|
Name |
Accession |
Description |
Interval |
E-value |
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
14-553 |
0e+00 |
|
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239167 [Multi-domain] Cd Length: 501 Bit Score: 755.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 14 SVCSLDCPDQCGLLIHKKDGKIVKVQGDPDHPVTAGNICNKVRNMTERIYDEKRLTTPLKRTGAKGqAIFEPISWDEAID 93
Cdd:cd02766 2 SVCPLDCPDTCSLLVTVEDGRIVRVEGDPAHPYTRGFICAKGARYVERVYSPDRLLTPLKRVGRKG-GQWERISWDEALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 94 TITSRWKQLIDEEGAESILPYSFYGNMGKLTAEGMdRRFFYRMGSSQLERTICSKAGSEGYKYTMGISAGIDPEETIHTK 173
Cdd:cd02766 81 TIAAKLKEIKAEYGPESILPYSYAGTMGLLQRAAR-GRFFHALGASELRGTICSGAGIEAQKYDFGASLGNDPEDMVNAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 174 LFIFWGINAVSTNMHQITIAQKVRKQGAKIVVIDVHKNQTGRLADWFIPIKPGTDSALALGIMHILFKENLHDEAFLSEY 253
Cdd:cd02766 160 LIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDPYRTATAARADLHIQIRPGTDGALALGVAKVLFREGLYDRDFLARH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 254 TVGYEDLREHVKQYDPEKVSLITGVSTEDIYQLARMYGESSPSFIRIGNGIQHHDNGGMIVRTIACLPAITGQWLHKGGG 333
Cdd:cd02766 240 TEGFEELKAHLETYTPEWAAEITGVSAEEIEELARLYGEAKPPSIRLGYGMQRYRNGGQNVRAIDALPALTGNIGVPGGG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 334 AIKHNSGileyntnalqrpdllkgrtprsfnmnqlgkvlletdPPIRSLFIYGTNPAVVAPEANKVRQGLLREDLFTVVH 413
Cdd:cd02766 320 AFYSNSG------------------------------------PPVKALWVYNSNPVAQAPDSNKVRKGLAREDLFVVVH 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 414 DLFLTETAAYADIVLPATSAFENTDFYTSYWHHYIQLQQPVIERYGESKSNTEVFRLLAEAMGFTDQELKDSDEELIRQA 493
Cdd:cd02766 364 DQFMTDTARYADIVLPATTFLEHEDVYASYWHYYLQYNEPAIPPPGEARSNTEIFRELAKRLGFGEPPFEESDEEWLDQA 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 494 LDHPDnPYLAEIDYDSLtKHSFMKAKRKKPLFPGKLPTPSGKIELYSEKMKQDGFPALPT 553
Cdd:cd02766 444 LDGTG-LPLEGIDLERL-LGPRKAGFPLVAWEDRGFPTPSGKFEFYSERAAKRGLPPLPE 501
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
11-680 |
0e+00 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 702.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 11 IFKSVCSlDCPDQCGLLIHKKDGKIVKVQGDPDHPVTAGNICNKVRNMTERIYDEKRLTTPLKRTGAKGQAIFEPISWDE 90
Cdd:COG0243 23 TVKTTCP-GCGVGCGLGVKVEDGRVVRVRGDPDHPVNRGRLCAKGAALDERLYSPDRLTYPMKRVGPRGSGKFERISWDE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 91 AIDTITSRWKQLIDEEGAESILPYSFYGNMGKLTAEG--MDRRFFYRMGSSQLE--RTICSKAGSEGYKYTMGISAG-ID 165
Cdd:COG0243 102 ALDLIAEKLKAIIDEYGPEAVAFYTSGGSAGRLSNEAayLAQRFARALGTNNLDdnSRLCHESAVAGLPRTFGSDKGtVS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 166 PEETIHTKLFIFWGINAVSTNMHQIT-IAQKVRKQGAKIVVIDVHKNQTGRLADWFIPIKPGTDSALALGIMHILFKENL 244
Cdd:COG0243 182 YEDLEHADLIVLWGSNPAENHPRLLRrLREAAKKRGAKIVVIDPRRTETAAIADEWLPIRPGTDAALLLALAHVLIEEGL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 245 HDEAFLSEYTVGYEDLREHVKQYDPEKVSLITGVSTEDIYQLARMYGESSPSFIRIGNGIQHHDNGGMIVRTIACLPAIT 324
Cdd:COG0243 262 YDRDFLARHTVGFDELAAYVAAYTPEWAAEITGVPAEDIRELAREFATAKPAVILWGMGLQQHSNGTQTVRAIANLALLT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 325 GQWLHKGGGAIkhnsgileyntnalqrpdllkgrtPRSFNMnqlgkVLLETDPPIRSLFIYGTNPAVVAPEANKVRQGLL 404
Cdd:COG0243 342 GNIGKPGGGPF------------------------SLTGEA-----ILDGKPYPIKALWVYGGNPAVSAPDTNRVREALR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 405 REDlFTVVHDLFLTETAAYADIVLPATSAFENTDFYTSYWHHYIQLQQPVIERYGESKSNTEVFRLLAEAMGFTDQ-ELK 483
Cdd:COG0243 393 KLD-FVVVIDTFLTETARYADIVLPATTWLERDDIVTNSEDRRVHLSRPAVEPPGEARSDWEIFAELAKRLGFEEAfPWG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 484 DSDEELIRQALDHPDNpylAEIDYDSLTKHSFMK-AKRKKPLFP--GKLPTPSGKIELYSEKMKQDGFPAL--PTYTPLV 558
Cdd:COG0243 472 RTEEDYLRELLEATRG---RGITFEELREKGPVQlPVPPEPAFRndGPFPTPSGKAEFYSETLALPPLPRYapPYEGAEP 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 559 SDNEHPFMYVPAPNHNFLNSTFSNNEKHIRLEKTPKLFINTKDADEHGIVDGDPVRIWNSRGECELTAAVGEQVLPGVVV 638
Cdd:COG0243 549 LDAEYPLRLITGRSRDQWHSTTYNNPRLREIGPRPVVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTEGIRPGVVF 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 2234329652 639 SQGLWADEP--GKKQLVNALTPDRLSDMGGGATFFSGRVQIEKA 680
Cdd:COG0243 629 APHGWWYEPadDKGGNVNVLTPDATDPLSGTPAFKSVPVRVEKA 672
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
13-680 |
1.27e-125 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 388.09 E-value: 1.27e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 13 KSVCSLdCPDQCGLLIHKKDGKIVKVQGDPDHPVTAGNICNKVRNMTERIYDEKRLTTPLKRTGAKgqaiFEPISWDEAI 92
Cdd:COG3383 8 KTVCPY-CGVGCGIDLEVKDGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVNSPDRLTTPLIRRGGE----FREVSWDEAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 93 DTITSRWKQLIDEEGAESIlpySFYG-----N-----MGKLTaegmdrRFFyrMGSSQLE--RTICSKAGSEGYKYTMGI 160
Cdd:COG3383 83 DLVAERLREIQAEHGPDAV---AFYGsgqltNeenylLQKLA------RGV--LGTNNIDnnARLCMASAVAGLKQSFGS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 161 SAGIDP-EETIHTKLFIFWGINAvsTNMHQItIAQKVR---KQGAKIVVIDVHKNQTGRLADWFIPIKPGTDSALALGIM 236
Cdd:COG3383 152 DAPPNSyDDIEEADVILVIGSNP--AEAHPV-LARRIKkakKNGAKLIVVDPRRTETARLADLHLQIKPGTDLALLNGLL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 237 HILFKENLHDEAFLSEYTVGYEDLREHVKQYDPEKVSLITGVSTEDIYQLARMYGESSPSFIRIGNGIQHHDNGGMIVRT 316
Cdd:COG3383 229 HVIIEEGLVDEDFIAERTEGFEELKASVAKYTPERVAEITGVPAEDIREAARLIAEAKRAMILWGMGVNQHTQGTDNVNA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 317 IACLPAITGQWLHKGGGAikhNSgILEYNtNAL------QRPDLLKGRTP------RSFNMNQLGKVLLETDPP------ 378
Cdd:COG3383 309 IINLALATGNIGRPGTGP---FP-LTGQN-NVQggrdmgALPNVLPGYRDvtdpehRAKVADAWGVPPLPDKPGltavem 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 379 --------IRSLFIYGTNPAVVAPEANKVRQGLLREDlFTVVHDLFLTETAAYADIVLPATSAFENTDFYTSyWHHYIQL 450
Cdd:COG3383 384 fdaiadgeIKALWIIGENPAVSDPDANHVREALEKLE-FLVVQDIFLTETAEYADVVLPAASWAEKDGTFTN-TERRVQR 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 451 QQPVIERYGESKSNTEVFRLLAEAMGFtDQELKDSDE--ELIRQAldhpdNPYLAEIDYDSLTKHSFM------KAKRKK 522
Cdd:COG3383 462 VRKAVEPPGEARPDWEIIAELARRLGY-GFDYDSPEEvfDEIARL-----TPDYSGISYERLEALGGVqwpcpsEDHPGT 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 523 P-LFPGKLPTPSGKIELysekmkqdgFPALPTYTPLVSDNEHPFMYVPAPN-HNFLNSTFSNN-EKHIRLEKTPKLFINT 599
Cdd:COG3383 536 PrLFTGRFPTPDGKARF---------VPVEYRPPAELPDEEYPLVLTTGRLlDQWHTGTRTRRsPRLNKHAPEPFVEIHP 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 600 KDADEHGIVDGDPVRIWNSRGECELTAAVGEQVLPGVVVSQGLWADEPgkkqlVNALTPDRLSDMGGGATFFSGRVQIEK 679
Cdd:COG3383 607 EDAARLGIKDGDLVRVSSRRGEVVLRARVTDRVRPGTVFMPFHWGEGA-----ANALTNDALDPVSKQPEYKACAVRVEK 681
|
.
