD 407
Cdd:cd02751 84 LVASELKRIREKYGNEAI-FGGSYGWA---SAGRLHHAQSLLHrflnliggyLGSYGT---YSTGAAQVILPHVVGSDEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 408 SG---SIED-LEKAAMSVLIGTNTAE--------AHPVIASRMKRAQKlFGQKIHVFDIRKHE-MAERADRFYQPKPGTD 474
Cdd:cd02751 157 YEqgtSWDDiAEHSDLVVLFGANPLKtrqgggggPDHGSYYYLKQAKD-AGVRFICIDPRYTDtAAVLAAEWIPIRPGTD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 475 LAWLSAVTKYIIDHDLHDKAFIDEWVDDFDEYYKSLE------TFTMAFAEEATGIPKSELIKFAEECAKaESVVICWAM 548
Cdd:cd02751 236 VALMLAMAHTLITEDLHDQAFLARYTVGFDEFKDYLLgesdgvPKTPEWAAEITGVPAETIRALAREIAS-KRTMIAQGW 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 549 GITQQDIGSDSSTAISNLLLVTGNYRRPG--TGAYPLRGHNNVQGCSDMGS--MP-------DKITGYQSIEA-DDIRAK 616
Cdd:cd02751 315 GLQRAHHGEQPAWMLVTLAAMLGQIGLPGggFGFGYGYSNGGGPPRGGAGGpgLPqgknpvkDSIPVARIADAlLNPGKE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 617 FEKEYGVKLNPKagkdnhemvegihdgeVHSLYLYGEDTGIVDSNINFVQAAFEKLDFMVVQDEFLTFTATYADVVLPAS 696
Cdd:cd02751 395 FTANGKLKTYPD----------------IKMIYWAGGNPLHHHQDLNRLIKALRKDETIVVHDIFWTASARYADIVLPAT 458
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 686208005 697 PSLEKD--GTFTNTERRIQRLY-QALEPLGDSKPDWKIFQAIANKLGFD 742
Cdd:cd02751 459 TSLERNdiGLTGNYSNRYLIAMkQAVEPLGEARSDYEIFAELAKRLGVE 507
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
261-739 |
5.38e-40 |
|
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1), found in beta- and gammaproteobacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239173 [Multi-domain] Cd Length: 414 Bit Score: 153.28 E-value: 5.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 261 KTVCTYCGVGCSFEVWTKDREILKVQPSHDSPANKIATCVKGKFSWGHINSDQRLTKPLVRKNGEFHEVEWDEALNVIAD 340
Cdd:cd02772 1 KSVSPHDALGSNLVVHVKNNKVMRVVPRENEAINECWLSDRDRFSYEGLNSEDRLTKPMIKKDGQWQEVDWETALEYVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 341 NFTSIKEKYGPDALSFISSSKATNEESYLMQKLARQViGTNNVDNcsRYCQAPatkglFRTVGHGGD----SGSIEDLEK 416
Cdd:cd02772 81 GLSAIIKKHGADQIGALASPHSTLEELYLLQKLARGL-GSDNIDH--RLRQSD-----FRDDAKASGapwlGMPIAEISE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 417 AAMSVLIGTNTAEAHPVIASRMKRAQKLFGQ--KIHVFDirkhemaeraDRFYQPKPGTDL----AWLSAVTKyiidhdl 490
Cdd:cd02772 153 LDRVLVIGSNLRKEHPLLAQRLRQAVKKGAKlsAINPAD----------DDFLFPLSGKAIvapsALANALAQ------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 491 hdkafidewvddfdeyyksletfTMAFAEEATGIPKSELIKFAEECAKAESVvicwamgitqqdigSDSSTAISNLLLVT 570
Cdd:cd02772 216 -----------------------VAKALAEEKGLAVPDEDAKVEASEEARKI--------------AASLVSAERAAVFL 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 571 GNYRRPGTGAYPLrgHNNVQGCSDM-----GSMPdkiTGYQSIEAddirakfekeYGVKLNPKAGKDNHEMVEgihDGEV 645
Cdd:cd02772 259 GNLAQNHPQAATL--RALAQEIAKLtgatlGVLG---EGANSVGA----------YLAGALPHGGLNAAAMLE---QPRK 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 646 HSLyLYGEDTGIVDSNINFVQAAFEKLDFMVVQDEFLT-FTATYADVVLPASPSLEKDGTFTNTERRIQRLYQALEPLGD 724
Cdd:cd02772 321 AYL-LLNVEPELDCANPAQALAALNQAEFVVALSAFASaALLDYADVLLPIAPFTETSGTFVNLEGRVQSFKGVVKPLGE 399
|
490
....*....|....*
gi 686208005 725 SKPDWKIFQAIANKL 739
Cdd:cd02772 400 ARPAWKVLRVLGNLL 414
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
258-807 |
1.18e-39 |
|
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin. Arsenite oxidase is a heterodimeric enzyme containing a large and a small subunit. The large catalytic subunit harbors the molybdopterin cofactor and the [3Fe-4S] cluster; and the small subunit belongs to the structural class of the Rieske proteins. The small subunit is not included in this alignment. Members of MopB_Arsenite-Ox CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239157 [Multi-domain] Cd Length: 676 Bit Score: 157.26 E-value: 1.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 258 KKTKTVCTYCGVGCSFEV--WTKDRE-------------------------------------------ILKVqPSHDSP 292
Cdd:cd02756 11 ERYNVTCHFCIVGCGYHVyvWPVGEEggpspgqnaigydlvdqvpplnlqwypktmhyvvvtqdgrevyIVIV-PDKECP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 293 ANKIATCVKG----KFSWGHINSD--QRLTKPLVRKNGEFHEVEWDEALNVIADNFTSIKEKYGPDALSFIS-----SSK 361
Cdd:cd02756 90 VNSGNYSTRGgtnaERIWSPDNRVgeTRLTTPLVRRGGQLQPTTWDDAIDLVARVIKGILDKDGNDDAVFASrfdhgGGG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 362 ATNEESYLMQKLARQVIGTNNVDNCSRYCQAPATKGLfRTVGHGGDSGSIEDLEKAAMSVLIGTNTAEAHPVI------- 434
Cdd:cd02756 170 GGFENNWGVGKFFFMALQTPFVRIHNRPAYNSEVHAT-REMGVGELNNSYEDARLADTIVLWGNNPYETQTVYflnhwlp 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 435 ---ASRMKRAQKLF--GQ-----KIHVFDIRKHE---MAERA---DRFY--QPKPGTDLAWLSAVTKYIIDHdlhdkafI 496
Cdd:cd02756 249 nlrGATVSEKQQWFppGEpvppgRIIVVDPRRTEtvhAAEAAagkDRVLhlQVNPGTDTALANAIARYIYES-------L 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 497 DEWvddfdeyyksletftMAFAEEATGIPKSELIKFAEECAKAES------VVICWAMGITQQDIGSDSSTAISNLLLVT 570
Cdd:cd02756 322 DEV---------------LAEAEQITGVPRAQIEKAADWIAKPKEggyrkrVMFEYEKGIIWGNDNYRPIYSLVNLAIIT 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 571 GNYRRPGTGAYPLRGHNnvQGCSDMGSMPDKITgYQSIEADDIRAKFEKEYG-----VKLNP-KAGKDNHEMVEGIHD-G 643
Cdd:cd02756 387 GNIGRPGTGCVRQGGHQ--EGYVRPPPPPPPWY-PQYQYAPYIDQLLISGKGkvlwvIGCDPyKTTPNAQRLRETINHrS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 644 EVHSLYLYGEDTGIVDSNINFVQAAFEKLD----FMVVQDEFLTFTATYADVVLPASPSLEKDGTFTN-TERRIqRLYQA 718
Cdd:cd02756 464 KLVTDAVEAALYAGTYDREAMVCLIGDAIQpgglFIVVQDIYPTKLAEDAHVILPAAANGEMNETSMNgHERRL-RLYEK 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 719 -LEPLGDSKPDWKIFQAIANKL------------------GFDW-----NYKHPSE--------IMDEVARLTPLYAGVS 766
Cdd:cd02756 543 fMDPPGEAMPDWWIAAMIANRIyelyqeegkggsaqyqffGFIWkteedNFMDGSQefadggefSEDYYVLGQERYEGVT 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 686208005 767 YDRLE--GFNSLQWPVQPDgTDEPIL------YLEGFNFDNGKAKLFPL 807
Cdd:cd02756 623 YNRLKavGVNGIQLPVTTD-TVTKILvtnvlrTEGVFDTEDGKAYVIDL 670
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
300-652 |
1.67e-38 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 154.43 E-value: 1.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 300 VKGKFSWG--HINSDQRLTKPLVRK--NGEFHEVEWDEALNVIADNFTSIKEkygPDALSFISSSKATNEESYLMQKLAR 375
Cdd:PRK09939 92 VQSLLTWGdhELEAAGRLTQPLKYDavSDCYKPLSWQQAFDEIGARLQSYSD---PNQVEFYTSGRTSNEAAFLYQLFAR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 376 QViGTNNVDNCSRYCQAPATKGLFRTVGHGGDSGSIEDLEKAAMSVLIGTNTAEAHPVIASRM----KRAQKL------- 444
Cdd:PRK09939 169 EY-GSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLralvKRGAKMiainplq 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 445 ------FGQKIHVFDIRKHEMAERADRFYQPKPGTDLAWLSAVTKYIIDHD----------LHDKAFIDEWVDDFDEYYK 508
Cdd:PRK09939 248 erglerFTAPQNPFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDdaasaagrpsLLDDEFIQTHTVGFDELRR 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 509 SLETFTMAFAEEATGIPKSELIKFAEECAKAESVVICWAMGITQQDIGSDSSTAISNLLLVTGNYRRPGTGAYPLRGHNN 588
Cdd:PRK09939 328 DVLNSEWKDIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSN 407
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 686208005 589 VQGcsdmgsmpDKITGYQSIEADDIRAKFEKEYGVKLNPKAGKDNHEMVEGIHDGEVHSLYLYG 652
Cdd:PRK09939 408 VQG--------DRTVGITEKPSAEFLARLGERYGFTPPHAPGHAAIASMQAICTGQARALICMG 463
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
819-937 |
4.52e-38 |
|
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and other related proteins. Formate dehydrogenase H is a component of the anaerobic formate hydrogen lyase complex and catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. Formate dehydrogenase N (alpha subunit) is the major electron donor to the bacterial nitrate respiratory chain and nitrate reductases, Nap and Nas, catalyze the reduction of nitrate to nitrite. This CD (MopB_CT_Fdh-Nap-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 238282 [Multi-domain] Cd Length: 120 Bit Score: 138.02 E-value: 4.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 819 YDIHVNNGRLLEHFHEGNMTYQTPMIKYKVPRAFVEISPELAEDRGIHEGAEVKLISETGEAVLQVHVTDRVKGKEIYIP 898
Cdd:cd00508 3 YPLVLTTGRLLEHWHTGTMTRRSPRLAALAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRPGTVFMP 82
|
90 100 110
....*....|....*....|....*....|....*....
