|
Name |
Accession |
Description |
Interval |
E-value |
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
1-529 |
0e+00 |
|
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate dehydrogenase alpha chains found mainly archaea but also in alpha and gamma proteobacteria and a small number of gram positive bacteria. The alpha chain contains domains for molybdopterin dinucleotide binding and molybdopterin oxidoreductase (pfam01568 and pfam00384, respectively). The holo-enzyme also contains beta and gamma subunits. The enzyme catalyzes the oxidation of formate (produced from pyruvate during anaerobic growth) to carbon dioxide with the concomitant release of two electrons and two protons. The enzyme's purpose is to allow growth on formate in some circumstances and, in the case of FdhH in gamma proteobacteria, to pass electrons to hydrogenase (by which process acid is neutralized). This model is well-defined, with only a single fragmentary sequence falling between trusted and noise. The alpha subunit of a version of nitrate reductase is closely related.
Pssm-ID: 130652 [Multi-domain] Cd Length: 671 Bit Score: 904.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 1 MSNAINEIDNTDLVFVFGYNPADSHPIVANHVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAMGHVIIE 80
Cdd:TIGR01591 146 MSNTISEIENADLIVIIGYNPAESHPVVAQYLKNAKRNGAKIIVIDPRKTETAKIADLHIPLKPGTDIALLNAMANVIIE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 81 ENLYDKAFVASRTEGFEEYSKIVEGYTPESVEEITGVSAQEIRQAARMYASAKSAAILWGMGVTQFYQGVETVRSLTSLA 160
Cdd:TIGR01591 226 EGLYDKAFIEKRTEGFEEFREIVKGYTPEYVEDITGVPADLIREAARMYAKAGSAAILWGMGVTQHSQGVETVMALINLA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 161 MLTGNLGKPSAGVNPVRGQNNVQGACDMGALPDTYPGYQYVKFPENREKFAKAWGVESLPAHTGYRISELPHRAAHGEVR 240
Cdd:TIGR01591 306 MLTGNIGKPGGGVNPLRGQNNVQGACDMGALPDFLPGYQPVSDEEVREKFAKAWGVVKLPAEPGLRIPEMIDAAADGDVK 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 241 AAYIMGEDPLQTDAELSAVRKAFEDLELVIVQGIFMTKTASAADVILPSTSWGEHEGVFSAADRGFQRFFKAVEPKWDLK 320
Cdd:TIGR01591 386 ALYIMGEDPLQSDPNTSKVRKALEKLELLVVQDIFMTETAKYADVVLPAAAWLEKEGTFTNAERRIQRFFKAVEPKGESK 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 321 TDWQIISEIATRMGYPMHYNNTQEIWDELRHLCPDFYGATYEKMGELGYIQWPCRDtsDADQGTSYLFKEKFDTPNGLAQ 400
Cdd:TIGR01591 466 PDWEIIQELANALGLDWNYNHPQEIMDEIRELTPLFAGLTYERLDELGSLQWPCND--SDASPTSYLYKDKFATPDGKAK 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 401 FFTCDWVAPIDKLTEEYPMVLSTVREVGHYSCRSMTGNCAALAALADEPgYAQINTADAARLGIEDEALVWVHSRKGKII 480
Cdd:TIGR01591 544 FIPLEWVAPIEEPDDEYPLILTTGRVLTHYNVGEMTRRVAGLRRLSPEP-YVEINTEDAKKLGIKDGDLVKVKSRRGEIT 622
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 879957582 481 TRAQVSDRPNKGAIYMTYQWWIGACNELVTENLSPITKTPEYKYCAVRV 529
Cdd:TIGR01591 623 LRAKVSDRVNKGAIYITMHFWDGAVNNLTTDDLDPISGTPEYKYTAVRI 671
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
1-534 |
0e+00 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 779.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 1 MSNAINEIDNTDLVFVFGYNPADSHPIVANHVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAMGHVIIE 80
Cdd:COG3383 154 PPNSYDDIEEADVILVIGSNPAEAHPVLARRIKKAKKNGAKLIVVDPRRTETARLADLHLQIKPGTDLALLNGLLHVIIE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 81 ENLYDKAFVASRTEGFEEYSKIVEGYTPESVEEITGVSAQEIRQAARMYASAKSAAILWGMGVTQFYQGVETVRSLTSLA 160
Cdd:COG3383 234 EGLVDEDFIAERTEGFEELKASVAKYTPERVAEITGVPAEDIREAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLA 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 161 MLTGNLGKPSAGVNPVRGQNNVQGACDMGALPDTYPGYQYVKFPENREKFAKAWGVESLPAHTGYRISELPHRAAHGEVR 240
Cdd:COG3383 314 LATGNIGRPGTGPFPLTGQNNVQGGRDMGALPNVLPGYRDVTDPEHRAKVADAWGVPPLPDKPGLTAVEMFDAIADGEIK 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 241 AAYIMGEDPLQTDAELSAVRKAFEDLELVIVQGIFMTKTASAADVILPSTSWGEHEGVFSAADRGFQRFFKAVEPKWDLK 320
Cdd:COG3383 394 ALWIIGENPAVSDPDANHVREALEKLEFLVVQDIFLTETAEYADVVLPAASWAEKDGTFTNTERRVQRVRKAVEPPGEAR 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 321 TDWQIISEIATRMGYPMHYNNTQEIWDELRHLCPDFYGATYEKMGELGYIQWPCRDtsDADQGTSYLFKEKFDTPNGLAQ 400
Cdd:COG3383 474 PDWEIIAELARRLGYGFDYDSPEEVFDEIARLTPDYSGISYERLEALGGVQWPCPS--EDHPGTPRLFTGRFPTPDGKAR 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 401 FFTCDWVAPIDKLTEEYPMVLSTVREVGHYSCRSMTGNCAALAALADEPgYAQINTADAARLGIEDEALVWVHSRKGKII 480
Cdd:COG3383 552 FVPVEYRPPAELPDEEYPLVLTTGRLLDQWHTGTRTRRSPRLNKHAPEP-FVEIHPEDAARLGIKDGDLVRVSSRRGEVV 630
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 879957582 481 TRAQVSDRPNKGAIYMTYQWWIGACNELVTENLSPITKTPEYKYCAVRVEPIAD 534
Cdd:COG3383 631 LRARVTDRVRPGTVFMPFHWGEGAANALTNDALDPVSKQPEYKACAVRVEKVAE 684
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
1-408 |
0e+00 |
|
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. Members of the MopB_Formate-Dh-H CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239154 [Multi-domain] Cd Length: 512 Bit Score: 614.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 1 MSNAINEIDNTDLVFVFGYNPADSHPIVANHVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAMGHVIIE 80
Cdd:cd02753 147 MTNSIADIEEADVILVIGSNTTEAHPVIARRIKRAKRNGAKLIVADPRRTELARFADLHLQLRPGTDVALLNAMAHVIIE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 81 ENLYDKAFVASRTEGFEEYSKIVEGYTPESVEEITGVSAQEIRQAARMYASAKSAAILWGMGVTQFYQGVETVRSLTSLA 160
Cdd:cd02753 227 EGLYDEEFIEERTEGFEELKEIVEKYTPEYAERITGVPAEDIREAARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLA 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 161 MLTGNLGKPSAGVNPVRGQNNVQGACDMGALPDTYPGYqyvkfpenrekfakawgveslpahtgyriselphraahgeVR 240
Cdd:cd02753 307 LLTGNIGRPGTGVNPLRGQNNVQGACDMGALPNVLPGY----------------------------------------VK 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 241 AAYIMGEDPLQTDAELSAVRKAFEDLELVIVQGIFMTKTASAADVILPSTSWGEHEGVFSAADRGFQRFFKAVEPKWDLK 320
Cdd:cd02753 347 ALYIMGENPALSDPNTNHVRKALESLEFLVVQDIFLTETAELADVVLPAASFAEKDGTFTNTERRVQRVRKAVEPPGEAR 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 321 TDWQIISEIATRMGYPMHYNNTQEIWDELRHLCPDFYGATYEKMGELGYIQWPCRDtsDADQGTSYLFKEKFDTPNGLAQ 400
Cdd:cd02753 427 PDWEIIQELANRLGYPGFYSHPEEIFDEIARLTPQYAGISYERLERPGGLQWPCPD--EDHPGTPILHTERFATPDGKAR 504
|
....*...