gi 2234329652 680 A 680
Cdd:COG3383 682 V 682
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
20-556 |
4.44e-120 |
|
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: 366.63 E-value: 4.44e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 20 CPDQCGLLIHKKDGKIVKVQGDPDHPVTAGNICNKVRNMTERIYDEKRLTTPLKRTGAKGQAIFEPISWDEAIDTITSRW 99
Cdd:cd02759 7 CHSGCGVLVYVKDGKLVKVEGDPNHPTNKGRLCMRGLAAPEIVYHPDRLLYPLKRVGERGENKWERISWDEALDEIAEKL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 100 KQLIDEEGAESIlpySFYGNMGKLTAEgMDRRFFYRM----GSSQ--LERTICSKAGSEGYKYTMGISAGIDPEETIHTK 173
Cdd:cd02759 87 AEIKAEYGPESI---ATAVGTGRGTMW-QDSLFWIRFvrlfGSPNlfLSGESCYWPRDMAHALTTGFGLGYDEPDWENPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 174 LFIFWGINAVSTN----MHQITIAqkvRKQGAKIVVIDVHKNQTGRLADWFIPIKPGTDSALALGIMHILFKENLHDEAF 249
Cdd:cd02759 163 CIVLWGKNPLNSNldlqGHWLVAA---MKRGAKLIVVDPRLTWLAARADLWLPIRPGTDAALALGMLNVIINEGLYDKDF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 250 LSEYTVGYEDLREHVKQYDPEKVSLITGVSTEDIYQLARMYGESSPSFIRIGNGIQHHDNGGMIVRTIACLPAITGqWLH 329
Cdd:cd02759 240 VENWCYGFEELAERVQEYTPEKVAEITGVPAEKIRKAARLYATAKPACIQWGLAIDQQKNGTQTSRAIAILRAITG-NLD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 330 KGGGaikhnsgileyntnalqrpDLLkgrTPrsfnmnqlgkvlletdPPIRSLFIYGTNPAVVAPEANKVRQGLLREDlF 409
Cdd:cd02759 319 VPGG-------------------NLL---IP----------------YPVKMLIVFGTNPLASYADTAPVLEALKALD-F 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 410 TVVHDLFLTETAAYADIVLPATSAFENTDFYTSY--WHHYiQLQQPVIERYGESKSNTEVFRLLAEAMGftdqelkdsde 487
Cdd:cd02759 360 IVVVDLFMTPTAMLADIVLPVAMSLERPGLRGGFeaENFV-QLRQKAVEPYGEAKSDYEIVLELGKRLG----------- 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2234329652 488 elirqaldhpdnpylaeidydsLTKHSFMKAKRKKPLFPGK--LPTPSGKIELYSEKMKQDGFPALPTYTP 556
Cdd:cd02759 428 ----------------------PEEAEYYKYEKGLLRPDGQpgFNTPTGKVELYSTMLEELGYDPLPYYRE 476
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
13-475 |
1.65e-119 |
|
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: 361.65 E-value: 1.65e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 13 KSVCSLdCPDQCGLLIHKKDGKIVKVQGDPDHPVTAGNICNKVRNMTERIYDEKRLTTPLKRTGAKGQaiFEPISWDEAI 92
Cdd:cd00368 1 PSVCPF-CGVGCGILVYVKDGKVVRIEGDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGGRGK--FVPISWDEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 93 DTITSRWKQLIDEEGAESILPYSFYGNMGKLTAEGMDRRFFYRMGSSQLERTICSKAGSEGYKYTMGISAGIDPEETIHT 172
Cdd:cd00368 78 DEIAEKLKEIREKYGPDAIAFYGGGGASNEEAYLLQKLLRALGSNNVDSHARLCHASAVAALKAFGGGAPTNTLADIENA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 173 KLFIFWGINAVSTNMHQITIAQKVRKQGAKIVVIDVHKNQTGRLADWFIPIKPGTDSALALGimhilfkenlhdeaflse 252
Cdd:cd00368 158 DLILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRRTETAAKADEWLPIRPGTDAALALA------------------ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 253 ytvgyedlrehvkqydpEKVSLITGVSTEDIYQLARMYGESSPSFIRIGNGIQHHDNGGMIVRTIACLPAITGQWLHKGG 332
Cdd:cd00368 220 -----------------EWAAEITGVPAETIRALAREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 333 GaikhnsgileyntnalqrpdllkgrtprsfnmnqlgkvlletdppirslFIYGTNPAVVAPEANKVRQGLLREDlFTVV 412
Cdd:cd00368 283 G-------------------------------------------------LGPGGNPLVSAPDANRVRAALKKLD-FVVV 312
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2234329652 413 HDLFLTETAAYADIVLPATSAFENTDFYTSyWHHYIQLQQPVIERYGESKSNTEVFRLLAEAM 475
Cdd:cd00368 313 IDIFMTETAAYADVVLPAATYLEKEGTYTN-TEGRVQLFRQAVEPPGEARSDWEILRELAKRL 374
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
14-556 |
4.53e-101 |
|
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: 321.96 E-value: 4.53e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 14 SVCSLDCPDQCGLLIHKKDGKIVKVQGDPDHPVTAGN----ICNKVRNMTERIYDEKRLTTPLKRTGAKGQAIFEPISWD 89
Cdd:cd02770 2 SACTVNCGGRCPLKAHVKDGVITRIETDDTGDDDPGFhqirACLRGRSQRKRVYNPDRLKYPMKRVGKRGEGKFVRISWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 90 EAIDTITSRWKQLIDEEGAESIlpYSFYGN---MGKLTAEGMDRRFFYRMGSsQLER--TICSKAGSEGYKYTMGISA-G 163
Cdd:cd02770 82 EALDTIASELKRIIEKYGNEAI--YVNYGTgtyGGVPAGRGAIARLLNLTGG-YLNYygTYSWAQITTATPYTYGAAAsG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 164 IDPEETIHTKLFIFWGINAVSTNM---HQITIAQKVRKQGAKIVVIDVHKNQTGR-LADWFIPIKPGTDSALALGIMHIL 239
Cdd:cd02770 159 SSLDDLKDSKLVVLFGHNPAETRMgggGSTYYYLQAKKAGAKFIVIDPRYTDTAVtLADEWIPIRPGTDAALVAAMAYVM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 240 FKENLHDEAFLSEYTVGY------------EDLREHV--KQYD-----PEKVSLITGVSTEDIYQLARMYGESSPSFIRI 300
Cdd:cd02770 239 ITENLHDQAFLDRYCVGFdaehlpegappnESYKDYVlgTGYDgtpktPEWASEITGVPAETIRRLAREIATTKPAAILQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 301 GNGIQHHDNGGMIVRTIACLPAITGQWLHKGGgaikhNSGILEYNTnALQRPDLLKGRTP-------------------- 360
Cdd:cd02770 319 GWGPQRHANGEQAARAIMMLAAMTGNVGIPGG-----NTGARPGGS-AYNGAGLPAGKNPvktsipcfmwtdaiergeem 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 361 RSFNMNQLGKVllETDPPIRSLFIYGTNPAV--VAPEANKVRQgLLRED---LFTVVHDLFLTETAAYADIVLPATSAFE 435
Cdd:cd02770 393 TADDGGVKGAD--KLKSNIKMIWNYAGNTLInqHSDDNNTTRA-LLDDEskcEFIVVIDNFMTPSARYADILLPDTTELE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 436 NTDFY-TSYW--HHYIQLQQPVIERYGESKSNTEVFRLLAEAMGFTDQ--ELKdSDEELIRQALDHPDNPYLAEIDYDSL 510
Cdd:cd02770 470 REDIVlTSNAgmMEYLIYSQKAIEPLYECKSDYEICAELAKRLGVEDQftEGK-TEQEWLEELYGQTRAKEPGLPTYEEF 548
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2234329652 511 TKHSFMKAKRKKPL--------FPG--KLPTPSGKIELYSEKMKQ--------DGFPALPTYTP 556
Cdd:cd02770 549 REKGIYRVPRALPFvafedfreDPEnnPLKTPSGKIEIYSKALADmaktlpegDEIPAIPKYVP 612
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
24-556 |
1.42e-100 |
|
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: 320.33 E-value: 1.42e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 24 CGLLIHKKDGKIVKVQGDPDHPVtagNICNKVRNMTERIYDEKRLTTPLKRTG----------AKGQAIFEPISWDEAID 93
Cdd:cd02751 7 GPFKAHVKDGVIVRVEPDDTDQP---RPCPRGRSVRDRVYSPDRIKYPMKRVGwlgngpgsreLRGEGEFVRISWDEALD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 94 TITSRWKQLIDEEGAESIlpysfYGNMGKLTAEGmdrRFFYrmGSSQLER-------------TICSKAGSEGYKYTMGI 160
Cdd:cd02751 84 LVASELKRIREKYGNEAI-----FGGSYGWASAG---RLHH--AQSLLHRflnliggylgsygTYSTGAAQVILPHVVGS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 161 SAGIDPEETI-----HTKLFIFWGINAVSTNM-------HQITIA-QKVRKQGAKIVVIDVHKNQTGRL--ADWfIPIKP 225
Cdd:cd02751 154 DEVYEQGTSWddiaeHSDLVVLFGANPLKTRQgggggpdHGSYYYlKQAKDAGVRFICIDPRYTDTAAVlaAEW-IPIRP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 226 GTDSALALGIMHILFKENLHDEAFLSEYTVGYEDLREHV--------KqyDPEKVSLITGVSTEDIYQLARMYGeSSPSF 297
Cdd:cd02751 233 GTDVALMLAMAHTLITEDLHDQAFLARYTVGFDEFKDYLlgesdgvpK--TPEWAAEITGVPAETIRALAREIA-SKRTM 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 298 IRIGNGIQHHDNGGMIVRTIACLPAITGQWLHKGG--GAIKHNSGILEYNTNALQRPDLLKGRTPRS------------- 362
Cdd:cd02751 310 IAQGWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGgfGFGYGYSNGGGPPRGGAGGPGLPQGKNPVKdsipvariadall 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 363 ---FNMNQLGKVLleTDPPIRSLFIYGTNPAVVAPEANKVRQGLLREDLFtVVHDLFLTETAAYADIVLPATSAFENTDF 439
Cdd:cd02751 390 npgKEFTANGKLK--TYPDIKMIYWAGGNPLHHHQDLNRLIKALRKDETI-VVHDIFWTASARYADIVLPATTSLERNDI 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 440 --YTSYWHHYIQLQQPVIERYGESKSNTEVFRLLAEAMGFTDQ--ELKDSDE---ELIRQALDHPDNPYLAEIDYDSLTK 512
Cdd:cd02751 467 glTGNYSNRYLIAMKQAVEPLGEARSDYEIFAELAKRLGVEEEftEGRDEMEwleHLYEETRAKAAGPGPELPSFEEFWE 546
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 2234329652 513 HSFMKAKRKKPLFPG-----------KLPTPSGKIELYSEKMKQ---DGFPALPTYTP 556
Cdd:cd02751 547 KGIVRVPAAPKPFVAfadfredpeanPLGTPSGKIEIYSETLADfgyDDCPGHPTWIE 604
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
13-535 |
3.89e-98 |
|
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: 311.07 E-value: 3.89e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 13 KSVCSLdCPDQCGLLIHKKDGKIVKVQGDPDHPVTAGNICNKVRNMTERIYDEKRLTTPLKRTGAKgqaiFEPISWDEAI 92
Cdd:cd02753 1 KTVCPY-CGVGCGLELWVKDNKIVGVEPVKGHPVNRGKLCVKGRFGFDFVNSKDRLTKPLIRKNGK----FVEASWDEAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 93 DTITSRWKQLIDEEGAESIlpySFYGNmGKLTAE------GMDRRFFyrmGSSQLERT--ICSKAGSEGYKYTMGISAGI 164
Cdd:cd02753 76 SLVASRLKEIKDKYGPDAI---AFFGS-AKCTNEenylfqKLARAVG---GTNNVDHCarLCHSPTVAGLAETLGSGAMT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 165 DP-EETIHTKLFIFWGINavSTNMHQItIAQKVR---KQGAKIVVIDVHKNQTGRLADWFIPIKPGTDSALALGIMHILF 240
Cdd:cd02753 149 NSiADIEEADVILVIGSN--TTEAHPV-IARRIKrakRNGAKLIVADPRRTELARFADLHLQLRPGTDVALLNAMAHVII 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 241 KENLHDEAFLSEYTVGYEDLREHVKQYDPEKVSLITGVSTEDIYQLARMYGESSPSFIRIGNGIQHHDNGGMIVRTIACL 320
Cdd:cd02753 226 EEGLYDEEFIEERTEGFEELKEIVEKYTPEYAERITGVPAEDIREAARMYATAKSAAILWGMGVTQHSHGTDNVMALSNL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 321 PAITGQWLHKGGGAikhnsgileyntNALqrpdllkgrtpRSFNMNQ----LGkvLLETDPP--IRSLFIYGTNPAVVAP 394
Cdd:cd02753 306 ALLTGNIGRPGTGV------------NPL-----------RGQNNVQgacdMG--ALPNVLPgyVKALYIMGENPALSDP 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 395 EANKVRQGLLREDLFtVVHDLFLTETAAYADIVLPATSAFENTDFYTSYwHHYIQLQQPVIERYGESKSNTEVFRLLAEA 474
Cdd:cd02753 361 NTNHVRKALESLEFL-VVQDIFLTETAELADVVLPAASFAEKDGTFTNT-ERRVQRVRKAVEPPGEARPDWEIIQELANR 438
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 475 MGFTDQELKDSD--EElIRQAldhpdNPYLAEIDYDSLTKHSFM------KAKRKKP-LFPGKLPTPSGK 535
Cdd:cd02753 439 LGYPGFYSHPEEifDE-IARL-----TPQYAGISYERLERPGGLqwpcpdEDHPGTPiLHTERFATPDGK 502
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
13-535 |
4.64e-91 |
|
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: 294.13 E-value: 4.64e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 13 KSVCSLdCPDQCGLLIHKKDGKIVKVQGDPDHPVTAGNICNKVRNMTERIYDEKRLTTPLKRTGaKGQaiFEPISWDEAI 92
Cdd:cd02754 1 KTTCPY-CGVGCGVEIGVKDGKVVAVRGDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLLRRN-GGE--LVPVSWDEAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 93 DTITSRWKQLIDEEGAESIlpySFYGNmGKLTAE-----GMDRRFFyrMGSSQLE--RTICSKAGSEGYKYTMGISAGID 165