gi 686208005 899 LNNDAMENGdlGAINLLTNSDVDQYTDTPSYKRTSCRLE 937
Cdd:cd00508 83 FHWGGEVSG--GAANALTNDALDPVSGQPEFKACAVRIE 119
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
261-805 |
8.00e-36 |
|
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239166 [Multi-domain] Cd Length: 567 Bit Score: 144.16 E-value: 8.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 261 KTVCT-YCGVGCSFEVWTKDREILKVQPShDSPA---NKIatCVKGKFSWGHINSDQRLTKPLVR----KNGEFHEVEWD 332
Cdd:cd02765 1 YTACPpNCGGRCPLKCHVRDGKIVKVEPN-EWPDktyKRG--CTRGLSHLQRVYSPDRLKYPMKRvgerGEGKFERITWD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 333 EALNVIADNFTSIKEKYGPDALSFISSSKATNEESYLMQKL---ARQVIGTNNVDNCSRYCQAPATKGLFRTVGHggdsg 409
Cdd:cd02765 78 EALDTIADKLTEAKREYGGKSILWMSSSGDGAILSYLRLALlggGLQDALTYGIDTGVGQGFNRVTGGGFMPPTN----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 410 SIEDLEKAAMSVLIGTNTAEAHPVIASRMKRAQKLfGQKIHVFDIRKHEMAERADRFYQPKPGTDLAWLSAVTKYIIDHD 489
Cdd:cd02765 153 EITDWVNAKTIIIWGSNILETQFQDAEFFLDAREN-GAKIVVIDPVYSTTAAKADQWVPIRPGTDPALALGMINYILEHN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 490 LHDKAFIDEW------VDDFDEYYKSLETFTMAFAEE----------------ATGIP--------------KSELIKFA 533
Cdd:cd02765 232 WYDEAFLKSNtsapflVREDNGTLLRQADVTATPAEDgyvvwdtnsdspepvaATNINpalegeytingvkvHTVLTALR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 534 EECAK---AESVVICwamGITQQDIgsdssTAISNLLLvtgnyRRPGTGAYPLRGhnnvqgcsdmgsmPDKI----TGYQ 606
Cdd:cd02765 312 EQAASyppKAAAEIC---GLEEAII-----ETLAEWYA-----TGKPSGIWGFGG-------------VDRYyhshVFGR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 607 SIEaddIRAKFEKEYGVklnpkagkdnhemVEGIHdGEVHSLYLYGEDTGIVDSNINFVQAAFEKLDFMVVQDEFLTFTA 686
Cdd:cd02765 366 TAA---ILAALTGNIGR-------------VGGGV-GQIKFMYFMGSNFLGNQPDRDRWLKVMKNLDFIVVVDIFHTPTV 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 687 TYADVVLPASPSLEKDGTFTNTERRIQRLYQ--ALEPLGDSKPDWKIFQAIANKLGFD--WNyKHPSEIMDevARLT--- 759
Cdd:cd02765 429 RYADIVLPAAHWFEVEDLLVRYTTHPHVLLQqkAIEPLFESKSDFEIEKGLAERLGLGdyFP-KTPEDYVR--AFMNsdd 505
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 686208005 760 PLYAGVSYDRLEGFNSLqwpVQPDGTDEPILYLEG--FNFDNGKAKLF 805
Cdd:cd02765 506 PALDGITWEALKEEGII---MRLATPEDPYVAYLDqkFGTPSGKLEFY 550
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
261-756 |
3.48e-32 |
|
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other related proteins. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239158 [Multi-domain] Cd Length: 523 Bit Score: 132.56 E-value: 3.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 261 KTVCTYCGVGCSFEVWTKDREILKVQPSHDSPANKIATCVKGKFSWGHINSDQRLTKPLVRKN--------GEFHEVEWD 332
Cdd:cd02757 3 PSTCQGCTAWCGLQAYVEDGRVTKVEGNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRTNprkgrdvdPKFVPISWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 333 EALNVIADNFTSIKEKYGPDALSfISSSKATNEESYLMQKLARqVIGTNNVDNCSRYCQAPATKGLFRTVGhGGDSGSIe 412
Cdd:cd02757 83 EALDTIADKIRALRKENEPHKIM-LHRGRYGHNNSILYGRFTK-MIGSPNNISHSSVCAESEKFGRYYTEG-GWDYNSY- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 413 DLEKAAMSVLIGTNTAEA-HPVIASRMKRAQKLFGQKIHVFDIRKHEMAERADRFYQPKPGTDLAWLSAVTKYIIDHDLH 491
Cdd:cd02757 159 DYANAKYILFFGADPLESnRQNPHAQRIWGGKMDQAKVVVVDPRLSNTAAKADEWLPIKPGEDGALALAIAHVILTEGLW 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 492 DKAFIDEWVD--------------DFDEyyKSLETF-----------TMAFAEEATGIPKSELIKFAEECAKAESVVICW 546
Cdd:cd02757 239 DKDFVGDFVDgknyfkagetvdeeSFKE--KSTEGLvkwwnlelkdyTPEWAAKISGIPAETIERVAREFATAAPAAAAF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 547 AM-GITQQDIGSDSSTAISNLLLVTGNYRRPGtgayplrghnnvqGCSDMGSMPdkitgyqsieadDIRAKFEKEYgvkl 625
Cdd:cd02757 317 TWrGATMQNRGSYNSMACHALNGLVGSIDSKG-------------GLCPNMGVP------------KIKVYFTYLD---- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 626 NPK-AGKDNHEMVEgihdgevhslylygedtgivdsninfvqaAFEKLDFMVVQDEFLTFTATYADVVLPASPSLEKDG- 703
Cdd:cd02757 368 NPVfSNPDGMSWEE-----------------------------ALAKIPFHVHLSPFMSETTYFADIVLPDGHHFERWDv 418
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 686208005 704 --TFTNTERRIQRLYQALEPLGDSKPDWKIFQAIANKL---GFD-------WNYKHPSEIMDEVA 756
Cdd:cd02757 419 msQENNLHPWLSIRQPVVKSLGEVREETEILIELAKKLdpkGSDgmkryapGQFKDPETGKNNRW 483
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
632-760 |
5.45e-32 |
|
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440657 [Multi-domain] Cd Length: 453 Bit Score: 130.73 E-value: 5.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 632 DNHEMVEGIHDGEVHSLYLYGEDtgIVDSNINFVQAAFEKLDFMVVQDEFLTFTATYADVVLPASPSLEKDGTFTNTERR 711
Cdd:COG1034 320 DAAAILEAAEAGKLKALVLLGAD--PYDLDPAAALAALAKADFVVVLDHFGSATAERADVVLPAAAFAEKSGTFVNLEGR 397
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 686208005 712 IQRLYQALEPLGDSKPDWKIFQAIANKLGFDWNYKHPSEIMDEVARLTP 760
Cdd:COG1034 398 VQRFNAAVPPPGEARPDWRVLRALANALGAGLPYDSLEEVRAELAAEAP 446
|
|
| PRK07569 |
PRK07569 |
bidirectional hydrogenase complex protein HoxU; Validated |
6-207 |
9.71e-31 |
|
bidirectional hydrogenase complex protein HoxU; Validated
Pssm-ID: 181037 [Multi-domain] Cd Length: 234 Bit Score: 121.30 E-value: 9.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 6 VVTL--DGKDYLVEPGTNLLEFIKSQDTFVPSICYNESMGPIQTCDTCTVEIDG--KIERSCSTVIDRPMTVNTVNNDVK 81
Cdd:PRK07569 3 VKTLtiDDQLVSAREGETLLEAAREAGIPIPTLCHLDGLSDVGACRLCLVEIEGsnKLLPACVTPVAEGMVVQTNTPRLQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 82 DAQKEALDRILEKHMLYCTVCdYNNGDCEIHNTMDAWGLQHQTYEYKEKPYEKDYG-PFYRYDPNQCILCGRCVEACQDI 160
Cdd:PRK07569 83 EYRRMIVELLFAEGNHVCAVC-VANGNCELQDLAIEVGMDHVRFPYLFPRRPVDIShPRFGIDHNRCVLCTRCVRVCDEI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 686208005 161 EVNETiridWD---R-EHPRVIWDNDVPINES-SCVSCGQCATVCPCNAMME 207
Cdd:PRK07569 162 EGAHT----WDvagRgAKSRVITDLNQPWGTSeTCTSCGKCVQACPTGAIFR 209
|
|
| FeFe_hydrog_A6 |
NF040763 |
NADH-dependent [FeFe] hydrogenase, group A6; |
7-209 |
6.98e-30 |
|
NADH-dependent [FeFe] hydrogenase, group A6;
Pssm-ID: 468723 [Multi-domain] Cd Length: 571 Bit Score: 126.06 E-value: 6.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 7 VTLDGKDYLVEPGTNLLEFIKSQDTFVPSICYNESMGPIQTCDTCTVEIDG--KIERSCSTVIDRPMTVNTVNNDVKDAQ 84
Cdd:NF040763 3 LTINGKEVEVPEGTTILEAAKKAGIKIPTLCYLKDINEIGACRVCVVEVEGarNLVAACATPVAEGMVVKTNTPRVREAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 85 KEALDRILEKHMLYCTVCDyNNGDCEIHNTMDAWGLQHQTYEYKEK--PYEKDY-GPFYRYDPNQCILCGRCVEACQDIE 161
Cdd:NF040763 83 KTVLELILSNHPQDCLTCV-RNGNCELQKLAAELGIREIRYEGGEEksYYIDDTsSPSIVRDPNKCILCRRCVTVCNEVQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 686208005 162 -VNetiridwdrehprVI-WDN-----------DVPINESSCVSCGQCATVCPCNAMMEVN 209
Cdd:NF040763 162 gVG-------------ALgAVNrgfktvvgpafGKPLADTACTNCGQCIAVCPTGALTEKD 209
|
|
| PRK08493 |
PRK08493 |
NADH-quinone oxidoreductase subunit G; |
7-898 |
1.47e-26 |
|
NADH-quinone oxidoreductase subunit G;
Pssm-ID: 236277 [Multi-domain] Cd Length: 819 Bit Score: 117.11 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 7 VTLDGKDYLVEPGTNLLEFIKSQDTFVPSICYNESMGPIQTCDTCTVEIDGKIERSCSTVIDRPMTVNTVNNDVKDAQKE 86
Cdd:PRK08493 4 ITINGKECEAQEGEYILNVARRNGIFIPAICYLSGCSPTLACRLCMVEADGKRVYSCNTKAKEGMNILTNTPNLMDERNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 87 ALDRILEKHMLYCTVCDyNNGDCEIHNTMDAWGLQHQTYEYKE--KPYeKDYGpFYRYDPNQCILCGRCVEACQDI---- 160
Cdd:PRK08493 84 IMQTYDVNHPLECGVCD-KSGECELQNFTHEMGVNHQPYAIKDthKPH-KHWG-KINYDPSLCIVCERCVTVCKDKiges 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 161 --------------EVNETIRID----WDREHPRVIwdndVPIN--ESSCVSCGQCATVCPCNAmmevnmegnagymtdt 220
Cdd:PRK08493 161 alktvprgldapdkSFKESMPKDayavWSKKQKSLI----GPVGgeTLDCSFCGECIAVCPVGA---------------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 221 epgslaamidLTKKAepgygplFAISDSEAEMrkeriKKTKTVCTYCGVGCSFEVWTKDREILkvqpshdSPANKIATcV 300
Cdd:PRK08493 221 ----------LSSSD-------FQYTSNAWEL-----KKIPATCPHCSDCCLIYYDVKHSSIL-------NQESKIYR-V 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 301 KGKFSWGHINsdqrltkplvrKNGEF-----HEVEWDE-ALNVIADNFTSIkekygpDALSFisSSKATNEESYLMQKLa 374
Cdd:PRK08493 271 SNDFYFNPLC-----------GAGRFafdfqNEADKDEkAFKEAVEAFKEA------KAIKF--NSFITNEEALILQRL- 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 375 RQVIGTNNVDNCSRYCQAPATkgLFRTVGHGGDSGSIEDLEKAAMSVLIGTNTAEAHPVIASRMKRAQKLFGQKIHVFdi 454
Cdd:PRK08493 331 KKKFGLKLINEEALKFQQFLK--VFSEVSGKSYSANLEDIKTSDFVVVAGSALKTDNPLLRYAINNALKMNKASGLYF-- 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 455 rkHEMAERADRFYQP-------KPGTDLAWLsavtkYIIDHDLHDKAFIDewvddfdeyyKSLETFTMAFAEEATGIPKS 527
Cdd:PRK08493 407 --HPIKDNVIANLSKnffcithEVGAEEIIL-----YFLLKKFLEEEAIL----------KSLEEFKQSIVKEAALSILE 469
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 528 ELIKFAEECAKAESVVICWAMGITQQDIGSDSSTAISNLLLVTGnyrrpgtgayplrghNNVQGCSDMGSMPDKITGYQS 607
Cdd:PRK08493 470 EIREKVLEQAEQGCENQEEVKKEVPKKVKKIPEVDTYLLLEELG---------------INEETYEKLEALLAKKNNFTL 534
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 608 IEADDI----RAK--------FEK--EYGVKLNPKagKDNHEMVEGIHDGEvhslylygedtgiVDSNINFVQAAFEKLD 673
Cdd:PRK08493 535 VVGEDLyahkNAKnlakllglIQKytAFKVILIPP--STNTLGVALICDLS-------------EEIEGGKTVGYNEKGD 599
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 674 FMVVQDEFltftatyADVVLPASPSLEkdGTFTNTERRIQRLYQALEPLGDSKPDwkifqaIANKLGFDwnykhpseiMD 753
Cdd:PRK08493 600 FTISSLEK-------GDLALPALNQQE--GTFTNIDKRVVPTNAALPFEGYDLND------IANALGFD---------EE 655
