|
Name |
Accession |
Description |
Interval |
E-value |
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
53-620 |
0e+00 |
|
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: 698.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 53 RNACPRNCYDTCSLKTWVKDDVITFVEGAPESTFTHGTPCVKGLSYPRRVYSPDRIKYPMVQDVRGSGNWRRISWDEAMQ 132
Cdd:cd02766 1 RSVCPLDCPDTCSLLVTVEDGRIVRVEGDPAHPYTRGFICAKGARYVERVYSPDRLLTPLKRVGRKGGQWERISWDEALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 133 RIATKMLEIKKKDGSmLGLALTKYSGKFGVLNYAVEGMMSSLGYTTRFAGTPCWPAGIDAQNYDMGDMWCNDPEDMVKAK 212
Cdd:cd02766 81 TIAAKLKEIKAEYGP-ESILPYSYAGTMGLLQRAARGRFFHALGASELRGTICSGAGIEAQKYDFGASLGNDPEDMVNAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 213 YIIIWGANPAWCSMHTMKYIYQAREKGAKVVVIDPLLTQTAAKADLYLRVRPGSDGALALGMARHLVDKGLVDQDFVNNY 292
Cdd:cd02766 160 LIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDPYRTATAARADLHIQIRPGTDGALALGVAKVLFREGLYDRDFLARH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 293 SHGYAEFEEYLRnNVTVEWASEICGLSADVIRQLAEEFTAVNPATVWIGYGMQRHVNGGANVRAIDAFVAMTGNIGIEGG 372
Cdd:cd02766 240 TEGFEELKAHLE-TYTPEWAAEITGVSAEEIEELARLYGEAKPPSIRLGYGMQRYRNGGQNVRAIDALPALTGNIGVPGG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 373 GARYGHLhtwgfnynamlqkpplgsigmpgaagttsefgsgeevaqysdrslninqtakgileanEPPVRMLWVACKNPF 452
Cdd:cd02766 319 GAFYSNS----------------------------------------------------------GPPVKALWVYNSNPV 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 453 AQDFDRSKMEK-AFEKLEMVVCADQFFNETVQHADIVLPVTTAFEEWNVDASYWHYWLSINQPAIKPMYEAKCDLEIAVL 531
Cdd:cd02766 341 AQAPDSNKVRKgLAREDLFVVVHDQFMTDTARYADIVLPATTFLEHEDVYASYWHYYLQYNEPAIPPPGEARSNTEIFRE 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 532 LSRTINKLEPgsctfPQEFDHKRWLDQEFNDGMAKMFGISSWDdllEGPKKAILPSSAAWYDRKFKTPSGKFEFKSELCE 611
Cdd:cd02766 421 LAKRLGFGEP-----PFEESDEEWLDQALDGTGLPLEGIDLER---LLGPRKAGFPLVAWEDRGFPTPSGKFEFYSERAA 492
|
....*....
gi 2524489867 612 KNGHTALPE 620
Cdd:cd02766 493 KRGLPPLPE 501
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
46-729 |
0e+00 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 611.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 46 PKTYKIYRNACPrNCYDTCSLKTWVKDDVITFVEGAPESTFTHGTPCVKGLSYPRRVYSPDRIKYPMVQD-VRGSGNWRR 124
Cdd:COG0243 18 AAGTKTVKTTCP-GCGVGCGLGVKVEDGRVVRVRGDPDHPVNRGRLCAKGAALDERLYSPDRLTYPMKRVgPRGSGKFER 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 125 ISWDEAMQRIATKMLEIKKKDGSMlGLALTKYSGKFGVLN----YAVEGMMSSLGYTTRFA-GTPCWPAGIDAQNYDMG- 198
Cdd:COG0243 97 ISWDEALDLIAEKLKAIIDEYGPE-AVAFYTSGGSAGRLSneaaYLAQRFARALGTNNLDDnSRLCHESAVAGLPRTFGs 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 199 DMWCNDPEDMVKAKYIIIWGANPAWCSMHTMKYIYQA-REKGAKVVVIDPLLTQTAAKADLYLRVRPGSDGALALGMARH 277
Cdd:COG0243 176 DKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREAaKKRGAKIVVIDPRRTETAAIADEWLPIRPGTDAALLLALAHV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 278 LVDKGLVDQDFVNNYSHGYAEFEEYLRnNVTVEWASEICGLSADVIRQLAEEFTAVNPATVWIGYGMQRHVNGGANVRAI 357
Cdd:COG0243 256 LIEEGLYDRDFLARHTVGFDELAAYVA-AYTPEWAAEITGVPAEDIRELAREFATAKPAVILWGMGLQQHSNGTQTVRAI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 358 DAFVAMTGNIGIEGGGARYGhlhtwgfnynamlqkpplgsigmpgaagttsefgsgeevaqysdrslninqTAKGILEAN 437
Cdd:COG0243 335 ANLALLTGNIGKPGGGPFSL---------------------------------------------------TGEAILDGK 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 438 EPPVRMLWVACKNPFAQDFDRSKMEKAFEKLEMVVCADQFFNETVQHADIVLPVTTAFEEWNVDASYWHYWLSINQPAIK 517
Cdd:COG0243 364 PYPIKALWVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARYADIVLPATTWLERDDIVTNSEDRRVHLSRPAVE 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 518 PMYEAKCDLEIAVLLSRTINKLEPgsctFPQEFDHKRWLDQEFNDGMAKMFgisSWDDLLE-GPKKAILPSSAAWY-DRK 595
Cdd:COG0243 444 PPGEARSDWEIFAELAKRLGFEEA----FPWGRTEEDYLRELLEATRGRGI---TFEELREkGPVQLPVPPEPAFRnDGP 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 596 FKTPSGKFEFKSELCEKNGH---TALPEYKPEAKSTLPFHLFTPHVQFGIHSQFINLDWMQVFYPEPFVYMHPVSAGKRG 672
Cdd:COG0243 517 FPTPSGKAEFYSETLALPPLpryAPPYEGAEPLDAEYPLRLITGRSRDQWHSTTYNNPRLREIGPRPVVEINPEDAAALG 596
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524489867 673 IAENDLVKVFNTAGEVELRAKVTANVPEDFLVMYEAW----FPKRKYNVQNVVADTPADMG 729
Cdd:COG0243 597 IKDGDLVRVESDRGEVLARAKVTEGIRPGVVFAPHGWwyepADDKGGNVNVLTPDATDPLS 657
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
53-534 |
4.67e-113 |
|
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: 347.01 E-value: 4.67e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 53 RNACPRnCYDTCSLKTWVKDDVITFVEGAPESTFTHGTPCVKGLSYPRRVYSPDRIKYPMVqDVRGSGNWRRISWDEAMQ 132
Cdd:cd00368 1 PSVCPF-CGVGCGILVYVKDGKVVRIEGDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLI-RVGGRGKFVPISWDEALD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 133 RIATKMLEIKKKDGSmLGLALTKYSGKFGVLNYAVEGMMSSLG-YTTRFAGTPCWPAGIDAQNYDMGDMWCNDPEDMVKA 211
Cdd:cd00368 79 EIAEKLKEIREKYGP-DAIAFYGGGGASNEEAYLLQKLLRALGsNNVDSHARLCHASAVAALKAFGGGAPTNTLADIENA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 212 KYIIIWGANPAWCSMHTMKYIYQAREKGAKVVVIDPLLTQTAAKADLYLRVRPGSDGALALGmarhlvdkglvdqdfvnn 291
Cdd:cd00368 158 DLILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRRTETAAKADEWLPIRPGTDAALALA------------------ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 292 yshgyaefeeylrnnvtvEWASEICGLSADVIRQLAEEFTAVNPATVWIGYGMQRHVNGGANVRAIDAFVAMTGNIGIEG 371
Cdd:cd00368 220 ------------------EWAAEITGVPAETIRALAREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 372 GGARYGHlhtwgfnynamlqkpplgsigmpgaagttsefgsgeevaqysdrslninqtakgileaneppvrmlwvackNP 451
Cdd:cd00368 282 GGLGPGG-----------------------------------------------------------------------NP 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 452 FAQDFDRSKMEKAFEKLEMVVCADQFFNETVQHADIVLPVTTAFEEWNVdASYWHYWLSINQPAIKPMYEAKCDLEIAVL 531
Cdd:cd00368 291 LVSAPDANRVRAALKKLDFVVVIDIFMTETAAYADVVLPAATYLEKEGT-YTNTEGRVQLFRQAVEPPGEARSDWEILRE 369
|
...
gi 2524489867 532 LSR 534
Cdd:cd00368 370 LAK 372
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
64-623 |
8.23e-113 |
|
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: 354.61 E-value: 8.23e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 64 CSLKTWVKDDVITFVEGAPEstfTHGTPCVKGLSYPRRVYSPDRIKYPMV-----------QDVRGSGNWRRISWDEAMQ 132
Cdd:cd02751 7 GPFKAHVKDGVIVRVEPDDT---DQPRPCPRGRSVRDRVYSPDRIKYPMKrvgwlgngpgsRELRGEGEFVRISWDEALD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 133 RIATKMLEIKKKDG--SMLGlalTKYSGKF-GVLNYA---VEGMMSSLGYTTRFAGTPCWPAGIDAQNYDMGDMW----C 202
Cdd:cd02751 84 LVASELKRIREKYGneAIFG---GSYGWASaGRLHHAqslLHRFLNLIGGYLGSYGTYSTGAAQVILPHVVGSDEvyeqG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 203 NDPEDMVK-AKYIIIWGANPAWCSM-------HTMKYIY-QAREKGAKVVVIDPLLTQTAA-KADLYLRVRPGSDGALAL 272
Cdd:cd02751 161 TSWDDIAEhSDLVVLFGANPLKTRQgggggpdHGSYYYLkQAKDAGVRFICIDPRYTDTAAvLAAEWIPIRPGTDVALML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 273 GMARHLVDKGLVDQDFVNNYSHGYAEFEEYLR---NNV--TVEWASEICGLSADVIRQLAEEFtAVNPATVWIGYGMQRH 347
Cdd:cd02751 241 AMAHTLITEDLHDQAFLARYTVGFDEFKDYLLgesDGVpkTPEWAAEITGVPAETIRALAREI-ASKRTMIAQGWGLQRA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 348 VNGGANVRAIDAFVAMTGNIGIEGGGARYGHlHTWGFNYNAMLqkpPLGSIGMPGAAGTTSEFGSgeeVAQYSDRSLNIN 427
Cdd:cd02751 320 HHGEQPAWMLVTLAAMLGQIGLPGGGFGFGY-GYSNGGGPPRG---GAGGPGLPQGKNPVKDSIP---VARIADALLNPG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 428 Q--TAKGILEANePPVRMLWVACKNPFAQDFDRSKMEKAFEKLEMVVCADQFFNETVQHADIVLPVTTAFEEWNVDAS-- 503
Cdd:cd02751 393 KefTANGKLKTY-PDIKMIYWAGGNPLHHHQDLNRLIKALRKDETIVVHDIFWTASARYADIVLPATTSLERNDIGLTgn 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 504 YWHYWLSINQPAIKPMYEAKCDLEIAVLLSRTINKLEpgscTFPQEFDHKRWLDQEFNDGMAKM----FGISSWDDLLE- 578
Cdd:cd02751 472 YSNRYLIAMKQAVEPLGEARSDYEIFAELAKRLGVEE----EFTEGRDEMEWLEHLYEETRAKAagpgPELPSFEEFWEk 547
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 2524489867 579 -GPKKAILPSSAAWYD--------RKFKTPSGKFEFKSELCEKNGHT---ALPEYKP 623
Cdd:cd02751 548 gIVRVPAAPKPFVAFAdfredpeaNPLGTPSGKIEIYSETLADFGYDdcpGHPTWIE 604
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
56-709 |
7.20e-111 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 351.88 E-value: 7.20e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 56 CPRnCYDTCSLKTWVKDDVITFVEGAPESTFTHGTPCVKGLSYPRRVYSPDRIKYPMVqdvRGSGNWRRISWDEAMQRIA 135
Cdd:COG3383 11 CPY-CGVGCGIDLEVKDGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVNSPDRLTTPLI---RRGGEFREVSWDEALDLVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 136 TKMLEIKKKDGS----MLGLA------------LTKysGKFGVLNY----------AVEGMMSSLGYTtrfAGTPCWpag 189
Cdd:COG3383 87 ERLREIQAEHGPdavaFYGSGqltneenyllqkLAR--GVLGTNNIdnnarlcmasAVAGLKQSFGSD---APPNSY--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 190 idaqnydmgdmwcndpEDMVKAKYIIIWGANPAWCsmH--TMKYIYQAREKGAKVVVIDPLLTQTAAKADLYLRVRPGSD 267
Cdd:COG3383 159 ----------------DDIEEADVILVIGSNPAEA--HpvLARRIKKAKKNGAKLIVVDPRRTETARLADLHLQIKPGTD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 268 GALALGMARHLVDKGLVDQDFVNNYSHGYAEFEEYLRnNVTVEWASEICGLSADVIRQLAEEFTAVNPATVWIGYGMQRH 347
Cdd:COG3383 221 LALLNGLLHVIIEEGLVDEDFIAERTEGFEELKASVA-KYTPERVAEITGVPAEDIREAARLIAEAKRAMILWGMGVNQH 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 348 VNGGANVRAIDAFVAMTGNIGIEGGGA---RyghlhtwGFNyNAMlqkpplGSIGMpgaaGTTSEFGSG------EEVAQ 418
Cdd:COG3383 300 TQGTDNVNAIINLALATGNIGRPGTGPfplT-------GQN-NVQ------GGRDM----GALPNVLPGyrdvtdPEHRA 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 419 YSDRSLNINQ-------TAKGILEA-NEPPVRMLWVACKNPFAQDFDRSKMEKAFEKLEMVVCADQFFNETVQHADIVLP 490
Cdd:COG3383 362 KVADAWGVPPlpdkpglTAVEMFDAiADGEIKALWIIGENPAVSDPDANHVREALEKLEFLVVQDIFLTETAEYADVVLP 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 491 VTTAFEEwnvDASYwhywlsIN--------QPAIKPMYEAKCDLEIAVLLSRtinKLEpgsctFPQEFDHKRWLDQEFND 562
Cdd:COG3383 442 AASWAEK---DGTF------TNterrvqrvRKAVEPPGEARPDWEIIAELAR---RLG-----YGFDYDSPEEVFDEIAR 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 563 GMAKMFGIsSWDDL------------LEGPKKAILpssaawYDRKFKTPSGKFEFKSElceknGHTALPEyKPEAKStlP 630
Cdd:COG3383 505 LTPDYSGI-SYERLealggvqwpcpsEDHPGTPRL------FTGRFPTPDGKARFVPV-----EYRPPAE-LPDEEY--P 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 631 FHLFTPHVQFGIHSQFI-----NLDWMqvfYPEPFVYMHPVSAGKRGIAENDLVKVFNTAGEVELRAKVTANVPEDFLVM 705
Cdd:COG3383 570 LVLTTGRLLDQWHTGTRtrrspRLNKH---APEPFVEIHPEDAARLGIKDGDLVRVSSRRGEVVLRARVTDRVRPGTVFM 646
|
....
gi 2524489867 706 YEAW 709
Cdd:COG3383 647 PFHW 650
|
|
| dmsA_ynfE |
TIGR02166 |
anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family; Members of this family ... |
8-710 |
3.45e-106 |
|
anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family; Members of this family include known and probable dimethyl sulfoxide reductase (DMSO reductase) A chains. In E. coli, dmsA encodes the canonical anaerobic DMSO reductase A chain. The paralog ynfE, as part of ynfFGH expressed from a multicopy plasmid, could complement a dmsABC deletion, suggesting a similar function and some overlap in specificity, although YnfE could not substitute for DmsA in a mixed complex.
