|
Name |
Accession |
Description |
Interval |
E-value |
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
6-685 |
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: 1138.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 6 TVCPYCASGCKINLVVDNGKIVRAEAAQG-KTNQGTLCLKGYYGWDFINDTqiltPRLKTPMIRRqrGGKLEAVSWDEAL 84
Cdd:TIGR01591 1 TVCPYCGVGCSLNLVVKDGKIVRVEPYQGhKANRGHLCVKGYFAWEFINSK----DRLTTPLIRE--GDKFREVSWDEAI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 85 DYVATRLSAIKAKYGPDAIQTTGSSRGTgNETNYVMQKFARAVIGTNNVDCCARVUHGPSVAGLHQSVGNGAMSNAITEI 164
Cdd:TIGR01591 75 SYIAEKLKEIKEKYGPDSIGFIGSSRGT-NEENYLLQKLARAVIGTNNVDNCARVCHGPSVAGLKQTVGIGAMSNTISEI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 165 DNTDLVFIFGYNPADSHPIVANHVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAIGHVIIEEDLYDKSF 244
Cdd:TIGR01591 154 ENADLIVIIGYNPAESHPVVAQYLKNAKRNGAKIIVIDPRKTETAKIADLHIPLKPGTDIALLNAMANVIIEEGLYDKAF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 245 VASRSEGFEEYRKIVEGYTPESVEEITGVSAQEIRACARMYASAKSAAILWGMGVTQFYQGVETVRSLTSLAILTGNLGK 324
Cdd:TIGR01591 234 IEKRTEGFEEFREIVKGYTPEYVEDITGVPADLIREAARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 325 PNVGVNPVRGQNNVQGACDMGALPDTYPGYQYVKFPENREKFAKAWGVESLPAHTGYRISELPHRAAHGEVRAAYIMGED 404
Cdd:TIGR01591 314 PGGGVNPLRGQNNVQGACDMGALPDFLPGYQPVSDEEVREKFAKAWGVVKLPAEPGLRIPEMIDAAADGDVKALYIMGED 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 405 PLQTDAELSAVRKAFDDLELVIVQDIFMTKTASAADVILPSTSWGEHEGVYTAADRGFQRFFKAVEPKWDLKTDWQIISE 484
Cdd:TIGR01591 394 PLQSDPNTSKVRKALEKLELLVVQDIFMTETAKYADVVLPAAAWLEKEGTFTNAERRIQRFFKAVEPKGESKPDWEIIQE 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 485 IATRMGYPMHYNNTQEIWDELRHLCPDFYGATYEKMGELGYVMWPCRDEsdADQGTSYLFKEKFDTPNGLAQFFTCDWVA 564
Cdd:TIGR01591 474 LANALGLDWNYNHPQEIMDEIRELTPLFAGLTYERLDELGSLQWPCNDS--DASPTSYLYKDKFATPDGKAKFIPLEWVA 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 565 PIDKLTDEYPMVLSTVREVGHYSCRSMTGNCAALAALADEPgYAQINTADAERLGIEDEELVWVNSRKGRIITRAQVSDR 644
Cdd:TIGR01591 552 PIEEPDDEYPLILTTGRVLTHYNVGEMTRRVAGLRRLSPEP-YVEINTEDAKKLGIKDGDLVKVKSRRGEITLRAKVSDR 630
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1148879094 645 PNKGAVYMTYQWWIGACNELVSENLSPITKTPEYKYCAVNV 685
Cdd:TIGR01591 631 VNKGAIYITMHFWDGAVNNLTTDDLDPISGTPEYKYTAVRI 671
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
1-690 |
0e+00 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 1002.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 1 MKKVVTVCPYCASGCKINLVVDNGKIVRAEA-AQGKTNQGTLCLKGYYGWDFINDTQiltpRLKTPMIRRqrGGKLEAVS 79
Cdd:COG3383 4 MKKVKTVCPYCGVGCGIDLEVKDGKIVKVEGdPDHPVNRGRLCVKGRFGFEFVNSPD----RLTTPLIRR--GGEFREVS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 80 WDEALDYVATRLSAIKAKYGPDAIQTTGSSRGTgNETNYVMQKFARAVIGTNNVDCCARVUHGPSVAGLHQSVGNGAMSN 159
Cdd:COG3383 78 WDEALDLVAERLREIQAEHGPDAVAFYGSGQLT-NEENYLLQKLARGVLGTNNIDNNARLCMASAVAGLKQSFGSDAPPN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 160 AITEIDNTDLVFIFGYNPADSHPIVANHVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAIGHVIIEEDL 239
Cdd:COG3383 157 SYDDIEEADVILVIGSNPAEAHPVLARRIKKAKKNGAKLIVVDPRRTETARLADLHLQIKPGTDLALLNGLLHVIIEEGL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 240 YDKSFVASRSEGFEEYRKIVEGYTPESVEEITGVSAQEIRACARMYASAKSAAILWGMGVTQFYQGVETVRSLTSLAILT 319
Cdd:COG3383 237 VDEDFIAERTEGFEELKASVAKYTPERVAEITGVPAEDIREAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLALAT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 320 GNLGKPNVGVNPVRGQNNVQGACDMGALPDTYPGYQYVKFPENREKFAKAWGVESLPAHTGYRISELPHRAAHGEVRAAY 399
Cdd:COG3383 317 GNIGRPGTGPFPLTGQNNVQGGRDMGALPNVLPGYRDVTDPEHRAKVADAWGVPPLPDKPGLTAVEMFDAIADGEIKALW 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 400 IMGEDPLQTDAELSAVRKAFDDLELVIVQDIFMTKTASAADVILPSTSWGEHEGVYTAADRGFQRFFKAVEPKWDLKTDW 479
Cdd:COG3383 397 IIGENPAVSDPDANHVREALEKLEFLVVQDIFLTETAEYADVVLPAASWAEKDGTFTNTERRVQRVRKAVEPPGEARPDW 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 480 QIISEIATRMGYPMHYNNTQEIWDELRHLCPDFYGATYEKMGELGYVMWPCRDEsdADQGTSYLFKEKFDTPNGLAQFFT 559
Cdd:COG3383 477 EIIAELARRLGYGFDYDSPEEVFDEIARLTPDYSGISYERLEALGGVQWPCPSE--DHPGTPRLFTGRFPTPDGKARFVP 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 560 CDWVAPIDKLTDEYPMVLSTVREVGHYSCRSMTGNCAALAALADEPgYAQINTADAERLGIEDEELVWVNSRKGRIITRA 639
Cdd:COG3383 555 VEYRPPAELPDEEYPLVLTTGRLLDQWHTGTRTRRSPRLNKHAPEP-FVEIHPEDAARLGIKDGDLVRVSSRRGEVVLRA 633
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1148879094 640 QVSDRPNKGAVYMTYQWWIGACNELVSENLSPITKTPEYKYCAVNVERIAD 690
Cdd:COG3383 634 RVTDRVRPGTVFMPFHWGEGAANALTNDALDPVSKQPEYKACAVRVEKVAE 684
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
6-564 |
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: 839.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 6 TVCPYCASGCKINLVVDNGKIVRAEAAQG-KTNQGTLCLKGYYGWDFINDTQiltpRLKTPMIRRqrGGKLEAVSWDEAL 84
Cdd:cd02753 2 TVCPYCGVGCGLELWVKDNKIVGVEPVKGhPVNRGKLCVKGRFGFDFVNSKD----RLTKPLIRK--NGKFVEASWDEAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 85 DYVATRLSAIKAKYGPDAIQTTGSSRGTgNETNYVMQKFARAVIGTNNVDCCARVUHGPSVAGLHQSVGNGAMSNAITEI 164
Cdd:cd02753 76 SLVASRLKEIKDKYGPDAIAFFGSAKCT-NEENYLFQKLARAVGGTNNVDHCARLCHSPTVAGLAETLGSGAMTNSIADI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 165 DNTDLVFIFGYNPADSHPIVANHVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAIGHVIIEEDLYDKSF 244
Cdd:cd02753 155 EEADVILVIGSNTTEAHPVIARRIKRAKRNGAKLIVADPRRTELARFADLHLQLRPGTDVALLNAMAHVIIEEGLYDEEF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 245 VASRSEGFEEYRKIVEGYTPESVEEITGVSAQEIRACARMYASAKSAAILWGMGVTQFYQGVETVRSLTSLAILTGNLGK 324
Cdd:cd02753 235 IEERTEGFEELKEIVEKYTPEYAERITGVPAEDIREAARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 325 PNVGVNPVRGQNNVQGACDMGALPDTYPGYqyvkfpenrekfakawgveslpahtgyriselphraahgeVRAAYIMGED 404
Cdd:cd02753 315 PGTGVNPLRGQNNVQGACDMGALPNVLPGY----------------------------------------VKALYIMGEN 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 405 PLQTDAELSAVRKAFDDLELVIVQDIFMTKTASAADVILPSTSWGEHEGVYTAADRGFQRFFKAVEPKWDLKTDWQIISE 484
Cdd:cd02753 355 PALSDPNTNHVRKALESLEFLVVQDIFLTETAELADVVLPAASFAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIQE 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 485 IATRMGYPMHYNNTQEIWDELRHLCPDFYGATYEKMGELGYVMWPCRDEsdADQGTSYLFKEKFDTPNGLAQFFTCDWVA 564
Cdd:cd02753 435 LANRLGYPGFYSHPEEIFDEIARLTPQYAGISYERLERPGGLQWPCPDE--DHPGTPILHTERFATPDGKARFMPVEYRP 512
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
1-690 |
0e+00 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 604.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 1 MKKVVTVCPYCASGCKINLVVDNGKIVRAEA-AQGKTNQGTLCLKGYYGWDFINDTQiltpRLKTPMIRR-QRG-GKLEA 77
Cdd:COG0243 21 TKTVKTTCPGCGVGCGLGVKVEDGRVVRVRGdPDHPVNRGRLCAKGAALDERLYSPD----RLTYPMKRVgPRGsGKFER 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 78 VSWDEALDYVATRLSAIKAKYGPDAI---QTTGSSRGTGNETNYVMQKFARAvIGTNNVDCCARVUHGPSVAGLHQSVGN 154
Cdd:COG0243 97 ISWDEALDLIAEKLKAIIDEYGPEAVafyTSGGSAGRLSNEAAYLAQRFARA-LGTNNLDDNSRLCHESAVAGLPRTFGS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 155 GAMSNAITEIDNTDLVFIFGYNPADSHPIVANHVINA-KRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAIGHV 233
Cdd:COG0243 176 DKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREAaKKRGAKIVVIDPRRTETAAIADEWLPIRPGTDAALLLALAHV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 234 IIEEDLYDKSFVASRSEGFEEYRKIVEGYTPESVEEITGVSAQEIRACARMYASAKSAAILWGMGVTQFYQGVETVRSLT 313
Cdd:COG0243 256 LIEEGLYDRDFLARHTVGFDELAAYVAAYTPEWAAEITGVPAEDIRELAREFATAKPAVILWGMGLQQHSNGTQTVRAIA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 314 SLAILTGNLGKPNVGVNPVRGQNNVQGacdmgalpDTYPgyqyvkfpenrekfakawgveslpahtgyriselphraahg 393
Cdd:COG0243 336 NLALLTGNIGKPGGGPFSLTGEAILDG--------KPYP----------------------------------------- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 394 eVRAAYIMGEDPLQTDAELSAVRKAFDDLELVIVQDIFMTKTASAADVILPSTSWGEHEGVYTAA-DRGFQRFFKAVEPK 472
Cdd:COG0243 367 -IKALWVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARYADIVLPATTWLERDDIVTNSeDRRVHLSRPAVEPP 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 473 WDLKTDWQIISEIATRMGYPMHYNNTQEIWDELRHLC--PDFYGATYEKMGELGYVMWPCRDEsdadqgTSYLFKEKFDT 550
Cdd:COG0243 446 GEARSDWEIFAELAKRLGFEEAFPWGRTEEDYLRELLeaTRGRGITFEELREKGPVQLPVPPE------PAFRNDGPFPT 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 551 PNGLAQFFTC--------DWVAPI---DKLTDEYPMVLSTVREVGHYScrSMTGNCAALAALADEPgYAQINTADAERLG 619
Cdd:COG0243 520 PSGKAEFYSEtlalpplpRYAPPYegaEPLDAEYPLRLITGRSRDQWH--STTYNNPRLREIGPRP-VVEINPEDAAALG 596
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1148879094 620 IEDEELVWVNSRKGRIITRAQVSDRPNKGAVYMTYQWW-------IGACNELVSENLSPITKTPEYKYCAVNVERIAD 690
Cdd:COG0243 597 IKDGDLVRVESDRGEVLARAKVTEGIRPGVVFAPHGWWyepaddkGGNVNVLTPDATDPLSGTPAFKSVPVRVEKAAA 674
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
6-565 |
3.13e-175 |
|
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: 512.93 E-value: 3.13e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 6 TVCPYCASGCKINLVVDNGKIVRAEA-AQGKTNQGTLCLKGYYGWDFINDTQiltpRLKTPMIRRQrGGKLEAVSWDEAL 84
Cdd:cd02754 2 TTCPYCGVGCGVEIGVKDGKVVAVRGdPEHPVNRGRLCIKGLNLHKTLNGPE----RLTRPLLRRN-GGELVPVSWDEAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 85 DYVATRLSAIKAKYGPDAIQTTGSSRGTgNETNYVMQKFARAVIGTNNVDCCARVUHGPSVAGLHQSVGNGAMSNAITEI 164
Cdd:cd02754 77 DLIAERFKAIQAEYGPDSVAFYGSGQLL-TEEYYAANKLAKGGLGTNNIDTNSRLCMASAVAGYKRSFGADGPPGSYDDI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 165 DNTDLVFIFGYNPADSHPIVANHVINAKRN--GAKIIVCDPRKIETARIADMHIALKNGSNIALLNAIGHVIIEEDLYDK 242
Cdd:cd02754 156 EHADCFFLIGSNMAECHPILFRRLLDRKKAnpGAKIIVVDPRRTRTADIADLHLPIRPGTDLALLNGLLHVLIEEGLIDR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 243 SFVASRSEGFEEYRKIVEGYTPESVEEITGVSAQEIRACARMYASAKSAAILWGMGVTQFYQGVETVRSLTSLAILTGNL 322
Cdd:cd02754 236 DFIDAHTEGFEELKAFVADYTPEKVAEITGVPEADIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHLATGKI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 323 GKPNVGVNPVRGQNNVQGACDMGALPDTYPGYQYVKFPENREKFAKAWGV--ESLPAHTGYRISELPHRAAHGEVRAAYI 400
Cdd:cd02754 316 GRPGSGPFSLTGQPNAMGGREVGGLANLLPGHRSVNNPEHRAEVAKFWGVpeGTIPPKPGLHAVEMFEAIEDGEIKALWV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 401 MGEDPLQTDAELSAVRKAFDDLELVIVQDIF-MTKTASAADVILPSTSWGEHEGVYTAADRGFQRFFKAVEPKWDLKTDW 479
Cdd:cd02754 396 MCTNPAVSLPNANRVREALERLEFVVVQDAFaDTETAEYADLVLPAASWGEKEGTMTNSERRVSLLRAAVEPPGEARPDW 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 480 QIISEIATRMGYPM--HYNNTQEIWDELRHLCP----DFYGATYEKMGELGyVMWPCRDEsdADQGTSYLF-KEKFDTPN 552
Cdd:cd02754 476 WILADVARRLGFGElfPYTSPEEVFEEYRRLSRgrgaDLSGLSYERLRDGG-VQWPCPDG--PPEGTRRLFeDGRFPTPD 552
|
570
....*....|...
