|
Name |
Accession |
Description |
Interval |
E-value |
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
16-773 |
0e+00 |
|
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: 1340.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 16 TTTCYMCACRCGIRVHLREGEVRYIDGNPEHPLNQGVICAKGASGIMKQYSPARLTQPLMRKPdaERGSAQFEPVSWEHA 95
Cdd:cd02763 1 TTTCYMCACRCGIRVHLRDGKVRYIKGNPDHPLNKGVICAKGSSGIMKQYSPARLTKPLLRKG--PRGSGQFEEIEWEEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 96 FDVLEKRLGEIRATDPKKFALFTGRDQMQALTGLFAKQFGTPNYAAHGGFCSANMAAGMIYTIGGSFWEFGGPDLDSAKL 175
Cdd:cd02763 79 FSIATKRLKAARATDPKKFAFFTGRDQMQALTGWFAGQFGTPNYAAHGGFCSVNMAAGGLYSIGGSFWEFGGPDLEHTKY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 176 FFMIGTAEDHHSNPLKIAISKFKRAGGRFIAINPIRTGYAAIADEWVPIKPGTDGALFMAFLHELIAADAWDHEFVRRYT 255
Cdd:cd02763 159 FMMIGVAEDHHSNPFKIGIQKLKRRGGKFVAVNPVRTGYAAIADEWVPIKPGTDGAFILALAHELLKAGLIDWEFLKRYT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 256 NAAELVDldeasenfglfvrdperpvgnplfpqnhlwwdaqaaravphhtpgvepaldgrytlddgtpvtpsfallrerv 335
Cdd:cd02763 239 NAAELVD------------------------------------------------------------------------- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 336 adCTPEWAAGITGISADTIRRLAGEMIQTSRDHRITLPIRWTDAWGETHETVTGNPVAFHAMRGLAAHSNGFQSIRALAV 415
Cdd:cd02763 246 --YTPEWVEKITGIPADTIRRIAKELGVTARDQPIELPIAWTDVWGRKHEKITGRPVSFHAMRGIAAHSNGFQTIRALFV 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 416 LMSLLGTIDTPGGFRHKSPFPRAVPPSAKPPNSPDAVKPNTPLATGPLGWPAAPEDLFIDEQGGPVRIDKAFSWEYPLAV 495
Cdd:cd02763 324 LMMLLGTIDRPGGFRHKPPYPRHIPPLPKPPKIPSADKPFTPLYGPPLGWPASPDDLLVDEDGNPLRIDKAYSWEYPLAA 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 496 HGLMHSVITNAWRGDPYPIDTLMIFMANMAWNSSMNTMKVREMLVDKHASGEYKIPFLVVCDAFQSEMTAFADLILPDTT 575
Cdd:cd02763 404 HGCMQNVITNAWRGDPYPIDTLMIYMANMAWNSSMNTPEVREMLTDKDASGNYKIPFIIVCDAFYSEMVAFADLVLPDTT 483
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 576 YLERHDAMSMLDRPISEFDGPVDSVRVPVVPPTGECKPFQEVLIELASRLKFPAFTTAEGARRYRDYPDFVVNFTTSPds 655
Cdd:cd02763 484 YLERHDAMSLLDRPISEADGPVDAIRVPIVEPKGDVKPFQEVLIELGTRLGLPGFTNEDGTRKYRDYPDFIVNFETTP-- 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 656 GVGFLIGWRGKDGDKALVGEPNPNQWEQYAKNNCVFHYRLPETLQYMRNCNGPYLEWAVKHGFRKFGEPILIQLYSDVMQ 735
Cdd:cd02763 562 GVGFLAGWRGKDGDKAFVGEPNPNQLEQYAKNNGFFHYPLPEHMRYYRNVNKDYLEWAVRVGFVKFTDPIIMQLYSEVLQ 641
|
730 740 750
....*....|....*....|....*....|....*...
gi 1588214711 736 KFRLAAQGRTSGRQPPDHLRARVEKYFDPLPFWYAPLE 773
Cdd:cd02763 642 KFRLAGQGLWEGEQPPEALRERVETYFDPLPFWYPPFE 679
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
5-927 |
1.12e-170 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 513.62 E-value: 1.12e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 5 ARTQDERLDIKTTTCYMCACRCGIRVHLREGEVRYIDGNPEHPLNQGVICAKGASGIMKQYSPARLTQPLMRKpdAERGS 84
Cdd:COG0243 14 AALEAAGTKTVKTTCPGCGVGCGLGVKVEDGRVVRVRGDPDHPVNRGRLCAKGAALDERLYSPDRLTYPMKRV--GPRGS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 85 AQFEPVSWEHAFDVLEKRLGEIRAT-DPKKFALFTGRDQMQALTG-------LFAKQFGTPNYAAHGGFCSANMAAGMIY 156
Cdd:COG0243 92 GKFERISWDEALDLIAEKLKAIIDEyGPEAVAFYTSGGSAGRLSNeaaylaqRFARALGTNNLDDNSRLCHESAVAGLPR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 157 TIGGSFWEFGGPDLDSAKLFFMIGTAEDHHSNPLKIAISKF-KRAGGRFIAINPIRTGYAAIADEWVPIKPGTDGALFMA 235
Cdd:COG0243 172 TFGSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREAaKKRGAKIVVIDPRRTETAAIADEWLPIRPGTDAALLLA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 236 FLHELIAADAWDHEFVRRYTNAaelvdldeasenfglfvrdperpvgnplfpqnhlwwdaqaaravphhtpgvepaldgr 315
Cdd:COG0243 252 LAHVLIEEGLYDRDFLARHTVG---------------------------------------------------------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 316 ytlddgtpvtpsFALLRERVADCTPEWAAGITGISADTIRRLAGEMIQTsrdhritlpirwtdawgethetvtgNPVAFH 395
Cdd:COG0243 274 ------------FDELAAYVAAYTPEWAAEITGVPAEDIRELAREFATA-------------------------KPAVIL 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 396 AMRGLAAHSNGFQSIRALAVLMSLLGTIDTPGGFRHKSPFpravppsakppnspDAVKpntplatgplgwpaapedlfid 475
Cdd:COG0243 317 WGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGGPFSLTG--------------EAIL---------------------- 360
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 476 eqggpvridkafsweyplavhglmhsvitnawRGDPYPIDTLMIFMANMAWnSSMNTMKVREMLvdkhasgeYKIPFLVV 555
Cdd:COG0243 361 --------------------------------DGKPYPIKALWVYGGNPAV-SAPDTNRVREAL--------RKLDFVVV 399
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 556 CDAFQSEMTAFADLILPDTTYLERHDAMSMldrpiseFDGPVDSVRVPVVPPTGECKPFQEVLIELASRLKFP-AFTTAE 634
Cdd:COG0243 400 IDTFLTETARYADIVLPATTWLERDDIVTN-------SEDRRVHLSRPAVEPPGEARSDWEIFAELAKRLGFEeAFPWGR 472
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 635 GARRYRDYpdfvvnfttspdsgvgFLIGWRGKDGDkalvgepnpnqWEQYAKNNcVFHYRLPETLQYMRNcngpylewav 714
Cdd:COG0243 473 TEEDYLRE----------------LLEATRGRGIT-----------FEELREKG-PVQLPVPPEPAFRND---------- 514
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 715 khgfRKFGEPiliqlySdvmQKFRLAAQgrtsgrqppdhlrarvEKYFDPLPFWYAPLESAATDLDQFPLAAVTQRPMAM 794
Cdd:COG0243 515 ----GPFPTP------S---GKAEFYSE----------------TLALPPLPRYAPPYEGAEPLDAEYPLRLITGRSRDQ 565
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 795 YHSWDSQNAWLRQIHGENYLYMNPLMAAENGIADGAWIYAESQWGRVRCMARFSETVEPGTVWTWNaigkasGAWNlgpg 874
Cdd:COG0243 566 WHSTTYNNPRLREIGPRPVVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTEGIRPGVVFAPH------GWWY---- 635
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 1588214711 875 ANESQRGFLLNHLITDelpgrdddvarrmsNSDPVTGQAAWYDVRVRIYPAEA 927
Cdd:COG0243 636 EPADDKGGNVNVLTPD--------------ATDPLSGTPAFKSVPVRVEKAAA 674
|
|
| MopB_CT_2 |
cd02783 |
The MopB_CT_2 CD includes a group of related uncharacterized bacterial and archaeal ... |
781-937 |
1.40e-90 |
|
The MopB_CT_2 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: 239184 [Multi-domain] Cd Length: 156 Bit Score: 285.12 E-value: 1.40e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 781 QFPLAAVTQRPMAMYHSWDSQNAWLRQIHGENYLYMNPLMAAENGIADGAWIYAESQWGRVRCMARFSETVEPGTVWTWN 860
Cdd:cd02783 1 QYPLTAFTQRPMAMYHSWGSQNAWLRQIHTRNYLYMHPKTAKELGIKDGDWVWVESVNGRVKGQARFTETVEPGTVWTWN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1588214711 861 AIGKASGAWNLGPGANESQRGFLLNHLITDELPGRDDdvARRMSNSDPVTGQAAWYDVRVRIYPAEADAR-HTLPQFA 937
Cdd:cd02783 81 AIGKRPGAWGLKPDAPESVKGFLLNHLINDSLPPPGD--AKRISNSDPVTGQAAWFDLRVRIVKAADSEQqETQPQFT 156
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
17-631 |
3.60e-81 |
|
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: 270.71 E-value: 3.60e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 17 TTCYMCACRCGIRVHLREGEVRYIDGNPEHPLNQGVICAKGASGIMKQYSPARLTQPLMRKpdAERGSAQFEPVSWEHAF 96
Cdd:cd02755 3 SICEMCSSRCGILARVEDGRVVKIDGNPLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRV--GERGEGKFREASWDEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 97 DVLEKRLGEIRATDPKKFALFTGRDQ-MQALTGLFAKQFGTPNYAAHGGFCSANMAAG---MIYTIGGSFwefgGPDLDS 172
Cdd:cd02755 81 QYIASKLKEIKEQHGPESVLFGGHGGcYSPFFKHFAAAFGSPNIFSHESTCLASKNLAwklVIDSFGGEV----NPDFEN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 173 AKLFFMIGT--AEDHHsNPLKIAISKFKRAGGRFIAINPIRTGYAAIADEWVPIKPGTDGALFMAFLHELIAADAWDHEF 250
Cdd:cd02755 157 ARYIILFGRnlAEAII-VVDARRLMKALENGAKVVVVDPRFSELASKADEWIPIKPGTDLAFVLALIHVLISENLYDAAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 251 VRRYTNAaelvdldeasenfglfvrdperpvgnplfpqnhlwwdaqaaravphhtpgvepaldgrytlddgtpvtpsFAL 330
Cdd:cd02755 236 VEKYTNG----------------------------------------------------------------------FEL 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 331 LRERVADCTPEWAAGITGISADTIRRLAGEMIQTSRdhRITLPIRWTDAWGethetvtgnpvafhamrglaahSNGFQSI 410
Cdd:cd02755 246 LKAHVKPYTPEWAAQITDIPADTIRRIAREFAAAAP--HAVVDPGWRGTFY----------------------SNSFQTR 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 411 RALAVLMSLLGTIDTPGGFrhkspfpravPPSAKPPnspdavkpntplatgplgwpaapedlfideqggpvridkafswe 490
Cdd:cd02755 302 RAIAIINALLGNIDKRGGL----------YYAGSAK-------------------------------------------- 327
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 491 yplavhglmhsvitnawrgdPYPIDTLMIFMANMAwNSSMNTMKVREMLVdkhasgeyKIPFLVVCDAFQSEMTAFADLI 570
Cdd:cd02755 328 --------------------PYPIKALFIYRTNPF-HSMPDRARLIKALK--------NLDLVVAIDILPSDTALYADVI 378
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1588214711 571 LPDTTYLERHDamsmldrPISEFDGPVDSV--RVPVVPPTGECKPFQEVLIELASRL-KFPAFT 631
Cdd:cd02755 379 LPEATYLERDE-------PFSDKGGPAPAVatRQRAIEPLYDTRPGWDILKELARRLgLFGTPS 435
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
17-640 |
8.85e-76 |
|
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: 258.14 E-value: 8.85e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 17 TTCYMCACRCGIRVHLREGEVRYIDGNPEHPLNQGVICAKGASGIMKQYSPARLTQPLMRK-PDAERG-SAQFEPVSWEH 94
Cdd:cd02757 4 STCQGCTAWCGLQAYVEDGRVTKVEGNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRTnPRKGRDvDPKFVPISWDE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 95 AFDVLEKRLGEIRATD-PKKFALFTGR--DQMQALTGLFAKQFGTPNYAAHGGFCSANMAAGMIYTIGGsfWEFGGPDLD 171
