|
Name |
Accession |
Description |
Interval |
E-value |
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
40-606 |
0e+00 |
|
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: 670.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 40 VYQICEGCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRLCPRGQGAPQTTYDPDRLKRPLIRVEgsQRGEGKYRVATWEE 119
Cdd:cd02755 1 VPSICEMCSSRCGILARVEDGRVVKIDGNPLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRVG--ERGEGKFREASWDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 120 ALDHIAKKMLEIREKYGPEAIAFFGHGTGDYWFVDFLPAAWGSPNAAKPSvSLCTAPREVASQWVFgRPIGGHEPIDWEN 199
Cdd:cd02755 79 ALQYIASKLKEIKEQHGPESVLFGGHGGCYSPFFKHFAAAFGSPNIFSHE-STCLASKNLAWKLVI-DSFGGEVNPDFEN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 200 ARYIVLIGHHIGEDTHNTQLQDFALALKNGAKVVVVDPRFSTAAAKAHRWLPIKPGTDTALLLAWIHVLIYEDLYDKEYV 279
Cdd:cd02755 157 ARYIILFGRNLAEAIIVVDARRLMKALENGAKVVVVDPRFSELASKADEWIPIKPGTDLAFVLALIHVLISENLYDAAFV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 280 AKYTVGFEELKAHVKDFTPEWAEKHTEIPAQVIREVAREMAAHKPRAVLPPTRHNVWYGDDTYRVMALLYVNVLLGNYGR 359
Cdd:cd02755 237 EKYTNGFELLKAHVKPYTPEWAAQITDIPADTIRRIAREFAAAAPHAVVDPGWRGTFYSNSFQTRRAIAIINALLGNIDK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 360 PGGFYIAQSPYlekyplpplplepaaggcsgpsggdhepegfkpradkgkffarstaiqeliepmitgePYPIKGLFAYG 439
Cdd:cd02755 317 RGGLYYAGSAK----------------------------------------------------------PYPIKALFIYR 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 440 INLFHSIPNVPRTKEALKNLDLYVAIDVLPQEHVMWADVILPEATYLERYDDFVLVAHKTPFIQLRTPAHEPLFDTKPGW 519
Cdd:cd02755 339 TNPFHSMPDRARLIKALKNLDLVVAIDILPSDTALYADVILPEATYLERDEPFSDKGGPAPAVATRQRAIEPLYDTRPGW 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 520 WIARELGLRLGLeqyfpwktieeyletrlqslgldletmkgmgtlvqrgkpwledwekegrlpFGTASGKIELYCQRFKE 599
Cdd:cd02755 419 DILKELARRLGL---------------------------------------------------FGTPSGKIELYSPILAK 447
|
....*..
gi 1886399248 600 AGHQPLP 606
Cdd:cd02755 448 AGYDPLP 454
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
17-745 |
0e+00 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 631.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 17 MALRGSGPAKALKAPWYAQEVKSVYQICEGCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRLCPRGQGAPQTTYDPDRLK 96
Cdd:COG0243 1 MSLRDFKAAGAGAAALEAAGTKTVKTTCPGCGVGCGLGVKVEDGRVVRVRGDPDHPVNRGRLCAKGAALDERLYSPDRLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 97 RPLIRVegSQRGEGKYRVATWEEALDHIAKKMLEIREKYGPEAIAFFGHG-------TGDYWFVDFLPAAWGSPNAAKPS 169
Cdd:COG0243 81 YPMKRV--GPRGSGKFERISWDEALDLIAEKLKAIIDEYGPEAVAFYTSGgsagrlsNEAAYLAQRFARALGTNNLDDNS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 170 vSLCTAPREVASQWVFGRPIGGHEPIDWENARYIVLIGHHIGEdTHNTQLQDF-ALALKNGAKVVVVDPRFSTAAAKAHR 248
Cdd:COG0243 159 -RLCHESAVAGLPRTFGSDKGTVSYEDLEHADLIVLWGSNPAE-NHPRLLRRLrEAAKKRGAKIVVIDPRRTETAAIADE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 249 WLPIKPGTDTALLLAWIHVLIYEDLYDKEYVAKYTVGFEELKAHVKDFTPEWAEKHTEIPAQVIREVAREMAAHKPRAVL 328
Cdd:COG0243 237 WLPIRPGTDAALLLALAHVLIEEGLYDRDFLARHTVGFDELAAYVAAYTPEWAAEITGVPAEDIRELAREFATAKPAVIL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 329 P---PTRHNvwYGDDTYRVMALLyvNVLLGNYGRPGGFYiaqspylekyplpplplepaaggcsGPSGGDHepegfkpra 405
Cdd:COG0243 317 WgmgLQQHS--NGTQTVRAIANL--ALLTGNIGKPGGGP-------------------------FSLTGEA--------- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 406 dkgkffarstaiqeliepMITGEPYPIKGLFAYGINLFHSIPNVPRTKEALKNLDLYVAIDVLPQEHVMWADVILPEATY 485
Cdd:COG0243 359 ------------------ILDGKPYPIKALWVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARYADIVLPATTW 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 486 LERYDDFVLVAHktPFIQLRTPAHEPLFDTKPGWWIARELGLRLGLEQYFPW-KTIEEYLETRLQS---LGLDLETMKGM 561
Cdd:COG0243 421 LERDDIVTNSED--RRVHLSRPAVEPPGEARSDWEIFAELAKRLGFEEAFPWgRTEEDYLRELLEAtrgRGITFEELREK 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 562 GtLVQRGKPWLEDWEKEGrlPFGTASGKIELYCQRFKeagHQPLPVFTPPEEP-----PEGFYRLLYGRSPVHTFARTQN 636
Cdd:COG0243 499 G-PVQLPVPPEPAFRNDG--PFPTPSGKAEFYSETLA---LPPLPRYAPPYEGaepldAEYPLRLITGRSRDQWHSTTYN 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 637 NWVLMEMDPENEVWIHKEEAKRLGLKEGDYVMLVNQDGVKEGPVRVkpTARIRKDCVYIVHGFGHKAplmrlAHGRGASD 716
Cdd:COG0243 573 NPRLREIGPRPVVEINPEDAAALGIKDGDLVRVESDRGEVLARAKV--TEGIRPGVVFAPHGWWYEP-----ADDKGGNV 645
|
730 740
....*....|....*....|....*....