gi 1148879094 553 GLAQFFTCDWVAP 565
Cdd:cd02754 553 GRARFVAVPYRPP 565
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
6-489 |
2.49e-133 |
|
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: 398.24 E-value: 2.49e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 6 TVCPYCASGCKINLVVDNGKIVRAEA-AQGKTNQGTLCLKGYYGWDFINDTQiltpRLKTPMIRRQRGGKLEAVSWDEAL 84
Cdd:cd00368 2 SVCPFCGVGCGILVYVKDGKVVRIEGdPNHPVNEGRLCDKGRAGLDGLYSPD----RLKYPLIRVGGRGKFVPISWDEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 85 DYVATRLSAIKAKYGPDAIQTtGSSRGTGNETNYVMQKFARAvIGTNNVDCCARVUHGPSVAGLhQSVGNGAMSNAITEI 164
Cdd:cd00368 78 DEIAEKLKEIREKYGPDAIAF-YGGGGASNEEAYLLQKLLRA-LGSNNVDSHARLCHASAVAAL-KAFGGGAPTNTLADI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 165 DNTDLVFIFGYNPADSHPIVANHVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAighviieedlydksf 244
Cdd:cd00368 155 ENADLILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRRTETAAKADEWLPIRPGTDAALALA--------------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 245 vasrsegfeeyrkivegytpESVEEITGVSAQEIRACARMYASAKSAAILWGMGVTQFYQGVETVRSLTSLAILTGNLGK 324
Cdd:cd00368 220 --------------------EWAAEITGVPAETIRALAREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGR 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 325 PNVGVNPvrgqnnvqgacdmgalpdtypgyqyvkfpenrekfakawgveslpahtgyriselphraahgevraayimGED 404
Cdd:cd00368 280 PGGGLGP----------------------------------------------------------------------GGN 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 405 PLQTDAELSAVRKAFDDLELVIVQDIFMTKTASAADVILPSTSWGEHEGVYTAADRGFQRFFKAVEPKWDLKTDWQIISE 484
Cdd:cd00368 290 PLVSAPDANRVRAALKKLDFVVVIDIFMTETAAYADVVLPAATYLEKEGTYTNTEGRVQLFRQAVEPPGEARSDWEILRE 369
|
....*
gi 1148879094 485 IATRM 489
Cdd:cd00368 370 LAKRL 374
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
6-490 |
4.33e-113 |
|
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: 355.55 E-value: 4.33e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 6 TVCPYCASGCKINLVVDNGKIVRAE-AAQGKTNQGTLCLKGYYGWDFINDTQiltpRLKTPMIRRQRGGKLEAVSWDEAL 84
Cdd:cd02752 2 TICPYCSVGCGLIAYVQNGVWVHQEgDPDHPVNRGSLCPKGAALRDFVHSPK----RLKYPMYRAPGSGKWEEISWDEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 85 DYVATRLSAIKAK------------YGPDAIQTTGSSrGTGNETNYVMQKFARAvIGTNNVDCCARVUHGPSVAGLHQSV 152
Cdd:cd02752 78 DEIARKMKDIRDAsfveknaagvvvNRPDSIAFLGSA-KLSNEECYLIRKFARA-LGTNNLDHQARIUHSPTVAGLANTF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 153 GNGAMSNAITEIDNTDLVFIFGYNPADSHPIVANHVINAK-RNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAIG 231
Cdd:cd02752 156 GRGAMTNSWNDIKNADVILVMGGNPAEAHPVSFKWILEAKeKNGAKLIVVDPRFTRTAAKADLYVPIRSGTDIAFLGGMI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 232 HVIIEedlydksfvasrsegfeeyrkivegYTPESVEEITGVSAQEIRACARMYAS----AKSAAILWGMGVTQFYQGVE 307
Cdd:cd02752 236 NYIIR-------------------------YTPEEVEDICGVPKEDFLKVAEMFAAtgrpDKPGTILYAMGWTQHTVGSQ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 308 TVRSLTSLAILTGNLGKPNVGVNPVRGQNNVQGACDMGALPDTYPGyqyvkfpenrekfakawgveslpahtgyriselp 387
Cdd:cd02752 291 NIRAMCILQLLLGNIGVAGGGVNALRGHSNVQGATDLGLLSHNLPG---------------------------------- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 388 hraahgevraaYIMGEDPLQTDAELSAVRKAFDDLELVIVQDIFMTKTASAAD-------------VILPSTSWGEHEGV 454
Cdd:cd02752 337 -----------YLGGQNPNSSFPNANKVRRALDKLDWLVVIDPFPTETAAFWKnpgmdpksiqtevFLLPAACQYEKEGS 405
|
490 500 510
....*....|....*....|....*....|....*.
gi 1148879094 455 YTAADRGFQRFFKAVEPKWDLKTDWQIISEIATRMG 490
Cdd:cd02752 406 ITNSGRWLQWRYKVVEPPGEAKSDGDILVELAKRLG 441
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
61-488 |
5.96e-109 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 334.75 E-value: 5.96e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 61 RLKTPMIRRQRGgKLEAVSWDEALDYVATRLSAIKAKYGPDAIQT-TGSSRGTGNETNYVMQKFARAVIGTN--NVDCCA 137
Cdd:pfam00384 1 RLKYPMVRRGDG-KFVRVSWDEALDLIAKKLKRIIKKYGPDAIAInGGSGGLTDVESLYALKKLLNRLGSKNgnTEDHNG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 138 RVUHGPSVAGLHQSVGNGAMSNAITEIDNTDLVFIFGYNPADSHPIVANHVINA-KRNGAKIIVCDPRKieTARIADMHI 216
Cdd:pfam00384 80 DLCTAAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRKAaLKGKAKVIVIGPRL--DLTYADEHL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 217 ALKNGSNIALLNAIGHVIIEEDLYDKSFvasrsegfeeyrkivegytpesveeitgvsaqeiracarmyasAKSAAILWG 296
Cdd:pfam00384 158 GIKPGTDLALALAGAHVFIKELKKDKDF-------------------------------------------APKPIIIVG 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 297 MGVTQFYQGVETVRSLTSLAILTGNLGKPNVGVNPVrgqNNVQG-ACDMGALpdtypgyqyvkfpenrekfakawgveSL 375
Cdd:pfam00384 195 AGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGL---NILQGaASPVGAL--------------------------DL 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 376 PAHTGYRISELPHRAAHGEVRAAYIMGEDPLQTDAELSAVRKAFDDLELVIVQDIFM-TKTASAADVILPSTSWGEHEGV 454
Cdd:pfam00384 246 GLVPGIKSVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFVVYDGHHgDKTAKYADVILPAAAYTEKNGT 325
|
410 420 430
....*....|....*....|....*....|....
gi 1148879094 455 YTAADRGFQRFFKAVEPKWDLKTDWQIISEIATR 488
Cdd:pfam00384 326 YVNTEGRVQSTKQAVPPPGEAREDWKILRALSEV 359
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
5-558 |
1.09e-89 |
|
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: 289.53 E-value: 1.09e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 5 VTVCPY-CASGCKINLVVDNGKIVRAEA-AQGKTNQGTLCLKGYYgwdFINDTQilTP-RLKTPMIRRQR-GGKLEAVSW 80
Cdd:cd02766 1 RSVCPLdCPDTCSLLVTVEDGRIVRVEGdPAHPYTRGFICAKGAR---YVERVY--SPdRLLTPLKRVGRkGGQWERISW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 81 DEALDYVATRLSAIKAKYGPDAIQTTGSSRGTGNETNYVMQKFARAvIGTNNVDccARVUHGPSVAGLHQSVGNgAMSNA 160
Cdd:cd02766 76 DEALDTIAAKLKEIKAEYGPESILPYSYAGTMGLLQRAARGRFFHA-LGASELR--GTICSGAGIEAQKYDFGA-SLGND 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 161 ITEIDNTDLVFIFGYNPADSHPIVANHVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAIGHVIIEEDLY 240
Cdd:cd02766 152 PEDMVNADLIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDPYRTATAARADLHIQIRPGTDGALALGVAKVLFREGLY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 241 DKSFVASRSEGFEEYRKIVEGYTPESVEEITGVSAQEIRACARMYASAKSAAILWGMGVTQFYQGVETVRSLTSLAILTG 320
Cdd:cd02766 232 DRDFLARHTEGFEELKAHLETYTPEWAAEITGVSAEEIEELARLYGEAKPPSIRLGYGMQRYRNGGQNVRAIDALPALTG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 321 NLGKPNVGVNpvrgqnnvqgacdmgalpdtypgyqyvkfpenrekfakawgveslpahtgYRISELPhraahgeVRAAYI 400
Cdd:cd02766 312 NIGVPGGGAF--------------------------------------------------YSNSGPP-------VKALWV 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 401 MGEDPLQTDAELSAVRK-AFDDLELVIVQDIFMTKTASAADVILPSTSWGEHEGVYTA-ADRGFQRFFKAVEPKWDLKTD 478
Cdd:cd02766 335 YNSNPVAQAPDSNKVRKgLAREDLFVVVHDQFMTDTARYADIVLPATTFLEHEDVYASyWHYYLQYNEPAIPPPGEARSN 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 479 WQIISEIATRMGY---PMHYNNTQEIWDELRHLCPDFYGATYEKmgELGYVMWPCRDESDADqgtsylfkEKFDTPNGLA 555
Cdd:cd02766 415 TEIFRELAKRLGFgepPFEESDEEWLDQALDGTGLPLEGIDLER--LLGPRKAGFPLVAWED--------RGFPTPSGKF 484
|
...
gi 1148879094 556 QFF 558
Cdd:cd02766 485 EFY 487
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
5-491 |
5.20e-87 |
|
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: 281.89 E-value: 5.20e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 5 VTVCPYCASGCKINLVVDNGKIVRAEA-AQGKTNQGTLCLKGyygwdFINDTQILTP-RLKTPMIR-RQRG-GKLEAVSW 80
Cdd:cd02759 1 KGTCPGCHSGCGVLVYVKDGKLVKVEGdPNHPTNKGRLCMRG-----LAAPEIVYHPdRLLYPLKRvGERGeNKWERISW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 81 DEALDYVATRLSAIKAKYGPDAIqttGSSRGTGNETNYVMQKFARAVI---GTNNVDCCARVUHGPSVAGLHQSVGNGAm 157
Cdd:cd02759 76 DEALDEIAEKLAEIKAEYGPESI---ATAVGTGRGTMWQDSLFWIRFVrlfGSPNLFLSGESCYWPRDMAHALTTGFGL- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 158 SNAITEIDNTDLVFIFGYNPADSHPI-VANHVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAIGHVIIE 236
Cdd:cd02759 152 GYDEPDWENPECIVLWGKNPLNSNLDlQGHWLVAAMKRGAKLIVVDPRLTWLAARADLWLPIRPGTDAALALGMLNVIIN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 237 EDLYDKSFVASRSEGFEEYRKIVEGYTPESVEEITGVSAQEIRACARMYASAKSAAILWGMGVTQFYQGVETVRSLTSLA 316
Cdd:cd02759 232 EGLYDKDFVENWCYGFEELAERVQEYTPEKVAEITGVPAEKIRKAARLYATAKPACIQWGLAIDQQKNGTQTSRAIAILR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 317 ILTGNLGKPNVGVNpvrgqnnvqgacdmgaLPdtYPgyqyvkfpenrekfakawgveslpahtgyriselphraahgeVR 396
Cdd:cd02759 312 AITGNLDVPGGNLL----------------IP--YP------------------------------------------VK 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 397 AAYIMGEDPLQTDAELSAVRKAFDDLELVIVQDIFMTKTASAADVILPSTSWGEHEGVYTAADRG--FQRFFKAVEPKWD 474
Cdd:cd02759 332 MLIVFGTNPLASYADTAPVLEALKALDFIVVVDLFMTPTAMLADIVLPVAMSLERPGLRGGFEAEnfVQLRQKAVEPYGE 411
|
490
....*....|....*..
gi 1148879094 475 LKTDWQIISEIATRMGY 491
Cdd:cd02759 412 AKSDYEIVLELGKRLGP 428
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
61-444 |
1.23e-84 |
|
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: 278.42 E-value: 1.23e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 61 RLKTPMIRRQRGGKLEAVSWDEALDYVATRLSAIKakygPDAIQTTGSSRGTgNETNYVMQKFARAvIGTNNVDCCARVU 140
Cdd:cd02767 64 RLTYPMRYDAGSDHYRPISWDEAFAEIAARLRALD----PDRAAFYTSGRAS-NEAAYLYQLFARA-YGTNNLPDCSNMC 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 141 HGPSVAGLHQSVGNGAMSNAITEIDNTDLVFIFGYNPADSHPIVANHVINAKRNGAKIIVCDPRKiETA----------- 209
Cdd:cd02767 138 HEPSSVGLKKSIGVGKGTVSLEDFEHTDLIFFIGQNPGTNHPRMLHYLREAKKRGGKIIVINPLR-EPGlerfanpqnpe 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 210 -------RIADMHIALKNGSNIALLNAIGHVIIEED-----LYDKSFVASRSEGFEEYRKIVEGYTPESVEEITGVSAQE 277
Cdd:cd02767 217 smltggtKIADEYFQVRIGGDIALLNGMAKHLIERDdepgnVLDHDFIAEHTSGFEEYVAALRALSWDEIERASGLSREE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 278 IRACARMYASAKSAAILWGMGVTQFYQGVETVRSLTSLAILTGNLGKPNVGVNPVRGQNNVQGACDMGAlpdtypgyqYV 357
Cdd:cd02767 297 IEAFAAMYAKSERVVFVWGMGITQHAHGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQGDRTMGI---------TE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 358 K-FPENREKFAKAWGVEsLPAHTGYRISELPHRAAHGEVRAAYIMGEDPLQTDAELSAVRKAFDDLELVIVQDIF----M 432
Cdd:cd02767 368 KpFPEFLDALEEVFGFT-PPRDPGLDTVEAIEAALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLTVHVATKlnrsH 446
|
410
....*....|..