Pssm-ID: 274006 [Multi-domain] Cd Length: 797 Bit Score: 342.91 E-value: 3.45e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 8 LNRRSFLKGLIALGTVAALPGGLLTSRCALAQPPIPFNPKTYKIYRNACPRNCYDTCSLKTWVKDDVITFVEG---APES 84
Cdd:TIGR02166 1 ISRRHFLKTSAALGGLAAASGALSLPFSVNAAAEATPTGPDEKVVWSACTVNCGSRCPLRVHVKDGEITRIETdntGDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 85 TFTHGT-PCVKGLSYPRRVYSPDRIKYPMVQ-DVRGSGNWRRISWDEAMQRIATKMLEIKKKDGS---MLGLALTKYSGK 159
Cdd:TIGR02166 81 YGNHQVrACLRGRSMRRRVYNPDRLKYPMKRvGKRGEGKFERISWDEATDTIADNLKRIIEKYGNeaiYVNYGTGTTGGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 160 F--GVLNYAVEGMMSSLGYTTRFAGTPCWPAGIDAQNYDMGdMWC--NDPEDMVKAKYIIIWGANPAWCSM----HTMKY 231
Cdd:TIGR02166 161 MsrSWPPTAVARLLNLCGGYLNQYGSYSTAQINEAMPYTYG-ISAdgSSLDDIENSKLVVMFGNNPAETRMsgggQTYYF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 232 IyQAREK-GAKVVVIDPLLTQTAA-KADLYLRVRPGSDGALALGMARHLVDKGLVDQDFVNNYSHGYAE----------- 298
Cdd:TIGR02166 240 L-QALEKsNARVIVIDPRYTDTVAgREDEWIPIRPGTDAALVAAIAYVMISENLHDQAFLDRYCVGFDEktlpasapkng 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 299 -FEEYL----RNNV--TVEWASEICGLSADVIRQLAEEFTAVNPATVWIGYGMQRHVNGGANVRAIDAFVAMTGNIGIEG 371
Cdd:TIGR02166 319 sYKDYIlgegADGTpkTPEWASKITGIPADTIIKLAREIGNAKPAFISQGWGPQRHANGEQAARAIMMLALLTGNVGIKG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 372 GGAryghlHTWGFNYNAMLQKPPlgsiGMPGAAGT-------TSEFGSGEEVaqySDRSLNINQTAKgiLEANeppVRML 444
Cdd:TIGR02166 399 GNN-----GAREGNYSLPFARMP----ELPNPVKTsiscflwTDAIDRGTEM---TAIKDGVRGKDK--LDSN---IKFL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 445 WVACKNPFA-QDFDRSKMEKAFE---KLEMVVCADQFFNETVQHADIVLPVTTAFEEWN-VDASY---WHYwLSINQPAI 516
Cdd:TIGR02166 462 WNYAGNCLInQHSDINRTHKILQdesKCEMIVVIDNHMTSSAKYADILLPDTTTLEQNDfIEDSYasnMSY-LIFMQKAI 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 517 KPMYEAKCDLEIAVLLSRTINKLEpgscTFPQEFDHKRWLDQEFNDGMAKMFGISSWDDLLE-GPKKAILPSSA--AWYD 593
Cdd:TIGR02166 541 EPLFECKPIYDMLSEVAKRLGVEA----EFTEGRTQEEWLEHLYAQTRAADPALPSFAELRKqGIYKAKSAPGPfvAFED 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 594 -------RKFKTPSGKFEFKSELCEKNGH----------TALPEYKP-------EAKSTLPFHLFTPHVQFGIHSQFINL 649
Cdd:TIGR02166 617 frrdpeaNPLKTPSGKIEIYSERLAQIAHtwelpegdviTPLPEYVPtfegpddPLRKDFPLQLTGFHYKGRTHSTYGNV 696
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524489867 650 DWMQVFYPEPfVYMHPVSAGKRGIAENDLVKVFNTAGEVELRAKVTANVPEDFLVMYE-AWF 710
Cdd:TIGR02166 697 DWLREAAPQE-LWINPIDAQKRGITNGDMVRIFNSRGEVEIPAKVTPRIMPGVVALGQgAWY 757
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
55-623 |
1.51e-98 |
|
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: 317.34 E-value: 1.51e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 55 ACPRNCYDTCSLKTWVKDDVITFVEGAPESTFTHGTP----CVKGLSYPRRVYSPDRIKYPMvQDV--RGSGNWRRISWD 128
Cdd:cd02770 3 ACTVNCGGRCPLKAHVKDGVITRIETDDTGDDDPGFHqiraCLRGRSQRKRVYNPDRLKYPM-KRVgkRGEGKFVRISWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 129 EAMQRIATKMLEIKKKDGS---MLGLALTKYSGKFGVLNyAVEGMMSSLGYTTRFAGTPCWPAGIDAQNYDMG-DMWCND 204
Cdd:cd02770 82 EALDTIASELKRIIEKYGNeaiYVNYGTGTYGGVPAGRG-AIARLLNLTGGYLNYYGTYSWAQITTATPYTYGaAASGSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 205 PEDMVKAKYIIIWGANPAWCSM---HTMKYIYQAREKGAKVVVIDPLLTQTAA-KADLYLRVRPGSDGALALGMARHLVD 280
Cdd:cd02770 161 LDDLKDSKLVVLFGHNPAETRMgggGSTYYYLQAKKAGAKFIVIDPRYTDTAVtLADEWIPIRPGTDAALVAAMAYVMIT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 281 KGLVDQDFVNNYSHGYAE------------FEEYL----RNNV--TVEWASEICGLSADVIRQLAEEFTAVNPATVWIGY 342
Cdd:cd02770 241 ENLHDQAFLDRYCVGFDAehlpegappnesYKDYVlgtgYDGTpkTPEWASEITGVPAETIRRLAREIATTKPAAILQGW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 343 GMQRHVNGGANVRAIDAFVAMTGNIGIEGGGA-RYGHLHTWGFNYNAMLQKPPLGSIgmPGAAGTTSEFgSGEEVAQYSD 421
Cdd:cd02770 321 GPQRHANGEQAARAIMMLAAMTGNVGIPGGNTgARPGGSAYNGAGLPAGKNPVKTSI--PCFMWTDAIE-RGEEMTADDG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 422 RSLNINQTAKGIleaneppvRMLW-VACKNPFAQDFDRSK----MEKAFEKLEMVVCADQFFNETVQHADIVLPVTTAFE 496
Cdd:cd02770 398 GVKGADKLKSNI--------KMIWnYAGNTLINQHSDDNNttraLLDDESKCEFIVVIDNFMTPSARYADILLPDTTELE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 497 EWN-VDASYW--HYWLSINQPAIKPMYEAKCDLEIAVLLSRTINKLEpgscTFPQEFDHKRWLDQEFNDGMAKMFGISSW 573
Cdd:cd02770 470 REDiVLTSNAgmMEYLIYSQKAIEPLYECKSDYEICAELAKRLGVED----QFTEGKTEQEWLEELYGQTRAKEPGLPTY 545
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524489867 574 DDLLE-GPKKAILPSSAAWYD--------RKFKTPSGKFEFKSELCEKNGH--------TALPEYKP 623
Cdd:cd02770 546 EEFREkGIYRVPRALPFVAFEdfredpenNPLKTPSGKIEIYSKALADMAKtlpegdeiPAIPKYVP 612
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
56-621 |
9.81e-96 |
|
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: 305.77 E-value: 9.81e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 56 CPRNCYDTCSLKTWVKDDVITFVEGAPESTFTHGTPCVKGLSYPRRVYSPDRIKYPM--VQDvRGSGNWRRISWDEAMQR 133
Cdd:cd02759 3 TCPGCHSGCGVLVYVKDGKLVKVEGDPNHPTNKGRLCMRGLAAPEIVYHPDRLLYPLkrVGE-RGENKWERISWDEALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 134 IATKMLEIKKKDG-SMLGLALTKYSGKFGVLNYAVEGMMSSLGY-TTRFAGTPCWPAGIDAQNYDMGDMWCNDPEDMVKA 211
Cdd:cd02759 82 IAEKLAEIKAEYGpESIATAVGTGRGTMWQDSLFWIRFVRLFGSpNLFLSGESCYWPRDMAHALTTGFGLGYDEPDWENP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 212 KYIIIWGANPAWCS----MHTMKyiyQAREKGAKVVVIDPLLTQTAAKADLYLRVRPGSDGALALGMARHLVDKGLVDQD 287
Cdd:cd02759 162 ECIVLWGKNPLNSNldlqGHWLV---AAMKRGAKLIVVDPRLTWLAARADLWLPIRPGTDAALALGMLNVIINEGLYDKD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 288 FVNNYSHGYAEFEEYLrNNVTVEWASEICGLSADVIRQLAEEFTAVNPATVWIGYGMQRHVNGGANVRAIDAFVAMTGNI 367
Cdd:cd02759 239 FVENWCYGFEELAERV-QEYTPEKVAEITGVPAEKIRKAARLYATAKPACIQWGLAIDQQKNGTQTSRAIAILRAITGNL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 368 GIEGggaryghlhtwgfnynamlqkpplGSIGMPgaagttsefgsgeevaqysdrslninqtakgileanePPVRMLWVA 447
Cdd:cd02759 318 DVPG------------------------GNLLIP-------------------------------------YPVKMLIVF 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 448 CKNPFAQDFDRSKMEKAFEKLEMVVCADQFFNETVQHADIVLPVTTAFEEWNVdaSYWHYW---LSINQPAIKPMYEAKC 524
Cdd:cd02759 337 GTNPLASYADTAPVLEALKALDFIVVVDLFMTPTAMLADIVLPVAMSLERPGL--RGGFEAenfVQLRQKAVEPYGEAKS 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 525 DLEIAVLLSRTINklepgsctfPQEFDHKRWldqefndgmakMFGisswddLLEGPKKAilpssaawydrKFKTPSGKFE 604
Cdd:cd02759 415 DYEIVLELGKRLG---------PEEAEYYKY-----------EKG------LLRPDGQP-----------GFNTPTGKVE 457
|
570
....*....|....*..
gi 2524489867 605 FKSELCEKNGHTALPEY 621
Cdd:cd02759 458 LYSTMLEELGYDPLPYY 474
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
55-623 |
4.40e-88 |
|
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: 288.22 E-value: 4.40e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 55 ACPRNCYDTCSLKTWVKDDVITFVEGAPESTFTHGTPCVKGLSYPRRVYSPDRIKYPMVQ-DVRGSGNWRRISWDEAMQR 133
Cdd:cd02765 3 ACPPNCGGRCPLKCHVRDGKIVKVEPNEWPDKTYKRGCTRGLSHLQRVYSPDRLKYPMKRvGERGEGKFERITWDEALDT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 134 IATKMLEIKKKDGsmlGLALTKYSGKfgvlnyAVEGMMSSLGYTTRFAGTP-CWPAGID-----AQNYDMGDMW---CND 204
Cdd:cd02765 83 IADKLTEAKREYG---GKSILWMSSS------GDGAILSYLRLALLGGGLQdALTYGIDtgvgqGFNRVTGGGFmppTNE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 205 PEDMVKAKYIIIWGANPAWCSMHTMKYIYQAREKGAKVVVIDPLLTQTAAKADLYLRVRPGSDGALALGMARHLVDKGLV 284
Cdd:cd02765 154 ITDWVNAKTIIIWGSNILETQFQDAEFFLDARENGAKIVVIDPVYSTTAAKADQWVPIRPGTDPALALGMINYILEHNWY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 285 DQDFVNNYS-------------------------HGYAEFE--------------------EYLRNNVTV---------- 309
Cdd:cd02765 234 DEAFLKSNTsapflvredngtllrqadvtatpaeDGYVVWDtnsdspepvaatninpalegEYTINGVKVhtvltalreq 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 310 ------EWASEICGLSADVIRQLAEEFTAVNPATVWIGYGMQRHVNGGANVRAIDAFVAMTGNIGIEGGGAryGHLHTWG 383
Cdd:cd02765 314 aasyppKAAAEICGLEEAIIETLAEWYATGKPSGIWGFGGVDRYYHSHVFGRTAAILAALTGNIGRVGGGV--GQIKFMY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 384 FNYNAMLQkpplgsigmpgaagttsefgsgeevaqysdrslninqtakgileaneppvrmlwvacknpfaQDFDRSKMEK 463
Cdd:cd02765 392 FMGSNFLG--------------------------------------------------------------NQPDRDRWLK 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 464 AFEKLEMVVCADQFFNETVQHADIVLPVTTAFEEWNVDASY-WHYWLSINQPAIKPMYEAKCDLEIAVLLSRtinKLEPG 542
Cdd:cd02765 410 VMKNLDFIVVVDIFHTPTVRYADIVLPAAHWFEVEDLLVRYtTHPHVLLQQKAIEPLFESKSDFEIEKGLAE---RLGLG 486
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 543 ScTFPQefDHKRWLDQEFNDGMAKMFGIsSWDDLLEgpkKAILPSSA-------AWYDRKFKTPSGKFEFKSELCEKNgH 615
Cdd:cd02765 487 D-YFPK--TPEDYVRAFMNSDDPALDGI-TWEALKE---EGIIMRLAtpedpyvAYLDQKFGTPSGKLEFYNEAAPEL-E 558
|
....*...