gi 879957582 401 FFTCDWVA 408
Cdd:cd02753 505 FMPVEYRP 512
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
7-534 |
7.42e-153 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 453.53 E-value: 7.42e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 7 EIDNTDLVFVFGYNPADSHPIVANHVINA-KRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAMGHVIIEENLYD 85
Cdd:COG0243 184 DLEHADLIVLWGSNPAENHPRLLRRLREAaKKRGAKIVVIDPRRTETAAIADEWLPIRPGTDAALLLALAHVLIEEGLYD 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 86 KAFVASRTEGFEEYSKIVEGYTPESVEEITGVSAQEIRQAARMYASAKSAAILWGMGVTQFYQGVETVRSLTSLAMLTGN 165
Cdd:COG0243 264 RDFLARHTVGFDELAAYVAAYTPEWAAEITGVPAEDIRELAREFATAKPAVILWGMGLQQHSNGTQTVRAIANLALLTGN 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 166 LGKPSAGVNPVRGQNNVQGacdmgalpDTYPgyqyvkfpenrekfakawgveslpahtgyriselphraahgeVRAAYIM 245
Cdd:COG0243 344 IGKPGGGPFSLTGEAILDG--------KPYP------------------------------------------IKALWVY 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 246 GEDPLQTDAELSAVRKAFEDLELVIVQGIFMTKTASAADVILPSTSWGEHEGVF-SAADRGFQRFFKAVEPKWDLKTDWQ 324
Cdd:COG0243 374 GGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARYADIVLPATTWLERDDIVtNSEDRRVHLSRPAVEPPGEARSDWE 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 325 IISEIATRMGYPMHYNNTQEIWDELRHLC--PDFYGATYEKMGELGYIQWPCRDtsdadqGTSYLFKEKFDTPNGLAQFF 402
Cdd:COG0243 454 IFAELAKRLGFEEAFPWGRTEEDYLRELLeaTRGRGITFEELREKGPVQLPVPP------EPAFRNDGPFPTPSGKAEFY 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 403 TC--------DWVAPI---DKLTEEYPMVLSTVREVGHYScrSMTGNCAALAALADEPgYAQINTADAARLGIEDEALVW 471
Cdd:COG0243 528 SEtlalpplpRYAPPYegaEPLDAEYPLRLITGRSRDQWH--STTYNNPRLREIGPRP-VVEINPEDAAALGIKDGDLVR 604
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 472 VHSRKGKIITRAQVSDRPNKGAIYMTYQWW-------IGACNELVTENLSPITKTPEYKYCAVRVEPIAD 534
Cdd:COG0243 605 VESDRGEVLARAKVTEGIRPGVVFAPHGWWyepaddkGGNVNVLTPDATDPLSGTPAFKSVPVRVEKAAA 674
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
7-409 |
1.88e-128 |
|
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: 387.35 E-value: 1.88e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 7 EIDNTDLVFVFGYNPADSHPIVANHVINAKRN--GAKIIVCDPRKIETARIADMHIALKNGSNIALLNAMGHVIIEENLY 84
Cdd:cd02754 154 DIEHADCFFLIGSNMAECHPILFRRLLDRKKAnpGAKIIVVDPRRTRTADIADLHLPIRPGTDLALLNGLLHVLIEEGLI 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 85 DKAFVASRTEGFEEYSKIVEGYTPESVEEITGVSAQEIRQAARMYASAKSAAILWGMGVTQFYQGVETVRSLTSLAMLTG 164
Cdd:cd02754 234 DRDFIDAHTEGFEELKAFVADYTPEKVAEITGVPEADIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHLATG 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 165 NLGKPSAGVNPVRGQNNVQGACDMGALPDTYPGYQYVKFPENREKFAKAWGV--ESLPAHTGYRISELPHRAAHGEVRAA 242
Cdd:cd02754 314 KIGRPGSGPFSLTGQPNAMGGREVGGLANLLPGHRSVNNPEHRAEVAKFWGVpeGTIPPKPGLHAVEMFEAIEDGEIKAL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 243 YIMGEDPLQTDAELSAVRKAFEDLELVIVQGIF-MTKTASAADVILPSTSWGEHEGVFSAADRGFQRFFKAVEPKWDLKT 321
Cdd:cd02754 394 WVMCTNPAVSLPNANRVREALERLEFVVVQDAFaDTETAEYADLVLPAASWGEKEGTMTNSERRVSLLRAAVEPPGEARP 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 322 DWQIISEIATRMGYPM--HYNNTQEIWDELRHLCP----DFYGATYEKMGELGyIQWPCRDtsDADQGTSYLF-KEKFDT 394
Cdd:cd02754 474 DWWILADVARRLGFGElfPYTSPEEVFEEYRRLSRgrgaDLSGLSYERLRDGG-VQWPCPD--GPPEGTRRLFeDGRFPT 550
|
410
....*....|....*
gi 879957582 395 PNGLAQFFTCDWVAP 409
Cdd:cd02754 551 PDGRARFVAVPYRPP 565
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
1-332 |
1.63e-74 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 240.76 E-value: 1.63e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 1 MSNAINEIDNTDLVFVFGYNPADSHPIVANHVINA-KRNGAKIIVCDPRKieTARIADMHIALKNGSNIALLNAMGHVII 79
Cdd:pfam00384 99 FNSSIADIENADLILLIGTNPREEAPILNARIRKAaLKGKAKVIVIGPRL--DLTYADEHLGIKPGTDLALALAGAHVFI 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 80 EENLYDKAFvasrtegfeeyskivegytpesveeitgvsaqeirqaarmyasAKSAAILWGMGVTQFYQGVETVRSLTSL 159
Cdd:pfam00384 177 KELKKDKDF-------------------------------------------APKPIIIVGAGVLQRQDGEAIFRAIANL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 160 AMLTGNLGKPSAGVNPVrgqNNVQG-ACDMGALpdtypgyqyvkfpenrekfakawgveSLPAHTGYRISELPHRAAHGE 238
Cdd:pfam00384 214 ADLTGNIGRPGGGWNGL---NILQGaASPVGAL--------------------------DLGLVPGIKSVEMINAIKKGG 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 239 VRAAYIMGEDPLQTDAELSAVRKAFEDLELVIVQGIFM-TKTASAADVILPSTSWGEHEGVFSAADRGFQRFFKAVEPKW 317
Cdd:pfam00384 265 IKVLYLLGNNPFVTHADENRVVKALQKLDLFVVYDGHHgDKTAKYADVILPAAAYTEKNGTYVNTEGRVQSTKQAVPPPG 344
|
330
....*....|....*
gi 879957582 318 DLKTDWQIISEIATR 332
Cdd:pfam00384 345 EAREDWKILRALSEV 359
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
1-333 |
2.92e-74 |
|
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: 240.69 E-value: 2.92e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 1 MSNAINEIDNTDLVFVFGYNPADSHPIVANHVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAmghviie 80
Cdd:cd00368 147 PTNTLADIENADLILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRRTETAAKADEWLPIRPGTDAALALA------- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 81 enlydkafvasrtegfeeyskivegytpESVEEITGVSAQEIRQAARMYASAKSAAILWGMGVTQFYQGVETVRSLTSLA 160
Cdd:cd00368 220 ----------------------------EWAAEITGVPAETIRALAREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLA 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 161 MLTGNLGKPSAGVNPvrgqnnvqgacdmgalpdtypgyqyvkfpenrekfakawgveslpahtgyriselphraahgevr 240
Cdd:cd00368 272 ALTGNIGRPGGGLGP----------------------------------------------------------------- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 241 aayimGEDPLQTDAELSAVRKAFEDLELVIVQGIFMTKTASAADVILPSTSWGEHEGVFSAADRGFQRFFKAVEPKWDLK 320
Cdd:cd00368 287 -----GGNPLVSAPDANRVRAALKKLDFVVVIDIFMTETAAYADVVLPAATYLEKEGTYTNTEGRVQLFRQAVEPPGEAR 361
|
330
....*....|...
gi 879957582 321 TDWQIISEIATRM 333
Cdd:cd00368 362 SDWEILRELAKRL 374
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
1-334 |
2.84e-64 |
|
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: 221.89 E-value: 2.84e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 1 MSNAINEIDNTDLVFVFGYNPADSHPIVANHVINAK-RNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAMGHVII 79
Cdd:cd02752 160 MTNSWNDIKNADVILVMGGNPAEAHPVSFKWILEAKeKNGAKLIVVDPRFTRTAAKADLYVPIRSGTDIAFLGGMINYII 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 80 EenlydkafvasrtegfeeyskivegYTPESVEEITGVSAQEIRQAARMYAS----AKSAAILWGMGVTQFYQGVETVRS 155
Cdd:cd02752 240 R-------------------------YTPEEVEDICGVPKEDFLKVAEMFAAtgrpDKPGTILYAMGWTQHTVGSQNIRA 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 156 LTSLAMLTGNLGKPSAGVNPVRGQNNVQGACDMGALPDTYPGyqyvkfpenrekfakawgveslpahtgyriselphraa 235
Cdd:cd02752 295 MCILQLLLGNIGVAGGGVNALRGHSNVQGATDLGLLSHNLPG-------------------------------------- 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 236 hgevraaYIMGEDPLQTDAELSAVRKAFEDLELVIVQGIFMTKTASAAD-------------VILPSTSWGEHEGVFSAA 302
Cdd:cd02752 337 -------YLGGQNPNSSFPNANKVRRALDKLDWLVVIDPFPTETAAFWKnpgmdpksiqtevFLLPAACQYEKEGSITNS 409
|
330 340 350
....*....|....*....|....*....|..
gi 879957582 303 DRGFQRFFKAVEPKWDLKTDWQIISEIATRMG 334
Cdd:cd02752 410 GRWLQWRYKVVEPPGEAKSDGDILVELAKRLG 441
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
1-402 |
2.52e-63 |
|
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: 215.58 E-value: 2.52e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 1 MSNAINEIDNTDLVFVFGYNPADSHPIVANHVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAMGHVIIE 80
Cdd:cd02766 148 LGNDPEDMVNADLIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDPYRTATAARADLHIQIRPGTDGALALGVAKVLFR 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 81 ENLYDKAFVASRTEGFEEYSKIVEGYTPESVEEITGVSAQEIRQAARMYASAKSAAILWGMGVTQFYQGVETVRSLTSLA 160
Cdd:cd02766 228 EGLYDRDFLARHTEGFEELKAHLETYTPEWAAEITGVSAEEIEELARLYGEAKPPSIRLGYGMQRYRNGGQNVRAIDALP 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 161 MLTGNLGKPSAGVNpvrgqnnvqgacdmgalpdtypgyqyvkfpenrekfakawgveslpahtgYRISELPhraahgeVR 240
Cdd:cd02766 308 ALTGNIGVPGGGAF--------------------------------------------------YSNSGPP-------VK 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 241 AAYIMGEDPLQTDAELSAVRK-AFEDLELVIVQGIFMTKTASAADVILPSTSWGEHEGV-FSAADRGFQRFFKAVEPKWD 318
Cdd:cd02766 331 ALWVYNSNPVAQAPDSNKVRKgLAREDLFVVVHDQFMTDTARYADIVLPATTFLEHEDVyASYWHYYLQYNEPAIPPPGE 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 319 LKTDWQIISEIATRMGY---PMHYNNTQEIWDELRHLCPDFYGATYEKMGE---LGYIQWPCRDtsdadqgtsylfkEKF 392
Cdd:cd02766 411 ARSNTEIFRELAKRLGFgepPFEESDEEWLDQALDGTGLPLEGIDLERLLGprkAGFPLVAWED-------------RGF 477
|
410
....*....|
gi 879957582 393 DTPNGLAQFF 402
Cdd:cd02766 478 PTPSGKFEFY 487
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
10-335 |
1.68e-57 |
|
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: 199.45 E-value: 1.68e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 10 NTDLVFVFGYNPADSHPI-VANHVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAMGHVIIEENLYDKAF 88
Cdd:cd02759 160 NPECIVLWGKNPLNSNLDlQGHWLVAAMKRGAKLIVVDPRLTWLAARADLWLPIRPGTDAALALGMLNVIINEGLYDKDF 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 89 VASRTEGFEEYSKIVEGYTPESVEEITGVSAQEIRQAARMYASAKSAAILWGMGVTQFYQGVETVRSLTSLAMLTGNLGK 168
Cdd:cd02759 240 VENWCYGFEELAERVQEYTPEKVAEITGVPAEKIRKAARLYATAKPACIQWGLAIDQQKNGTQTSRAIAILRAITGNLDV 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 169 PSAGVNpvrgqnnvqgacdmgaLPdtYPgyqyvkfpenrekfakawgveslpahtgyriselphraahgeVRAAYIMGED 248
Cdd:cd02759 320 PGGNLL----------------IP--YP------------------------------------------VKMLIVFGTN 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 249 PLQTDAELSAVRKAFEDLELVIVQGIFMTKTASAADVILPSTSWGEHEGVFSAADRG--FQRFFKAVEPKWDLKTDWQII 326
Cdd:cd02759 340 PLASYADTAPVLEALKALDFIVVVDLFMTPTAMLADIVLPVAMSLERPGLRGGFEAEnfVQLRQKAVEPYGEAKSDYEIV 419
|
....*....