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 754 EVARLTPL------YAGVSYDRLEGFNSlqwpvqPDGTDEPILYLEGFNFD-NGKAKLF---PLSFDNYFKQDEIYDIHV 823
Cdd:PRK08493 656 YTIDYTKKlptekgFKAIEFDDLENYYT------NDGSNHRGYELETSSFEkSAKEETIecePIKPLKEKIGINIYLANP 729
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 686208005 824 NNgrlleHFHE-GNMTYQTPMikykvpRAFVEISPELAEDRGIHEGAEVKLISETGEAVLQVHVTDRVKGkEIYIP 898
Cdd:PRK08493 730 IT-----QFNNfTNKAENLNE------KAGLYVSEAFLKKLNLKDGDNVTLKKEEEELTGSVYLDESLKG-GAYLP 793
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
262-916 |
2.83e-26 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 116.28 E-value: 2.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 262 TVCTY-CGVGCSFEVWTKDREILKVQPSHDSPAN-----KIATCVKGKFSWGHINSDQRLTKPL----VRKNGEFHEVEW 331
Cdd:PRK14990 61 SACTVnCGSRCPLRMHVVDGEIKYVETDNTGDDNydglhQVRACLRGRSMRRRVYNPDRLKYPMkrvgARGEGKFERISW 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 332 DEALNVIADNFTSIKEKYGPDALSF---ISSSKATNEESY-----LMQKLARQVIGTNNvdNCSRYCQAPATKGLFRTVG 403
Cdd:PRK14990 141 EEAYDIIATNMQRLIKEYGNESIYLnygTGTLGGTMTRSWppgntLVARLMNCCGGYLN--HYGDYSSAQIAEGLNYTYG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 404 HGGDSGSIEDLEKAAMSVLIGTNTAEAHPV---IASRMKRAQKLFGQKIHVFDIRKHEM-AERADRFYQPKPGTDLAWLS 479
Cdd:PRK14990 219 GWADGNSPSDIENSKLVVLFGNNPGETRMSgggVTYYLEQARQKSNARMIIIDPRYTDTgAGREDEWIPIRPGTDAALVN 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 480 AVTKYIIDHDLHDKAFIDEWVDDFDE-----------YYKSL--------ETFTMAFAEEATGIPKSELIKFAEECAKAE 540
Cdd:PRK14990 299 GLAYVMITENLVDQPFLDKYCVGYDEktlpasapkngHYKAYilgegpdgVAKTPEWASQITGVPADKIIKLAREIGSTK 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 541 SVVICWAMGITQQDIGSDSSTAISNLLLVTGNY--------RRPGTGAYPLRG----HNNVQGCSDMGSMPDKITGYQSI 608
Cdd:PRK14990 379 PAFISQGWGPQRHANGEIATRAISMLAILTGNVginggnsgAREGSYSLPFVRmptlENPIQTSISMFMWTDAIERGPEM 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 609 EA--DDIRAKFEKEYGVKLN-PKAGK---DNHEMVEGIHDgevhslyLYGEDtgivdsninfvqaafEKLDFMVVQDEFL 682
Cdd:PRK14990 459 TAlrDGVRGKDKLDVPIKMIwNYAGNcliNQHSEINRTHE-------ILQDD---------------KKCELIVVIDCHM 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 683 TFTATYADVVLPASPSLEK-----DGTFTNTERRIQRlYQALEPLGDSKPDWKIFQAIANKLGFDWNY----------KH 747
Cdd:PRK14990 517 TSSAKYADILLPDCTASEQmdfalDASCGNMSYVIFN-DQVIKPRFECKTIYEMTSELAKRLGVEQQFtegrtqeewmRH 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 748 PSEIMDEVARLTPLYAG----------------VSYD----------------RLEGFN------SLQWPVQPDGTDEPI 789
Cdd:PRK14990 596 LYAQSREAIPELPTFEEfrkqgifkkrdpqghhVAYKafredpqanplttpsgKIEIYSqaladiAATWELPEGDVIDPL 675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 790 -LYLEGF-NFDNGKAKLFPLSFDNYFKQDEIYDihvnngrllehfhegnmTYQTPMIKYKVPRAFVEISPELAEDRGIHE 867
Cdd:PRK14990 676 pIYTPGFeSYQDPLNKQYPLQLTGFHYKSRVHS-----------------TYGNVDVLKAACRQEMWINPLDAQKRGINN 738
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 686208005 868 GAEVKLISETGEAVLQVHVTDRVKGKEIYIP----LNNDAMENGDLGAINLLT 916
Cdd:PRK14990 739 GDKVRIFNDRGEVHIEAKVTPRMMPGVVALGegawYDPDAKRVDKGGCINVLT 791
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
273-742 |
8.69e-26 |
|
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239170 [Multi-domain] Cd Length: 609 Bit Score: 113.51 E-value: 8.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 273 FEVWTKDREILKVQPSHDSPA-NKIATCVKGkfswgHINSDQRLTKPLVRK---------------NGEFHEVEWDEALN 336
Cdd:cd02769 9 FRARVKDGRIVGVRPFEEDPDpSPLLDGVPD-----AVYSPTRIKYPMVRRgwlekgpgsdrslrgKEEFVRVSWDEALD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 337 VIADNFTSIKEKYGPDALsFISSSKATNeesylmqklarqvigtnnvdnCSRYcqAPATKGLFRTVG-HGGDSGSIEDLE 415
Cdd:cd02769 84 LVAAELKRVRKTYGNEAI-FGGSYGWSS---------------------AGRF--HHAQSLLHRFLNlAGGYVGSVGDYS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 416 KAA-----------MSVLIGTNTAeaHPVIAS-----------RMKRAQ-KLFGQKIHVFDIRKHEMAERADRFY----- 467
Cdd:cd02769 140 TGAaqvilphvvgsMEVYTEQQTS--WPVIAEhtelvvafgadPLKNAQiAWGGIPDHQAYSYLKALKDRGIRFIsispl 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 468 -------------QPKPGTDLAWLSAVTKYIIDHDLHDKAFIDEWVDDFDEYYKSL--ET----FTMAFAEEATGIPKSE 528
Cdd:cd02769 218 rddtaaelgaewiAIRPGTDVALMLALAHTLVTEGLHDKAFLARYTVGFDKFLPYLlgESdgvpKTPEWAAAICGIPAET 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 529 LIKFAEECAKAESVVICwAMGITQQDIGSDSSTAISNLLLVTGNYRRPGTG-AYPLRGHNNVQGCSDMGSMPDKITGYQS 607
Cdd:cd02769 298 IRELARRFASKRTMIMA-GWSLQRAHHGEQPHWMAVTLAAMLGQIGLPGGGfGFGYHYSNGGGPPRGAAPPPALPQGRNP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 608 IE--------ADDIrakfekeygvkLNPKAGKDnhemvegiHDGE------VHSLYLYGEDTGIVDSNINFVQAAFEKLD 673
Cdd:cd02769 377 VSsfipvariADML-----------LNPGKPFD--------YNGKkltypdIKLVYWAGGNPFHHHQDLNRLIRAWQKPE 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 674 FMVVQDEFLTFTATYADVVLPASPSLEK-DGTFTNTERRIQRLYQALEPLGDSKPDWKIFQAIANKLGFD 742
Cdd:cd02769 438 TVIVHEPFWTATARHADIVLPATTSLERnDIGGSGDNRYIVAMKQVVEPVGEARDDYDIFADLAERLGVE 507
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
3-911 |
1.75e-24 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 110.42 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 3 EHLVVTLDGKDYLVEPGTNLL---EFIKSQdtfVPSICYNESMGPIQTCDTCTVEIDG--KIERSCSTVIDRPMTVNT-V 76
Cdd:PRK07860 3 DLVTLTIDGVEVSVPKGTLVIraaELLGIQ---IPRFCDHPLLDPVGACRQCLVEVEGqrKPQASCTTTVTDGMVVKTqL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 77 NNDVKD-AQKEALDRILEKHMLYCTVCDyNNGDCEIHNTMDAWGLQHQTYEYKEKPYEKdygPF-----YRYDPNQCILC 150
Cdd:PRK07860 80 TSPVADkAQHGVMELLLINHPLDCPVCD-KGGECPLQNQAMSNGRAESRFTDVKRTFPK---PInistqVLLDRERCVLC 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 151 GRCVEACQDIEVNETIRIDWDREHPRV-IWDNDvPINesSCVScGQCATVCPCNAMMevnmegNAGYMTDTEPgslaamI 229
Cdd:PRK07860 156 ARCTRFSDQIAGDPFIDLQERGALQQVgIYEGE-PFQ--SYFS-GNTVQICPVGALT------GAAYRFRARP------F 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 230 DLtkkaepgygplfaISdseaemrkerikkTKTVCTYCGVGCSFEVwtkDREILKVQP--SHDSPA-NKIATCVKGKFSW 306
Cdd:PRK07860 220 DL-------------VS-------------TPSVCEHCASGCAQRT---DHRRGKVLRrlAGDDPEvNEEWNCDKGRWAF 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 307 GHINSDQRLTKPLVR-KNGEFHEVEWDEALNVIADNFTSIKEKYGpdalsFISSSKATNEESYLMQKLARQVIGTNNVDN 385
Cdd:PRK07860 271 TYATQPDRITTPLVRdEDGELEPASWSEALAVAARGLAAARGRVG-----VLVGGRLTVEDAYAYAKFARVALGTNDIDF 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 386 CSRYCQAPATKGLFRTVGHGGDSGSIEDLEKAAMSVLIGTNTAEAHPVIASRMKRAQKLFGQKihVFDIRKHemAER--- 462
Cdd:PRK07860 346 RARPHSAEEADFLAARVAGRGLGVTYADLEKAPAVLLVGFEPEEESPIVFLRLRKAARKHGLK--VYSIAPF--ATRgle 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 463 --ADRFYQPKPGTDLAWLSAVTKYIIDHDlhdkafidewvddfdeyyksletftmafaeEATGIPKSeLIKFAEECAKAE 540
Cdd:PRK07860 422 kmGGTLLRTAPGGEAAALDALATGAPDVA------------------------------ELLRTPGA-VILVGERLATVP 470
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 541 SVVicwamgitqqdigsdssTAISNLLLVTGNY-----RRPGTgayplrghnnvQGCSDMGSMPDKITGYQSIEADDIRA 615
Cdd:PRK07860 471 GAL-----------------SAAARLADATGARlawvpRRAGE-----------RGALEAGALPTLLPGGRPVADPAARA 522
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 616 KFEKEYGV-KLNPKAGKDNHEMVEGIHDGEVHSLYLYG---EDTgivdSNINFVQAAFEKLDFmVVQDEfLTFTA--TYA 689
Cdd:PRK07860 523 EVAAAWGVdELPAAPGRDTAGILAAAAAGELGALLVGGvepADL----PDPAAALAALDAAGF-VVSLE-LRHSAvtERA 596
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 690 DVVLPASPSLEKDGTFTNTERRIQRLYQALEPLGdSKPDWKIFQAIANKLGFDWNYKHPSEIMDEVARLtPLYAGvsyDR 769
Cdd:PRK07860 597 DVVLPVAPVAEKAGTFLNWEGRLRPFEAALRTTG-ALSDLRVLDALADEMGVDLGLPTVAAARAELARL-GAWDG---AR 671
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 770 LEGFNSLQWPVQPDGTDEPILylegfnfdngkaklfplsfdnyfkqdEIYDIHVNNGRLLehfhEGNmtyqtPMIKYKVP 849
Cdd:PRK07860 672 AAAPAVPAAAPPQPGAGEAVL--------------------------ATWRMLLDDGRLQ----DGE-----PHLAGTAR 716
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 686208005 850 RAFVEISPELAEDRGIHEGAEVKLISETGEAVLQVHVT---DRVkgkeIYIPLNNDAME-NGDLGA 911
Cdd:PRK07860 717 PPVARLSAATAAEIGVADGDAVTVSTERGSITLPLAITdmpDRV----VWLPLNSPGSTvRRTLGA 778
|
|
| FwdB |
COG1029 |
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion]; |
263-605 |
7.09e-23 |
|
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion];
Pssm-ID: 440652 [Multi-domain] Cd Length: 428 Bit Score: 102.62 E-value: 7.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 263 VCTYCGVGC-SFEVWTKDREILKVQPShdspankiatCVKG--KFSwgHINSDQRLTKPLVRkngeFHEVEWDEALNVIA 339
Cdd:COG1029 9 VCPFCGCLCdDLEVEVEGGKIVVVKNA----------CAIGaaKFE--RAVSDHRITSPRIR----GKEVSLEEAIDKAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 340 DNFTSIKEkygpdALSFISSSKATNEESYLMqKLARQVIGTnnVDNCSRYCQAPATKGLFRtVGH-GGDSGSIEDleKAA 418
Cdd:COG1029 73 EILANAKR-----PLIYGLSSTDCEAMRAGL-ALAERVGAV--VDNTASVCHGPSLLALQD-VGWpTCTLGEVKN--RAD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 419 MSVLIGTNTAEAHPVIASR-------MKRAQKLFGQKIHVFDIRKHEMAERADRFYQPKPGTDLAWLSAVTKYIIDHDLH 491
Cdd:COG1029 142 VIIYWGCNPVHAHPRHMSRysvfprgFFTPKGRKDRTVIVVDPRPTDTAKVADLHLQVKPGRDYEVLSALRALVRGKELS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 492 dkafidewvddfdeyyksletftmafAEEATGIPKSELIKFAEECAKAESVVICWAMGITQQDIGSDSSTAISNLLLVTG 571
Cdd:COG1029 222 --------------------------PEEVAGIPVEDLEELAERLKNAKYGVIFWGMGLTQSPGKHLNVDAAIELVRDLN 275
|
330 340 350
....*....|....*....|....*....|....