gi 2524489867 616 TALPEYKP 623
Cdd:cd02765 559 EALPLPEE 566
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
56-737 |
3.16e-84 |
|
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: 280.89 E-value: 3.16e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 56 CPRnCYDTCSLKTWVKDDVITFVEGAPESTFTHGTPCVKGLSYPRRVYSPDRIKYPMvqdVRGSGNWRRISWDEAMQRIA 135
Cdd:TIGR01591 3 CPY-CGVGCSLNLVVKDGKIVRVEPYQGHKANRGHLCVKGYFAWEFINSKDRLTTPL---IREGDKFREVSWDEAISYIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 136 TKMLEIKKKDG--SMLGLALTKYSGKFGVLNY----AVEGmMSSLGYTTRFAGTPCwPAGIdAQNYDMGDMwCNDPEDMV 209
Cdd:TIGR01591 79 EKLKEIKEKYGpdSIGFIGSSRGTNEENYLLQklarAVIG-TNNVDNCARVCHGPS-VAGL-KQTVGIGAM-SNTISEIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 210 KAKYIIIWGANPAwcSMH--TMKYIYQAREKGAKVVVIDPLLTQTAAKADLYLRVRPGSDGALALGMARHLVDKGLVDQD 287
Cdd:TIGR01591 155 NADLIVIIGYNPA--ESHpvVAQYLKNAKRNGAKIIVIDPRKTETAKIADLHIPLKPGTDIALLNAMANVIIEEGLYDKA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 288 FVNNYSHGYAEFEEYLRNNvTVEWASEICGLSADVIRQLAEEFTAVNPATVWIGYGMQRHVNGGANVRAIDAFVAMTGNI 367
Cdd:TIGR01591 233 FIEKRTEGFEEFREIVKGY-TPEYVEDITGVPADLIREAARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 368 GIEGGGAryghlhtwgfnynamlqKPPLGSIGMPGAA--GTTSEF--G----SGEEVAQY-----------SDRSLNINQ 428
Cdd:TIGR01591 312 GKPGGGV-----------------NPLRGQNNVQGACdmGALPDFlpGyqpvSDEEVREKfakawgvvklpAEPGLRIPE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 429 TAKGILEANeppVRMLWVACKNPFAQDFDRSKMEKAFEKLEMVVCADQFFNETVQHADIVLPVTTAFEEwnvDASYWHYW 508
Cdd:TIGR01591 375 MIDAAADGD---VKALYIMGEDPLQSDPNTSKVRKALEKLELLVVQDIFMTETAKYADVVLPAAAWLEK---EGTFTNAE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 509 LSIN--QPAIKPMYEAKCDLEIavlLSRTINKL-EPGSCTFPQE-FDHKRWLDQEF-NDGMAKMFGISSwddlLEGP--K 581
Cdd:TIGR01591 449 RRIQrfFKAVEPKGESKPDWEI---IQELANALgLDWNYNHPQEiMDEIRELTPLFaGLTYERLDELGS----LQWPcnD 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 582 KAILPSSAAWYDRkFKTPSGKFEFKSelCEKNGhtalPEYKPEAKStlPFHLFTPHV--QFGIHSQFINLDWMQVFYPEP 659
Cdd:TIGR01591 522 SDASPTSYLYKDK-FATPDGKAKFIP--LEWVA----PIEEPDDEY--PLILTTGRVltHYNVGEMTRRVAGLRRLSPEP 592
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524489867 660 FVYMHPVSAGKRGIAENDLVKVFNTAGEVELRAKVTANV-PEDFLVMYEAWFPKrkynVQNVVADTPADmglmKTGAPG 737
Cdd:TIGR01591 593 YVEINTEDAKKLGIKDGDLVKVKSRRGEITLRAKVSDRVnKGAIYITMHFWDGA----VNNLTTDDLDP----ISGTPE 663
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
64-605 |
8.06e-78 |
|
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: 259.45 E-value: 8.06e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 64 CSLKTWVKDDVITFVEGAPESTFTHGTPCVKGLSYPRRVYSPDRIKYPMVqdvRGSGNWRRISWDEAMQRIATKMLEIKK 143
Cdd:cd02753 11 CGLELWVKDNKIVGVEPVKGHPVNRGKLCVKGRFGFDFVNSKDRLTKPLI---RKNGKFVEASWDEALSLVASRLKEIKD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 144 KDG--SMLGLALTKYSGKfgvLNYAVEGMMSSLGYT------TRFAGTPCwPAGIdAQNYDMGDMWcNDPEDMVKAKYII 215
Cdd:cd02753 88 KYGpdAIAFFGSAKCTNE---ENYLFQKLARAVGGTnnvdhcARLCHSPT-VAGL-AETLGSGAMT-NSIADIEEADVIL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 216 IWGANPAWCSMHTMKYIYQAREKGAKVVVIDPLLTQTAAKADLYLRVRPGSDGALALGMARHLVDKGLVDQDFVNNYSHG 295
Cdd:cd02753 162 VIGSNTTEAHPVIARRIKRAKRNGAKLIVADPRRTELARFADLHLQLRPGTDVALLNAMAHVIIEEGLYDEEFIEERTEG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 296 YAEFEEYLRNNvTVEWASEICGLSADVIRQLAEEFTAVNPATVWIGYGMQRHVNGGANVRAIDAFVAMTGNIGIEGGGAR 375
Cdd:cd02753 242 FEELKEIVEKY-TPEYAERITGVPAEDIREAARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGTGVN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 376 yghlhtwgfnynamlqkpPL-------GSIGMpgaaGTTSEFGSGeevaqYsdrslninqtakgileaneppVRMLWVAC 448
Cdd:cd02753 321 ------------------PLrgqnnvqGACDM----GALPNVLPG-----Y---------------------VKALYIMG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 449 KNPFAQDFDRSKMEKAFEKLEMVVCADQFFNETVQHADIVLPVTTAFEEwnvDASYwhywlsIN--------QPAIKPMY 520
Cdd:cd02753 353 ENPALSDPNTNHVRKALESLEFLVVQDIFLTETAELADVVLPAASFAEK---DGTF------TNterrvqrvRKAVEPPG 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 521 EAKCDLEIavlLSRTINKLepGsctFPQEFDHKRwldqEFNDGMAKMF----GIsSWDDL------------LEGPKKAI 584
Cdd:cd02753 424 EARPDWEI---IQELANRL--G---YPGFYSHPE----EIFDEIARLTpqyaGI-SYERLerpgglqwpcpdEDHPGTPI 490
|
570 580
....*....|....*....|.
gi 2524489867 585 LpssaawYDRKFKTPSGKFEF 605
Cdd:cd02753 491 L------HTERFATPDGKARF 505
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
8-710 |
3.46e-77 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 265.35 E-value: 3.46e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 8 LNRRSFLKgLIALGTVAALPGGLLT--SRCALAQPPIPFNPKTYKIYRNACPRNCYDTCSLKTWVKDDVITFVE----GA 81
Cdd:PRK14990 14 VSRRGLVK-TTAIGGLAMASSALTLpfSRIAHAVDSAIPTKSDEKVIWSACTVNCGSRCPLRMHVVDGEIKYVEtdntGD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 82 PESTFTHGT-PCVKGLSYPRRVYSPDRIKYPMVQ-DVRGSGNWRRISWDEAMQRIATKMLEIKKKdgsmlglaltkYSGK 159
Cdd:PRK14990 93 DNYDGLHQVrACLRGRSMRRRVYNPDRLKYPMKRvGARGEGKFERISWEEAYDIIATNMQRLIKE-----------YGNE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 160 FGVLNYAVegmmSSLGYTTrfagTPCWPAG---------------------IDAQ-----NYDMGDmWC--NDPEDMVKA 211
Cdd:PRK14990 162 SIYLNYGT----GTLGGTM----TRSWPPGntlvarlmnccggylnhygdySSAQiaeglNYTYGG-WAdgNSPSDIENS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 212 KYIIIWGANPAWCSMH---TMKYIYQAREKG-AKVVVIDPLLTQTAA-KADLYLRVRPGSDGALALGMARHLVDKGLVDQ 286
Cdd:PRK14990 233 KLVVLFGNNPGETRMSgggVTYYLEQARQKSnARMIIIDPRYTDTGAgREDEWIPIRPGTDAALVNGLAYVMITENLVDQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 287 DFVNNYSHGYAE------------FEEYLRNN------VTVEWASEICGLSADVIRQLAEEFTAVNPATVWIGYGMQRHV 348
Cdd:PRK14990 313 PFLDKYCVGYDEktlpasapknghYKAYILGEgpdgvaKTPEWASQITGVPADKIIKLAREIGSTKPAFISQGWGPQRHA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 349 NGGANVRAIDAFVAMTGNIGIEGG--GARYGHlHTWGFNYNAMLQKPPLGSIGMpgaAGTTSEFGSGEEVAQYSDrslni 426
Cdd:PRK14990 393 NGEIATRAISMLAILTGNVGINGGnsGAREGS-YSLPFVRMPTLENPIQTSISM---FMWTDAIERGPEMTALRD----- 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 427 NQTAKGILEAnepPVRMLWVACKNPFAQdfDRSKMEKAFE------KLEMVVCADQFFNETVQHADIVLPVTTAFEEWN- 499
Cdd:PRK14990 464 GVRGKDKLDV---PIKMIWNYAGNCLIN--QHSEINRTHEilqddkKCELIVVIDCHMTSSAKYADILLPDCTASEQMDf 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 500 -VDASYWHY-WLSINQPAIKPMYEAKCDLEIAVLLSRTINKLEpgscTFPQEFDHKRWLDQEFNDGMAKMFGISSWDDLL 577
Cdd:PRK14990 539 aLDASCGNMsYVIFNDQVIKPRFECKTIYEMTSELAKRLGVEQ----QFTEGRTQEEWMRHLYAQSREAIPELPTFEEFR 614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 578 -EGPKKAILPSSAAWYDRKFK---------TPSGKFEFKS----------ELCEKNGHTALPEYKPEAKS-------TLP 630
Cdd:PRK14990 615 kQGIFKKRDPQGHHVAYKAFRedpqanpltTPSGKIEIYSqaladiaatwELPEGDVIDPLPIYTPGFESyqdplnkQYP 694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 631 FHLFTPHVQFGIHSQFINLDWMQVFYPEPfVYMHPVSAGKRGIAENDLVKVFNTAGEVELRAKVTANVPEDFLVMYE-AW 709
Cdd:PRK14990 695 LQLTGFHYKSRVHSTYGNVDVLKAACRQE-MWINPLDAQKRGINNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGEgAW 773
|
.