gi 1148879094 433 TKTASAAdVILP 444
Cdd:cd02767 447 LVHGEEA-LILP 457
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
4-490 |
1.27e-71 |
|
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: 240.28 E-value: 1.27e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 4 VVTVCPYCASGCKINLVVDNGKIVRAEA-AQGKTNQGTLCLKGYYGWDFINDTQiltpRLKTPMIR-RQRG-GKLEAVSW 80
Cdd:cd02755 1 VPSICEMCSSRCGILARVEDGRVVKIDGnPLSPLSRGKLCARGNAGIQLLYDPD----RLKKPLIRvGERGeGKFREASW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 81 DEALDYVATRLSAIKAKYGPDAIqtTGSSRGTGNETnyVMQKFARAvIGTNNVDCCARVUHGPSVAGLhQSVGNGAMSNA 160
Cdd:cd02755 77 DEALQYIASKLKEIKEQHGPESV--LFGGHGGCYSP--FFKHFAAA-FGSPNIFSHESTCLASKNLAW-KLVIDSFGGEV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 161 ITEIDNTDLVFIFGYNPADS-HPIVANHVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAIGHVIIEEDL 239
Cdd:cd02755 151 NPDFENARYIILFGRNLAEAiIVVDARRLMKALENGAKVVVVDPRFSELASKADEWIPIKPGTDLAFVLALIHVLISENL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 240 YDKSFVASRSEGFEEYRKIVEGYTPESVEEITGVSAQEIRACARMYASAKSAAILWGMGVTQFY-QGVETVRSLTSLAIL 318
Cdd:cd02755 231 YDAAFVEKYTNGFELLKAHVKPYTPEWAAQITDIPADTIRRIAREFAAAAPHAVVDPGWRGTFYsNSFQTRRAIAIINAL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 319 TGNLGKPnvgvnpvrgqnnvqGACDMGALPDTYPgyqyvkfpenrekfakawgveslpahtgyriselphraahgeVRAA 398
Cdd:cd02755 311 LGNIDKR--------------GGLYYAGSAKPYP------------------------------------------IKAL 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 399 YIMGEDPLQTDAELSAVRKAFDDLELVIVQDIFMTKTASAADVILPSTSWGEHEGVYT----AADRGFQRfFKAVEPKWD 474
Cdd:cd02755 335 FIYRTNPFHSMPDRARLIKALKNLDLVVAIDILPSDTALYADVILPEATYLERDEPFSdkggPAPAVATR-QRAIEPLYD 413
|
490
....*....|....*.
gi 1148879094 475 LKTDWQIISEIATRMG 490
Cdd:cd02755 414 TRPGWDILKELARRLG 429
|
|
| formate-DH-alph |
TIGR01553 |
formate dehydrogenase-N alpha subunit; This model describes a subset of formate dehydrogenase ... |
2-489 |
2.11e-71 |
|
formate dehydrogenase-N alpha subunit; This model describes a subset of formate dehydrogenase alpha chains found mainly in proteobacteria but also in Aquifex. 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 of 32 and 20 kDa. 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 electrons are utilized mainly in the nitrate respiration by nitrate reductase. In E. coli and Salmonella, there are two forms of the formate dehydrogenase, one induced by nitrate which is strictly anaerobic (fdn), and one incuced during the transition from aerobic to anaerobic growth (fdo). This subunit is one of only three proteins in E. coli which contain selenocysteine. This model is well-defined, with a large, unpopulated trusted/noise gap. [Energy metabolism, Anaerobic, Energy metabolism, Electron transport]
Pssm-ID: 273689 [Multi-domain] Cd Length: 1009 Bit Score: 251.37 E-value: 2.11e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 2 KKVVTVCPYCASGCKINL--VVDNGKIVRAEA--AQGK----TNQGTLCLKGYYGWDFINDTQiltpRLKTPMIRRQRGG 73
Cdd:TIGR01553 43 KQTTSVCCYCSVSCGLLVysSSHTGDNKTNRAihVEGDpdhpINRGSLCPKGASTWDLVNNER----RPANPLYRAPGSD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 74 KLEAVSWDEALDYVATRLS-------AIKAKYGP-----DAIQTTGSSrGTGNETNYVMQKFARAvIGTNNVDCCARVUH 141
Cdd:TIGR01553 119 QWEEISWDWAIDTIARRVKdtrdatfVTKDAKGQvvnrcDGIASVGSS-AMDNEECWLYQKWLRS-LGLFYIEHQARIUH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 142 GPSVAGLHQSVGNGAMSNAITEIDNTDLVFIFGYNPADSHPIVANHVINAKRNGAKIIVCDPRKIETARIADMHIALKNG 221
Cdd:TIGR01553 197 SPTVASLAPSFGRGAMTNNWVDIKNSDLILVMGGNPAENHPIGFKWAIRAKKKGAKIIHIDPRFNRTATVADLYAPIRSG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 222 SNIALLNAIGHVIIEEDLYDKSFVASRS-------EGF-----------EEYRKI------------------------- 258
Cdd:TIGR01553 277 SDIAFLNGMIKYILEKELYQKEYVVNYTnasfivgEGFafedglfagynKETRKYdkskwgyefdengnpkrdetlkhpr 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 259 ---------VEGYTPESVEEITGVSAQEIRACARMYASA----KSAAILWGMGVTQFYQGVETVRSLTSLAILTGNLGKP 325
Cdd:TIGR01553 357 cvfnilkehYSRYTPEKVSAICGTPKELFLKVYEEYCKTgkpnKAMTILYALGWTQHSVGTQNIRAMSINQLLLGNIGVP 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 326 NVGVNPVRGQNNVQGACDMGALPDTYPGY------------QYVK-----------------FPENREKFAKA------- 369
Cdd:TIGR01553 437 GGGINALRGHSNVQGSTDHGLLMHILPGYlgtprasiptyeQYTKkftpvskdpqsanywsnFPKFFASYIKSmwgdaat 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 370 ----WGVESLPAHTGYRISELPH--RAAHGEVRAAYIMGEDPLQTDAELSAVRKAFDDLELVIVQDIFMTKTAS---AAD 440
Cdd:TIGR01553 517 nengWAYDYLPKGEDGYDSWLTLfdDMFQGKIKGFFAWGQNPLNSGPNSNKTREALTKLKWMVVMDPFDNETGSfwrGPG 596
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1148879094 441 V----------ILPSTSWGEHEGVYTAADRGFQRFFKAVEPKWDLKTDWQIISEIATRM 489
Cdd:TIGR01553 597 MdpkeiktevfFLPTAVFIEKEGSISNSGRWMQWRYKGPDPPGNAIPDGDIIVELAKRV 655
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
6-489 |
4.64e-70 |
|
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: 238.45 E-value: 4.64e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 6 TVCPYCASGCKINLVVDNGKIVRAEAAQGKT-NQGTLCLKGYYGWDFINDTQiltpRLKTPMIRRqrGGKLEAVSWDEAL 84
Cdd:cd02762 2 RACILCEANCGLVVTVEDGRVASIRGDPDDPlSKGYICPKAAALGDYQNDPD----RLRTPMRRR--GGSFEEIDWDEAF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 85 DYVATRLSAIKAKYGPDAIqttGSSRGTGNETNYVMQKFARAV---IGTNNVDCCARVUHGPSVAGLHQSVGNGaMSNAI 161
Cdd:cd02762 76 DEIAERLRAIRARHGGDAV---GVYGGNPQAHTHAGGAYSPALlkaLGTSNYFSAATADQKPGHFWSGLMFGHP-GLHPV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 162 TEIDNTDLVFIFGYNPADSH------PIVANHVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAIGHVII 235
Cdd:cd02762 152 PDIDRTDYLLILGANPLQSNgslrtaPDRVLRLKAAKDRGGSLVVIDPRRTETAKLADEHLFVRPGTDAWLLAAMLAVLL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 236 EEDLYDKSFVASRSEGFEEYRKIVEGYTPESVEEITGVSAQEIRACARMYASAKSAAILWGMGVTQFYQGVETVRSLTSL 315
Cdd:cd02762 232 AEGLTDRRFLAEHCDGLDEVRAALAEFTPEAYAPRCGVPAETIRRLAREFAAAPSAAVYGRLGVQTQLFGTLCSWLVKLL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 316 AILTGNLGKPNvgvnpvrGQNNVQGACDmgalpdtypgyqYVKFPENREKFAKAW--GVESLPAHTG-YRISELPH---R 389
Cdd:cd02762 312 NLLTGNLDRPG-------GAMFTTPALD------------LVGQTSGRTIGRGEWrsRVSGLPEIAGeLPVNVLAEeilT 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 390 AAHGEVRAAYIMGEDPLQTDAELSAVRKAFDDLELVIVQDIFMTKTASAADVILPSTSWGEHE---GVYTAADRGFQRFF 466
Cdd:cd02762 373 DGPGRIRAMIVVAGNPVLSAPDGARLEAALGGLEFMVSVDVYMTETTRHADYILPPASQLEKPhatFFNLEFPRNAFRYR 452
|
490 500
....*....|....*....|....
gi 1148879094 467 KA-VEPKWDLKTDWQIISEIATRM 489
Cdd:cd02762 453 RPlFPPPPGTLPEWEILARLVEAL 476
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
11-523 |
1.24e-69 |
|
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: 239.53 E-value: 1.24e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 11 CASGCKINLVVDNGKIVRAEAAQGKTNQGTL-----CLKG------YYGWDfindtqiltpRLKTPMIRR-QRG-GKLEA 77
Cdd:cd02770 8 CGGRCPLKAHVKDGVITRIETDDTGDDDPGFhqiraCLRGrsqrkrVYNPD----------RLKYPMKRVgKRGeGKFVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 78 VSWDEALDYVATRLSAIKAKYGPDAIQTTGSSRGTGNETNYvMQKFAR--AVIGT-----NNVdccarvuhgpSVAGLHQ 150
Cdd:cd02770 78 ISWDEALDTIASELKRIIEKYGNEAIYVNYGTGTYGGVPAG-RGAIARllNLTGGylnyyGTY----------SWAQITT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 151 SV----GNGAMSNAITEIDNTDLVFIFGYNPADSHPIVANHVIN---AKRNGAKIIVCDPRKIETAR-IADMHIALKNGS 222
Cdd:cd02770 147 ATpytyGAAASGSSLDDLKDSKLVVLFGHNPAETRMGGGGSTYYylqAKKAGAKFIVIDPRYTDTAVtLADEWIPIRPGT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 223 NIALLNAIGHVIIEEDLYDKSFVASRSEGFEE------------YRKIVEGY-------TPESVEEITGVSAQEIRACAR 283
Cdd:cd02770 227 DAALVAAMAYVMITENLHDQAFLDRYCVGFDAehlpegappnesYKDYVLGTgydgtpkTPEWASEITGVPAETIRRLAR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 284 MYASAKSAAILWGMGVTQFYQGVETVRSLTSLAILTGNLGKPNVGVNPVRGQNNVQGAcdmgALP-------DTYPGYQY 356
Cdd:cd02770 307 EIATTKPAAILQGWGPQRHANGEQAARAIMMLAAMTGNVGIPGGNTGARPGGSAYNGA----GLPagknpvkTSIPCFMW 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 357 VKFPENREKFAKAWGVESLPAHTGYRISELPHRAAHgevraaYIMGedplQTDAELSAVRKAFDD---LELVIVQDIFMT 433
Cdd:cd02770 383 TDAIERGEEMTADDGGVKGADKLKSNIKMIWNYAGN------TLIN----QHSDDNNTTRALLDDeskCEFIVVIDNFMT 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 434 KTASAADVILPSTSWGEHEGVYTAADRG----FQRFFKAVEPKWDLKTDWQIISEIATRMGYPMHYNN--TQEIWdeLRH 507
Cdd:cd02770 453 PSARYADILLPDTTELEREDIVLTSNAGmmeyLIYSQKAIEPLYECKSDYEICAELAKRLGVEDQFTEgkTEQEW--LEE 530
|
570
....*....|....*.
gi 1148879094 508 LcpdfYGATYEKMGEL 523
Cdd:cd02770 531 L----YGQTRAKEPGL 542
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
15-524 |
1.60e-69 |
|
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: 238.67 E-value: 1.60e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 15 CKINLVVDNGKIVRAEAAQGKTNQGTLCLKGYYGWDFINDtqiltpRLKTPMIRR-----------QRG-GKLEAVSWDE 82
Cdd:cd02751 7 GPFKAHVKDGVIVRVEPDDTDQPRPCPRGRSVRDRVYSPD------RIKYPMKRVgwlgngpgsreLRGeGEFVRISWDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 83 ALDYVATRLSAIKAKYGPDAI---QTTGSSRGTGNETNYVMQKFArAVIG--TNNVD----CCARVUhGPSVAGlhqSVG 153
Cdd:cd02751 81 ALDLVASELKRIREKYGNEAIfggSYGWASAGRLHHAQSLLHRFL-NLIGgyLGSYGtystGAAQVI-LPHVVG---SDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 154 NGAMSNAITEI-DNTDLVFIFGYNPAD---SHPIVANHVIN-----AKRNGAKIIVCDPRKIETAR-IADMHIALKNGSN 223
Cdd:cd02751 156 VYEQGTSWDDIaEHSDLVVLFGANPLKtrqGGGGGPDHGSYyylkqAKDAGVRFICIDPRYTDTAAvLAAEWIPIRPGTD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 224 IALLNAIGHVIIEEDLYDKSFVASRSEGFEEYRKIVEGY------TPESVEEITGVSAQEIRACARMYASaKSAAILWGM 297
Cdd:cd02751 236 VALMLAMAHTLITEDLHDQAFLARYTVGFDEFKDYLLGEsdgvpkTPEWAAEITGVPAETIRALAREIAS-KRTMIAQGW 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 298 GVTQFYQGVETVRSLTSLAILTGNLGKPNVGVNPVRGQNNVQGAcdmGALPDTYPGYQYVKFPenrekfakawGVESLPA 377
Cdd:cd02751 315 GLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGYGYSNGGGP---PRGGAGGPGLPQGKNP----------VKDSIPV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 378 htgYRISEL------PHRAAHGE-----VRAAYIMGEDPL--QTDaeLSAVRKAFDDLELVIVQDIFMTKTASAADVILP 444
Cdd:cd02751 382 ---ARIADAllnpgkEFTANGKLktypdIKMIYWAGGNPLhhHQD--LNRLIKALRKDETIVVHDIFWTASARYADIVLP 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 445 STSWGEHEGVYTAADRGFQRFF---KAVEPKWDLKTDWQIISEIATRMGYPMHYNNTQEIWDELRHlcpdFYGATYEKMG 521
Cdd:cd02751 457 ATTSLERNDIGLTGNYSNRYLIamkQAVEPLGEARSDYEIFAELAKRLGVEEEFTEGRDEMEWLEH----LYEETRAKAA 532
|
...