gi 686208005 572 NYRRpgTGAYPLRGHNNVQGcsdMGSMPDKITGY 605
Cdd:COG1029 276 RYTK--FSILPLRGHYNVAG---ANQVASWQTGY 304
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
819-937 |
1.03e-22 |
|
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. This CD (MopB_CT_Nitrate-R-Nap) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
Pssm-ID: 239192 [Multi-domain] Cd Length: 122 Bit Score: 94.18 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 819 YDIHVNNGRLLEHFHEGNMTYQTPMIKYKVPRAFVEISPELAEDRGIHEGAEVKLISETGEAVLQVHVTDRVKGKEIYIP 898
Cdd:cd02791 3 YPLWLNTGRVRDQWHTMTRTGRVPRLNAHVPEPYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPGEVFVP 82
|
90 100 110
....*....|....*....|....*....|....*....
gi 686208005 899 LnNDAMENGDLGAINLLTNSDVDQYTDTPSYKRTSCRLE 937
Cdd:cd02791 83 M-HWGDQFGRSGRVNALTLDATDPVSGQPEFKHCAVRIE 120
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
261-740 |
2.82e-22 |
|
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239164 [Multi-domain] Cd Length: 679 Bit Score: 102.99 E-value: 2.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 261 KTVCTYCGVGCSFEVWTKDREILKVQPSHDSPANKIATCVKGKFSWGHINSDQRLTKPLVRK----NGEFHEVEWDEALN 336
Cdd:cd02763 1 TTTCYMCACRCGIRVHLRDGKVRYIKGNPDHPLNKGVICAKGSSGIMKQYSPARLTKPLLRKgprgSGQFEEIEWEEAFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 337 VIADNFTSIKEKyGPDALSFISSSKAtneesylMQKL----ARQvIGTNNVDNCSRYCQAPATKGLFRTVGHGGDSGSIE 412
Cdd:cd02763 81 IATKRLKAARAT-DPKKFAFFTGRDQ-------MQALtgwfAGQ-FGTPNYAAHGGFCSVNMAAGGLYSIGGSFWEFGGP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 413 DLEKAAMSVLIGtnTAEAHPviASRMKRAQKLF----GQKIHVFDIRKhEMAERADRFYQPKPGTDLAWLSAVTKYIIDH 488
Cdd:cd02763 152 DLEHTKYFMMIG--VAEDHH--SNPFKIGIQKLkrrgGKFVAVNPVRT-GYAAIADEWVPIKPGTDGAFILALAHELLKA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 489 DLHDKAFIDEWVDdfdeyYKSLETFTMAFAEEATGIPKSELIKFAEECA-----KAESVVICW----------------- 546
Cdd:cd02763 227 GLIDWEFLKRYTN-----AAELVDYTPEWVEKITGIPADTIRRIAKELGvtardQPIELPIAWtdvwgrkhekitgrpvs 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 547 --AM-GITQQDIGSDSSTAISNLLLVTGNYRRPG----TGAYPlrghNNVQGCSDMGSMPDKITGYQ------------- 606
Cdd:cd02763 302 fhAMrGIAAHSNGFQTIRALFVLMMLLGTIDRPGgfrhKPPYP----RHIPPLPKPPKIPSADKPFTplygpplgwpasp 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 607 ---SIEADDIRAKFEKEYGVKLNPKAGKDNHEMVEGIHDGE---VHSLYLYGEDTGIVDS-NINFVQAAFE--------K 671
Cdd:cd02763 378 ddlLVDEDGNPLRIDKAYSWEYPLAAHGCMQNVITNAWRGDpypIDTLMIYMANMAWNSSmNTPEVREMLTdkdasgnyK 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 686208005 672 LDFMVVQDEFLTFTATYADVVLPASPSLEKDGTFTNTERRIQRL--------YQALEPLGDSKPDWKIFQAIANKLG 740
Cdd:cd02763 458 IPFIIVCDAFYSEMVAFADLVLPDTTYLERHDAMSLLDRPISEAdgpvdairVPIVEPKGDVKPFQEVLIELGTRLG 534
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
268-736 |
8.63e-22 |
|
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone oxidoreductase/respiratory complex I/NADH dehydrogenase-1(NDH-1) of eukaryotes and the Nqo3/G subunit of alphaproteobacteria NDH-1. The NADH-quinone oxidoreductase is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The nad11 gene codes for the largest (75 kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Paracoccus denitrificans, this subunit is encoded by the nqo3 gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The Nad11/Nqo3 subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239174 [Multi-domain] Cd Length: 375 Bit Score: 98.49 E-value: 8.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 268 GVGCSFEVWTKDREILKVQPSHDSPANK--IATcvKGKFSWGHINSdQRLTKPLVRKNGEFHEVEWDEALNVIADNFTSI 345
Cdd:cd02773 8 AVGSNIRVDTRGGEVMRILPRLNEDINEewISD--KTRFAYDGLKR-QRLDKPYIRKNGKLKPATWEEALAAIAKALKGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 346 KekygPDALSFISSSKATNEESY----LMQKL------ARQVIGTNNVDNCSRYcqapatkgLFRTvghggdsgSIEDLE 415
Cdd:cd02773 85 K----PDEIAAIAGDLADVESMValkdLLNKLgsenlaCEQDGPDLPADLRSNY--------LFNT--------TIAGIE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 416 KAAMSVLIGTNTAEAHPVIASRMKRAQKLFGQKIHVFDirkhemaeradrfyqpkPGTDLAwlsavtkYIIDHDLHDKAF 495
Cdd:cd02773 145 EADAVLLVGTNPRFEAPVLNARIRKAWLHGGLKVGVIG-----------------PPVDLT-------YDYDHLGTDAKT 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 496 IDEWVDDFDEYYKSLetftmafaeeatgipkselikfaeECAKAESVVIcwAMGITQQDIGSDSSTAISNLLLVTGNYRR 575
Cdd:cd02773 201 LQDIASGKHPFSKAL------------------------KDAKKPMIIV--GSGALARKDGAAILAAVAKLAKKNGVVRE 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 576 PGTGAYPLRGHNNVQGCSDMGsmpdkitgyqsieaddirakfekeygvkLNPKAGkdnhemvEGIHDGEVHSLYLYGEDT 655
Cdd:cd02773 255 GWNGFNVLHRAASRVGALDLG----------------------------FVPGAG-------AIRKSGPPKVLYLLGADE 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 656 GIVDsninfvqaAFEKLDFMVVQDEFLTFTATYADVVLPASPSLEKDGTFTNTERRIQRLYQALEPLGDSKPDWKIFQAI 735
Cdd:cd02773 300 IDIT--------PIPKDAFVVYQGHHGDRGAQIADVILPGAAYTEKSGTYVNTEGRVQQTRKAVSPPGDAREDWKILRAL 371
|
.
gi 686208005 736 A 736
Cdd:cd02773 372 S 372
|
|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
257-311 |
6.36e-21 |
|
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for which the structure is known. This first domain (residues 1 to 60) of PDB:1aa6 is an Fe4S4 cluster just below the protein surface.
Pssm-ID: 428168 [Multi-domain] Cd Length: 55 Bit Score: 86.96 E-value: 6.36e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 686208005 257 IKKTKTVCTYCGVGCSFEVWTKDREILKVQPSHDSPANKIATCVKGKFSWGHINS 311
Cdd:pfam04879 1 MKVVKTICPYCGVGCGLEVHVKDGKIVKVEGDPDHPVNEGRLCVKGRFGYERVYN 55
|
|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
263-739 |
7.66e-21 |
|
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, subunit B (FmdB/FwdB), and other related proteins. Formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and some eubacteria. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239162 [Multi-domain] Cd Length: 415 Bit Score: 96.25 E-value: 7.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 263 VCTYCGVGCS-FEVWTKDREILKVQPShdspankiatCVKGKFSWGHINsdQRLTKPLVRKngefHEVEWDEALNVIADN 341
Cdd:cd02761 3 VCPFCGLLCDdIEVEVEDNKITKVRNA----------CRIGAAKFARYE--RRITTPRIDG----KPVSLEEAIEKAAEI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 342 FTSIKEkygpdALSFISSSKATNEESYLMQkLARQVIGTnnVDNCSRYCQAPATKGLFrtvghggDSGSI-----EDLEK 416
Cdd:cd02761 67 LKEAKR-----PLFYGLGTTVCEAQRAGIE-LAEKLGAI--IDHAASVCHGPNLLALQ-------DSGWPtttlgEVKNR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 417 AAMSVLIGTNTAEAHPVIASR-------MKRAQKLFGQKIHVFDIRKHEMAERADRFYQPKPGTDLAWLSAVTKYIIDHD 489
Cdd:cd02761 132 ADVIVYWGTNPMHAHPRHMSRysvfprgFFREGGREDRTLIVVDPRKSDTAKLADIHLQIDPGSDYELLAALRALLRGAG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 490 LHdkafidewvddfdeyyksletftmafAEEATGIPKSELIKFAEECAKAESVVICWAMGITQQDIGSDSSTAISNLLLV 569
Cdd:cd02761 212 LV--------------------------PDEVAGIPAETILELAERLKNAKFGVIFWGLGLLPSRGAHRNIEAAIRLVKA 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 570 TGNYRRPGTGayPLRGHNNVQGCSDMGSmpdKITGYQsieaddIRAKFEKEYGVKlNPKAGKDNHEMVEgihdGEVHSLY 649
Cdd:cd02761 266 LNEYTKFALL--PLRGHYNVRGFNQVLT---WLTGYP------FRVDFSRGYPRY-NPGEFTAVDLLAE----GEADALL 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 650 LYGEDTGivdsnINFVQAAFEKLDFM--VVQDEFLTFTATYADVVLPAS-PSLEKDGTFTNTERRIQRLYQALEPlgDSK 726
Cdd:cd02761 330 IIASDPP-----AHFPQSAVKHLAEIpvIVIDPPPTPTTRVADVVIPVAiPGIEAGGTAYRMDGVVVLPLKAVET--ERL 402
|
490
....*....|...
gi 686208005 727 PDWKIFQAIANKL 739
Cdd:cd02761 403 PDEEILKQLLEKV 415
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
824-937 |
1.14e-20 |
|
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. This CD (MopB_CT_Formate-Dh_H) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239191 [Multi-domain] Cd Length: 116 Bit Score: 88.06 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 824 NNGRLLEHFHEGNMTYQTPMIKYKVPRAFVEISPELAEDRGIHEGAEVKLISETGEAVLQVHVTDRVKGKEIYIPLN-ND 902
Cdd:cd02790 8 TTGRVLYHYHTGTMTRRAEGLDAIAPEEYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGVVFMPFHfAE 87
|
90 100 110
....*....|....*....|....*....|....*
gi 686208005 903 AmengdlgAINLLTNSDVDQYTDTPSYKRTSCRLE 937
Cdd:cd02790 88 A-------AANLLTNAALDPVAKIPEFKVCAVRVE 115
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
821-932 |
7.23e-20 |
|
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - containing oxidoreductases and tungsten formylmethanofuran dehydrogenase subunit d (FwdD) and molybdenum formylmethanofuran dehydrogenase subunit (FmdD); where the domain constitutes almost the entire subunit. The formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and has a molybdopterin dinucleotide cofactor. This domain corresponds to the C-terminal domain IV in dimethyl sulfoxide (DMSO)reductase which interacts with the 2-amino pyrimidone ring of both molybdopterin guanine dinucleotide molecules.