Cdd:cd02757 84 ALDTIADKIRALRKENePHKIMLHRGRygHNNSILYGRFTKMIGSPNNISHSSVCAESEKFGRYYTEGG--WDYNSYDYA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 172 SAKLFFMIGTA--EDHHSNPLKIAISKFKRAGGRFIAINPIRTGYAAIADEWVPIKPGTDGALFMAFLHELIAADAWDHE 249
Cdd:cd02757 162 NAKYILFFGADplESNRQNPHAQRIWGGKMDQAKVVVVDPRLSNTAAKADEWLPIKPGEDGALALAIAHVILTEGLWDKD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 250 FVRRYTNAAElvdldeasenfgLFVrdPERPVGNPLFPqnhlwwdaqaaravPHHTPGVEPAldgrytlddgtpvtpsfa 329
Cdd:cd02757 242 FVGDFVDGKN------------YFK--AGETVDEESFK--------------EKSTEGLVKW------------------ 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 330 lLRERVADCTPEWAAGITGISADTIRRLAGEMIQtsrdhritlpirwtdawgethetvTGNPVAFHAMRGLAAHSNGFQS 409
Cdd:cd02757 276 -WNLELKDYTPEWAAKISGIPAETIERVAREFAT------------------------AAPAAAAFTWRGATMQNRGSYN 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 410 IRALAVLMSLLGTIDTPGGfrhkspfpravppsakppnspdavkpntplaTGPlgwpaapedlfideQGGPVRIDKAFSW 489
Cdd:cd02757 331 SMACHALNGLVGSIDSKGG-------------------------------LCP--------------NMGVPKIKVYFTY 365
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 490 EYPLavhglmhsVITNAwrgdpypidtlmifmANMAWNSSMntmkvremlvdkhasgeYKIPFLVVCDAFQSEMTAFADL 569
Cdd:cd02757 366 LDNP--------VFSNP---------------DGMSWEEAL-----------------AKIPFHVHLSPFMSETTYFADI 405
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1588214711 570 ILPDTTYLERHDAMSMldrpiSEFDGPVDSVRVPVVPPTGECKPFQEVLIELASRLKFPAFttaEGARRYR 640
Cdd:cd02757 406 VLPDGHHFERWDVMSQ-----ENNLHPWLSIRQPVVKSLGEVREETEILIELAKKLDPKGS---DGMKRYA 468
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
17-625 |
9.19e-76 |
|
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: 253.40 E-value: 9.19e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 17 TTCYMCACRCGIRVHLREGEVRYIDGNPEHPLNQGVICAKGASGIMKQYSPARLTQPLMRKPdaerGSAQFEPVSWEHAF 96
Cdd:cd00368 2 SVCPFCGVGCGILVYVKDGKVVRIEGDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVG----GRGKFVPISWDEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 97 DVLEKRLGEIRAT-DPKKFALFTGRDQM---QALTGLFAKQFGTPNYAAHGGFCSANMAAGMIYtIGGSFWEFGGPDLDS 172
Cdd:cd00368 78 DEIAEKLKEIREKyGPDAIAFYGGGGASneeAYLLQKLLRALGSNNVDSHARLCHASAVAALKA-FGGGAPTNTLADIEN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 173 AKLFFMIGT--AEDHhsNPLKIAISKFKRAGGRFIAINPIRTGYAAIADEWVPIKPGTDGALFMAflheliaadawdhef 250
Cdd:cd00368 157 ADLILLWGSnpAETH--PVLAARLRRAKKRGAKLIVIDPRRTETAAKADEWLPIRPGTDAALALA--------------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 251 vrrytnaaelvdldeasenfglfvrdperpvgnplfpqnhlwwdaqaaravphhtpgvepaldgrytlddgtpvtpsfal 330
Cdd:cd00368 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 331 lrervadctpEWAAGITGISADTIRRLAGEMIQTsrdhritlpirwtdawgethetvtgNPVAFHAMRGLAAHSNGFQSI 410
Cdd:cd00368 220 ----------EWAAEITGVPAETIRALAREFAAA-------------------------KRAVILWGMGLTQHTNGTQNV 264
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 411 RALAVLMSLLGTIDTPGGfrhkspfpravppsakppnspdavkpntplatgplgwpaapedlfideqggpvridkafswe 490
Cdd:cd00368 265 RAIANLAALTGNIGRPGG-------------------------------------------------------------- 282
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 491 yplavhglmhsvitnawrgdpypidtLMIFMANMAWNSSmNTMKVREMLvdkhasgeYKIPFLVVCDAFQSEMTAFADLI 570
Cdd:cd00368 283 --------------------------GLGPGGNPLVSAP-DANRVRAAL--------KKLDFVVVIDIFMTETAAYADVV 327
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1588214711 571 LPDTTYLERHDAMSMLDRPISEFDgpvdsvrvPVVPPTGECKPFQEVLIELASRL 625
Cdd:cd00368 328 LPAATYLEKEGTYTNTEGRVQLFR--------QAVEPPGEARSDWEILRELAKRL 374
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
17-858 |
2.68e-71 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 250.19 E-value: 2.68e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 17 TTCYMCACRCGIRVHLREGEVRYIDGNPEHPLNQGVICAKGASGIMKQYSPARLTQPLMRKPDaergsaQFEPVSWEHAF 96
Cdd:COG3383 9 TVCPYCGVGCGIDLEVKDGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVNSPDRLTTPLIRRGG------EFREVSWDEAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 97 DVLEKRLGEIRATD-PKKFALFTGrDQM----QALTGLFAKQ-FGTPNYAAHGGFCSANMAAGMIYTIGGSFWEFGGPDL 170
Cdd:COG3383 83 DLVAERLREIQAEHgPDAVAFYGS-GQLtneeNYLLQKLARGvLGTNNIDNNARLCMASAVAGLKQSFGSDAPPNSYDDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 171 DSAKLFFMIG--TAEDHhsnPlkIAISKFKRA---GGRFIAINPIRTGYAAIADEWVPIKPGTDGALFMAFLHELIAADA 245
Cdd:COG3383 162 EEADVILVIGsnPAEAH---P--VLARRIKKAkknGAKLIVVDPRRTETARLADLHLQIKPGTDLALLNGLLHVIIEEGL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 246 WDHEFVRRYTNAaelvdldeasenfglfvrdperpvgnplfpqnhlwwdaqaaravphhtpgvepaldgrytlddgtpvt 325
Cdd:COG3383 237 VDEDFIAERTEG-------------------------------------------------------------------- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 326 psFALLRERVADCTPEWAAGITGISADTIRRLAgEMIQTSrdhritlpirwtdawgethetvtGNPVAFHAMrGLAAHSN 405
Cdd:COG3383 249 --FEELKASVAKYTPERVAEITGVPAEDIREAA-RLIAEA-----------------------KRAMILWGM-GVNQHTQ 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 406 GFQSIRALAVLMSLLGTIDTPGGfrhkSPFP-R-------AVPPSAKPPNSPDAVKPNTPLATGPLG--WPAAPedlfID 475
Cdd:COG3383 302 GTDNVNAIINLALATGNIGRPGT----GPFPlTgqnnvqgGRDMGALPNVLPGYRDVTDPEHRAKVAdaWGVPP----LP 373
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 476 EQGGpvridkafsweypLAVHGLMHSVItnawRGDpypIDTLMIFMANMAwNSSMNTMKVREMLVdkhasgeyKIPFLVV 555
Cdd:COG3383 374 DKPG-------------LTAVEMFDAIA----DGE---IKALWIIGENPA-VSDPDANHVREALE--------KLEFLVV 424
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 556 CDAFQSEMTAFADLILPDTTYLERHDAMSMLDRPISefdgpvdsvRV-PVVPPTGECKPFQEVLIELASRLKFP-AFTTA 633
Cdd:COG3383 425 QDIFLTETAEYADVVLPAASWAEKDGTFTNTERRVQ---------RVrKAVEPPGEARPDWEIIAELARRLGYGfDYDSP 495
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 634 EGARR-YRdypdfvvnfTTSPD-SGVGFligwrgkdgdkALVGEPNPNQWeqyaknncvfhyrlPetlqymrnCNGPYLE 711
Cdd:COG3383 496 EEVFDeIA---------RLTPDySGISY-----------ERLEALGGVQW--------------P--------CPSEDHP 533
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 712 wavkhgfrkfGEPIliqLYSDvmqKFRLAaqgrtSGrqppdhlRARvekyFDPLPfWYAPLESAAtdlDQFPLAAVTQRP 791
Cdd:COG3383 534 ----------GTPR---LFTG---RFPTP-----DG-------KAR----FVPVE-YRPPAELPD---EEYPLVLTTGRL 577
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 792 MAMYHSwDSQNAW---LRQIHGENYLYMNPLMAAENGIADGAWIYAESQWGRVRCMARFSETVEPGTVWT 858
Cdd:COG3383 578 LDQWHT-GTRTRRsprLNKHAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGEVVLRARVTDRVRPGTVFM 646
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
17-625 |
5.34e-67 |
|
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: 239.87 E-value: 5.34e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 17 TTCYMCACRCGIRVH-LREGEVRYIDGNPE----HPlNQGVICAKGASGIMKQYSPARLTQPlMRKPDAERGSAQ---FE 88
Cdd:cd02760 2 TYCYNCVAGPDFMAVkVVDGVATEIEPNFAaediHP-ARGRVCVKAYGLVQKTYNPNRVLQP-MKRTNPKKGRNEdpgFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 89 PVSWEHAFDVLEKRLGEIRATD-------PKKFALF----TGRDQMQALTGLFAKqFGTPNYAAHGGFCSANMAAGMIYt 157
Cdd:cd02760 80 PISWDEALDLVAAKLRRVREKGlldekglPRLAATFghggTPAMYMGTFPAFLAA-WGPIDFSFGSGQGVKCVHSEHLY- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 158 igGSFWEFG---GPDLDSAKLFFMIGTAEDHHSNPLKIAISKFKRAGG-RFIAINPIRTGYAAIADEWVPIKPGTDGALF 233
Cdd:cd02760 158 --GEFWHRAftvAADTPLANYVISFGSNVEASGGPCAVTRHADARVRGyKRVQVEPHLSVTGACSAEWVPIRPKTDPAFM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 234 MAFLHELI---AADAWDHEFVRRYTNAAELVDLDeasenfGLFVRDPerPVGNPLFpqnhlwWDAQAARAVPHHTPGVEP 310
Cdd:cd02760 236 FAMIHVMVheqGLGKLDVPFLRDRTSSPYLVGPD------GLYLRDA--ATGKPLV------WDERSGRAVPFDTRGAVP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 311 ALDGRYTLD--------------DGTPVTPSFALLRERVADCTPEWAAGITGISADTIRRLAGEMIQTSRDHR------I 370
Cdd:cd02760 302 AVAGDFAVDgavsvdaddetaihQGVEGTTAFTMLVEHMRKYTPEWAESICDVPAATIRRIAREFLENASIGStievdgV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 371 TLPIRwtdawgethetvtgnPVAFHAMRGLAAHSNGFQSIRALAVLMSLLGTIDTPG---GFRHKSPFPRAVPPSAKPPN 447
Cdd:cd02760 382 TLPYR---------------PVAVTLGKSVNNGWGAFECCWARTLLATLVGALEVPGgtlGTTVRLNRPHDDRLASVKPG 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 448 SPDAVKPNTPLaTGPLGWPAAPEDLFIDEQGGPVRIDKAFSWEYPLAVHGLMHSVITNAWRG--DPYPIDTLMIFMANMA 525
Cdd:cd02760 447 EDGFMAQGFNP-TDKEHWVVKPTGRNAHRTLVPIVGNSAWSQALGPTQLAWMFLREVPLDWKfeLPTLPDVWFNYRTNPA 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 526 ---WNSSmntmkvreMLVDKHAsgeyKIPFLVVCDAFQSEMTAFADLILPDTTYLERHDAMSMLDRPISEFDGPVDSV-- 600
Cdd:cd02760 526 isfWDTA--------TLVDNIA----KFPFTVSFAYTEDETNWMADVLLPEATDLESLQMIKVGGTKFVEQFWEHRGVvl 593
|
650 660
....*....|....*....|....*
gi 1588214711 601 RVPVVPPTGECKPFQEVLIELASRL 625
Cdd:cd02760 594 RQPAVEPQGEARDFTWISTELAKRT 618
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
19-868 |
3.34e-62 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 225.70 E-value: 3.34e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 19 CYMCACRCGIRVHLREGEVRYIDGNPEHPLNQGVICAKGASGIMKQYSPARLTQPLMRKpdAERGSAQFEPVSWEHAFDV 98