gi 879957582 327 SEIATRMGY 335
Cdd:cd02759 420 LELGKRLGP 428
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
415-531 |
1.97e-57 |
|
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: 187.45 E-value: 1.97e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 415 EEYPMVLSTVREVGHYSCRSMTGNCAALAALADEPgYAQINTADAARLGIEDEALVWVHSRKGKIITRAQVSDRPNKGAI 494
Cdd:cd02790 1 EEYPLVLTTGRVLYHYHTGTMTRRAEGLDAIAPEE-YVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGVV 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 879957582 495 YMTYQWWIGACNELVTENLSPITKTPEYKYCAVRVEP 531
Cdd:cd02790 80 FMPFHFAEAAANLLTNAALDPVAKIPEFKVCAVRVEK 116
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
9-401 |
4.83e-57 |
|
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: 200.61 E-value: 4.83e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 9 DNTDLVFVFGYNPADSHPIVANHVINAKRNGAKIIVCDPRKiETA------------------RIADMHIALKNGSNIAL 70
Cdd:cd02767 162 EHTDLIFFIGQNPGTNHPRMLHYLREAKKRGGKIIVINPLR-EPGlerfanpqnpesmltggtKIADEYFQVRIGGDIAL 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 71 LNAMGHVIIEE-----NLYDKAFVASRTEGFEEYSKIVEGYTPESVEEITGVSAQEIRQAARMYASAKSAAILWGMGVTQ 145
Cdd:cd02767 241 LNGMAKHLIERddepgNVLDHDFIAEHTSGFEEYVAALRALSWDEIERASGLSREEIEAFAAMYAKSERVVFVWGMGITQ 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 146 FYQGVETVRSLTSLAMLTGNLGKPSAGVNPVRGQNNVQGACDMGAlpdtypgyqYVK-FPENREKFAKAWGVEsLPAHTG 224
Cdd:cd02767 321 HAHGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQGDRTMGI---------TEKpFPEFLDALEEVFGFT-PPRDPG 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 225 YRISELPHRAAHGEVRAAYIMGEDPLQTDAELSAVRKAFEDLELVIVQGIF----MTKTASAAdVILPSTSWGE------ 294
Cdd:cd02767 391 LDTVEAIEAALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLTVHVATKlnrsHLVHGEEA-LILPCLGRTEidmqag 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 295 --------------HEGVFSAADRGFQRF---------FKAVEPkwDLKTDWQIISEIATRMG-------YPM--HYNNT 342
Cdd:cd02767 470 gaqavtvedsmsmtHTSRGRLKPASRVLLseeaivagiAGARLG--EAKPEWEILVEDYDRIRdeiaaviYEGfaDFNQR 547
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 879957582 343 QEIWDElRHLCPdfygatyekmgelGYIQWpcrdtsdadqgtsylfkeKFDTPNGLAQF 401
Cdd:cd02767 548 GDQPGG-FHLPN-------------GARER------------------KFNTPSGKAQF 574
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
8-368 |
2.26e-53 |
|
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: 191.29 E-value: 2.26e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 8 IDNTDLVFVFGYNPAD---SHPIVANHVIN-----AKRNGAKIIVCDPRKIETAR-IADMHIALKNGSNIALLNAMGHVI 78
Cdd:cd02751 167 AEHSDLVVLFGANPLKtrqGGGGGPDHGSYyylkqAKDAGVRFICIDPRYTDTAAvLAAEWIPIRPGTDVALMLAMAHTL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 79 IEENLYDKAFVASRTEGFEEYSKIVEGY------TPESVEEITGVSAQEIRQAARMYASaKSAAILWGMGVTQFYQGVET 152
Cdd:cd02751 247 ITEDLHDQAFLARYTVGFDEFKDYLLGEsdgvpkTPEWAAEITGVPAETIRALAREIAS-KRTMIAQGWGLQRAHHGEQP 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 153 VRSLTSLAMLTGNLGKPSAGVNPVRGQNNVQGAcdmGALPDTYPGYQYVKFPenrekfakawGVESLPAhtgYRISEL-- 230
Cdd:cd02751 326 AWMLVTLAAMLGQIGLPGGGFGFGYGYSNGGGP---PRGGAGGPGLPQGKNP----------VKDSIPV---ARIADAll 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 231 ----PHRAAHGE-----VRAAYIMGEDPL--QTDaeLSAVRKAFEDLELVIVQGIFMTKTASAADVILPSTSWGEHE--G 297
Cdd:cd02751 390 npgkEFTANGKLktypdIKMIYWAGGNPLhhHQD--LNRLIKALRKDETIVVHDIFWTASARYADIVLPATTSLERNdiG 467
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 879957582 298 VFSAADRGFQRFF-KAVEPKWDLKTDWQIISEIATRMGYPMHYNNTQEIWDELRHlcpdFYGATYEKMGELG 368
Cdd:cd02751 468 LTGNYSNRYLIAMkQAVEPLGEARSDYEIFAELAKRLGVEEEFTEGRDEMEWLEH----LYEETRAKAAGPG 535
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
2-367 |
2.35e-52 |
|
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: 188.69 E-value: 2.35e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 2 SNAINEIDNTDLVFVFGYNPADSHPIVANHVIN---AKRNGAKIIVCDPRKIETAR-IADMHIALKNGSNIALLNAMGHV 77
Cdd:cd02770 158 GSSLDDLKDSKLVVLFGHNPAETRMGGGGSTYYylqAKKAGAKFIVIDPRYTDTAVtLADEWIPIRPGTDAALVAAMAYV 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 78 IIEENLYDKAFVASRTEGFEE------------YSKIVEGY-------TPESVEEITGVSAQEIRQAARMYASAKSAAIL 138
Cdd:cd02770 238 MITENLHDQAFLDRYCVGFDAehlpegappnesYKDYVLGTgydgtpkTPEWASEITGVPAETIRRLAREIATTKPAAIL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 139 WGMGVTQFYQGVETVRSLTSLAMLTGNLGKPSAGVNPVRGQNNVQGAcdmgALP-------DTYPGYQYVKFPENREKFA 211
Cdd:cd02770 318 QGWGPQRHANGEQAARAIMMLAAMTGNVGIPGGNTGARPGGSAYNGA----GLPagknpvkTSIPCFMWTDAIERGEEMT 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 212 KAWGVESLPAHTGYRISELPHRAAHgevraaYIMGEDPLQTDAeLSAVRKAFEDLELVIVQGIFMTKTASAADVILPSTS 291
Cdd:cd02770 394 ADDGGVKGADKLKSNIKMIWNYAGN------TLINQHSDDNNT-TRALLDDESKCEFIVVIDNFMTPSARYADILLPDTT 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 292 WGEHEGVFSAADRG----FQRFFKAVEPKWDLKTDWQIISEIATRMGYPMHYNN--TQEIWdeLRHLcpdfYGATYEKMG 365
Cdd:cd02770 467 ELEREDIVLTSNAGmmeyLIYSQKAIEPLYECKSDYEICAELAKRLGVEDQFTEgkTEQEW--LEEL----YGQTRAKEP 540
|
..
gi 879957582 366 EL 367
Cdd:cd02770 541 GL 542
|
|
| formate-DH-alph |
TIGR01553 |
formate dehydrogenase-N alpha subunit; This model describes a subset of formate dehydrogenase ... |
1-333 |
4.76e-49 |
|
formate dehydrogenase-N alpha subunit; This model describes a subset of formate dehydrogenase alpha chains found mainly in proteobacteria but also in Aquifex. The alpha chain contains domains for molybdopterin dinucleotide binding and molybdopterin oxidoreductase (pfam01568 and pfam00384, respectively). The holo-enzyme also contains beta and gamma subunits of 32 and 20 kDa. The enzyme catalyzes the oxidation of formate (produced from pyruvate during anaerobic growth) to carbon dioxide with the concomitant release of two electrons and two protons. The electrons are utilized mainly in the nitrate respiration by nitrate reductase. In E. coli and Salmonella, there are two forms of the formate dehydrogenase, one induced by nitrate which is strictly anaerobic (fdn), and one incuced during the transition from aerobic to anaerobic growth (fdo). This subunit is one of only three proteins in E. coli which contain selenocysteine. This model is well-defined, with a large, unpopulated trusted/noise gap. [Energy metabolism, Anaerobic, Energy metabolism, Electron transport]
Pssm-ID: 273689 [Multi-domain] Cd Length: 1009 Bit Score: 182.80 E-value: 4.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 1 MSNAINEIDNTDLVFVFGYNPADSHPIVANHVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAMGHVIIE 80
Cdd:TIGR01553 212 MTNNWVDIKNSDLILVMGGNPAENHPIGFKWAIRAKKKGAKIIHIDPRFNRTATVADLYAPIRSGSDIAFLNGMIKYILE 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 81 ENLYDKAFVASRTEG---------FEE------------YSKI-------------------------------VEGYTP 108
Cdd:TIGR01553 292 KELYQKEYVVNYTNAsfivgegfaFEDglfagynketrkYDKSkwgyefdengnpkrdetlkhprcvfnilkehYSRYTP 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 109 ESVEEITGVSAQEIRQAARMYASA----KSAAILWGMGVTQFYQGVETVRSLTSLAMLTGNLGKPSAGVNPVRGQNNVQG 184
Cdd:TIGR01553 372 EKVSAICGTPKELFLKVYEEYCKTgkpnKAMTILYALGWTQHSVGTQNIRAMSINQLLLGNIGVPGGGINALRGHSNVQG 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 185 ACDMGALPDTYPGY------------QYVK-----------------FPENREKFAKA-----------WGVESLPAHTG 224
Cdd:TIGR01553 452 STDHGLLMHILPGYlgtprasiptyeQYTKkftpvskdpqsanywsnFPKFFASYIKSmwgdaatnengWAYDYLPKGED 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 225 YRISELPH--RAAHGEVRAAYIMGEDPLQTDAELSAVRKAFEDLELVIVQGIFMTKTAS---AADV----------ILPS 289
Cdd:TIGR01553 532 GYDSWLTLfdDMFQGKIKGFFAWGQNPLNSGPNSNKTREALTKLKWMVVMDPFDNETGSfwrGPGMdpkeiktevfFLPT 611
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 879957582 290 TSWGEHEGVFSAADRGFQRFFKAVEPKWDLKTDWQIISEIATRM 333
Cdd:TIGR01553 612 AVFIEKEGSISNSGRWMQWRYKGPDPPGNAIPDGDIIVELAKRV 655
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
1-333 |
3.22e-48 |
|
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: 175.66 E-value: 3.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 1 MSNAINEIDNTDLVFVFGYNPADSH------PIVANHVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAM 74
Cdd:cd02762 147 GLHPVPDIDRTDYLLILGANPLQSNgslrtaPDRVLRLKAAKDRGGSLVVIDPRRTETAKLADEHLFVRPGTDAWLLAAM 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 75 GHVIIEENLYDKAFVASRTEGFEEYSKIVEGYTPESVEEITGVSAQEIRQAARMYASAKSAAILWGMGVTQFYQGVETVR 154
Cdd:cd02762 227 LAVLLAEGLTDRRFLAEHCDGLDEVRAALAEFTPEAYAPRCGVPAETIRRLAREFAAAPSAAVYGRLGVQTQLFGTLCSW 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 155 SLTSLAMLTGNLGKPSagvnpvrGQNNVQGACDmgalpdtypgyqYVKFPENREKFAKAW--GVESLPAHTG-YRISELP 231
Cdd:cd02762 307 LVKLLNLLTGNLDRPG-------GAMFTTPALD------------LVGQTSGRTIGRGEWrsRVSGLPEIAGeLPVNVLA 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 232 H---RAAHGEVRAAYIMGEDPLQTDAELSAVRKAFEDLELVIVQGIFMTKTASAADVILPSTSWGEHE---GVFSAADRG 305
Cdd:cd02762 368 EeilTDGPGRIRAMIVVAGNPVLSAPDGARLEAALGGLEFMVSVDVYMTETTRHADYILPPASQLEKPhatFFNLEFPRN 447
|
330 340
....*....|....*....|....*....