Pssm-ID: 426328 [Multi-domain] Cd Length: 110 Bit Score: 85.79 E-value: 7.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 821 IHVNNGRLLEHFHEGNMTYQTPMiKYKVPRAFVEISPELAEDRGIHEGAEVKLISETGEAVLQVHVTDRVKGKEIYIPLN 900
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLR-LAKPEPEVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFG 79
|
90 100 110
....*....|....*....|....*....|..
gi 686208005 901 ndAMENGDLGAINLLTNSDVDQYTDTPSYKRT 932
Cdd:pfam01568 80 --WWYEPRGGNANALTDDATDPLSGGPEFKTC 109
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
828-930 |
1.08e-18 |
|
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site. This hierarchy is of the conserved MopB_CT domain present in many, but not all, MopB homologs.
Pssm-ID: 239176 [Multi-domain] Cd Length: 101 Bit Score: 81.98 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 828 LLEHFHEGNMTyQTPMIKYKVPRAFVEISPELAEDRGIHEGAEVKLISETGEAVLQVHVTDRVKGKEIYIPlNNDAMENG 907
Cdd:cd02775 1 LRDHFHSGTRT-RNPWLRELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLP-HGWGHRGG 78
|
90 100
....*....|....*....|...
gi 686208005 908 DLGAINLLTNSDVDQYTDTPSYK 930
Cdd:cd02775 79 RGGNANVLTPDALDPPSGGPAYK 101
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
258-311 |
1.61e-16 |
|
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is found in a number of reductase/dehydrogenase families, which include the periplasmic nitrate reductase precursor and the formate dehydrogenase alpha chain.
Pssm-ID: 197994 [Multi-domain] Cd Length: 55 Bit Score: 74.21 E-value: 1.61e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 686208005 258 KKTKTVCTYCGVGCSFEVWTKDREILKVQPSHDSPANKIATCVKGKFSWGHINS 311
Cdd:smart00926 2 KWVPTVCPLCGVGCGLLVEVKDGRVVRVRGDPDHPVNRGRLCPKGRAGLEQVYS 55
|
|
| FeFe_hydrog_A |
TIGR02512 |
[FeFe] hydrogenase, group A; This model describes iron-only hydrogenases of anaerobic and ... |
143-209 |
2.42e-13 |
|
[FeFe] hydrogenase, group A; This model describes iron-only hydrogenases of anaerobic and microaerophilic bacteria and protozoa. This model is narrower, and covers a longer stretch of sequence, than pfam02906. This family represents a division among families that belong to pfam02906, which also includes proteins such as nuclear prelamin A recognition factor in animals. Note that this family shows some heterogeneity in terms of periplasmic, cytosolic, or hydrogenosome location, NAD or NADP dependence, and overal protein protein length.
Pssm-ID: 274171 [Multi-domain] Cd Length: 374 Bit Score: 72.74 E-value: 2.42e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 686208005 143 DPNQCILCGRCVEACQDIEVNETIRIDWDREHPRVIWDNDVPINESSCVSCGQCATVCPCNAMMEVN 209
Cdd:TIGR02512 5 DMSKCIGCGRCVRACTNVQIVGALGFLNRGGKTEVAPKFGRLLDESNCIGCGQCSLVCPVGAITEKD 71
|
|
| PTZ00305 |
PTZ00305 |
NADH:ubiquinone oxidoreductase; Provisional |
21-187 |
2.66e-13 |
|
NADH:ubiquinone oxidoreductase; Provisional
Pssm-ID: 140326 [Multi-domain] Cd Length: 297 Bit Score: 71.61 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 21 NLLEFIKSQDTFVPSICYNESMGPIQTCDTCTVEIDG--KIERSCSTVIDRPMTVNTVNNDVKDAQKEALDRILEKHMLY 98
Cdd:PTZ00305 86 NLLEVLEREGIRVPKFCYHPILSVAGNCRMCLVQVDGtqNLVVSCATVALPGMSIITDSRLVRDAREGNVELILINHPND 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 99 CTVCDYNNgDCEIHNTMDAWGLQHQTYEYKEKPYEKDY-GPFYRYDPNQCILCGRCV----EACQDIEVNETIR-----I 168
Cdd:PTZ00305 166 CPICEQAT-NCDLQNVSMNYGTDIPRYKEDKRAVQDFYfDPQTRVVLNRCIHCTRCVrflnEHAQDFNLGMIGRgglseI 244
|
170
....*....|....*....
gi 686208005 169 DWDREHPRVIWDNDVPINE 187
Cdd:PTZ00305 245 STFLDELEVKTDNNMPVSQ 263
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
307-763 |
1.11e-12 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 72.40 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 307 GHINSDQRLTKPLVR----KNGE-----------FHEVEWDEALNVIADNFTSIKEKYGPDALsfissskatneesYLMQ 371
Cdd:PRK15102 83 GHVYNPSRIRYPMVRldwlRKRHksdtsqrgdnrFVRVSWDEALDLFYEELERVQKTYGPSAL-------------HTGQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 372 KLARQvigTNNVDNCSRYCQ-APATKGLFrtVGHGGDS-------------GSIED----------LEKAAMSVLIGTN- 426
Cdd:PRK15102 150 TGWQS---TGQFHSATGHMQrAIGMHGNS--VGTVGDYstgagqvilpyvlGSTEVyeqgtswpliLENSKTIVLWGSDp 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 427 --------TAEAHPVIASRMKRAQKLFGQKIHVFDI-----RKHEMAERADRFYQPKpgTDLAWLSAVTKYIIDHDLHDK 493
Cdd:PRK15102 225 vknlqvgwNCETHESYAYLAQLKEKVAKGEINVISIdpvvtKTQNYLGCEHLYVNPQ--TDVPLMLALAHTLYSENLYDK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 494 AFIDEWVDDFDEYYKSL--ET----FTMAFAEEATGIPKSELIKFAEECAKAESVVIC-WAmgITQQDIGSDSSTAISNL 566
Cdd:PRK15102 303 KFIDNYCLGFEQFLPYLlgEKdgvpKTPEWAEKICGIDAETIRELARQMAKGRTQIIAgWC--IQRQQHGEQPYWMGAVL 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 567 LLVTGNYRRPGTG-AYplrGH--NNVQGCSDMGSMPdkiTGYQSIEADDIRAKFE----KEYGVKLnPKAgkdnhEMVEG 639
Cdd:PRK15102 381 AAMLGQIGLPGGGiSY---GHhySGIGVPSSGGAIP---GGFPGNLDTGQKPKHDnsdyKGYSSTI-PVA-----RFIDA 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 640 I-HDGEV-----HSLYLYGEDTGIVDSN--------INFVQAAFEKLDFMVVQDEFLTFTATYADVVLPASPSLEKD--- 702
Cdd:PRK15102 449 IlEPGKTinwngKKVTLPPLKMMIFSGTnpwhrhqdRNRMKEAFRKLETVVAIDNQWTATCRFADIVLPACTQFERNdid 528
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 686208005 703 --GTFTNteRRIQRLYQALEPLGDSKPDWKIFQAIANKLGFDWNYkhpSEIMDEVARLTPLYA 763
Cdd:PRK15102 529 qyGSYSN--RGIIAMKKVVEPLFESRSDFDIFRELCRRFGREKEY---TRGMDEMGWLKRLYQ 586
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
55-209 |
1.36e-12 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 71.21 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 55 IDGKIERSCSTVIDRPMTVNTVNNDVKDAQKEALDRILEKHMLYCTVCDyNNGDCEIHNTMDAWGLQHQTYEYKEKPYEK 134
Cdd:COG4624 1 LLLLLRACCCCCIEEGDELLLLEEAERVLRIIILEALLPEHVDDDSACS-CCPRCCLCCCCCCRCCVAISCIQVRGIIII 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 686208005 135 DYGPFYRY-DPNQCILCGRCVEACQDievnETIRIDwdrehprviwDNDVPINESSCVSCGQCATVCPCNAMMEVN 209
Cdd:COG4624 80 DKRGPSIIrDKEKCKNCYPCVRACPV----KAIKVD----------DGKAEIDEEKCISCGQCVAVCPFGAITEKS 141
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
5-111 |
7.85e-11 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 65.91 E-value: 7.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 5 LVVTLDGKDYLVEPGTNLLEFIKSQDTFVPSICYNESMGPIQTCDTCTVEIDGKiER---SCSTVIDRPMTVNTVNNDVK 81
Cdd:PRK12814 4 ISLTINGRSVTAAPGTSILEAAASAGITIPTLCFHQELEATGSCWMCIVEIKGK-NRfvpACSTAVSEGMVIETENAELH 82
|
90 100 110
....*....|....*....|....*....|
gi 686208005 82 DAQKEALDRILEKHmlyCTVCdynNGDCEI 111
Cdd:PRK12814 83 AMRRQSLERLIEQH---CGDC---LGPCEL 106
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
142-204 |
1.57e-10 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 59.72 E-value: 1.57e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 686208005 142 YDPNQCILCGRCVEACQdievNETIRIDWDREhPRVIWDNDVPINESSCVSCGQCATVCPCNA 204
Cdd:cd10549 37 IDEDKCVFCGACVEVCP----TGAIELTPEGK-EYVPKEKEAEIDEEKCIGCGLCVKVCPVDA 94
|
|
| Fer4_7 |
pfam12838 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
147-204 |
4.40e-10 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 463724 [Multi-domain] Cd Length: 51 Bit Score: 56.00 E-value: 4.40e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 686208005 147 CILCGRCVEACqdievnETIRIDWDREHPRVIWDnDVPINESSCVSCGQCATVCPCNA 204
Cdd:pfam12838 1 CIGCGACVAAC------PVGAITLDEVGEKKGTK-TVVIDPERCVGCGACVAVCPTGA 51
|
|
| PRK12387 |
PRK12387 |
formate hydrogenlyase complex iron-sulfur subunit; Provisional |
124-204 |
9.48e-10 |
|
formate hydrogenlyase complex iron-sulfur subunit; Provisional
Pssm-ID: 183492 [Multi-domain] Cd Length: 180 Bit Score: 58.89 E-value: 9.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 124 TYEYKEKPYEKDYGpfYR----YDPNQCILCGRCVEACQdievNETIRIDWDREHPRVIWDndvpINESSCVSCGQCATV 199
Cdd:PRK12387 15 TSSYPLEPIAVDKN--FRgkpeYNPQQCIGCAACVNACP----SNALTVETDLATGELAWE----FNLGRCIFCGRCEEV 84
|
....*
gi 686208005 200 CPCNA 204
Cdd:PRK12387 85 CPTAA 89
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
144-204 |
1.36e-09 |
|
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440758 [Multi-domain] Cd Length: 66 Bit Score: 55.14 E-value: 1.36e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 686208005 144 PNQCILCGRCVEACQdievNETIRIDWDREHPRVIwdndvpINESSCVSCGQCATVCPCNA 204
Cdd:COG1143 1 EDKCIGCGLCVRVCP----VDAITIEDGEPGKVYV------IDPDKCIGCGLCVEVCPTGA 51
|
|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
819-932 |
1.54e-09 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase (Arsenite-Ox) and related proteins. Arsenite oxidase oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin.