Cdd:PRK15488 48 CEMCSTRCPIEARVVNGKNVFIQGNPKAKSFGTKVCARGGSGHSLLYDPQRIVKPLKRV--GERGEGKWQEISWDEAYQE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 99 LEKRLGEIRAT-DPKKFAlFTGRD-QMQALTGLFAKQFGTPNYAAHGGFCSA--NMAAGMIYtiGGSFwefgGPDLDSAK 174
Cdd:PRK15488 126 IAAKLNAIKQQhGPESVA-FSSKSgSLSSHLFHLATAFGSPNTFTHASTCPAgyAIAAKVMF--GGKL----KRDLANSK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 175 --------LFFMIGTAEDHHSnpLKIAISKfkraGGRFIAINPIRTGYAAIADEWVPIKPGTDGALFMAFLHELIAADAW 246
Cdd:PRK15488 199 yiinfghnLYEGINMSDTRGL--MTAQMEK----GAKLVVFEPRFSVVASKADEWHAIRPGTDLAVVLALCHVLIEENLY 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 247 DHEFVRRYTnaaelvdldeasenfglfvrdperpVGnplfpqnhlwwdaqaaravphhtpgvepaldgrytlddgtpvtp 326
Cdd:PRK15488 273 DKAFVERYT-------------------------SG-------------------------------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 327 sFALLRERVADCTPEWAAGITGISADTIRRLAGEmIQTSRDHRITlpirwtdAWGetHETvTGNPVAFHaMRglaahsng 406
Cdd:PRK15488 284 -FEELAASVKEYTPEWAEAISDVPADDIRRIARE-LAAAAPHAIV-------DFG--HRA-TFTPEEFD-MR-------- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 407 fqsiRALAVLMSLLGTIDTPGG--FRHKSPF-----PRAVPPSAKPPNSPDAVKPNTPlatgplgwpaapedlfideqgg 479
Cdd:PRK15488 343 ----RAIFAANVLLGNIERKGGlyFGKNASVynklaGEKVAPTLAKPGVKGMPKPTAK---------------------- 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 480 pvRIDKAF-SWEYPLAVHGLMHSVITNAWRGDPYPIDTLMifmanMAWNSSMNTMKVREMLVDKHAsgeyKIPFLVVCDA 558
Cdd:PRK15488 397 --RIDLVGeQFKYIAAGGGVVQSIIDATLTQKPYQIKGWV-----MSRHNPMQTVTDRADVVKALK----KLDLVVVCDV 465
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 559 FQSEMTAFADLILPDTTYLERhdamsmlDRPISEFDG--PVDSVRVPVVPPTGECKPFQEVLIELASRLKFPAFTTAEGA 636
Cdd:PRK15488 466 YLSESAAYADVVLPESTYLER-------DEEISDKSGknPAYALRQRVVEPIGDTKPSWQIFKELGEKMGLGQYYPWQDM 538
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 637 RRYRDYPdfvvnfttspdsgvgfligwrgKDGDKALVGEPNPNQWEQYAK----------NNCVFHYrlPETLQymRNCN 706
Cdd:PRK15488 539 ETLQLYQ----------------------VNGDHALLKELKKKGYVSFGVplllrepkmvAKFVARY--PNAKA--VDED 592
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 707 GPYLEWAvkhgfrKFGEPI-LIQLYSDVMQKFrlaAQGRTSGRQPPDHLRARVEKYFdplpfwyaplesaatdldqfpla 785
Cdd:PRK15488 593 GTYGSQL------KFKTPSgKIELFSAKLEAL---APGYGVPRYRDVALKKEDELYF----------------------- 640
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 786 avTQRPMAMYHSWDSQNA-WLRQIHGENYLYMNPLMAAENGIADGAWIYAESQWGRVRCMARFSETVEPGTVWTWNAIGK 864
Cdd:PRK15488 641 --IQGKVAVHTNGATQNVpLLANLMSDNAVWIHPQTAGKLGIKNGDEIRLENSVGKEKGKALVTPGIRPDTLFAYMGFGS 718
|
....
gi 1588214711 865 ASGA 868
Cdd:PRK15488 719 KNKE 722
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
16-625 |
1.57e-61 |
|
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239160 [Multi-domain] Cd Length: 477 Bit Score: 217.17 E-value: 1.57e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 16 TTTCYMCACRCGIRVHLREGEVRYIDGNPEHPLNQGVICAKGASGIMKQYSPARLTQPLMRKpdAERGSAQFEPVSWEHA 95
Cdd:cd02759 1 KGTCPGCHSGCGVLVYVKDGKLVKVEGDPNHPTNKGRLCMRGLAAPEIVYHPDRLLYPLKRV--GERGENKWERISWDEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 96 FDVLEKRLGEIRATDPKK---FALFTGRDQMQALTGL---FAKQFGTPNYAAHGGFCSANMAAGMIYTIGGSfWEFGGPD 169
Cdd:cd02759 79 LDEIAEKLAEIKAEYGPEsiaTAVGTGRGTMWQDSLFwirFVRLFGSPNLFLSGESCYWPRDMAHALTTGFG-LGYDEPD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 170 LDSAKLFFMIG-TAEDHHSNPLKIAISKFKRAGGRFIAINPIRTGYAAIADEWVPIKPGTDGALFMAFLHELIAADAWDH 248
Cdd:cd02759 158 WENPECIVLWGkNPLNSNLDLQGHWLVAAMKRGAKLIVVDPRLTWLAARADLWLPIRPGTDAALALGMLNVIINEGLYDK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 249 EFVRRYTNAaelvdldeasenfglfvrdperpvgnplfpqnhlwwdaqaaravphhtpgvepaldgrytlddgtpvtpsF 328
Cdd:cd02759 238 DFVENWCYG----------------------------------------------------------------------F 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 329 ALLRERVADCTPEWAAGITGISADTIRRLAgEMIQTSRDHRItlpirwtdAWGethetvtgnpvafhamRGLAAHSNGFQ 408
Cdd:cd02759 248 EELAERVQEYTPEKVAEITGVPAEKIRKAA-RLYATAKPACI--------QWG----------------LAIDQQKNGTQ 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 409 SIRALAVLMSLLGTIDTPGGfrhkspfpravppsakppnspdavkpntplatgplgwpaapeDLFIdeqggpvridkafs 488
Cdd:cd02759 303 TSRAIAILRAITGNLDVPGG------------------------------------------NLLI-------------- 326
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 489 weyplavhglmhsvitnawrgdPYPIDTLMIFMANMAwNSSMNTMKVREMLVdkhasgeyKIPFLVVCDAFQSEMTAFAD 568
Cdd:cd02759 327 ----------------------PYPVKMLIVFGTNPL-ASYADTAPVLEALK--------ALDFIVVVDLFMTPTAMLAD 375
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1588214711 569 LILPDTTYLERHDAMSMldrpiSEFDGPVdSVRVPVVPPTGECKPFQEVLIELASRL 625
Cdd:cd02759 376 IVLPVAMSLERPGLRGG-----FEAENFV-QLRQKAVEPYGEAKSDYEIVLELGKRL 426
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
17-630 |
3.98e-58 |
|
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: 213.74 E-value: 3.98e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 17 TTCYMCACRCGIRVHL--REGEVRYIDGNPEHPLNQ---------------------------GVICAKGASGIMKQYSP 67
Cdd:cd02758 2 SSCLGCWTQCGIRVRVdkETGKVLRIAGNPYHPLNTapslpyntplkeslylslvgenglkarATACARGNAGLQYLYDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 68 ARLTQPLMRkpDAERGSAQFEPVSWEHAFD-VLEK--------RLGEIRATDPKKFA----------------LFTGRDQ 122
Cdd:cd02758 82 YRVLQPLKR--VGPRGSGKWKPISWEQLIEeVVEGgdlfgeghVEGLKAIRDLDTPIdpdhpdlgpkanqllyTFGRDEG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 123 MQALTGLFAKQ-FGTPNYAAHGGFCS----ANMAAGMIYTIGGSFWEfggPDLDSAKLFFMIGTAEDHHSNPLKIA---- 193
Cdd:cd02758 160 RTPFIKRFANQaFGTVNFGGHGSYCGlsyrAGNGALMNDLDGYPHVK---PDFDNAEFALFIGTSPAQAGNPFKRQarrl 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 194 ISKFKRAGGRFIAINPI--RTGYAA-IADEWVPIKPGTDGALFMAFLHELIAADAWDHEFvrrytnaaelvdLDEASEnf 270
Cdd:cd02758 237 AEARTEGNFKYVVVDPVlpNTTSAAgENIRWVPIKPGGDGALAMAMIRWIIENERYNAEY------------LSIPSK-- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 271 glfvrdperpvgnplfpqnhlwwDAQAARAVPHHTPGVEPALDGRytlddgtpVTPSFALLRERVADCT-PEWAAgITGI 349
Cdd:cd02758 303 -----------------------EAAKAAGEPSWTNATHLVITVR--------VKSALQLLKEEAFSYSlEEYAE-ICGV 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 350 SADTIRRLAGEMiqtsRDHritlpirwtdawgethetvtGNPVAFHAmRGLAAHSNGFQSIRALAVLMSLLGTIDTPGGF 429
Cdd:cd02758 351 PEAKIIELAKEF----TSH--------------------GRAAAVVH-HGGTMHSNGFYNAYAIRMLNALIGNLNWKGGL 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 430 RHK-SPFpravPPSAKPPNSPDAVKPNTPlatGPLGWPAAPEDlFIDEQGGPVRIDKAFS---------WeYPLAVhGLM 499
Cdd:cd02758 406 LMSgGGF----ADNSAGPRYDFKKFFGEV---KPWGVPIDRSK-KAYEKTSEYKRKVAAGenpypakrpW-YPLTP-ELY 475
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 500 HSVITNAWRGDPYPIDTLMIFMANMAWNSSMNTMKVREMLVDkhasgEYKIPFLVVCDAFQSEMTAFADLILPDTTYLER 579
Cdd:cd02758 476 TEVIASAAEGYPYKLKALILWMANPVYGAPGLVKQVEEKLKD-----PKKLPLFIAIDAFINETSAYADYIVPDTTYYES 550
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1588214711 580 HD-AMSMLDRPIsefdgPVDSVRVPVVPP------TGECKPFQEVLIELASRLKFPAF 630
Cdd:cd02758 551 WGfSTPWGGVPT-----KASTARWPVIAPltektaNGHPVSMESFLIDLAKALGLPGF 603
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
22-654 |
7.00e-52 |
|
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: 191.92 E-value: 7.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 22 CACRCGIRVHLREGEVRYIDGN----PEHPlnqgVICAKGASGIMKQYSPARLTQPLMRKpdAERGSAQFEPVSWEHAFD 97
Cdd:cd02765 8 CGGRCPLKCHVRDGKIVKVEPNewpdKTYK----RGCTRGLSHLQRVYSPDRLKYPMKRV--GERGEGKFERITWDEALD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 98 VLEKRLGEI-RATDPKKFALFTGRDQMQALTGLFAKQFGTPNYAAHGGFCSANMAAGMIYTIGGSFwEFGG---PDLDSA 173
Cdd:cd02765 82 TIADKLTEAkREYGGKSILWMSSSGDGAILSYLRLALLGGGLQDALTYGIDTGVGQGFNRVTGGGF-MPPTneiTDWVNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 174 KLFFMIGtaedhhSNPLKIAIS------KFKRAGGRFIAINPIRTGYAAIADEWVPIKPGTDGALFMAFLHELIAADAWD 247
Cdd:cd02765 161 KTIIIWG------SNILETQFQdaefflDARENGAKIVVIDPVYSTTAAKADQWVPIRPGTDPALALGMINYILEHNWYD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 248 HEFVRRYTNAAELVDLDEasenfGLFVRDPERPVGNPlfPQNHLWWDAQAARAVPHHTPGVEPALDGRYTLdDGTPVTPS 327
Cdd:cd02765 235 EAFLKSNTSAPFLVREDN-----GTLLRQADVTATPA--EDGYVVWDTNSDSPEPVAATNINPALEGEYTI-NGVKVHTV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 328 FALLRERVADCTPEWAAGITGISADTIRRLagemiqtsrdhritlpirwtdawgeTHETVTGNPVAFHAMRGLAAHSNGF 407
Cdd:cd02765 307 LTALREQAASYPPKAAAEICGLEEAIIETL-------------------------AEWYATGKPSGIWGFGGVDRYYHSH 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 408 QSIRALAVLMSLLGTIDTPGGFrhkspfpravppsakppnspdavkpntplatgplgwpaapedlfideqggpvridkaf 487
Cdd:cd02765 362 VFGRTAAILAALTGNIGRVGGG---------------------------------------------------------- 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 488 sweyplavhglmHSVITNAWrgdpypidtlmiFMANMAWNssmntmkvreMLVDKHASGEY--KIPFLVVCDAFQSEMTA 565
Cdd:cd02765 384 ------------VGQIKFMY------------FMGSNFLG----------NQPDRDRWLKVmkNLDFIVVVDIFHTPTVR 429
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 566 FADLILPDTTYLERHDAMSMLDrpisefDGPVDSVRVPVVPPTGECKPFQEVLIELASRL----KFPafttaegarryRD 641
Cdd:cd02765 430 YADIVLPAAHWFEVEDLLVRYT------THPHVLLQQKAIEPLFESKSDFEIEKGLAERLglgdYFP-----------KT 492
|
650
....*....|...