Cdd:cd02754 77 DLIAERFKAIQAEYGPDSV---AFYGS-GQLLTEeyyaaNKLAKGG--LGTNNIDtnSRLCMASAVAGYKRSFGADGPPG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 166 PEETI-HTKLFIFWGINAVStnMHQItIAQKVRK-----QGAKIVVIDVHKNQTGRLADWFIPIKPGTDSALALGIMHIL 239
Cdd:cd02754 151 SYDDIeHADCFFLIGSNMAE--CHPI-LFRRLLDrkkanPGAKIIVVDPRRTRTADIADLHLPIRPGTDLALLNGLLHVL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 240 FKENLHDEAFLSEYTVGYEDLREHVKQYDPEKVSLITGVSTEDIYQLARMYGESSPSFIRIGNGIQHHDNG--------- 310
Cdd:cd02754 228 IEEGLIDRDFIDAHTEGFEELKAFVADYTPEKVAEITGVPEADIREAARLFGEARKVMSLWTMGVNQSTQGtaannaiin 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 311 -----GMIVRTIACLPAITGQWLHKGG---GAIKHNSGILEYNTNALQR----------PDLLKGRTPRSFnMNQLGKVL 372
Cdd:cd02754 308 lhlatGKIGRPGSGPFSLTGQPNAMGGrevGGLANLLPGHRSVNNPEHRaevakfwgvpEGTIPPKPGLHA-VEMFEAIE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 373 letDPPIRSLFIYGTNPAVVAPEANKVRQGLLREDlFTVVHDLFL-TETAAYADIVLPATSAFENTDFYTSYwHHYIQLQ 451
Cdd:cd02754 387 ---DGEIKALWVMCTNPAVSLPNANRVREALERLE-FVVVQDAFAdTETAEYADLVLPAASWGEKEGTMTNS-ERRVSLL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 452 QPVIERYGESKSNTEVFRLLAEAMGFTDQELKDSDEEL---IRQAldHPDNPY-LAEIDYDSLTKHSF-----MKAKRKK 522
Cdd:cd02754 462 RAAVEPPGEARPDWWILADVARRLGFGELFPYTSPEEVfeeYRRL--SRGRGAdLSGLSYERLRDGGVqwpcpDGPPEGT 539
|
570
....*....|....*
gi 2234329652 523 P-LF-PGKLPTPSGK 535
Cdd:cd02754 540 RrLFeDGRFPTPDGR 554
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
13-551 |
5.81e-91 |
|
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: 294.00 E-value: 5.81e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 13 KSVCSLDCPDQCGLLIHKKDGKIVKVQG----DPDHPvtagNICnkVRNMTE--RIYDEKRLTTPLKRTGAKGQAIFEPI 86
Cdd:cd02765 1 YTACPPNCGGRCPLKCHVRDGKIVKVEPnewpDKTYK----RGC--TRGLSHlqRVYSPDRLKYPMKRVGERGEGKFERI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 87 SWDEAIDTITSRWKQLIDEEGAESILPYSFYGNMGKLTAEGMdrRFFYRMGSSQLERTICSKAGSeGYKYTMG---ISAG 163
Cdd:cd02765 75 TWDEALDTIADKLTEAKREYGGKSILWMSSSGDGAILSYLRL--ALLGGGLQDALTYGIDTGVGQ-GFNRVTGggfMPPT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 164 IDPEETIHTKLFIFWGINAVSTNMHQITIAQKVRKQGAKIVVIDVHKNQTGRLADWFIPIKPGTDSALALGIMHILFKEN 243
Cdd:cd02765 152 NEITDWVNAKTIIIWGSNILETQFQDAEFFLDARENGAKIVVIDPVYSTTAAKADQWVPIRPGTDPALALGMINYILEHN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 244 LHDEAFL-------------------------------------------------------SEYTV-------GYEDLR 261
Cdd:cd02765 232 WYDEAFLksntsapflvredngtllrqadvtatpaedgyvvwdtnsdspepvaatninpaleGEYTIngvkvhtVLTALR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 262 EHVKQYDPEKVSLITGVSTEDIYQLARMYGESSPSFIRIGNGIQHHDNGGMIVRTIACLPAITGQWLHKGGGAiKHNSGI 341
Cdd:cd02765 312 EQAASYPPKAAAEICGLEEAIIETLAEWYATGKPSGIWGFGGVDRYYHSHVFGRTAAILAALTGNIGRVGGGV-GQIKFM 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 342 LEYNTNALQrpdllkgrtpRSFNMNQLGKVLLETDppirslfiygtnpavvapeankvrqgllredlFTVVHDLFLTETA 421
Cdd:cd02765 391 YFMGSNFLG----------NQPDRDRWLKVMKNLD--------------------------------FIVVVDIFHTPTV 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 422 AYADIVLPATSAFENTDFYTSYWHH-YIQLQQPVIERYGESKSNTEVFRLLAEAMGFtDQELKDSDEELIRQALDHPDnP 500
Cdd:cd02765 429 RYADIVLPAAHWFEVEDLLVRYTTHpHVLLQQKAIEPLFESKSDFEIEKGLAERLGL-GDYFPKTPEDYVRAFMNSDD-P 506
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 2234329652 501 YLAEIDYDSLTKHSFMkAKRKKPLFP------GKLPTPSGKIELYSEKMKQD--GFPAL 551
Cdd:cd02765 507 ALDGITWEALKEEGII-MRLATPEDPyvayldQKFGTPSGKLEFYNEAAPELeeALPLP 564
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
14-552 |
4.31e-86 |
|
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: 277.64 E-value: 4.31e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 14 SVCSLdCPDQCGLLIHKKDGKIVKVQGDPDHPVTAGNICNKVRNMTERIYDEKRLTTPLKRTGAKGQAIFEPISWDEAID 93
Cdd:cd02755 3 SICEM-CSSRCGILARVEDGRVVKIDGNPLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRVGERGEGKFREASWDEALQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 94 TITSRWKQLIDEEGAESILpysFYGnmgkltAEGMDRRFFYR----MGSSQL---ERTiCSKAGSEGYKYTMGISAGIDP 166
Cdd:cd02755 82 YIASKLKEIKEQHGPESVL---FGG------HGGCYSPFFKHfaaaFGSPNIfshEST-CLASKNLAWKLVIDSFGGEVN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 167 EETIHTKLFIFWGINA----VSTNMHQITIAqkvRKQGAKIVVIDVHKNQTGRLADWFIPIKPGTDSALALGIMHILFKE 242
Cdd:cd02755 152 PDFENARYIILFGRNLaeaiIVVDARRLMKA---LENGAKVVVVDPRFSELASKADEWIPIKPGTDLAFVLALIHVLISE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 243 NLHDEAFLSEYTVGYEDLREHVKQYDPEKVSLITGVSTEDIYQLARMYGESSP-SFIRIGNGIQHHDNGGMIVRTIACLP 321
Cdd:cd02755 229 NLYDAAFVEKYTNGFELLKAHVKPYTPEWAAQITDIPADTIRRIAREFAAAAPhAVVDPGWRGTFYSNSFQTRRAIAIIN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 322 AITGQWLHKGGgaikhnsgileyntnalqrpdLLKGRTPRSFnmnqlgkvlletdpPIRSLFIYGTNPAVVAPEANKVRQ 401
Cdd:cd02755 309 ALLGNIDKRGG---------------------LYYAGSAKPY--------------PIKALFIYRTNPFHSMPDRARLIK 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 402 GLLREDLFtVVHDLFLTETAAYADIVLPATSAFENTDFYT--SYWHHYIQLQQPVIERYGESKSNTEVFRLLAEAMGFtd 479
Cdd:cd02755 354 ALKNLDLV-VAIDILPSDTALYADVILPEATYLERDEPFSdkGGPAPAVATRQRAIEPLYDTRPGWDILKELARRLGL-- 430
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2234329652 480 qelkdsdeelirqaldhpdnpylaeidydsltkhsfmkakrkkplfpgkLPTPSGKIELYSEKMKQDGFPALP 552
Cdd:cd02755 431 -------------------------------------------------FGTPSGKIELYSPILAKAGYDPLP 454
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
5-679 |
4.64e-84 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 281.92 E-value: 4.64e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 5 ATQQNGIFKSVCSLDCPDQCGLLIHKKDGKIVKVQ----GDPD----HPVTAgniCNKVRNMTERIYDEKRLTTPLKRTG 76
Cdd:PRK14990 52 TKSDEKVIWSACTVNCGSRCPLRMHVVDGEIKYVEtdntGDDNydglHQVRA---CLRGRSMRRRVYNPDRLKYPMKRVG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 77 AKGQAIFEPISWDEAIDTITSRWKQLIDEEGAESIlpysfYGNMGKLTAEGMDRRfFYRMGSSQLERTICSKAG------ 150
Cdd:PRK14990 129 ARGEGKFERISWEEAYDIIATNMQRLIKEYGNESI-----YLNYGTGTLGGTMTR-SWPPGNTLVARLMNCCGGylnhyg 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 151 -------SEGYKYTMGISA-GIDPEETIHTKLFIFWGINAVSTNMH----QITIAQKVRKQGAKIVVIDVHKNQT--GRL 216
Cdd:PRK14990 203 dyssaqiAEGLNYTYGGWAdGNSPSDIENSKLVVLFGNNPGETRMSgggvTYYLEQARQKSNARMIIIDPRYTDTgaGRE 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 217 ADWfIPIKPGTDSALALGIMHILFKENLHDEAFLSEYTVGYED--------LREHVKQY-----------DPEKVSLITG 277
Cdd:PRK14990 283 DEW-IPIRPGTDAALVNGLAYVMITENLVDQPFLDKYCVGYDEktlpasapKNGHYKAYilgegpdgvakTPEWASQITG 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 278 VSTEDIYQLARMYGESSPSFIRIGNGIQHHDNGGMIVRTIACLPAITGQWLHKGGgaikhNSGILE--YNTNALQRPDL- 354
Cdd:PRK14990 362 VPADKIIKLAREIGSTKPAFISQGWGPQRHANGEIATRAISMLAILTGNVGINGG-----NSGAREgsYSLPFVRMPTLe 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 355 -----------LKGRTPRSFNMNQL-----GKVLLetDPPIRSLFIYGTNPAVVA-PEANKVRQgLLREDL---FTVVHD 414
Cdd:PRK14990 437 npiqtsismfmWTDAIERGPEMTALrdgvrGKDKL--DVPIKMIWNYAGNCLINQhSEINRTHE-ILQDDKkceLIVVID 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 415 LFLTETAAYADIVLPATSAFENTDFYTSYW---HHYIQLQQPVIERYGESKSNTEVFRLLAEAMGFTDQ--ELKDSDE-- 487
Cdd:PRK14990 514 CHMTSSAKYADILLPDCTASEQMDFALDAScgnMSYVIFNDQVIKPRFECKTIYEMTSELAKRLGVEQQftEGRTQEEwm 593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 488 ----ELIRQALdhPDNPYLAEIDYDSLTK-------HSFMKAKRKKPLfPGKLPTPSGKIELYSEKMKQ----------D 546
Cdd:PRK14990 594 rhlyAQSREAI--PELPTFEEFRKQGIFKkrdpqghHVAYKAFREDPQ-ANPLTTPSGKIEIYSQALADiaatwelpegD 670
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 547 GFPALPTYTPLVSDNEHPFMY-VPAPNHNF-----LNSTFSNNEKhIRLEKTPKLFINTKDADEHGIVDGDPVRIWNSRG 620
Cdd:PRK14990 671 VIDPLPIYTPGFESYQDPLNKqYPLQLTGFhyksrVHSTYGNVDV-LKAACRQEMWINPLDAQKRGINNGDKVRIFNDRG 749
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2234329652 621 ECELTAAVGEQVLPGVV-VSQGLWADePGKKQL-----VNALTPDRLSDMGGGATFFSGRVQIEK 679
Cdd:PRK14990 750 EVHIEAKVTPRMMPGVVaLGEGAWYD-PDAKRVdkggcINVLTTQRPSPLAKGNPSHTNLVQVEK 813
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
11-548 |
1.72e-78 |
|
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: 259.68 E-value: 1.72e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 11 IFKSVCSlDCPDQCGLLIHKKDGKIVKVQGDPDHPVTAGNICNKVRNMTERIYDEKRLTTPLKRTGAKG----QAIFEPI 86
Cdd:cd02757 1 WVPSTCQ-GCTAWCGLQAYVEDGRVTKVEGNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRTNPRKgrdvDPKFVPI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 87 SWDEAIDTITSRWKQLIDE-EGAESILPYSFYGNMGKLTAEgmdrRFFYRMGSSQL--ERTICSKAGSEGYKYTMGISAG 163
Cdd:cd02757 80 SWDEALDTIADKIRALRKEnEPHKIMLHRGRYGHNNSILYG----RFTKMIGSPNNisHSSVCAESEKFGRYYTEGGWDY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 164 IDPEETiHTKLFIFWGINAVSTNM---HQITIAQKVRKQgAKIVVIDVHKNQTGRLADWFIPIKPGTDSALALGIMHILF 240
Cdd:cd02757 156 NSYDYA-NAKYILFFGADPLESNRqnpHAQRIWGGKMDQ-AKVVVVDPRLSNTAAKADEWLPIKPGEDGALALAIAHVIL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 241 KENLHDEAFLSEYTVGYEDLR-----------------------EHVKQYDPEKVSLITGVSTEDIYQLARMYGESSPSF 297
Cdd:cd02757 234 TEGLWDKDFVGDFVDGKNYFKagetvdeesfkeksteglvkwwnLELKDYTPEWAAKISGIPAETIERVAREFATAAPAA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 298 IR-IGNGIQHHDNGGMIVRTIACLPAITGQWLHKGGgaikhnsgileYNTNAlqrpdllkgrtprsfnmnqlgkvlleTD 376
Cdd:cd02757 314 AAfTWRGATMQNRGSYNSMACHALNGLVGSIDSKGG-----------LCPNM--------------------------GV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 377 PPIRSLFIYGTNPAVVAPEaNKVRQGLLREDLFTVVHDLFLTETAAYADIVLPATSAFENTDFYTSY--WHHYIQLQQPV 454
Cdd:cd02757 357 PKIKVYFTYLDNPVFSNPD-GMSWEEALAKIPFHVHLSPFMSETTYFADIVLPDGHHFERWDVMSQEnnLHPWLSIRQPV 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 455 IERYGESKSNTEVFRLLAEAMGftdqelKDSDEELIRQALdhpdNPYLAEIDYDSlTKHSFMKAkrkkplfpgkLPTPSG 534
Cdd:cd02757 436 VKSLGEVREETEILIELAKKLD------PKGSDGMKRYAP----GQFKDPETGKN-NRWEFENV----------FPTETG 494
|
570
....*....|....