gi 879957582 306 FQRFFKA-VEPKWDLKTDWQIISEIATRM 333
Cdd:cd02762 448 AFRYRRPlFPPPPGTLPEWEILARLVEAL 476
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
8-334 |
2.30e-47 |
|
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: 171.33 E-value: 2.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 8 IDNTDLVFVFGYNPADS-HPIVANHVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAMGHVIIEENLYDK 86
Cdd:cd02755 154 FENARYIILFGRNLAEAiIVVDARRLMKALENGAKVVVVDPRFSELASKADEWIPIKPGTDLAFVLALIHVLISENLYDA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 87 AFVASRTEGFEEYSKIVEGYTPESVEEITGVSAQEIRQAARMYASAKSAAILWGMGVTQFY-QGVETVRSLTSLAMLTGN 165
Cdd:cd02755 234 AFVEKYTNGFELLKAHVKPYTPEWAAQITDIPADTIRRIAREFAAAAPHAVVDPGWRGTFYsNSFQTRRAIAIINALLGN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 166 LGKPsagvnpvrgqnnvqGACDMGALPDTYPgyqyvkfpenrekfakawgveslpahtgyriselphraahgeVRAAYIM 245
Cdd:cd02755 314 IDKR--------------GGLYYAGSAKPYP------------------------------------------IKALFIY 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 246 GEDPLQTDAELSAVRKAFEDLELVIVQGIFMTKTASAADVILPSTSWGEHEGVFS----AADRGFQRfFKAVEPKWDLKT 321
Cdd:cd02755 338 RTNPFHSMPDRARLIKALKNLDLVVAIDILPSDTALYADVILPEATYLERDEPFSdkggPAPAVATR-QRAIEPLYDTRP 416
|
330
....*....|...
gi 879957582 322 DWQIISEIATRMG 334
Cdd:cd02755 417 GWDILKELARRLG 429
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
35-496 |
2.19e-46 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 173.70 E-value: 2.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 35 AKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAMGHVIIEENLYDKAFVASRTEGFEEYSKIVEGYTPESVEEI 114
Cdd:PRK15488 223 QMEKGAKLVVFEPRFSVVASKADEWHAIRPGTDLAVVLALCHVLIEENLYDKAFVERYTSGFEELAASVKEYTPEWAEAI 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 115 TGVSAQEIRQAARMYASAKSAAIL-WGMGVTQFYQGVETVRSLTSLAMLTGN--------LGKPSAGVNPVRGQNNVQGA 185
Cdd:PRK15488 303 SDVPADDIRRIARELAAAAPHAIVdFGHRATFTPEEFDMRRAIFAANVLLGNierkgglyFGKNASVYNKLAGEKVAPTL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 186 CDMGalPDTYPGYQYVKFPENREKFAKAWG----VESLPAHTgyrISELPHraahgEVRAAYIMGEDPLQTDAELSAVRK 261
Cdd:PRK15488 383 AKPG--VKGMPKPTAKRIDLVGEQFKYIAAgggvVQSIIDAT---LTQKPY-----QIKGWVMSRHNPMQTVTDRADVVK 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 262 AFEDLELVIVQGIFMTKTASAADVILPSTSWGEH-EGV--FSAADRGFQRFFKAVEPKWDLKTDWQIISEIATRMGYPMH 338
Cdd:PRK15488 453 ALKKLDLVVVCDVYLSESAAYADVVLPESTYLERdEEIsdKSGKNPAYALRQRVVEPIGDTKPSWQIFKELGEKMGLGQY 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 339 Y--NNTQEIwdELRHLCPDFygATYEKMGELGYIQW--PC--RDTSD-------------ADQGTSYLFKEKFDTPNGLA 399
Cdd:PRK15488 533 YpwQDMETL--QLYQVNGDH--ALLKELKKKGYVSFgvPLllREPKMvakfvarypnakaVDEDGTYGSQLKFKTPSGKI 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 400 QFFTCDWVA-----------PIDkLTEEYPMVL----STVREVGHyscrsmTGNCAALAAL-ADEPGYAQINTadAARLG 463
Cdd:PRK15488 609 ELFSAKLEAlapgygvpryrDVA-LKKEDELYFiqgkVAVHTNGA------TQNVPLLANLmSDNAVWIHPQT--AGKLG 679
|
490 500 510
....*....|....*....|....*....|....*
gi 879957582 464 IEDEALVWVHSRKGKIITRAQVSD--RPNKGAIYM 496
Cdd:PRK15488 680 IKNGDEIRLENSVGKEKGKALVTPgiRPDTLFAYM 714
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
415-531 |
3.82e-45 |
|
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: 154.97 E-value: 3.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 415 EEYPMVLSTVREVGHYSCRSMTGNCAALAALADEPgYAQINTADAARLGIEDEALVWVHSRKGKIITRAQVSDRPNKGAI 494
Cdd:cd00508 1 EEYPLVLTTGRLLEHWHTGTMTRRSPRLAALAPEP-FVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRPGTV 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 879957582 495 YMTYQWWI----GACNELVTENLSPITKTPEYKYCAVRVEP 531
Cdd:cd00508 80 FMPFHWGGevsgGAANALTNDALDPVSGQPEFKACAVRIEK 120
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
10-338 |
2.90e-41 |
|
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: 154.78 E-value: 2.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 10 NTDLVFVFGYNPADSHPIVANHVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAMGHVIIEENLYDKAFV 89
Cdd:cd02750 170 NADYIIMWGSNVPVTRTPDAHFLTEARYNGAKVVVVSPDYSPSAKHADLWVPIKPGTDAALALAMAHVIIKEKLYDEDYL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 90 asrtegfEEYSK---IVegYTPESVEEITGVSAQEIRQAARMYASAKSAAILWGMGVTQFYQGVETVRSLTSLAMLTGNL 166
Cdd:cd02750 250 -------KEYTDlpfLV--YTPAWQEAITGVPRETVIRLAREFATNGRSMIIVGAGINHWYHGDLCYRALILLLALTGNE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 167 GKPSAGVNpvrgqnnvqgacdmgalpdtypgyQYVkfpenrekfakawgveslpahtgyriselphraahGEVRAAYIMG 246
Cdd:cd02750 321 GKNGGGWA------------------------HYV-----------------------------------GQPRVLFVWR 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 247 EDPLQTDAELSAVRKA--FEDLELVIVQGIFMTKTASAADVILPSTSWGE-HEGVFSAADRGFQRFFKAVEPKWDLKTDW 323
Cdd:cd02750 342 GNLFGSSGKGHEYFEDapEGKLDLIVDLDFRMDSTALYSDIVLPAATWYEkHDLSTTDMHPFIHPFSPAVDPLWEAKSDW 421
|
330
....*....|....*
gi 879957582 324 QIISEIATRMGYPMH 338
Cdd:cd02750 422 EIFKALAKKVPWRTL 436
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
6-403 |
2.64e-39 |
|
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: 151.09 E-value: 2.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 6 NEID---NTDLVFVFGYNPADSHPIVANHVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAMGHVIIEEN 82
Cdd:cd02765 152 NEITdwvNAKTIIIWGSNILETQFQDAEFFLDARENGAKIVVIDPVYSTTAAKADQWVPIRPGTDPALALGMINYILEHN 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 83 LYDKAFVASRT------------------------------------------------EGFEEYSkiVEG--------- 105
Cdd:cd02765 232 WYDEAFLKSNTsapflvredngtllrqadvtatpaedgyvvwdtnsdspepvaatninpALEGEYT--INGvkvhtvlta 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 106 -------YTPESVEEITGVSAQEIRQAARMYASAKSAAILWGMGVTQFYQGVETVRSLTSLAMLTGNLGKPSAGvnpvrg 178
Cdd:cd02765 310 lreqaasYPPKAAAEICGLEEAIIETLAEWYATGKPSGIWGFGGVDRYYHSHVFGRTAAILAALTGNIGRVGGG------ 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 179 qnnvqgacdmgalpdtypgyqyvkfpenrekfakawgveslpahtgyriselphraaHGEVRAAYIMGEDPLQTDAELSA 258
Cdd:cd02765 384 ---------------------------------------------------------VGQIKFMYFMGSNFLGNQPDRDR 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 259 VRKAFEDLELVIVQGIFMTKTASAADVILPSTSWGEHEGVFSAADRGFQRFF--KAVEPKWDLKTDWQIISEIATRMGYP 336
Cdd:cd02765 407 WLKVMKNLDFIVVVDIFHTPTVRYADIVLPAAHWFEVEDLLVRYTTHPHVLLqqKAIEPLFESKSDFEIEKGLAERLGLG 486
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 879957582 337 MHYNNTQEiwDELRHLC----PDFYGATYEKMGELGYIQwpcRDTSDADQGTSYLfKEKFDTPNGLAQFFT 403
Cdd:cd02765 487 DYFPKTPE--DYVRAFMnsddPALDGITWEALKEEGIIM---RLATPEDPYVAYL-DQKFGTPSGKLEFYN 551
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
6-531 |
1.36e-38 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 151.20 E-value: 1.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 6 NEIDNTDLVFVFGYNPADSHPIVANHVINAK--RNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAMGHVIIEENL 83
Cdd:PRK13532 202 DDIEAADAFVLWGSNMAEMHPILWSRVTDRRlsNPDVKVAVLSTFEHRSFELADNGIIFTPQTDLAILNYIANYIIQNNA 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 84 YDKAFVASRTE----------------------------------GFEEYSKIVEGYTPESVEEITGVSAQEIRQAARMY 129
Cdd:PRK13532 282 VNWDFVNKHTNfrkgatdigyglrpthplekaaknpgtagksepiSFEEFKKFVAPYTLEKTAKMSGVPKEQLEQLAKLY 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 130 ASAKSAAI-LWGMGVTQFYQGVETVRSLTSLAMLTGNLGKPSAGVNPVRGQNNVQG-ACDMGALPDTYPGYQYVKFPENR 207
