|
Name |
Accession |
Description |
Interval |
E-value |
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
10-624 |
0e+00 |
|
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: 743.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 10 KTACILCSLNCGLEVQTENGRISKIRGDDDHPASQGYVCEKSQRMDYYQNGADRLDTPMRRRPdGSYEAIDWDTAIREVA 89
Cdd:cd02762 1 KRACILCEANCGLVVTVEDGRVASIRGDPDDPLSKGYICPKAAALGDYQNDPDRLRTPMRRRG-GSFEEIDWDEAFDEIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 90 EKFLAIKRRHGGESILYYGGGAQGN-HLGGAYGDSTLKALG-VKYRSNALAQEKTGEFWVQG--KMFGTGVHGDFEHCEG 165
Cdd:cd02762 80 ERLRAIRARHGGDAVGVYGGNPQAHtHAGGAYSPALLKALGtSNYFSAATADQKPGHFWSGLmfGHPGLHPVPDIDRTDY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 166 AILIGKNPWQSHGFARA---RVLLNAMAKDPARSIIVIDPRLSETAALADFHLQIRPGTDAWCLAALVGIIVQDGLLARD 242
Cdd:cd02762 160 LLILGANPLQSNGSLRTapdRVLRLKAAKDRGGSLVVIDPRRTETAKLADEHLFVRPGTDAWLLAAMLAVLLAEGLTDRR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 243 WLAEHTSGYEHIVDELNAIPVAYCAETCGVAEDKLRAAARRIASASSVSALEDLGMQMNLHSTLGSYLQRLVWLLTGHYG 322
Cdd:cd02762 240 FLAEHCDGLDEVRAALAEFTPEAYAPRCGVPAETIRRLAREFAAAPSAAVYGRLGVQTQLFGTLCSWLVKLLNLLTGNLD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 323 RPGTSNAFVPFLSLSKASKGDTSMGKrgaprvEKRSPVANAKIIIGLIPCNVIPEEILTDHPKRYRAMLVETGNPLHSLA 402
Cdd:cd02762 320 RPGGAMFTTPALDLVGQTSGRTIGRG------EWRSRVSGLPEIAGELPVNVLAEEILTDGPGRIRAMIVVAGNPVLSAP 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 403 DSQRMREAMRALELSVVIDVAMTETARHADYVLPAASQFEKAEATFFNLEFPRNAFHLRAPLFPARPGTLPEAEIHARLL 482
Cdd:cd02762 394 DGARLEAALGGLEFMVSVDVYMTETTRHADYILPPASQLEKPHATFFNLEFPRNAFRYRRPLFPPPPGTLPEWEILARLV 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 483 EAMgvlgekdyrplrlalklgrkafsaaflaaaatrpkvmkyapvllyrtlgptlpagmeaaaaiwgicqlhvlnnrKTA 562
Cdd:cd02762 474 EAL--------------------------------------------------------------------------DAV 479
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597910 563 ARAGFDGLPPLaADRLFQAMLDNPSGVVFAETTYAEsWQAVARPEQRINLHIPELLPELAKL 624
Cdd:cd02762 480 LRAGFYGERAG-GTLLLAALLERPSGVDLGPLTPRL-WQRLRTPDGRIHLAPPELLDELRRL 539
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
1-762 |
4.00e-142 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 433.50 E-value: 4.00e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 1 MTTPSPQWKKTACILCSLNCGLEVQTENGRISKIRGDDDHPASQGYVCEKSQRMDYYQNGADRLDTPMRR---RPDGSYE 77
Cdd:COG0243 16 LEAAGTKTVKTTCPGCGVGCGLGVKVEDGRVVRVRGDPDHPVNRGRLCAKGAALDERLYSPDRLTYPMKRvgpRGSGKFE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 78 AIDWDTAIREVAEKFLAIKRRHGGESILYYGGGAQGNHLGG--AYGDSTL-KALGVKYRSNALAQEKTGEFWVQGKMFGT 154
Cdd:COG0243 96 RISWDEALDLIAEKLKAIIDEYGPEAVAFYTSGGSAGRLSNeaAYLAQRFaRALGTNNLDDNSRLCHESAVAGLPRTFGS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 155 GVHG----DFEHCEGAILIGKNPWQSHGFARARvLLNAMAKDPARsIIVIDPRLSETAALADFHLQIRPGTDAWCLAALV 230
Cdd:COG0243 176 DKGTvsyeDLEHADLIVLWGSNPAENHPRLLRR-LREAAKKRGAK-IVVIDPRRTETAAIADEWLPIRPGTDAALLLALA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 231 GIIVQDGLLARDWLAEHTSGYEHIVDELNAIPVAYCAETCGVAEDKLRAAARRIASASSVSALEDLGMQMNLHSTLGSYL 310
Cdd:COG0243 254 HVLIEEGLYDRDFLARHTVGFDELAAYVAAYTPEWAAEITGVPAEDIRELAREFATAKPAVILWGMGLQQHSNGTQTVRA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 311 QRLVWLLTGHYGRPGTSnafvpflslskaskgdtsmgkrgaprvekrspvanakiiigliPCNVIPEEILTDHPKRYRAM 390
Cdd:COG0243 334 IANLALLTGNIGKPGGG-------------------------------------------PFSLTGEAILDGKPYPIKAL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 391 LVETGNPLHSLADSQRMREAMRALELSVVIDVAMTETARHADYVLPAASQFEKAEaTFFNLEfpRNAFHLRAPLFPARPG 470
Cdd:COG0243 371 WVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARYADIVLPATTWLERDD-IVTNSE--DRRVHLSRPAVEPPGE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 471 TLPEAEIHARLLEAMGVLGEKDYRP-----LRLALKlgrkafsaaflaaaATRPKVMKYApvlLYRTLGPtlpagmeaaa 545
Cdd:COG0243 448 ARSDWEIFAELAKRLGFEEAFPWGRteedyLRELLE--------------ATRGRGITFE---ELREKGP---------- 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 546 aiwgicqlhvlnnrktaARAGFDGLPPLAADRLFQamldNPSGvvfaettyaeswqavarpeqRINLHIPEL----LPEL 621
Cdd:COG0243 501 -----------------VQLPVPPEPAFRNDGPFP----TPSG--------------------KAEFYSETLalppLPRY 539
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 622 AKLAHSAPPHDPAYPFILAAGeRRSDTSNTAVRDTGWHRR-GRYGTLRISPQDAEALGCADGEVLRVVTRRGEVEAEVEI 700
Cdd:COG0243 540 APPYEGAEPLDAEYPLRLITG-RSRDQWHSTTYNNPRLREiGPRPVVEINPEDAAALGIKDGDLVRVESDRGEVLARAKV 618
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597910 701 SDMMQPGNISLPNGQGLDYRNaegevvRRGVAPNEVTDcTQRDFLAGTPWHKYVPARLERLA 762
Cdd:COG0243 619 TEGIRPGVVFAPHGWWYEPAD------DKGGNVNVLTP-DATDPLSGTPAFKSVPVRVEKAA 673
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
7-762 |
9.44e-85 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 282.93 E-value: 9.44e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 7 QWKKTACILCSLNCGLEVQTENGRISKIRGDDDHPASQGYVCEKSQRMDYYQNGADRLDTPMRRRpDGSYEAIDWDTAIR 86
Cdd:COG3383 5 KKVKTVCPYCGVGCGIDLEVKDGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVNSPDRLTTPLIRR-GGEFREVSWDEALD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 87 EVAEKFLAIKRRHGGESILYYGGGAQGN------------HLGGAYGD--------STLKALGvkyrsnalaqektgefw 146
Cdd:COG3383 84 LVAERLREIQAEHGPDAVAFYGSGQLTNeenyllqklargVLGTNNIDnnarlcmaSAVAGLK----------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 147 vqgKMFGTGVHG----DFEHCEGAILIGKNPWQSHGFARARVLlnaMAKDPARSIIVIDPRLSETAALADFHLQIRPGTD 222
Cdd:COG3383 147 ---QSFGSDAPPnsydDIEEADVILVIGSNPAEAHPVLARRIK---KAKKNGAKLIVVDPRRTETARLADLHLQIKPGTD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 223 AWCLAALVGIIVQDGLLARDWLAEHTSGYEHIVDELNAIPVAYCAETCGVAEDKLRAAARRIASASSVSALedLGMQMNL 302
Cdd:COG3383 221 LALLNGLLHVIIEEGLVDEDFIAERTEGFEELKASVAKYTPERVAEITGVPAEDIREAARLIAEAKRAMIL--WGMGVNQ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 303 HSTlGSYLQRLV---WLLTGHYGRPGTSnafvpFLSLSK----------ASKGDTSMGKRGAPRVEKRSPVANAKIIIGL 369
Cdd:COG3383 299 HTQ-GTDNVNAIinlALATGNIGRPGTG-----PFPLTGqnnvqggrdmGALPNVLPGYRDVTDPEHRAKVADAWGVPPL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 370 iPCNV------IPEEILTDHPKryrAMLVETGNPLHSLADSQRMREAMRALELSVVIDVAMTETARHADYVLPAASQFEK 443
Cdd:COG3383 373 -PDKPgltaveMFDAIADGEIK---ALWIIGENPAVSDPDANHVREALEKLEFLVVQDIFLTETAEYADVVLPAASWAEK 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 444 aEATFFNLEfpRNaFHLRAPLFPARPGTLPEAEIHARLLEAMGVlgEKDYrplrlalklgrkafsaaflaaaatrpkvmk 523
Cdd:COG3383 449 -DGTFTNTE--RR-VQRVRKAVEPPGEARPDWEIIAELARRLGY--GFDY------------------------------ 492
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 524 yapvllyrtlgptlpagmEAAAAIWG-ICQLHVLNNRKTAARagfdglppLAADRLFQ---AMLDNPSGVVFaettYAES 599
Cdd:COG3383 493 ------------------DSPEEVFDeIARLTPDYSGISYER--------LEALGGVQwpcPSEDHPGTPRL----FTGR 542
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 600 WqavARPEQRINLHIPELLPelaklahSAPPHDPAYPFILAAGeRRSDTSNTAVRdTGW----HRRGRYGTLRISPQDAE 675
Cdd:COG3383 543 F---PTPDGKARFVPVEYRP-------PAELPDEEYPLVLTTG-RLLDQWHTGTR-TRRsprlNKHAPEPFVEIHPEDAA 610
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 676 ALGCADGEVLRVVTRRGEVEAEVEISDMMQPGNISLPngqgldYRNAEGEVvrrgvapNEVTdCTQRDFLAGTPWHKYVP 755
Cdd:COG3383 611 RLGIKDGDLVRVSSRRGEVVLRARVTDRVRPGTVFMP------FHWGEGAA-------NALT-NDALDPVSKQPEYKACA 676
|
....*..