gi 1588214711 642 YPDFVVNFTTSPD 654
Cdd:cd02765 493 PEDYVRAFMNSDD 505
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
19-629 |
4.43e-51 |
|
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: 187.84 E-value: 4.43e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 19 CYMCacrCGIRVHLREGEVRYIDGNPEHPLNQGVICAKGASGIMKQYSPARLTQPLMRKpdaERGSAQFEPVSWEHAFDV 98
Cdd:cd02766 8 CPDT---CSLLVTVEDGRIVRVEGDPAHPYTRGFICAKGARYVERVYSPDRLLTPLKRV---GRKGGQWERISWDEALDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 99 LEKRLGEIRATD------PKKFALFTG---RDQMQALTGL--FAKQFGTPnyaahggfCSANMAAGMIYTIGgSFWEFGG 167
Cdd:cd02766 82 IAAKLKEIKAEYgpesilPYSYAGTMGllqRAARGRFFHAlgASELRGTI--------CSGAGIEAQKYDFG-ASLGNDP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 168 PDLDSAKLFFMIG---TAEDHHSNPLkiaISKFKRAGGRFIAINPIRTGYAAIADEWVPIKPGTDGALFMAFLHELIAAD 244
Cdd:cd02766 153 EDMVNADLIVIWGinpAATNIHLMRI---IQEARKRGAKVVVIDPYRTATAARADLHIQIRPGTDGALALGVAKVLFREG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 245 AWDHEFVRRYTnaaelVDLDEasenfglfvrdperpvgnplfpqnhlwwdaqaaravphhtpgvepaldgrytlddgtpv 324
Cdd:cd02766 230 LYDRDFLARHT-----EGFEE----------------------------------------------------------- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 325 tpsfalLRERVADCTPEWAAGITGISADTIRRLAGEmiqtsrdhritlpirwtdaWGEThetvtgNPVAFHAMRGLAAHS 404
Cdd:cd02766 246 ------LKAHLETYTPEWAAEITGVSAEEIEELARL-------------------YGEA------KPPSIRLGYGMQRYR 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 405 NGFQSIRALAVLMSLLGTIDTPGGfrhkspfpravppsakppnspdavkpntplatgplgwpaapedlfideqggpvrid 484
Cdd:cd02766 295 NGGQNVRAIDALPALTGNIGVPGG-------------------------------------------------------- 318
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 485 kafsweyplavhGLMHSvitnawRGDPyPIDTLMIFMANMAwNSSMNTMKVREMLVDKHasgeykiPFLVVCDAFQSEMT 564
Cdd:cd02766 319 ------------GAFYS------NSGP-PVKALWVYNSNPV-AQAPDSNKVRKGLARED-------LFVVVHDQFMTDTA 371
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1588214711 565 AFADLILPDTTYLERHDAM-SMLDRPIsefdgpvdSVRVPVVPPTGECKPFQEVLIELASRLKFPA 629
Cdd:cd02766 372 RYADIVLPATTFLEHEDVYaSYWHYYL--------QYNEPAIPPPGEARSNTEIFRELAKRLGFGE 429
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
22-631 |
1.80e-50 |
|
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase (DMSOR) of Escherichia coli and other related DMSOR-like enzymes. Unlike other DMSOR-like enzymes, this group has a predicted N-terminal iron-sulfur [4Fe-4S] cluster binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239171 [Multi-domain] Cd Length: 617 Bit Score: 188.69 E-value: 1.80e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 22 CACRCGIRVHLREGEVRYIDGNPEHPLNQGV----ICAKGASGIMKQYSPARLTQPLMRKPdaERGSAQFEPVSWEHAFD 97
Cdd:cd02770 8 CGGRCPLKAHVKDGVITRIETDDTGDDDPGFhqirACLRGRSQRKRVYNPDRLKYPMKRVG--KRGEGKFVRISWDEALD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 98 VLEKRLGEIR--------------ATDPKKFALFTGRDQMQALTGLFAKQFGTpnyaahggFCSANMAAGMIYTIGGSFW 163
Cdd:cd02770 86 TIASELKRIIekygneaiyvnygtGTYGGVPAGRGAIARLLNLTGGYLNYYGT--------YSWAQITTATPYTYGAAAS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 164 EFGGPDLDSAKLFFMIGtaedhhSNPLKIAISKF---------KRAGGRFIAINPIRTGYAA-IADEWVPIKPGTDGALF 233
Cdd:cd02770 158 GSSLDDLKDSKLVVLFG------HNPAETRMGGGgstyyylqaKKAGAKFIVIDPRYTDTAVtLADEWIPIRPGTDAALV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 234 MAFLHELIAADAWDHEFVRRYTnaaelvdldeasenfglfvrdperpVGnplfpqnhlwWDAQAAravPHHTPGVEPALD 313
Cdd:cd02770 232 AAMAYVMITENLHDQAFLDRYC-------------------------VG----------FDAEHL---PEGAPPNESYKD 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 314 grYTL---DDGTPVtpsfallrervadcTPEWAAGITGISADTIRRLAGEMIQTsrdhritlpirwtdawgethetvtgN 390
Cdd:cd02770 274 --YVLgtgYDGTPK--------------TPEWASEITGVPAETIRRLAREIATT-------------------------K 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 391 PVAFHAMRGLAAHSNGFQSIRALAVLMSLLGTIDTPGG----FRHKSPFPRAVPPSAKPPnspdaVKPNTPLatgplgwp 466
Cdd:cd02770 313 PAAILQGWGPQRHANGEQAARAIMMLAAMTGNVGIPGGntgaRPGGSAYNGAGLPAGKNP-----VKTSIPC-------- 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 467 aapedlfideqggpvridkaFSWeyplaVHGLMHSVITNAWRGDPYPIDTL-----MIFmaNMAWNSSMNTMKVREMLVD 541
Cdd:cd02770 380 --------------------FMW-----TDAIERGEEMTADDGGVKGADKLksnikMIW--NYAGNTLINQHSDDNNTTR 432
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 542 KHASGEYKIPFLVVCDAFqseMTA---FADLILPDTTYLERHDamsMLDrpiSEFDGPVDSVRV--PVVPPTGECKPFQE 616
Cdd:cd02770 433 ALLDDESKCEFIVVIDNF---MTPsarYADILLPDTTELERED---IVL---TSNAGMMEYLIYsqKAIEPLYECKSDYE 503
|
650
....*....|....*.
gi 1588214711 617 VLIELASRLKF-PAFT 631
Cdd:cd02770 504 ICAELAKRLGVeDQFT 519
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
16-636 |
1.53e-49 |
|
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: 185.12 E-value: 1.53e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 16 TTTCYMCACRCGIRVHLREGEVRYIDGNPEHPLNQGVICAKGASGIMKQYSPARLTQPLMRKPDAErgsaqFEPVSWEHA 95
Cdd:cd02754 1 KTTCPYCGVGCGVEIGVKDGKVVAVRGDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLLRRNGGE-----LVPVSWDEA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 96 FDVLEKRLGEIRAT-DPKKFALFTGRDQM---QALTGLFAKQF-GTPNYAAHGGFCSANMAAGMIYTIGgsfweFGGP-- 168
Cdd:cd02754 76 LDLIAERFKAIQAEyGPDSVAFYGSGQLLteeYYAANKLAKGGlGTNNIDTNSRLCMASAVAGYKRSFG-----ADGPpg 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 169 ---DLDSAKLFFMIG--TAEDHhsnP---LKIAISKFKRAGGRFIAINPIRTGYAAIADEWVPIKPGTDGALFMAFLHEL 240
Cdd:cd02754 151 sydDIEHADCFFLIGsnMAECH---PilfRRLLDRKKANPGAKIIVVDPRRTRTADIADLHLPIRPGTDLALLNGLLHVL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 241 IAADAWDHEFVRRYTNAaelvdldeasenfglfvrdperpvgnplfpqnhlwWDAqaaravphhtpgvepaldgrytldd 320
Cdd:cd02754 228 IEEGLIDRDFIDAHTEG-----------------------------------FEE------------------------- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 321 gtpvtpsfalLRERVADCTPEWAAGITGISADTIRRLAgEMIQTSRdhritlpiRWTDAWGethetvtgnpvafhamRGL 400
Cdd:cd02754 248 ----------LKAFVADYTPEKVAEITGVPEADIREAA-RLFGEAR--------KVMSLWT----------------MGV 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 401 AAHSNGFQSIRALAVLMSLLGTIDTPG-------------------GFRHKSPFPRAVppsakppNSPDAVKPNTPLatg 461
Cdd:cd02754 293 NQSTQGTAANNAIINLHLATGKIGRPGsgpfsltgqpnamggrevgGLANLLPGHRSV-------NNPEHRAEVAKF--- 362
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 462 plgWpAAPEDLFIDEQGgpvridkAFSWEYPLAVHglmhsvitnawRGDpypIDTLMIfMANMAWNSSMNTMKVREMLvd 541
Cdd:cd02754 363 ---W-GVPEGTIPPKPG-------LHAVEMFEAIE-----------DGE---IKALWV-MCTNPAVSLPNANRVREAL-- 414
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 542 khasgeYKIPFLVVCDAF-QSEMTAFADLILPDTTYLERHDAMSMLDRPIsefdgpvdSVRVPVVPPTGECKPFQEVLIE 620
Cdd:cd02754 415 ------ERLEFVVVQDAFaDTETAEYADLVLPAASWGEKEGTMTNSERRV--------SLLRAAVEPPGEARPDWWILAD 480
|
650
....*....|....*....