Cdd:PRK13532 362 ADPNRKVVsFWTMGFNQHTRGVWANNLVYNIHLLTGKISTPGNGPFSLTGQPSACGtAREVGTFSHRLPADMVVTNPKHR 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 208 EKFAKAWGVES--LPAHTGYRISELpHRAAH-GEVRAAYIMGEDPLQTDAELSAVR-KAFEDLE-LVIVQGIFMTKTASA 282
Cdd:PRK13532 442 EIAEKIWKLPEgtIPPKPGYHAVAQ-DRMLKdGKLNAYWVMCNNNMQAGPNINEERlPGWRNPDnFIVVSDPYPTVSALA 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 283 ADVILPSTSWGEHEGVFSAADRGFQRFFKAVEPKWDLKTD-WQIIsEIATRMgypmhynNTQEIW-DELRHLCPDFYGAT 360
Cdd:PRK13532 521 ADLILPTAMWVEKEGAYGNAERRTQFWRQQVKAPGEAKSDlWQLV-EFSKRF-------KTEEVWpEELLAKKPEYRGKT 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 361 -YE----------------KMGELG--------YIQ-------------------------------WPCRDTSDadqgT 384
Cdd:PRK13532 593 lYDvlfangqvdkfplselAEGYLNdeakhfgfYVQkglfeeyasfgrghghdlapfdtyhkvrglrWPVVDGKE----T 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 385 SYLFKEKFD-------------TPNGLAQFFTCDWVAPIDKLTEEYPMVLSTVREVGHYSCRSMTGNCAAL-AALADEPG 450
Cdd:PRK13532 669 LWRYREGYDpyvkagegfkfygKPDGKAVIFALPYEPPAESPDEEYDLWLSTGRVLEHWHTGSMTRRVPELyRAFPEAVC 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 451 YaqINTADAARLGIEDEALVWVHSRKGKIITRAQVS--DRPNKGAIYMTyqwWIGA---CNELVTENLSPITKTPEYKYC 525
Cdd:PRK13532 749 F--MHPEDAKARGLRRGDEVKVVSRRGEVKSRVETRgrNKPPRGLVFVP---FFDAaqlINKLTLDATDPLSKQTDFKKC 823
|
....*.
gi 879957582 526 AVRVEP 531
Cdd:PRK13532 824 AVKIEK 829
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
8-377 |
4.30e-36 |
|
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: 142.40 E-value: 4.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 8 IDNTDLVFVFGYNPADSHPI----VANHVI-----NAKRNGAKIIVCDPRKIETARIADM-HIALKNGSNIALLNAMGHV 77
Cdd:cd02769 168 AEHTELVVAFGADPLKNAQIawggIPDHQAysylkALKDRGIRFISISPLRDDTAAELGAeWIAIRPGTDVALMLALAHT 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 78 IIEENLYDKAFVASRTEGFEEYSKIVEGY------TPESVEEITGVSAQEIRQAARMYASaKSAAILWGMGVTQFYQGVE 151
Cdd:cd02769 248 LVTEGLHDKAFLARYTVGFDKFLPYLLGEsdgvpkTPEWAAAICGIPAETIRELARRFAS-KRTMIMAGWSLQRAHHGEQ 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 152 TVRSLTSLAMLTGNLGKPSAGVNPVRGQNNVQGACDMGALPDTYP-GYQYVK--FPENREkfakawgVESL--P----AH 222
Cdd:cd02769 327 PHWMAVTLAAMLGQIGLPGGGFGFGYHYSNGGGPPRGAAPPPALPqGRNPVSsfIPVARI-------ADMLlnPgkpfDY 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 223 TGYRIsELPHraahgeVRAAYIMGEDPLQTDAELSAVRKAFEDLELVIVQGIFMTKTASAADVILPSTSWGEHEGV-FSA 301
Cdd:cd02769 400 NGKKL-TYPD------IKLVYWAGGNPFHHHQDLNRLIRAWQKPETVIVHEPFWTATARHADIVLPATTSLERNDIgGSG 472
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 879957582 302 ADRGFQRFFKAVEPKWDLKTDWQIISEIATRMGYPMHYNNTQEIWDELRHlcpdFYGATYEKMGELGyIQWPCRDT 377
Cdd:cd02769 473 DNRYIVAMKQVVEPVGEARDDYDIFADLAERLGVEEQFTEGRDEMEWLRH----LYEESRAQAAARG-VEMPSFDE 543
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
3-532 |
4.28e-35 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 140.93 E-value: 4.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 3 NAINEIDNTDLVFVFGYNPAD---SHPIVANHVINAK-RNGAKIIVCDPRKIET-ARIADMHIALKNGSNIALLNAMGHV 77
Cdd:PRK14990 224 NSPSDIENSKLVVLFGNNPGEtrmSGGGVTYYLEQARqKSNARMIIIDPRYTDTgAGREDEWIPIRPGTDAALVNGLAYV 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 78 IIEENLYDKAFVASRTEGFEE------------YSKIVEGY-------TPESVEEITGVSAQEIRQAARMYASAKSAAIL 138
Cdd:PRK14990 304 MITENLVDQPFLDKYCVGYDEktlpasapknghYKAYILGEgpdgvakTPEWASQITGVPADKIIKLAREIGSTKPAFIS 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 139 WGMGVTQFYQGVETVRSLTSLAMLTGNLGkpsagvnpVRGQNNvqgacdmGALPDTYpGYQYVKFP--ENREKFAKA--- 213
Cdd:PRK14990 384 QGWGPQRHANGEIATRAISMLAILTGNVG--------INGGNS-------GAREGSY-SLPFVRMPtlENPIQTSISmfm 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 214 W--GVESLPAHTGYRISELPHRAAHGEVRAAY-IMGEDPLQTDAELSAVRKAFED---LELVIVQGIFMTKTASAADVIL 287
Cdd:PRK14990 448 WtdAIERGPEMTALRDGVRGKDKLDVPIKMIWnYAGNCLINQHSEINRTHEILQDdkkCELIVVIDCHMTSSAKYADILL 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 288 PSTSWGEHEGVFSAADRGFQRFF----KAVEPKWDLKTDWQIISEIATRMGYPMHYNN--TQEIWdeLRHL--------- 352
Cdd:PRK14990 528 PDCTASEQMDFALDASCGNMSYVifndQVIKPRFECKTIYEMTSELAKRLGVEQQFTEgrTQEEW--MRHLyaqsreaip 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 353 -CPDFygATYEKMGelgyiQWPCRDTsdadQGTSYLFKE--------KFDTPNGLAQFFTCD-------WVAP------- 409
Cdd:PRK14990 606 eLPTF--EEFRKQG-----IFKKRDP----QGHHVAYKAfredpqanPLTTPSGKIEIYSQAladiaatWELPegdvidp 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 410 -----------IDKLTEEYPMVLSTVrevgHYSCR--SMTGNCAALAALADEPGYaqINTADAARLGIEDEALVWVHSRK 476
Cdd:PRK14990 675 lpiytpgfesyQDPLNKQYPLQLTGF----HYKSRvhSTYGNVDVLKAACRQEMW--INPLDAQKRGINNGDKVRIFNDR 748
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 879957582 477 GKIITRAQVSDRPNKGAIYMTYQWWI----------GACNELVTENLSPITKTPEYKYCAVRVEPI 532
Cdd:PRK14990 749 GEVHIEAKVTPRMMPGVVALGEGAWYdpdakrvdkgGCINVLTTQRPSPLAKGNPSHTNLVQVEKV 814
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
415-532 |
7.31e-30 |
|
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: 113.44 E-value: 7.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 415 EEYPMVLSTVREVGHYSCRSMTGNCAALAALADEPgYAQINTADAARLGIEDEALVWVHSRKGKIITRAQVSDRPNKGAI 494
Cdd:cd02791 1 AEYPLWLNTGRVRDQWHTMTRTGRVPRLNAHVPEP-YVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPGEV 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 879957582 495 YMTYQW--WI---GACNELVTENLSPITKTPEYKYCAVRVEPI 532
Cdd:cd02791 80 FVPMHWgdQFgrsGRVNALTLDATDPVSGQPEFKHCAVRIEKV 122
|
|
| 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 ... |
1-334 |
1.41e-29 |
|
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: 121.73 E-value: 1.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 1 MSNAINEIDNTDLVFVFGYNPADSHPIVANHVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAMGHVIIE 80
Cdd:cd02771 136 YIPSLRDIESADAVLVLGEDLTQTAPRIALALRQAARRKAVELAALSGIPKWQDAAVRNIAQGAKSPLFIVNALATRLDD 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 81 enLYDKAFVASRTEGFEEYSKIVEGYTPESVEEITGVSAQEIRQAARMYASAKSAAILWGMGVtqfyQGVETVRSLTSLA 160
Cdd:cd02771 216 --IAAESIRASPGGQARLGAALARAVDASAAGVSGLAPKEKAARIAARLTGAKKPLIVSGTLS----GSLELIKAAANLA 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 161 MLTGNLGKpSAGVNPVRGQNNVQGACDMGALPDtypgyqyvkfpenrEKFAKAWGVEslpahtgyriselpHRAAHGEVR 240
Cdd:cd02771 290 KALKRRGE-NAGLTLAVEEGNSPGLLLLGGHVT--------------EPGLDLDGAL--------------AALEDGSAD 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 241 AAYIMGEDPLQTdAELSAVRKAFEDLELVIVQGIFMTKTASAADVILPSTSWGEHEGVFSAADRGFQRFFKAV-EPKWDL 319
Cdd:cd02771 341 ALIVLGNDLYRS-APERRVEAALDAAEFVVVLDHFLTETAERADVVLPAASFAEKSGTFVNYEGRAQRFFKAYdDPAGDA 419
|
330
....*....|....*
gi 879957582 320 KTDWQIISEIATRMG 334
Cdd:cd02771 420 RSDWRWLHALAAKLG 434
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
419-526 |
3.84e-29 |
|
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: 111.21 E-value: 3.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 419 MVLSTVREVGHYSCRSMTGNCAALAAlaDEPGYAQINTADAARLGIEDEALVWVHSRKGKIITRAQVSDRPNKGAIYMTY 498
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAK--PEPEVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPF 78
|
90 100 110
....*....|....*....|....*....|..