gi 15597910 756 ARLERLA 762
Cdd:COG3383 677 VRVEKVA 683
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
10-485 |
9.92e-78 |
|
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: 254.95 E-value: 9.92e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 10 KTACILCSLNCGLEVQTENGRISKIRGDDDHPASQGYVCEKSQRMDYYQNGADRLDTPMRRR-PDGSYEAIDWDTAIREV 88
Cdd:cd00368 1 PSVCPFCGVGCGILVYVKDGKVVRIEGDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVgGRGKFVPISWDEALDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 89 AEKFLAIKRRHGGESILYYGGGAQGNHLGGAYGDSTLKALGVKYRSNA-LAQEKTGEFWVQ-GKMFGTGVHGDFEHCEGA 166
Cdd:cd00368 81 AEKLKEIREKYGPDAIAFYGGGGASNEEAYLLQKLLRALGSNNVDSHArLCHASAVAALKAfGGGAPTNTLADIENADLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 167 ILIGKNPWQSHGFARARVllnAMAKDPARSIIVIDPRLSETAALADFHLQIRPGTDAWCLAAlvgiivqdgllardwlae 246
Cdd:cd00368 161 LLWGSNPAETHPVLAARL---RRAKKRGAKLIVIDPRRTETAAKADEWLPIRPGTDAALALA------------------ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 247 htsgyehivdelnaipvAYCAETCGVAEDKLRAAARRIASASSVSALEDLGMQMNLHSTLGSYLQRLVWLLTGHYGRPGT 326
Cdd:cd00368 220 -----------------EWAAEITGVPAETIRALAREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 327 snafvpflslskaskgdtsmgkrgaprvekrspvanakiiiGLIPCnvipeeiltdhpkryramlvetGNPLHSLADSQR 406
Cdd:cd00368 283 -----------------------------------------GLGPG----------------------GNPLVSAPDANR 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 407 MREAMRALELSVVIDVAMTETARHADYVLPAASQFEKaEATFFNLEfpRNAFHLRAPLFParPG-TLPEAEIHARLLEAM 485
Cdd:cd00368 300 VRAALKKLDFVVVIDIFMTETAAYADVVLPAATYLEK-EGTYTNTE--GRVQLFRQAVEP--PGeARSDWEILRELAKRL 374
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
10-487 |
1.21e-72 |
|
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: 247.14 E-value: 1.21e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 10 KTACILCSLNCGLEVQTENGRISKIRGDDDHPASQGYVCEKSQRMDYYQNGADRLDTPMRRRPDGSYEAIDWDTAIREVA 89
Cdd:cd02754 1 KTTCPYCGVGCGVEIGVKDGKVVAVRGDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLLRRNGGELVPVSWDEALDLIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 90 EKFLAIKRRHGGESILYYGGGAQ-------GNHLGGAY-------GDSTL---KALGVKYRSnalaqektgefwvqgkmF 152
Cdd:cd02754 81 ERFKAIQAEYGPDSVAFYGSGQLlteeyyaANKLAKGGlgtnnidTNSRLcmaSAVAGYKRS-----------------F 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 153 G----TGVHGDFEHCEGAILIGKNPWQSHGFARARVLLNAMAKDPARsIIVIDPRLSETAALADFHLQIRPGTDAWCLAA 228
Cdd:cd02754 144 GadgpPGSYDDIEHADCFFLIGSNMAECHPILFRRLLDRKKANPGAK-IIVVDPRRTRTADIADLHLPIRPGTDLALLNG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 229 LVGIIVQDGLLARDWLAEHTSGYEHIVDELNAIPVAYCAETCGVAEDKLRAAARRIASASSVSALEDLGMQ--------- 299
Cdd:cd02754 223 LLHVLIEEGLIDRDFIDAHTEGFEELKAFVADYTPEKVAEITGVPEADIREAARLFGEARKVMSLWTMGVNqstqgtaan 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 300 ---MNLHstlgsylqrlvwLLTGHYGRPGTSnafvPFlSLSkaskGD-TSMGKR---------GAPRV----EKRSPVAN 362
Cdd:cd02754 303 naiINLH------------LATGKIGRPGSG----PF-SLT----GQpNAMGGRevgglanllPGHRSvnnpEHRAEVAK 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 363 A-KIIIGLIPCNV------IPEEILTDHPKryrAMLVETGNPLHSLADSQRMREAMRALELSVVIDV-AMTETARHADYV 434
Cdd:cd02754 362 FwGVPEGTIPPKPglhaveMFEAIEDGEIK---ALWVMCTNPAVSLPNANRVREALERLEFVVVQDAfADTETAEYADLV 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 15597910 435 LPAASQFEKaEATFFNLEfpRNAFHLRAplFPARPG-TLPEAEIHARLLEAMGV 487
Cdd:cd02754 439 LPAASWGEK-EGTMTNSE--RRVSLLRA--AVEPPGeARPDWWILADVARRLGF 487
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
16-490 |
9.90e-62 |
|
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: 215.96 E-value: 9.90e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 16 CSLNC----GLEVQTENGRISKIRGDDDHPASQGYVCEKSQRMDYYQNGADRLDTPMRR--RPDGSYEAIDWDTAIREVA 89
Cdd:cd02766 4 CPLDCpdtcSLLVTVEDGRIVRVEGDPAHPYTRGFICAKGARYVERVYSPDRLLTPLKRvgRKGGQWERISWDEALDTIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 90 EKFLAIKRRHGGESILYYGG-GAQG----------NHLGGAygdSTLKalgvkyRSNALAQEKTGEFWVQGKMFGTGVHg 158
Cdd:cd02766 84 AKLKEIKAEYGPESILPYSYaGTMGllqraargrfFHALGA---SELR------GTICSGAGIEAQKYDFGASLGNDPE- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 159 DFEHCEGAILIGKNP-W-QSHGFARARvllnaMAKDPARSIIVIDPRLSETAALADFHLQIRPGTDAWCLAALVGIIVQD 236
Cdd:cd02766 154 DMVNADLIVIWGINPaAtNIHLMRIIQ-----EARKRGAKVVVIDPYRTATAARADLHIQIRPGTDGALALGVAKVLFRE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 237 GLLARDWLAEHTSGYEHIVDELNAIPVAYCAETCGVAEDKLRAAARRIASASSVSALEDLGMQ------MNLH--STLGS 308
Cdd:cd02766 229 GLYDRDFLARHTEGFEELKAHLETYTPEWAAEITGVSAEEIEELARLYGEAKPPSIRLGYGMQryrnggQNVRaiDALPA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 309 ylqrlvwlLTGHYGRPGtsnafvpflslskaskGDTSMGKRGAPrvekrspvanakiiiglipcnvipeeiltdhpkrYR 388
Cdd:cd02766 309 --------LTGNIGVPG----------------GGAFYSNSGPP----------------------------------VK 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 389 AMLVETGNPLHSLADSQRMREAM-RALELSVVIDVAMTETARHADYVLPAASQFEKAE--ATFFNLEFPRNafhlrAPLF 465
Cdd:cd02766 331 ALWVYNSNPVAQAPDSNKVRKGLaREDLFVVVHDQFMTDTARYADIVLPATTFLEHEDvyASYWHYYLQYN-----EPAI 405
|
490 500
....*....|....*....|....*
gi 15597910 466 PARPGTLPEAEIHARLLEAMGVLGE 490
Cdd:cd02766 406 PPPGEARSNTEIFRELAKRLGFGEP 430
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
11-758 |
3.91e-61 |
|
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: 218.10 E-value: 3.91e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 11 TACILCSLNCGLEVQTENGRISKIRGDDDHPASQGYVCEKSQRMDYYQNGADRLDTPMRRRPDgSYEAIDWDTAIREVAE 90
Cdd:TIGR01591 1 TVCPYCGVGCSLNLVVKDGKIVRVEPYQGHKANRGHLCVKGYFAWEFINSKDRLTTPLIREGD-KFREVSWDEAISYIAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 91 KFLAIKRRHGGESILYYGGGAQGNHLGGAYGDSTLKALGVKYRSNA--LAQEKTGEFWVQ--GKMFGTGVHGDFEHCEGA 166
Cdd:TIGR01591 80 KLKEIKEKYGPDSIGFIGSSRGTNEENYLLQKLARAVIGTNNVDNCarVCHGPSVAGLKQtvGIGAMSNTISEIENADLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 167 ILIGKNPWQSHGFArARVLLNAmaKDPARSIIVIDPRLSETAALADFHLQIRPGTDAWCLAALVGIIVQDGLLARDWLAE 246
Cdd:TIGR01591 160 VIIGYNPAESHPVV-AQYLKNA--KRNGAKIIVIDPRKTETAKIADLHIPLKPGTDIALLNAMANVIIEEGLYDKAFIEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 247 HTSGYEHIVDELNAIPVAYCAETCGVAEDKLRAAARRIASASSVSALEDLGMQMNLH--STLGSYLQRLvwLLTGHYGRP 324
Cdd:TIGR01591 237 RTEGFEEFREIVKGYTPEYVEDITGVPADLIREAARMYAKAGSAAILWGMGVTQHSQgvETVMALINLA--MLTGNIGKP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 325 GTSnafVPFLSLSKASKGDTSMGK--RGAPRVEKRSPVANAKIIIGL-----IPCNV---IPEEILTDHPKRYRAMLVET 394
Cdd:TIGR01591 315 GGG---VNPLRGQNNVQGACDMGAlpDFLPGYQPVSDEEVREKFAKAwgvvkLPAEPglrIPEMIDAAADGDVKALYIMG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 395 GNPLHSLADSQRMREAMRALELSVVIDVAMTETARHADYVLPAASQFEKaEATFFNLEfpRNAFHLRAPLFParPGTL-P 473
Cdd:TIGR01591 392 EDPLQSDPNTSKVRKALEKLELLVVQDIFMTETAKYADVVLPAAAWLEK-EGTFTNAE--RRIQRFFKAVEP--KGESkP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 474 EAEIHARLLEAMGVLGEKDYrplrlalklgrkafsaaflaaaatrPK-VMKYApvllyRTLGPtLPAGMeaaaaiwgicq 552
Cdd:TIGR01591 467 DWEIIQELANALGLDWNYNH-------------------------PQeIMDEI-----RELTP-LFAGL----------- 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 553 lhvlnNRKTAARAGFDGLPPLAADRLFQAML-----DNPSG-VVFAETTYaeswqaVARPEQRinlhipellpelaklah 626
Cdd:TIGR01591 505 -----TYERLDELGSLQWPCNDSDASPTSYLykdkfATPDGkAKFIPLEW------VAPIEEP----------------- 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 627 sapphDPAYPFILAAGE--RRSDTSNTAVRDTGWHRRGRYGTLRISPQDAEALGCADGEVLRVVTRRGEVEAEVEISDMM 704
Cdd:TIGR01591 557 -----DDEYPLILTTGRvlTHYNVGEMTRRVAGLRRLSPEPYVEINTEDAKKLGIKDGDLVKVKSRRGEITLRAKVSDRV 631
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 15597910 705 QPGNISLPngqgldYRNAEGEVvrrgvapNEVTdCTQRDFLAGTPWHKYVPARL 758
Cdd:TIGR01591 632 NKGAIYIT------MHFWDGAV-------NNLT-TDDLDPISGTPEYKYTAVRI 671
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
10-486 |
1.94e-60 |
|
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: 212.46 E-value: 1.94e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 10 KTACILCSLNCGLEVQTENGRISKIRGDDDHPASQGYVCEKSQRMDYYQNGADRLDTPMRRRPDGSYEAiDWDTAIREVA 89
Cdd:cd02753 1 KTVCPYCGVGCGLELWVKDNKIVGVEPVKGHPVNRGKLCVKGRFGFDFVNSKDRLTKPLIRKNGKFVEA-SWDEALSLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 90 EKFLAIKRRHGGESILYYGGGAQGNH------------LGGAYGD--------STLKALgvkyrsnalaQEKTGEfwvqG 149
Cdd:cd02753 80 SRLKEIKDKYGPDAIAFFGSAKCTNEenylfqklaravGGTNNVDhcarlchsPTVAGL----------AETLGS----G 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 150 KMfgTGVHGDFEHCEGAILIGKNPWQSHGFARARVLLnaMAKDPARsIIVIDPRLSETAALADFHLQIRPGTDAWCLAAL 229
Cdd:cd02753 146 AM--TNSIADIEEADVILVIGSNTTEAHPVIARRIKR--AKRNGAK-LIVADPRRTELARFADLHLQLRPGTDVALLNAM 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 230 VGIIVQDGLLARDWLAEHTSGYEHIVDELNAIPVAYCAETCGVAEDKLRAAARRIASASSVSALEDLGMQMNLHstlGSY 309
Cdd:cd02753 221 AHVIIEEGLYDEEFIEERTEGFEELKEIVEKYTPEYAERITGVPAEDIREAARMYATAKSAAILWGMGVTQHSH---GTD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 310 LQRLV---WLLTGHYGRPGTsnAFVPFlslskaskgdtsmgkRGAPRVEKRSPVanakiiiGLIPcNVIPEEIltdhpkr 386
Cdd:cd02753 298 NVMALsnlALLTGNIGRPGT--GVNPL---------------RGQNNVQGACDM-------GALP-NVLPGYV------- 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 387 yRAMLVETGNPLHSLADSQRMREAMRALELSVVIDVAMTETARHADYVLPAASQFEKaEATFFNLEfpRNaFHLRAPLFP 466
Cdd:cd02753 346 -KALYIMGENPALSDPNTNHVRKALESLEFLVVQDIFLTETAELADVVLPAASFAEK-DGTFTNTE--RR-VQRVRKAVE 420
|
490 500
....*....|....*....|.