gi 1148879094 522 ELG 524
Cdd:cd02751 533 GPG 535
|
|
| 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 ... |
6-490 |
1.57e-68 |
|
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: 232.66 E-value: 1.57e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 6 TVCPYCASGCKINLVVDNGKIVRAEAA-QGKTNQGTLCLKGYYGWDFINdtqiLTPRLKTPMIRRqrGGKLEAVSWDEAL 84
Cdd:cd02771 2 SICHHCSVGCNISLGERYGELRRVENRyNGAVNHYFLCDRGRFGYGYVN----SRDRLTQPLIRR--GGTLVPVSWNEAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 85 DYVATRLSAIKakygpDAIQTTGSSRGTgNETNYVMQKFARAVIGTNNVDCCARVUHGPSVAGlhqsvgNGAMSNAITEI 164
Cdd:cd02771 76 DVAAARLKEAK-----DKVGGIGSPRAS-NESNYALQKLVGAVLGTNNVDHRARRLIAEILRN------GPIYIPSLRDI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 165 DNTDLVFIFGYNPADSHPIVANHVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAIGHVIieEDLYDKSF 244
Cdd:cd02771 144 ESADAVLVLGEDLTQTAPRIALALRQAARRKAVELAALSGIPKWQDAAVRNIAQGAKSPLFIVNALATRL--DDIAAESI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 245 VASRSEGFEEYRKIVEGYTPESVEEITGVSAQEIRACARMYASAKSAAILWGMGVtqfyQGVETVRSLTSLAILTGNLGK 324
Cdd:cd02771 222 RASPGGQARLGAALARAVDASAAGVSGLAPKEKAARIAARLTGAKKPLIVSGTLS----GSLELIKAAANLAKALKRRGE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 325 pNVGVNPVRGQNNVQGACDMGALPDtypgyqyvkfpenrEKFAKAWGVeslpahtgyriselPHRAAHGEVRAAYIMGED 404
Cdd:cd02771 298 -NAGLTLAVEEGNSPGLLLLGGHVT--------------EPGLDLDGA--------------LAALEDGSADALIVLGND 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 405 PLQTdAELSAVRKAFDDLELVIVQDIFMTKTASAADVILPSTSWGEHEGVYTAADRGFQRFFKAV-EPKWDLKTDWQIIS 483
Cdd:cd02771 349 LYRS-APERRVEAALDAAEFVVVLDHFLTETAERADVVLPAASFAEKSGTFVNYEGRAQRFFKAYdDPAGDARSDWRWLH 427
|
....*..
gi 1148879094 484 EIATRMG 490
Cdd:cd02771 428 ALAAKLG 434
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
2-652 |
7.17e-67 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 234.95 E-value: 7.17e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 2 KKVVTVCPYCASGCKINLVVDNGKIVRAEA-AQGKTNQGTLCLKGYYGWDFINDTQiltpRLKTPMIRR-QRG-GKLEAV 78
Cdd:PRK15488 42 KLTPSICEMCSTRCPIEARVVNGKNVFIQGnPKAKSFGTKVCARGGSGHSLLYDPQ----RIVKPLKRVgERGeGKWQEI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 79 SWDEALDYVATRLSAIKAKYGPDAIQTTGSSrgtgNETNYVMQKFARAvIGTNNVdccarVUHGPSVAGLHQSVGNGAMS 158
Cdd:PRK15488 118 SWDEAYQEIAAKLNAIKQQHGPESVAFSSKS----GSLSSHLFHLATA-FGSPNT-----FTHASTCPAGYAIAAKVMFG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 159 NAIT-EIDNTDLVFIFGYN------PADSHPIVANhvinAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAIG 231
Cdd:PRK15488 188 GKLKrDLANSKYIINFGHNlyeginMSDTRGLMTA----QMEKGAKLVVFEPRFSVVASKADEWHAIRPGTDLAVVLALC 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 232 HVIIEEDLYDKSFVASRSEGFEEYRKIVEGYTPESVEEITGVSAQEIRACARMYASAKSAAIL-WGMGVTQFYQGVETVR 310
Cdd:PRK15488 264 HVLIEENLYDKAFVERYTSGFEELAASVKEYTPEWAEAISDVPADDIRRIARELAAAAPHAIVdFGHRATFTPEEFDMRR 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 311 SLTSLAILTGN--------LGKPNVGVNPVRGQNNVQGACDMGalPDTYPGYQYVKFPENREKFAKAWG----VESLPAH 378
Cdd:PRK15488 344 AIFAANVLLGNierkgglyFGKNASVYNKLAGEKVAPTLAKPG--VKGMPKPTAKRIDLVGEQFKYIAAgggvVQSIIDA 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 379 TgyrISELPHraahgEVRAAYIMGEDPLQTDAELSAVRKAFDDLELVIVQDIFMTKTASAADVILPSTSWGEH-EGVytA 457
Cdd:PRK15488 422 T---LTQKPY-----QIKGWVMSRHNPMQTVTDRADVVKALKKLDLVVVCDVYLSESAAYADVVLPESTYLERdEEI--S 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 458 ADRGFQRFF----KAVEPKWDLKTDWQIISEIATRMGYPMHY--NNTQEIwdELRHLCPDFygATYEKMGELGYVMW--P 529
Cdd:PRK15488 492 DKSGKNPAYalrqRVVEPIGDTKPSWQIFKELGEKMGLGQYYpwQDMETL--QLYQVNGDH--ALLKELKKKGYVSFgvP 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 530 C--RDESD-------------ADQGTSYLFKEKFDTPNGLAQFFTCDWVA-----------PIDkLTDEYPMVL----ST 579
Cdd:PRK15488 568 LllREPKMvakfvarypnakaVDEDGTYGSQLKFKTPSGKIELFSAKLEAlapgygvpryrDVA-LKKEDELYFiqgkVA 646
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1148879094 580 VREVGHyscrsmTGNCAALAAL-ADEPGYAQINTadAERLGIEDEELVWVNSRKGRIITRAQVSD--RPNKGAVYM 652
Cdd:PRK15488 647 VHTNGA------TQNVPLLANLmSDNAVWIHPQT--AGKLGIKNGDEIRLENSVGKEKGKALVTPgiRPDTLFAYM 714
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
7-687 |
1.62e-65 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 232.10 E-value: 1.62e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 7 VCPYCASGCKINLVVDNGKIVraeAAQG----KTNQGTLCLKGY------YGWDfindtqiltpRLKTPMIRRQRG---- 72
Cdd:PRK13532 46 PCRFCGTGCGVLVGTKDGRVV---ATQGdpdaPVNRGLNCIKGYflskimYGKD----------RLTQPLLRMKDGkydk 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 73 -GKLEAVSWDEALDYVATRL-SAIKAKyGPDAIQTTGSSRGTGNEtNYVMQKFARAVIGTNNVDCCARVUHGPSVAGLHQ 150
Cdd:PRK13532 113 eGEFTPVSWDQAFDVMAEKFkKALKEK-GPTAVGMFGSGQWTIWE-GYAASKLMKAGFRSNNIDPNARHCMASAVVGFMR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 151 SVGNGAMSNAITEIDNTDLVFIFGYNPADSHPIVANHVINAK--RNGAKIIVCDPRKIETARIADMHIALKNGSNIALLN 228
Cdd:PRK13532 191 TFGIDEPMGCYDDIEAADAFVLWGSNMAEMHPILWSRVTDRRlsNPDVKVAVLSTFEHRSFELADNGIIFTPQTDLAILN 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 229 AIGHVIIEEDLYDKSFV----------------------------------ASRSEGFEEYRKIVEGYTPESVEEITGVS 274
Cdd:PRK13532 271 YIANYIIQNNAVNWDFVnkhtnfrkgatdigyglrpthplekaaknpgtagKSEPISFEEFKKFVAPYTLEKTAKMSGVP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 275 AQEIRACARMYASAKSAAI-LWGMGVTQFYQGVETVRSLTSLAILTGNLGKPNVGVNPVRGQNNVQG-ACDMGALPDTYP 352
Cdd:PRK13532 351 KEQLEQLAKLYADPNRKVVsFWTMGFNQHTRGVWANNLVYNIHLLTGKISTPGNGPFSLTGQPSACGtAREVGTFSHRLP 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 353 GYQYVKFPENREKFAKAWGVES--LPAHTGYRISELpHRAAH-GEVRAAYIMGEDPLQTDAELSAVR-KAFDDLE-LVIV 427
Cdd:PRK13532 431 ADMVVTNPKHREIAEKIWKLPEgtIPPKPGYHAVAQ-DRMLKdGKLNAYWVMCNNNMQAGPNINEERlPGWRNPDnFIVV 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 428 QDIFMTKTASAADVILPSTSWGEHEGVYTAADRGFQRFFKAVEPKWDLKTD-WQII-------------SEIATRMGY-- 491
Cdd:PRK13532 510 SDPYPTVSALAADLILPTAMWVEKEGAYGNAERRTQFWRQQVKAPGEAKSDlWQLVefskrfkteevwpEELLAKKPEyr 589
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 492 ----------------------PMHYNNTQE----------IWDELR-------HLCPDFygATYEKMGELgyvMWPCRD 532
Cdd:PRK13532 590 gktlydvlfangqvdkfplselAEGYLNDEAkhfgfyvqkgLFEEYAsfgrghgHDLAPF--DTYHKVRGL---RWPVVD 664
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 533 ESDadqgTSYLFKEKFD-------------TPNGLAQFFTCDWVAPIDKLTDEYPMVLSTVREVGHYSCRSMTGNCAAL- 598
Cdd:PRK13532 665 GKE----TLWRYREGYDpyvkagegfkfygKPDGKAVIFALPYEPPAESPDEEYDLWLSTGRVLEHWHTGSMTRRVPELy 740
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 599 AALADEPGYaqINTADAERLGIEDEELVWVNSRKGRIITRAQVS--DRPNKGAVYMTyqwWIGA---CNELVSENLSPIT 673
Cdd:PRK13532 741 RAFPEAVCF--MHPEDAKARGLRRGDEVKVVSRRGEVKSRVETRgrNKPPRGLVFVP---FFDAaqlINKLTLDATDPLS 815
|
810
....*....|....
gi 1148879094 674 KTPEYKYCAVNVER 687
Cdd:PRK13532 816 KQTDFKKCAVKIEK 829
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
6-559 |
3.94e-58 |
|
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: 206.56 E-value: 3.94e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 6 TVC-PYCASGCKINLVVDNGKIVRAEA---AQGKTNQGtlCLKGyygwdfINDTQ-ILTP-RLKTPMIRRQRGG--KLEA 77
Cdd:cd02765 2 TACpPNCGGRCPLKCHVRDGKIVKVEPnewPDKTYKRG--CTRG------LSHLQrVYSPdRLKYPMKRVGERGegKFER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 78 VSWDEALDYVATRLSAIKAKYGPDAIqttGSSRGTGNEtnYVMQKFARAVIGTN-NVDCCARVUHGPSvAGLHQSVGNGA 156
Cdd:cd02765 74 ITWDEALDTIADKLTEAKREYGGKSI---LWMSSSGDG--AILSYLRLALLGGGlQDALTYGIDTGVG-QGFNRVTGGGF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 157 M--SNAITEIDNTDLVFIFGYNPADSHPIVANHVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAIGHVI 234
Cdd:cd02765 148 MppTNEITDWVNAKTIIIWGSNILETQFQDAEFFLDARENGAKIVVIDPVYSTTAAKADQWVPIRPGTDPALALGMINYI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 235 IEEDLYDKSFVASRS------------------------------------------------EGFEEYrkIVEG----- 261
Cdd:cd02765 228 LEHNWYDEAFLKSNTsapflvredngtllrqadvtatpaedgyvvwdtnsdspepvaatninpALEGEY--TINGvkvht 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 262 -----------YTPESVEEITGVSAQEIRACARMYASAKSAAILWGMGVTQFYQGVETVRSLTSLAILTGNLGKPNVGvn 330
Cdd:cd02765 306 vltalreqaasYPPKAAAEICGLEEAIIETLAEWYATGKPSGIWGFGGVDRYYHSHVFGRTAAILAALTGNIGRVGGG-- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 331 pvrgqnnvqgacdmgalpdtypgyqyvkfpenrekfakawgveslpahtgyriselphraaHGEVRAAYIMGEDPLQTDA 410
Cdd:cd02765 384 -------------------------------------------------------------VGQIKFMYFMGSNFLGNQP 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 411 ELSAVRKAFDDLELVIVQDIFMTKTASAADVILPSTSWGEHEGVYTAADRGFQRFF--KAVEPKWDLKTDWQIISEIATR 488
Cdd:cd02765 403 DRDRWLKVMKNLDFIVVVDIFHTPTVRYADIVLPAAHWFEVEDLLVRYTTHPHVLLqqKAIEPLFESKSDFEIEKGLAER 482
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1148879094 489 MGYPMHYNNTQEiwDELRHLC----PDFYGATYEKMGELGYVMwpcRDESDADQGTSYLfKEKFDTPNGLAQFFT 559
Cdd:cd02765 483 LGLGDYFPKTPE--DYVRAFMnsddPALDGITWEALKEEGIIM---RLATPEDPYVAYL-DQKFGTPSGKLEFYN 551
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
3-494 |
1.75e-55 |
|
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: 196.77 E-value: 1.75e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 3 KVV--TVCPYCASGCKINLVVDNGkIVRAEAAQGKTNQGTL---------CLKGY-YGWDFINDTqiltpRLKTPMIR-R 69
Cdd:cd02750 2 KVVrsTHGVNCTGSCSWNVYVKNG-IVTREEQATDYPETPPdlpdynprgCQRGAsFSWYLYSPD-----RVKYPLKRvG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 70 QRG-GKLEAVSWDEALDYVATRLSAIKAKYGPDAIQTTGSSRGTGNETNYVMQKFArAVIGTNNVDCCARVUHGPsvAGL 148
Cdd:cd02750 76 ARGeGKWKRISWDEALELIADAIIDTIKKYGPDRVIGFSPIPAMSMVSYAAGSRFA-SLIGGVSLSFYDWYGDLP--PGS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 149 HQSVGNGAMSNAITEIDNTDLVFIFGYNPADSHPIVANHVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLN 228
Cdd:cd02750 153 PQTWGEQTDVPESADWYNADYIIMWGSNVPVTRTPDAHFLTEARYNGAKVVVVSPDYSPSAKHADLWVPIKPGTDAALAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 229 AIGHVIIEEDLYDKSFVasrsegfEEYRK---IVegYTPESVEEITGVSAQEIRACARMYASAKSAAILWGMGVTQFYQG 305
Cdd:cd02750 233 AMAHVIIKEKLYDEDYL-------KEYTDlpfLV--YTPAWQEAITGVPRETVIRLAREFATNGRSMIIVGAGINHWYHG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 306 VETVRSLTSLAILTGNLGKPNVGVNpvrgqnnvqgacdmgalpdtypgyQYVkfpenrekfakawgveslpahtgyrise 385
Cdd:cd02750 304 DLCYRALILLLALTGNEGKNGGGWA------------------------HYV---------------------------- 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 386 lphraahGEVRAAYIMGEDPLQTDAELSAVRKA--FDDLELVIVQDIFMTKTASAADVILPSTSWGE-HEGVYTAADRGF 462
Cdd:cd02750 332 -------GQPRVLFVWRGNLFGSSGKGHEYFEDapEGKLDLIVDLDFRMDSTALYSDIVLPAATWYEkHDLSTTDMHPFI 404
|
490 500 510
....*....|....*....|....*....|..
gi 1148879094 463 QRFFKAVEPKWDLKTDWQIISEIATRMGYPMH 494
Cdd:cd02750 405 HPFSPAVDPLWEAKSDWEIFKALAKKVPWRTL 436
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
571-687 |
6.45e-55 |
|
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: 183.59 E-value: 6.45e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 571 DEYPMVLSTVREVGHYSCRSMTGNCAALAALADEPgYAQINTADAERLGIEDEELVWVNSRKGRIITRAQVSDRPNKGAV 650
Cdd:cd02790 1 EEYPLVLTTGRVLYHYHTGTMTRRAEGLDAIAPEE-YVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGVV 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 1148879094 651 YMTYQWWIGACNELVSENLSPITKTPEYKYCAVNVER 687
Cdd:cd02790 80 FMPFHFAEAAANLLTNAALDPVAKIPEFKVCAVRVEK 116
|
|
| formate_DH_Act |
NF041513 |
formate dehydrogenase; Members of this family are the enzyme formate dehydrogenase, of a type ... |
4-489 |
2.73e-51 |
|
formate dehydrogenase; Members of this family are the enzyme formate dehydrogenase, of a type found in the Actinomycetota, as in the genera Streptomyces, Nocardiopsis, Gordonia, and Saccharomonospora. Many are selenoproteins.