gi 879957582 499 QWW----IGACNELVTENLSPITKTPEYKYCA 526
Cdd:pfam01568 79 GWWyeprGGNANALTDDATDPLSGGPEFKTCA 110
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
5-184 |
3.32e-27 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 116.68 E-value: 3.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 5 INEIDNTDLVFVFGYNPADSHPIVANHVINAKRNGAKIIVCDP---RKIE--TA-------------RIADMHIALKNGS 66
Cdd:PRK09939 203 LEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPlqeRGLErfTApqnpfemltnsetQLASAYYNVRIGG 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 67 NIALLNAMGHVIIEEN----------LYDKAFVASRTEGFEEYSKIVEGYTPESVEEITGVSAQEIRQAARMYASAKSAA 136
Cdd:PRK09939 283 DMALLKGMMRLLIERDdaasaagrpsLLDDEFIQTHTVGFDELRRDVLNSEWKDIERISGLSQTQIAELADAYAAAERTI 362
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 879957582 137 ILWGMGVTQFYQGVETVRSLTSLAMLTGNLGKPSAGVNPVRGQNNVQG 184
Cdd:PRK09939 363 ICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQG 410
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
415-531 |
2.90e-26 |
|
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: 103.46 E-value: 2.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 415 EEYPMVLSTVREVGHYSCRSMTGNCAALAALADEPgYAQINTADAARLGIEDEALVWVHSRKGKIITRAQVSDRPNKGAI 494
Cdd:cd02792 1 EEFPLVLTTGRLTEHFHGGNMTRNSPYLAELQPEM-FVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHEV 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 879957582 495 YMTYQW-WIG-----ACNELVTENLSPITKTPEYKYCAVRVEP 531
Cdd:cd02792 80 GIPYHWgGMGlvigdSANTLTPYVGDPNTQTPEYKAFLVNIEK 122
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
41-494 |
3.56e-26 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 113.61 E-value: 3.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 41 KIIVCDPRKIETAR-IADMHIALKNGSNIALLNAMGHVIIEENLYDKAFVASRTEGFEEYSKIVEG------YTPESVEE 113
Cdd:PRK15102 256 NVISIDPVVTKTQNyLGCEHLYVNPQTDVPLMLALAHTLYSENLYDKKFIDNYCLGFEQFLPYLLGekdgvpKTPEWAEK 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 114 ITGVSAQEIRQAARMYASAKSaAILWGMGVTQFYQGVETVRSLTSLAMLTGNLGKPSAGVNPVRGQNNV----QGACDMG 189
Cdd:PRK15102 336 ICGIDAETIRELARQMAKGRT-QIIAGWCIQRQQHGEQPYWMGAVLAAMLGQIGLPGGGISYGHHYSGIgvpsSGGAIPG 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 190 ALPDTYPGYQYVKFPENREKFAKA------WgVESLpAHTGYRISELPHRAAHGEVRAAYIMGEDPLQTDAELSAVRKAF 263
Cdd:PRK15102 415 GFPGNLDTGQKPKHDNSDYKGYSStipvarF-IDAI-LEPGKTINWNGKKVTLPPLKMMIFSGTNPWHRHQDRNRMKEAF 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 264 EDLELVIVQGIFMTKTASAADVILPSTSWGEH---EGVFSAADRGFQRFFKAVEPKWDLKTDWQIISEIATRMGYPMHYN 340
Cdd:PRK15102 493 RKLETVVAIDNQWTATCRFADIVLPACTQFERndiDQYGSYSNRGIIAMKKVVEPLFESRSDFDIFRELCRRFGREKEYT 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 341 NTQEIWDELRHLCPD--------FYGATYEKMGELGYIQWPcrdtsdadQGTSYL----FKEKFD-----TPNGLAQFFT 403
Cdd:PRK15102 573 RGMDEMGWLKRLYQEckqqnkgkFHMPEFDEFWKKGYVEFG--------EGQPWVrhadFREDPElnplgTPSGLIEIYS 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 404 ----------CD----WVAPIDKL-----TEEYPMVLSTVrevgHYSCRSMTGNC------AALAALADEPGYaqINTAD 458
Cdd:PRK15102 645 rkiadmgyddCQghpmWFEKIERShggpgSDKYPLWLQSV----HPDKRLHSQLCeseelrETYTVQGREPVY--INPQD 718
|
490 500 510
....*....|....*....|....*....|....*.
gi 879957582 459 AARLGIEDEALVWVHSRKGKIITRAQVSDRPNKGAI 494
Cdd:PRK15102 719 AKARGIKDGDVVRVFNDRGQVLAGAVVSDRYPPGVI 754
|
|
| FwdB |
COG1029 |
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion]; |
12-333 |
1.74e-25 |
|
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion];
Pssm-ID: 440652 [Multi-domain] Cd Length: 428 Bit Score: 109.17 E-value: 1.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 12 DLVFVFGYNPADSHPivaNH----VINAK-------RNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAMghviie 80
Cdd:COG1029 141 DVIIYWGCNPVHAHP---RHmsrySVFPRgfftpkgRKDRTVIVVDPRPTDTAKVADLHLQVKPGRDYEVLSAL------ 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 81 enlydkafvasRTegfeeyskIVEGYTPeSVEEITGVSAQEIRQAARMYASAKSAAILWGMGVTQFYQGVETVRSLTSLA 160
Cdd:COG1029 212 -----------RA--------LVRGKEL-SPEEVAGIPVEDLEELAERLKNAKYGVIFWGMGLTQSPGKHLNVDAAIELV 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 161 MLTGNLGKPSAGvnPVRGQNNVQGAcdmGALPDTYPGYQYvkfpenREKFAKAWGVESlPAHTGyrISELphrAAHGEVR 240
Cdd:COG1029 272 RDLNRYTKFSIL--PLRGHYNVAGA---NQVASWQTGYPF------RVDFSRGYPRYN-PGETS--AVDL---LARGEVD 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 241 AAYIMGEDPLqtdAELSavRKAFEDLEL--VIVQGIFMTKTASAADVILPSTSWG-EHEGVFSAADRGFQRFFKAVEPkw 317
Cdd:COG1029 335 ALLWVASDPG---AHFP--PDAVEHLAKipTIVIDPHGTPTTEVADVVIPVAIPGiEHGGTAYRMDNVPLPLRKLRDS-- 407
|
330
....*....|....*.
gi 879957582 318 DLKTDWQIISEIATRM 333
Cdd:COG1029 408 PLPSDEEVLKAIEERV 423
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
9-406 |
7.11e-25 |
|
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: 108.30 E-value: 7.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 9 DNTDLVFVFGYNP-ADSHPI-VANHVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAMGHVIIEENLYDK 86
Cdd:cd02757 161 ANAKYILFFGADPlESNRQNpHAQRIWGGKMDQAKVVVVDPRLSNTAAKADEWLPIKPGEDGALALAIAHVILTEGLWDK 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 87 AFVASRTEG--------------FEEYS--KIVE-------GYTPESVEEITGVSAQEIRQAARMYASAKSAAILW-GMG 142
Cdd:cd02757 241 DFVGDFVDGknyfkagetvdeesFKEKSteGLVKwwnlelkDYTPEWAAKISGIPAETIERVAREFATAAPAAAAFtWRG 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 143 VTQFYQGVETVRSLTSLAMLTGNLGKPsAGVNPVRGQNNVqgacdmgalpDTYPGYQYvkfpenrekfakawgveslpah 222
Cdd:cd02757 321 ATMQNRGSYNSMACHALNGLVGSIDSK-GGLCPNMGVPKI----------KVYFTYLD---------------------- 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 223 tgyriselphraahgevraayimgeDPLQTDAELSAVRKAFEDLELVIVQGIFMTKTASAADVILPSTSWGEHEGVFSAA 302
Cdd:cd02757 368 -------------------------NPVFSNPDGMSWEEALAKIPFHVHLSPFMSETTYFADIVLPDGHHFERWDVMSQE 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 303 DRG-----FQRffKAVEPKWDLKTDWQIISEIATRMGYPMHYNntqeIWDelrhlcpdfygatyekmgelgYIQWPCRDT 377
Cdd:cd02757 423 NNLhpwlsIRQ--PVVKSLGEVREETEILIELAKKLDPKGSDG----MKR---------------------YAPGQFKDP 475
|
410 420
....*....|....*....|....*....