gi 15597910 467 ArPGTL-PEAEIHARLLEAMG 486
Cdd:cd02753 421 P-PGEArPDWEIIQELANRLG 440
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
10-481 |
2.73e-58 |
|
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: 205.62 E-value: 2.73e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 10 KTACILCSLNCGLEVQTENGRISKIRGDDDHPASQGYVCEKSQRMDYYQNGADRLDTPMRR---RPDGSYEAIDWDTAIR 86
Cdd:cd02759 1 KGTCPGCHSGCGVLVYVKDGKLVKVEGDPNHPTNKGRLCMRGLAAPEIVYHPDRLLYPLKRvgeRGENKWERISWDEALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 87 EVAEKFLAIKRRHGGESILYYGGGAQGnhlgGAYGDSTLKALGVK--------------YRSNALAQEKTGEFWvqgkmf 152
Cdd:cd02759 81 EIAEKLAEIKAEYGPESIATAVGTGRG----TMWQDSLFWIRFVRlfgspnlflsgescYWPRDMAHALTTGFG------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 153 GTGVHGDFEHCEGAILIGKNPWQSHGFARARVLLNAMAKdpARSIIVIDPRLSETAALADFHLQIRPGTDAWCLAALVGI 232
Cdd:cd02759 151 LGYDEPDWENPECIVLWGKNPLNSNLDLQGHWLVAAMKR--GAKLIVVDPRLTWLAARADLWLPIRPGTDAALALGMLNV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 233 IVQDGLLARDWLAEHTSGYEHIVDELNAIPVAYCAETCGVAEDKLRAAARRIASASSVSALEDLGMQMNLHSTLGSYLQR 312
Cdd:cd02759 229 IINEGLYDKDFVENWCYGFEELAERVQEYTPEKVAEITGVPAEKIRKAARLYATAKPACIQWGLAIDQQKNGTQTSRAIA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 313 LVWLLTGHYGRPGtsnafvpflslskaskgdtsmGKRGAPRvekrsPVanakiiiglipcnvipeeiltdhpkryRAMLV 392
Cdd:cd02759 309 ILRAITGNLDVPG---------------------GNLLIPY-----PV---------------------------KMLIV 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 393 ETGNPLHSLADSQRMREAMRALELSVVIDVAMTETARHADYVLPAASQFEK--AEATFFNLEFPRNAFHLRAPLFPARPG 470
Cdd:cd02759 336 FGTNPLASYADTAPVLEALKALDFIVVVDLFMTPTAMLADIVLPVAMSLERpgLRGGFEAENFVQLRQKAVEPYGEAKSD 415
|
490
....*....|.
gi 15597910 471 TLPEAEIHARL 481
Cdd:cd02759 416 YEIVLELGKRL 426
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
634-761 |
4.75e-57 |
|
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: 190.68 E-value: 4.75e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 634 AYPFILAAGERRSDTSNT-AVRDTGWHRRGRYGTLRISPQDAEALGCADGEVLRVVTRRGEVEAEVEISDMMQPGNISLP 712
Cdd:cd02782 1 DYPFLLLIGRRHLRSNNSwLHNDPRLVKGRNRCTLRIHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMPGVVSLP 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 15597910 713 NGQGLDYRNAEGEVVRRGVAPNEVTDCTQRDFLAGTPWHKYVPARLERL 761
Cdd:cd02782 81 HGWGHDYPGVSGAGSRPGVNVNDLTDDTQRDPLSGNAAHNGVPVRLARV 129
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
11-489 |
1.33e-50 |
|
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: 183.65 E-value: 1.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 11 TACILCSLNCGLEVQTENGRISKIRGDDDHPASQGYVCEKSQRMDYYQNGADRLDTPMRR---RPDGSYEAIDWDTAIRE 87
Cdd:cd02755 3 SICEMCSSRCGILARVEDGRVVKIDGNPLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRvgeRGEGKFREASWDEALQY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 88 VAEKFLAIKRRHGGESILYYGGGAQGN----HLGGAYGDST-LKALGVKYRSNALAQEktgefWVQGkMFGTGVHGDFEH 162
Cdd:cd02755 83 IASKLKEIKEQHGPESVLFGGHGGCYSpffkHFAAAFGSPNiFSHESTCLASKNLAWK-----LVID-SFGGEVNPDFEN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 163 CEGAILIGKNPWQSHGFARARVLLNAMAKDpARsIIVIDPRLSETAALADFHLQIRPGTDAWCLAALVGIIVQDGLLARD 242
Cdd:cd02755 157 ARYIILFGRNLAEAIIVVDARRLMKALENG-AK-VVVVDPRFSELASKADEWIPIKPGTDLAFVLALIHVLISENLYDAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 243 WLAEHTSGYEHIVDELNAIPVAYCAETCGVAEDKLRAAARRIASASSVSALEDLGM-QMNLHSTLGSYLQRLVWLLTGHY 321
Cdd:cd02755 235 FVEKYTNGFELLKAHVKPYTPEWAAQITDIPADTIRRIAREFAAAAPHAVVDPGWRgTFYSNSFQTRRAIAIINALLGNI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 322 GRPGtsnafvpflslskaskgdtsmgkrgaprvekrspvanakiiiGLIPCNVIpeeiltdHPKRYRAMLVETGNPLHSL 401
Cdd:cd02755 315 DKRG------------------------------------------GLYYAGSA-------KPYPIKALFIYRTNPFHSM 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 402 ADSQRMREAMRALELSVVIDVAMTETARHADYVLPAASQFEKAEaTFFNLEFPRNAFHLRAPLFPARPGTLPEAEIHARL 481
Cdd:cd02755 346 PDRARLIKALKNLDLVVAIDILPSDTALYADVILPEATYLERDE-PFSDKGGPAPAVATRQRAIEPLYDTRPGWDILKEL 424
|
....*...
gi 15597910 482 LEAMGVLG 489
Cdd:cd02755 425 ARRLGLFG 432
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
16-493 |
4.25e-39 |
|
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: 153.54 E-value: 4.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 16 CSLNCGLEVQTENGRISKIRGDDDH---PASQGyvceKSQRMDYYqnGADRLDTPMRR-------------RPDGSYEAI 79
Cdd:cd02751 3 ACHWGPFKAHVKDGVIVRVEPDDTDqprPCPRG----RSVRDRVY--SPDRIKYPMKRvgwlgngpgsrelRGEGEFVRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 80 DWDTAIREVAEKFLAIKRRHGGESIL--YYGGGAQGN-HLGGAYGDSTLKALG--VKYR---SNALAQEKTGEFWVQGKM 151
Cdd:cd02751 77 SWDEALDLVASELKRIREKYGNEAIFggSYGWASAGRlHHAQSLLHRFLNLIGgyLGSYgtySTGAAQVILPHVVGSDEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 152 FGTGVHGD--FEHCEGAILIGKNPW---QSHGFARARVLLNAM--AKDPARSIIVIDPRLSETAA-LADFHLQIRPGTDA 223
Cdd:cd02751 157 YEQGTSWDdiAEHSDLVVLFGANPLktrQGGGGGPDHGSYYYLkqAKDAGVRFICIDPRYTDTAAvLAAEWIPIRPGTDV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 224 WCLAALVGIIVQDGLLARDWLAEHTSGYEHIVDEL----NAIP--VAYCAETCGVAEDKLRaaarriasassvsaleDLG 297
Cdd:cd02751 237 ALMLAMAHTLITEDLHDQAFLARYTVGFDEFKDYLlgesDGVPktPEWAAEITGVPAETIR----------------ALA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 298 MQMNLHSTL---GSYLQR------LVWLL------TGHYGRPGTSNAFVPFlslSKASKGDTSMGkRGAPRVekrSPVAN 362
Cdd:cd02751 301 REIASKRTMiaqGWGLQRahhgeqPAWMLvtlaamLGQIGLPGGGFGFGYG---YSNGGGPPRGG-AGGPGL---PQGKN 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 363 AkiIIGLIPCNVIPEEILTDHPKRYRAMLVET-----------GNPLHSLADSQRMREAMRALELSVVIDVAMTETARHA 431
Cdd:cd02751 374 P--VKDSIPVARIADALLNPGKEFTANGKLKTypdikmiywagGNPLHHHQDLNRLIKALRKDETIVVHDIFWTASARYA 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597910 432 DYVLPAASQFEKAEATFFNLEFPRNAFHLRA---PLFPARpgtlPEAEIHARLLEAMGVLGEKDY 493
Cdd:cd02751 452 DIVLPATTSLERNDIGLTGNYSNRYLIAMKQavePLGEAR----SDYEIFAELAKRLGVEEEFTE 512
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
13-498 |
6.49e-37 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 148.66 E-value: 6.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 13 CILCSLNCGLEVQTENGRISKIRGDDDHPASQGYVCEK-----SQRMDyyqngADRLDTPMRR---RPDGSYEAIDWDTA 84
Cdd:PRK15488 48 CEMCSTRCPIEARVVNGKNVFIQGNPKAKSFGTKVCARggsghSLLYD-----PQRIVKPLKRvgeRGEGKWQEISWDEA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 85 IREVAEKFLAIKRRHGGESILYYGGGAQGN----HLGGAYGDStlkalgvkyrsNALAQEKT--GEFWVQGK-MFGTGVH 157
Cdd:PRK15488 123 YQEIAAKLNAIKQQHGPESVAFSSKSGSLSshlfHLATAFGSP-----------NTFTHASTcpAGYAIAAKvMFGGKLK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 158 GDFEHCEGAILIGKNPWQSHGFARARVLLNAMAKDPARsIIVIDPRLSETAALADFHLQIRPGTDAWCLAALVGIIVQDG 237
Cdd:PRK15488 192 RDLANSKYIINFGHNLYEGINMSDTRGLMTAQMEKGAK-LVVFEPRFSVVASKADEWHAIRPGTDLAVVLALCHVLIEEN 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 238 LLARDWLAEHTSGYEHIVDELNAIPVAYCAETCGVAEDKLRAAARRIASASSvSALEDLG--------------MQMNLH 303
Cdd:PRK15488 271 LYDKAFVERYTSGFEELAASVKEYTPEWAEAISDVPADDIRRIARELAAAAP-HAIVDFGhratftpeefdmrrAIFAAN 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 304 STLGSYLQRlvwllTGHYGRPGTS--NAFV---PFLSLSKAskGDTSMGKRGAPRVEKRSP----VANAKIIIGLipcnv 374
Cdd:PRK15488 350 VLLGNIERK-----GGLYFGKNASvyNKLAgekVAPTLAKP--GVKGMPKPTAKRIDLVGEqfkyIAAGGGVVQS----- 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 375 IPEEILTDHPKRYRAMLVETGNPLHSLADSQRMREAMRALELSVVIDVAMTETARHADYVLPAASQFEKAEAtFFNLEFP 454
Cdd:PRK15488 418 IIDATLTQKPYQIKGWVMSRHNPMQTVTDRADVVKALKKLDLVVVCDVYLSESAAYADVVLPESTYLERDEE-ISDKSGK 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 15597910 455 RNAFHLR----APLFPARPGtlpeAEIHARLLEAMGvLGE----KDYRPLRL 498
Cdd:PRK15488 497 NPAYALRqrvvEPIGDTKPS----WQIFKELGEKMG-LGQyypwQDMETLQL 543
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
10-492 |