gi 2234329652 535 KIELYSEKMKQDGF 548
Cdd:cd02757 495 KFEFYSETLKKYLQ 508
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
13-546 |
4.56e-71 |
|
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: 240.38 E-value: 4.56e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 13 KSVCSLdCPDQCGLLIHKKDGKIVKVQGDPDHPVTAGNICNKVRNMTERIYDEKRLTTPLKRTGAKgqaiFEPISWDEAI 92
Cdd:cd02762 1 KRACIL-CEANCGLVVTVEDGRVASIRGDPDDPLSKGYICPKAAALGDYQNDPDRLRTPMRRRGGS----FEEIDWDEAF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 93 DTITSRWKQLIDEEGAESILPYSfyGNMGKLTAEGM-----------DRRFFYRMGSSQLERTICSkagsegykYTMGIS 161
Cdd:cd02762 76 DEIAERLRAIRARHGGDAVGVYG--GNPQAHTHAGGayspallkalgTSNYFSAATADQKPGHFWS--------GLMFGH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 162 AGIDPEETI-HTKLFIFWGINAVSTNMHQITIAQKV------RKQGAKIVVIDVHKNQTGRLADWFIPIKPGTDSALALG 234
Cdd:cd02762 146 PGLHPVPDIdRTDYLLILGANPLQSNGSLRTAPDRVlrlkaaKDRGGSLVVIDPRRTETAKLADEHLFVRPGTDAWLLAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 235 IMHILFKENLHDEAFLSEYTVGYEDLREHVKQYDPEKVSLITGVSTEDIYQLARMYGESSPSFIRIGNGIQHHDNGGMIV 314
Cdd:cd02762 226 MLAVLLAEGLTDRRFLAEHCDGLDEVRAALAEFTPEAYAPRCGVPAETIRRLAREFAAAPSAAVYGRLGVQTQLFGTLCS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 315 RTIACLPAITGQwLHKGGGAIKHNSGILEYNTNALQRPDLLKGRTPRS--------FNMNQLGKVLLETDP-PIRSLFIY 385
Cdd:cd02762 306 WLVKLLNLLTGN-LDRPGGAMFTTPALDLVGQTSGRTIGRGEWRSRVSglpeiageLPVNVLAEEILTDGPgRIRAMIVV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 386 GTNPAVVAPEANKVRQGLLREDLFTVVhDLFLTETAAYADIVLPATSAFENTD---FYTSYWHHYIQLQQPVIERYGESK 462
Cdd:cd02762 385 AGNPVLSAPDGARLEAALGGLEFMVSV-DVYMTETTRHADYILPPASQLEKPHatfFNLEFPRNAFRYRRPLFPPPPGTL 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 463 SNTEVFRLLAEAM------GFTDqeLKDSDEELIRQALDHPDNPYLAEIDYDsltkhsfmkakrkkplFPGKLPTPSGKI 536
Cdd:cd02762 464 PEWEILARLVEALdavlraGFYG--ERAGGTLLLAALLERPSGVDLGPLTPR----------------LWQRLRTPDGRI 525
|
570
....*....|
gi 2234329652 537 ELYSEKMKQD 546
Cdd:cd02762 526 HLAPPELLDE 535
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
14-680 |
1.35e-64 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 227.63 E-value: 1.35e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 14 SVCSLdCPDQCGLLIHKKDGKIVKVQGDPDHPVTAGNICNKVRNMTERIYDEKRLTTPLKRTGAKGQAIFEPISWDEAID 93
Cdd:PRK15488 46 SICEM-CSTRCPIEARVVNGKNVFIQGNPKAKSFGTKVCARGGSGHSLLYDPQRIVKPLKRVGERGEGKWQEISWDEAYQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 94 TITSRWKQLIDEEGAESIlpySFYGNMGKLtaEGMDRRFFYRMGSSQL--ERTICSKAGSEGYKYTMGISAGIDPEETIH 171
Cdd:PRK15488 125 EIAAKLNAIKQQHGPESV---AFSSKSGSL--SSHLFHLATAFGSPNTftHASTCPAGYAIAAKVMFGGKLKRDLANSKY 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 172 TKLF---IFWGINAVSTnmHQITIAQKvrKQGAKIVVIDVHKNQTGRLADWFIPIKPGTDSALALGIMHILFKENLHDEA 248
Cdd:PRK15488 200 IINFghnLYEGINMSDT--RGLMTAQM--EKGAKLVVFEPRFSVVASKADEWHAIRPGTDLAVVLALCHVLIEENLYDKA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 249 FLSEYTVGYEDLREHVKQYDPEKVSLITGVSTEDIYQLARMYGESSPSFI-RIGNGIQHHDNGGMIVRTIACLPAITGQW 327
Cdd:PRK15488 276 FVERYTSGFEELAASVKEYTPEWAEAISDVPADDIRRIARELAAAAPHAIvDFGHRATFTPEEFDMRRAIFAANVLLGNI 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 328 LHKGGGAIKHNSGIleYNTNA-------LQRPDL----------LKGRTPRSFNMNQLGKVL-------LETDP-PIRSL 382
Cdd:PRK15488 356 ERKGGLYFGKNASV--YNKLAgekvaptLAKPGVkgmpkptakrIDLVGEQFKYIAAGGGVVqsiidatLTQKPyQIKGW 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 383 FIYGTNPAVVAPEANKVRQGLLREDlFTVVHDLFLTETAAYADIVLPATSAFENTDFYT--SYWHHYIQLQQPVIERYGE 460
Cdd:PRK15488 434 VMSRHNPMQTVTDRADVVKALKKLD-LVVVCDVYLSESAAYADVVLPESTYLERDEEISdkSGKNPAYALRQRVVEPIGD 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 461 SKSNTEVFRLLAEAMG----FTDQELKD-------SDEELIRQaldhpdnpyLAEIDYDSLTKHSFMKAK------RKKp 523
Cdd:PRK15488 513 TKPSWQIFKELGEKMGlgqyYPWQDMETlqlyqvnGDHALLKE---------LKKKGYVSFGVPLLLREPkmvakfVAR- 582
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 524 lFPG--------------KLPTPSGKIELYSEKMKQDgFP--ALPTYTP--LVSDNEHPFM-------------YVPapn 572
Cdd:PRK15488 583 -YPNakavdedgtygsqlKFKTPSGKIELFSAKLEAL-APgyGVPRYRDvaLKKEDELYFIqgkvavhtngatqNVP--- 657
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 573 hnFLNSTFSNNekhirlektpKLFINTKDADEHGIVDGDPVRIWNSRGECELTAAVGEQVLPGVV-VSQGLWADEPGKKQ 651
Cdd:PRK15488 658 --LLANLMSDN----------AVWIHPQTAGKLGIKNGDEIRLENSVGKEKGKALVTPGIRPDTLfAYMGFGSKNKELTR 725
|
730 740 750
....*....|....*....|....*....|....*
gi 2234329652 652 L------VNALTPDRLSDMGGGATFFSGrVQIEKA 680
Cdd:PRK15488 726 AtgkgihCGNLLPHVTSPVSGTNVHTTG-VTLSKA 759
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
11-472 |
1.72e-62 |
|
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: 215.26 E-value: 1.72e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 11 IFKSVCSLDCPDQCGLLIHKKDGKIVKVQGDPDHPVTAGNI-------CNKVRNMTERIYDEKRLTTPLKRTGAKGQAIF 83
Cdd:cd02750 3 VVRSTHGVNCTGSCSWNVYVKNGIVTREEQATDYPETPPDLpdynprgCQRGASFSWYLYSPDRVKYPLKRVGARGEGKW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 84 EPISWDEAIDTITSRWKQLIDEEGAESILPYSFYGNMGKLT-AEGMdrRFFYRMGSSQLErticskagseGYKYTMGISA 162
Cdd:cd02750 83 KRISWDEALELIADAIIDTIKKYGPDRVIGFSPIPAMSMVSyAAGS--RFASLIGGVSLS----------FYDWYGDLPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 163 GI-----------DPEETIHTKLFIFWGINAVST---NMHQITIAqkvRKQGAKIVVIDVHKNQTGRLADWFIPIKPGTD 228
Cdd:cd02750 151 GSpqtwgeqtdvpESADWYNADYIIMWGSNVPVTrtpDAHFLTEA---RYNGAKVVVVSPDYSPSAKHADLWVPIKPGTD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 229 SALALGIMHILFKENLHDEAFLSEYTvgyeDLREHVkqYDPEKVSLITGVSTEDIYQLARMYGESSPSFIRIGNGIQHHD 308
Cdd:cd02750 228 AALALAMAHVIIKEKLYDEDYLKEYT----DLPFLV--YTPAWQEAITGVPRETVIRLAREFATNGRSMIIVGAGINHWY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 309 NGGMIVRTIACLPAITGQWLHKGGGAikhnsgileyNTNALQrpdllkgrtprsfnmnqlgkvlletdppIRSLFIYGTN 388
Cdd:cd02750 302 HGDLCYRALILLLALTGNEGKNGGGW----------AHYVGQ----------------------------PRVLFVWRGN 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 389 PAVVAPEANKVRQGLLREDL-FTVVHDLFLTETAAYADIVLPATSAFENTDFYTSYWHHYIQLQQPVIERYGESKSNTEV 467
Cdd:cd02750 344 LFGSSGKGHEYFEDAPEGKLdLIVDLDFRMDSTALYSDIVLPAATWYEKHDLSTTDMHPFIHPFSPAVDPLWEAKSDWEI 423
|
....*
gi 2234329652 468 FRLLA 472
Cdd:cd02750 424 FKALA 428
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
31-554 |
1.97e-60 |
|
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: 213.28 E-value: 1.97e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 31 KDGKIVKVQGDPDHPVTAGNIcnkvRNMTERIYDEKRLTTPLKR-----------TGAKGQAIFEPISWDEAIDTITSRW 99
Cdd:cd02769 14 KDGRIVGVRPFEEDPDPSPLL----DGVPDAVYSPTRIKYPMVRrgwlekgpgsdRSLRGKEEFVRVSWDEALDLVAAEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 100 KQLIDEEGAESILPYSfYG--NMGKL-TAEGMDRRFFYRMGSSqlerticskAGSEGyKYTMGISAGIDPE--------- 167
Cdd:cd02769 90 KRVRKTYGNEAIFGGS-YGwsSAGRFhHAQSLLHRFLNLAGGY---------VGSVG-DYSTGAAQVILPHvvgsmevyt 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 168 ------ETI--HTKLFIFWGINAVSTNM--------HQITIA-QKVRKQGAKIVVIDVHKNQTGRL--ADWfIPIKPGTD 228