gi 1588214711 621 LASRLKFP---AFTTAEGA 636
Cdd:cd02754 481 VARRLGFGelfPYTSPEEV 499
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
23-631 |
1.13e-46 |
|
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: 177.42 E-value: 1.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 23 AC-RCGIRVHLREGEVRYIDGNPEHplnQGVICAKGASGIMKQYSPARLTQPLMRK--------PDAERGSAQFEPVSWE 93
Cdd:cd02751 3 AChWGPFKAHVKDGVIVRVEPDDTD---QPRPCPRGRSVRDRVYSPDRIKYPMKRVgwlgngpgSRELRGEGEFVRISWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 94 HAFDVLEKRLGEIRatdpKKF---ALFTGRDqmqalTGLFAKQFGTPN------YAAHGGFCS-------ANMAAGMIYT 157
Cdd:cd02751 80 EALDLVASELKRIR----EKYgneAIFGGSY-----GWASAGRLHHAQsllhrfLNLIGGYLGsygtystGAAQVILPHV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 158 IGGSFWEFGGPDLDS----AKLFFMIGtaedhhSNPLK--------------IAISKFKRAGGRFIAINPIRT-GYAAIA 218
Cdd:cd02751 151 VGSDEVYEQGTSWDDiaehSDLVVLFG------ANPLKtrqgggggpdhgsyYYLKQAKDAGVRFICIDPRYTdTAAVLA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 219 DEWVPIKPGTDGALFMAFLHELIAADAWDHEFVRRYTnaaelvdldeasenfglfvrdperpVGnplfpqnhlwWDaqaa 298
Cdd:cd02751 225 AEWIPIRPGTDVALMLAMAHTLITEDLHDQAFLARYT-------------------------VG----------FD---- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 299 RAVPHhtpgvepaLDGRytlDDGTPVtpsfallrervadcTPEWAAGITGISADTIRRLAGEMIQtsrdhritlpirwtd 378
Cdd:cd02751 266 EFKDY--------LLGE---SDGVPK--------------TPEWAAEITGVPAETIRALAREIAS--------------- 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 379 awgethetvtgNPVAFHAMRGLAAHSNGFQSIRALAVLMSLLGTIDTPG---GFR-HKSPF---PRAVPPSAKPPNSPDA 451
Cdd:cd02751 306 -----------KRTMIAQGWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGggfGFGyGYSNGggpPRGGAGGPGLPQGKNP 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 452 VKPNTPLATgplgWPAApedlfIDEQGGPVRIDKAfSWEYPlavhglmhsvitnawrgdpyPIDtlmifmanMAWNSSMN 531
Cdd:cd02751 375 VKDSIPVAR----IADA-----LLNPGKEFTANGK-LKTYP--------------------DIK--------MIYWAGGN 416
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 532 T---MKVREMLVDKHASGEykipFLVVCDAFqseMTA---FADLILPDTTYLERHDamsmldrpISEFDGPVDSVRVP-- 603
Cdd:cd02751 417 PlhhHQDLNRLIKALRKDE----TIVVHDIF---WTAsarYADIVLPATTSLERND--------IGLTGNYSNRYLIAmk 481
|
650 660 670
....*....|....*....|....*....|
gi 1588214711 604 -VVPPTGECKPFQEVLIELASRL-KFPAFT 631
Cdd:cd02751 482 qAVEPLGEARSDYEIFAELAKRLgVEEEFT 511
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
17-630 |
1.03e-44 |
|
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: 169.70 E-value: 1.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 17 TTCYMCACRCGIRVHLREGEVRYIDGNPEHPLNQGVICAKGASGIMKQYSPARLTQPLMRKPDAergsaqFEPVSWEHAF 96
Cdd:cd02753 2 TVCPYCGVGCGLELWVKDNKIVGVEPVKGHPVNRGKLCVKGRFGFDFVNSKDRLTKPLIRKNGK------FVEASWDEAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 97 DVLEKRLGEIRATdpkkfalfTGRDQMQALTG---------LFAK----QFGTPN--YAAHggFCSANMAAGMIYTIG-- 159
Cdd:cd02753 76 SLVASRLKEIKDK--------YGPDAIAFFGSakctneenyLFQKlaraVGGTNNvdHCAR--LCHSPTVAGLAETLGsg 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 160 ---GSFwefggPDLDSAKLFFMIG--TAEDHhsnPLkIA--ISKFKRAGGRFIAINPIRTGYAAIADEWVPIKPGTDGAL 232
Cdd:cd02753 146 amtNSI-----ADIEEADVILVIGsnTTEAH---PV-IArrIKRAKRNGAKLIVADPRRTELARFADLHLQLRPGTDVAL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 233 FMAFLHELIAADAWDHEFVRRYTnaaelvdldeasENFglfvrdperpvgnplfpqnhlwWDaqaaravphhtpgvepal 312
Cdd:cd02753 217 LNAMAHVIIEEGLYDEEFIEERT------------EGF----------------------EE------------------ 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 313 dgrytlddgtpvtpsfalLRERVADCTPEWAAGITGISADTIRRLAgEMIQTSRdhriTLPIRWtdawgethetvtgnpv 392
Cdd:cd02753 245 ------------------LKEIVEKYTPEYAERITGVPAEDIREAA-RMYATAK----SAAILW---------------- 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 393 afhAMrGLAAHSNGFQSIRALAVLMSLLGTIDTPGGfrhkspfprAVPPSAKPPNSpdavkpntplatgplgwpaapedl 472
Cdd:cd02753 286 ---GM-GVTQHSHGTDNVMALSNLALLTGNIGRPGT---------GVNPLRGQNNV------------------------ 328
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 473 fideQG----GpvridkAFSWEYPLAVHGLmhsvitnawrgdpYpidtlmIFMANMAWnSSMNTMKVREMLvdkhasgeY 548
Cdd:cd02753 329 ----QGacdmG------ALPNVLPGYVKAL-------------Y------IMGENPAL-SDPNTNHVRKAL--------E 370
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 549 KIPFLVVCDAFQSEMTAFADLILPDTTYLERHDAMSMLDRPISEFdgpvdsvrVPVVPPTGECKPFQEVLIELASRLKFP 628
Cdd:cd02753 371 SLEFLVVQDIFLTETAELADVVLPAASFAEKDGTFTNTERRVQRV--------RKAVEPPGEARPDWEIIQELANRLGYP 442
|
..
gi 1588214711 629 AF 630
Cdd:cd02753 443 GF 444
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
17-875 |
3.83e-44 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 173.64 E-value: 3.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 17 TTCYMCACRCGIRVH--LREGEVRYIDGNPEHPLNQ--------------------------GVICAKGASGIMKQYSPA 68
Cdd:PRK14991 77 TQCLGCWTQCGVRVRvdNATNKILRIAGNPYHPLSTdhhidmstpvkeafeslsgesglegrSTACARGNAMLEQLDSPY 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 69 RLTQPLMRKpdAERGSAQFEPVSWEHAFD-VLE----------KRLGEIRAT----DPKKFAL----------FTGRDQM 123
Cdd:PRK14991 157 RVLQPLKRV--GKRGSGKWQRISFEQLVEeVVEggdlfgeghvDGLRAIRDLdtpiDAKNPEYgpkanqllvtNASDEGR 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 124 QALTGLFAKQ-FGTPNYAAHGGFCsanmaaGMIYTIG-GSFWE------FGGPDLDSAKLFFMIGTAEDHHSNPlkiais 195
Cdd:PRK14991 235 DAFIKRFAFNsFGTRNFGNHGSYC------GLAYRAGsGALMGdldknpHVKPDWDNVEFALFIGTSPAQSGNP------ 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 196 kFKRAGgRFIAINPIRTGY----------------AAIADEWVPIKPGTDGALFMAFLHELIAADAWDHEFV-------- 251
Cdd:PRK14991 303 -FKRQA-RQLANARTRGNFeyvvvapalplssslaAGDNNRWLPIRPGTDSALAMGMIRWIIDNQRYNADYLaqpgvaam 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 252 -----RRYTNAAELVDLDEASENFGLFVR--DPERPV-GNPLFPQ-NHLWWDAQAARAVPH-HTPGVEPALDGRYTLDDG 321
Cdd:PRK14991 381 qaageASWTNATHLVIADPGHPRYGQFLRasDLGLPFeGEARGDGeDTLVVDAADGELVPAtQAQPARLFVEQYVTLADG 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 322 TPVT--PSFALLRERVADCTPEWAAGITGISADTIRRLAGEMiqTSRDHRitlpirwtdAWGETHetvtgnpvafhamrG 399
Cdd:PRK14991 461 QRVRvkSSLQLLKEAARKLSLAEYSEQCGVPEAQIIALAEEF--TSHGRK---------AAVISH--------------G 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 400 LAAHSNGFQSIRALAVLMSLLGTIDTPGGFRHKS-PFpravPPSAKPP-----NSPDAVKPN-TPLATGPLGWPAAPEDL 472
Cdd:PRK14991 516 GTMSGNGFYNAWAIMMLNALIGNLNLKGGVVVGGgKF----PGFGDGPrynlaSFAGKVKPKgVSLSRSKFPYEKSSEYR 591
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 473 FIDEQGGPVRIDKAfSWeYPlAVHGLMHSVITNAWRGDPYPIDTLMIFMAN----MAwnssmntmKVREMLVDKHASGEy 548
Cdd:PRK14991 592 RKVEAGQSPYPAKA-PW-YP-FVAGLLTEMLTAALEGYPYPLKAWINHMSNpiygVP--------GLRAVIEEKLKDPK- 659
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 549 KIPFLVVCDAFQSEMTAFADLILPDTTYLER-------HDAMSmldrpisefdgPVDSVRVPVVPP----TGECKP--FQ 615
Cdd:PRK14991 660 KLPLFISIDAFINETTALADYIVPDTHTYESwgftapwGGVPT-----------KASTARWPVVEPrtakTADGQPvcME 728
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 616 EVLIELASRLKFPAF-----TTAEGAR----RYRDYpdfvvnfttspdsgvgFL-----IGWRGK-------DGDKALVG 674
Cdd:PRK14991 729 SFLIAVAKRLQLPGFgdnaiKDAQGNThplnRAEDF----------------YLrgaanIAYLGKtpvadasDEDIALTG 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 675 ----EP------NPNQWEQYAknncvfhyrlpetLQYMR-----NCNGPYLEWAVKHGFRKfgePilIQLYSDVMQKFRL 739
Cdd:PRK14991 793 vsriLPalqatlKPDEVRRVA-------------FIYARggrfaPAESAYDEERMGNRWKK---P--LQIWNEDVAAARH 854
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 740 AAQG-RTSGrqppdhlrarvekyfdpLPFWYAPLESAATDLDQ-FPLAavtQRPMAMYhSWDS--QNAW------LRQIH 809
Cdd:PRK14991 855 SMTGeRYSG-----------------CPTWYPPRLADGTPLREqFPES---QWPLLLI-SFKSnlMSSMsiasprLRQVK 913
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1588214711 810 GENYLYMNPLMAAENGIADGAWIYAESQWGRVRCMARFSETVEPGTVwtwnAIGKASGAWNLGPGA 875
Cdd:PRK14991 914 PANPVALNPQDAARLGIQHGDRVRISTPGGSVVAQASVLNGVMPGVI----AIEHGYGHRELGARA 975
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
22-889 |
4.68e-37 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 150.18 E-value: 4.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 22 CACRCGIRVHLREGEVRYID----GNPEHP-LNQGVICAKGASGIMKQYSPARLTQPLMRKpdAERGSAQFEPVSWEHAF 96
Cdd:PRK14990 67 CGSRCPLRMHVVDGEIKYVEtdntGDDNYDgLHQVRACLRGRSMRRRVYNPDRLKYPMKRV--GARGEGKFERISWEEAY 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 97 DVLE---KRLGEIRATDPKKFALFTGrdqmqALTGLFAKQFGTPN------------YAAH-GGFCSANMAAGMIYTIGG 160
Cdd:PRK14990 145 DIIAtnmQRLIKEYGNESIYLNYGTG-----TLGGTMTRSWPPGNtlvarlmnccggYLNHyGDYSSAQIAEGLNYTYGG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 161 sfWEFGGP--DLDSAKLFFMIGtaedhhSNPLKIAIS----------KFKRAGGRFIAINPIRTGYAA-IADEWVPIKPG 227
Cdd:PRK14990 220 --WADGNSpsDIENSKLVVLFG------NNPGETRMSgggvtyyleqARQKSNARMIIIDPRYTDTGAgREDEWIPIRPG 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 228 TDGALFMAFLHELIAADAWDHEFVRRYTnaaelVDLDEASenfglfvrdpeRPVGNPlfpqnhlwwdaqaarAVPHHTPg 307
Cdd:PRK14990 292 TDAALVNGLAYVMITENLVDQPFLDKYC-----VGYDEKT-----------LPASAP---------------KNGHYKA- 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 308 vepaldgrYTLDDGTpvtpsfallrERVADcTPEWAAGITGISADTIRRLAGEMIQTSrdhritlPIRWTDAWGETHetv 387
Cdd:PRK14990 340 --------YILGEGP----------DGVAK-TPEWASQITGVPADKIIKLAREIGSTK-------PAFISQGWGPQR--- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 388 tgnpvafhamrglaaHSNGFQSIRALAVLMSLLGTIDTPGGF------RHKSPFPRAvppsakpPNSPDAVKPNTPLatg 461
Cdd:PRK14990 391 ---------------HANGEIATRAISMLAILTGNVGINGGNsgaregSYSLPFVRM-------PTLENPIQTSISM--- 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 462 pLGWPAAPEdlfideqggpvridkafsweyplavHGLMHSVITNAWRGD---PYPIDTLMIFMANMAWNSSMNTMKVREM 538
Cdd:PRK14990 446 -FMWTDAIE-------------------------RGPEMTALRDGVRGKdklDVPIKMIWNYAGNCLINQHSEINRTHEI 499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 539 LVDkhasgEYKIPFLVVCDAFQSEMTAFADLILPDTTYLERHDAmsMLDRPISEFDGPVDSVRvpVVPPTGECKPFQEVL 618
Cdd:PRK14990 500 LQD-----DKKCELIVVIDCHMTSSAKYADILLPDCTASEQMDF--ALDASCGNMSYVIFNDQ--VIKPRFECKTIYEMT 570
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 619 IELASRL----KFPAFTTAEGARRYRDypdfvvnfttspdsgvgfligwrgKDGDKALvgePNPNQWEQYAKNNcVFHYR 694
Cdd:PRK14990 571 SELAKRLgveqQFTEGRTQEEWMRHLY------------------------AQSREAI---PELPTFEEFRKQG-IFKKR 622
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 695 LPEtlqymrncnGPYLEWavkHGFRK--FGEPIL-----IQLYSDVMQKfrLAAqgrtSGRQPPDHLrarvekyFDPLPF 767
Cdd:PRK14990 623 DPQ---------GHHVAY---KAFREdpQANPLTtpsgkIEIYSQALAD--IAA----TWELPEGDV-------IDPLPI 677
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 768 WYAPLESAATDLD-QFPLAAV----TQRPMAMYHSWDSQNAWLRQihgenYLYMNPLMAAENGIADGAWIYAESQWGRVR 842
Cdd:PRK14990 678 YTPGFESYQDPLNkQYPLQLTgfhyKSRVHSTYGNVDVLKAACRQ-----EMWINPLDAQKRGINNGDKVRIFNDRGEVH 752
|
890 900 910 920
....*....|....*....|....*....|....*....|....*..