Pssm-ID: 239180 [Multi-domain] Cd Length: 115 Bit Score: 56.31 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 819 YDIHVNNGRLLEHFHEGNMTYQTPMIKYKVPRAFVEISPELAEDRGIHEGAEVKLISETGEAVLQVHVTDRVKGKEIYIp 898
Cdd:cd02779 1 YKYWVNNGRANIIWQTAYHDQNNSEIAERVPLPYIEVNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKPGQTFM- 79
|
90 100 110
....*....|....*....|....*....|....
gi 686208005 899 lnndAMENGDLGAiNLLTNSDVDQYTDTPSYKRT 932
Cdd:cd02779 80 ----LMAHPRPGA-NGLVTPYVDPETIIPYYKGT 108
|
|
| DsrA |
COG2221 |
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ... |
141-201 |
1.66e-09 |
|
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];
Pssm-ID: 441823 [Multi-domain] Cd Length: 69 Bit Score: 55.06 E-value: 1.66e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 686208005 141 RYDPNQCILCGRCVEACQDievnETIRIDwdrehprviwDNDVPINESSCVSCGQCATVCP 201
Cdd:COG2221 11 KIDEEKCIGCGLCVAVCPT----GAISLD----------DGKLVIDEEKCIGCGACIRVCP 57
|
|
| COG1149 |
COG1149 |
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
136-205 |
2.23e-09 |
|
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];
Pssm-ID: 440763 [Multi-domain] Cd Length: 68 Bit Score: 54.35 E-value: 2.23e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 686208005 136 YGPFYRYDPNQCILCGRCVEACQdievNETIRIDwdrehprviwDNDVP-INESSCVSCGQCATVCPCNAM 205
Cdd:COG1149 2 KRKIPVIDEEKCIGCGLCVEVCP----EGAIKLD----------DGGAPvVDPDLCTGCGACVGVCPTGAI 58
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
143-205 |
2.97e-09 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 55.87 E-value: 2.97e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 686208005 143 DPNQCILCGRCVEAC-QD-IEVNETIRIDwdrehprviwdndvpINESSCVSCGQCATVCPCNAM 205
Cdd:cd10549 76 DEEKCIGCGLCVKVCpVDaITLEDELEIV---------------IDKEKCIGCGICAEVCPVNAI 125
|
|
| IorA |
COG4231 |
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ... |
140-204 |
4.16e-09 |
|
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];
Pssm-ID: 443375 [Multi-domain] Cd Length: 76 Bit Score: 53.89 E-value: 4.16e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 686208005 140 YRYDPNQCILCGRCVEACQdievNETIRIDwdrehprviwDNDVPINESSCVSCGQCATVCPCNA 204
Cdd:COG4231 17 YVIDEDKCTGCGACVKVCP----ADAIEEG----------DGKAVIDPDLCIGCGSCVQVCPVDA 67
|
|
| NapF |
COG1145 |
Ferredoxin [Energy production and conversion]; |
128-205 |
4.71e-09 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440760 [Multi-domain] Cd Length: 238 Bit Score: 58.20 E-value: 4.71e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 686208005 128 KEKPYEKDYGPFYRYDPNQCILCGRCVEACQdievNETIRIDwDREHPRVIWDNDvpinessCVSCGQCATVCPCNAM 205
Cdd:COG1145 165 EEELKIAIKKAKAVIDAEKCIGCGLCVKVCP----TGAIRLK-DGKPQIVVDPDK-------CIGCGACVKVCPVGAI 230
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
142-204 |
4.82e-09 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 55.48 E-value: 4.82e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 686208005 142 YDPNQCILCGRCVEACQdievNETIRIDwDREHPRVIWDndvpINESSCVSCGQCATVCPCNA 204
Cdd:cd10549 3 YDPEKCIGCGICVKACP----TDAIELG-PNGAIARGPE----IDEDKCVFCGACVEVCPTGA 56
|
|
| NADH-G_4Fe-4S_3 |
smart00929 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
84-125 |
5.14e-09 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 214918 [Multi-domain] Cd Length: 41 Bit Score: 52.59 E-value: 5.14e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 686208005 84 QKEALDRILEKHMLYCTVCDyNNGDCEIHNTMDAWGLQHQTY 125
Cdd:smart00929 1 RKTILELLLANHPLDCPVCD-KNGECELQDLAYELGVDEQRY 41
|
|
| PorD |
COG1144 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ... |
142-204 |
1.72e-08 |
|
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440759 [Multi-domain] Cd Length: 84 Bit Score: 52.36 E-value: 1.72e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 686208005 142 YDPNQCILCGRCVEACQD--IEVNETIRIDWDREHprviwdndvpinessCVSCGQCATVCPCNA 204
Cdd:COG1144 27 VDEDKCIGCGLCWIVCPDgaIRVDDGKYYGIDYDY---------------CKGCGICAEVCPVKA 76
|
|
| Fer4_9 |
pfam13187 |
4Fe-4S dicluster domain; |
146-205 |
2.29e-08 |
|
4Fe-4S dicluster domain;
Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 51.02 E-value: 2.29e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 146 QCILCGRCVEACQdievNETIRIDWDREHPRVIWDNDvpinesSCVSCGQCATVCPCNAM 205
Cdd:pfam13187 1 KCTGCGACVAACP----AGAIVPDLVGQTIRGDIAGL------ACIGCGACVDACPRGAI 50
|
|
| PreA |
COG1146 |
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
143-204 |
3.18e-08 |
|
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];
Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 51.25 E-value: 3.18e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 686208005 143 DPNQCILCGRCVEACQdievNETIRIDWDREHPrviwdndVPINESSCVSCGQCATVCPCNA 204
Cdd:COG1146 6 DTDKCIGCGACVEVCP----VDVLELDEEGKKA-------LVINPEECIGCGACELVCPVGA 56
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
141-201 |
6.90e-08 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 404174 [Multi-domain] Cd Length: 56 Bit Score: 49.94 E-value: 6.90e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 686208005 141 RYDPNQCILCGRCVEAC-QDIEVNETIRIDWDREHPRviwdndvpINESSCVSCGQCATVCP 201
Cdd:pfam13237 3 VIDPDKCIGCGRCTAACpAGLTRVGAIVERLEGEAVR--------IGVWKCIGCGACVEACP 56
|
|
| COG2768 |
COG2768 |
Uncharacterized Fe-S cluster protein [Function unknown]; |
143-205 |
1.43e-07 |
|
Uncharacterized Fe-S cluster protein [Function unknown];
Pssm-ID: 442050 [Multi-domain] Cd Length: 74 Bit Score: 49.73 E-value: 1.43e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 686208005 143 DPNQCILCGRCVEACQdievNETIRIDwdrehprviwDNDVPINESSCVSCGQCATVCPCNAM 205
Cdd:COG2768 9 DEEKCIGCGACVKVCP----VGAISIE----------DGKAVIDPEKCIGCGACIEVCPVGAI 57
|
|
| Fer4_21 |
pfam14697 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
143-201 |
1.54e-07 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 434137 [Multi-domain] Cd Length: 59 Bit Score: 48.82 E-value: 1.54e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 686208005 143 DPNQCILCGRCVEACQDIEVnETIRIDWDREHprviwdndvPINESSCVSCGQCATVCP 201
Cdd:pfam14697 4 DEDTCIGCGKCYIACPDTSH-QAIVGDGKRHH---------TVIEDECTGCNLCVSVCP 52
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
298-740 |
1.57e-07 |
|
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other related proteins. The Salmonella enterica tetrathionate reductase catalyses the reduction of trithionate but not sulfur or thiosulfate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239159 [Multi-domain] Cd Length: 735 Bit Score: 55.43 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 298 TCVKGKFSWGHINSDQRLTKPLVR--KNGE--FHEVEWDEALNVIA-----------DNFTSIKEK----------YGPD 352
Cdd:cd02758 67 ACARGNAGLQYLYDPYRVLQPLKRvgPRGSgkWKPISWEQLIEEVVeggdlfgeghvEGLKAIRDLdtpidpdhpdLGPK 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 353 ALSFISSSKATNEESYLMQKLARQVIGTNNVDNCSRYCQAP--ATKGLFRTvGHGGDSGSIEDLEKAAMSVLIGTNTAEA 430
Cdd:cd02758 147 ANQLLYTFGRDEGRTPFIKRFANQAFGTVNFGGHGSYCGLSyrAGNGALMN-DLDGYPHVKPDFDNAEFALFIGTSPAQA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 431 HPVI---ASRMKRAQKLFGQKIHVFD---IRKHEMAERADRFYQPKPGTDLAWLSAVTKYIIDHDLHDKAFI---DEWVD 501
Cdd:cd02758 226 GNPFkrqARRLAEARTEGNFKYVVVDpvlPNTTSAAGENIRWVPIKPGGDGALAMAMIRWIIENERYNAEYLsipSKEAA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 502 DFDEY--------------YKSL------ETFTMAFAE--EATGIPKSELIKFAEECAKAESVVICWAMGITQQDIGSDS 559
Cdd:cd02758 306 KAAGEpswtnathlvitvrVKSAlqllkeEAFSYSLEEyaEICGVPEAKIIELAKEFTSHGRAAAVVHHGGTMHSNGFYN 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 560 STAISNLLLVTGNYRRPG----TGAYplrGHNNVQGCSDMGSMPDKITGYQSIEADDIRAKFEK--EYGVKL-------- 625
Cdd:cd02758 386 AYAIRMLNALIGNLNWKGgllmSGGG---FADNSAGPRYDFKKFFGEVKPWGVPIDRSKKAYEKtsEYKRKVaagenpyp 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 626 -----NPKAGKDNHEMVEGIHDGevhslYLYGEDTGIVDSN-----INFVQAAFE-------KLDFMVVQDEFLTFTATY 688
Cdd:cd02758 463 akrpwYPLTPELYTEVIASAAEG-----YPYKLKALILWMAnpvygAPGLVKQVEeklkdpkKLPLFIAIDAFINETSAY 537
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 686208005 689 ADVVLPASPSLEKdGTFTNTERRIQRLYQ-----ALEPLGDSKPD------WKIFQAIANKLG 740
Cdd:cd02758 538 ADYIVPDTTYYES-WGFSTPWGGVPTKAStarwpVIAPLTEKTANghpvsmESFLIDLAKALG 599
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
849-938 |
2.01e-07 |
|
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239183 [Multi-domain] Cd Length: 129 Bit Score: 50.85 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 849 PRAFVEISPELAEDRGIHEGAEVKLISETGEAVLQVHVTDRVKGKEIYIP------LNNDAMENGDLG-AINLLTN-SDV 920
Cdd:cd02782 31 NRCTLRIHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMPGVVSLPhgwghdYPGVSGAGSRPGvNVNDLTDdTQR 110
|
90
....*....|....*...