5.32e-36 |
|
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: 144.85 E-value: 5.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 10 KTACILCSLNCGLEVQTENGRISKIRGDDDHPASQGYVCEKSQRMDYYQNGADRLDTPMRRRP-DGSYEAIDWDTAIREV 88
Cdd:cd02752 1 RTICPYCSVGCGLIAYVQNGVWVHQEGDPDHPVNRGSLCPKGAALRDFVHSPKRLKYPMYRAPgSGKWEEISWDEALDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 89 AEKFLAIKRRH------------GGESILYYGGGAQGNHlGGAYGDSTLKALGVKYRSN-----------ALAqektgEF 145
Cdd:cd02752 81 ARKMKDIRDASfveknaagvvvnRPDSIAFLGSAKLSNE-ECYLIRKFARALGTNNLDHqariuhsptvaGLA-----NT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 146 WVQGKMfgTGVHGDFEHCEGAILIGKNPWQSH--GFaraRVLLNAMAKDPARsIIVIDPRLSETAALADFHLQIRPGTDa 223
Cdd:cd02752 155 FGRGAM--TNSWNDIKNADVILVMGGNPAEAHpvSF---KWILEAKEKNGAK-LIVVDPRFTRTAAKADLYVPIRSGTD- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 224 wcLAALVGIIvqdgllarDWLAEHTsgyehiVDELNAIpvaycaetCGVAEDKLRAAARRIASASSVSALEDLGMQMNL- 302
Cdd:cd02752 228 --IAFLGGMI--------NYIIRYT------PEEVEDI--------CGVPKEDFLKVAEMFAATGRPDKPGTILYAMGWt 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 303 HSTLGSYLQR---LVWLLTGHYGRPGTS-NAFvpflslskaskgdtsmgkRGAPRVEKRSPvanakiiIGLIPCNVipee 378
Cdd:cd02752 284 QHTVGSQNIRamcILQLLLGNIGVAGGGvNAL------------------RGHSNVQGATD-------LGLLSHNL---- 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 379 iltdhPKRYRAMlvetgNPLHSLADSQRMREAMRALELSVVIDVAMTETARHAD-------------YVLPAASQFEKaE 445
Cdd:cd02752 335 -----PGYLGGQ-----NPNSSFPNANKVRRALDKLDWLVVIDPFPTETAAFWKnpgmdpksiqtevFLLPAACQYEK-E 403
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 15597910 446 ATFFN----LEFPRNAFHlraPLFPARpgtlPEAEIHARLLEAMGVLGEKD 492
Cdd:cd02752 404 GSITNsgrwLQWRYKVVE---PPGEAK----SDGDILVELAKRLGFLYEKE 447
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
11-493 |
3.34e-35 |
|
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: 142.08 E-value: 3.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 11 TACIL-CSLNCGLEVQTENGRISKIRGDDDHPASQGY----VCEK--SQRMDYYqnGADRLDTPMRR---RPDGSYEAID 80
Cdd:cd02770 2 SACTVnCGGRCPLKAHVKDGVITRIETDDTGDDDPGFhqirACLRgrSQRKRVY--NPDRLKYPMKRvgkRGEGKFVRIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 81 WDTAIREVAEKFLAIKRRHGGESILY-YGGGAQG-NHLGGAYGDSTLKALG---VKYRSNALAQEKtgefWVQGKMFGTG 155
Cdd:cd02770 80 WDEALDTIASELKRIIEKYGNEAIYVnYGTGTYGgVPAGRGAIARLLNLTGgylNYYGTYSWAQIT----TATPYTYGAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 156 VHG----DFEHCEGAILIGKNPWQSH--GFARARVLLNAMaKDPARsIIVIDPRLSETAA-LADFHLQIRPGTDAWCLAA 228
Cdd:cd02770 156 ASGssldDLKDSKLVVLFGHNPAETRmgGGGSTYYYLQAK-KAGAK-FIVIDPRYTDTAVtLADEWIPIRPGTDAALVAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 229 LVGIIVQDGLLARDWLAEHTSGY--EHIVD--ELNAIPVAY---------------CAETCGVAEDKLRAAARRIASASS 289
Cdd:cd02770 234 MAYVMITENLHDQAFLDRYCVGFdaEHLPEgaPPNESYKDYvlgtgydgtpktpewASEITGVPAETIRRLAREIATTKP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 290 VSALEDLGMQMNL---HSTLGSYlqrLVWLLTGHYGRPGTSNAFVPFLSLSKASKGdtSMGKrgaprvekrSPVANAkii 366
Cdd:cd02770 314 AAILQGWGPQRHAngeQAARAIM---MLAAMTGNVGIPGGNTGARPGGSAYNGAGL--PAGK---------NPVKTS--- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 367 iglIPCNVIPEEILTDHPKRYRAMLVETGNPL------------HSLA-----DSQRMREAMRA---LELSVVIDVAMTE 426
Cdd:cd02770 377 ---IPCFMWTDAIERGEEMTADDGGVKGADKLksnikmiwnyagNTLInqhsdDNNTTRALLDDeskCEFIVVIDNFMTP 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597910 427 TARHADYVLPAASQFEKAEATFFNLEFPRNAFHL--RA--PLFPARpgtlPEAEIHARLLEAMGVLGEKDY 493
Cdd:cd02770 454 SARYADILLPDTTELEREDIVLTSNAGMMEYLIYsqKAiePLYECK----SDYEICAELAKRLGVEDQFTE 520
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
16-442 |
8.87e-30 |
|
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: 124.90 E-value: 8.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 16 CSLNCG----LEVQTENGRISKIRGDDdhPASQGY--VCEKSqrMDYYQN--GADRLDTPMRR---RPDGSYEAIDWDTA 84
Cdd:cd02765 4 CPPNCGgrcpLKCHVRDGKIVKVEPNE--WPDKTYkrGCTRG--LSHLQRvySPDRLKYPMKRvgeRGEGKFERITWDEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 85 IREVAEKFLAIKRRHGGESILYYGGGAQGNHLGGAYGDSTLKALGVKYRSNALAQEKTGEFWVQGKMFGTGVH--GDFEH 162
Cdd:cd02765 80 LDTIADKLTEAKREYGGKSILWMSSSGDGAILSYLRLALLGGGLQDALTYGIDTGVGQGFNRVTGGGFMPPTNeiTDWVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 163 CEGAILIGKNPWQSHgFARARVLLNAmaKDPARSIIVIDPRLSETAALADFHLQIRPGTDAWCLAALVGIIVQDGLLARD 242
Cdd:cd02765 160 AKTIIIWGSNILETQ-FQDAEFFLDA--RENGAKIVVIDPVYSTTAAKADQWVPIRPGTDPALALGMINYILEHNWYDEA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 243 WLAEHTS--------------------------------------------------------------GYEHIVDELNA 260
Cdd:cd02765 237 FLKSNTSapflvredngtllrqadvtatpaedgyvvwdtnsdspepvaatninpalegeytingvkvhtVLTALREQAAS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 261 IPVAYCAETCGVAEDKLRAAARRIASASSVSALEDLGMQMNLHSTLGSYLQRLVWLLTGHYGRPGTSnafvpflslskas 340
Cdd:cd02765 317 YPPKAAAEICGLEEAIIETLAEWYATGKPSGIWGFGGVDRYYHSHVFGRTAAILAALTGNIGRVGGG------------- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 341 kgdtsmgkrgaprvekrspVANAKiiiglipcnvipeeiltdhpkryrAMLVETGNPLHSLADSQRMREAMRALELSVVI 420
Cdd:cd02765 384 -------------------VGQIK------------------------FMYFMGSNFLGNQPDRDRWLKVMKNLDFIVVV 420
|
490 500
....*....|....*....|..
gi 15597910 421 DVAMTETARHADYVLPAASQFE 442
Cdd:cd02765 421 DIFHTPTVRYADIVLPAAHWFE 442
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
8-443 |
6.81e-29 |
|
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: 121.78 E-value: 6.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 8 WKKTACILCSLNCGLEVQTENGRISKIRGDDDHPASQGYVCEKSQRMDYYQNGADRLDTPMRR-------RPDGSYEAID 80
Cdd:cd02757 1 WVPSTCQGCTAWCGLQAYVEDGRVTKVEGNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRtnprkgrDVDPKFVPIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 81 WDTAIREVAEKFLAI---KRRHggESILYYGggaQGNHLGGAYGDSTLKALGVK---YRSNALAQ-EKTGEFWVQGkmfG 153
Cdd:cd02757 81 WDEALDTIADKIRALrkeNEPH--KIMLHRG---RYGHNNSILYGRFTKMIGSPnniSHSSVCAEsEKFGRYYTEG---G 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 154 TGVHG-DFEHCEGAILIGKNPWQSHgfaraRVLLNAM----AKDPARSIIVIDPRLSETAALADFHLQIRPGTDAWCLAA 228
Cdd:cd02757 153 WDYNSyDYANAKYILFFGADPLESN-----RQNPHAQriwgGKMDQAKVVVVDPRLSNTAAKADEWLPIKPGEDGALALA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 229 LVGIIVQDGLLARDWLAEHTSG-------------------YEHIVDELNA-----IPvAYCAETCGVAEDK-LRAAARR 283
Cdd:cd02757 228 IAHVILTEGLWDKDFVGDFVDGknyfkagetvdeesfkeksTEGLVKWWNLelkdyTP-EWAAKISGIPAETiERVAREF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 284 IASASSVSALEDLGMQMNLHstlGSYLQRLVWLLTGHYGrpgtsnafvpflslSKASKGDTSMGkRGAPRVEkrspvana 363
Cdd:cd02757 307 ATAAPAAAAFTWRGATMQNR---GSYNSMACHALNGLVG--------------SIDSKGGLCPN-MGVPKIK-------- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 364 kiiiglipcnvipeeiltdhpkryrAMLVETGNPLHSLADSQRMREAMRALELSVVIDVAMTETARHADYVLPAASQFEK 443
Cdd:cd02757 361 -------------------------VYFTYLDNPVFSNPDGMSWEEALAKIPFHVHLSPFMSETTYFADIVLPDGHHFER 415
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
3-751 |
2.58e-27 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 118.59 E-value: 2.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 3 TPSPQWKKTACILCSLNCG----LEVQTENGRISKIR----GDDDHPA-SQGYVCEKSQRMDYYQNGADRLDTPMRR--- 70
Cdd:PRK14990 50 IPTKSDEKVIWSACTVNCGsrcpLRMHVVDGEIKYVEtdntGDDNYDGlHQVRACLRGRSMRRRVYNPDRLKYPMKRvga 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 71 RPDGSYEAIDWDTAIREVAEKFLAIKRRHGGESI-LYYGGGAQGNHLGGAY--GDSTLKAL-----GV--KYRSNALAQE 140
Cdd:PRK14990 130 RGEGKFERISWEEAYDIIATNMQRLIKEYGNESIyLNYGTGTLGGTMTRSWppGNTLVARLmnccgGYlnHYGDYSSAQI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 141 KTGEFWVQGKMFGTGVHGDFEHCEGAILIGKNPWQSH--GFARARVLLNAMAKDPARsIIVIDPRLSETAA-LADFHLQI 217