Cdd:cd02769 159 eqqtswPVIaeHTELVVAFGADPLKNAQiawggipdHQAYSYlKALKDRGIRFISISPLRDDTAAElgAEW-IAIRPGTD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 229 SALALGIMHILFKENLHDEAFLSEYTVGYEDLREHV--------KqyDPEKVSLITGVSTEDIYQLARMYgESSPSFIRI 300
Cdd:cd02769 238 VALMLALAHTLVTEGLHDKAFLARYTVGFDKFLPYLlgesdgvpK--TPEWAAAICGIPAETIRELARRF-ASKRTMIMA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 301 GNGIQHHDNGGMIVRTIACLPAITGQWLHKGGG--AIKHNSGILEYNTNALQRPDLLKGRTPRS---------------- 362
Cdd:cd02769 315 GWSLQRAHHGEQPHWMAVTLAAMLGQIGLPGGGfgFGYHYSNGGGPPRGAAPPPALPQGRNPVSsfipvariadmllnpg 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 363 --FNMNqlGKVLleTDPPIRslFIY--GTNPAVVAPEANKVRQGLLREDLFtVVHDLFLTETAAYADIVLPATSAFENTD 438
Cdd:cd02769 395 kpFDYN--GKKL--TYPDIK--LVYwaGGNPFHHHQDLNRLIRAWQKPETV-IVHEPFWTATARHADIVLPATTSLERND 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 439 FYTSYWHHYIQLQQPVIERYGESKSNTEVFRLLAEAMGFTDQELKDSDE-ELIR--------QALDH----PD------- 498
Cdd:cd02769 468 IGGSGDNRYIVAMKQVVEPVGEARDDYDIFADLAERLGVEEQFTEGRDEmEWLRhlyeesraQAAARgvemPSfdefwaq 547
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 499 NPYLAEIDYDSLTKH-SFmkakRKKPLFpGKLPTPSGKIELYSEK---MKQDGFPALPTY 554
Cdd:cd02769 548 GYVELPIPEADFVRLaDF----REDPEA-NPLGTPSGRIEIFSETiagFGYDDCPGHPTW 602
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
13-506 |
1.77e-56 |
|
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: 203.40 E-value: 1.77e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 13 KSVCSLdCPDQCGLLIHKKDGKIVKVQGDPDHPVTAGNICNKVRNMTERIYDEKRLTTPLKRTGAKGQaiFEPISWDEAI 92
Cdd:cd02752 1 RTICPY-CSVGCGLIAYVQNGVWVHQEGDPDHPVNRGSLCPKGAALRDFVHSPKRLKYPMYRAPGSGK--WEEISWDEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 93 DTITSRWKQLIDEEGAESilpysfygNMGKLTAEGMDRRFFyrMGSSQLerticskAGSEGYKYT-----MGISAgIDPE 167
Cdd:cd02752 78 DEIARKMKDIRDASFVEK--------NAAGVVVNRPDSIAF--LGSAKL-------SNEECYLIRkfaraLGTNN-LDHQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 168 ETI--------------------------HTKLFIFWGINA-----VStnMHQITIAQKvrKQGAKIVVIDVHKNQTGRL 216
Cdd:cd02752 140 ARIuhsptvaglantfgrgamtnswndikNADVILVMGGNPaeahpVS--FKWILEAKE--KNGAKLIVVDPRFTRTAAK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 217 ADWFIPIKPGTDSALALGIMHILFKenlhdeaflseytvgyedlrehvkqYDPEKVSLITGVSTEDIYQLARMYGESS-- 294
Cdd:cd02752 216 ADLYVPIRSGTDIAFLGGMINYIIR-------------------------YTPEEVEDICGVPKEDFLKVAEMFAATGrp 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 295 --PSFIRIGNGIQHHDNGGMIVRTIACLPAITGQWLHKGGGaikhnsgileynTNALQRPDLLKGRTPRSFNMNQLgkvl 372
Cdd:cd02752 271 dkPGTILYAMGWTQHTVGSQNIRAMCILQLLLGNIGVAGGG------------VNALRGHSNVQGATDLGLLSHNL---- 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 373 letdPPirslFIYGTNPAVVAPEANKVRQGLLREDLFtVVHDLFLTETAAYAD-------------IVLPATSAFEnTDF 439
Cdd:cd02752 335 ----PG----YLGGQNPNSSFPNANKVRRALDKLDWL-VVIDPFPTETAAFWKnpgmdpksiqtevFLLPAACQYE-KEG 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2234329652 440 YTSYWHHYIQLQQPVIERYGESKSNTEVFRLLAEAMGFTDQELKDS-DEELIRQALDHPDNPYLAEID 506
Cdd:cd02752 405 SITNSGRWLQWRYKVVEPPGEAKSDGDILVELAKRLGFLYEKEGGAfPEPITKWNYGYGDEPTPEEIA 472
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
563-677 |
2.53e-46 |
|
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: 159.75 E-value: 2.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 563 HPFMYVPAPNHNFLNSTFSNNEKHIRLEKTPKLFINTKDADEHGIVDGDPVRIWNSRGECELTAAVGEQVLPGVVVSQGL 642
Cdd:cd02786 1 YPLRLITPPAHNFLNSTFANLPELRAKEGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVVVAEGG 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 2234329652 643 WADEPGKK-QLVNALTPDRLSDMGGGATFFSGRVQI 677
Cdd:cd02786 81 WWREHSPDgRGVNALTSARLTDLGGGSTFHDTRVEV 116
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
13-476 |
8.26e-43 |
|
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: 164.62 E-value: 8.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 13 KSVCSLdCPDQCGLLIHKKDGKIVKVQGDPDHPVTAGNICNKVRNMTERIYDEKRLTTPLKRTGAKGQAIFEPISWDEAI 92
Cdd:cd02763 1 TTTCYM-CACRCGIRVHLRDGKVRYIKGNPDHPLNKGVICAKGSSGIMKQYSPARLTKPLLRKGPRGSGQFEEIEWEEAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 93 DTITSRWKQLIDEEgaesilPYSFYGNMGKLTAEGMDRRFFYRMGSSQLER--TICSKAGSEGYKYTMGIS----AGIDP 166
Cdd:cd02763 80 SIATKRLKAARATD------PKKFAFFTGRDQMQALTGWFAGQFGTPNYAAhgGFCSVNMAAGGLYSIGGSfwefGGPDL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 167 EetiHTKLFIFWGInAVSTNMHQITIA-QKVRKQGAKIVVIDVHKNQTGRLADWFIPIKPGTDSALALGIMHILFKENLH 245
Cdd:cd02763 154 E---HTKYFMMIGV-AEDHHSNPFKIGiQKLKRRGGKFVAVNPVRTGYAAIADEWVPIKPGTDGAFILALAHELLKAGLI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 246 DEAFLSEYTVGYEdlrehVKQYDPEKVSLITGVSTEDIYQLARMYGESS-------------------------PSFIRI 300
Cdd:cd02763 230 DWEFLKRYTNAAE-----LVDYTPEWVEKITGIPADTIRRIAKELGVTArdqpielpiawtdvwgrkhekitgrPVSFHA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 301 GNGIQHHDNGGMIVRTIACLPAITGQ------WLHK---------------GGGAIKHNSGILEYNTNALQRPDLL---- 355
Cdd:cd02763 305 MRGIAAHSNGFQTIRALFVLMMLLGTidrpggFRHKppyprhipplpkppkIPSADKPFTPLYGPPLGWPASPDDLlvde 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 356 KG---RTPRSFN----------MNQLGKVLLETDP-PIRSLFIYGTNPAVVAP-EANKVRQGLLREDL-------FTVVH 413
Cdd:cd02763 385 DGnplRIDKAYSweyplaahgcMQNVITNAWRGDPyPIDTLMIYMANMAWNSSmNTPEVREMLTDKDAsgnykipFIIVC 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2234329652 414 DLFLTETAAYADIVLPATSAFENTDfYTSYWHHYIQ--------LQQPVIERYGESKSNTEVFRLLAEAMG 476
Cdd:cd02763 465 DAFYSEMVAFADLVLPDTTYLERHD-AMSLLDRPISeadgpvdaIRVPIVEPKGDVKPFQEVLIELGTRLG 534
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
67-474 |
2.44e-41 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 154.10 E-value: 2.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 67 RLTTPLKRTGaKGQaiFEPISWDEAIDTITSRWKQLIDEEGAESILPY----------SFYgNMGKLTAEGMDRRFFYRM 136
Cdd:pfam00384 1 RLKYPMVRRG-DGK--FVRVSWDEALDLIAKKLKRIIKKYGPDAIAINggsggltdveSLY-ALKKLLNRLGSKNGNTED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 137 GSSQLERTICSKAGS-EGYKYTMGIS-AGIDpeetiHTKLFIFWGIN----AVSTNMHqitIAQKVRKQGAKIVVIDVHK 210
Cdd:pfam00384 77 HNGDLCTAAAAAFGSdLRSNYLFNSSiADIE-----NADLILLIGTNpreeAPILNAR---IRKAALKGKAKVIVIGPRL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 211 NQTgrLADWFIPIKPGTDSALALGIMHILFKENLHDEAFlseytvgyedlrehvkqydpekvslitgvstediyqlarmy 290
Cdd:pfam00384 149 DLT--YADEHLGIKPGTDLALALAGAHVFIKELKKDKDF----------------------------------------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 291 gESSPSFIrIGNGIQHHDNGGMIVRTIACLPAITGQWLHKGGG--AIKHNSGILEYnTNALQRPDLLKGRTPRSFNMNQL 368
Cdd:pfam00384 186 -APKPIII-VGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGwnGLNILQGAASP-VGALDLGLVPGIKSVEMINAIKK 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 369 GKvlletdppIRSLFIYGTNPAVVAPEANKVRQGLLREDLFtVVHDLFL-TETAAYADIVLPATSAFENTDFYTSYwHHY 447
Cdd:pfam00384 263 GG--------IKVLYLLGNNPFVTHADENRVVKALQKLDLF-VVYDGHHgDKTAKYADVILPAAAYTEKNGTYVNT-EGR 332
|
410 420
....*....|....*....|....*..