gi 2524489867 710 F 710
Cdd:PRK14990 774 Y 774
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
8-706 |
8.00e-77 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 263.07 E-value: 8.00e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 8 LNRRSFLKGLIALGTVAAL----PGGLLtsrcalAQPPIPFNPKTyKIYRNACpRNCYDTCSLKTWVKDDVITFVEGAPE 83
Cdd:PRK15488 3 LSRRDFLKGAGAGCAACALgsllPGALA------ANEIAQLKGKT-KLTPSIC-EMCSTRCPIEARVVNGKNVFIQGNPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 84 STFTHGTPCVKGLSYPRRVYSPDRIKYPMVQ-DVRGSGNWRRISWDEAMQRIATKMLEIKKKDGSMlGLALTKYSGkfgv 162
Cdd:PRK15488 75 AKSFGTKVCARGGSGHSLLYDPQRIVKPLKRvGERGEGKWQEISWDEAYQEIAAKLNAIKQQHGPE-SVAFSSKSG---- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 163 lnyAVEGMMSSLGYTTrfaGTP-------CWPAGIDAQNYDM--GDMwcndPEDMVKAKYIIIWGAN--PAWCSMHTMKY 231
Cdd:PRK15488 150 ---SLSSHLFHLATAF---GSPntfthasTCPAGYAIAAKVMfgGKL----KRDLANSKYIINFGHNlyEGINMSDTRGL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 232 IYQAREKGAKVVVIDPLLTQTAAKADLYLRVRPGSDGALALGMARHLVDKGLVDQDFVNNYSHGYAEFEEYLRNnVTVEW 311
Cdd:PRK15488 220 MTAQMEKGAKLVVFEPRFSVVASKADEWHAIRPGTDLAVVLALCHVLIEENLYDKAFVERYTSGFEELAASVKE-YTPEW 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 312 ASEICGLSADVIRQLAEEFTAVNPATVwIGYG----------MQRhvngganvRAIDAFVAMTGNIGIEGG------GAR 375
Cdd:PRK15488 299 AEAISDVPADDIRRIARELAAAAPHAI-VDFGhratftpeefDMR--------RAIFAANVLLGNIERKGGlyfgknASV 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 376 YGHLHtwGFNYNAMLQKPplGSIGMPGAAGTTSEFgSGEEVAqYSDRSLNINQTakgILEA--NEPPVRML-WVACK-NP 451
Cdd:PRK15488 370 YNKLA--GEKVAPTLAKP--GVKGMPKPTAKRIDL-VGEQFK-YIAAGGGVVQS---IIDAtlTQKPYQIKgWVMSRhNP 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 452 FAQDFDRSKMEKAFEKLEMVVCADQFFNETVQHADIVLPVTTAFE--EWNVDASYWHYWLSINQPAIKPMYEAKCDLEIA 529
Cdd:PRK15488 441 MQTVTDRADVVKALKKLDLVVVCDVYLSESAAYADVVLPESTYLErdEEISDKSGKNPAYALRQRVVEPIGDTKPSWQIF 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 530 VLLSRtinKLEPGScTFPQEfDHKRWLDQEFNDGMA-----KMFGISSWDD--LLEGPK----------KAILPSSAAWY 592
Cdd:PRK15488 521 KELGE---KMGLGQ-YYPWQ-DMETLQLYQVNGDHAllkelKKKGYVSFGVplLLREPKmvakfvarypNAKAVDEDGTY 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 593 DR--KFKTPSGKFEFKSELCEKnghtALPEYKpeAKSTLPFHLFTPHVQFGI----------HSQfiNLDWMQVFYPEPF 660
Cdd:PRK15488 596 GSqlKFKTPSGKIELFSAKLEA----LAPGYG--VPRYRDVALKKEDELYFIqgkvavhtngATQ--NVPLLANLMSDNA 667
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 2524489867 661 VYMHPVSAGKRGIAENDLVKVFNTAGEVELRAKVTANVPEDFLVMY 706
Cdd:PRK15488 668 VWIHPQTAGKLGIKNGDEIRLENSVGKEKGKALVTPGIRPDTLFAY 713
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
50-557 |
1.25e-72 |
|
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: 244.15 E-value: 1.25e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 50 KIYRNACPRNCYDTCSLKTWVKDDVITFVEGA---PEstFTHGTP------CVKGLSYPRRVYSPDRIKYPMVQ-DVRGS 119
Cdd:cd02750 2 KVVRSTHGVNCTGSCSWNVYVKNGIVTREEQAtdyPE--TPPDLPdynprgCQRGASFSWYLYSPDRVKYPLKRvGARGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 120 GNWRRISWDEAMQRIATKMLEIKKKDGSMlglaltkysgkfGVLNYAVEGMMSSLGYT--TRFAGTpcwpagIDAQNYDM 197
Cdd:cd02750 80 GKWKRISWDEALELIADAIIDTIKKYGPD------------RVIGFSPIPAMSMVSYAagSRFASL------IGGVSLSF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 198 GDMWCNDP----------------EDMVKAKYIIIWGANPAWCSMHTMKYIYQAREKGAKVVVIDPLLTQTAAKADLYLR 261
Cdd:cd02750 142 YDWYGDLPpgspqtwgeqtdvpesADWYNADYIIMWGSNVPVTRTPDAHFLTEARYNGAKVVVVSPDYSPSAKHADLWVP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 262 VRPGSDGALALGMARHLVDKGLVDQDFVNNYSHgyAEFEEYlrnnvTVEWASEICGLSADVIRQLAEEFTAVNPATVWIG 341
Cdd:cd02750 222 IKPGTDAALALAMAHVIIKEKLYDEDYLKEYTD--LPFLVY-----TPAWQEAITGVPRETVIRLAREFATNGRSMIIVG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 342 YGMQRHVNGGANVRAIDAFVAMTGNIGIEGGGAryghlhtwgFNYnamlqkpplgsIGMPgaagttsefgsgeevaqysd 421
Cdd:cd02750 295 AGINHWYHGDLCYRALILLLALTGNEGKNGGGW---------AHY-----------VGQP-------------------- 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 422 rslninqtakgileaneppvRMLWVACKNPfaqdFDRSKMEKAF------EKLEMVVCADQFFNETVQHADIVLPVTTAF 495
Cdd:cd02750 335 --------------------RVLFVWRGNL----FGSSGKGHEYfedapeGKLDLIVDLDFRMDSTALYSDIVLPAATWY 390
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524489867 496 EEWNVDASYWHYWLSINQPAIKPMYEAKCDLEIAVLLSRtinKLEPGSCTFPQEF--DHKRWLD 557
Cdd:cd02750 391 EKHDLSTTDMHPFIHPFSPAVDPLWEAKSDWEIFKALAK---KVPWRTLTGRQQFylDHDWFLE 451
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
8-710 |
2.55e-72 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 251.90 E-value: 2.55e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 8 LNRRSFLKGLIALGTVAALPGGLLTSRCALA-QPPIPFNPKTYKIyrnacprncydTCS----LKTWVKDDVItfVEGAP 82
Cdd:PRK15102 1 ASRRRFLKGLGGLSAAGMLGPSLLTPRSALAaQAAAAETTKEWIL-----------TGShwgaFRAKVKNGRF--VEAKP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 83 ESTFTHGTPCVKGLsyPRRVYSPDRIKYPMVQ----------DVRGSGNWR--RISWDEAMQRIATKMLEIKKKDG-SML 149
Cdd:PRK15102 68 FELDKYPTKMINGI--KGHVYNPSRIRYPMVRldwlrkrhksDTSQRGDNRfvRVSWDEALDLFYEELERVQKTYGpSAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 150 GLALTKY--SGKF----GVLNYAVeGM----MSSLG-YTTRfAGTPCWPAGI-DAQNYDMGDMWcndPEDMVKAKYIIIW 217
Cdd:PRK15102 146 HTGQTGWqsTGQFhsatGHMQRAI-GMhgnsVGTVGdYSTG-AGQVILPYVLgSTEVYEQGTSW---PLILENSKTIVLW 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 218 GANPA-------WCSMH-TMKYIYQAREKGAK----VVVIDPLLTQTAAkadlYLR-----VRPGSDGALALGMARHLVD 280
Cdd:PRK15102 221 GSDPVknlqvgwNCETHeSYAYLAQLKEKVAKgeinVISIDPVVTKTQN----YLGcehlyVNPQTDVPLMLALAHTLYS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 281 KGLVDQDFVNNYSHGYAEFEEYL---RNNV--TVEWASEICGLSADVIRQLAEEFTAvNPATVWIGYGMQRHVNGGANVR 355
Cdd:PRK15102 297 ENLYDKKFIDNYCLGFEQFLPYLlgeKDGVpkTPEWAEKICGIDAETIRELARQMAK-GRTQIIAGWCIQRQQHGEQPYW 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 356 AIDAFVAMTGNIGIEGGGARYGHlhtwgfNYN---------AML----------QKPPLGSIGMPGAAGTTSefgsgeeV 416
Cdd:PRK15102 376 MGAVLAAMLGQIGLPGGGISYGH------HYSgigvpssggAIPggfpgnldtgQKPKHDNSDYKGYSSTIP-------V 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 417 AQYSDRSLNINQTakgiLEANE-----PPVRMLWVACKNPFAQDFDRSKMEKAFEKLEMVVCADQFFNETVQHADIVLPV 491
Cdd:PRK15102 443 ARFIDAILEPGKT----INWNGkkvtlPPLKMMIFSGTNPWHRHQDRNRMKEAFRKLETVVAIDNQWTATCRFADIVLPA 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 492 TTAFEEWNVDA--SYWHYWLSINQPAIKPMYEAKCDLEIAVLLSRTINKLEpgscTFPQEFDHKRWLDQEFNDGMAK--- 566
Cdd:PRK15102 519 CTQFERNDIDQygSYSNRGIIAMKKVVEPLFESRSDFDIFRELCRRFGREK----EYTRGMDEMGWLKRLYQECKQQnkg 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 567 MFGISSWDDLLEgpKKAIL-PSSAAWYDRK-FK---------TPSGKFEFKSELCEKNGHTALPEY-----KPE------ 624
Cdd:PRK15102 595 KFHMPEFDEFWK--KGYVEfGEGQPWVRHAdFRedpelnplgTPSGLIEIYSRKIADMGYDDCQGHpmwfeKIErshggp 672
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 625 AKSTLPFHLFTPHVQFGIHSQFINLDWMQVFYP----EPfVYMHPVSAGKRGIAENDLVKVFNTAGEVELRAKVTANVPE 700
Cdd:PRK15102 673 GSDKYPLWLQSVHPDKRLHSQLCESEELRETYTvqgrEP-VYINPQDAKARGIKDGDVVRVFNDRGQVLAGAVVSDRYPP 751
|
810
....*....|.
gi 2524489867 701 DFLVMYE-AWF 710
Cdd:PRK15102 752 GVIRIHEgAWY 762
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
60-534 |
4.91e-72 |
|
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: 242.20 E-value: 4.91e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 60 CYDTCSLKTWVKDDVITFVEGAPESTFTHGTPCVKGLSYPRRVYSPDRIKYPMVQ-DVRGSGNWRRISWDEAMQRIATKM 138
Cdd:cd02755 8 CSSRCGILARVEDGRVVKIDGNPLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRvGERGEGKFREASWDEALQYIASKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 139 LEIKKKDG--SMLGLAltkysgkfgvlnyAVEGMMSSLGYTTRFAGTPCW--PAGIDAQNYDMGDMWCNDP------EDM 208
Cdd:cd02755 88 KEIKEQHGpeSVLFGG-------------HGGCYSPFFKHFAAAFGSPNIfsHESTCLASKNLAWKLVIDSfggevnPDF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 209 VKAKYIIIWGAN--PAWCSMHTMKYIyQAREKGAKVVVIDPLLTQTAAKADLYLRVRPGSDGALALGMARHLVDKGLVDQ 286
Cdd:cd02755 155 ENARYIILFGRNlaEAIIVVDARRLM-KALENGAKVVVVDPRFSELASKADEWIPIKPGTDLAFVLALIHVLISENLYDA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 287 DFVNNYSHG----YAEFEEYlrnnvTVEWASEICGLSADVIRQLAEEFTAVNPATVWI-GYGMQRHVNGGANVRAIDAFV 361
Cdd:cd02755 234 AFVEKYTNGfellKAHVKPY-----TPEWAAQITDIPADTIRRIAREFAAAAPHAVVDpGWRGTFYSNSFQTRRAIAIIN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 362 AMTGNIGIEGGgaryghlhtWGFnynamlqkpplgsigmpgaAGTTSEFgsgeevaqysdrslninqtakgileanepPV 441
Cdd:cd02755 309 ALLGNIDKRGG---------LYY-------------------AGSAKPY-----------------------------PI 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 442 RMLWVACKNPFAQDFDRSKMEKAFEKLEMVVCADQFFNETVQHADIVLPVTTAFE--EWNVDASYWHYWLSINQPAIKPM 519
Cdd:cd02755 332 KALFIYRTNPFHSMPDRARLIKALKNLDLVVAIDILPSDTALYADVILPEATYLErdEPFSDKGGPAPAVATRQRAIEPL 411
|
490
....*....|....*
gi 2524489867 520 YEAKCDLEIAVLLSR 534
Cdd:cd02755 412 YDTRPGWDILKELAR 426
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
53-534 |
8.99e-72 |
|
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. Members of the MopB_Nitrate-R-NapA CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239155 [Multi-domain] Cd Length: 565 Bit Score: 244.83 E-value: 8.99e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 53 RNACPRnCYDTCSLKTWVKDDVITFVEGAPESTFTHGTPCVKGLSYPRRVYSPDRIKYPMVQdvRGSGNWRRISWDEAMQ 132
Cdd:cd02754 1 KTTCPY-CGVGCGVEIGVKDGKVVAVRGDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLLR--RNGGELVPVSWDEALD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 133 RIATKMLEIKKKD----------GSML---GLALTK-YSGKFGVLNY----------AVEGMMSSLGyttrFAGTPCwpa 188
Cdd:cd02754 78 LIAERFKAIQAEYgpdsvafygsGQLLteeYYAANKlAKGGLGTNNIdtnsrlcmasAVAGYKRSFG----ADGPPG--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 189 gidaqNYDmgdmwcndpeDMVKAKYIIIWGANPAWCsmHT--MKYIYQAREK--GAKVVVIDPLLTQTAAKADLYLRVRP 264
Cdd:cd02754 151 -----SYD----------DIEHADCFFLIGSNMAEC--HPilFRRLLDRKKAnpGAKIIVVDPRRTRTADIADLHLPIRP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 265 GSDGALALGMARHLVDKGLVDQDFVNNYSHGYAEFEEYLRnNVTVEWASEICGLSADVIRQLAEEFTAVNPATVWIGYGM 344
Cdd:cd02754 214 GTDLALLNGLLHVLIEEGLIDRDFIDAHTEGFEELKAFVA-DYTPEKVAEITGVPEADIREAARLFGEARKVMSLWTMGV 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 345 QRHVNGGANVRAIDAFVAMTGNIGIEGGGAryghlhtwgfnynamlqkpplGSI-GMPgAAGTTSEFGSG---------- 413
Cdd:cd02754 293 NQSTQGTAANNAIINLHLATGKIGRPGSGP---------------------FSLtGQP-NAMGGREVGGLanllpghrsv 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 414 ------EEVAQY---------SDRSLNINQTAKGILEANeppVRMLWVACKNPFAQDFDRSKMEKAFEKLEMVVCADQF- 477
Cdd:cd02754 351 nnpehrAEVAKFwgvpegtipPKPGLHAVEMFEAIEDGE---IKALWVMCTNPAVSLPNANRVREALERLEFVVVQDAFa 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524489867 478 FNETVQHADIVLPVTTAFEEW----NVDASywhywLSINQPAIKPMYEAKCDLEIAVLLSR 534
Cdd:cd02754 428 DTETAEYADLVLPAASWGEKEgtmtNSERR-----VSLLRAAVEPPGEARPDWWILADVAR 483
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
59-612 |
2.61e-71 |
|
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: 242.35 E-value: 2.61e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 59 NCYDTCSLKTWVKDDVITFVEGAPESTFTHGTPCVKGLSYPRRVYSPDRIKYPM-----VQDVRGSGNWRRISWDEAMQR 133
Cdd:cd02757 8 GCTAWCGLQAYVEDGRVTKVEGNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMkrtnpRKGRDVDPKFVPISWDEALDT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 134 IATKMLEIKKKDGSmlglalTKYS---GKFGVLN-YAVEGMMSSLGYTTRFAGTP-CWPAGIDAQNYDMGDMWCNDPeDM 208
Cdd:cd02757 88 IADKIRALRKENEP------HKIMlhrGRYGHNNsILYGRFTKMIGSPNNISHSSvCAESEKFGRYYTEGGWDYNSY-DY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 209 VKAKYIIIWGANPAWCSM---HTMKyIYQAREKGAKVVVIDPLLTQTAAKADLYLRVRPGSDGALALGMARHLVDKGLVD 285
Cdd:cd02757 161 ANAKYILFFGADPLESNRqnpHAQR-IWGGKMDQAKVVVVDPRLSNTAAKADEWLPIKPGEDGALALAIAHVILTEGLWD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 286 QDFVNNYSHG-----------YAEFEEYLRNNV-----------TVEWASEICGLSADVIRQLAEEF-TAVNPATVWIGY 342
Cdd:cd02757 240 KDFVGDFVDGknyfkagetvdEESFKEKSTEGLvkwwnlelkdyTPEWAAKISGIPAETIERVAREFaTAAPAAAAFTWR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 343 GMQRHVNGGANVRAIDAFVAMTGNIGIEGGgaryghlhtwgfnynamlqkpplgsigmpgaagtTSEFGSGEEVAQYSDR 422
Cdd:cd02757 320 GATMQNRGSYNSMACHALNGLVGSIDSKGG----------------------------------LCPNMGVPKIKVYFTY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 423 SLNINQTAkgileanepPVRMLWvacknpfaqdfdrskmEKAFEKLEMVVCADQFFNETVQHADIVLPVTTAFEEWNVDA 502
Cdd:cd02757 366 LDNPVFSN---------PDGMSW----------------EEALAKIPFHVHLSPFMSETTYFADIVLPDGHHFERWDVMS 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 503 SY--WHYWLSINQPAIKPMYEAKCDLEIAVLLSRTINKlePGSCTFpqefdhKRWLDQEFNDGMAKMFGISSWDDLlegp 580
Cdd:cd02757 421 QEnnLHPWLSIRQPVVKSLGEVREETEILIELAKKLDP--KGSDGM------KRYAPGQFKDPETGKNNRWEFENV---- 488
|
570 580 590
....*....|....*....|....*....|..