Cdd:PRK14990 210 AEGLNYTYGGWADGNSPSDIENSKLVVLFGNNPGETRmsGGGVTYYLEQARQKSNAR-MIIIDPRYTDTGAgREDEWIPI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 218 RPGTDAWCLAALVGIIVQDGLLARDWLAEHTSGYE----------------HIV----DELNAIPvAYCAETCGVAEDKL 277
Cdd:PRK14990 289 RPGTDAALVNGLAYVMITENLVDQPFLDKYCVGYDektlpasapknghykaYILgegpDGVAKTP-EWASQITGVPADKI 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 278 RAAARRIASASSVSALEDLGMQMNLHSTLGSYLQRLVWLLTGHYGRPGTSnafvpflslSKASKGDTSMGKRGAPRVEkr 357
Cdd:PRK14990 368 IKLAREIGSTKPAFISQGWGPQRHANGEIATRAISMLAILTGNVGINGGN---------SGAREGSYSLPFVRMPTLE-- 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 358 SPVANAkiIIGLIPCNVI---PE-EILTDHPKRYRAMLVE-------TGNPL---HSlaDSQRMREAM---RALELSVVI 420
Cdd:PRK14990 437 NPIQTS--ISMFMWTDAIergPEmTALRDGVRGKDKLDVPikmiwnyAGNCLinqHS--EINRTHEILqddKKCELIVVI 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 421 DVAMTETARHADYVLP---AASQFEKA-EATFFNLEFPRNAFHLRAPLFPARpgTLpeAEIHARLLEAMGVlgEKDYRPL 496
Cdd:PRK14990 513 DCHMTSSAKYADILLPdctASEQMDFAlDASCGNMSYVIFNDQVIKPRFECK--TI--YEMTSELAKRLGV--EQQFTEG 586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 497 RlalklgrkafsaaflaaaaTRPKVMKYapvlLY---RTLGPTLPagmeaaaaiwgicqlhvlnNRKTAARAG-FDGLPP 572
Cdd:PRK14990 587 R-------------------TQEEWMRH----LYaqsREAIPELP-------------------TFEEFRKQGiFKKRDP 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 573 LAADRLFQAMLDNPSGvvfaettyaeswQAVARPEQRINLHIpellPELAKLAHS--APPHDPAYPF-ILAAG-ERRSD- 647
Cdd:PRK14990 625 QGHHVAYKAFREDPQA------------NPLTTPSGKIEIYS----QALADIAATweLPEGDVIDPLpIYTPGfESYQDp 688
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 648 -TSNTAVRDTGWHRRGR----YGT-----------LRISPQDAEALGCADGEVLRVVTRRGEVEAEVEISDMMQPGNISL 711
Cdd:PRK14990 689 lNKQYPLQLTGFHYKSRvhstYGNvdvlkaacrqeMWINPLDAQKRGINNGDKVRIFNDRGEVHIEAKVTPRMMPGVVAL 768
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 15597910 712 pnGQGLDYrNAEGEVVRRGVAPNEVTdcTQR--DFLAGTPWH 751
Cdd:PRK14990 769 --GEGAWY-DPDAKRVDKGGCINVLT--TQRpsPLAKGNPSH 805
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
63-469 |
1.04e-26 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 112.49 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 63 RLDTPMRRRPDGSYEAIDWDTAIREVAEKFLAIKRRHGGESILYYGGGAQGNHLGGAYGDSTL-KALGVK--------YR 133
Cdd:pfam00384 1 RLKYPMVRRGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAINGGSGGLTDVESLYALKKLlNRLGSKngntedhnGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 134 SNALAQEKTGEFWVQGKMFGTGVHgDFEHCEGAILIGKNPWQSHGFARARvLLNAMAKDPARsIIVIDPRLSETaaLADF 213
Cdd:pfam00384 81 LCTAAAAAFGSDLRSNYLFNSSIA-DIENADLILLIGTNPREEAPILNAR-IRKAALKGKAK-VIVIGPRLDLT--YADE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 214 HLQIRPGTDAWCLAALVGIIVQDGLLARDwlaehtsgyehivdelnaipvaycaetcgvaedklraaarriasaSSVSAL 293
Cdd:pfam00384 156 HLGIKPGTDLALALAGAHVFIKELKKDKD---------------------------------------------FAPKPI 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 294 EDLGMQMNlHSTLGSYLQRLV---WLLTGHYGRPGTSNAFVPFLSlskaskgdtsmgkRGAPRVekrspvanAKIIIGLI 370
Cdd:pfam00384 191 IIVGAGVL-QRQDGEAIFRAIanlADLTGNIGRPGGGWNGLNILQ-------------GAASPV--------GALDLGLV 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 371 PCNVIPEEILTDHPKRYRAMLVETGNPLHSLADSQRMREAMRALELSVVIDVAM-TETARHADYVLPAASQFEKaEATFF 449
Cdd:pfam00384 249 PGIKSVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFVVYDGHHgDKTAKYADVILPAAAYTEK-NGTYV 327
|
410 420
....*....|....*....|.
gi 15597910 450 NLE-FPRNAFHLRAPLFPARP 469
Cdd:pfam00384 328 NTEgRVQSTKQAVPPPGEARE 348
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
23-487 |
2.87e-25 |
|
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: 111.20 E-value: 2.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 23 EVQTENGRISKIRG--DDDHPASQGyvceksqrmdyyQNGADRLDTPMR-----------RRPDGS---------YEAID 80
Cdd:cd02769 10 RARVKDGRIVGVRPfeEDPDPSPLL------------DGVPDAVYSPTRikypmvrrgwlEKGPGSdrslrgkeeFVRVS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 81 WDTAIREVAEKFLAIKRRHGGESILyygggaqgnhlGGAYGdstLKALGVKYRSNALAQE---KTGEFWVQGKMFGTG-- 155
Cdd:cd02769 78 WDEALDLVAAELKRVRKTYGNEAIF-----------GGSYG---WSSAGRFHHAQSLLHRflnLAGGYVGSVGDYSTGaa 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 156 ------VHGDF--------------EHCEGAILIGKNPW---QSHGFARAR-VLLNAMAKDPARSI--IVIDPRLSETAA 209
Cdd:cd02769 144 qvilphVVGSMevyteqqtswpviaEHTELVVAFGADPLknaQIAWGGIPDhQAYSYLKALKDRGIrfISISPLRDDTAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 210 LADF-HLQIRPGTDAWCLAALVGIIVQDGLLARDWLAEHTSGYEHIVDEL----NAIP--VAYCAETCGVAEDKLRaaar 282
Cdd:cd02769 224 ELGAeWIAIRPGTDVALMLALAHTLVTEGLHDKAFLARYTVGFDKFLPYLlgesDGVPktPEWAAAICGIPAETIR---- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 283 riasassvsaleDLGMQMNLHSTL--GSY-LQRL------VWLLT------GHYGRPGTSNAFvpflSLSKASKGDTSMG 347
Cdd:cd02769 300 ------------ELARRFASKRTMimAGWsLQRAhhgeqpHWMAVtlaamlGQIGLPGGGFGF----GYHYSNGGGPPRG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 348 KRGAPRVEK-RSPVANAkiiiglIPCNVIPEEILtdHP-KRY------------RAMLVETGNPLHSLADSQRMREAMRA 413
Cdd:cd02769 364 AAPPPALPQgRNPVSSF------IPVARIADMLL--NPgKPFdyngkkltypdiKLVYWAGGNPFHHHQDLNRLIRAWQK 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 414 LELSVVIDVAMTETARHADYVLPAASQFEKAEatffnLEFPRNAFHLRA------PLFPARpgtlPEAEIHARLLEAMGV 487
Cdd:cd02769 436 PETVIVHEPFWTATARHADIVLPATTSLERND-----IGGSGDNRYIVAmkqvvePVGEAR----DDYDIFADLAERLGV 506
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
11-445 |
5.53e-24 |
|
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: 105.86 E-value: 5.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 11 TACILCSLNCGLEVQTENGRISKIRGDDDHPA-SQGYV------CEKSQRMDYYQNGADRLDTPMRR---RPDGSYEAID 80
Cdd:cd02750 7 THGVNCTGSCSWNVYVKNGIVTREEQATDYPEtPPDLPdynprgCQRGASFSWYLYSPDRVKYPLKRvgaRGEGKWKRIS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 81 WDTAIREVAEKFLAIKRRHGGESI-----------LYYGGGAQGNHLGGA--------YGDSTlkalgvkyrsnalaqek 141
Cdd:cd02750 87 WDEALELIADAIIDTIKKYGPDRVigfspipamsmVSYAAGSRFASLIGGvslsfydwYGDLP----------------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 142 TGEFWVQGKMfgTGVH--GDFEHCEGAILIGKNPWQS-----HGFARARvllNAMAKdparsIIVIDPRLSETAALADFH 214
Cdd:cd02750 150 PGSPQTWGEQ--TDVPesADWYNADYIIMWGSNVPVTrtpdaHFLTEAR---YNGAK-----VVVVSPDYSPSAKHADLW 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 215 LQIRPGTDAWCLAALVGIIVQDGLLARDWLAEHTSgyehivDELNAIPVAYCAETCGVAEDKLRAAARRIASASSVSALE 294
Cdd:cd02750 220 VPIKPGTDAALALAMAHVIIKEKLYDEDYLKEYTD------LPFLVYTPAWQEAITGVPRETVIRLAREFATNGRSMIIV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 295 DLGMQMNLHSTLGSYLQRLVWLLTGHYGRPGTsnafvpflslskaskGDTSMgkRGAPRVekrspvanakiiiglipcnv 374
Cdd:cd02750 294 GAGINHWYHGDLCYRALILLLALTGNEGKNGG---------------GWAHY--VGQPRV-------------------- 336
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597910 375 ipeeiltdhpkryraMLVETGNPLHSLADSQRMREamRA----LELSVVIDVAMTETARHADYVLPAASQFEKAE 445
Cdd:cd02750 337 ---------------LFVWRGNLFGSSGKGHEYFE--DApegkLDLIVDLDFRMDSTALYSDIVLPAATWYEKHD 394
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
10-256 |
5.85e-20 |
|
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: 94.90 E-value: 5.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 10 KTACILCSLNCGLEVQTENGRISKIRGDDDHPASQGYVCEK--SQRMDYYQNGadRLDTPMRRRPD---GSYEAIDWDTA 84
Cdd:cd02763 1 TTTCYMCACRCGIRVHLRDGKVRYIKGNPDHPLNKGVICAKgsSGIMKQYSPA--RLTKPLLRKGPrgsGQFEEIEWEEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 85 IrEVAEKFLAIKRRHGGESILYYGGGAQGNHLGG----AYGDSTLKALGVKYRSNALA---QEKTGEFWvqgkMFGtgvH 157
Cdd:cd02763 79 F-SIATKRLKAARATDPKKFAFFTGRDQMQALTGwfagQFGTPNYAAHGGFCSVNMAAgglYSIGGSFW----EFG---G 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 158 GDFEHCEGAILIGKNpwQSHGFARARVLLNAMAKDPARsIIVIDPRLSETAALADFHLQIRPGTDAWCLAALVGIIVQDG 237
Cdd:cd02763 151 PDLEHTKYFMMIGVA--EDHHSNPFKIGIQKLKRRGGK-FVAVNPVRTGYAAIADEWVPIKPGTDGAFILALAHELLKAG 227
|
250
....*....|....*....