Pssm-ID: 469399 [Multi-domain] Cd Length: 1066 Bit Score: 193.02 E-value: 2.73e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 4 VVTVCPYCASGCKINLVVDNGKIVRAEA-AQGKTNQGTLCLKGYYGWDFINDTQiltpRLKTPMIRRQRGGKLEAVSWDE 82
Cdd:NF041513 43 VRSVCPYCAVGCGQKVYVKDEKVVQIEGdPDSPISRGRLCPKGSASLQLVTGPT----RVTTVLYRRPYGTEWEELDLDT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 83 ALDYVATRLSAIKAKYGPDAIQTTGSSRGT-----------GNETNYVMQKFARAvIGTNNVDCCARVUHGPSVAGLHQS 151
Cdd:NF041513 119 AMDMIADRVLDTRRETWQDEDDDGRRLRRTmgiaslggatlDNEENYLIKKLFTA-LGAVQVENQARIUHSSTVPGLGTS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 152 VGNGAMSNAITEIDNTDLVFIFGYNPADSHPIVANHVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAIG 231
Cdd:NF041513 198 FGRGGATTFLQDLANSDCIVIQGSNMAEAHPVGFQWVMEAKARGATVIHVDPRFTRTSALADLHVPIRAGSDIAFLGGLI 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 232 HVIIEEDLYDKSFV--------------------------------------------------ASRSEGFEEYRKIVEG 261
Cdd:NF041513 278 NHVLSNELYFREYVlaytnaativsedfrdtedldglfsgfdpetgsydpaswqyegvevaaaaGQRDQLYDSRGGAHES 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 262 ---------------------------------------YTPESVEEITGVSAQEIRACARMYAS----AKSAAILWGMG 298
Cdd:NF041513 358 argeehgsggapvagaprrdetlqdprcvfqilkrhfarYTPEMVEEICGIPRELFLKVADALTAnsgrERTTAFCYAVG 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 299 VTQFYQGVETVRSLTSLAILTGNLGKPNVGVNPVRGQNNVQGACDMGALPDTYPGY-------------QYVKFPENREK 365
Cdd:NF041513 438 WTQHTVGVQYIRAASILQLLLGNIGRPGGGIMALRGHASIQGSTDIPTLFNLLPGYlpmphahkhedldSYVEANASQKG 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 366 F-----------AKAWGVESLPAHTGYRISELPH------------RAAHGEVRAAYIMGEDPLQTDAELSAVRKAFDDL 422
Cdd:NF041513 518 FwanmraytvslLKAWWGDAATAENDFCFDYLPRltgdhstyqtvmAMLDGKVKGYFLMGENPAVGSANGRLQRLGMANL 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 423 ELVIVQDIFMTKTAS------------------AADV-ILPSTSWGEHEGVYTAADRGFQRFFKAVEPKWDLKTDWQIIS 483
Cdd:NF041513 598 DWLVVRDFSLIESATfwkdgpeietgelrtediGTEVfFFPAAAHTEKSGTFTNTQRLLQWRHQAVEPPGDARSDLWFFY 677
|
....*.
gi 1148879094 484 EIATRM 489
Cdd:NF041513 678 HLGRRI 683
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
6-489 |
4.23e-51 |
|
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: 182.48 E-value: 4.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 6 TVCPYCASGCKINLVVDNGKIVRAEAaqgKT----NQGTLCLKGYYGWDFINDTQiltpRLKTPMIRRqrGGKLEAVSWD 81
Cdd:cd02768 2 SIDVHDALGSNIRVDVRGGEVMRILP---REneaiNEEWISDKGRFGYDGLNSRQ----RLTQPLIKK--GGKLVPVSWE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 82 EALDYVATRLSAIKakygPDAIQTTGSSRGTgNETNYVMQKFARAViGTNNVDCCARvuhGPSVAGLHQSVGNGAMSNAI 161
Cdd:cd02768 73 EALKTVAEGLKAVK----GDKIGGIAGPRAD-LESLFLLKKLLNKL-GSNNIDHRLR---QSDLPADNRLRGNYLFNTSI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 162 TEIDNTDLVFIFGYNPADSHPIVANHVINA-KRNGAKIIVCDPrKIETARIADMHIALKNGSNIALLNAIghviieedly 240
Cdd:cd02768 144 AEIEEADAVLLIGSNLRKEAPLLNARLRKAvKKKGAKIAVIGP-KDTDLIADLTYPVSPLGASLATLLDI---------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 241 dksfvasrsegfeeyrkivegytpesveeITGVSAQEIracARMYASAKSAAILWGMGVTQFYQGvetvRSLTSLAILTG 320
Cdd:cd02768 213 -----------------------------AEGKHLKPF---AKSLKKAKKPLIILGSSALRKDGA----AILKALANLAA 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 321 NLGKPNVGVNPVRGQNNVqGACDMGALpdtypgyqyvkfpeNREKFAkawgveslpahtgyriselphrAAHGEVRAAYI 400
Cdd:cd02768 257 KLGTGAGLWNGLNVLNSV-GARLGGAG--------------LDAGLA----------------------LLEPGKAKLLL 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 401 MGEDPLQTDAELSAVrkAFDDLELVIVQDIFMTKTASAADVILPSTSWGEHEGVYTAADRGFQRFFKAVEPKWDLKTDWQ 480
Cdd:cd02768 300 LGEDELDRSNPPAAV--ALAAADAFVVYQGHHGDTGAQADVILPAAAFTEKSGTYVNTEGRVQRFKKAVSPPGDAREDWK 377
|
....*....
gi 1148879094 481 IISEIATRM 489
Cdd:cd02768 378 ILRALSNLL 386
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
11-688 |
2.48e-48 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 182.92 E-value: 2.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 11 CASGCKINLVVDNGKIVRAEAAQ-GKTN-----QGTLCLKGYYgwdfiNDTQILTP-RLKTPMIR-RQRG-GKLEAVSWD 81
Cdd:PRK14990 67 CGSRCPLRMHVVDGEIKYVETDNtGDDNydglhQVRACLRGRS-----MRRRVYNPdRLKYPMKRvGARGeGKFERISWE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 82 EALDYVATRLSAIKAKYGPDAIQTtgsSRGTGNETNYVMQKF--ARAVIGtNNVDCCARVUH-------GPSVAGLHQSV 152
Cdd:PRK14990 142 EAYDIIATNMQRLIKEYGNESIYL---NYGTGTLGGTMTRSWppGNTLVA-RLMNCCGGYLNhygdyssAQIAEGLNYTY 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 153 GNGAMSNAITEIDNTDLVFIFGYNPAD---SHPIVANHVINAK-RNGAKIIVCDPRKIET-ARIADMHIALKNGSNIALL 227
Cdd:PRK14990 218 GGWADGNSPSDIENSKLVVLFGNNPGEtrmSGGGVTYYLEQARqKSNARMIIIDPRYTDTgAGREDEWIPIRPGTDAALV 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 228 NAIGHVIIEEDLYDKSFVASRSEGFEE------------YRKIVEGY-------TPESVEEITGVSAQEIRACARMYASA 288
Cdd:PRK14990 298 NGLAYVMITENLVDQPFLDKYCVGYDEktlpasapknghYKAYILGEgpdgvakTPEWASQITGVPADKIIKLAREIGST 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 289 KSAAILWGMGVTQFYQGVETVRSLTSLAILTGNLGkpnvgvnpVRGQNNvqgacdmGALPDTYpGYQYVKFP--ENREKF 366
Cdd:PRK14990 378 KPAFISQGWGPQRHANGEIATRAISMLAILTGNVG--------INGGNS-------GAREGSY-SLPFVRMPtlENPIQT 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 367 AKA---W--GVESLPAHTGYRISELPHRAAHGEVRAAY-IMGEDPLQTDAELSAVRKAFDD---LELVIVQDIFMTKTAS 437
Cdd:PRK14990 442 SISmfmWtdAIERGPEMTALRDGVRGKDKLDVPIKMIWnYAGNCLINQHSEINRTHEILQDdkkCELIVVIDCHMTSSAK 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 438 AADVILPSTSWGEHEGVYTAADRGFQRFF----KAVEPKWDLKTDWQIISEIATRMGYPMHYNN--TQEIWdeLRHL--- 508
Cdd:PRK14990 522 YADILLPDCTASEQMDFALDASCGNMSYVifndQVIKPRFECKTIYEMTSELAKRLGVEQQFTEgrTQEEW--MRHLyaq 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 509 -------CPDFygATYEKMGelgyvMWPCRDEsdadQGTSYLFKE--------KFDTPNGLAQFFTCD-------WVAP- 565
Cdd:PRK14990 600 sreaipeLPTF--EEFRKQG-----IFKKRDP----QGHHVAYKAfredpqanPLTTPSGKIEIYSQAladiaatWELPe 668
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 566 -----------------IDKLTDEYPMVLSTVrevgHYSCR--SMTGNCAALAALADEPGYaqINTADAERLGIEDEELV 626
Cdd:PRK14990 669 gdvidplpiytpgfesyQDPLNKQYPLQLTGF----HYKSRvhSTYGNVDVLKAACRQEMW--INPLDAQKRGINNGDKV 742
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1148879094 627 WVNSRKGRIITRAQVSDRPNKGAVYMTYQWWI----------GACNELVSENLSPITKTPEYKYCAVNVERI 688
Cdd:PRK14990 743 RIFNDRGEVHIEAKVTPRMMPGVVALGEGAWYdpdakrvdkgGCINVLTTQRPSPLAKGNPSHTNLVQVEKV 814
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
571-687 |
1.91e-43 |
|
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: 152.28 E-value: 1.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 571 DEYPMVLSTVREVGHYSCRSMTGNCAALAALADEPgYAQINTADAERLGIEDEELVWVNSRKGRIITRAQVSDRPNKGAV 650
Cdd:cd00508 1 EEYPLVLTTGRLLEHWHTGTMTRRSPRLAALAPEP-FVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRPGTV 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1148879094 651 YMTYQWWI----GACNELVSENLSPITKTPEYKYCAVNVER 687
Cdd:cd00508 80 FMPFHWGGevsgGAANALTNDALDPVSGQPEFKACAVRIEK 120
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
17-527 |
1.42e-42 |
|
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: 163.59 E-value: 1.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 17 INLVVDNGKIVRAEAAQGKTNQGTLcLKGYYGWDFiNDTqiltpRLKTPMIRR------------QRG-GKLEAVSWDEA 83
Cdd:cd02769 9 FRARVKDGRIVGVRPFEEDPDPSPL-LDGVPDAVY-SPT-----RIKYPMVRRgwlekgpgsdrsLRGkEEFVRVSWDEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 84 LDYVATRLSAIKAKYGPDAI----------------QTT---------GSSRGTGNETNYVMQKFARAVIGTNNVdCCAR 138
Cdd:cd02769 82 LDLVAAELKRVRKTYGNEAIfggsygwssagrfhhaQSLlhrflnlagGYVGSVGDYSTGAAQVILPHVVGSMEV-YTEQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 139 VUHGPSVAglhqsvgngamsnaiteiDNTDLVFIFGYNPADSHPI----VANHVI-----NAKRNGAKIIVCDPRKIETA 209
Cdd:cd02769 161 QTSWPVIA------------------EHTELVVAFGADPLKNAQIawggIPDHQAysylkALKDRGIRFISISPLRDDTA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 210 RIADM-HIALKNGSNIALLNAIGHVIIEEDLYDKSFVASRSEGFEEYRKIVEGY------TPESVEEITGVSAQEIRACA 282
Cdd:cd02769 223 AELGAeWIAIRPGTDVALMLALAHTLVTEGLHDKAFLARYTVGFDKFLPYLLGEsdgvpkTPEWAAAICGIPAETIRELA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 283 RMYASaKSAAILWGMGVTQFYQGVETVRSLTSLAILTGNLGKPNVGVNPVRGQNNVQGACDMGALPDTYP-GYQYVK--F 359
Cdd:cd02769 303 RRFAS-KRTMIMAGWSLQRAHHGEQPHWMAVTLAAMLGQIGLPGGGFGFGYHYSNGGGPPRGAAPPPALPqGRNPVSsfI 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 360 PENREkfakawgVESL--P----AHTGYRIsELPHraahgeVRAAYIMGEDPLQTDAELSAVRKAFDDLELVIVQDIFMT 433
Cdd:cd02769 382 PVARI-------ADMLlnPgkpfDYNGKKL-TYPD------IKLVYWAGGNPFHHHQDLNRLIRAWQKPETVIVHEPFWT 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 434 KTASAADVILPSTSWGEHEGV-YTAADRGFQRFFKAVEPKWDLKTDWQIISEIATRMGYPMHYNNTQEIWDELRHlcpdF 512
Cdd:cd02769 448 ATARHADIVLPATTSLERNDIgGSGDNRYIVAMKQVVEPVGEARDDYDIFADLAERLGVEEQFTEGRDEMEWLRH----L 523
|
570
....*....|....*
gi 1148879094 513 YGATYEKMGELGYVM 527
Cdd:cd02769 524 YEESRAQAAARGVEM 538
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
61-340 |
3.89e-41 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 160.98 E-value: 3.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 61 RLKTPMIRRQRGGKLEAVSWDEALDYVATRLSAIKakyGPDAIQTTGSSRgTGNETNYVMQKFARAViGTNNVDCCARVU 140
Cdd:PRK09939 108 RLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYS---DPNQVEFYTSGR-TSNEAAFLYQLFAREY-GSNNFPDCSNMC 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 141 HGPSVAGLHQSVGNGAMSNAITEIDNTDLVFIFGYNPADSHPIVANHVINAKRNGAKIIVCDP---RKIE--TA------ 209
Cdd:PRK09939 183 HEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPlqeRGLErfTApqnpfe 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 210 -------RIADMHIALKNGSNIALLNAIGHVIIEED----------LYDKSFVASRSEGFEEYRKIVEGYTPESVEEITG 272
Cdd:PRK09939 263 mltnsetQLASAYYNVRIGGDMALLKGMMRLLIERDdaasaagrpsLLDDEFIQTHTVGFDELRRDVLNSEWKDIERISG 342
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1148879094 273 VSAQEIRACARMYASAKSAAILWGMGVTQFYQGVETVRSLTSLAILTGNLGKPNVGVNPVRGQNNVQG 340
Cdd:PRK09939 343 LSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQG 410
|
|
| FwdB |
COG1029 |
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion]; |
1-489 |
1.68e-40 |
|
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion];
Pssm-ID: 440652 [Multi-domain] Cd Length: 428 Bit Score: 153.85 E-value: 1.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 1 MKKVVT--VCPYCASGC-KINLVVDNGKIVRAEAAqgktnqgtlCLKGYYGwdFINDtqILTPRLKTPMIRrqrggkLEA 77
Cdd:COG1029 1 MPKVVKnvVCPFCGCLCdDLEVEVEGGKIVVVKNA---------CAIGAAK--FERA--VSDHRITSPRIR------GKE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 78 VSWDEALDYVATRLSAIKAK--YGPDAIQTTGSSRGtgnetnYVMQKFARAVigtnnVDCCARVUHGPSVAGLHQSvgnG 155
Cdd:COG1029 62 VSLEEAIDKAAEILANAKRPliYGLSSTDCEAMRAG------LALAERVGAV-----VDNTASVCHGPSLLALQDV---G 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 156 AMSNAITEIDN-TDLVFIFGYNPADSHPivaNH----VINAK-------RNGAKIIVCDPRKIETARIADMHIALKNGSN 223
Cdd:COG1029 128 WPTCTLGEVKNrADVIIYWGCNPVHAHP---RHmsrySVFPRgfftpkgRKDRTVIVVDPRPTDTAKVADLHLQVKPGRD 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 224 IALLNAIghviieedlydksfvasrsegfeeyRKIVEGYTPeSVEEITGVSAQEIRACARMYASAKSAAILWGMGVTQFY 303
Cdd:COG1029 205 YEVLSAL-------------------------RALVRGKEL-SPEEVAGIPVEDLEELAERLKNAKYGVIFWGMGLTQSP 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 304 QGVETVRSLTSLAILTGNLGKPNVGvnPVRGQNNVQGAcdmGALPDTYPGYQYvkfpenREKFAKAWGVESlPAHTGyrI 383
Cdd:COG1029 259 GKHLNVDAAIELVRDLNRYTKFSIL--PLRGHYNVAGA---NQVASWQTGYPF------RVDFSRGYPRYN-PGETS--A 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 384 SELphrAAHGEVRAAYIMGEDPLqtdAELSavRKAFDDLEL--VIVQDIFMTKTASAADVILPSTSWG-EHEGVYTAADR 460
Cdd:COG1029 325 VDL---LARGEVDALLWVASDPG---AHFP--PDAVEHLAKipTIVIDPHGTPTTEVADVVIPVAIPGiEHGGTAYRMDN 396
|
490 500
....*....|....*....|....*....