gi 1588214711 843 CMARFSETVEPGTVwtwnAIGKasGAWnLGPGANESQRGFLLNHLIT 889
Cdd:PRK14990 753 IEAKVTPRMMPGVV----ALGE--GAW-YDPDAKRVDKGGCINVLTT 792
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
17-626 |
1.44e-36 |
|
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: 146.00 E-value: 1.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 17 TTCYMCACRCGIRVHLREGEVRYIDGNPEHPLNQGVICAKGASGIMKQYSPARLTQPLMRKPDaergsaQFEPVSWEHAF 96
Cdd:cd02762 2 RACILCEANCGLVVTVEDGRVASIRGDPDDPLSKGYICPKAAALGDYQNDPDRLRTPMRRRGG------SFEEIDWDEAF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 97 DVLEKRLGEIRATD-PKKFALFTGRDQMQ-----ALTGLFAKQFGTPNYAahggfcSANMAAGMI--YTIGGSFWEFGG- 167
Cdd:cd02762 76 DEIAERLRAIRARHgGDAVGVYGGNPQAHthaggAYSPALLKALGTSNYF------SAATADQKPghFWSGLMFGHPGLh 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 168 --PDLDSAKLFFMIGtAEDHHSN---------PLKIAISKfKRaGGRFIAINPIRTGYAAIADEWVPIKPGTDGALFMAF 236
Cdd:cd02762 150 pvPDIDRTDYLLILG-ANPLQSNgslrtapdrVLRLKAAK-DR-GGSLVVIDPRRTETAKLADEHLFVRPGTDAWLLAAM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 237 LHELIAAdawdhefvrrytnaaelvdldeasenfGLFVRdperpvgnplfpqnhlwwdaqaaRAVPHHTPGVEPaldgry 316
Cdd:cd02762 227 LAVLLAE---------------------------GLTDR-----------------------RFLAEHCDGLDE------ 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 317 tlddgtpvtpsfalLRERVADCTPEWAAGITGISADTIRRLAgemiqtsrdhritlpirwtdawgetHETVTGNPVAFHA 396
Cdd:cd02762 251 --------------VRAALAEFTPEAYAPRCGVPAETIRRLA-------------------------REFAAAPSAAVYG 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 397 MRGLAAHSNGFQSIRALAVLMSLLGTIDTPGGFRHKSPFPRAVPPSAKPpnspdavkpntplATGPLGWPAapedlfide 476
Cdd:cd02762 292 RLGVQTQLFGTLCSWLVKLLNLLTGNLDRPGGAMFTTPALDLVGQTSGR-------------TIGRGEWRS--------- 349
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 477 qggPVRIDKAFSWEYPLAVhgLMHSVITNawrgDPYPIDTLMIFMANMAwNSSMNTMKVREMLvdkhasgeYKIPFLVVC 556
Cdd:cd02762 350 ---RVSGLPEIAGELPVNV--LAEEILTD----GPGRIRAMIVVAGNPV-LSAPDGARLEAAL--------GGLEFMVSV 411
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1588214711 557 DAFQSEMTAFADLILPDTTYLERHDAmsmlDRPISEFdgPVDSVRV--PVVPPTGECKPFQEVLIELASRLK 626
Cdd:cd02762 412 DVYMTETTRHADYILPPASQLEKPHA----TFFNLEF--PRNAFRYrrPLFPPPPGTLPEWEILARLVEALD 477
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
65-637 |
2.95e-27 |
|
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: 118.13 E-value: 2.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 65 YSPARLTQPLMRK---------PDAERGSAQFEPVSWEHAFDVLEKRLGEIRatdpKKF---ALFTGR------DQMQAL 126
Cdd:cd02769 42 YSPTRIKYPMVRRgwlekgpgsDRSLRGKEEFVRVSWDEALDLVAAELKRVR----KTYgneAIFGGSygwssaGRFHHA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 127 TGLFAKQFGTP-NYAAHGGFCSAnmAAG---MIYTIGGSF--------WE-----------FGGPDLDSAKLffMIGTAE 183
Cdd:cd02769 118 QSLLHRFLNLAgGYVGSVGDYST--GAAqviLPHVVGSMEvyteqqtsWPviaehtelvvaFGADPLKNAQI--AWGGIP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 184 DHHSNPlkiAISKFKRAGGRFIAINPIRTGYAAIAD-EWVPIKPGTDGALFMAFLHELIAADAWDHEFVRRYTnaaelvd 262
Cdd:cd02769 194 DHQAYS---YLKALKDRGIRFISISPLRDDTAAELGaEWIAIRPGTDVALMLALAHTLVTEGLHDKAFLARYT------- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 263 ldeasenfglfvrdperpVGNPLFpqnhlwwdaqaaravphhtpgvEPALDGRytlDDGTPVtpsfallrervadcTPEW 342
Cdd:cd02769 264 ------------------VGFDKF----------------------LPYLLGE---SDGVPK--------------TPEW 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 343 AAGITGISADTIRRLAGEMIqtsrDHRITLPIRWtdawgethetvtgnpvafhamrGLAAHSNGFQSIRALAVLMSLLGT 422
Cdd:cd02769 287 AAAICGIPAETIRELARRFA----SKRTMIMAGW----------------------SLQRAHHGEQPHWMAVTLAAMLGQ 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 423 IDTPG-GFRHKSPFPRAVPPSAKPPNSPDavkpntplatgpLGWPAAPEDLFIdeqggPV-RIDKAFswEYPLAVHGLMH 500
Cdd:cd02769 341 IGLPGgGFGFGYHYSNGGGPPRGAAPPPA------------LPQGRNPVSSFI-----PVaRIADML--LNPGKPFDYNG 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 501 SVITnawrgdpYPIDTLMIFMANMAWNSSMNTMKVREMLvdkhasgeyKIPFLVVCDAFQSEMTA-FADLILPDTTYLER 579
Cdd:cd02769 402 KKLT-------YPDIKLVYWAGGNPFHHHQDLNRLIRAW---------QKPETVIVHEPFWTATArHADIVLPATTSLER 465
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1588214711 580 HD-AMSMLDRPIsefdgpvdsvrVP---VVPPTGECKPFQEVLIELASRL-KFPAFTTAEGAR 637
Cdd:cd02769 466 NDiGGSGDNRYI-----------VAmkqVVEPVGEARDDYDIFADLAERLgVEEQFTEGRDEM 517
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
16-428 |
3.81e-26 |
|
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. 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: 114.80 E-value: 3.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 16 TTTCYMCACRCGIRVHLREGEVRYIDGNPEHPLNQGVICAKGASGIMKQYSPARLTQPLMRKPdaerGSAQFEPVSWEHA 95
Cdd:cd02752 1 RTICPYCSVGCGLIAYVQNGVWVHQEGDPDHPVNRGSLCPKGAALRDFVHSPKRLKYPMYRAP----GSGKWEEISWDEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 96 FDVLEKRLGEIR-ATDPKKFA---LFTGRDQMQALTGL------------FAKQFGTPNYAAHGGFCSANMAAGMIYTIG 159
Cdd:cd02752 77 LDEIARKMKDIRdASFVEKNAagvVVNRPDSIAFLGSAklsneecylirkFARALGTNNLDHQARIUHSPTVAGLANTFG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 160 -----GSFWefggpDLDSAKLFFMIGT--AEDHHSNPLKIAISKFKRaGGRFIAINPIRTGYAAIADEWVPIKPGTDgal 232
Cdd:cd02752 157 rgamtNSWN-----DIKNADVILVMGGnpAEAHPVSFKWILEAKEKN-GAKLIVVDPRFTRTAAKADLYVPIRSGTD--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 233 fMAFLHELIaadawdhefvrrytnaaelvdldeasenfglfvrdperpvgnplfpqNHLWwdaqaaravphhtpgvepal 312
Cdd:cd02752 228 -IAFLGGMI-----------------------------------------------NYII-------------------- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 313 dgRYtlddgtpvtpsfallrervadcTPEWAAGITGISADTIRRLAGEMIQTSRDHRiTLPIRWtdAWGETHetvtgnpv 392
Cdd:cd02752 240 --RY----------------------TPEEVEDICGVPKEDFLKVAEMFAATGRPDK-PGTILY--AMGWTQ-------- 284
|
410 420 430
....*....|....*....|....*....|....*.
gi 1588214711 393 afhamrglaaHSNGFQSIRALAVLMSLLGTIDTPGG 428
Cdd:cd02752 285 ----------HTVGSQNIRAMCILQLLLGNIGVAGG 310
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
15-646 |
9.82e-25 |
|
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: 108.95 E-value: 9.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 15 KTTTCYMCACRCGIRVHLREGEV-------RYIDGNPEHPLNQGVICAKGASGIMKQYSPARLTQPLMRKPdaERGSAQF 87
Cdd:cd02750 5 RSTHGVNCTGSCSWNVYVKNGIVtreeqatDYPETPPDLPDYNPRGCQRGASFSWYLYSPDRVKYPLKRVG--ARGEGKW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 88 EPVSWEHAFDVLEKRLGE-IRATDPKKFALFTGRDQMQALT---GL-FAKQFGTPNYAAHGGFCSANMAAGMIYTIGGSF 162
Cdd:cd02750 83 KRISWDEALELIADAIIDtIKKYGPDRVIGFSPIPAMSMVSyaaGSrFASLIGGVSLSFYDWYGDLPPGSPQTWGEQTDV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 163 WEFGgpDLDSAKLFFMIGtaedhhSNPL--KIAISKF----KRAGGRFIAINPIRTGYAAIADEWVPIKPGTDGALFMAF 236
Cdd:cd02750 163 PESA--DWYNADYIIMWG------SNVPvtRTPDAHFlteaRYNGAKVVVVSPDYSPSAKHADLWVPIKPGTDAALALAM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 237 LHELIAADAWDHEFVRRYTNAAELVdldeasenfglfvrdperpvgnplfpqnhlwwdaqaaravphhtpgvepaldgrY 316
Cdd:cd02750 235 AHVIIKEKLYDEDYLKEYTDLPFLV------------------------------------------------------Y 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 317 tlddgtpvtpsfallrervadcTPEWAAGITGISADTIRRLAGEMIQTSRDHRITLPirwtdawgethetvtgnpvafha 396
Cdd:cd02750 261 ----------------------TPAWQEAITGVPRETVIRLAREFATNGRSMIIVGA----------------------- 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 397 mrGLAAHSNGFQSIRALAVLMSLLGTIDTPGGfrhkspfpravppsakppnspdavkpntpLATGPLGWPAApedLFIde 476
Cdd:cd02750 296 --GINHWYHGDLCYRALILLLALTGNEGKNGG-----------------------------GWAHYVGQPRV---LFV-- 339
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 477 qggpvridkafsweyplavhglmhsvitnaWRGDPYpidtlmifmanmawNSSMNTMKVREMlvdkhaSGEYKIPFLVVC 556
Cdd:cd02750 340 ------------------------------WRGNLF--------------GSSGKGHEYFED------APEGKLDLIVDL 369
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 557 DaFQSEMTA-FADLILPDTTYLERHDaMSMLDrpISEFDGPVDsvrvPVVPPTGECKPFQEVLIELASrlKFPAFTTAEG 635
Cdd:cd02750 370 D-FRMDSTAlYSDIVLPAATWYEKHD-LSTTD--MHPFIHPFS----PAVDPLWEAKSDWEIFKALAK--KVPWRTLTGR 439
|
650
....*....|.
gi 1588214711 636 ARRYRDYPDFV 646
Cdd:cd02750 440 QQFYLDHDWFL 450
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
791-916 |
1.22e-18 |
|
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site. This hierarchy is of the conserved MopB_CT domain present in many, but not all, MopB homologs.