gi 2234329652 448 IQLQQPVIERYGESKSNTEVFRLLAEA 474
Cdd:pfam00384 333 VQSTKQAVPPPGEAREDWKILRALSEV 359
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
171-656 |
9.73e-37 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 147.51 E-value: 9.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 171 HTKLFIFWGINAV-------STNMHQI-----TIAQKVRKQGAKIVVIDVHKNQTGR-LADWFIPIKPGTDSALALGIMH 237
Cdd:PRK15102 213 NSKTIVLWGSDPVknlqvgwNCETHESyaylaQLKEKVAKGEINVISIDPVVTKTQNyLGCEHLYVNPQTDVPLMLALAH 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 238 ILFKENLHDEAFLSEYTVGYED-----LREHVKQ-YDPEKVSLITGVSTEDIYQLARMYGESSPSFIrIGNGIQHHDNGG 311
Cdd:PRK15102 293 TLYSENLYDKKFIDNYCLGFEQflpylLGEKDGVpKTPEWAEKICGIDAETIRELARQMAKGRTQII-AGWCIQRQQHGE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 312 MIVRTIACLPAITGQWLHKGGGaIK---HNSGILEYNTNAlqrpdLLKGRTPRSFNMNQLGK------------------ 370
Cdd:PRK15102 372 QPYWMGAVLAAMLGQIGLPGGG-ISyghHYSGIGVPSSGG-----AIPGGFPGNLDTGQKPKhdnsdykgysstipvarf 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 371 --VLLE------------TDPPIRSLFIYGTNPAVVAPEANKVRQGLLRedLFTVVH-DLFLTETAAYADIVLPATSAFE 435
Cdd:PRK15102 446 idAILEpgktinwngkkvTLPPLKMMIFSGTNPWHRHQDRNRMKEAFRK--LETVVAiDNQWTATCRFADIVLPACTQFE 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 436 NTDF--YTSYWHHYIQLQQPVIERYGESKSNTEVFRLLAEAMGFTDQELKDSDE---------ELIRQALDHPDNPYLAE 504
Cdd:PRK15102 524 RNDIdqYGSYSNRGIIAMKKVVEPLFESRSDFDIFRELCRRFGREKEYTRGMDEmgwlkrlyqECKQQNKGKFHMPEFDE 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 505 ------IDYDS---LTKHSfmkAKRKKP-LFPgkLPTPSGKIELYSEKMKQDGF---PALPTYT---------PlvSDNE 562
Cdd:PRK15102 604 fwkkgyVEFGEgqpWVRHA---DFREDPeLNP--LGTPSGLIEIYSRKIADMGYddcQGHPMWFekiershggP--GSDK 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 563 HPF-MYVPAPNHNfLNSTFSNNEKhIRLEKTPK----LFINTKDADEHGIVDGDPVRIWNSRGECELTAAVGEQVLPGVV 637
Cdd:PRK15102 677 YPLwLQSVHPDKR-LHSQLCESEE-LRETYTVQgrepVYINPQDAKARGIKDGDVVRVFNDRGQVLAGAVVSDRYPPGVI 754
|
570 580
....*....|....*....|
gi 2234329652 638 -VSQGLWADePGKKQLVNAL 656
Cdd:PRK15102 755 rIHEGAWYG-PDKGGEIGAL 773
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
14-508 |
5.22e-34 |
|
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other related proteins. The Salmonella enterica tetrathionate reductase catalyses the reduction of trithionate but not sulfur or thiosulfate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239159 [Multi-domain] Cd Length: 735 Bit Score: 138.63 E-value: 5.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 14 SVCsLDCPDQCGL--LIHKKDGKIVKVQGDPDHP----------------------VTAGN-----ICNKVRNMTERIYD 64
Cdd:cd02758 2 SSC-LGCWTQCGIrvRVDKETGKVLRIAGNPYHPlntapslpyntplkeslylslvGENGLkaratACARGNAGLQYLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 65 EKRLTTPLKRTGAKGQAIFEPISWDEAIDTITS----------------RWKQ-LIDEE----GAES-ILPYSFYGNMGk 122
Cdd:cd02758 81 PYRVLQPLKRVGPRGSGKWKPISWEQLIEEVVEggdlfgeghveglkaiRDLDtPIDPDhpdlGPKAnQLLYTFGRDEG- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 123 ltAEGMDRRFF-YRMGSSQLER--TICSKAGSEGYKYTMGISAGI-----DPEetiHTKLFIFWGIN-AVSTN---MHQI 190
Cdd:cd02758 160 --RTPFIKRFAnQAFGTVNFGGhgSYCGLSYRAGNGALMNDLDGYphvkpDFD---NAEFALFIGTSpAQAGNpfkRQAR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 191 TIAQKVRKQGAKIVVIDVHKNQTGRLAD----WfIPIKPGTDSALALGIMHILFKENLHDEAFLSE------YTVGYED- 259
Cdd:cd02758 235 RLAEARTEGNFKYVVVDPVLPNTTSAAGenirW-VPIKPGGDGALAMAMIRWIIENERYNAEYLSIpskeaaKAAGEPSw 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 260 ------------------LREHVKQYDPEKVSLITGVSTEDIYQLARMYGESSPSFIRIGNGIQHHDNGGMIVRTIACLP 321
Cdd:cd02758 314 tnathlvitvrvksalqlLKEEAFSYSLEEYAEICGVPEAKIIELAKEFTSHGRAAAVVHHGGTMHSNGFYNAYAIRMLN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 322 AITGQWLHKGGgaIKHNSGILEYNTNALqRPDLLK---GRTPRSFNMNQLG-----------KVLLETDP---------- 377
Cdd:cd02758 394 ALIGNLNWKGG--LLMSGGGFADNSAGP-RYDFKKffgEVKPWGVPIDRSKkayektseykrKVAAGENPypakrpwypl 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 378 ------------------PIRSLFIYGTNPAVVAPEANKVRQGLLRED----LFTVVhDLFLTETAAYADIVLPATSAFE 435
Cdd:cd02758 471 tpelyteviasaaegypyKLKALILWMANPVYGAPGLVKQVEEKLKDPkklpLFIAI-DAFINETSAYADYIVPDTTYYE 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 436 NTDFYTSYwhHYIQ-----LQQPVIERY------GESKSNTEVFRLLAEAM---GFTDQELKDSDEEliRQALDHPDNPY 501
Cdd:cd02758 550 SWGFSTPW--GGVPtkastARWPVIAPLtektanGHPVSMESFLIDLAKALglpGFGPNAIKDGQGN--KFPLNRAEDYY 625
|
650
....*....|
gi 2234329652 502 L---AEIDYD 508
Cdd:cd02758 626 LrvaANIAYD 635
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
67-431 |
1.08e-30 |
|
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: 127.42 E-value: 1.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 67 RLTTPLKRtgAKGQAIFEPISWDEAIDTITSRWKQLIDEEGAesilpysFYGNmGKLTAEG--MDRRFFYRMGSSQLERT 144
Cdd:cd02767 64 RLTYPMRY--DAGSDHYRPISWDEAFAEIAARLRALDPDRAA-------FYTS-GRASNEAayLYQLFARAYGTNNLPDC 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 145 --ICSKAGSEGYKYTMGISAG-IDPEETIHTKLFIFWGINAvSTN----MHQItiaQKVRKQGAKIVVIDVHKnQTG--- 214
Cdd:cd02767 134 snMCHEPSSVGLKKSIGVGKGtVSLEDFEHTDLIFFIGQNP-GTNhprmLHYL---REAKKRGGKIIVINPLR-EPGler 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 215 ---------------RLADWFIPIKPGTDSALALGIMHILFKE-----NLHDEAFLSEYTVGYEDLREHVKQYDPEKVSL 274
Cdd:cd02767 209 fanpqnpesmltggtKIADEYFQVRIGGDIALLNGMAKHLIERddepgNVLDHDFIAEHTSGFEEYVAALRALSWDEIER 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 275 ITGVSTEDIYQLARMYGESSPSFIRIGNGIQHHDNGGMIVRTIACLPAITGQWLHKGGGA--IKHNS---GILEYNTNAL 349
Cdd:cd02767 289 ASGLSREEIEAFAAMYAKSERVVFVWGMGITQHAHGVDNVRAIVNLALLRGNIGRPGAGLmpIRGHSnvqGDRTMGITEK 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 350 QRPDLLK------GRT-PRSFNMNQLgkVLLET--DPPIRSLFIYGTNPAVVAPEANKVRQGLLREDLfTVVHDLFLTET 420
Cdd:cd02767 369 PFPEFLDaleevfGFTpPRDPGLDTV--EAIEAalEGKVKAFISLGGNFAEAMPDPAATEEALRRLDL-TVHVATKLNRS 445
|
410
....*....|....
gi 2234329652 421 AAY---ADIVLPAT 431
Cdd:cd02767 446 HLVhgeEALILPCL 459
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
14-480 |
4.09e-27 |
|
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: 117.38 E-value: 4.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 14 SVCSLdCPDQCGLLIHK-KDGKIVKVQGDPD----HPvTAGNICNKVRNMTERIYDEKRLTTPLKRTGAKG----QAIFE 84
Cdd:cd02760 2 TYCYN-CVAGPDFMAVKvVDGVATEIEPNFAaediHP-ARGRVCVKAYGLVQKTYNPNRVLQPMKRTNPKKgrneDPGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 85 PISWDEAIDTITS-----RWKQLIDEEG--------AESILPYSFYGNMGKLTAE--GMDrrffYRMGSSQLertICSKA 149
Cdd:cd02760 80 PISWDEALDLVAAklrrvREKGLLDEKGlprlaatfGHGGTPAMYMGTFPAFLAAwgPID----FSFGSGQG---VKCVH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 150 GSEGYKYTMGISAGIDPEeTIHTKLFIFWGINA-VSTNMHQITIAQKVRKQGAKIVVIDVHKNQTGRLADWFIPIKPGTD 228
Cdd:cd02760 153 SEHLYGEFWHRAFTVAAD-TPLANYVISFGSNVeASGGPCAVTRHADARVRGYKRVQVEPHLSVTGACSAEWVPIRPKTD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 229 SALALGIMHILFKE---NLHDEAFL-----SEYTVG-------------------------------------------- 256
Cdd:cd02760 232 PAFMFAMIHVMVHEqglGKLDVPFLrdrtsSPYLVGpdglylrdaatgkplvwdersgravpfdtrgavpavagdfavdg 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 257 ---------------------YEDLREHVKQYDPEKVSLITGVSTEDIYQLARMYGESS----------------PSFIR 299
Cdd:cd02760 312 avsvdaddetaihqgvegttaFTMLVEHMRKYTPEWAESICDVPAATIRRIAREFLENAsigstievdgvtlpyrPVAVT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 300 IGNGIQHHDNGGMIVRTIACLPAITGQwLHKGGGAIKHN------------------SGILEYNTNALQR---PDLLKGR 358
Cdd:cd02760 392 LGKSVNNGWGAFECCWARTLLATLVGA-LEVPGGTLGTTvrlnrphddrlasvkpgeDGFMAQGFNPTDKehwVVKPTGR 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 359 T--------------PRSFNMNQLGKVLLET-------DPPIRS--LFIYGTNPAVVAPEANKVRQGLLREDlFTVVHDL 415
Cdd:cd02760 471 NahrtlvpivgnsawSQALGPTQLAWMFLREvpldwkfELPTLPdvWFNYRTNPAISFWDTATLVDNIAKFP-FTVSFAY 549
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2234329652 416 FLTETAAYADIVLPATSAFENTD--------FYTSYWHHY-IQLQQPVIERYGESKSNTEVFRLLAEAMGFTDQ 480
Cdd:cd02760 550 TEDETNWMADVLLPEATDLESLQmikvggtkFVEQFWEHRgVVLRQPAVEPQGEARDFTWISTELAKRTGLLAD 623
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
13-292 |
1.96e-24 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 108.83 E-value: 1.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 13 KSVCSLdCPDQCGLLIHKKDGKIVKVQGDPDHPVTAGNICNKVRNMTERIYDEKRLTTPLKRTgAKGQ----AIFEPISW 88
Cdd:PRK13532 44 KAPCRF-CGTGCGVLVGTKDGRVVATQGDPDAPVNRGLNCIKGYFLSKIMYGKDRLTQPLLRM-KDGKydkeGEFTPVSW 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 89 DEAIDTITSRWKQLIDEEGAESIlpysfygnmgkltaeGMdrrffyrMGSSQLerTIcskagSEGYKYTMGISAG----- 163
Cdd:PRK13532 122 DQAFDVMAEKFKKALKEKGPTAV---------------GM-------FGSGQW--TI-----WEGYAASKLMKAGfrsnn 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 164 IDP-------------------EETI-------HTKLFIFWGINAVStnMHQITIAQ----KVRKQGAKIVVIDVHKNQT 213
Cdd:PRK13532 173 IDPnarhcmasavvgfmrtfgiDEPMgcyddieAADAFVLWGSNMAE--MHPILWSRvtdrRLSNPDVKVAVLSTFEHRS 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 214 GRLADWFIPIKPGTDSALALGIMHILFKENLHDEAFLSEYTV--------GY--------------------------ED 259
Cdd:PRK13532 251 FELADNGIIFTPQTDLAILNYIANYIIQNNAVNWDFVNKHTNfrkgatdiGYglrpthplekaaknpgtagksepisfEE 330
|
330 340 350
....*....|....*....|....*....|...