gi 15597910 238 LLARDWLAEHTSGYEhIVD 256
Cdd:cd02763 228 LIDWEFLKRYTNAAE-LVD 245
|
|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
7-60 |
1.58e-17 |
|
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: 76.95 E-value: 1.58e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 15597910 7 QWKKTACILCSLNCGLEVQTENGRISKIRGDDDHPASQGYVCEKSQRMDYYQNG 60
Cdd:pfam04879 2 KVVKTICPYCGVGCGLEVHVKDGKIVKVEGDPDHPVNEGRLCVKGRFGYERVYN 55
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
11-485 |
4.16e-17 |
|
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: 85.86 E-value: 4.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 11 TACILCSLNCGLEVQ--TENGRISKIRGDDDHPASQ---------------------------GYVCEKSQRMDYYQNGA 61
Cdd:cd02758 2 SSCLGCWTQCGIRVRvdKETGKVLRIAGNPYHPLNTapslpyntplkeslylslvgenglkarATACARGNAGLQYLYDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 62 DRLDTPMRR---RPDGSYEAIDWDTAIREVAEkflaikrrhGGEsiLYYGGGAQGnhLGGAYGDSTL-----KALGVKyr 133
Cdd:cd02758 82 YRVLQPLKRvgpRGSGKWKPISWEQLIEEVVE---------GGD--LFGEGHVEG--LKAIRDLDTPidpdhPDLGPK-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 134 SNALA------QEKTG---EFWVQGkmFGT---GVHG--------------------------DFEHCEGAILIGKNPWQ 175
Cdd:cd02758 147 ANQLLytfgrdEGRTPfikRFANQA--FGTvnfGGHGsycglsyragngalmndldgyphvkpDFDNAEFALFIGTSPAQ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 176 SH-GFAR-ARVLLNAMAKDPARsIIVIDPRLSETAALADFH---LQIRPGTDAWCLAALVGIIVQDGLLARDWLAE---- 246
Cdd:cd02758 225 AGnPFKRqARRLAEARTEGNFK-YVVVDPVLPNTTSAAGENirwVPIKPGGDGALAMAMIRWIIENERYNAEYLSIpske 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 247 --------HTSGYEHIV-------------DELNAIPVAYCAETCGVAEDKLRAAARRIASASSVSALEDLGMQMnlHST 305
Cdd:cd02758 304 aakaagepSWTNATHLVitvrvksalqllkEEAFSYSLEEYAEICGVPEAKIIELAKEFTSHGRAAAVVHHGGTM--HSN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 306 lGSYLQRLVWLLT---GHYGRPGTSNA-FVPFLSLSKASKGDTSMG-----KRGAP-----RVEKRSPVANAKIIIGLIP 371
Cdd:cd02758 382 -GFYNAYAIRMLNaliGNLNWKGGLLMsGGGFADNSAGPRYDFKKFfgevkPWGVPidrskKAYEKTSEYKRKVAAGENP 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 372 ----------CNVIPEEILTDH----PKRYRAMLVETGNPLHSLADSQRMREAM----RALELSVVIDVAMTETARHADY 433
Cdd:cd02758 461 ypakrpwyplTPELYTEVIASAaegyPYKLKALILWMANPVYGAPGLVKQVEEKlkdpKKLPLFIAIDAFINETSAYADY 540
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 15597910 434 VLPAASQFEKAEATFFNLEFPRNAFHLRAPLFParPGTLPEAEIHARLLEAM 485
Cdd:cd02758 541 IVPDTTYYESWGFSTPWGGVPTKASTARWPVIA--PLTEKTANGHPVSMESF 590
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
20-469 |
8.57e-16 |
|
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: 81.00 E-value: 8.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 20 CGLEVQTENGRISKIRGDDDHPASQGYVCEKSQR--MDYYQngADRLDTPMRRRPDGSYEAIDWDTAIREVAEKFLAIKr 97
Cdd:cd02764 56 QGVLVKTVDGRPIKIEGNPDHPASLGGTSARAQAsvLSLYD--PDRAQGPLRRGIDGAYVASDWADFDAKVAEQLKAVK- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 98 rhGGESILYYGGGAQGNHLGGAYGDSTLKALGVKY-----RSNALAQEKTgefwvQGKMFGTGVHG-DFEHCEGAILIGK 171
Cdd:cd02764 133 --DGGKLAVLSGNVNSPTTEALIGDFLKKYPGAKHvvydpLSAEDVNEAW-----QASFGKDVVPGyDFDKAEVIVSIDA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 172 N---PWQS-----HGFARARvllNAMAKDPARSIIVIDPRLSETAALADFHLQIRPGTD---AWCLAALVGIIVQDGLLA 240
Cdd:cd02764 206 DflgSWISairhrHDFAAKR---RLGAEEPMSRLVAAESVYTLTGANADVRLAIRPSQEkafALGLAHKLIKKGAGSSLP 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 241 RDWLAEHTSGYEHIVDELNAIPvaycAETCGVAEDKLraaarRIASASSVSALEDLGmqmnlhSTLGSYLQRLVWLLTGH 320
Cdd:cd02764 283 DFFRALNLAFKPAKVAELTVDL----DKALAALAKAL-----AAAGKSLVVAGSELS------QTAGADTQVAVNALNSL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 321 YGRPGTSnafvpfLSLSKASKGDtsmgkrgaprvekrsPVANAKIIIGLIpcnvipEEILTDHPKryrAMLVETGNPLHS 400
Cdd:cd02764 348 LGNDGKT------VDHARPIKGG---------------ELGNQQDLKALA------SRINAGKVS---ALLVYDVNPVYD 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597910 401 LADSQRMREAMRALELSVVIDVAMTETARHADYVLPAASQFEK---AEAT--FFNLEFPrnafhLRAPLFPARP 469
Cdd:cd02764 398 LPQGLGFAKALEKVPLSVSFGDRLDETAMLCDWVAPMSHGLESwgdAETPdgTYSICQP-----VIAPLFDTRS 466
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
63-484 |
1.47e-15 |
|
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: 80.43 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 63 RLDTPMRRRP-DGSYEAIDWDTAIREVAEKFLAIKRrhggESILYYGGGAQGNH-------LGGAYGDSTL--------- 125
Cdd:cd02767 64 RLTYPMRYDAgSDHYRPISWDEAFAEIAARLRALDP----DRAAFYTSGRASNEaaylyqlFARAYGTNNLpdcsnmche 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 126 -------KALGVkyrsnalaqektgefwvqGKmfGTGVHGDFEHCEGAILIGKNPWQSHgfaraRVLLNAM--AKDPARS 196
Cdd:cd02767 140 pssvglkKSIGV------------------GK--GTVSLEDFEHTDLIFFIGQNPGTNH-----PRMLHYLreAKKRGGK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 197 IIVIDPrLSETA------------------ALADFHLQIRPGTDawcLAALVGII--------VQDGLLARDWLAEHTSG 250
Cdd:cd02767 195 IIVINP-LREPGlerfanpqnpesmltggtKIADEYFQVRIGGD---IALLNGMAkhlierddEPGNVLDHDFIAEHTSG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 251 YEHIVDELNAIPVAYCAETCGVAEDKLRAAARRIASASSVSALEDLGMQMNLHSTLGsyLQRLV--WLLTGHYGRPGT-- 326
Cdd:cd02767 271 FEEYVAALRALSWDEIERASGLSREEIEAFAAMYAKSERVVFVWGMGITQHAHGVDN--VRAIVnlALLRGNIGRPGAgl 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 327 ------SNAfvpflslskasKGDTSMGKRgaprvEKRSPVANAKI--IIGLIPcnviPEEILTDHPKRYRAML---VET- 394
Cdd:cd02767 349 mpirghSNV-----------QGDRTMGIT-----EKPFPEFLDALeeVFGFTP----PRDPGLDTVEAIEAALegkVKAf 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 395 ----GNPLHSLADSQRMREAMRALELSVVIDVAMTET----ARHAdYVLPAASQFEKAE----ATFFNLEFPRNAFHL-R 461
Cdd:cd02767 409 islgGNFAEAMPDPAATEEALRRLDLTVHVATKLNRShlvhGEEA-LILPCLGRTEIDMqaggAQAVTVEDSMSMTHTsR 487
|
490 500
....*....|....*....|...
gi 15597910 462 APLFPARPGTLPEAEIHARLLEA 484
Cdd:cd02767 488 GRLKPASRVLLSEEAIVAGIAGA 510
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
649-752 |
2.49e-15 |
|
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: 72.35 E-value: 2.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 649 SNTAVRDTGWHRRGRYGTLRISPQDAEALGCADGEVLRVVTRRGEVEAEVEISDMMQPGNISLPNGQGLDYrnaegevvR 728
Cdd:cd02775 7 SGTRTRNPWLRELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGHRG--------G 78
|
90 100
....*....|....*....|....
gi 15597910 729 RGVAPNEVTDCTQRDfLAGTPWHK 752
Cdd:cd02775 79 RGGNANVLTPDALDP-PSGGPAYK 101
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
635-760 |
3.67e-15 |
|
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: 72.27 E-value: 3.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 635 YPFILAAGER------RSDTSNTAVRDtgwhRRGRYGTLRISPQDAEALGCADGEVLRVVTRRGEVEAEVEISDMMQPGN 708
Cdd:cd02790 3 YPLVLTTGRVlyhyhtGTMTRRAEGLD----AIAPEEYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGV 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 15597910 709 ISLPngqgldYRNAEGevvrrgvAPNEVTDcTQRDFLAGTPWHKYVPARLER 760
Cdd:cd02790 79 VFMP------FHFAEA-------AANLLTN-AALDPVAKIPEFKVCAVRVEK 116
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
637-755 |
4.86e-15 |
|
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: 71.54 E-value: 4.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 637 FILAAGeRRSDTSNTAVRDTGWHRRGRYG--TLRISPQDAEALGCADGEVLRVVTRRGEVEAEVEISDMMQPGNISLPNG 714
Cdd:pfam01568 1 LYLITG-RVLGQYHSQTRTRRVLRLAKPEpeVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 15597910 715 QGLDYrnaegevvrRGVAPNEVTDcTQRDFLAGTPWHKYVP 755
Cdd:pfam01568 80 WWYEP---------RGGNANALTD-DATDPLSGGPEFKTCA 110
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
7-50 |
5.20e-14 |
|
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: 66.89 E-value: 5.20e-14
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 15597910 7 QWKKTACILCSLNCGLEVQTENGRISKIRGDDDHPASQGYVCEK 50
Cdd:smart00926 2 KWVPTVCPLCGVGCGLLVEVKDGRVVRVRGDPDHPVNRGRLCPK 45
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
7-248 |
1.21e-13 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 74.94 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 7 QWKKTACILCSLNCGLEVQTENGRISKIRGDDDHPASQGYVCEK----SQRMdYyqnGADRLDTPMRRRPDGSY------ 76
Cdd:PRK13532 41 KWDKAPCRFCGTGCGVLVGTKDGRVVATQGDPDAPVNRGLNCIKgyflSKIM-Y---GKDRLTQPLLRMKDGKYdkegef 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 77 EAIDWDTAIREVAEKFLAIKRRHGGESILYYGGGaQGNHLGGaYGDSTLKALGvkYRSNAL----------Aqektgefw 146
Cdd:PRK13532 117 TPVSWDQAFDVMAEKFKKALKEKGPTAVGMFGSG-QWTIWEG-YAASKLMKAG--FRSNNIdpnarhcmasA-------- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 147 VQGKM--FG----TGVHGDFEHCEGAILIGKNPWQSHGFARARVlLNAMAKDPARSIIVIDPRLSETAALADFHLQIRPG 220
Cdd:PRK13532 185 VVGFMrtFGidepMGCYDDIEAADAFVLWGSNMAEMHPILWSRV-TDRRLSNPDVKVAVLSTFEHRSFELADNGIIFTPQ 263
|
250 260 270
....*....|....*....|....*....|.