gi 879957582 378 SDADQGtSYLFKEKFDTPNGLAQFFTCDW 406
Cdd:cd02757 476 ETGKNN-RWEFENVFPTETGKFEFYSETL 503
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
234-355 |
5.30e-24 |
|
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440657 [Multi-domain] Cd Length: 453 Bit Score: 104.92 E-value: 5.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 234 AAHGEVRAAYIMGEDPLQTDAElsAVRKAFEDLELVIVQGIFMTKTASAADVILPSTSWGEHEGVFSAADRGFQRFFKAV 313
Cdd:COG1034 328 AEAGKLKALVLLGADPYDLDPA--AALAALAKADFVVVLDHFGSATAERADVVLPAAAFAEKSGTFVNLEGRVQRFNAAV 405
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 879957582 314 EPKWDLKTDWQIISEIATRMGYPMHYNNTQEIWDELRHLCPD 355
Cdd:COG1034 406 PPPGEARPDWRVLRALANALGAGLPYDSLEEVRAELAAEAPA 447
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
40-333 |
7.15e-22 |
|
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: 99.86 E-value: 7.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 40 AKIIVCDPRKIETARIAD--------MHIALKNGSNIALLNAMGHVIIEENlydkafvasrTEGFEEyskivegytpesV 111
Cdd:cd02756 271 GRIIVVDPRRTETVHAAEaaagkdrvLHLQVNPGTDTALANAIARYIYESL----------DEVLAE------------A 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 112 EEITGVSAQEIRQAARMYASAKSAA------------ILWGMgvtQFYQgveTVRSLTSLAMLTGNLGKPSAGVnpVRGQ 179
Cdd:cd02756 329 EQITGVPRAQIEKAADWIAKPKEGGyrkrvmfeyekgIIWGN---DNYR---PIYSLVNLAIITGNIGRPGTGC--VRQG 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 180 NNVQGACDMGALPD-TYPGYQYvkfpenrekfakawgveslPAHTGYRISElphraahGEVRAAYIMGEDPLQT------ 252
Cdd:cd02756 401 GHQEGYVRPPPPPPpWYPQYQY-------------------APYIDQLLIS-------GKGKVLWVIGCDPYKTtpnaqr 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 253 ----------------DAELSAV---RKAFEDLEL---------VIVQGIFMTKTASAADVILPSTSWGE-HEGVFSAAD 303
Cdd:cd02756 455 lretinhrsklvtdavEAALYAGtydREAMVCLIGdaiqpgglfIVVQDIYPTKLAEDAHVILPAAANGEmNETSMNGHE 534
|
330 340 350
....*....|....*....|....*....|
gi 879957582 304 RGFQRFFKAVEPKWDLKTDWQIISEIATRM 333
Cdd:cd02756 535 RRLRLYEKFMDPPGEAMPDWWIAAMIANRI 564
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
429-523 |
8.05e-21 |
|
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site. This hierarchy is of the conserved MopB_CT domain present in many, but not all, MopB homologs.
Pssm-ID: 239176 [Multi-domain] Cd Length: 101 Bit Score: 87.38 E-value: 8.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 429 HYSCRSMTGNcAALAALADEPgYAQINTADAARLGIEDEALVWVHSRKGKIITRAQVSDRPNKGAIYMTYQWW-----IG 503
Cdd:cd02775 4 HFHSGTRTRN-PWLRELAPEP-VVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGhrggrGG 81
|
90 100
....*....|....*....|
gi 879957582 504 ACNELVTENLSPITKTPEYK 523
Cdd:cd02775 82 NANVLTPDALDPPSGGPAYK 101
|
|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
9-332 |
5.89e-20 |
|
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: 92.40 E-value: 5.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 9 DNTDLVFVFGYNPADSHP-IVANHVINAK-------RNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAMGHVIIE 80
Cdd:cd02761 130 NRADVIVYWGTNPMHAHPrHMSRYSVFPRgffreggREDRTLIVVDPRKSDTAKLADIHLQIDPGSDYELLAALRALLRG 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 81 ENLydkafvasrtegfeeyskivegytpeSVEEITGVSAQEIRQAARMYASAKSAAILWGMGVTQFYQGvetVRSLTSLA 160
Cdd:cd02761 210 AGL--------------------------VPDEVAGIPAETILELAERLKNAKFGVIFWGLGLLPSRGA---HRNIEAAI 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 161 MLTGNLGKPS-AGVNPVRGQNNVQGACDMGALPDTYPgyqyvkfpeNREKFAKAWGVESlPAHTGYriSELphrAAHGEV 239
Cdd:cd02761 261 RLVKALNEYTkFALLPLRGHYNVRGFNQVLTWLTGYP---------FRVDFSRGYPRYN-PGEFTA--VDL---LAEGEA 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 240 RAAYIMGEDPLqtdaeLSAVRKAFEDLE--LVIVQGIFMTKTASAADVILPSTSWG-EHEGVFSAADRGFQRFFKAVEPk 316
Cdd:cd02761 326 DALLIIASDPP-----AHFPQSAVKHLAeiPVIVIDPPPTPTTRVADVVIPVAIPGiEAGGTAYRMDGVVVLPLKAVET- 399
|
330
....*....|....*.
gi 879957582 317 wDLKTDWQIISEIATR 332
Cdd:cd02761 400 -ERLPDEEILKQLLEK 414
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
1-333 |
4.63e-17 |
|
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: 83.10 E-value: 4.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 1 MSNAINEIDNTDLVFVFGYNPADSHPIVANHVINAkrngakiivcdprkietariadmhiALKNGSNIALLNAMGHVIIE 80
Cdd:cd02768 139 FNTSIAEIEEADAVLLIGSNLRKEAPLLNARLRKA-------------------------VKKKGAKIAVIGPKDTDLIA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 81 ENLYDKAFVasrtegfeeyskiveGYTPESVEEItgVSAQEIRQAARMYASAKSAAILWGMGVTQFYQGvetvRSLTSLA 160
Cdd:cd02768 194 DLTYPVSPL---------------GASLATLLDI--AEGKHLKPFAKSLKKAKKPLIILGSSALRKDGA----AILKALA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 161 MLTGNLGKPSAGVNPVRGQNNVqGACDMGALpdtypgyqyvkfpeNREKFAkawgveslpahtgyriselphrAAHGEVR 240
Cdd:cd02768 253 NLAAKLGTGAGLWNGLNVLNSV-GARLGGAG--------------LDAGLA----------------------LLEPGKA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 241 AAYIMGEDPLQTDAELSAVrkAFEDLELVIVQGIFMTKTASAADVILPSTSWGEHEGVFSAADRGFQRFFKAVEPKWDLK 320
Cdd:cd02768 296 KLLLLGEDELDRSNPPAAV--ALAAADAFVVYQGHHGDTGAQADVILPAAAFTEKSGTYVNTEGRVQRFKKAVSPPGDAR 373
|
330
....*....|...
gi 879957582 321 TDWQIISEIATRM 333
Cdd:cd02768 374 EDWKILRALSNLL 386
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
7-336 |
5.00e-16 |
|
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: 81.42 E-value: 5.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 7 EIDNTDLVFVFGY-NPADSHPIVANhVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAMGHVIIEENLYD 85
Cdd:cd02763 152 DLEHTKYFMMIGVaEDHHSNPFKIG-IQKLKRRGGKFVAVNPVRTGYAAIADEWVPIKPGTDGAFILALAHELLKAGLID 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 86 KAFVASRTEGFEEYSkivegYTPESVEEITGVSAQEIRQ-AARMYASAKSAAI--------LWGM--------------- 141
Cdd:cd02763 231 WEFLKRYTNAAELVD-----YTPEWVEKITGIPADTIRRiAKELGVTARDQPIelpiawtdVWGRkhekitgrpvsfham 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 142 -GVTQFYQGVETVRSLTSLAMLTGNLGKPSA---------GVNPVRGQNNVQGACDMGALPDTYPgYQYVKFPE------ 205
Cdd:cd02763 306 rGIAAHSNGFQTIRALFVLMMLLGTIDRPGGfrhkppyprHIPPLPKPPKIPSADKPFTPLYGPP-LGWPASPDdllvde 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 206 --NREKFAKAWGVEslpahtgYRISelPHRAAHGEVRAAYimGEDPLQTDAEL--------------SAVRKAFED---- 265
Cdd:cd02763 385 dgNPLRIDKAYSWE-------YPLA--AHGCMQNVITNAW--RGDPYPIDTLMiymanmawnssmntPEVREMLTDkdas 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 266 ----LELVIVQGIFMTKTASAADVILPSTSWGEHEGVFSAADRGFQRF--------FKAVEPKWDLKTDWQIISEIATRM 333
Cdd:cd02763 454 gnykIPFIIVCDAFYSEMVAFADLVLPDTTYLERHDAMSLLDRPISEAdgpvdairVPIVEPKGDVKPFQEVLIELGTRL 533
|
...
gi 879957582 334 GYP 336
Cdd:cd02763 534 GLP 536
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
416-516 |
1.03e-10 |
|
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: 59.63 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 416 EYPMVLSTVREVGhYSCRSMTGNCAALAALADEPgYAQINTADAARLGIEDEALVWVHSRKGKIITRAQVSDRPNKGAIY 495
Cdd:cd02781 1 EYPLILTTGARSY-YYFHSEHRQLPSLRELHPDP-VAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVR 78
|
90 100
....*....|....*....|.