gi 1148879094 461 GFQRFFKAVEPkwDLKTDWQIISEIATRM 489
Cdd:COG1029 397 VPLPLRKLRDS--PLPSDEEVLKAIEERV 423
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
4-496 |
2.62e-39 |
|
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: 152.59 E-value: 2.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 4 VVTVCPYCASGCKINLVVDNGKIVRAEAAQ-GKTNQGTLCLKGYYGwdfINdtQILTP-RLKTPMIR------RQRGGKL 75
Cdd:cd02757 2 VPSTCQGCTAWCGLQAYVEDGRVTKVEGNPlHPGSRGRLCAKGHLG---LQ--QVYDPdRILYPMKRtnprkgRDVDPKF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 76 EAVSWDEALDYVATRLSAIKAKYGPDAIQTTGSSRGTGNETNYvmQKFARAvIGTNNVDCCARVUhgPSVAGLHQSVGNG 155
Cdd:cd02757 77 VPISWDEALDTIADKIRALRKENEPHKIMLHRGRYGHNNSILY--GRFTKM-IGSPNNISHSSVC--AESEKFGRYYTEG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 156 AMSNAITEIDNTDLVFIFGYNP-ADSHPI-VANHVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAIGHV 233
Cdd:cd02757 152 GWDYNSYDYANAKYILFFGADPlESNRQNpHAQRIWGGKMDQAKVVVVDPRLSNTAAKADEWLPIKPGEDGALALAIAHV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 234 IIEEDLYDKSFVASRSEG--------------FEE---------YRKIVEGYTPESVEEITGVSAQEIRACARMYASAKS 290
Cdd:cd02757 232 ILTEGLWDKDFVGDFVDGknyfkagetvdeesFKEksteglvkwWNLELKDYTPEWAAKISGIPAETIERVAREFATAAP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 291 AAILW-GMGVTQFYQGVETVRSLTSLAILTGNLGKPNvGVNPVRGQNNVqgacdmgalpDTYPGYQYvkfpenrekfaka 369
Cdd:cd02757 312 AAAAFtWRGATMQNRGSYNSMACHALNGLVGSIDSKG-GLCPNMGVPKI----------KVYFTYLD------------- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 370 wgveslpahtgyriselphraahgevraayimgeDPLQTDAELSAVRKAFDDLELVIVQDIFMTKTASAADVILPSTSWG 449
Cdd:cd02757 368 ----------------------------------NPVFSNPDGMSWEEALAKIPFHVHLSPFMSETTYFADIVLPDGHHF 413
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1148879094 450 EHEGV---YTAADR--GFQRffKAVEPKWDLKTDWQIISEIATRMGYPMHYN 496
Cdd:cd02757 414 ERWDVmsqENNLHPwlSIRQ--PVVKSLGEVREETEILIELAKKLDPKGSDG 463
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
61-489 |
1.14e-35 |
|
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: 143.78 E-value: 1.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 61 RLKTPMIRRqrGGKLEAVSWDEALDYVATRLSAIKAKYGPD----AIQTTGSSRGTGNETNYVMQKFARAVIGTNNVDCC 136
Cdd:cd02756 117 RLTTPLVRR--GGQLQPTTWDDAIDLVARVIKGILDKDGNDdavfASRFDHGGGGGGFENNWGVGKFFFMALQTPFVRIH 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 137 ARVUHGPSVAGLHQsVGNGAMSNAITEIDNTDLVFIFGYNPADSHPI-VANHVINAKRNG-----------------AKI 198
Cdd:cd02756 195 NRPAYNSEVHATRE-MGVGELNNSYEDARLADTIVLWGNNPYETQTVyFLNHWLPNLRGAtvsekqqwfppgepvppGRI 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 199 IVCDPRKIETARIAD--------MHIALKNGSNIALLNAIGHVIIEedlydksfvaSRSEGFEEyrkivegytpesVEEI 270
Cdd:cd02756 274 IVVDPRRTETVHAAEaaagkdrvLHLQVNPGTDTALANAIARYIYE----------SLDEVLAE------------AEQI 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 271 TGVSAQEIRACARMYASAKSAA------------ILWGMgvtQFYQgveTVRSLTSLAILTGNLGKPNVGVnpVRGQNNV 338
Cdd:cd02756 332 TGVPRAQIEKAADWIAKPKEGGyrkrvmfeyekgIIWGN---DNYR---PIYSLVNLAIITGNIGRPGTGC--VRQGGHQ 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 339 QGACDMGALPD-TYPGYQYvkfpenrekfakawgveslPAHTGYRISElphraahGEVRAAYIMGEDPLQT--------- 408
Cdd:cd02756 404 EGYVRPPPPPPpWYPQYQY-------------------APYIDQLLIS-------GKGKVLWVIGCDPYKTtpnaqrlre 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 409 -------------DAELSAV---RKAFDDLEL---------VIVQDIFMTKTASAADVILPSTSWGE-HEGVYTAADRGF 462
Cdd:cd02756 458 tinhrsklvtdavEAALYAGtydREAMVCLIGdaiqpgglfIVVQDIYPTKLAEDAHVILPAAANGEmNETSMNGHERRL 537
|
490 500
....*....|....*....|....*..
gi 1148879094 463 QRFFKAVEPKWDLKTDWQIISEIATRM 489
Cdd:cd02756 538 RLYEKFMDPPGEAMPDWWIAAMIANRI 564
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
61-650 |
4.91e-33 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 136.34 E-value: 4.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 61 RLKTPMIR------------RQRG-GKLEAVSWDEALDYVATRLSAIKAKYGPDAIQTTGSS-RGTG---NETNYvMQkf 123
Cdd:PRK15102 90 RIRYPMVRldwlrkrhksdtSQRGdNRFVRVSWDEALDLFYEELERVQKTYGPSALHTGQTGwQSTGqfhSATGH-MQ-- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 124 aRAVigtnnvdccarVUHGPSVAGLHQ-SVGNGAM-------SNAITE--------IDNTDLVFIFGYNP---------A 178
Cdd:PRK15102 167 -RAI-----------GMHGNSVGTVGDySTGAGQVilpyvlgSTEVYEqgtswpliLENSKTIVLWGSDPvknlqvgwnC 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 179 DSHPI----------VANHVINakrngakIIVCDPRKIETAR-IADMHIALKNGSNIALLNAIGHVIIEEDLYDKSFVAS 247
Cdd:PRK15102 235 ETHESyaylaqlkekVAKGEIN-------VISIDPVVTKTQNyLGCEHLYVNPQTDVPLMLALAHTLYSENLYDKKFIDN 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 248 RSEGFEEYRKIVEG------YTPESVEEITGVSAQEIRACARMYASAKSaAILWGMGVTQFYQGVETVRSLTSLAILTGN 321
Cdd:PRK15102 308 YCLGFEQFLPYLLGekdgvpKTPEWAEKICGIDAETIRELARQMAKGRT-QIIAGWCIQRQQHGEQPYWMGAVLAAMLGQ 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 322 LGKPNVGVNPVRGQNNV----QGACDMGALPDTYPGYQYVKFPENREKFAKA------WgVESLpAHTGYRISELPHRAA 391
Cdd:PRK15102 387 IGLPGGGISYGHHYSGIgvpsSGGAIPGGFPGNLDTGQKPKHDNSDYKGYSStipvarF-IDAI-LEPGKTINWNGKKVT 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 392 HGEVRAAYIMGEDPLQTDAELSAVRKAFDDLELVIVQDIFMTKTASAADVILPS-TSWGEHE----GVYtaADRGFQRFF 466
Cdd:PRK15102 465 LPPLKMMIFSGTNPWHRHQDRNRMKEAFRKLETVVAIDNQWTATCRFADIVLPAcTQFERNDidqyGSY--SNRGIIAMK 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 467 KAVEPKWDLKTDWQIISEIATRMGYPMHY--NNTQEIWdeLRHLCPD--------FYGATYEKMGELGYVMWPcrdesda 536
Cdd:PRK15102 543 KVVEPLFESRSDFDIFRELCRRFGREKEYtrGMDEMGW--LKRLYQEckqqnkgkFHMPEFDEFWKKGYVEFG------- 613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 537 dQGTSYL----FKEKFD-----TPNGLAQFFT----------CD----WVAPIDKL-----TDEYPMVLSTVrevgHYSC 588
Cdd:PRK15102 614 -EGQPWVrhadFREDPElnplgTPSGLIEIYSrkiadmgyddCQghpmWFEKIERShggpgSDKYPLWLQSV----HPDK 688
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1148879094 589 RSMTGNC------AALAALADEPGYaqINTADAERLGIEDEELVWVNSRKGRIITRAQVSDRPNKGAV 650
Cdd:PRK15102 689 RLHSQLCeseelrETYTVQGREPVY--INPQDAKARGIKDGDVVRVFNDRGQVLAGAVVSDRYPPGVI 754
|
|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
7-488 |
3.00e-30 |
|
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: 123.98 E-value: 3.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 7 VCPYCASGCK-INLVVDNGKIvraeaaqgkTNQGTLCLKGYYGWDFINDtqiltpRLKTPMIRRqrggklEAVSWDEALD 85
Cdd:cd02761 3 VCPFCGLLCDdIEVEVEDNKI---------TKVRNACRIGAAKFARYER------RITTPRIDG------KPVSLEEAIE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 86 YVATRLSAIK--AKYGPDAIQTTGSSRGtgnetnYVMQKFARAVIgtnnvDCCARVUHGPSVAGLHQSvgnGAMSNAITE 163
Cdd:cd02761 62 KAAEILKEAKrpLFYGLGTTVCEAQRAG------IELAEKLGAII-----DHAASVCHGPNLLALQDS---GWPTTTLGE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 164 I-DNTDLVFIFGYNPADSHP-IVANHVINAK-------RNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAIGHVI 234
Cdd:cd02761 128 VkNRADVIVYWGTNPMHAHPrHMSRYSVFPRgffreggREDRTLIVVDPRKSDTAKLADIHLQIDPGSDYELLAALRALL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 235 IEEDLydksfvasrsegfeeyrkivegytpeSVEEITGVSAQEIRACARMYASAKSAAILWGMGVTQFYQGVETVRSLTS 314
Cdd:cd02761 208 RGAGL--------------------------VPDEVAGIPAETILELAERLKNAKFGVIFWGLGLLPSRGAHRNIEAAIR 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 315 LAILTGNlgKPNVGVNPVRGQNNVQGACDMGALPDTYPgyqyvkfpeNREKFAKAWGVESlPAHTGYriSELphrAAHGE 394
Cdd:cd02761 262 LVKALNE--YTKFALLPLRGHYNVRGFNQVLTWLTGYP---------FRVDFSRGYPRYN-PGEFTA--VDL---LAEGE 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 395 VRAAYIMGEDPLqtdaeLSAVRKAFDDLE--LVIVQDIFMTKTASAADVILPSTSWG-EHEGVYTAADRGFQRFFKAVEP 471
Cdd:cd02761 325 ADALLIIASDPP-----AHFPQSAVKHLAeiPVIVIDPPPTPTTRVADVVIPVAIPGiEAGGTAYRMDGVVVLPLKAVET 399
|
490
....*....|....*..