gi 2524489867 581 kkailpssaawydrkFKTPSGKFEFKSELCEK 612
Cdd:cd02757 489 ---------------FPTETGKFEFYSETLKK 505
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
70-614 |
1.10e-70 |
|
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: 242.94 E-value: 1.10e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 70 VKDDVITFVEGAPESTftHGTPCVKGLsyPRRVYSPDRIKYPMV------------QDVRGSGNWRRISWDEAMQRIATK 137
Cdd:cd02769 13 VKDGRIVGVRPFEEDP--DPSPLLDGV--PDAVYSPTRIKYPMVrrgwlekgpgsdRSLRGKEEFVRVSWDEALDLVAAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 138 MLEIKKKDGSMlglALtkYSGKFG-----VLNYA---VEGMMSSLGYTTRFAGTPCWPAGIDAQNYDMGDM-WCNDP--- 205
Cdd:cd02769 89 LKRVRKTYGNE---AI--FGGSYGwssagRFHHAqslLHRFLNLAGGYVGSVGDYSTGAAQVILPHVVGSMeVYTEQqts 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 206 -EDMVK-AKYIIIWGANP------AW--CSMHTMK-YIYQAREKGAKVVVIDPLLTQTAAKADL-YLRVRPGSDGALALG 273
Cdd:cd02769 164 wPVIAEhTELVVAFGADPlknaqiAWggIPDHQAYsYLKALKDRGIRFISISPLRDDTAAELGAeWIAIRPGTDVALMLA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 274 MARHLVDKGLVDQDFVNNYSHGYAEFEEYLR---NNV--TVEWASEICGLSADVIRQLAEEFtAVNPATVWIGYGMQRHV 348
Cdd:cd02769 244 LAHTLVTEGLHDKAFLARYTVGFDKFLPYLLgesDGVpkTPEWAAAICGIPAETIRELARRF-ASKRTMIMAGWSLQRAH 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 349 NGGANVRAIDAFVAMTGNIGIEGGGARYGhlhtWGFNYNAMlqkPPLGSIGMPGAAGTTSEFGSGEEVAQYSDRSLNINQ 428
Cdd:cd02769 323 HGEQPHWMAVTLAAMLGQIGLPGGGFGFG----YHYSNGGG---PPRGAAPPPALPQGRNPVSSFIPVARIADMLLNPGK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 429 T--AKGIlEANEPPVRMLWVACKNPFAQDFDRSKMEKAFEKLEMVVCADQFFNETVQHADIVLPVTTAFEEWNVDASYWH 506
Cdd:cd02769 396 PfdYNGK-KLTYPDIKLVYWAGGNPFHHHQDLNRLIRAWQKPETVIVHEPFWTATARHADIVLPATTSLERNDIGGSGDN 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 507 YWLSINQPAIKPMYEAKCDLEIAVLLSRTINKLEpgscTFPQEFDHKRWLDQEFNDG--MAKMFGIS--SWDDLLE--GP 580
Cdd:cd02769 475 RYIVAMKQVVEPVGEARDDYDIFADLAERLGVEE----QFTEGRDEMEWLRHLYEESraQAAARGVEmpSFDEFWAqgYV 550
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 2524489867 581 KKAILPSSAAWYD--------RKFKTPSGKFEFKSELCEKNG 614
Cdd:cd02769 551 ELPIPEADFVRLAdfredpeaNPLGTPSGRIEIFSETIAGFG 592
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
55-536 |
1.11e-62 |
|
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: 219.19 E-value: 1.11e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 55 ACPRnCYDTCSLKTWVKDDVITFVEGAPESTFTHGTPCVKGLSYPRRVYSPDRIKYPMVqdvRGSGNWRRISWDEAMQRI 134
Cdd:cd02762 3 ACIL-CEANCGLVVTVEDGRVASIRGDPDDPLSKGYICPKAAALGDYQNDPDRLRTPMR---RRGGSFEEIDWDEAFDEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 135 ATKMLEIKKKDGsmlGLALTKYSGKFGVLNYAvegMMSSLGYTTRFAGTPCW--PAGID------AQNYDMGDMWCNDPE 206
Cdd:cd02762 79 AERLRAIRARHG---GDAVGVYGGNPQAHTHA---GGAYSPALLKALGTSNYfsAATADqkpghfWSGLMFGHPGLHPVP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 207 DMVKAKYIIIWGANPAWC--SMHTM----KYIYQAREKGAKVVVIDPLLTQTAAKADLYLRVRPGSDGALALGMARHLVD 280
Cdd:cd02762 153 DIDRTDYLLILGANPLQSngSLRTApdrvLRLKAAKDRGGSLVVIDPRRTETAKLADEHLFVRPGTDAWLLAAMLAVLLA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 281 KGLVDQDFVNNYSHGYAEFEEYLRnNVTVEWASEICGLSADVIRQLAEEFTAVNPATVWIGYGMQRHVNGGANVRAIDAF 360
Cdd:cd02762 233 EGLTDRRFLAEHCDGLDEVRAALA-EFTPEAYAPRCGVPAETIRRLAREFAAAPSAAVYGRLGVQTQLFGTLCSWLVKLL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 361 VAMTGNIGIEGGgaryghlhtwgfnynAMLQKPPLGSIGMpgaagtTSEFGSGEEVAQYSDRSLNI-------NQTAKGI 433
Cdd:cd02762 312 NLLTGNLDRPGG---------------AMFTTPALDLVGQ------TSGRTIGRGEWRSRVSGLPEiagelpvNVLAEEI 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 434 LEANEPPVRMLWVACKNPFAQDFDRSKMEKAFEKLEMVVCADQFFNETVQHADIVLPVTTAFEEWNVD-------ASYWH 506
Cdd:cd02762 371 LTDGPGRIRAMIVVAGNPVLSAPDGARLEAALGGLEFMVSVDVYMTETTRHADYILPPASQLEKPHATffnlefpRNAFR 450
|
490 500 510
....*....|....*....|....*....|
gi 2524489867 507 YwlsiNQPAIKPMYEAKCDLEIAVLLSRTI 536
Cdd:cd02762 451 Y----RRPLFPPPPGTLPEWEILARLVEAL 476
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
53-540 |
5.97e-52 |
|
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: 191.84 E-value: 5.97e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 53 RNACPrNCYDTCSLKTWVKDDVITFVEGAPESTFTHGTPCVKGLSYPRRVYSPDRIKYPMVQdVRGSGNWRRISWDEAMQ 132
Cdd:cd02752 1 RTICP-YCSVGCGLIAYVQNGVWVHQEGDPDHPVNRGSLCPKGAALRDFVHSPKRLKYPMYR-APGSGKWEEISWDEALD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 133 RIATKMLEIKKKDGS----------------MLGLA---------LTKYSGKFGVLNY----------AVEGMMSSLGYT 177
Cdd:cd02752 79 EIARKMKDIRDASFVeknaagvvvnrpdsiaFLGSAklsneecylIRKFARALGTNNLdhqariuhspTVAGLANTFGRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 178 trfAGTPCWpagIDAQNydmgdmwcndpedmvkAKYIIIWGANPAWCSMHTMKYIYQAREK-GAKVVVIDPLLTQTAAKA 256
Cdd:cd02752 159 ---AMTNSW---NDIKN----------------ADVILVMGGNPAEAHPVSFKWILEAKEKnGAKLIVVDPRFTRTAAKA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 257 DLYLRVRPGSDGALALGMARHLVdkglvdqdfvnnyshgyaefeEYlrnnvTVEWASEICGLSADVIRQLAEEF----TA 332
Cdd:cd02752 217 DLYVPIRSGTDIAFLGGMINYII---------------------RY-----TPEEVEDICGVPKEDFLKVAEMFaatgRP 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 333 VNPATVWIGYGMQRHVNGGANVRAIDAFVAMTGNIGIEGGGAryghlhtwgfnyNAMlqkpplgsigmpgaagttsefgS 412
Cdd:cd02752 271 DKPGTILYAMGWTQHTVGSQNIRAMCILQLLLGNIGVAGGGV------------NAL----------------------R 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 413 GEEVAQYSdrslninqTAKGILEANEPPvrmlWVACKNPFAQDFDRSKMEKAFEKLEMVVCADQFFNET----------- 481
Cdd:cd02752 317 GHSNVQGA--------TDLGLLSHNLPG----YLGGQNPNSSFPNANKVRRALDKLDWLVVIDPFPTETaafwknpgmdp 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524489867 482 --VQHADIVLPVTTAFE-EWNVDASywHYWLSINQPAIKPMYEAKCDLEIAVLLSRTINKLE 540
Cdd:cd02752 385 ksIQTEVFLLPAACQYEkEGSITNS--GRWLQWRYKVVEPPGEAKSDGDILVELAKRLGFLY 444
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
107-533 |
5.43e-47 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 171.04 E-value: 5.43e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 107 RIKYPMVQdvRGSGNWRRISWDEAMQRIATKMLEIKKKDGSMLGLALTKYSGKFGVLNYAV-----EGMMSSLGYTTRFA 181
Cdd:pfam00384 1 RLKYPMVR--RGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAINGGSGGLTDVESLYAlkkllNRLGSKNGNTEDHN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 182 GTPCwPAGIDAQNYDMGDMWC--NDPEDMVKAKYIIIWGANPAWCSMHTMKYIYQA-REKGAKVVVIDPLLTQTaaKADL 258
Cdd:pfam00384 79 GDLC-TAAAAAFGSDLRSNYLfnSSIADIENADLILLIGTNPREEAPILNARIRKAaLKGKAKVIVIGPRLDLT--YADE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 259 YLRVRPGSDGALALGMARHLVDKGLVDQDFvnnyshgyaefeeylrnnvtvewaseicglsadvirqlaeeftAVNPATV 338
Cdd:pfam00384 156 HLGIKPGTDLALALAGAHVFIKELKKDKDF-------------------------------------------APKPIII 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 339 WiGYGMQRHVNGGANVRAIDAFVAMTGNIGIEGGG-ARYGHLHTWGfNYNAML---QKPPLGSIGMPGAAGTTsefgsge 414
Cdd:pfam00384 193 V-GAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGwNGLNILQGAA-SPVGALdlgLVPGIKSVEMINAIKKG------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 415 evaqysdrslninqtakgileanepPVRMLWVACKNPFAQDFDRSKMEKAFEKLEMVVCADQF-FNETVQHADIVLPVTT 493
Cdd:pfam00384 264 -------------------------GIKVLYLLGNNPFVTHADENRVVKALQKLDLFVVYDGHhGDKTAKYADVILPAAA 318
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2524489867 494 AFE--EWNVDASYWHywlSINQPAIKPMYEAKCDLEIAVLLS 533
Cdd:pfam00384 319 YTEknGTYVNTEGRV---QSTKQAVPPPGEAREDWKILRALS 357
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
60-500 |
4.56e-39 |
|
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: 154.22 E-value: 4.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 60 CYDTCSLKTWVKDDVITFVEGAPESTFTHGTPCVKGLSYPRRVYSPDRIKYPMVQ-DVRGSGNWRRISWDEAMQRIATKM 138
Cdd:cd02763 7 CACRCGIRVHLRDGKVRYIKGNPDHPLNKGVICAKGSSGIMKQYSPARLTKPLLRkGPRGSGQFEEIEWEEAFSIATKRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 139 LEIKKKDGSMLGL--------ALTK-YSGKFGVLNYAVEGMMSSLGYTTrfagtpcwpAGIdaqnYDMG-DMWCNDPEDM 208
Cdd:cd02763 87 KAARATDPKKFAFftgrdqmqALTGwFAGQFGTPNYAAHGGFCSVNMAA---------GGL----YSIGgSFWEFGGPDL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 209 VKAKYIIIWGANPAWCSMHTMKYIYQAREKGAKVVVIDPLLTQTAAKADLYLRVRPGSDGALALGMARHLVDKGLVDQDF 288
Cdd:cd02763 154 EHTKYFMMIGVAEDHHSNPFKIGIQKLKRRGGKFVAVNPVRTGYAAIADEWVPIKPGTDGAFILALAHELLKAGLIDWEF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 289 VNNYSHGyAEFEEYlrnnvTVEWASEICGLSADVIRQLAEEFTAV-------------------------NPATVWIGYG 343
Cdd:cd02763 234 LKRYTNA-AELVDY-----TPEWVEKITGIPADTIRRIAKELGVTardqpielpiawtdvwgrkhekitgRPVSFHAMRG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 344 MQRHVNGGANVRAIDAFVAMTGNIGIEGggaryGHLHTWGFNYNAM-LQKPPLG-SIGMPGAAGTTSEFG---------- 411
Cdd:cd02763 308 IAAHSNGFQTIRALFVLMMLLGTIDRPG-----GFRHKPPYPRHIPpLPKPPKIpSADKPFTPLYGPPLGwpaspddllv 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 412 --SGEEVAQYSDRSLNINQTAKGILE-------ANEP-PV--------RMLWVACKN-PFAQDFDRSKMEKAFEKLEMVV 472
Cdd:cd02763 383 deDGNPLRIDKAYSWEYPLAAHGCMQnvitnawRGDPyPIdtlmiymaNMAWNSSMNtPEVREMLTDKDASGNYKIPFII 462
|
490 500
....*....|....*....|....*...