gi 686208005 921 DQYTDTPSYKRTSCRLEV 938
Cdd:cd02782 111 DPLSGNAAHNGVPVRLAR 128
|
|
| NADH-G_4Fe-4S_3 |
pfam10588 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
84-123 |
9.64e-07 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 463159 [Multi-domain] Cd Length: 40 Bit Score: 46.29 E-value: 9.64e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 686208005 84 QKEALDRILEKHMLYCTVCDyNNGDCEIHNTMDAWGLQHQ 123
Cdd:pfam10588 1 RKTILELLLSNHPLDCPTCD-KNGNCELQDLAYELGVDEV 39
|
|
| Fer4_8 |
pfam13183 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
146-203 |
1.57e-06 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 433017 [Multi-domain] Cd Length: 64 Bit Score: 46.15 E-value: 1.57e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 686208005 146 QCILCGRCVEAC--------QDIEVNETIRIDWDREHPRVIWDNDVPineSSCVSCGQCATVCPCN 203
Cdd:pfam13183 1 RCIRCGACLAACpvylvtggRFPGDPRGGAAALLGRLEALEGLAEGL---WLCTLCGACTEVCPVG 63
|
|
| DMSOR_beta_like |
cd16370 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
141-207 |
3.20e-06 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319892 [Multi-domain] Cd Length: 131 Bit Score: 47.27 E-value: 3.20e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 141 RYDPNQCILCGRCVEACqdievneTIR-IDWDREhprviwdNDVPInesSCVSCGQCATVCP--CNAMME 207
Cdd:cd16370 79 VLDKEKCIGCGNCVKAC-------IVGaIFWDEE-------TNKPI---ICIHCGYCARYCPhdVLAMEE 131
|
|
| NapH |
COG0348 |
Polyferredoxin NapH [Energy production and conversion]; |
135-201 |
3.51e-06 |
|
Polyferredoxin NapH [Energy production and conversion];
Pssm-ID: 440117 [Multi-domain] Cd Length: 263 Bit Score: 49.68 E-value: 3.51e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 686208005 135 DYGPF-YRYDPNQCILCGRCVEACqdiEVNETIRidwdrehprviwdnDVPINESSCVSCGQCATVCP 201
Cdd:COG0348 199 DLSTLrVRYDRGDCIDCGLCVKVC---PMGIDIR--------------KGEINQSECINCGRCIDACP 249
|
|
| PRK08318 |
PRK08318 |
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
141-221 |
4.54e-06 |
|
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 50.33 E-value: 4.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 141 RYDPNQCILCGRCVEACQDIEVNEtirIDWDRE---HPRVIwdndvpinESSCVSCGQCATVCP---CNAMMEVnmEGNA 214
Cdd:PRK08318 338 RIDQDKCIGCGRCYIACEDTSHQA---IEWDEDgtrTPEVI--------EEECVGCNLCAHVCPvegCITMGEV--KFGK 404
|
....*..
gi 686208005 215 GYMTDTE 221
Cdd:PRK08318 405 PYANWTT 411
|
|
| DMSOR_beta_like |
cd10550 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
140-204 |
5.69e-06 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319872 [Multi-domain] Cd Length: 130 Bit Score: 46.80 E-value: 5.69e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 686208005 140 YRYDPNQCILCGRCVEACQDievnETIRIDWDREHPRViwdndvpinessCVSCG---QCATVCPCNA 204
Cdd:cd10550 75 VVVDEDKCIGCGMCVEACPF----GAIRVDPETGKAIK------------CDLCGgdpACVKVCPTGA 126
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
143-205 |
9.20e-06 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 49.47 E-value: 9.20e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 686208005 143 DPNQCILCGRCVEAC--QDIEVNETiridwdrehpRVIWdndvpINESSCVSCGQCATVCPCNAM 205
Cdd:COG1148 494 DPEKCTGCGRCVEVCpyGAISIDEK----------GVAE-----VNPALCKGCGTCAAACPSGAI 543
|
|
| MopB_Res-Cmplx1_Nad11-M |
cd02774 |
MopB_Res_Cmplx1_Nad11_M: Mitochondrial-encoded NADH-quinone oxidoreductase/respiratory complex ... |
268-454 |
1.34e-05 |
|
MopB_Res_Cmplx1_Nad11_M: Mitochondrial-encoded NADH-quinone oxidoreductase/respiratory complex I, the second domain of the Nad11/75-kDa subunit of some protists. NADH-quinone oxidoreductase is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The nad11 gene codes for the largest (75-kDa) subunit of the mitochondrial NADH-quinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. The Nad11 subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239175 [Multi-domain] Cd Length: 366 Bit Score: 48.52 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 268 GVGCSFEVWTKDREILKVQPSHDSPANKIATCVKGKFSWGHINSdQRLTKPLVR-KNGEFHEVEWDEALNVIaDNFTSIK 346
Cdd:cd02774 8 SLGSNIRVDIKGNEILRILPKINDELNEEWISDKIRFSYDSLKY-QRIKTPLLKlSNNSFLEIGWKTAFKFL-NKFILLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 347 EkygPDALSFISSSKATNEESY----LMQKLARQVIGTNNVDNCSRYCQAPATKGLFrtvghggdSGSIEDLEKAAMSVL 422
Cdd:cd02774 86 K---FSKLNFIIGSKIDLETLFyykkLLNKLGSLNTNSNNFLENNNYFNLDLENYLF--------NNSLKNLDKSDLCLL 154
|
170 180 190
....*....|....*....|....*....|..
gi 686208005 423 IGTNTAEAHPVIASRMKraQKLFGQKIHVFDI 454
Cdd:cd02774 155 IGSNLRVESPILNIRLR--NRYNKGNKKIFVI 184
|
|
| Fer4_17 |
pfam13534 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
147-201 |
1.44e-05 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 433287 [Multi-domain] Cd Length: 61 Bit Score: 43.60 E-value: 1.44e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 686208005 147 CILCGRCVEACQdievnetiRIDWDREHPRVI---WDNDVPINE------SSCVSCGQCATVCP 201
Cdd:pfam13534 2 CIQCGCCVDECP--------RYLLNGDEPKKLmraAYLGDLEELqankvaNLCSECGLCEYACP 57
|
|
| DMSOR_beta_like |
cd16373 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
141-201 |
1.47e-05 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319895 [Multi-domain] Cd Length: 154 Bit Score: 46.09 E-value: 1.47e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 686208005 141 RYDPNQCIL------CGRCVEAC--QDIevneTIRIDWDREHPRViwdndvpiNESSCVSCGQCATVCP 201
Cdd:cd16373 87 VIDKDRCLAwqggtdCGVCVEACptEAI----AIVLEDDVLRPVV--------DEDKCVGCGLCEYVCP 143
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
836-920 |
1.86e-05 |
|
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239187 [Multi-domain] Cd Length: 116 Bit Score: 44.96 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 836 NMTY-QTPMIKYKVPRAFVEISPELAEDRGIHEGAEVKLISETGEAVLQVHVTDRVKGKEIYIPLN--NDAMENGdlGAI 912
Cdd:cd02786 15 NSTFaNLPELRAKEGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVVVAEGGwwREHSPDG--RGV 92
|
....*...
gi 686208005 913 NLLTNSDV 920
Cdd:cd02786 93 NALTSARL 100
|
|
| PRK07118 |
PRK07118 |
Fe-S cluster domain-containing protein; |
147-209 |
2.61e-05 |
|
Fe-S cluster domain-containing protein;
Pssm-ID: 235941 [Multi-domain] Cd Length: 280 Bit Score: 47.24 E-value: 2.61e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 686208005 147 CILCGRCVEACQDievnETIRIDwdrehprviwDNDVPINESSCVSCGQCATVCPCNAMMEVN 209
Cdd:PRK07118 215 CIGCGKCVKACPA----GAITME----------NNLAVIDQEKCTSCGKCVEKCPTKAIRILN 263
|
|
| DMSOR_beta_like |
cd10550 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
136-205 |
3.35e-05 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319872 [Multi-domain] Cd Length: 130 Bit Score: 44.49 E-value: 3.35e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 686208005 136 YGPFYRYDPNQCILCGR--CVEAC--QDIEVNEtiridwdrehprviWDNDVPINESSCVSCGQCATVCPCNAM 205
Cdd:cd10550 38 FEPEGLDVPVVCRQCEDapCVEACpvGAISRDE--------------ETGAVVVDEDKCIGCGMCVEACPFGAI 97
|
|
| DMSOR_beta_like |
cd16372 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
142-206 |
6.46e-05 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319894 [Multi-domain] Cd Length: 125 Bit Score: 43.48 E-value: 6.46e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 686208005 142 YDPNQCILCGRCVEACqdievnETIRIDwdREHPRVIWdndvpINESSCVSCGQCATVCPCNAMM 206
Cdd:cd16372 44 YAINVCNQCGECIDVC------PTGAIT--RDANGVVM-----INKKLCVGCLMCVGFCPEGAMF 95
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
826-935 |
1.03e-04 |
|
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239182 [Multi-domain] Cd Length: 130 Bit Score: 43.07 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 826 GRLLEHFHEGNmtYQTPMIKYKVPRAFVEISPELAEDRGIHEGAEVKLISETGEAVLQVHVTDRVKGKEIYI-------- 897
Cdd:cd02781 10 ARSYYYFHSEH--RQLPSLRELHPDPVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVRAehgwwype 87
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 686208005 898 -PLNNDAMENGDLGAINLLTNSDV-DQYTDTPSYKRTSCR 935
Cdd:cd02781 88 rEAGEPALGGVWESNANALTSDDWnDPVSGSSPLRSMLCK 127
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
262-348 |
1.29e-04 |
|
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), and other related proteins. The phenylacetyl-CoA:acceptor oxidoreductase has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239161 [Multi-domain] Cd Length: 760 Bit Score: 46.12 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 262 TVCTYCGVGCSF-EVWTKDREILKVQPSHDSPANKIA---TCVKGKFSWGHINSDQRLTKPLVRKNGE--------FHEV 329
Cdd:cd02760 2 TYCYNCVAGPDFmAVKVVDGVATEIEPNFAAEDIHPArgrVCVKAYGLVQKTYNPNRVLQPMKRTNPKkgrnedpgFVPI 81
|
90
....*....|....*....
gi 686208005 330 EWDEALNVIADNFTSIKEK 348
Cdd:cd02760 82 SWDEALDLVAAKLRRVREK 100
|
|
| MopB_CT_FmdC-FwdD |
cd02789 |
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran ... |
851-930 |
1.54e-04 |
|
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran dehydrogenase (FmdC) and subunit D of tungsten formylmethanofuran dehydrogenase (FwdD), and other related proteins. Formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and some eubacteria. Members of this CD belong to the molybdopterin_binding superfamily of proteins. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239190 [Multi-domain] Cd Length: 106 Bit Score: 42.03 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 851 AFVEISPELAEDRGIHEGAEVKLISETGEAVLQVHVTDRVKGKEIYIPLNNDAmengdlgainlltNSDVDQYTD---TP 927
Cdd:cd02789 31 AYCEINPEDYKLLGKPEGDKVKVTSEFGEVVVFAKENEGVPEGMVFIPMGPWA-------------NVVVDPYTDstgSP 97
|
...
gi 686208005 928 SYK 930
Cdd:cd02789 98 IFK 100
|
|
| Fer4 |
pfam00037 |
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ... |
183-204 |
3.20e-04 |
|
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 459642 [Multi-domain] Cd Length: 24 Bit Score: 38.77 E-value: 3.20e-04
|
| PRK08222 |
PRK08222 |
hydrogenase 4 subunit H; Validated |
124-205 |
5.21e-04 |
|
hydrogenase 4 subunit H; Validated
Pssm-ID: 181301 [Multi-domain] Cd Length: 181 Bit Score: 42.05 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 124 TYEYKEKPYEKDYGpfYR----YDPNQCILCGRCVEACQdievNETIRIDWDREHPRVIWDndvpINESSCVSCGQCATV 199
Cdd:PRK08222 15 TVKYPFAPLEVSPG--FRgkpdLMPSQCIACGACTCACP----ANALTIQTDDQQNSRTWQ----LYLGRCIYCGRCEEV 84
|
....*.
gi 686208005 200 CPCNAM 205
Cdd:PRK08222 85 CPTRAI 90
|
|
| SIMIBI_bact_arch |
cd03110 |
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ... |
143-272 |
5.58e-04 |
|
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.