gi 15597910 221 TDawcLAALVGI---IVQDGLLARDWLAEHT 248
Cdd:PRK13532 264 TD---LAILNYIanyIIQNNAVNWDFVNKHT 291
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
10-221 |
1.24e-12 |
|
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: 70.64 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 10 KTACILCSLNCGLEVQTENGRISKIRGDDDHPASQGYVCEKSqRMDY-YQNGADRLDTPMRRRpDGSYEAIDWDTAIREV 88
Cdd:COG1034 219 PSICPHCSVGCNIRVDVRGGKVYRVLPRENEAVNEEWLCDKG-RFGYdGLNSPDRLTRPLVRK-DGELVEASWEEALAAA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 89 AEKFLAIKRrhggesilyyGGGAQGNHLGGAYGDSTlkalgvkyrsNALAQEKTGEFwvqgkmfgtgvhgdfehcEGAIL 168
Cdd:COG1034 297 AEGLKALKK----------AENSVGAALLGALPDAA----------AILEAAEAGKL------------------KALVL 338
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15597910 169 IGKNPWQSHGFARARVLlnamakDPARSIIVIDPRLSETAALADFHLQIRPGT 221
Cdd:COG1034 339 LGADPYDLDPAAALAAL------AKADFVVVLDHFGSATAERADVVLPAAAFA 385
|
|
| 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 ... |
10-470 |
1.40e-11 |
|
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: 67.41 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 10 KTACILCSLNCGLEVQTENGRISKIRGDDDHPASQGYVCEKSqRMDY-YQNGADRLDTPMRRRpDGSYEAIDWDTAIREV 88
Cdd:cd02771 1 PSICHHCSVGCNISLGERYGELRRVENRYNGAVNHYFLCDRG-RFGYgYVNSRDRLTQPLIRR-GGTLVPVSWNEALDVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 89 AEKFLAIKRRHGGesilyYGGGAQGNHLGGAYGDSTLKALG---VKYRSNALAQEKTGEFWVQgkmfgTGVHGDFEHCEG 165
Cdd:cd02771 79 AARLKEAKDKVGG-----IGSPRASNESNYALQKLVGAVLGtnnVDHRARRLIAEILRNGPIY-----IPSLRDIESADA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 166 AILIGKNPWQSHgfARARVLLNAMAKDPARSiIVIDPRLSETAALADFHLQIRPGTDawclAALVGIIVQDGLLARDWLA 245
Cdd:cd02771 149 VLVLGEDLTQTA--PRIALALRQAARRKAVE-LAALSGIPKWQDAAVRNIAQGAKSP----LFIVNALATRLDDIAAESI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 246 EHTSGyeHIVDELNAIPVAYCAETCGVAEDKLRAAARRIASASSVS--ALEDLGMQMNLHSTLGSyLQRLVWLLtghyGR 323
Cdd:cd02771 222 RASPG--GQARLGAALARAVDASAAGVSGLAPKEKAARIAARLTGAkkPLIVSGTLSGSLELIKA-AANLAKAL----KR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 324 PGtSNAFVPFLSLSKASKGDTSMGkrGAPRVEKRSpvanakiiiglipcnviPEEILTDHPKRYRAMLVETGNPLHSLAD 403
Cdd:cd02771 295 RG-ENAGLTLAVEEGNSPGLLLLG--GHVTEPGLD-----------------LDGALAALEDGSADALIVLGNDLYRSAP 354
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597910 404 SQRMREAMRALELSVVIDVAMTETARHADYVLPAASQFEKaEATFFNLEFPRNAFH--LRAPLFPARPG 470
Cdd:cd02771 355 ERRVEAALDAAEFVVVLDHFLTETAERADVVLPAASFAEK-SGTFVNYEGRAQRFFkaYDDPAGDARSD 422
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
11-239 |
1.00e-10 |
|
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: 65.38 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 11 TACILCSLNCG-LEVQTENGRISKIRGD----DDHPAsQGYVCEKSQRMDYYQNGADRLDTPMRR-------RPDGSYEA 78
Cdd:cd02760 2 TYCYNCVAGPDfMAVKVVDGVATEIEPNfaaeDIHPA-RGRVCVKAYGLVQKTYNPNRVLQPMKRtnpkkgrNEDPGFVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 79 IDWDTAIREVAEKFLAIKRRHGGESIL-------YYGGGAQGNHLG------GAYGDSTLKALGVKYRSNALAQEKTGEF 145
Cdd:cd02760 81 ISWDEALDLVAAKLRRVREKGLLDEKGlprlaatFGHGGTPAMYMGtfpaflAAWGPIDFSFGSGQGVKCVHSEHLYGEF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 146 WVQGkmfgTGVHGDFEHCEGAILIGKNPWQSHGFARARVLLNAMAKDPARsiIVIDPRLSETAALADFHLQIRPGTDAWC 225
Cdd:cd02760 161 WHRA----FTVAADTPLANYVISFGSNVEASGGPCAVTRHADARVRGYKR--VQVEPHLSVTGACSAEWVPIRPKTDPAF 234
|
250
....*....|....
gi 15597910 226 LAALVGIIVQDGLL 239
Cdd:cd02760 235 MFAMIHVMVHEQGL 248
|
|
| FwdB |
COG1029 |
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion]; |
8-233 |
1.06e-10 |
|
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion];
Pssm-ID: 440652 [Multi-domain] Cd Length: 428 Bit Score: 64.48 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 8 WKKTACILCSLNCG-LEVQTENGRISKIRGDddhpasqgyvCEKSQRMDYYQNGADRLDTPMRRrpdgsYEAIDWDTAIR 86
Cdd:COG1029 5 VKNVVCPFCGCLCDdLEVEVEGGKIVVVKNA----------CAIGAAKFERAVSDHRITSPRIR-----GKEVSLEEAID 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 87 EVAEKFLAIKRrhggesILYYGGG-----AQ--GNHLG---GAYGDSTLkalGVKYRSNALA-QEKtgefwvqGKMFGTg 155
Cdd:COG1029 70 KAAEILANAKR------PLIYGLSstdceAMraGLALAervGAVVDNTA---SVCHGPSLLAlQDV-------GWPTCT- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 156 vHGDFEH-CEGAILIGKNPWQSHG--FARARVLLNAM-AKDP--ARSIIVIDPRLSETAALADFHLQIRPGTDAWCLAAL 229
Cdd:COG1029 133 -LGEVKNrADVIIYWGCNPVHAHPrhMSRYSVFPRGFfTPKGrkDRTVIVVDPRPTDTAKVADLHLQVKPGRDYEVLSAL 211
|
....
gi 15597910 230 VGII 233
Cdd:COG1029 212 RALV 215
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
197-493 |
9.02e-10 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 62.38 E-value: 9.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 197 IIVIDPRLSETAA-LADFHLQIRPGTDAWCLAALVGIIVQDGLLARDWLAEHTSGYEHIV-------DELNAIPvAYCAE 268
Cdd:PRK15102 257 VISIDPVVTKTQNyLGCEHLYVNPQTDVPLMLALAHTLYSENLYDKKFIDNYCLGFEQFLpyllgekDGVPKTP-EWAEK 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 269 TCGVAEDKLraaarriasassvsalEDLGMQMNLHST---LGSYLQRL------VWL------LTGHYGRPGT------- 326
Cdd:PRK15102 336 ICGIDAETI----------------RELARQMAKGRTqiiAGWCIQRQqhgeqpYWMgavlaaMLGQIGLPGGgisyghh 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 327 -SNAFVPflslskaSKGDTSMGkrGAPRV--EKRSPVANAKIIIG---LIPCNVIPEEILtdHPKR-------------Y 387
Cdd:PRK15102 400 ySGIGVP-------SSGGAIPG--GFPGNldTGQKPKHDNSDYKGyssTIPVARFIDAIL--EPGKtinwngkkvtlppL 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 388 RAMLVETGNPLHSLADSQRMREAMRALELSVVIDVAMTETARHADYVLPAASQFEKAEATFFNLEFPRN--AFH-LRAPL 464
Cdd:PRK15102 469 KMMIFSGTNPWHRHQDRNRMKEAFRKLETVVAIDNQWTATCRFADIVLPACTQFERNDIDQYGSYSNRGiiAMKkVVEPL 548
|
330 340
....*....|....*....|....*....
gi 15597910 465 FPARpgtlPEAEIHARLLEAMGvlGEKDY 493
Cdd:PRK15102 549 FESR----SDFDIFRELCRRFG--REKEY 571
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
635-760 |
1.47e-09 |
|
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: 56.43 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 635 YPFILAAGerRsdtsntaVRDTgWH---RRGRYGTLR---------ISPQDAEALGCADGEVLRVVTRRGEVEAEVEISD 702
Cdd:cd02791 3 YPLWLNTG--R-------VRDQ-WHtmtRTGRVPRLNahvpepyveIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTD 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 15597910 703 MMQPGNISLPNGQGldYRNAEGEVVrrgvapNEVT-DCTqrDFLAGTPWHKYVPARLER 760
Cdd:cd02791 73 RVRPGEVFVPMHWG--DQFGRSGRV------NALTlDAT--DPVSGQPEFKHCAVRIEK 121
|
|
| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
655-737 |
1.48e-09 |
|
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: 56.49 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 655 DTGWHRR-----GRYgTLRISPQDAEALGCADGEVLRVVTRRGEVEAEVEISDMMQPGNISLPNGQGLD--YRNAEGEVV 727
Cdd:cd02793 19 DHGSLSRaykvqGRE-PIRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPGVVQLPTGAWYDpdDPGEPGPLC 97
|
90
....*....|
gi 15597910 728 RRGvAPNEVT 737
Cdd:cd02793 98 KHG-NPNVLT 106
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
669-760 |
1.82e-09 |
|
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: 55.98 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 669 ISPQDAEALGCADGEVLRVVTRRGEVEAEVEISDMMQPGNISLP---NGQGldyrnaegevvrRGVAPNEVTDcTQRDFL 745
Cdd:cd00508 39 IHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRPGTVFMPfhwGGEV------------SGGAANALTN-DALDPV 105
|
90
....*....|....*
gi 15597910 746 AGTPWHKYVPARLER 760
Cdd:cd00508 106 SGQPEFKACAVRIEK 120
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
657-751 |
2.78e-09 |
|
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: 55.67 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 657 GWHRRG----RYGTLRISPQDAEALGCADGEVLRVVTRRGEVEAEVEISDMMQPGNISLPNGQGLDYrNAEGEVVRRGvA 732
Cdd:cd02777 22 PWLREAykvkGREPVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPGVVALPEGAWYDP-DDNGGLDKGG-N 99
|
90 100
....*....|....*....|
gi 15597910 733 PNEVT-DCTQRDFLAGTPWH 751
Cdd:cd02777 100 PNVLTsDIPTSKLAQGNPAN 119
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
55-484 |
6.76e-09 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 59.29 E-value: 6.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 55 DYYQNGADRLDTPMRRRP-DGSYEAIDWDTAIREVAEKFLAIKRRHGGEsilYYGGGAQGNHLGGAYgdstlKALGVKYR 133
Cdd:PRK09939 100 DHELEAAGRLTQPLKYDAvSDCYKPLSWQQAFDEIGARLQSYSDPNQVE---FYTSGRTSNEAAFLY-----QLFAREYG 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 134 SNA------LAQEKT--GEFWVQGKMFGTGVHGDFEHCEGAILIGKNPWQSHgfARARVLLNAMAKDPARsIIVIDP--- 202
Cdd:PRK09939 172 SNNfpdcsnMCHEPTsvGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNH--PRMLTSLRALVKRGAK-MIAINPlqe 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 203 ----RL------------SETaALADFHLQIRPGTDAWCLAALVGIIV----------QDGLLARDWLAEHTSGYEHIVD 256
Cdd:PRK09939 249 rgleRFtapqnpfemltnSET-QLASAYYNVRIGGDMALLKGMMRLLIerddaasaagRPSLLDDEFIQTHTVGFDELRR 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 257 ELNAIPVAYCAETCGVAEDKLRAAARRIASASSVSALEDLGMQMNLHSTlgSYLQRLV--WLLTGHYGRPGTsnAFVPFL 334
Cdd:PRK09939 328 DVLNSEWKDIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGT--QNVQQLVnlLLMKGNIGKPGA--GICPLR 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 335 SLSKAsKGDTSMGKRGAPRVEKrspVANAKIIIGLIPCNVIPEEILTDHPK----RYRAMLVETGNPLHSLADSQRMREA 410
Cdd:PRK09939 404 GHSNV-QGDRTVGITEKPSAEF---LARLGERYGFTPPHAPGHAAIASMQAictgQARALICMGGNFALAMPDREASAVP 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 411 MRALELSVVIDVAMTE----TARHAdYVLPAASQFE----KAEATFFNLEFPRNAFHL-RAPLFPARPGTLPEAEIHARL 481
Cdd:PRK09939 480 LTQLDLAVHVATKLNRshllTARHS-YILPVLGRSEidmqKSGAQAVTVEDSMSMIHAsRGVLKPAGVMLKSECAVVAGI 558
|
...