gi 2524489867 473 CADQFFNETVQHADIVLPVTTAFEEWNV 500
Cdd:cd02763 463 VCDAFYSEMVAFADLVLPDTTYLERHDA 490
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
107-378 |
5.75e-35 |
|
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: 140.91 E-value: 5.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 107 RIKYPMVQDvRGSGNWRRISWDEAMQRIATKMLEIKKKDgsmlglALTKYSGKfgvlnyavegmmSSL--GYTT----RF 180
Cdd:cd02767 64 RLTYPMRYD-AGSDHYRPISWDEAFAEIAARLRALDPDR------AAFYTSGR------------ASNeaAYLYqlfaRA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 181 AGTPCWPagiDAQNYdmgdmwCNDP------------------EDMVKAKYIIIWGANPAWCSMHTMKYIYQAREKGAKV 242
Cdd:cd02767 125 YGTNNLP---DCSNM------CHEPssvglkksigvgkgtvslEDFEHTDLIFFIGQNPGTNHPRMLHYLREAKKRGGKI 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 243 VVIDPL-----------------LTQTAAKADLYLRVRPGSDGALALGMARHLVD-----KGLVDQDFVNNYSHGYAEFE 300
Cdd:cd02767 196 IVINPLrepglerfanpqnpesmLTGGTKIADEYFQVRIGGDIALLNGMAKHLIErddepGNVLDHDFIAEHTSGFEEYV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 301 EYLRNnvtVEWaSEI---CGLSADVIRQLAEEFtAVNPATVWI-GYGMQRHVNGGANVRAIDAFVAMTGNIGIEGGGA-- 374
Cdd:cd02767 276 AALRA---LSW-DEIeraSGLSREEIEAFAAMY-AKSERVVFVwGMGITQHAHGVDNVRAIVNLALLRGNIGRPGAGLmp 350
|
....*
gi 2524489867 375 -RyGH 378
Cdd:cd02767 351 iR-GH 354
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
83-519 |
5.39e-34 |
|
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: 139.40 E-value: 5.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 83 ESTFTHGTPCVKGLSYPRRVYSPDRIKYPMVQD-VRGSGNWRRISWDEAMQRIATK-MLEIkkkDGSMLGLALTKY---- 156
Cdd:cd02758 59 NGLKARATACARGNAGLQYLYDPYRVLQPLKRVgPRGSGKWKPISWEQLIEEVVEGgDLFG---EGHVEGLKAIRDldtp 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 157 -----------SGKFGVLNYAVEGmmsSLGYTTRFA----GTPCWP-----------AGIDAQNYDMGDMWCNDPeDMVK 210
Cdd:cd02758 136 idpdhpdlgpkANQLLYTFGRDEG---RTPFIKRFAnqafGTVNFGghgsycglsyrAGNGALMNDLDGYPHVKP-DFDN 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 211 AKYIIIWGANPA-------WCSMHTMkyiyQAR-EKGAKVVVIDPLLTQT---AAKADLYLRVRPGSDGALALGMARHLV 279
Cdd:cd02758 212 AEFALFIGTSPAqagnpfkRQARRLA----EARtEGNFKYVVVDPVLPNTtsaAGENIRWVPIKPGGDGALAMAMIRWII 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 280 DKGLVDQDFVNN------YSHGYAEFEE--YLRNNVTV-----------------EWAsEICGLSADVIRQLAEEFTAVN 334
Cdd:cd02758 288 ENERYNAEYLSIpskeaaKAAGEPSWTNatHLVITVRVksalqllkeeafsysleEYA-EICGVPEAKIIELAKEFTSHG 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 335 PATVWIGYGMQRHVNGGANVRAIDAFVAMTGNIGIEGG-GARYGHLHTWGFNYNAMLQKPPlgsiGMPGAAG-------- 405
Cdd:cd02758 367 RAAAVVHHGGTMHSNGFYNAYAIRMLNALIGNLNWKGGlLMSGGGFADNSAGPRYDFKKFF----GEVKPWGvpidrskk 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 406 ---TTSEFGSGEEVAQ--YSDRS----LNINQTAK---GILEANEPPVRMLWVACKNPF-AQDFDRSKME---KAFEKLE 469
Cdd:cd02758 443 ayeKTSEYKRKVAAGEnpYPAKRpwypLTPELYTEviaSAAEGYPYKLKALILWMANPVyGAPGLVKQVEeklKDPKKLP 522
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2524489867 470 MVVCADQFFNETVQHADIVLPVTTAFEEWNVdASYWHYWLSINQ----PAIKPM 519
Cdd:cd02758 523 LFIAIDAFINETSAYADYIVPDTTYYESWGF-STPWGGVPTKAStarwPVIAPL 575
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
59-523 |
1.99e-22 |
|
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: 102.74 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 59 NCYDTCSLKTW-VKDDVITFVEGAPESTFTH---GTPCVKGLSYPRRVYSPDRIKYPMVQDVRGSG-----NWRRISWDE 129
Cdd:cd02760 6 NCVAGPDFMAVkVVDGVATEIEPNFAAEDIHparGRVCVKAYGLVQKTYNPNRVLQPMKRTNPKKGrnedpGFVPISWDE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 130 AMQRIATKMLEIKKKDGSMLGLaLTKYSGKFGvlnyavegmmsSLGYTTRFAGT-PCWPAGIDAQNYDMGD---MWCNDP 205
Cdd:cd02760 86 ALDLVAAKLRRVREKGLLDEKG-LPRLAATFG-----------HGGTPAMYMGTfPAFLAAWGPIDFSFGSgqgVKCVHS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 206 E---------------DMVKAKYIIIWGAN-PAWCSMHTMKYIYQAREKGAKVVVIDPLLTQTAAKADLYLRVRPGSDGA 269
Cdd:cd02760 154 EhlygefwhraftvaaDTPLANYVISFGSNvEASGGPCAVTRHADARVRGYKRVQVEPHLSVTGACSAEWVPIRPKTDPA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 270 LALGMARHLV-DKGL----------------------------------------------------------------- 283
Cdd:cd02760 234 FMFAMIHVMVhEQGLgkldvpflrdrtsspylvgpdglylrdaatgkplvwdersgravpfdtrgavpavagdfavdgav 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 284 -VDQDFVNNYSHG------YAEFEEYLRNNvTVEWASEICGLSADVIRQLAEEFT----------------AVNPATVWI 340
Cdd:cd02760 314 sVDADDETAIHQGvegttaFTMLVEHMRKY-TPEWAESICDVPAATIRRIAREFLenasigstievdgvtlPYRPVAVTL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 341 GYGMQRHVNGGANVRAIDAFVAMTGNIGIEGGgaryghlhTWGFN------YNAMLQKPPLGSIG-----------MPGA 403
Cdd:cd02760 393 GKSVNNGWGAFECCWARTLLATLVGALEVPGG--------TLGTTvrlnrpHDDRLASVKPGEDGfmaqgfnptdkEHWV 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 404 AGTTSEFGSGEEVAQYSDRSLN----------INQTAKGILEANEPPVRM-LWVACKNPFAQDF-DRSKMEKAFEKLEMV 471
Cdd:cd02760 465 VKPTGRNAHRTLVPIVGNSAWSqalgptqlawMFLREVPLDWKFELPTLPdVWFNYRTNPAISFwDTATLVDNIAKFPFT 544
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524489867 472 VCADQFFNETVQHADIVLPVTTAFEEWNV--------DASYWHYW-LSINQPAIKPMYEAK 523
Cdd:cd02760 545 VSFAYTEDETNWMADVLLPEATDLESLQMikvggtkfVEQFWEHRgVVLRQPAVEPQGEAR 605
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
630-735 |
2.21e-20 |
|
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239186 [Multi-domain] Cd Length: 124 Bit Score: 87.42 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 630 PFHLFTPHVQFGIHSQFINLDWMQVFYPEPFVYMHPVSAGKRGIAENDLVKVFNTAGEVELRAKVTANVPEDFLVMYEAW 709
Cdd:cd02785 3 PLACIQRHSRFRVHSQFSNVPWLLELQPEPRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGVVTAEQGW 82
|
90 100
....*....|....*....|....*...
gi 2524489867 710 FPK--RKYNVQNVVADTPADMGLMKTGA 735
Cdd:cd02785 83 WSRyfQEGSLQDLTSPFVNPVHEYIYGP 110
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
636-729 |
4.60e-19 |
|
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: 82.75 E-value: 4.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 636 PHVQFgiHSQF-INLDWMQVFYPEPFVYMHPVSAGKRGIAENDLVKVFNTAGEVELRAKVTANVPEDFLVMYEAW--FPK 712
Cdd:cd02775 1 LRDHF--HSGTrTRNPWLRELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWghRGG 78
|
90
....*....|....*..
gi 2524489867 713 RKYNVQNVVADTPADMG 729
Cdd:cd02775 79 RGGNANVLTPDALDPPS 95
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
10-597 |
5.65e-18 |
|
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like homologs (PHLH) of molybdopterin binding (MopB) proteins. This CD is of the PHLH region homologous to the catalytic molybdopterin-binding subunit of MopB homologs.
Pssm-ID: 239165 [Multi-domain] Cd Length: 524 Bit Score: 87.93 E-value: 5.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 10 RRSFLKgLIALGTVAALPGGlltsrCAL-AQPPIPFNPK--------TYKIYRNACPRNcyDTCSLKTWVKDDVITFVEG 80
Cdd:cd02764 1 RRGFLK-LMGASLAMASAAA-----CRYpVEKIVPYVIWpenivpgeTVYYATSLVPAG--EGQGVLVKTVDGRPIKIEG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 81 APESTFTHG------TPCVKGLsyprrvYSPDRIKYPMvqdvRGSGNWRRI--SWDEAMQRIATKMLEIKKKDG------ 146
Cdd:cd02764 73 NPDHPASLGgtsaraQASVLSL------YDPDRAQGPL----RRGIDGAYVasDWADFDAKVAEQLKAVKDGGKlavlsg 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 147 --------SMLGLALTKYSGK---FGVLNYA---VEGMMSSLGyttrfagtpcwpaGIDAQNYDMGdmwcndpedmvKAK 212
Cdd:cd02764 143 nvnsptteALIGDFLKKYPGAkhvVYDPLSAedvNEAWQASFG-------------KDVVPGYDFD-----------KAE 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 213 YIIIWGAN--PAWCSMHTMKYIYQAREKGAK------VVVIDPLLTQTAAKADLYLRVRPGSDGALALGMARHLVDKGLV 284
Cdd:cd02764 199 VIVSIDADflGSWISAIRHRHDFAAKRRLGAeepmsrLVAAESVYTLTGANADVRLAIRPSQEKAFALGLAHKLIKKGAG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 285 DQDFVNNYSHGYAEFEEYlrnnvtvewASEICGLSADVIRQLAEEFTAVNPATVwigygmqrhVNGGANVRAIDAFVAMT 364
Cdd:cd02764 279 SSLPDFFRALNLAFKPAK---------VAELTVDLDKALAALAKALAAAGKSLV---------VAGSELSQTAGADTQVA 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 365 GNigiegggaryghlhtwgfNYNAMLqkpplgsigmpGAAGTT-SEFGSGEEVAQYSDRSLNinqtaKGILEANEPPVRM 443
Cdd:cd02764 341 VN------------------ALNSLL-----------GNDGKTvDHARPIKGGELGNQQDLK-----ALASRINAGKVSA 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 444 LWVACKNPFAQDFDRSKMEKAFEKLEMVVCADQFFNETVQHADIVLPVTTAFEEWNvDASYWHYWLSINQPAIKPMYEAK 523
Cdd:cd02764 387 LLVYDVNPVYDLPQGLGFAKALEKVPLSVSFGDRLDETAMLCDWVAPMSHGLESWG-DAETPDGTYSICQPVIAPLFDTR 465
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524489867 524 CDLEIAVLLSrtinklePGSCTFPQEF-DHKRWldqefndgMAKMFGISSWDDLLEgpKKAILPSSAAWYDRKFK 597
Cdd:cd02764 466 SAQESLLLAL-------GGSLGGYEKLrRYTSW--------IKAAIGDRSWEQALR--DGVAADVNVSAGSTSFR 523
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
631-727 |
6.31e-18 |
|
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: 80.01 E-value: 6.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 631 FHLFTPHVQFGIHSQFINLDWMQVFYPEP-FVYMHPVSAGKRGIAENDLVKVFNTAGEVELRAKVTANVPEDFLVMYEAW 709
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKPEPeVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFGW 80
|
90
....*....|....*...
gi 2524489867 710 FPKRKYNVQNVVADTPAD 727
Cdd:pfam01568 81 WYEPRGGNANALTDDATD 98
|
|
| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
630-709 |
9.73e-18 |
|
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: 80.50 E-value: 9.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 630 PFHLFTPHVQFGIHSQFINLDWM-QVFYPEPFVYMHPVSAGKRGIAENDLVKVFNTAGEVELRAKVTANVPEDFLVMYEA 708
Cdd:cd02776 1 PLNYLTPHGKWSIHSTYRDNLLMlRLQRGGPVVWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTVFMYHA 80
|
.
gi 2524489867 709 W 709
Cdd:cd02776 81 Q 81
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
630-710 |
5.42e-17 |
|
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: 77.62 E-value: 5.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 630 PFHLFTPHVQFGIHSQFINLDWMQVFYP----EPfVYMHPVSAGKRGIAENDLVKVFNTAGEVELRAKVTANVPEDFLVM 705
Cdd:cd02777 2 PLQLISPHPKRRLHSQLDNVPWLREAYKvkgrEP-VWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPGVVAL 80
|
....*.