gi 1148879094 472 kwDLKTDWQIISEIATR 488
Cdd:cd02761 400 --ERLPDEEILKQLLEK 414
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
571-688 |
2.41e-29 |
|
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: 112.67 E-value: 2.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 571 DEYPMVLSTVREVGHYSCRSMTGNCAALAALADEPgYAQINTADAERLGIEDEELVWVNSRKGRIITRAQVSDRPNKGAV 650
Cdd:cd02791 1 AEYPLWLNTGRVRDQWHTMTRTGRVPRLNAHVPEP-YVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPGEV 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1148879094 651 YMTYQW--WI---GACNELVSENLSPITKTPEYKYCAVNVERI 688
Cdd:cd02791 80 FVPMHWgdQFgrsGRVNALTLDATDPVSGQPEFKHCAVRIEKV 122
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
575-682 |
1.02e-28 |
|
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: 110.44 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 575 MVLSTVREVGHYSCRSMTGNCAALAAlaDEPGYAQINTADAERLGIEDEELVWVNSRKGRIITRAQVSDRPNKGAVYMTY 654
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAK--PEPEVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPF 78
|
90 100 110
....*....|....*....|....*....|..
gi 1148879094 655 QWW----IGACNELVSENLSPITKTPEYKYCA 682
Cdd:pfam01568 79 GWWyeprGGNANALTDDATDPLSGGPEFKTCA 110
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
6-496 |
6.39e-28 |
|
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: 119.94 E-value: 6.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 6 TVCPYCASGCKINLVVDNGKIVRAEA-AQGKTNQGTLCLKGYYGWdfindTQILTP-RLKTPMIRR-QRG-GKLEAVSWD 81
Cdd:cd02763 2 TTCYMCACRCGIRVHLRDGKVRYIKGnPDHPLNKGVICAKGSSGI-----MKQYSPaRLTKPLLRKgPRGsGQFEEIEWE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 82 EALDYVATRLSAIKAKyGPDAIqttgsSRGTGNETNYVMQKFARAVIGTNNVDCCARVUHGPSVAGLHQSVGNGAMSNAI 161
Cdd:cd02763 77 EAFSIATKRLKAARAT-DPKKF-----AFFTGRDQMQALTGWFAGQFGTPNYAAHGGFCSVNMAAGGLYSIGGSFWEFGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 162 TEIDNTDLVFIFGY-NPADSHPIVANhVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAIGHVIIEEDLY 240
Cdd:cd02763 151 PDLEHTKYFMMIGVaEDHHSNPFKIG-IQKLKRRGGKFVAVNPVRTGYAAIADEWVPIKPGTDGAFILALAHELLKAGLI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 241 DKSFVASRSEGFEeyrkIVEgYTPESVEEITGVSAQEIRACAR-MYASAKSAAI--------LWGM-------------- 297
Cdd:cd02763 230 DWEFLKRYTNAAE----LVD-YTPEWVEKITGIPADTIRRIAKeLGVTARDQPIelpiawtdVWGRkhekitgrpvsfha 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 298 --GVTQFYQGVETVRSLTSLAILTGNLGKPN---------VGVNPVRGQNNVQGACDMGALPDTYPgYQYVKFPE----- 361
Cdd:cd02763 305 mrGIAAHSNGFQTIRALFVLMMLLGTIDRPGgfrhkppypRHIPPLPKPPKIPSADKPFTPLYGPP-LGWPASPDdllvd 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 362 ---NREKFAKAWGVEslpahtgYRISelPHRAAHGEVRAAYimGEDPLQTDAEL--------------SAVRKAFDD--- 421
Cdd:cd02763 384 edgNPLRIDKAYSWE-------YPLA--AHGCMQNVITNAW--RGDPYPIDTLMiymanmawnssmntPEVREMLTDkda 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 422 -----LELVIVQDIFMTKTASAADVILPSTSWGEHEGVYTAADRGFQRF--------FKAVEPKWDLKTDWQIISEIATR 488
Cdd:cd02763 453 sgnykIPFIIVCDAFYSEMVAFADLVLPDTTYLERHDAMSLLDRPISEAdgpvdairVPIVEPKGDVKPFQEVLIELGTR 532
|
....*...
gi 1148879094 489 MGYPMHYN 496
Cdd:cd02763 533 LGLPGFTN 540
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
61-482 |
2.51e-26 |
|
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: 112.06 E-value: 2.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 61 RLKTPMIRRqrGGKLEAVSWDEALDYVATRLSAIKAKYGPDAIQTTGSSRGTgNETNYVMQKFARAViGTNNVDccARVU 140
Cdd:cd02772 54 RLTKPMIKK--DGQWQEVDWETALEYVAEGLSAIIKKHGADQIGALASPHST-LEELYLLQKLARGL-GSDNID--HRLR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 141 HgpsVAGLHQSVGNGA--MSNAITEIDNTDLVFIFGYNPADSHPIVANHVINAKRNGAKIIVCDPRKietariADMHIAL 218
Cdd:cd02772 128 Q---SDFRDDAKASGApwLGMPIAEISELDRVLVIGSNLRKEHPLLAQRLRQAVKKGAKLSAINPAD------DDFLFPL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 219 KNGSNIA---LLNAIGHVIieedlydksfvasrsegfeeyrKIVEGYTPESVEEIT--GVSAQEIRACARMYASAKSAAI 293
Cdd:cd02772 199 SGKAIVApsaLANALAQVA----------------------KALAEEKGLAVPDEDakVEASEEARKIAASLVSAERAAV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 294 LWGMGVTQFYQGvETVRSLTS-LAILTG-NLGKPNVGVNPVrgqnnvqGACDMGALPdtypgyqyvkfpeNREKFAKAwg 371
Cdd:cd02772 257 FLGNLAQNHPQA-ATLRALAQeIAKLTGaTLGVLGEGANSV-------GAYLAGALP-------------HGGLNAAA-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 372 veslpahtgyrISELPhraahgeVRAAYIMGEDPLQTDAELSAVRKAFDDLELVIVQDIFMTKTA-SAADVILPSTSWGE 450
Cdd:cd02772 314 -----------MLEQP-------RKAYLLLNVEPELDCANPAQALAALNQAEFVVALSAFASAALlDYADVLLPIAPFTE 375
|
410 420 430
....*....|....*....|....*....|..
gi 1148879094 451 HEGVYTAADRGFQRFFKAVEPKWDLKTDWQII 482
Cdd:cd02772 376 TSGTFVNLEGRVQSFKGVVKPLGEARPAWKVL 407
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
390-511 |
1.14e-24 |
|
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: 107.62 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 390 AAHGEVRAAYIMGEDPLQTDAElsAVRKAFDDLELVIVQDIFMTKTASAADVILPSTSWGEHEGVYTAADRGFQRFFKAV 469
Cdd:COG1034 328 AEAGKLKALVLLGADPYDLDPA--AALAALAKADFVVVLDHFGSATAERADVVLPAAAFAEKSGTFVNLEGRVQRFNAAV 405
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1148879094 470 EPKWDLKTDWQIISEIATRMGYPMHYNNTQEIWDELRHLCPD 511
Cdd:COG1034 406 PPPGEARPDWRVLRALANALGAGLPYDSLEEVRAELAAEAPA 447
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
571-687 |
1.74e-24 |
|
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: 98.83 E-value: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 571 DEYPMVLSTVREVGHYSCRSMTGNCAALAALADEPgYAQINTADAERLGIEDEELVWVNSRKGRIITRAQVSDRPNKGAV 650
Cdd:cd02792 1 EEFPLVLTTGRLTEHFHGGNMTRNSPYLAELQPEM-FVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHEV 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1148879094 651 YMTYQW-WIG-----ACNELVSENLSPITKTPEYKYCAVNVER 687
Cdd:cd02792 80 GIPYHWgGMGlvigdSANTLTPYVGDPNTQTPEYKAFLVNIEK 122
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
1-213 |
1.12e-22 |
|
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: 101.84 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 1 MKKVVTVCPYCASGCKINLVVDNGKIVRAEA-AQGKTNQGTLCLKGYYGWDFINDTQiltpRLKTPMIRrqRGGKLEAVS 79
Cdd:COG1034 215 LKKTPSICPHCSVGCNIRVDVRGGKVYRVLPrENEAVNEEWLCDKGRFGYDGLNSPD----RLTRPLVR--KDGELVEAS 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 80 WDEALDYVATRLSAIKAKygpdaiqttGSSRGtgnetnyvmqkfaravigtnnvdcCARVUHGPSVAGLHQSVGNGAMsn 159
Cdd:COG1034 289 WEEALAAAAEGLKALKKA---------ENSVG------------------------AALLGALPDAAAILEAAEAGKL-- 333
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1148879094 160 aiteidntDLVFIFGYNPADSHPIVANhviNAKRNGAKIIVCDPRKIETARIAD 213
Cdd:COG1034 334 --------KALVLLGADPYDLDPAAAL---AALAKADFVVVLDHFGSATAERAD 376
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
6-490 |
6.48e-22 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 101.18 E-value: 6.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 6 TVCPYCASGCKINlvVDN--GKIVRAEAAQG-KTNQGTLCLKGYygWDFINDTQilTPRLKTPMIRRQRGgKLEAVSWDE 82
Cdd:PRK07860 226 SVCEHCASGCAQR--TDHrrGKVLRRLAGDDpEVNEEWNCDKGR--WAFTYATQ--PDRITTPLVRDEDG-ELEPASWSE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 83 ALDYVATRLSAIKAKYGpdaIQTTGssRGTgNETNYVMQKFARAVIGTNNVDCCARVuH--------GPSVAGLHQSVgn 154
Cdd:PRK07860 299 ALAVAARGLAAARGRVG---VLVGG--RLT-VEDAYAYAKFARVALGTNDIDFRARP-HsaeeadflAARVAGRGLGV-- 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 155 gamsnAITEIDNTDLVFIFGYNPADSHPIV------AnhvinAKRNGAKIIVCDPrkIETARIADMH---IALKNGSNIA 225
Cdd:PRK07860 370 -----TYADLEKAPAVLLVGFEPEEESPIVflrlrkA-----ARKHGLKVYSIAP--FATRGLEKMGgtlLRTAPGGEAA 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 226 LLNAIGHVIIEEDlydksfVASRSEGfeeyRKIVEGytpESVEEITGVsaqeIRACARMyASAKSAAILWgmgVtqfyqg 305
Cdd:PRK07860 438 ALDALATGAPDVA------ELLRTPG----AVILVG---ERLATVPGA----LSAAARL-ADATGARLAW---V------ 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 306 vetvrsltslailtgnlgkpnvgvnPVR-GQnnvQGACDMGALPDTYPGYQYVKFPENREKFAKAWGVESLPAHTGYRIS 384
Cdd:PRK07860 491 -------------------------PRRaGE---RGALEAGALPTLLPGGRPVADPAARAEVAAAWGVDELPAAPGRDTA 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 385 ELPHRAAHGEVRAAYIMGEDPlqtdAEL---SAVRKAFDDLELVIVQDIFMTKTASAADVILPSTSWGEHEGVYTAADrG 461
Cdd:PRK07860 543 GILAAAAAGELGALLVGGVEP----ADLpdpAAALAALDAAGFVVSLELRHSAVTERADVVLPVAPVAEKAGTFLNWE-G 617
|
490 500
....*....|....*....|....*....
gi 1148879094 462 FQRFFKAVEPKWDLKTDWQIISEIATRMG 490
Cdd:PRK07860 618 RLRPFEAALRTTGALSDLRVLDALADEMG 646
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
585-679 |
9.59e-21 |
|
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: 87.38 E-value: 9.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 585 HYSCRSMTGNcAALAALADEPgYAQINTADAERLGIEDEELVWVNSRKGRIITRAQVSDRPNKGAVYMTYQWW-----IG 659
Cdd:cd02775 4 HFHSGTRTRN-PWLRELAPEP-VVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGhrggrGG 81
|
90 100
....*....|....*....|
gi 1148879094 660 ACNELVSENLSPITKTPEYK 679
Cdd:cd02775 82 NANVLTPDALDPPSGGPAYK 101
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
6-492 |
2.73e-19 |
|
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: 92.79 E-value: 2.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 6 TVCPYCASGCKINLVVDN--GKIVRAEA----------------------------AQGKTNQGTLCLKGYYGWDFINDT 55
Cdd:cd02758 2 SSCLGCWTQCGIRVRVDKetGKVLRIAGnpyhplntapslpyntplkeslylslvgENGLKARATACARGNAGLQYLYDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 56 QiltpRLKTPMIRR-QRG-GKLEAVSWDEALDYVAT-----------RLSAIKAK----------YGPDAIQTTgSSRGT 112
Cdd:cd02758 82 Y----RVLQPLKRVgPRGsGKWKPISWEQLIEEVVEggdlfgeghveGLKAIRDLdtpidpdhpdLGPKANQLL-YTFGR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 113 GNETNYVMQKFARAVIGTNNVdccarVUHGpSVAGLHQSVGNGAMSNAI-------TEIDNTDLVFIFGYNPADSHP--- 182
Cdd:cd02758 157 DEGRTPFIKRFANQAFGTVNF-----GGHG-SYCGLSYRAGNGALMNDLdgyphvkPDFDNAEFALFIGTSPAQAGNpfk 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 183 IVANHVINAK-RNGAKIIVCDPRKIETARIADMH---IALKNGSNIALLNAIGHVIIEEDLYDKSFVASRSE-------- 250
Cdd:cd02758 231 RQARRLAEARtEGNFKYVVVDPVLPNTTSAAGENirwVPIKPGGDGALAMAMIRWIIENERYNAEYLSIPSKeaakaage 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 251 -----------------GFEEYRKIVEGYTPESVEEITGVSAQEIRACARMYASAKSAAILWGMGVTQFYQGVETVRSLT 313
Cdd:cd02758 311 pswtnathlvitvrvksALQLLKEEAFSYSLEEYAEICGVPEAKIIELAKEFTSHGRAAAVVHHGGTMHSNGFYNAYAIR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 314 SLAILTGNLgkpnvgvnpvrgqnNVQGACDMGALPDTYPGYQY----VKFPE---------NREKFA----------KAW 370
Cdd:cd02758 391 MLNALIGNL--------------NWKGGLLMSGGGFADNSAGPrydfKKFFGevkpwgvpiDRSKKAyektseykrkVAA 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 371 GVESLPA------HTGYRISELPHRAAHG---------EVRAAYIMGEDPLQTDAElsAVRKAFDDLELVIVQDIFMTKT 435
Cdd:cd02758 457 GENPYPAkrpwypLTPELYTEVIASAAEGypyklkaliLWMANPVYGAPGLVKQVE--EKLKDPKKLPLFIAIDAFINET 534
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1148879094 436 ASAADVILPST----SWG---EHEGVYTAAD--RgfqrfFKAVEPKWDLKTD------WQIISEIATRMGYP 492
Cdd:cd02758 535 SAYADYIVPDTtyyeSWGfstPWGGVPTKAStaR-----WPVIAPLTEKTANghpvsmESFLIDLAKALGLP 601
|
|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
1-54 |
4.15e-18 |
|
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: 78.49 E-value: 4.15e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1148879094 1 MKKVVTVCPYCASGCKINLVVDNGKIVRAE-AAQGKTNQGTLCLKGYYGWDFIND 54
Cdd:pfam04879 1 MKVVKTICPYCGVGCGLEVHVKDGKIVKVEgDPDHPVNEGRLCVKGRFGYERVYN 55
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
1-54 |
1.67e-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: 73.82 E-value: 1.67e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1148879094 1 MKKVVTVCPYCASGCKINLVVDNGKIVRAE-AAQGKTNQGTLCLKGYYGWDFIND 54
Cdd:smart00926 1 EKWVPTVCPLCGVGCGLLVEVKDGRVVRVRgDPDHPVNRGRLCPKGRAGLEQVYS 55
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
61-455 |
9.80e-12 |
|
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like homologs (PHLH) of molybdopterin binding (MopB) proteins. This CD is of the PHLH region homologous to the catalytic molybdopterin-binding subunit of MopB homologs.