Pssm-ID: 239176 [Multi-domain] Cd Length: 101 Bit Score: 81.98 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 791 PMAMYHS-WDSQNAWLRQIHGENYLYMNPLMAAENGIADGAWIYAESQWGRVRCMARFSETVEPGTVWTWNAIGKASGaw 869
Cdd:cd02775 1 LRDHFHSgTRTRNPWLRELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGHRGG-- 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1588214711 870 nlgpganesqRGFLLNHLITDELpgrdddvarrmsnsDPVTGQAAWY 916
Cdd:cd02775 79 ----------RGGNANVLTPDAL--------------DPPSGGPAYK 101
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
69-256 |
6.56e-18 |
|
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: 88.52 E-value: 6.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 69 RLTQPLMRKPdaerGSAQFEPVSWEHAFDVLEKRLgeiRATDPKKFALFT-GRDQMQA--LTGLFAKQFGTPNYAAHGGF 145
Cdd:cd02767 64 RLTYPMRYDA----GSDHYRPISWDEAFAEIAARL---RALDPDRAAFYTsGRASNEAayLYQLFARAYGTNNLPDCSNM 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 146 CSANMAAGMIYTIGGSFWEFGGPDLDSAKLFFMIGtaedhhSNP-------LKiAISKFKRAGGRFIAINPIR------- 211
Cdd:cd02767 137 CHEPSSVGLKKSIGVGKGTVSLEDFEHTDLIFFIG------QNPgtnhprmLH-YLREAKKRGGKIIVINPLRepglerf 209
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 212 ----------TGYAAIADEWVPIKPGTDGALFMAFLHELIAADAW-----DHEFVRRYTN 256
Cdd:cd02767 210 anpqnpesmlTGGTKIADEYFQVRIGGDIALLNGMAKHLIERDDEpgnvlDHDFIAEHTS 269
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
26-266 |
7.11e-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: 88.31 E-value: 7.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 26 CGIRVHLREGEVRYIDGNPEHPLNQGVICAKGASGIMKQYSPARLTQPLMRKPDAERGSaqfepVSWEHAFDVLEKRLGE 105
Cdd:cd02764 56 QGVLVKTVDGRPIKIEGNPDHPASLGGTSARAQASVLSLYDPDRAQGPLRRGIDGAYVA-----SDWADFDAKVAEQLKA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 106 IRATDpkKFALFTGRDQ---MQALTGLFA-KQFGT------PNYAahGGFCSANMA--------------AGMIYTIGGS 161
Cdd:cd02764 131 VKDGG--KLAVLSGNVNsptTEALIGDFLkKYPGAkhvvydPLSA--EDVNEAWQAsfgkdvvpgydfdkAEVIVSIDAD 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 162 FWEFGGPDLDSAKLFfmigtAEDHHSNPLKIAiskfkragGRFIAINPIRTGYAAIADEWVPIKPGTDGALFMAFLHELI 241
Cdd:cd02764 207 FLGSWISAIRHRHDF-----AAKRRLGAEEPM--------SRLVAAESVYTLTGANADVRLAIRPSQEKAFALGLAHKLI 273
|
250 260 270
....*....|....*....|....*....|....
gi 1588214711 242 AADA--WDHEFVRRYTNA------AEL-VDLDEA 266
Cdd:cd02764 274 KKGAgsSLPDFFRALNLAfkpakvAELtVDLDKA 307
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
14-66 |
3.09e-17 |
|
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: 76.52 E-value: 3.09e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1588214711 14 IKTTTCYMCACRCGIRVHLREGEVRYIDGNPEHPLNQGVICAKGASGIMKQYS 66
Cdd:smart00926 3 WVPTVCPLCGVGCGLLVEVKDGRVVRVRGDPDHPVNRGRLCPKGRAGLEQVYS 55
|
|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
17-66 |
2.77e-16 |
|
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: 73.48 E-value: 2.77e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1588214711 17 TTCYMCACRCGIRVHLREGEVRYIDGNPEHPLNQGVICAKGASGIMKQYS 66
Cdd:pfam04879 6 TICPYCGVGCGLEVHVKDGKIVKVEGDPDHPVNEGRLCVKGRFGYERVYN 55
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
19-256 |
2.93e-15 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 80.71 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 19 CYMCACRCGIRVHLREGEVRYIDGNPEHPLNQGVICAKG--ASGIMkqYSPARLTQPLMRKPDAE-RGSAQFEPVSWEHA 95
Cdd:PRK13532 47 CRFCGTGCGVLVGTKDGRVVATQGDPDAPVNRGLNCIKGyfLSKIM--YGKDRLTQPLLRMKDGKyDKEGEFTPVSWDQA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 96 FDVLEKRLGE-IRATDPKKFALFtGRDQMQ-----ALTGLFAKQFGT----PNyAAHggfCSANMAAGMIYTIG-----G 160
Cdd:PRK13532 125 FDVMAEKFKKaLKEKGPTAVGMF-GSGQWTiwegyAASKLMKAGFRSnnidPN-ARH---CMASAVVGFMRTFGidepmG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 161 SFwefggPDLDSAKLFFMIGT--AEDHH-----------SNP-LKIA-ISKFKRaggrfiainpiRTgyAAIADEWVPIK 225
Cdd:PRK13532 200 CY-----DDIEAADAFVLWGSnmAEMHPilwsrvtdrrlSNPdVKVAvLSTFEH-----------RS--FELADNGIIFT 261
|
250 260 270
....*....|....*....|....*....|.
gi 1588214711 226 PGTDGALFMAFLHELIAADAWDHEFVRRYTN 256
Cdd:PRK13532 262 PQTDLAILNYIANYIIQNNAVNWDFVNKHTN 292
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
69-301 |
2.97e-15 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 78.60 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 69 RLTQPLMRkpdaeRGSAQFEPVSWEHAFDVLEKRLGEIRAT-DPKKFALFTGRDQMQALTGLFA-----KQFGTPNYAAH 142
Cdd:pfam00384 1 RLKYPMVR-----RGDGKFVRVSWDEALDLIAKKLKRIIKKyGPDAIAINGGSGGLTDVESLYAlkkllNRLGSKNGNTE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 143 GGFCSANMAAgmIYTIGGSF---WEFGGP--DLDSAKLFFMIGTaedhhsNPLKIA-------ISKFKRAGGRFIAINPI 210
Cdd:pfam00384 76 DHNGDLCTAA--AAAFGSDLrsnYLFNSSiaDIENADLILLIGT------NPREEApilnariRKAALKGKAKVIVIGPR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 211 RTgyAAIADEWVPIKPGTDGALFMAFLHELIAADAWDHEFVRR--------YTNAAELVDLDEASENFGLFVRDPERPVG 282
Cdd:pfam00384 148 LD--LTYADEHLGIKPGTDLALALAGAHVFIKELKKDKDFAPKpiiivgagVLQRQDGEAIFRAIANLADLTGNIGRPGG 225
|
250
....*....|....*....
gi 1588214711 283 NPlFPQNHLwwdAQAARAV 301
Cdd:pfam00384 226 GW-NGLNIL---QGAASPV 240
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
782-922 |
1.18e-13 |
|
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: 69.24 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 782 FPLAAVTQRPMAMYHSwdSQNA-WLRQIHGENYLYMNPLMAAENGIADGAWIYAESQWGRVRCMARFSETVEPGTV---- 856
Cdd:cd02780 1 YPFILVTFKSNLNSHR--SANApWLKEIKPENPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRPGVVaieh 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 857 ----WTWNAIGKASGAwNLGPGANESQRGFLLNHLitdelpGRDDDVARRMSNSDPVTGQAAWYDVRVRI 922
Cdd:cd02780 79 gyghWAYGAVASTIDG-KDLPGDAWRGAGVNINDI------GLVDPSRGGWSLVDWVGGAAARYDTPVKI 141
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
783-922 |
1.35e-13 |
|
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: 68.45 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 783 PLAAVTQRPMAMYHSWDSQNAWLRQIHGENYLYMNPLMAAENGIADGAWIYAESQWGRVRCMARFSETVEPGTVWTWNAI 862
Cdd:cd02778 1 EFRLIYGKSPVHTHGHTANNPLLHELTPENTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMPHGF 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 863 GKASGAWNLGPGANESqrgflLNHLItdelPGRdddvarrmsnSDPVTGQAAWYDVRVRI 922
Cdd:cd02778 81 GHWAPALSRAYGGGVN-----DNNLL----PGS----------TEPVSGGAGLQEFTVTV 121
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
780-857 |
3.26e-13 |
|
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: 67.33 E-value: 3.26e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1588214711 780 DQFPLAAVTQRPMAMYHSWDSQNAWLRQIHGENYLYMNPLMAAENGIADGAWIYAESQWGRVRCMARFSETVEPGTVW 857
Cdd:cd02781 1 EYPLILTTGARSYYYFHSEHRQLPSLRELHPDPVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVR 78
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
56-581 |
2.26e-12 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 71.24 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 56 KGASGIMkqYSPARLTQPLMR--------KPDAE-RGSAQFEPVSWEHAFDVLEKRLGEIRaTDPKKFALFTGRDQMQAl 126
Cdd:PRK15102 79 NGIKGHV--YNPSRIRYPMVRldwlrkrhKSDTSqRGDNRFVRVSWDEALDLFYEELERVQ-KTYGPSALHTGQTGWQS- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 127 TGLFAKQFGTPNYAA--HGGFCS-----ANMAAGMI--YTIG-------GSFWEFggpDLDSAKLFFMIGT--------- 181
Cdd:PRK15102 155 TGQFHSATGHMQRAIgmHGNSVGtvgdySTGAGQVIlpYVLGstevyeqGTSWPL---ILENSKTIVLWGSdpvknlqvg 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 182 --AEDHHSNPLkIAISKFKRAGG--RFIAINPIRTGYAA-IADEWVPIKPGTDGALFMAFLHELIAADAWDHEFVRRYTN 256
Cdd:PRK15102 232 wnCETHESYAY-LAQLKEKVAKGeiNVISIDPVVTKTQNyLGCEHLYVNPQTDVPLMLALAHTLYSENLYDKKFIDNYCL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 257 AaelvdldeasenFGLFVrdperpvgnplfpqnhlwwdaqaaravphhtpgvePALDGRytlDDGTPVTPsfallrerva 336
Cdd:PRK15102 311 G------------FEQFL-----------------------------------PYLLGE---KDGVPKTP---------- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 337 dctpEWAAGITGISADTIRRLAGEMIQtsrdHRITLPIRWTdawgethetvtgnpvafhamrgLAAHSNGFQSIRALAVL 416
Cdd:PRK15102 331 ----EWAEKICGIDAETIRELARQMAK----GRTQIIAGWC----------------------IQRQQHGEQPYWMGAVL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 417 MSLLGTIDTPGG---FRHK-----SPFPRAVPPSAKPPNSPDAVKP---NTPLatgplgwpaapedlfideqggpvridK 485
Cdd:PRK15102 381 AAMLGQIGLPGGgisYGHHysgigVPSSGGAIPGGFPGNLDTGQKPkhdNSDY--------------------------K 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 486 AFSWEYPLA--VHGLMHSVITNAWRGDP--YPIDTLMIFMANMAWN--SSMNTMKvremlvdkhaSGEYKIPFLVVCDAF 559
Cdd:PRK15102 435 GYSSTIPVArfIDAILEPGKTINWNGKKvtLPPLKMMIFSGTNPWHrhQDRNRMK----------EAFRKLETVVAIDNQ 504
|
570 580
....*....|....*....|..
gi 1588214711 560 QSEMTAFADLILPDTTYLERHD 581
Cdd:PRK15102 505 WTATCRFADIVLPACTQFERND 526
|
|
| 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 ... |
17-107 |
4.01e-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: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 17 TTCYMCACRCGIRVHLREGEVRYIDGNPEHPLNQGVICAKGASGIMKQYSPARLTQPLMRKPDAergsaqFEPVSWEHAF 96
Cdd:cd02771 2 SICHHCSVGCNISLGERYGELRRVENRYNGAVNHYFLCDRGRFGYGYVNSRDRLTQPLIRRGGT------LVPVSWNEAL 75
|
90
....*....|.