gi 2524489867 706 YE-AWF 710
Cdd:cd02777 81 PEgAWY 86
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
81-563 |
3.27e-16 |
|
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: 82.92 E-value: 3.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 81 APESTFTHGTPCVKGLSYPRRVYSPD------RIKYPMVqdvRGSGNWRRISWDEAMQRIATKMLEIKKKDGSMLGLALT 154
Cdd:cd02756 85 DKECPVNSGNYSTRGGTNAERIWSPDnrvgetRLTTPLV---RRGGQLQPTTWDDAIDLVARVIKGILDKDGNDDAVFAS 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 155 KY----SGKFGVLNYAVeGMMSSLGYTTRFA--------GTPCWP---AGIDAQNYDMgdmwcndpEDMVKAKYIIIWGA 219
Cdd:cd02756 162 RFdhggGGGGFENNWGV-GKFFFMALQTPFVrihnrpayNSEVHAtreMGVGELNNSY--------EDARLADTIVLWGN 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 220 NPAwcSMHTMKYI---------------YQAREKG-----AKVVVIDPLLTQTAAKAD--------LYLRVRPGSDGALA 271
Cdd:cd02756 233 NPY--ETQTVYFLnhwlpnlrgatvsekQQWFPPGepvppGRIIVVDPRRTETVHAAEaaagkdrvLHLQVNPGTDTALA 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 272 LGMARHLVDkglvdqdfvnnyshGYAEFeeylrnnvtVEWASEICGLSADVIRQ----LAEEFTAVNPATVWIGY----- 342
Cdd:cd02756 311 NAIARYIYE--------------SLDEV---------LAEAEQITGVPRAQIEKaadwIAKPKEGGYRKRVMFEYekgii 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 343 -GMQRHVNGGANVRaidaFVAMTGNIGIEGGGARYGHLHTWGFnynAMLQKPPLGSIGMPGAAGTTSEF---GSGEEV-- 416
Cdd:cd02756 368 wGNDNYRPIYSLVN----LAIITGNIGRPGTGCVRQGGHQEGY---VRPPPPPPPWYPQYQYAPYIDQLlisGKGKVLwv 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 417 --AQYSDRSLNINQTAKGILEANEPPVRMLWVAcknPFAQDFDRSKMEKAFEKLE-----MVVCADQFFNETVQHADIVL 489
Cdd:cd02756 441 igCDPYKTTPNAQRLRETINHRSKLVTDAVEAA---LYAGTYDREAMVCLIGDAIqpgglFIVVQDIYPTKLAEDAHVIL 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 490 PVTTAFE----EWNVDASYwhywLSINQPAIKPMYEAKCDLEIAVLLSRTINKL--EPGSCTFPQ-EFDHKRWLDQE--F 560
Cdd:cd02756 518 PAAANGEmnetSMNGHERR----LRLYEKFMDPPGEAMPDWWIAAMIANRIYELyqEEGKGGSAQyQFFGFIWKTEEdnF 593
|
...
gi 2524489867 561 NDG 563
Cdd:cd02756 594 MDG 596
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
102-528 |
1.23e-15 |
|
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: 79.63 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 102 VYSPDRIKYPMVqdvRGSGNWRRISWDEAMQRIATKMLEIKKKD-----GSMLGL----ALTKYSGKFGVLNYAVEGMMS 172
Cdd:cd02768 49 LNSRQRLTQPLI---KKGGKLVPVSWEEALKTVAEGLKAVKGDKiggiaGPRADLeslfLLKKLLNKLGSNNIDHRLRQS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 173 SLGYTTRFAGTPCWPAGIdaqnydmgdmwcndpEDMVKAKYIIIWGANPAW-CSMHTMKYIYQAREKGAKVVVIdplltq 251
Cdd:cd02768 126 DLPADNRLRGNYLFNTSI---------------AEIEEADAVLLIGSNLRKeAPLLNARLRKAVKKKGAKIAVI------ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 252 taakadlylrvrpgsdgalalgmarhlvdkGLVDQDFVNNYSHGYAefeeYLRNNVtvewASEICGLSADVIRQLAEEFT 331
Cdd:cd02768 185 ------------------------------GPKDTDLIADLTYPVS----PLGASL----ATLLDIAEGKHLKPFAKSLK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 332 AVNPATVWIGYGMQRHvNGGANVRAIDAFVamtgnigiegggARYGHLHTWGFNYNAmlqkppLGSIGM-PGAAGTTSEF 410
Cdd:cd02768 227 KAKKPLIILGSSALRK-DGAAILKALANLA------------AKLGTGAGLWNGLNV------LNSVGArLGGAGLDAGL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 411 GSGEEVAQYsdrSLNINqtakgileANEPpvrmlwvacknpfaqDFDRSKMEKAFEKLEMVVCADQFFNETVQHADIVLP 490
Cdd:cd02768 288 ALLEPGKAK---LLLLG--------EDEL---------------DRSNPPAAVALAAADAFVVYQGHHGDTGAQADVILP 341
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2524489867 491 VTTAFEEwnvDASYwhywlsIN--------QPAIKPMYEAKCDLEI 528
Cdd:cd02768 342 AAAFTEK---SGTY------VNtegrvqrfKKAVSPPGDAREDWKI 378
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
629-747 |
2.11e-15 |
|
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: 72.70 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 629 LPFHLFTPHVQFGIHSQFINLDWMQVFYPEPFVYMHPVSAGKRGIAENDLVKVFNTAGEVELRAKVTANVPEDFLVMYEA 708
Cdd:cd02786 1 YPLRLITPPAHNFLNSTFANLPELRAKEGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVVVAEGG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2524489867 709 WFPK---RKYNVQNVVADTPADMGlmktgaPGAAIHSQFADI 747
Cdd:cd02786 81 WWREhspDGRGVNALTSARLTDLG------GGSTFHDTRVEV 116
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
8-350 |
1.42e-14 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 77.63 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 8 LNRRSFLKGLIALGTVAA----LPgglltsrcALAQPPIPFNPKTYKIYRNACpRNCYDTCSLKTWVKDDVITFVEGAPE 83
Cdd:PRK13532 3 LSRRDFMKANAAAAAAAAaglsLP--------AVANAVVGSAQTAIKWDKAPC-RFCGTGCGVLVGTKDGRVVATQGDPD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 84 STFTHGTPCVKGLSYPRRVYSPDRIKYPMVQDVRGS----GNWRRISWDEAMQRIATKMLEIKKKDGSMlglaltkysgk 159
Cdd:PRK13532 74 APVNRGLNCIKGYFLSKIMYGKDRLTQPLLRMKDGKydkeGEFTPVSWDQAFDVMAEKFKKALKEKGPT----------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 160 fgvlnyAVeGMMSSLGYTTR--FAGTPCWPAGIDAQNYD------MGD--------------MWCNDpeDMVKAKYIIIW 217
Cdd:PRK13532 143 ------AV-GMFGSGQWTIWegYAASKLMKAGFRSNNIDpnarhcMASavvgfmrtfgidepMGCYD--DIEAADAFVLW 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 218 GANPAwcSMHTmkyIYQAR-------EKGAKVVVIDPLLTQTAAKADLYLRVRPGSDGALALGMARHLVDKGLVDQDFVN 290
Cdd:PRK13532 214 GSNMA--EMHP---ILWSRvtdrrlsNPDVKVAVLSTFEHRSFELADNGIIFTPQTDLAILNYIANYIIQNNAVNWDFVN 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 291 NYSH--------GY-----------AE------------FEEYLR--NNVTVEWASEICGLSADVIRQLAEEFtaVNPAT 337
Cdd:PRK13532 289 KHTNfrkgatdiGYglrpthplekaAKnpgtagksepisFEEFKKfvAPYTLEKTAKMSGVPKEQLEQLAKLY--ADPNR 366
|
410
....*....|....*.
gi 2524489867 338 VWIGY---GMQRHVNG 350
Cdd:PRK13532 367 KVVSFwtmGFNQHTRG 382
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
206-393 |
7.22e-14 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 75.47 E-value: 7.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 206 EDMVKAKYIIIWGANPAWCSMHTMKYIYQAREKGAKVVVIDPL-----------------LTQTAAK-ADLYLRVRPGSD 267
Cdd:PRK09939 204 EDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPLqerglerftapqnpfemLTNSETQlASAYYNVRIGGD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 268 GALALGMARHLVDK----------GLVDQDFVNNYSHGYAEFEEYLRNNvtvEWA--SEICGLSADVIRQLAEEFTAVNP 335
Cdd:PRK09939 284 MALLKGMMRLLIERddaasaagrpSLLDDEFIQTHTVGFDELRRDVLNS---EWKdiERISGLSQTQIAELADAYAAAER 360
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 336 ATVWIGYGMQRHVNGGANVRAIDAFVAMTGNIGIEGGG--ARYGHLHTWGFNYNAMLQKP 393
Cdd:PRK09939 361 TIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGicPLRGHSNVQGDRTVGITEKP 420
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
630-710 |
1.01e-12 |
|
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: 65.39 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 630 PFHLFTPHVQFGIHSQFINLDWMQVFYPEPfVYMHPVSAGKRGIAENDLVKVFNTAGEVELRAKVTANVPEDFLVMYE-A 708
Cdd:cd02794 2 PLQLIGWHYKRRTHSTFDNVPWLREAFPQE-VWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVVALPQgA 80
|
..
gi 2524489867 709 WF 710
Cdd:cd02794 81 WY 82
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
50-104 |
1.67e-12 |
|
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is found in a number of reductase/dehydrogenase families, which include the periplasmic nitrate reductase precursor and the formate dehydrogenase alpha chain.
Pssm-ID: 197994 [Multi-domain] Cd Length: 55 Bit Score: 62.65 E-value: 1.67e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2524489867 50 KIYRNACPRnCYDTCSLKTWVKDDVITFVEGAPESTFTHGTPCVKGLSYPRRVYS 104
Cdd:smart00926 2 KWVPTVCPL-CGVGCGLLVEVKDGRVVRVRGDPDHPVNRGRLCPKGRAGLEQVYS 55
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
630-715 |
2.32e-12 |
|
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: 64.64 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 630 PFHLFTPH-VQFGIHSQFINLDWMQVFYPEPFVYMHPVSAGKRGIAENDLVKVFNTAGEVELRAKVTANVPEDfLVMYEA 708
Cdd:cd02781 3 PLILTTGArSYYYFHSEHRQLPSLRELHPDPVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPG-VVRAEH 81
|
....*....
gi 2524489867 709 --WFPKRKY 715
Cdd:cd02781 82 gwWYPEREA 90
|
|
| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
630-710 |
4.05e-12 |
|
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: 63.81 E-value: 4.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 630 PFHLFTPHVQFGIHSQfinLD--WMQVFYP----EPfVYMHPVSAGKRGIAENDLVKVFNTAGEVELRAKVTANVPEDFL 703
Cdd:cd02793 2 PLHLLSNQPATRLHSQ---LDhgSLSRAYKvqgrEP-IRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPGVV 77
|
....*...
gi 2524489867 704 VMYE-AWF 710
Cdd:cd02793 78 QLPTgAWY 85
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
64-260 |
1.58e-11 |
|
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: 67.17 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 64 CSLKTWVKDDVITFVEGAPESTFTHGTPCVKG-LSYpRRVYSPDRIKYPMvqdVRGSGNWRRISWDEAMQRIATKMLEIK 142
Cdd:COG1034 229 CNIRVDVRGGKVYRVLPRENEAVNEEWLCDKGrFGY-DGLNSPDRLTRPL---VRKDGELVEASWEEALAAAAEGLKALK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 143 KKDGSMLGLALTKYSGKFGVLNYAVEGmmsslgyttrfagtpcwpagidaqnydmgdmwcndpedmvKAKYIIIWGANPA 222
Cdd:COG1034 305 KAENSVGAALLGALPDAAAILEAAEAG----------------------------------------KLKALVLLGADPY 344
|
170 180 190
....*....|....*....|....*....|....*...