gi 2234329652 260 LREHVKQYDPEKVSLITGVSTEDIYQLARMYGE 292
Cdd:PRK13532 331 FKKFVAPYTLEKTAKMSGVPKEQLEQLAKLYAD 363
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
573-671 |
2.33e-22 |
|
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: 92.00 E-value: 2.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 573 HNFLNSTFSNNEKHIR-LEKTPKLFINTKDADEHGIVDGDPVRIWNSRGECELTAAVGEQVLPGVVVSQGLWADEPGKKQ 651
Cdd:cd02775 2 RDHFHSGTRTRNPWLReLAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGHRGGRGG 81
|
90 100
....*....|....*....|
gi 2234329652 652 LVNALTPDRLSDMGGGATFF 671
Cdd:cd02775 82 NANVLTPDALDPPSGGPAYK 101
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
576-679 |
1.25e-19 |
|
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: 85.33 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 576 LNSTFSNNEKHIRLEKTPK---LFINTKDADEHGIVDGDPVRIWNSRGECELTAAVGEQVLPGVV-VSQGLWADEPGKKQ 651
Cdd:cd02777 14 LHSQLDNVPWLREAYKVKGrepVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPGVVaLPEGAWYDPDDNGG 93
|
90 100 110
....*....|....*....|....*....|....
gi 2234329652 652 L-----VNALTPDRL-SDMGGGATFFSGRVQIEK 679
Cdd:cd02777 94 LdkggnPNVLTSDIPtSKLAQGNPANTCLVEIEK 127
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
24-491 |
3.29e-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: 3.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 24 CGLLIHKKDGKIVKVQGDPDHPVTAGNICNKVRNMTERIYDEKRLTTPLKRTGAKGQAIfepISWDEAIDTITSrwkQLI 103
Cdd:cd02764 56 QGVLVKTVDGRPIKIEGNPDHPASLGGTSARAQASVLSLYDPDRAQGPLRRGIDGAYVA---SDWADFDAKVAE---QLK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 104 DEEGAESILPYSfyGNMGKLTAEGM----------DRRFFYRMGSSQLERticskagsEGYKYTMG--ISAGIDPEE--- 168
Cdd:cd02764 130 AVKDGGKLAVLS--GNVNSPTTEALigdflkkypgAKHVVYDPLSAEDVN--------EAWQASFGkdVVPGYDFDKaev 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 169 --TIHTKLFIFWGinAVSTNMHQITIAQKVRKQG--AKIVVIDVHKNQTGRLADWFIPIKPGTDSALALGIMHILFKenl 244
Cdd:cd02764 200 ivSIDADFLGSWI--SAIRHRHDFAAKRRLGAEEpmSRLVAAESVYTLTGANADVRLAIRPSQEKAFALGLAHKLIK--- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 245 hdeafLSEYTVGYEDLREHVKQYDPEKVSLITGVSTEDIYQLARMYGESSPSFIRIGNgiqhHDNGGMIVRTIACLPAIT 324
Cdd:cd02764 275 -----KGAGSSLPDFFRALNLAFKPAKVAELTVDLDKALAALAKALAAAGKSLVVAGS----ELSQTAGADTQVAVNALN 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 325 GQwLHKGGGAIKHNSGIleyntnaLQRPDLLKGRTPRSFN-MNQlGKVlletdppiRSLFIYGTNPAVVAPEANKVRQGL 403
Cdd:cd02764 346 SL-LGNDGKTVDHARPI-------KGGELGNQQDLKALASrINA-GKV--------SALLVYDVNPVYDLPQGLGFAKAL 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 404 LREDlFTVVHDLFLTETAAYADIVLPATSAFENTDFYTSYWHHYiQLQQPVIERYGESKSNTEVfrllaeAMGFTDQELk 483
Cdd:cd02764 409 EKVP-LSVSFGDRLDETAMLCDWVAPMSHGLESWGDAETPDGTY-SICQPVIAPLFDTRSAQES------LLLALGGSL- 479
|
....*...
gi 2234329652 484 dSDEELIR 491
Cdd:cd02764 480 -GGYEKLR 486
|
|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
13-64 |
3.61e-18 |
|
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for which the structure is known. This first domain (residues 1 to 60) of PDB:1aa6 is an Fe4S4 cluster just below the protein surface.
Pssm-ID: 428168 [Multi-domain] Cd Length: 55 Bit Score: 78.49 E-value: 3.61e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2234329652 13 KSVCSlDCPDQCGLLIHKKDGKIVKVQGDPDHPVTAGNICNKVRNMTERIYD 64
Cdd:pfam04879 5 KTICP-YCGVGCGLEVHVKDGKIVKVEGDPDHPVNEGRLCVKGRFGYERVYN 55
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
13-475 |
1.26e-17 |
|
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone oxidoreductase (NADH-Q-OR)/respiratory complex I/NADH dehydrogenase-1 (NDH-1). The NADH-Q-OR is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The atomic structure of complex I is not known and the mechanisms of electron transfer and proton pumping are not established. The nad11 gene codes for the largest (75-kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Escherichia coli, this subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The nad11 gene is nuclear-encoded in animals, plants, and fungi, but is still encoded in the mitochondrial genome of some protists. The Nad11/NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain family belongs to the molybdopterin_binding (MopB) superfamily of proteins. Bacterial type II NADH-quinone oxidoreductases and NQR-type sodium-motive NADH-quinone oxidoreductases are not homologs of this domain family.
Pssm-ID: 239169 [Multi-domain] Cd Length: 386 Bit Score: 85.41 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 13 KSVCSLDCPDqCGLLIHKKDGKIVKVQGDPDHPVTAGNICNKVRNMTERIYDEKRLTTPLKRTGAKgqaiFEPISWDEAI 92
Cdd:cd02768 1 ESIDVHDALG-SNIRVDVRGGEVMRILPRENEAINEEWISDKGRFGYDGLNSRQRLTQPLIKKGGK----LVPVSWEEAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 93 DTItsrwKQLIDEEGAESIlpySFYGNmGKLTAEGMD--RRFFYRMGSSQLE------RTICSKAGSEGYKYTMGIsAGI 164
Cdd:cd02768 76 KTV----AEGLKAVKGDKI---GGIAG-PRADLESLFllKKLLNKLGSNNIDhrlrqsDLPADNRLRGNYLFNTSI-AEI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 165 DpeetiHTKLFIFWGinavsTNMHQ------ITIAQKVRKQGAKIVVIDVHKnqTGRLADWFIPIKPGTDSALALgimhi 238
Cdd:cd02768 147 E-----EADAVLLIG-----SNLRKeapllnARLRKAVKKKGAKIAVIGPKD--TDLIADLTYPVSPLGASLATL----- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 239 lfkenlhdeaflseytvgyedlrehvkqydpekVSLITGVSTEDIyqlARMYGESSPSFIRIGNGIQHHDNGGMI--VRT 316
Cdd:cd02768 210 ---------------------------------LDIAEGKHLKPF---AKSLKKAKKPLIILGSSALRKDGAAILkaLAN 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 317 IACLPAITGQWLhkGGGAIKHNSG--ILEYNTNAlqrpdllkgrtprsfnmnqlgKVLLETDPPIRSLFIYGTNPAVVAP 394
Cdd:cd02768 254 LAAKLGTGAGLW--NGLNVLNSVGarLGGAGLDA---------------------GLALLEPGKAKLLLLGEDELDRSNP 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 395 EAnkvRQGLLREDLFtVVHDLFLTETAAYADIVLPATSAFENTDFYTSyWHHYIQLQQPVIERYGESKSNTEVFRLLAEA 474
Cdd:cd02768 311 PA---AVALAAADAF-VVYQGHHGDTGAQADVILPAAAFTEKSGTYVN-TEGRVQRFKKAVSPPGDAREDWKILRALSNL 385
|
.
gi 2234329652 475 M 475
Cdd:cd02768 386 L 386
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
67-333 |
2.07e-17 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 86.64 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 67 RLTTPLKRTGAKGQaiFEPISWDEAIDTITSRWKQLIDEEGAEsilpysFYGNmGKLTAEGMdrrFFYRM-----GSSQL 141
Cdd:PRK09939 108 RLTQPLKYDAVSDC--YKPLSWQQAFDEIGARLQSYSDPNQVE------FYTS-GRTSNEAA---FLYQLfareyGSNNF 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 142 E--RTICSKAGSEGYKYTMGISAG-IDPEETIHTKLFIFWGINAVSTNMHQITIAQKVRKQGAKIVVI------------ 206
Cdd:PRK09939 176 PdcSNMCHEPTSVGLAASIGVGKGtVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAInplqerglerft 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 207 ------DVHKNQTGRLADWFIPIKPGTDSALALGIMHILFKEN----------LHDEAFLSEYTVGYEDLREHVKQYDPE 270
Cdd:PRK09939 256 apqnpfEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDdaasaagrpsLLDDEFIQTHTVGFDELRRDVLNSEWK 335
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2234329652 271 KVSLITGVSTEDIYQLARMYGESSPSFIRIGNGIQHHDNGGMIVRTIACLPAITGQWLHKGGG 333
Cdd:PRK09939 336 DIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAG 398
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
577-679 |
2.28e-17 |
|
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: 78.49 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 577 NSTFSNNEkHIRLEKTPKLFINTKDADEHGIVDGDPVRIWNSRGECELTAAVGEQVLPGVV-VSQGLWA--DEPG--KKQ 651
Cdd:cd02794 15 HSTFDNVP-WLREAFPQEVWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVVaLPQGAWYepDANGidKGG 93
|
90 100
....*....|....*....|....*...
gi 2234329652 652 LVNALTPDRLSDMGGGATFFSGRVQIEK 679
Cdd:cd02794 94 CINTLTGLRPSPLAKGNPQHTNLVQVEK 121
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
13-64 |
2.51e-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: 76.13 E-value: 2.51e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2234329652 13 KSVCSLdCPDQCGLLIHKKDGKIVKVQGDPDHPVTAGNICNKVRNMTERIYD 64
Cdd:smart00926 5 PTVCPL-CGVGCGLLVEVKDGRVVRVRGDPDHPVNRGRLCPKGRAGLEQVYS 55
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
593-670 |
1.45e-16 |
|
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: 75.77 E-value: 1.45e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2234329652 593 PKLFINTKDADEHGIVDGDPVRIWNSRGECELTAAVGEQVLPGVV-VSQGLWADEPGKKqlVNALTPDRLSDMGGGATF 670
Cdd:pfam01568 30 EVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVfMPFGWWYEPRGGN--ANALTDDATDPLSGGPEF 106
|
|
| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
595-679 |
7.51e-15 |
|
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: 71.51 E-value: 7.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 595 LFINTKDADEHGIVDGDPVRIWNSRGECELTAAVGEQVLPGVV-VSQGLW---ADEPGKKQL-----VNALTPDR-LSDM 664
Cdd:cd02793 35 IRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPGVVqLPTGAWydpDDPGEPGPLckhgnPNVLTLDIgTSSL 114
|
90
....*....|....*
gi 2234329652 665 GGGATFFSGRVQIEK 679
Cdd:cd02793 115 AQGCSAQTCLVQIEK 129
|
|
| 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 ... |
13-476 |
5.51e-14 |
|
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: 74.73 E-value: 5.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 13 KSVCSlDCPDQCGLLIHKKDGKIVKVQGDPDHPVTAGNICNKVRNMTERIYDEKRLTTPLKRtgakGQAIFEPISWDEAI 92
Cdd:cd02771 1 PSICH-HCSVGCNISLGERYGELRRVENRYNGAVNHYFLCDRGRFGYGYVNSRDRLTQPLIR----RGGTLVPVSWNEAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 93 DTITSRWKQLIDEEGA--------ESILPYS-FYGN---MGKLTAEGmDRRFFYRMGSSQLErtICSKAGSEGYKYTMGI 160
Cdd:cd02771 76 DVAAARLKEAKDKVGGigsprasnESNYALQkLVGAvlgTNNVDHRA-RRLIAEILRNGPIY--IPSLRDIESADAVLVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 161 saGIDPEETiHTKlfIFWGIN-AVSTNMHQITIAQKV------------RKQGAKIVVIDVHKNQTGRLADWFIPIKPGT 227
Cdd:cd02771 153 --GEDLTQT-APR--IALALRqAARRKAVELAALSGIpkwqdaavrniaQGAKSPLFIVNALATRLDDIAAESIRASPGG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 228 DSALALGIMHILfkenlhdeaflseytvgyedlrehvkqyDPEKVSLITGVSTEDIYQLARMYGESSPSFIRIGNGIQHH 307
Cdd:cd02771 228 QARLGAALARAV----------------------------DASAAGVSGLAPKEKAARIAARLTGAKKPLIVSGTLSGSL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 308 DnggmIVRTIACLPAITGQWLHKGGgaikhnSGILEYNTNALQRpdLLKGRTPRSFNMNQLGKVLLETDPPIRSLFIYGT 387
Cdd:cd02771 280 E----LIKAAANLAKALKRRGENAG------LTLAVEEGNSPGL--LLLGGHVTEPGLDLDGALAALEDGSADALIVLGN 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 388 NPAVVAPEAnKVRQGLLREDlFTVVHDLFLTETAAYADIVLPATSAFENTDFYTSYWHHYIQLQQPVIERYGESKSNTEV 467
Cdd:cd02771 348 DLYRSAPER-RVEAALDAAE-FVVVLDHFLTETAERADVVLPAASFAEKSGTFVNYEGRAQRFFKAYDDPAGDARSDWRW 425
|
....*....