gi 15597910 482 LEA 484
Cdd:PRK09939 559 AQA 561
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
635-736 |
1.63e-08 |
|
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: 53.84 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 635 YPFILAagERRSDTSNTAVRDTGWHRRGRY-GTLRISPQDAEALGCADGEVLRVVTRRGEVEAEVEISDMMQPGNISLPN 713
Cdd:cd02780 1 YPFILV--TFKSNLNSHRSANAPWLKEIKPeNPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRPGVVAIEH 78
|
90 100 110
....*....|....*....|....*....|....
gi 15597910 714 GQG----------LDYRNAEGEVVR-RGVAPNEV 736
Cdd:cd02780 79 GYGhwaygavastIDGKDLPGDAWRgAGVNINDI 112
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
10-96 |
2.48e-08 |
|
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: 56.91 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 10 KTACILCSLNCGLEVQTENGRISKIRGDDDHPASQGYVCEKSqRMDY-YQNGADRLDTPMRRRpDGSYEAIDWDTAIREV 88
Cdd:cd02768 1 ESIDVHDALGSNIRVDVRGGEVMRILPRENEAINEEWISDKG-RFGYdGLNSRQRLTQPLIKK-GGKLVPVSWEEALKTV 78
|
....*...
gi 15597910 89 AEKFLAIK 96
Cdd:cd02768 79 AEGLKAVK 86
|
|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
13-240 |
4.14e-08 |
|
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: 56.19 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 13 CILCSLNCG-LEVQTENGRISKIRGdddhpasqgyVCEKSQRmdYYQNGADRLDTPMRRRpdgsyEAIDWDTAIREVAEK 91
Cdd:cd02761 4 CPFCGLLCDdIEVEVEDNKITKVRN----------ACRIGAA--KFARYERRITTPRIDG-----KPVSLEEAIEKAAEI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 92 FLAIKRRhggesiLYYGGGAQ-------GNHLG---GAYGDSTLKALGVKyrsNALAQEKTGEFwvqgkmfgTGVHGDFE 161
Cdd:cd02761 67 LKEAKRP------LFYGLGTTvceaqraGIELAeklGAIIDHAASVCHGP---NLLALQDSGWP--------TTTLGEVK 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 162 H-CEGAILIGKNPWQSH--------GFARARVllnaMAKDPA-RSIIVIDPRLSETAALADFHLQIRPGTDAWCLAALVG 231
Cdd:cd02761 130 NrADVIVYWGTNPMHAHprhmsrysVFPRGFF----REGGREdRTLIVVDPRKSDTAKLADIHLQIDPGSDYELLAALRA 205
|
....*....
gi 15597910 232 IIVQDGLLA 240
Cdd:cd02761 206 LLRGAGLVP 214
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
656-714 |
2.13e-07 |
|
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: 50.37 E-value: 2.13e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597910 656 TGWHRRGR----YG-----------TLRISPQDAEALGCADGEVLRVVTRRGEVEAEVEISDMMQPGNISLPNG 714
Cdd:cd02794 6 IGWHYKRRthstFDnvpwlreafpqEVWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVVALPQG 79
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
666-707 |
6.35e-07 |
|
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: 48.82 E-value: 6.35e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 15597910 666 TLRISPQDAEALGCADGEVLRVVTRRGEVEAEVEISDMMQPG 707
Cdd:cd02786 32 TLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPG 73
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
60-492 |
9.54e-07 |
|
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: 52.48 E-value: 9.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 60 GADRLDTPMRRRpDGSYEAIDWDTAIREVAEKFLAIKRRHGGE-----SILYYGGGAQGNHLGGAYGDSTLKALGVKYRS 134
Cdd:cd02756 114 GETRLTTPLVRR-GGQLQPTTWDDAIDLVARVIKGILDKDGNDdavfaSRFDHGGGGGGFENNWGVGKFFFMALQTPFVR 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 135 --NALAQekTGEFWVQGKMfgtGVHG------DFEHCEGAILIGKNPWQS-------HGF--------ARARVLLNAMAK 191
Cdd:cd02756 193 ihNRPAY--NSEVHATREM---GVGElnnsyeDARLADTIVLWGNNPYETqtvyflnHWLpnlrgatvSEKQQWFPPGEP 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 192 DPARSIIVIDPRLSETAALAD--------FHLQIRPGTDAwCLAALVGIIVQDGLlaRDWLAEhtsgyehivdelnaipv 263
Cdd:cd02756 268 VPPGRIIVVDPRRTETVHAAEaaagkdrvLHLQVNPGTDT-ALANAIARYIYESL--DEVLAE----------------- 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 264 ayCAETCGVAEDKLRAaarriasassvsALEDLGMqmnlhSTLGSYLQR--------LVW---------------LLTGH 320
Cdd:cd02756 328 --AEQITGVPRAQIEK------------AADWIAK-----PKEGGYRKRvmfeyekgIIWgndnyrpiyslvnlaIITGN 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 321 YGRPGTSNAfvpflSLSKASKGDTSMGKRGAPRVEKRSPVANA-KIIIG-------LIPCNvipEEILTDHPKRYRAMLV 392
Cdd:cd02756 389 IGRPGTGCV-----RQGGHQEGYVRPPPPPPPWYPQYQYAPYIdQLLISgkgkvlwVIGCD---PYKTTPNAQRLRETIN 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 393 ETGNPLHSLADSQR-----MREAMRALELS---------VVIDVAMTETARHADYVLPAASQFEKAEaTFFNLEFPRnaF 458
Cdd:cd02756 461 HRSKLVTDAVEAALyagtyDREAMVCLIGDaiqpgglfiVVQDIYPTKLAEDAHVILPAAANGEMNE-TSMNGHERR--L 537
|
490 500 510
....*....|....*....|....*....|....*
gi 15597910 459 HLRAPlFPARPGT-LPEAEIHARLLEAMGVLGEKD 492
Cdd:cd02756 538 RLYEK-FMDPPGEaMPDWWIAAMIANRIYELYQEE 571
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
667-714 |
1.67e-05 |
|
The MopB_CT_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. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239186 [Multi-domain] Cd Length: 124 Bit Score: 44.66 E-value: 1.67e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 15597910 667 LRISPQDAEALGCADGEVLRVVTRRGEVEAEVEISDMMQPGNISLPNG 714
Cdd:cd02785 34 VKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGVVTAEQG 81
|
|
| 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 ... |
668-717 |
1.75e-05 |
|
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: 43.84 E-value: 1.75e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 15597910 668 RISPQDAEALGCADGEVLRVVTRRGEVEAEVEISDMMQPGNISLPNGQGL 717
Cdd:cd02788 32 RLSPADAARLGLADGDLVEFSLGDGTLTLPVQISKYLPAGVVGLPLGAGF 81
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
669-760 |
2.11e-05 |
|
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: 44.52 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 669 ISPQDAEALGCADGEVLRVVTRRGEVEAEVEISDMMQPGNISLPngqgldyRNAEGEVVRRGVAPNEVT----DCTqrdf 744
Cdd:cd02792 39 ISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHEVGIP-------YHWGGMGLVIGDSANTLTpyvgDPN---- 107
|
90
....*....|....*.
gi 15597910 745 lAGTPWHKYVPARLER 760
Cdd:cd02792 108 -TQTPEYKAFLVNIEK 122
|
|
| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
659-715 |
2.92e-05 |
|
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: 44.68 E-value: 2.92e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 15597910 659 HRRGRYgTLRISPQDAEALGCADGEVLRVVTRRGEVEAEVEISDMMQPGNISLPNGQ 715
Cdd:cd02776 26 LQRGGP-VVWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTVFMYHAQ 81
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
59-104 |
5.57e-05 |
|
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: 46.19 E-value: 5.57e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 15597910 59 NGADRLDTPMRRRpDGSYEAIDWDTAIREVAEKFLAIKRRHGGESI 104
Cdd:cd02772 50 NSEDRLTKPMIKK-DGQWQEVDWETALEYVAEGLSAIIKKHGADQI 94
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
627-736 |
3.37e-04 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 44.17 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 627 SAPPHDPAYPFILAAGErrsdtsntAVRdTGWHR---RGRY--------GT-----LRISPQDAEALGCADGEVLRVVTR 690
Cdd:PRK07860 673 AAPAVPAAAPPQPGAGE--------AVL-ATWRMlldDGRLqdgephlaGTarppvARLSAATAAEIGVADGDAVTVSTE 743
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 15597910 691 RGEVEAEVEISDmMQPGNISLPNgqgldyrNAEGEVVRR--GVAPNEV 736
Cdd:PRK07860 744 RGSITLPLAITD-MPDRVVWLPL-------NSPGSTVRRtlGATAGAV 783
|
|
| MopB_CT_FmdC-FwdD |
cd02789 |
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran ... |
669-714 |
3.76e-04 |
|
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran dehydrogenase (FmdC) and subunit D of tungsten formylmethanofuran dehydrogenase (FwdD), and other related proteins. Formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and some eubacteria. Members of this CD belong to the molybdopterin_binding superfamily of proteins. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239190 [Multi-domain] Cd Length: 106 Bit Score: 40.49 E-value: 3.76e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 15597910 669 ISPQDAEALGCADGEVLRVVTRRGEVEAEVEISDMMQPGNISLPNG 714
Cdd:cd02789 35 INPEDYKLLGKPEGDKVKVTSEFGEVVVFAKENEGVPEGMVFIPMG 80
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
634-760 |
1.17e-03 |
|
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: 39.60 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 634 AYPFILAAGERRSDTSNTAVRDTGWHRRGR-YGTLRISPQDAEALGCADGEVLRVVTRRGEVEAEVEISDMMQPGNISLP 712
Cdd:cd02781 1 EYPLILTTGARSYYYFHSEHRQLPSLRELHpDPVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVRAE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 15597910 713 NGQGLDYRNAEGEVV--RRGVAPNEVTDCTQRDFLAGTPWHKYVPARLER 760
Cdd:cd02781 81 HGWWYPEREAGEPALggVWESNANALTSDDWNDPVSGSSPLRSMLCKIYK 130
|
|
| FwdD |
COG1153 |
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion]; |
665-760 |
1.26e-03 |
|
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion];
Pssm-ID: 440767 [Multi-domain] Cd Length: 127 Bit Score: 39.45 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 665 GTLRISPQDAEALGCADGEVLRVVTRRGEVEAEVEISDMMQPGNISLPNGQgldYRNAegevvrrgVAPNEvTDCTqrdf 744
Cdd:COG1153 31 AVCELNPEDMKKLGIKEGDKVKVTSEYGEVVVKAKESEDLHPGLVFIPMGP---WANA--------VVPPE-THST---- 94
|
90
....*....|....*.
gi 15597910 745 laGTPWHKYVPARLER 760
Cdd:COG1153 95 --GMPDFKGVPVEVEP 108
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
668-761 |
1.58e-03 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 41.91 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597910 668 RISPQDAEALGCADGEVLRVVTRRGEVEAEVEISDMMQPGNISLPNGQGL-----------DYRNAEGEVVRRGVAPNE- 735
Cdd:PRK14991 919 ALNPQDAARLGIQHGDRVRISTPGGSVVAQASVLNGVMPGVIAIEHGYGHrelgarahsidGKPMPANPQIRAGVNLNDl 998
|
90 100 110
....*....|....*....|....*....|...
gi 15597910 736 -VTDCTQR------DFLAGTPWHKYVPARLERL 761
Cdd:PRK14991 999 gLADPTREitnvwvDWVSGAAVRQGLPAKIEKI 1031
|
|
| |