gi 2524489867 223 WCSMHTMKyiyQAREKGAKVVVIDPLLTQTAAKADLYL 260
Cdd:COG1034 345 DLDPAAAL---AALAKADFVVVLDHFGSATAERADVVL 379
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
657-701 |
1.75e-11 |
|
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: 61.75 E-value: 1.75e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2524489867 657 PEPFVYMHPVSAGKRGIAENDLVKVFNTAGEVELRAKVTANVPED 701
Cdd:cd00508 33 PEPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRPG 77
|
|
| 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 ... |
56-497 |
2.35e-11 |
|
MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1) found in various bacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Unique to this group, compared to the other prokaryotic and eukaryotic groups in this domain protein family (NADH-Q-OR-NuoG2), is an N-terminal [4Fe-4S] cluster (N7/N1c) present in the second domain. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239172 [Multi-domain] Cd Length: 472 Bit Score: 66.64 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 56 CPrNCYDTCSLKTWVKDDVITFVEGAPESTFTHGTPCVKGLSYPRRVYSPDRIKYPMvqdVRGSGNWRRISWDEAMQRIA 135
Cdd:cd02771 4 CH-HCSVGCNISLGERYGELRRVENRYNGAVNHYFLCDRGRFGYGYVNSRDRLTQPL---IRRGGTLVPVSWNEALDVAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 136 TKmleikkkdgsmlglaLTKYSGKFGVL---------NYAVEgmmsslgyttRFAGTpcwPAGIDaqNYDMGDMWCNdpE 206
Cdd:cd02771 80 AR---------------LKEAKDKVGGIgsprasnesNYALQ----------KLVGA---VLGTN--NVDHRARRLI--A 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 207 DMVKAKYIiiwganpawcSMHTMKYIyqarEKGAKVVVIDPLLTQTAAKADLYLR--VRpGSDGALALGMARHlvdkglV 284
Cdd:cd02771 128 EILRNGPI----------YIPSLRDI----ESADAVLVLGEDLTQTAPRIALALRqaAR-RKAVELAALSGIP------K 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 285 DQDFVNNYSHGYAEFEEYLRNNV------------------TVEW----ASEICGLSADVIRQLAEEFTAV--------- 333
Cdd:cd02771 187 WQDAAVRNIAQGAKSPLFIVNALatrlddiaaesiraspggQARLgaalARAVDASAAGVSGLAPKEKAARiaarltgak 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 334 NPATVWiGygmqrhvNGGANVRAIDAfvamTGNIGIEGGGARYGHlhtwgfnyNAMLQKPPLGSIGM-PGAAGTTSEFGS 412
Cdd:cd02771 267 KPLIVS-G-------TLSGSLELIKA----AANLAKALKRRGENA--------GLTLAVEEGNSPGLlLLGGHVTEPGLD 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 413 GEEVaqysdrslnINQTAKGILEAneppvrmLWVACKNPFAQdFDRSKMEKAFEKLEMVVCADQFFNETVQHADIVLPVT 492
Cdd:cd02771 327 LDGA---------LAALEDGSADA-------LIVLGNDLYRS-APERRVEAALDAAEFVVVLDHFLTETAERADVVLPAA 389
|
....*
gi 2524489867 493 TAFEE 497
Cdd:cd02771 390 SFAEK 394
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
657-699 |
9.95e-11 |
|
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: 59.51 E-value: 9.95e-11
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2524489867 657 PEPFVYMHPVSAGKRGIAENDLVKVFNTAGEVELRAKVTANVP 699
Cdd:cd02791 33 PEPYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVR 75
|
|
| FwdB |
COG1029 |
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion]; |
72-275 |
1.25e-10 |
|
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion];
Pssm-ID: 440652 [Multi-domain] Cd Length: 428 Bit Score: 64.10 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 72 DDVITFVEGAPESTFTHGtpCVKGLSYPRRVYSPDRIKYPMVqdvrgsgNWRRISWDEAMQRIAtKMLEIKKK------- 144
Cdd:COG1029 18 DDLEVEVEGGKIVVVKNA--CAIGAAKFERAVSDHRITSPRI-------RGKEVSLEEAIDKAA-EILANAKRpliygls 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 145 ----DGSMLGLALTKYSGkfGVL-NYAvegmmsslgyttrfagTPC-WPAGIDAQnyDMGDMWCNDPEdmVK--AKYIII 216
Cdd:COG1029 88 stdcEAMRAGLALAERVG--AVVdNTA----------------SVChGPSLLALQ--DVGWPTCTLGE--VKnrADVIIY 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 217 WGANPAwCSM--HTMKYIYQAR-------EKGAKVVVIDPLLTQTAAKADLYLRVRPGSDGAL--ALGMA 275
Cdd:COG1029 146 WGCNPV-HAHprHMSRYSVFPRgfftpkgRKDRTVIVVDPRPTDTAKVADLHLQVKPGRDYEVlsALRAL 214
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
630-709 |
3.73e-10 |
|
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: 58.05 E-value: 3.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 630 PFHLFTPHVQFGIHSQFINLDWMQVFYPEPFVYMHPVSAGKRGIAENDLVKVFNTAGEVELRAKVTANVPEDFLVMYEAW 709
Cdd:cd02778 1 EFRLIYGKSPVHTHGHTANNPLLHELTPENTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMPHGF 80
|
|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
50-104 |
6.73e-09 |
|
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for which the structure is known. This first domain (residues 1 to 60) of PDB:1aa6 is an Fe4S4 cluster just below the protein surface.
Pssm-ID: 428168 [Multi-domain] Cd Length: 55 Bit Score: 52.30 E-value: 6.73e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2524489867 50 KIYRNACPrNCYDTCSLKTWVKDDVITFVEGAPESTFTHGTPCVKGLSYPRRVYS 104
Cdd:pfam04879 2 KVVKTICP-YCGVGCGLEVHVKDGKIVKVEGDPDHPVNEGRLCVKGRFGYERVYN 55
|
|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
106-499 |
1.13e-08 |
|
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, subunit B (FmdB/FwdB), and other related proteins. Formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and some eubacteria. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239162 [Multi-domain] Cd Length: 415 Bit Score: 58.11 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 106 DRIKYPMVqdvrgsgNWRRISWDEAMQRIATKMLEIKK----------KDGSMLGLALTKYSGkfgvlnyAVEGMMSSLG 175
Cdd:cd02761 42 RRITTPRI-------DGKPVSLEEAIEKAAEILKEAKRplfyglgttvCEAQRAGIELAEKLG-------AIIDHAASVC 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 176 YTtrfagtpcwPAGIDAQnyDMGDMWCNDPEDMVKAKYIIIWGANPawcsMHTM-----KYIYQAREKGA-------KVV 243
Cdd:cd02761 108 HG---------PNLLALQ--DSGWPTTTLGEVKNRADVIVYWGTNP----MHAHprhmsRYSVFPRGFFReggredrTLI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 244 VIDPLLTQTAAKADLYLRVRPGSDGALALGMARHLVDKGLVDQdfvnnyshgyaefeeylrnnvtvewasEICGLSADVI 323
Cdd:cd02761 173 VVDPRKSDTAKLADIHLQIDPGSDYELLAALRALLRGAGLVPD---------------------------EVAGIPAETI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 324 RQLAEEFTAVNPATVWIG----YGMQRHVNGGANVRAID--------AFVAMTGNIGIEGggarYGHLHTWGFNYnamlq 391
Cdd:cd02761 226 LELAERLKNAKFGVIFWGlgllPSRGAHRNIEAAIRLVKalneytkfALLPLRGHYNVRG----FNQVLTWLTGY----- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 392 kpPLGSIGMPGAAgttsEFGSGEevaqYSDRSLNINQTAKGileaneppvrMLWVAC--KNPFAQdfdrskmeKAFEKLE 469
Cdd:cd02761 297 --PFRVDFSRGYP----RYNPGE----FTAVDLLAEGEADA----------LLIIASdpPAHFPQ--------SAVKHLA 348
|
410 420 430
....*....|....*....|....*....|..
gi 2524489867 470 M--VVCADQFFNETVQHADIVLPVTTAFEEWN 499
Cdd:cd02761 349 EipVIVIDPPPTPTTRVADVVIPVAIPGIEAG 380
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
652-705 |
2.15e-08 |
|
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: 53.01 E-value: 2.15e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2524489867 652 MQVFYPEPFVYMHPVSAGKRGIAENDLVKVFNTAGEVELRAKVTANVPEDFLVM 705
Cdd:cd02790 28 LDAIAPEEYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGVVFM 81
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
90-506 |
5.45e-08 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 56.54 E-value: 5.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 90 TPCVKGLSYPRRVYSPDRIKYPMvQDV--RGSGNWRRISWDEAMQRI----------------ATKMLE--IKKKDGSmL 149
Cdd:PRK14991 140 TACARGNAMLEQLDSPYRVLQPL-KRVgkRGSGKWQRISFEQLVEEVveggdlfgeghvdglrAIRDLDtpIDAKNPE-Y 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 150 G-----LALTKYS--GK-----------FGVLNYAVEGmmSSLGYTTRfagtpcwpAGIDAQnydMGDMWCN---DPeDM 208
Cdd:PRK14991 218 GpkanqLLVTNASdeGRdafikrfafnsFGTRNFGNHG--SYCGLAYR--------AGSGAL---MGDLDKNphvKP-DW 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 209 VKAKYIIIWGANPAWcSMHTMKYiyQAR-------EKGAKVVVIDPLLTQT----AAKADLYLRVRPGSDGALALGMARH 277
Cdd:PRK14991 284 DNVEFALFIGTSPAQ-SGNPFKR--QARqlanartRGNFEYVVVAPALPLSsslaAGDNNRWLPIRPGTDSALAMGMIRW 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 278 LVDKGLVDQDFVN----------------NYSH------GYAEFEEYLRNN----------------------------- 306
Cdd:PRK14991 361 IIDNQRYNADYLAqpgvaamqaageaswtNATHlviadpGHPRYGQFLRASdlglpfegeargdgedtlvvdaadgelvp 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 307 --------------------------------------VTVEWASEICGLSADVIRQLAEEFTAVNPATVWIGYGMQRHV 348
Cdd:PRK14991 441 atqaqparlfveqyvtladgqrvrvksslqllkeaarkLSLAEYSEQCGVPEAQIIALAEEFTSHGRKAAVISHGGTMSG 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 349 NGGANVRAIDAFVAMTGNIGIEGGGARYGHlhtwGFN-------YNamLQKPPlgsiGMPGAAGT-----------TSEF 410
Cdd:PRK14991 521 NGFYNAWAIMMLNALIGNLNLKGGVVVGGG----KFPgfgdgprYN--LASFA----GKVKPKGVslsrskfpyekSSEY 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 411 GSGEEVAQ--YSDRS--------LNINQTAKGiLEANEPPVRMLWVACKNP-FAQDFDRSKMEKAF---EKLEMVVCADQ 476
Cdd:PRK14991 591 RRKVEAGQspYPAKApwypfvagLLTEMLTAA-LEGYPYPLKAWINHMSNPiYGVPGLRAVIEEKLkdpKKLPLFISIDA 669
|
570 580 590
....*....|....*....|....*....|
gi 2524489867 477 FFNETVQHADIVLPVTTAFEEWNVDASyWH 506
Cdd:PRK14991 670 FINETTALADYIVPDTHTYESWGFTAP-WG 698
|
|
| NarG |
COG5013 |
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and ... |
635-708 |
9.67e-08 |
|
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 444037 [Multi-domain] Cd Length: 1231 Bit Score: 55.98 E-value: 9.67e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524489867 635 TPHVQFGIHSQFI-NLDWMQVFYPEPFVYMHPVSAGKRGIAENDLVKVFNTAGEVELRAKVTANVPEDFLVMYEA 708
Cdd:COG5013 1086 TPHQKWGIHSTYQdNLLMLTLSRGGPTVWMSEEDAAKIGIKDNDWIEAFNRNGVVVARAVVSHRIPEGTVFMYHA 1160
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
630-698 |
1.41e-07 |
|
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: 51.14 E-value: 1.41e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524489867 630 PFHLFTPHVQFgIHSQFINLDWMQVFYPEPFVYMHPVSAGKRGIAENDLVKVFNTAGEVELRAKVTANV 698
Cdd:cd02780 2 PFILVTFKSNL-NSHRSANAPWLKEIKPENPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGV 69
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
635-695 |
5.72e-07 |
|
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: 48.76 E-value: 5.72e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524489867 635 TPHVQFGIHSQfiNLDWMQVFYPEPFVYMHPVSAGKRGIAENDLVKVFNTAGEVELRAKVT 695
Cdd:cd02792 13 TEHFHGGNMTR--NSPYLAELQPEMFVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVT 71
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
429-534 |
8.27e-07 |
|
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: 52.15 E-value: 8.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 429 TAKGILEANEP-PVRMLWVACKNPFaqDFDRSKMEKAFEKLEMVVCADQFFNETVQHADIVLPVTTAFEEwnvDASYwhy 507
Cdd:COG1034 320 DAAAILEAAEAgKLKALVLLGADPY--DLDPAAALAALAKADFVVVLDHFGSATAERADVVLPAAAFAEK---SGTF--- 391
|
90 100 110
....*....|....*....|....*....|....*
gi 2524489867 508 wlsINQ--------PAIKPMYEAKCDLEIAVLLSR 534
Cdd:COG1034 392 ---VNLegrvqrfnAAVPPPGEARPDWRVLRALAN 423
|
|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
639-706 |
1.00e-04 |
|
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: 42.45 E-value: 1.00e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 639 QFGIHSQfiNLDWMQVFYPEPFVYMHPVSAGKRGIAENDLVKVFNTAGEVELRAKVTANVP--EDFLVMY 706
Cdd:cd02779 15 QTAYHDQ--NNSEIAERVPLPYIEVNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKpgQTFMLMA 82
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
102-394 |
1.61e-04 |
|
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1), found in beta- and gammaproteobacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239173 [Multi-domain] Cd Length: 414 Bit Score: 44.65 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 102 VYSPDRIKYPMVqdvRGSGNWRRISWDEAMQRIATKMLEIKKKDG-SMLGLALTKYSgkfgvlnyAVEGMMsslgYTTRF 180
Cdd:cd02772 49 LNSEDRLTKPMI---KKDGQWQEVDWETALEYVAEGLSAIIKKHGaDQIGALASPHS--------TLEELY----LLQKL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 181 AgtpcwpAGIDAQNYDM--------------GDMWCNDP-EDMVKAKYIIIWGAN-----PAwcsMHTMkyIYQAREKGA 240
Cdd:cd02772 114 A------RGLGSDNIDHrlrqsdfrddakasGAPWLGMPiAEISELDRVLVIGSNlrkehPL---LAQR--LRQAVKKGA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 241 KVVVIDPLltqtaakADLYLRVRPGSDGALALGMARHLVDKGLvdqdfvnnyshgyAEFEEylrNNVTVEWASEIcGLSA 320
Cdd:cd02772 183 KLSAINPA-------DDDFLFPLSGKAIVAPSALANALAQVAK-------------ALAEE---KGLAVPDEDAK-VEAS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524489867 321 DVIRQLAEEFTAVNPATVWIGYGMQRHvNGGANVRAIDAFVA-MTG-NIGIEGGGAR------YGHLHTWGFNYNAMLQK 392
Cdd:cd02772 239 EEARKIAASLVSAERAAVFLGNLAQNH-PQAATLRALAQEIAkLTGaTLGVLGEGANsvgaylAGALPHGGLNAAAMLEQ 317
|
..
gi 2524489867 393 PP 394
Cdd:cd02772 318 PR 319
|
|
| FwdD |
COG1153 |
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion]; |
662-700 |
5.71e-04 |
|
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion];
Pssm-ID: 440767 [Multi-domain] Cd Length: 127 Bit Score: 40.60 E-value: 5.71e-04
10 20 30
....*....|....*....|....*....|....*....
gi 2524489867 662 YMHPVSAGKRGIAENDLVKVFNTAGEVELRAKVTANVPE 700
Cdd:COG1153 34 ELNPEDMKKLGIKEGDKVKVTSEYGEVVVKAKESEDLHP 72
|
|
| TAT_signal |
pfam10518 |
TAT (twin-arginine translocation) pathway signal sequence; |
8-32 |
1.25e-03 |
|
TAT (twin-arginine translocation) pathway signal sequence;
Pssm-ID: 463131 [Multi-domain] Cd Length: 26 Bit Score: 36.58 E-value: 1.25e-03
|
| |