gi 2234329652 468 FRLLAEAMG 476
Cdd:cd02771 426 LHALAAKLG 434
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
30-475 |
9.52e-14 |
|
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin. Arsenite oxidase is a heterodimeric enzyme containing a large and a small subunit. The large catalytic subunit harbors the molybdopterin cofactor and the [3Fe-4S] cluster; and the small subunit belongs to the structural class of the Rieske proteins. The small subunit is not included in this alignment. Members of MopB_Arsenite-Ox CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239157 [Multi-domain] Cd Length: 676 Bit Score: 74.83 E-value: 9.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 30 KKDGKIVKVQGDPDH--PVTAGNICNKVRNMTERIYD------EKRLTTPLKRTGakGQaiFEPISWDEAIDTITSRWKQ 101
Cdd:cd02756 72 TQDGREVYIVIVPDKecPVNSGNYSTRGGTNAERIWSpdnrvgETRLTTPLVRRG--GQ--LQPTTWDDAIDLVARVIKG 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 102 LIDEEGAESILPYS----------FYGNM--GKLTAEGMDR---RFFYRMG-SSQLERTICSKAGSEGYKYtmgisagid 165
Cdd:cd02756 148 ILDKDGNDDAVFASrfdhggggggFENNWgvGKFFFMALQTpfvRIHNRPAyNSEVHATREMGVGELNNSY--------- 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 166 pEETIHTKLFIFWGINAVST-----------NMHQITIAQKVRK-------QGAKIVVIDVHKNQTGRLAD--------W 219
Cdd:cd02756 219 -EDARLADTIVLWGNNPYETqtvyflnhwlpNLRGATVSEKQQWfppgepvPPGRIIVVDPRRTETVHAAEaaagkdrvL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 220 FIPIKPGTDSALALGImhilfkenlhdeaflseYTVGYEDLREHVKQydpekVSLITGVSTEDIYQLARMYGESSPSFIR 299
Cdd:cd02756 298 HLQVNPGTDTALANAI-----------------ARYIYESLDEVLAE-----AEQITGVPRAQIEKAADWIAKPKEGGYR 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 300 ----------IGNGIQHHDNGGMIVRtiacLPAITGQWLHKGGGAIK---HNSGileyntnALQRPDLLKGRTPRSFNMN 366
Cdd:cd02756 356 krvmfeyekgIIWGNDNYRPIYSLVN----LAIITGNIGRPGTGCVRqggHQEG-------YVRPPPPPPPWYPQYQYAP 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 367 QLGKVLLETDPPIrsLFIYGTNPAVVAPEANKVRQGLL-RED--------------------------------LFTVVH 413
Cdd:cd02756 425 YIDQLLISGKGKV--LWVIGCDPYKTTPNAQRLRETINhRSKlvtdaveaalyagtydreamvcligdaiqpggLFIVVQ 502
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2234329652 414 DLFLTETAAYADIVLPATSAFENTDFYTSYWHHYIQLQQPVIERYGESKSNTEVFRLLAEAM 475
Cdd:cd02756 503 DIYPTKLAEDAHVILPAAANGEMNETSMNGHERRLRLYEKFMDPPGEAMPDWWIAAMIANRI 564
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
588-679 |
9.30e-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: 65.79 E-value: 9.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 588 RLEKTPKLFINTKDADEHGIVDGDPVRIWNSRGECELTAAVGEQVLPGVVVSQGLWA---DEPGKKQL-------VNALT 657
Cdd:cd02781 28 ELHPDPVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVRAEHGWWypeREAGEPALggvwesnANALT 107
|
90 100
....*....|....*....|...
gi 2234329652 658 PDRLSD-MGGGATFFSGRVQIEK 679
Cdd:cd02781 108 SDDWNDpVSGSSPLRSMLCKIYK 130
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
588-680 |
1.66e-12 |
|
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: 64.52 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 588 RLEKTPKLFINTKDADEHGIVDGDPVRIWNSRGECELTAAVGEQVLPGVVVSQGLWADEPGKKQLVNALTPDRLSDMGGG 667
Cdd:cd02791 30 AHVPEPYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPGEVFVPMHWGDQFGRSGRVNALTLDATDPVSGQ 109
|
90
....*....|...
gi 2234329652 668 ATFFSGRVQIEKA 680
Cdd:cd02791 110 PEFKHCAVRIEKV 122
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
588-679 |
7.03e-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: 57.13 E-value: 7.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 588 RLEKTPKLFINTKDADEHGIVDGDPVRIWNSRGECELTAAVGEQVLPGVVvsqGL---WADEpGKKQLVNALTPDRLSDM 664
Cdd:cd00508 30 ALAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRPGTV---FMpfhWGGE-VSGGAANALTNDALDPV 105
|
90
....*....|....*
gi 2234329652 665 GGGATFFSGRVQIEK 679
Cdd:cd00508 106 SGQPEFKACAVRIEK 120
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
378-494 |
2.98e-09 |
|
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: 59.85 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 378 PIRSLFIYGTNPAVVAPEANKvrqGLLREDLFTVVHDLFLTETAAYADIVLPATSAFENTDFYTSyWHHYIQLQQPVIER 457
Cdd:COG1034 332 KLKALVLLGADPYDLDPAAAL---AALAKADFVVVLDHFGSATAERADVVLPAAAFAEKSGTFVN-LEGRVQRFNAAVPP 407
|
90 100 110
....*....|....*....|....*....|....*..
gi 2234329652 458 YGESKSNTEVFRLLAEAMGftdQELKDSDEELIRQAL 494
Cdd:COG1034 408 PGEARPDWRVLRALANALG---AGLPYDSLEEVRAEL 441
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
14-251 |
8.73e-09 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 58.85 E-value: 8.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 14 SVCsLDCPDQCGLL--IHKKDGKIVKVQGDPDHPV-----------------------------TAgniCNKVRNMTERI 62
Cdd:PRK14991 77 TQC-LGCWTQCGVRvrVDNATNKILRIAGNPYHPLstdhhidmstpvkeafeslsgesglegrsTA---CARGNAMLEQL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 63 YDEKRLTTPLKRTGAKGQAIFEPISWDEAIDTITS-----------------RWKQLIDEEGAE-----SILPYSFYGNm 120
Cdd:PRK14991 153 DSPYRVLQPLKRVGKRGSGKWQRISFEQLVEEVVEggdlfgeghvdglrairDLDTPIDAKNPEygpkaNQLLVTNASD- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 121 gkltaEGMD---RRF-FYRMGSSQLerticSKAGSE-GYKYTMGISAGI-DPEETIHTK---------LFIfwGIN-AVS 184
Cdd:PRK14991 232 -----EGRDafiKRFaFNSFGTRNF-----GNHGSYcGLAYRAGSGALMgDLDKNPHVKpdwdnvefaLFI--GTSpAQS 299
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2234329652 185 TNMHQITIAQ--KVRKQGA-KIVVID-VHKNQTGRLAD----WfIPIKPGTDSALALGIMHILFKENLHDEAFLS 251
Cdd:PRK14991 300 GNPFKRQARQlaNARTRGNfEYVVVApALPLSSSLAAGdnnrW-LPIRPGTDSALAMGMIRWIIDNQRYNADYLA 373
|
|
| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
564-637 |
1.01e-08 |
|
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: 54.31 E-value: 1.01e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2234329652 564 PFMYV-PAPNHNFlNSTFSNNEKHIRLEK-TPKLFINTKDADEHGIVDGDPVRIWNSRGECELTAAVGEQVLPGVV 637
Cdd:cd02776 1 PLNYLtPHGKWSI-HSTYRDNLLMLRLQRgGPVVWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTV 75
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
595-680 |
4.31e-07 |
|
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239183 [Multi-domain] Cd Length: 129 Bit Score: 49.31 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 595 LFINTKDADEHGIVDGDPVRIWNSRGECELTAAVGEQVLPGVV-VSQGLWADEPGKKQL-------VNALTPDRLSDMGG 666
Cdd:cd02782 35 LRIHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMPGVVsLPHGWGHDYPGVSGAgsrpgvnVNDLTDDTQRDPLS 114
|
90
....*....|....*
gi 2234329652 667 GATFFSG-RVQIEKA 680
Cdd:cd02782 115 GNAAHNGvPVRLARV 129
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
576-679 |
1.33e-06 |
|
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: 48.44 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 576 LNSTFSNNEKHIR--LEKTPkLFINTKDADEHGIVDGDPVRIWNSRGECELTAAVGEQVLPGVVV---SQGLWA------ 644
Cdd:cd02780 12 LNSHRSANAPWLKeiKPENP-VWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRPGVVAiehGYGHWAygavas 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2234329652 645 -----DEPGKKQ--------LVNALTPDR----LSDMGGGATFFSG-RVQIEK 679
Cdd:cd02780 91 tidgkDLPGDAWrgagvninDIGLVDPSRggwsLVDWVGGAAARYDtPVKIEK 143
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
588-637 |
2.51e-05 |
|
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. This CD (MopB_CT_Formate-Dh_H) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239191 [Multi-domain] Cd Length: 116 Bit Score: 43.77 E-value: 2.51e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2234329652 588 RLEKTPKLFINTKDADEHGIVDGDPVRIWNSRGECELTAAVGEQVLPGVV 637
Cdd:cd02790 30 AIAPEEYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGVV 79
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
590-659 |
2.52e-04 |
|
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: 41.06 E-value: 2.52e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2234329652 590 EKTPKLF--INTKDADEHGIVDGDPVRIWNSRGECELTAAVGEQVLPGVVvsqGL---WADE-PGKKQLVNALTPD 659
Cdd:cd02792 30 ELQPEMFveISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHEV---GIpyhWGGMgLVIGDSANTLTPY 102
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
565-679 |
4.83e-03 |
|
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: 37.64 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234329652 565 FMYVPAPNHNFLNSTFSNNEKHIRLEKTpkLFINTKDADEHGIVDGDPVRIWNSRGECELTAAVGEQVLPGVV--VSQ-G 641
Cdd:cd02778 4 LIYGKSPVHTHGHTANNPLLHELTPENT--LWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVfmPHGfG 81
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2234329652 642 LWADE----PGKKQLVNALTPDRLSDMGGGATFFSGRVQIEK 679
Cdd:cd02778 82 HWAPAlsraYGGGVNDNNLLPGSTEPVSGGAGLQEFTVTVRK 123
|
|
| |