Pssm-ID: 239165 [Multi-domain] Cd Length: 524 Bit Score: 67.90 E-value: 9.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 61 RLKTPMiRRQRGGKLEAVSWDEALDYVATRLSAIKAkyGPDAIQTTGSSRGTGNETnyVMQKFARAVIGTNNVDccarvu 140
Cdd:cd02764 99 RAQGPL-RRGIDGAYVASDWADFDAKVAEQLKAVKD--GGKLAVLSGNVNSPTTEA--LIGDFLKKYPGAKHVV------ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 141 HGPSVAGLHQSVGNGAMSNAIT---EIDNTDLVFIFGYN--PADSHPIVANHVINAKRNGAK------IIVCDPRKIETA 209
Cdd:cd02764 168 YDPLSAEDVNEAWQASFGKDVVpgyDFDKAEVIVSIDADflGSWISAIRHRHDFAAKRRLGAeepmsrLVAAESVYTLTG 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 210 RIADMHIALKNGSNIALLNAIGHVIIEEDlydksfvASRSEGfEEYRKIVEGYTPESVEEITGVSAQEIRACARMYASAK 289
Cdd:cd02764 248 ANADVRLAIRPSQEKAFALGLAHKLIKKG-------AGSSLP-DFFRALNLAFKPAKVAELTVDLDKALAALAKALAAAG 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 290 SAAILWGmGVTQFYQGVETVRSLTSLAILTGNLGKpnvGVNPVRGqnNVQGACDmgalpdtypgyqyvkfpeNREKFaKA 369
Cdd:cd02764 320 KSLVVAG-SELSQTAGADTQVAVNALNSLLGNDGK---TVDHARP--IKGGELG------------------NQQDL-KA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 370 WGVeslpahtgyriselphRAAHGEVRAAYIMGEDPLQTDAELSAVRKAFDDLELVIVQDIFMTKTASAADVILPST--- 446
Cdd:cd02764 375 LAS----------------RINAGKVSALLVYDVNPVYDLPQGLGFAKALEKVPLSVSFGDRLDETAMLCDWVAPMShgl 438
|
410
....*....|...
gi 1148879094 447 -SWGEHE---GVY 455
Cdd:cd02764 439 eSWGDAEtpdGTY 451
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
6-497 |
2.46e-11 |
|
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: 67.30 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 6 TVCPYCASGCKI-NLVVDNGKIVRAE----AAQGKTNQGTLCLKGYYG-WDFINDTQILTPRLKT-PMIRRQRGGKLEAV 78
Cdd:cd02760 2 TYCYNCVAGPDFmAVKVVDGVATEIEpnfaAEDIHPARGRVCVKAYGLvQKTYNPNRVLQPMKRTnPKKGRNEDPGFVPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 79 SWDEALDYVATRLSAIKAK-YGPDA--IQTTGSSRGTGNETNYvMQKFAR--AVIGTNNVDCCArvuhGPSVAGLH-QSV 152
Cdd:cd02760 82 SWDEALDLVAAKLRRVREKgLLDEKglPRLAATFGHGGTPAMY-MGTFPAflAAWGPIDFSFGS----GQGVKCVHsEHL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 153 GNGAMSNAITEIDNTDL---VFIFGYN-PADSHPIVANHVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLN 228
Cdd:cd02760 157 YGEFWHRAFTVAADTPLanyVISFGSNvEASGGPCAVTRHADARVRGYKRVQVEPHLSVTGACSAEWVPIRPKTDPAFMF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 229 AIGHVIIEE---DLYDKSFVASRS-------------------------------------------------------- 249
Cdd:cd02760 237 AMIHVMVHEqglGKLDVPFLRDRTsspylvgpdglylrdaatgkplvwdersgravpfdtrgavpavagdfavdgavsvd 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 250 -----------EGFEEYRKIVEG---YTPESVEEITGVSAQEIRACARMYASAKS----------------AAILWGMGV 299
Cdd:cd02760 317 addetaihqgvEGTTAFTMLVEHmrkYTPEWAESICDVPAATIRRIAREFLENASigstievdgvtlpyrpVAVTLGKSV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 300 TQFYQGVETVRSLTSLAILTGNLGKPN--VGVNPV--RGQNN----VQGACDMGALPDTYPGYQ--YVKFPENRE---KF 366
Cdd:cd02760 397 NNGWGAFECCWARTLLATLVGALEVPGgtLGTTVRlnRPHDDrlasVKPGEDGFMAQGFNPTDKehWVVKPTGRNahrTL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 367 AKAWGVESLPAHTGyriselPHRAAHGEVRAAYIMGEDPLQTDAEL-----SAVRKAFDD----------LELVIVQDIF 431
Cdd:cd02760 477 VPIVGNSAWSQALG------PTQLAWMFLREVPLDWKFELPTLPDVwfnyrTNPAISFWDtatlvdniakFPFTVSFAYT 550
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1148879094 432 MTKTASAADVILPSTSWGEHEGVYTA----------ADRGFQRFFKAVEPKWDLKTDWQIISEIATRMGYPMHYNN 497
Cdd:cd02760 551 EDETNWMADVLLPEATDLESLQMIKVggtkfveqfwEHRGVVLRQPAVEPQGEARDFTWISTELAKRTGLLADYNA 626
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
572-672 |
3.37e-11 |
|
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: 61.17 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 572 EYPMVLSTVREVGhYSCRSMTGNCAALAALADEPgYAQINTADAERLGIEDEELVWVNSRKGRIITRAQVSDRPNKGAVY 651
Cdd:cd02781 1 EYPLILTTGARSY-YYFHSEHRQLPSLRELHPDP-VAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVR 78
|
90 100
....*....|....*....|.
gi 1148879094 652 MTYQWWiGACNELVSENLSPI 672
Cdd:cd02781 79 AEHGWW-YPEREAGEPALGGV 98
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
61-486 |
7.62e-10 |
|
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: 61.51 E-value: 7.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 61 RLKTPMIRRqrGGKLEAVSWDEALDYVATRLSA-----IKAKYGP--DAiqttgssrgtgnETNYVMQKFARAViGTNNV 133
Cdd:cd02773 53 RLDKPYIRK--NGKLKPATWEEALAAIAKALKGvkpdeIAAIAGDlaDV------------ESMVALKDLLNKL-GSENL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 134 DCcarvuhgpSVAGLHQSVGNGA---MSNAITEIDNTDLVFIFGYNPADSHPIVanhvinakrngakiivcdprkieTAR 210
Cdd:cd02773 118 AC--------EQDGPDLPADLRSnylFNTTIAGIEEADAVLLVGTNPRFEAPVL-----------------------NAR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 211 IADMhiALKNGSNIALlnaIGHviiEEDL-YDKSFVasrsegfeeyrkiveGYTPESVEEItgvsAQEIRACARMYASAK 289
Cdd:cd02773 167 IRKA--WLHGGLKVGV---IGP---PVDLtYDYDHL---------------GTDAKTLQDI----ASGKHPFSKALKDAK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 290 SAAILWGMGVTQFYQGVETVRSLTSLAILTGNLGKPNVGVNPVRGQNNVQGACDMGALPDTypgyqyvkfpenrekfaka 369
Cdd:cd02773 220 KPMIIVGSGALARKDGAAILAAVAKLAKKNGVVREGWNGFNVLHRAASRVGALDLGFVPGA------------------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 370 wgveslpahtgyriselPHRAAHGEVRAAYIMGEDPLQTDAelsAVRKAFddlelVIVQDIFMTKTASAADVILPSTSWG 449
Cdd:cd02773 281 -----------------GAIRKSGPPKVLYLLGADEIDITP---IPKDAF-----VVYQGHHGDRGAQIADVILPGAAYT 335
|
410 420 430
....*....|....*....|....*....|....*..
gi 1148879094 450 EHEGVYTAADRGFQRFFKAVEPKWDLKTDWQIISEIA 486
Cdd:cd02773 336 EKSGTYVNTEGRVQQTRKAVSPPGDAREDWKILRALS 372
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
573-685 |
1.37e-08 |
|
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: 53.44 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 573 YPMVLSTVRevGHYSCRSMTGNCAALAALADEPgYAQINTADAERLGIEDEELVWVNSRKGRIITRAQVSDRPNKGAVYM 652
Cdd:cd02786 1 YPLRLITPP--AHNFLNSTFANLPELRAKEGEP-TLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVVVA 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1148879094 653 TYQWWI------GACNELVSENLSPITKTPEYKYCAVNV 685
Cdd:cd02786 78 EGGWWRehspdgRGVNALTSARLTDLGGGSTFHDTRVEV 116
|
|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
607-688 |
8.65e-07 |
|
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: 48.22 E-value: 8.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 607 YAQINTADAERLGIEDEELVWVNSRKGRIITRAQVSDRPNKGAVYMTYQWWIGACNELVSENLSPITKTPEYKYCAVNVE 686
Cdd:cd02779 34 YIEVNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKPGQTFMLMAHPRPGANGLVTPYVDPETIIPYYKGTWANIR 113
|
..
gi 1148879094 687 RI 688
Cdd:cd02779 114 KI 115
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
610-687 |
2.36e-06 |
|
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: 46.90 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 610 INTADAERLGIEDEELVWVNSRKGRIITRAQVSDRPNKGAVYMTYQWWI----------GACNELVSENLSPITKTPEYK 679
Cdd:cd02794 34 INPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVVALPQGAWYepdangidkgGCINTLTGLRPSPLAKGNPQH 113
|
....*...
gi 1148879094 680 YCAVNVER 687
Cdd:cd02794 114 TNLVQVEK 121
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
573-687 |
1.20e-05 |
|
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: 45.27 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 573 YPMVLSTVrevgHYSCR--SMTGNCAALAALADEPGY--AQINTADAERLGIEDEELVWVNSRKGRIITRAQVSDRPNKG 648
Cdd:cd02777 1 YPLQLISP----HPKRRlhSQLDNVPWLREAYKVKGRepVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPG 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1148879094 649 AVYMTYQWWI-----------GACNELVSENLSP-ITKTPEYKYCAVNVER 687
Cdd:cd02777 77 VVALPEGAWYdpddnggldkgGNPNVLTSDIPTSkLAQGNPANTCLVEIEK 127
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
573-641 |
2.12e-05 |
|
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: 44.98 E-value: 2.12e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1148879094 573 YPMVLSTVREVGHyscRSMTGNCAALAALADEpGYAQINTADAERLGIEDEELVWVNSRKGRIITRAQV 641
Cdd:cd02780 1 YPFILVTFKSNLN---SHRSANAPWLKEIKPE-NPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKV 65
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| FwdD |
COG1153 |
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion]; |
603-687 |
2.69e-05 |
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Formylmethanofuran dehydrogenase subunit D [Energy production and conversion];
Pssm-ID: 440767 [Multi-domain] Cd Length: 127 Bit Score: 44.07 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 603 DEPGYAQINTADAERLGIEDEELVWVNSRKGRIITRAQVSDRPNKGAVYMTYQWWigaCNELVSENLSPiTKTPEYKYCA 682
Cdd:COG1153 28 DACAVCELNPEDMKKLGIKEGDKVKVTSEYGEVVVKAKESEDLHPGLVFIPMGPW---ANAVVPPETHS-TGMPDFKGVP 103
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....*
gi 1148879094 683 VNVER 687
Cdd:COG1153 104 VEVEP 108
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| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
590-656 |
3.40e-05 |
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The MopB_CT_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. Also included in this CD is the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), which has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. The MopB_CT_Thiosulfate-R-like CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239179 [Multi-domain] Cd Length: 123 Bit Score: 43.80 E-value: 3.40e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1148879094 590 SMTGNCAALAALaDEPGYAQINTADAERLGIEDEELVWVNSRKGRIITRAQVSDRPNKGAVYMTYQW 656
Cdd:cd02778 15 GHTANNPLLHEL-TPENTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMPHGF 80
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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 ... |
590-650 |
4.12e-05 |
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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: 42.68 E-value: 4.12e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1148879094 590 SMTGNCAALAALADEPgYAQINTADAERLGIEDEELVWVNSRKGRIITRAQVSDRPNKGAV 650
Cdd:cd02788 14 ELSQRSPVIAERAPAP-YARLSPADAARLGLADGDLVEFSLGDGTLTLPVQISKYLPAGVV 73
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| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
606-687 |
4.94e-05 |
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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: 43.54 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148879094 606 GYAQINTADAERLGIEDEELVWVNSRKGRIITRAQVSDRPNKGAVYMTYQWWIG-------------ACNELVSEN-LSP 671
Cdd:cd02782 33 CTLRIHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMPGVVSLPHGWGHDypgvsgagsrpgvNVNDLTDDTqRDP 112
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90
....*....|....*.
gi 1148879094 672 ITKTPEYKYCAVNVER 687
Cdd:cd02782 113 LSGNAAHNGVPVRLAR 128
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| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
604-652 |
4.08e-04 |
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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.This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239194 [Multi-domain] Cd Length: 129 Bit Score: 40.70 E-value: 4.08e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1148879094 604 EPgyAQINTADAERLGIEDEELVWVNSRKGRIITRAQVSDRPNKGAVYM 652
Cdd:cd02793 33 EP--IRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPGVVQL 79
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| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
610-657 |
7.38e-04 |
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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. This CD (MopB_CT_Nitrate-R-NarG-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239177 [Multi-domain] Cd Length: 141 Bit Score: 40.44 E-value: 7.38e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1148879094 610 INTADAERLGIEDEELVWVNSRKGRIITRAQVSDRPNKGAVYMtYQWW 657
Cdd:cd02776 35 MNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTVFM-YHAQ 81
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| MopB_CT_FmdC-FwdD |
cd02789 |
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran ... |
603-657 |
3.90e-03 |
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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: 37.41 E-value: 3.90e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1148879094 603 DEPGYAQINTADAERLGIEDEELVWVNSRKGRIITRAQVSDRPNKGAVYMTYQWW 657
Cdd:cd02789 28 DACAYCEINPEDYKLLGKPEGDKVKVTSEFGEVVVFAKENEGVPEGMVFIPMGPW 82
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