Pssm-ID: 349764 [Multi-domain] Cd Length: 246 Bit Score: 42.76 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 143 DPNQCILCGRCVEACQdievnetiridwdreHPRVIWD-NDVPINESSCVSCGQCATVCPCNAMMEVNMEgnAGYMTDTE 221
Cdd:cd03110 62 DQEKCIRCGNCERVCK---------------FGAILEFfQKLIVDESLCEGCGACVIICPRGAIYLKDRD--TGKIFISS 124
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 686208005 222 PGSLAAMIDLTKKAEPGYGPLFaisdseAEMRKErIKKTKTVCTYC------GVGCS 272
Cdd:cd03110 125 SDGGPLVHGRLNIGEENSGKLV------TELRKK-ALERSKECDLAiidgppGTGCP 174
|
|
| HycB |
COG1142 |
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion]; |
139-205 |
5.88e-04 |
|
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
Pssm-ID: 440757 [Multi-domain] Cd Length: 138 Bit Score: 41.18 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 139 FYRYDPNQCILCGRCVEACqdIEVNEtiRIDWDREHPRV-------------------------------IWDNDVP-IN 186
Cdd:COG1142 4 FIIADPEKCIGCRTCEAAC--AVAHE--GEEGEPFLPRIrvvrkagvsapvqcrhcedapcaevcpvgaiTRDDGAVvVD 79
|
90
....*....|....*....
gi 686208005 187 ESSCVSCGQCATVCPCNAM 205
Cdd:COG1142 80 EEKCIGCGLCVLACPFGAI 98
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
133-157 |
8.30e-04 |
|
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440758 [Multi-domain] Cd Length: 66 Bit Score: 38.57 E-value: 8.30e-04
10 20
....*....|....*....|....*
gi 686208005 133 EKDYGPFYRYDPNQCILCGRCVEAC 157
Cdd:COG1143 23 DGEPGKVYVIDPDKCIGCGLCVEVC 47
|
|
| RnfB |
COG2878 |
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ... |
143-209 |
1.13e-03 |
|
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase
Pssm-ID: 442125 [Multi-domain] Cd Length: 254 Bit Score: 41.90 E-value: 1.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 686208005 143 DPNQCILCGRCVEACQ-D-IEVNEtiridwdrehprviwdNDVP-INESSCVSCGQCATVCP--CNAMMEVN 209
Cdd:COG2878 135 CEYGCIGCGDCIKACPfDaIVGAA----------------KGMHtVDEDKCTGCGLCVEACPvdCIEMVPVS 190
|
|
| DMSOR_beta_like |
cd16372 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
47-205 |
1.16e-03 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319894 [Multi-domain] Cd Length: 125 Bit Score: 40.01 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 47 TCDTCtveidGKIERSCSTVIdrpmtvntvnNDVKDAQKEALdRILEK-HMLYCTVCDyNNGDCeihntMDAWGLQHQTy 125
Cdd:cd16372 9 KCIGC-----LQCEEACSKTF----------FKEEDREKSCI-RITETeGGYAINVCN-QCGEC-----IDVCPTGAIT- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 126 eykekpyeKDYGPFYRYDPNQCILCGRCVEACQdievNETIRIDWDREHPrviwdndvpineSSCVSCGQCATVCPCNAM 205
Cdd:cd16372 66 --------RDANGVVMINKKLCVGCLMCVGFCP----EGAMFKHEDYPEP------------FKCIACGICVKACPTGAL 121
|
|
| PRK05888 |
PRK05888 |
NADH-quinone oxidoreductase subunit NuoI; |
124-209 |
1.50e-03 |
|
NADH-quinone oxidoreductase subunit NuoI;
Pssm-ID: 235637 [Multi-domain] Cd Length: 164 Bit Score: 40.25 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 124 TYEYkekPYEK-DYGPFYRY------DPNQ---CILCGRCVEACqdieVNETIRIDW-DREHPRviWDNDV-PINESSCV 191
Cdd:PRK05888 30 TIQY---PEEKlPLSPRFRGrhalrrDPNGeerCIACKLCAAIC----PADAITIEAaEREDGR--RRTTRyDINFGRCI 100
|
90
....*....|....*...
gi 686208005 192 SCGQCATVCPCNAMMEVN 209
Cdd:PRK05888 101 FCGFCEEACPTDAIVETP 118
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
839-916 |
1.65e-03 |
|
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase (DMSOR) of Escherichia coli and other related DMSOR-like enzymes. Unlike other DMSOR-like enzymes, this group has a predicted N-terminal iron-sulfur [4Fe-4S] cluster binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239195 [Multi-domain] Cd Length: 121 Bit Score: 39.20 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 839 YQTPMIKYKVPRAFVeISPELAEDRGIHEGAEVKLISETGEAVLQVHVTDRVKGKEIYIP------LNNDAMENGdlGAI 912
Cdd:cd02794 19 DNVPWLREAFPQEVW-INPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVVALPqgawyePDANGIDKG--GCI 95
|
....
gi 686208005 913 NLLT 916
Cdd:cd02794 96 NTLT 99
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
855-916 |
1.88e-03 |
|
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239178 [Multi-domain] Cd Length: 127 Bit Score: 39.49 E-value: 1.88e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 686208005 855 ISPELAEDRGIHEGAEVKLISETGEAVLQVHVTDRVKGKEI-------YIPLNNDAMENGdlGAINLLT 916
Cdd:cd02777 38 INPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPGVValpegawYDPDDNGGLDKG--GNPNVLT 104
|
|
| NapF |
COG1145 |
Ferredoxin [Energy production and conversion]; |
151-221 |
2.19e-03 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440760 [Multi-domain] Cd Length: 238 Bit Score: 40.86 E-value: 2.19e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 686208005 151 GRCVEACQDIEVNETIRIDWDREHPRVIWDNDVP--INESSCVSCGQCATVCPCNAMMEVnmEGNAGYMTDTE 221
Cdd:COG1145 143 GLAILGAAAPVDALAISGGKKIEEELKIAIKKAKavIDAEKCIGCGLCVKVCPTGAIRLK--DGKPQIVVDPD 213
|
|
| GlpC |
COG0247 |
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ... |
145-210 |
2.41e-03 |
|
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];
Pssm-ID: 440017 [Multi-domain] Cd Length: 420 Bit Score: 41.60 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 145 NQCILCGRCVEAC--------------QDIEV-----NETIRIDWDREHPRVIWdndvpinesSCVSCGQCATVCPcnam 205
Cdd:COG0247 78 DACVGCGFCRAMCpsykatgdekdsprGRINLlrevlEGELPLDLSEEVYEVLD---------LCLTCKACETACP---- 144
|
....*
gi 686208005 206 MEVNM 210
Cdd:COG0247 145 SGVDI 149
|
|
| HybA |
COG0437 |
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ... |
142-205 |
2.56e-03 |
|
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion];
Pssm-ID: 440206 [Multi-domain] Cd Length: 184 Bit Score: 39.93 E-value: 2.56e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 686208005 142 YDPNQCILCGRCVEACQ---DIEVNET-IRID--WDREHPRVIWDNdVPInesSCVSCGQ--CATVCPCNAM 205
Cdd:COG0437 10 IDLTKCIGCRACVVACKeenNLPVGVTwRRVRryEEGEFPNVEWLF-VPV---LCNHCDDppCVKVCPTGAT 77
|
|
| PRK14028 |
PRK14028 |
pyruvate ferredoxin oxidoreductase subunit gamma/delta; Provisional |
143-208 |
3.06e-03 |
|
pyruvate ferredoxin oxidoreductase subunit gamma/delta; Provisional
Pssm-ID: 172522 [Multi-domain] Cd Length: 312 Bit Score: 40.75 E-value: 3.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 686208005 143 DPNQCILCGRCVEACQDIEVNETIRidwDREHPR--VIWDNDVPINESSCVSCGQCATVCPCNAMMEV 208
Cdd:PRK14028 245 DHSKCIMCRKCWLYCPDDAIIEAWR---EAEGPRgrKFRMKMIDFDYQYCKGCGVCAEVCPTGAIQMV 309
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|
| MopB_CT_NDH-1_NuoG2-N7 |
cd02788 |
MopB_CT_NDH-1_NuoG2-N7: C-terminal region of the NuoG-like subunit (of the variant with a ... |
832-904 |
3.47e-03 |
|
MopB_CT_NDH-1_NuoG2-N7: C-terminal region of the NuoG-like subunit (of the variant with a [4Fe-4S] cluster, N7) of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1) found in various bacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain, is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Unique to this group, compared to the other prokaryotic and eukaryotic groups in this domain protein family (NADH-Q-OR-NuoG2), is an N-terminal [4Fe-4S] cluster (N7/N1c) present in the second domain and a C-terminal region (this CD) homologous to the formate dehydrogenase C-terminal molybdopterin_binding (MopB) region.
Pssm-ID: 239189 [Multi-domain] Cd Length: 96 Bit Score: 37.67 E-value: 3.47e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 686208005 832 FHEGNMTYQTPMIKYKVPRAFVEISPELAEDRGIHEGAEVKLISETGEAVLQVHVTDRVKGKEIYIPLNNDAM 904
Cdd:cd02788 10 FGSEELSQRSPVIAERAPAPYARLSPADAARLGLADGDLVEFSLGDGTLTLPVQISKYLPAGVVGLPLGAGFP 82
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|
| Fer4_16 |
pfam13484 |
4Fe-4S double cluster binding domain; |
147-201 |
4.33e-03 |
|
4Fe-4S double cluster binding domain;
Pssm-ID: 463893 [Multi-domain] Cd Length: 65 Bit Score: 36.70 E-value: 4.33e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 686208005 147 CILCGRCVEAC---------QDIEVNETIRIDwDREHPRVIWDNDVPINESSCVSCGQCATVCP 201
Cdd:pfam13484 1 CGSCGKCIDACptgaivgpeGVLDARRCISYL-TIEKKGLIPDELRCLLGNRCYGCDICQDVCP 63
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|
| PRK08348 |
PRK08348 |
NADH-plastoquinone oxidoreductase subunit; Provisional |
142-205 |
4.99e-03 |
|
NADH-plastoquinone oxidoreductase subunit; Provisional
Pssm-ID: 181399 [Multi-domain] Cd Length: 120 Bit Score: 37.89 E-value: 4.99e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 686208005 142 YDPNQCILCGRCVEACqdievnETIRIDWDREHPRV-IWdndvpinESSCVSCGQCATVCPCNAM 205
Cdd:PRK08348 39 YDVDKCVGCRMCVTVC------PAGVFVYLPEIRKVaLW-------TGRCVFCGQCVDVCPTGAL 90
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|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
849-890 |
5.52e-03 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate reductase, subunit A, (TtrA); respiratory arsenate As(V) reductase, catalytic subunit (ArrA); and other related proteins.
Pssm-ID: 239181 [Multi-domain] Cd Length: 143 Bit Score: 38.43 E-value: 5.52e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 686208005 849 PRAFVEISPELAEDRGIHEGAEVKLISETGEAVLQVHVTDRV 890
Cdd:cd02780 28 PENPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGV 69
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|
| PRK13795 |
PRK13795 |
hypothetical protein; Provisional |
147-201 |
5.96e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237510 [Multi-domain] Cd Length: 636 Bit Score: 40.36 E-value: 5.96e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 686208005 147 CILCGRCVEACQdievNETIRIDwdrEHPRVIwdndvPINESSCVSCGQCATVCP 201
Cdd:PRK13795 583 CVGCGVCVGACP----TGAIRIE---EGKRKI-----SVDEEKCIHCGKCTEVCP 625
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|
| NapF_like |
cd10564 |
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ... |
146-201 |
6.80e-03 |
|
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319886 [Multi-domain] Cd Length: 139 Bit Score: 37.99 E-value: 6.80e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 686208005 146 QCILCGRCVEAC-QDIevnetIRIDwDREHPRViwDndvpINESSCVSCGQCATVCP 201
Cdd:cd10564 14 LCTRCGDCVEACpEGI-----IVRG-DGGFPEL--D----FSRGECTFCGACAEACP 58
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| Fer4_6 |
pfam12837 |
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ... |
185-204 |
7.26e-03 |
|
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 432822 [Multi-domain] Cd Length: 24 Bit Score: 34.90 E-value: 7.26e-03
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| ACS_1 |
cd01916 |
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ... |
145-249 |
7.88e-03 |
|
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, 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, CoA, and a methyl group donated by another protein (CoFeSP). ACS has three structural domains, an N-terminal rossman fold domain with a helical region at its N-terminus which interacts with CODH, and two alpha + beta fold domains. A Ni-Fe-S center referred to as the A-cluster is located in the C-terminal domain. A large cavity exists between the three domains which may bind CoA.
Pssm-ID: 238897 [Multi-domain] Cd Length: 731 Bit Score: 40.09 E-value: 7.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686208005 145 NQCILCGRCVEAC-QDIEVNETIRI--DWDREHPRVIWDndvpinesSCVSCGQCATVCPCNAMMeVNMEGNAGYmtdte 221
Cdd:cd01916 365 AKCTDCGWCTRACpNSLRIKEAMEAakEGDFSGLADLFD--------QCVGCGRCEQECPKEIPI-INMIEKAAR----- 430
|
90 100
....*....|....*....|....*...
gi 686208005 222 pgslAAMIDLTKKAEPGYGPlfaISDSE 249
Cdd:cd01916 431 ----ERIKEEKGKMRAGRGP---IKDTE 451
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