gi 1588214711 97 DVLEKRLGEIR 107
Cdd:cd02771 76 DVAAARLKEAK 86
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
17-258 |
5.15e-11 |
|
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: 65.77 E-value: 5.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 17 TTCYMCACRCGIRVHLREGEVRYI--DGNPEhpLNQGVICAKGA---SGImkqYSPARLTQPLMRKPDaergsaQFEPVS 91
Cdd:cd02768 2 SIDVHDALGSNIRVDVRGGEVMRIlpRENEA--INEEWISDKGRfgyDGL---NSRQRLTQPLIKKGG------KLVPVS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 92 WEHAFDVLEKRLgeiRATDPKKFALFTGrdQMQALTGLFA-----KQFGTPNYaAHGGFcsaNMAAGMIYTIGGSFWeFG 166
Cdd:cd02768 71 WEEALKTVAEGL---KAVKGDKIGGIAG--PRADLESLFLlkkllNKLGSNNI-DHRLR---QSDLPADNRLRGNYL-FN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 167 GP--DLDSAKLFFMIGtaedhhSNPLKIA-------ISKFKRAGGRFIAINPirTGYAAIADEWVPIKPGtdGALFMAFL 237
Cdd:cd02768 141 TSiaEIEEADAVLLIG------SNLRKEApllnarlRKAVKKKGAKIAVIGP--KDTDLIADLTYPVSPL--GASLATLL 210
|
250 260
....*....|....*....|.
gi 1588214711 238 hELIAADAWDhEFVRRYTNAA 258
Cdd:cd02768 211 -DIAEGKHLK-PFAKSLKKAK 229
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
780-868 |
1.01e-10 |
|
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: 59.83 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 780 DQFPLAAVTQRPMAMYHSWD--SQNAWLRQIHGENYLYMNPLMAAENGIADGAWIYAESQWGRVRCMARFSETVEPGTVW 857
Cdd:cd00508 1 EEYPLVLTTGRLLEHWHTGTmtRRSPRLAALAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRPGTVF 80
|
90
....*....|....
gi 1588214711 858 T---WNAIGKASGA 868
Cdd:cd00508 81 MpfhWGGEVSGGAA 94
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
17-110 |
2.54e-10 |
|
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: 63.71 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 17 TTCYMCACRCGIRVHLREGEVRYIDGNPEHPLNQGVICAKGASGIMKQYSPARLTQPLMRKPDaergsaQFEPVSWEHAF 96
Cdd:COG1034 220 SICPHCSVGCNIRVDVRGGKVYRVLPRENEAVNEEWLCDKGRFGYDGLNSPDRLTRPLVRKDG------ELVEASWEEAL 293
|
90
....*....|....
gi 1588214711 97 DVLEKRLGEIRATD 110
Cdd:COG1034 294 AAAAEGLKALKKAE 307
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
784-877 |
4.52e-10 |
|
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: 57.67 E-value: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 784 LAAVTQRPMAMYHSW-DSQNAWLRQIHGENYLYMNPLMAAENGIADGAWIYAESQWGRVRCMARFSETVEPGTVWtwnaI 862
Cdd:pfam01568 1 LYLITGRVLGQYHSQtRTRRVLRLAKPEPEVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVF----M 76
|
90
....*....|....*
gi 1588214711 863 GKASGAWNLGPGANE 877
Cdd:pfam01568 77 PFGWWYEPRGGNANA 91
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
66-428 |
6.58e-10 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 63.14 E-value: 6.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 66 SPARLTQPLmrKPDAerGSAQFEPVSWEHAFDVLEKRLGEIRatDPKKFALFT-GRDQMQA--LTGLFAKQFGTPNYAAH 142
Cdd:PRK09939 105 AAGRLTQPL--KYDA--VSDCYKPLSWQQAFDEIGARLQSYS--DPNQVEFYTsGRTSNEAafLYQLFAREYGSNNFPDC 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 143 GGFCSANMAAGMIYTIGGSFWEFGGPDLDSAKLFFMIGTAEDHHSNPLKIAISKFKRAGGRFIAINPIRTgyAAIADEWV 222
Cdd:PRK09939 179 SNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPLQE--RGLERFTA 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 223 PIKPgtdgaLFMAFLHELIAADAWDHefVRRYTNAAELVDLDEAsenfgLFVRDperpvgnplfpqnhlwwdaQAARAVp 302
Cdd:PRK09939 257 PQNP-----FEMLTNSETQLASAYYN--VRIGGDMALLKGMMRL-----LIERD-------------------DAASAA- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 303 hhtpGVEPALDGRYTLDDgtpvTPSFALLRERVADCTPEWAAGITGISADTIRRLagemiqtsrdhritlpirwTDAWGE 382
Cdd:PRK09939 305 ----GRPSLLDDEFIQTH----TVGFDELRRDVLNSEWKDIERISGLSQTQIAEL-------------------ADAYAA 357
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1588214711 383 THETVTgnpvaFHAMrGLAAHSNGFQSIRALAVLMSLLGTIDTPGG 428
Cdd:PRK09939 358 AERTII-----CYGM-GITQHEHGTQNVQQLVNLLLMKGNIGKPGA 397
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
781-856 |
1.57e-08 |
|
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: 53.91 E-value: 1.57e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1588214711 781 QFPLAAVTQRPMAMYHSWDSQNAWLRQIHGENYLYMNPLMAAENGIADGAWIYAESQWGRVRCMARFSETVEPGTV 856
Cdd:cd02785 1 KYPLACIQRHSRFRVHSQFSNVPWLLELQPEPRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGVV 76
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
782-922 |
4.91e-08 |
|
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239187 [Multi-domain] Cd Length: 116 Bit Score: 52.28 E-value: 4.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 782 FPLAAVTQRPMAMYHSWDSQNAWLRQIHGENYLYMNPLMAAENGIADGAWIYAESQWGRVRCMARFSETVEPGTVWTwna 861
Cdd:cd02786 1 YPLRLITPPAHNFLNSTFANLPELRAKEGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVVVA--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1588214711 862 igkASGAWNLgpganESQRGFLLNHLITDELPgrdddvarrmsnsDPvTGQAAWYDVRVRI 922
Cdd:cd02786 78 ---EGGWWRE-----HSPDGRGVNALTSARLT-------------DL-GGGSTFHDTRVEV 116
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
780-866 |
1.06e-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: 51.46 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 780 DQFPLAAVTQRPMAMYHSWDS--QNAWLRQIHGENYLYMNPLMAAENGIADGAWIYAESQWGRVRCMARFSETVEPGTV- 856
Cdd:cd02792 1 EEFPLVLTTGRLTEHFHGGNMtrNSPYLAELQPEMFVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHEVg 80
|
90
....*....|....*.
gi 1588214711 857 ------WTWNAIGKAS 866
Cdd:cd02792 81 ipyhwgGMGLVIGDSA 96
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
805-870 |
9.63e-07 |
|
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: 48.72 E-value: 9.63e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1588214711 805 LRQIHGENYLYMNPLMAAENGIADGAWIYAESQWGRVRCMARFSETVEPGTV---WTWNAIGKASGAWN 870
Cdd:cd02791 28 LNAHVPEPYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPGEVfvpMHWGDQFGRSGRVN 96
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
782-869 |
1.08e-06 |
|
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239178 [Multi-domain] Cd Length: 127 Bit Score: 48.73 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 782 FPLAAVTQRPMAMYHSWDSQNAWLRQ---IHGENYLYMNPLMAAENGIADGAWIYAESQWGRVRCMARFSETVEPGTVwt 858
Cdd:cd02777 1 YPLQLISPHPKRRLHSQLDNVPWLREaykVKGREPVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPGVV-- 78
|
90
....*....|.
gi 1588214711 859 wnAIGKasGAW 869
Cdd:cd02777 79 --ALPE--GAW 85
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
796-869 |
2.42e-06 |
|
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase (DMSOR) of Escherichia coli and other related DMSOR-like enzymes. Unlike other DMSOR-like enzymes, this group has a predicted N-terminal iron-sulfur [4Fe-4S] cluster binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239195 [Multi-domain] Cd Length: 121 Bit Score: 47.29 E-value: 2.42e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1588214711 796 HSWDSQNAWLRQIHgENYLYMNPLMAAENGIADGAWIYAESQWGRVRCMARFSETVEPGTVwtwnAIGKasGAW 869
Cdd:cd02794 15 HSTFDNVPWLREAF-PQEVWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVV----ALPQ--GAW 81
|
|
| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
796-861 |
3.58e-06 |
|
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: 47.37 E-value: 3.58e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1588214711 796 HSWDSQNAW-LRQIHGENYLYMNPLMAAENGIADGAWIYAESQWGRVRCMARFSETVEPGTVWTWNA 861
Cdd:cd02776 14 HSTYRDNLLmLRLQRGGPVVWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTVFMYHA 80
|
|
| NarG |
COG5013 |
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and ... |
218-265 |
5.32e-06 |
|
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 444037 [Multi-domain] Cd Length: 1231 Bit Score: 50.59 E-value: 5.32e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1588214711 218 ADEWVPIKPGTDGALFMAFLHELIAADAWDH------EFVRRYTNAAELVDLDE 265
Cdd:COG5013 295 ADEWLPPKQGTDAALAMAMGHVILKEFHVDRqvpyftDYARRYTDLPFLVTLEE 348
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
17-98 |
1.01e-05 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 49.56 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 17 TTCYMCACRCGIRVHLREGEV-RYIDGN-PEhpLNQGVICAKGASGIMKQYSPARLTQPLMRKPDAErgsaqFEPVSWEH 94
Cdd:PRK07860 226 SVCEHCASGCAQRTDHRRGKVlRRLAGDdPE--VNEEWNCDKGRWAFTYATQPDRITTPLVRDEDGE-----LEPASWSE 298
|
....
gi 1588214711 95 AFDV 98
Cdd:PRK07860 299 ALAV 302
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
28-145 |
2.04e-04 |
|
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone oxidoreductase/respiratory complex I/NADH dehydrogenase-1(NDH-1) of eukaryotes and the Nqo3/G subunit of alphaproteobacteria NDH-1. The NADH-quinone oxidoreductase is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The nad11 gene codes for the largest (75 kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Paracoccus denitrificans, this subunit is encoded by the nqo3 gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The Nad11/Nqo3 subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239174 [Multi-domain] Cd Length: 375 Bit Score: 44.95 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 28 IRVHLREGEVRYIDGNPEHPLNQGVICAKG---ASGIMKQyspaRLTQPLMRKPDaergsaQFEPVSWEHAFDVLEKRLg 104
Cdd:cd02773 13 IRVDTRGGEVMRILPRLNEDINEEWISDKTrfaYDGLKRQ----RLDKPYIRKNG------KLKPATWEEALAAIAKAL- 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1588214711 105 eiRATDPKKFALFTGR----DQMQALTGLFAKqFGTPNYAAHGGF 145
Cdd:cd02773 82 --KGVKPDEIAAIAGDladvESMVALKDLLNK-LGSENLACEQDG 123
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| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
782-869 |
3.67e-04 |
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The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO.This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239194 [Multi-domain] Cd Length: 129 Bit Score: 41.47 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 782 FPLAAVTQRPMAMYHSwdsQ--NAWLRQ---IHGENYLYMNPLMAAENGIADGAWIYAESQWGRVRCMARFSETVEPGTV 856
Cdd:cd02793 1 YPLHLLSNQPATRLHS---QldHGSLSRaykVQGREPIRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPGVV 77
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90
....*....|...
gi 1588214711 857 wtwnAIgkASGAW 869
Cdd:cd02793 78 ----QL--PTGAW 84
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| PRK03642 |
PRK03642 |
putative periplasmic esterase; Provisional |
358-465 |
1.08e-03 |
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putative periplasmic esterase; Provisional
Pssm-ID: 179620 [Multi-domain] Cd Length: 432 Bit Score: 42.47 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588214711 358 AGEMIQTSRDHRITLP-IRWTDAWGETHETVtgnpvAFHAMRGLAAHSNGFQSIRALAVLMSllgTIDTPGGFRHKSPFP 436
Cdd:PRK03642 256 ATELNGNTRDGVIHFPnIRTNTLWGQVHDEK-----AFYSMGGVSGHAGLFSNTGDMAVLMQ---VMLNGGGYGNVQLFD 327
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90 100
....*....|....*....|....*....
gi 1588214711 437 RAVPPSAKPPNSPDavkpntplATGPLGW 465
Cdd:PRK03642 328 AETVKMFTTSSKED--------ATFGLGW 348
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