gi 879957582 496 MTYQWWiGACNELVTENLSPI 516
Cdd:cd02781 79 AEHGWW-YPEREAGEPALGGV 98
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
7-336 |
9.83e-09 |
|
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: 58.12 E-value: 9.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 7 EIDNTDLVFVFGYNPADSHP---IVANHVINAK-RNGAKIIVCDPRKIETARIADMH---IALKNGSNIALLNAMGHVII 79
Cdd:cd02758 208 DFDNAEFALFIGTSPAQAGNpfkRQARRLAEARtEGNFKYVVVDPVLPNTTSAAGENirwVPIKPGGDGALAMAMIRWII 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 80 EENLYDKAFVAS------RTEGFEEYS-------------------KIVEGYTPESVEEITGVSAQEIRQAARMYASAKS 134
Cdd:cd02758 288 ENERYNAEYLSIpskeaaKAAGEPSWTnathlvitvrvksalqllkEEAFSYSLEEYAEICGVPEAKIIELAKEFTSHGR 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 135 AAILWGMGVTQFYQGVETVRSLTSLAMLTGNLgkpsagvnpvrgqnNVQGACDMGALPDTYPGYQY----VKFPE----- 205
Cdd:cd02758 368 AAAVVHHGGTMHSNGFYNAYAIRMLNALIGNL--------------NWKGGLLMSGGGFADNSAGPrydfKKFFGevkpw 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 206 ----NREKFA----------KAWGVESLPA------HTGYRISELPHRAAHG---------EVRAAYIMGEDPLQTDAEl 256
Cdd:cd02758 434 gvpiDRSKKAyektseykrkVAAGENPYPAkrpwypLTPELYTEVIASAAEGypyklkaliLWMANPVYGAPGLVKQVE- 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 257 sAVRKAFEDLELVIVQGIFMTKTASAADVILPST----SWG---EHEGVFSAAD--RgfqrfFKAVEPKWDLKTD----- 322
Cdd:cd02758 513 -EKLKDPKKLPLFIAIDAFINETSAYADYIVPDTtyyeSWGfstPWGGVPTKAStaR-----WPVIAPLTEKTANghpvs 586
|
410
....*....|....*
gi 879957582 323 -WQIISEIATRMGYP 336
Cdd:cd02758 587 mESFLIDLAKALGLP 601
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
184-334 |
1.14e-08 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 58.03 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 184 GACDMGALPDTYPGYQYVKFPENREKFAKAWGVESLPAHTGYRISELPHRAAHGEVRAAYIMGEDPlqtdAEL---SAVR 260
Cdd:PRK07860 498 GALEAGALPTLLPGGRPVADPAARAEVAAAWGVDELPAAPGRDTAGILAAAAAGELGALLVGGVEP----ADLpdpAAAL 573
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 879957582 261 KAFEDLELVIVQGIFMTKTASAADVILPSTSWGEHEGVFSAADrGFQRFFKAVEPKWDLKTDWQIISEIATRMG 334
Cdd:PRK07860 574 AALDAAGFVVSLELRHSAVTERADVVLPVAPVAEKAGTFLNWE-GRLRPFEAALRTTGALSDLRVLDALADEMG 646
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
417-529 |
2.50e-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: 49.59 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 417 YPMVLSTVRevGHYSCRSMTGNCAALAALADEPgYAQINTADAARLGIEDEALVWVHSRKGKIITRAQVSDRPNKGAIYM 496
Cdd:cd02786 1 YPLRLITPP--AHNFLNSTFANLPELRAKEGEP-TLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVVVA 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 879957582 497 TYQWWI------GACNELVTENLSPITKTPEYKYCAVRV 529
Cdd:cd02786 78 EGGWWRehspdgRGVNALTSARLTDLGGGSTFHDTRVEV 116
|
|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
451-523 |
2.47e-06 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase (Arsenite-Ox) and related proteins. Arsenite oxidase oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin.
Pssm-ID: 239180 [Multi-domain] Cd Length: 115 Bit Score: 46.68 E-value: 2.47e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 879957582 451 YAQINTADAARLGIEDEALVWVHSRKGKIITRAQVSDRPNKGAIYMTYQWWIGACNELVTENLSPITKTPEYK 523
Cdd:cd02779 34 YIEVNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKPGQTFMLMAHPRPGANGLVTPYVDPETIIPYYK 106
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
454-530 |
4.87e-06 |
|
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase (DMSOR) of Escherichia coli and other related DMSOR-like enzymes. Unlike other DMSOR-like enzymes, this group has a predicted N-terminal iron-sulfur [4Fe-4S] cluster binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239195 [Multi-domain] Cd Length: 121 Bit Score: 45.75 E-value: 4.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 454 INTADAARLGIEDEALVWVHSRKGKIITRAQVSDRPNKGAIYMTYQWWI----------GACNELVTENLSPITKTPEYK 523
Cdd:cd02794 34 INPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVVALPQGAWYepdangidkgGCINTLTGLRPSPLAKGNPQH 113
|
....*..
gi 879957582 524 YCAVRVE 530
Cdd:cd02794 114 TNLVQVE 120
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
417-496 |
5.88e-06 |
|
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239178 [Multi-domain] Cd Length: 127 Bit Score: 45.65 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 417 YPMVLSTVrevgHYSCR--SMTGNCAALAALADEPGY--AQINTADAARLGIEDEALVWVHSRKGKIITRAQVSDRPNKG 492
Cdd:cd02777 1 YPLQLISP----HPKRRlhSQLDNVPWLREAYKVKGRepVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPG 76
|
....
gi 879957582 493 AIYM 496
Cdd:cd02777 77 VVAL 80
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
434-500 |
3.10e-05 |
|
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and other related proteins. Thiosulfate reductase catalyzes the cleavage of sulfur-sulfur bonds in thiosulfate. Polysulfide reductase is a membrane-bound enzyme that catalyzes the reduction of polysulfide using either hydrogen or formate as the electron donor. Also included in this CD is the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), which has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. The MopB_CT_Thiosulfate-R-like CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239179 [Multi-domain] Cd Length: 123 Bit Score: 43.42 E-value: 3.10e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 879957582 434 SMTGNCAALAALaDEPGYAQINTADAARLGIEDEALVWVHSRKGKIITRAQVSDRPNKGAIYMTYQW 500
Cdd:cd02778 15 GHTANNPLLHEL-TPENTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMPHGF 80
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
233-330 |
3.45e-05 |
|
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone oxidoreductase/respiratory complex I/NADH dehydrogenase-1(NDH-1) of eukaryotes and the Nqo3/G subunit of alphaproteobacteria NDH-1. The NADH-quinone oxidoreductase is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The nad11 gene codes for the largest (75 kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Paracoccus denitrificans, this subunit is encoded by the nqo3 gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The Nad11/Nqo3 subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239174 [Multi-domain] Cd Length: 375 Bit Score: 46.10 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 233 RAAHGEVRAAYIMGEDPLQTDAelsAVRKAFedlelVIVQGIFMTKTASAADVILPSTSWGEHEGVFSAADRGFQRFFKA 312
Cdd:cd02773 283 IRKSGPPKVLYLLGADEIDITP---IPKDAF-----VVYQGHHGDRGAQIADVILPGAAYTEKSGTYVNTEGRVQQTRKA 354
|
90
....*....|....*...
gi 879957582 313 VEPKWDLKTDWQIISEIA 330
Cdd:cd02773 355 VSPPGDAREDWKILRALS 372
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
450-531 |
6.62e-05 |
|
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: 42.76 E-value: 6.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 450 GYAQINTADAARLGIEDEALVWVHSRKGKIITRAQVSDRPNKGAIYMTYQWWIG-------------ACNELV-TENLSP 515
Cdd:cd02782 33 CTLRIHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMPGVVSLPHGWGHDypgvsgagsrpgvNVNDLTdDTQRDP 112
|
90
....*....|....*.
gi 879957582 516 ITKTPEYKYCAVRVEP 531
Cdd:cd02782 113 LSGNAAHNGVPVRLAR 128
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| NarG |
COG5013 |
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and ... |
35-101 |
8.23e-05 |
|
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 444037 [Multi-domain] Cd Length: 1231 Bit Score: 45.58 E-value: 8.23e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 879957582 35 AKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAMGHVIIEENlydkaFVASRTEGFEEYSK 101
Cdd:COG5013 274 ARYKGTKVVVVSPDYAENTKFADEWLPPKQGTDAALAMAMGHVILKEF-----HVDRQVPYFTDYAR 335
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| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
454-501 |
9.08e-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: 42.75 E-value: 9.08e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 879957582 454 INTADAARLGIEDEALVWVHSRKGKIITRAQVSDRPNKGAIYMtYQWW 501
Cdd:cd02776 35 MNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTVFM-YHAQ 81
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| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
417-485 |
3.16e-04 |
|
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: 41.13 E-value: 3.16e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 879957582 417 YPMVLSTVREVGHyscRSMTGNCAALAALADEpGYAQINTADAARLGIEDEALVWVHSRKGKIITRAQV 485
Cdd:cd02780 1 YPFILVTFKSNLN---SHRSANAPWLKEIKPE-NPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKV 65
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| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
448-496 |
3.47e-04 |
|
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO.This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239194 [Multi-domain] Cd Length: 129 Bit Score: 40.70 E-value: 3.47e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 879957582 448 EPgyAQINTADAARLGIEDEALVWVHSRKGKIITRAQVSDRPNKGAIYM 496
Cdd:cd02793 33 EP--IRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPGVVQL 79
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| MopB_CT_NDH-1_NuoG2-N7 |
cd02788 |
MopB_CT_NDH-1_NuoG2-N7: C-terminal region of the NuoG-like subunit (of the variant with a ... |
434-494 |
3.85e-04 |
|
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: 39.60 E-value: 3.85e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 879957582 434 SMTGNCAALAALADEPgYAQINTADAARLGIEDEALVWVHSRKGKIITRAQVSDRPNKGAI 494
Cdd:cd02788 14 ELSQRSPVIAERAPAP-YARLSPADAARLGLADGDLVEFSLGDGTLTLPVQISKYLPAGVV 73
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| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
94-341 |
5.96e-04 |
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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: 42.65 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 94 EGFEEYSKIVEG---YTPESVEEITGVSAQEIRQAARMYASAKS----------------AAILWGMGVTQFYQGVETVR 154
Cdd:cd02760 328 EGTTAFTMLVEHmrkYTPEWAESICDVPAATIRRIAREFLENASigstievdgvtlpyrpVAVTLGKSVNNGWGAFECCW 407
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 155 SLTSLAMLTGNLGKPSA--GVNPV--RGQNN----VQGACDMGALPDTYPGYQ--YVKFPENRE---KFAKAWGVESLPA 221
Cdd:cd02760 408 ARTLLATLVGALEVPGGtlGTTVRlnRPHDDrlasVKPGEDGFMAQGFNPTDKehWVVKPTGRNahrTLVPIVGNSAWSQ 487
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 222 HTGyriselPHRAAHGEVRAAYIMGEDPLQTDAEL-----SAVRKAFED----------LELVIVQGIFMTKTASAADVI 286
Cdd:cd02760 488 ALG------PTQLAWMFLREVPLDWKFELPTLPDVwfnyrTNPAISFWDtatlvdniakFPFTVSFAYTEDETNWMADVL 561
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250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 879957582 287 LPSTSWGE-------HEGVFSA---ADRGFQRFFKAVEPKWDLKTDWQIISEIATRMGYPMHYNN 341
Cdd:cd02760 562 LPEATDLEslqmikvGGTKFVEqfwEHRGVVLRQPAVEPQGEARDFTWISTELAKRTGLLADYNA 626
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| MopB_CT_ydeP |
cd02787 |
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial ... |
454-529 |
2.74e-03 |
|
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative 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: 239188 [Multi-domain] Cd Length: 112 Bit Score: 37.64 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 879957582 454 INTADAARLGIEDEALVWVHSRKGKIITRAQVSDRPN-----KGAIYMTYQwwigACNELVT-ENLSPITKTPEYKYCAV 527
Cdd:cd02787 35 MNPDDIARLGLKAGDRVDLESAFGDGQGRIVRGFRVVeydipRGCLAAYYP----EGNVLVPlDHRDPQSKTPAYKSVPV 110
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..
gi 879957582 528 RV 529
Cdd:cd02787 111 RL 112
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