gi 1886399248 717 NYLqTRYKLDPISGGAGLRVNFVRLEKAE 745
Cdd:COG0243 646 NVL-TPDATDPLSGTPAFKSVPVRVEKAA 673
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
1-744 |
0e+00 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 539.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 1 MQRREFLKLSALGVGAMALRGSGPAK--ALKAPWYAQEVKSVYQICEGCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRL 78
Cdd:PRK15488 3 LSRRDFLKGAGAGCAACALGSLLPGAlaANEIAQLKGKTKLTPSICEMCSTRCPIEARVVNGKNVFIQGNPKAKSFGTKV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 79 CPRGQGAPQTTYDPDRLKRPLIRVegSQRGEGKYRVATWEEALDHIAKKMLEIREKYGPEAIAFFGH-GTGDYWFVDFlP 157
Cdd:PRK15488 83 CARGGSGHSLLYDPQRIVKPLKRV--GERGEGKWQEISWDEAYQEIAAKLNAIKQQHGPESVAFSSKsGSLSSHLFHL-A 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 158 AAWGSPNAAKpSVSLCTAPREVASQWVFGRPIGghepIDWENARYIVLIGHHIGE-----DTHntQLQDFALalKNGAKV 232
Cdd:PRK15488 160 TAFGSPNTFT-HASTCPAGYAIAAKVMFGGKLK----RDLANSKYIINFGHNLYEginmsDTR--GLMTAQM--EKGAKL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 233 VVVDPRFSTAAAKAHRWLPIKPGTDTALLLAWIHVLIYEDLYDKEYVAKYTVGFEELKAHVKDFTPEWAEKHTEIPAQVI 312
Cdd:PRK15488 231 VVFEPRFSVVASKADEWHAIRPGTDLAVVLALCHVLIEENLYDKAFVERYTSGFEELAASVKEYTPEWAEAISDVPADDI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 313 REVAREMAAHKPRAVLPPTrHNVWYGDDTY-RVMALLYVNVLLGNYGRPGGFYIAQSPylEKYPLPplplepaAGGCSGP 391
Cdd:PRK15488 311 RRIARELAAAAPHAIVDFG-HRATFTPEEFdMRRAIFAANVLLGNIERKGGLYFGKNA--SVYNKL-------AGEKVAP 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 392 SGGDHEPEGFK----PRAD----KGKFFARSTAI-QELIEPMITGEPYPIKGLFAYGINLFHSIPNVPRTKEALKNLDLY 462
Cdd:PRK15488 381 TLAKPGVKGMPkptaKRIDlvgeQFKYIAAGGGVvQSIIDATLTQKPYQIKGWVMSRHNPMQTVTDRADVVKALKKLDLV 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 463 VAIDVLPQEHVMWADVILPEATYLERYDDFVLVAHKTPFIQLRTPAHEPLFDTKPGWWIARELGLRLGLEQYFPWKTIEE 542
Cdd:PRK15488 461 VVCDVYLSESAAYADVVLPESTYLERDEEISDKSGKNPAYALRQRVVEPIGDTKPSWQIFKELGEKMGLGQYYPWQDMET 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 543 YletRLQSLGLD---LETMKGMGtLVQRGKPWL---------------------EDWEKEGRLPFGTASGKIELYCQRFK 598
Cdd:PRK15488 541 L---QLYQVNGDhalLKELKKKG-YVSFGVPLLlrepkmvakfvarypnakavdEDGTYGSQLKFKTPSGKIELFSAKLE 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 599 EA-------GHQPLPVFTPPEeppegfYRLLYGRSPVHTFARTQNNWVLMEMDPENEVWIHKEEAKRLGLKEGDYVMLVN 671
Cdd:PRK15488 617 ALapgygvpRYRDVALKKEDE------LYFIQGKVAVHTNGATQNVPLLANLMSDNAVWIHPQTAGKLGIKNGDEIRLEN 690
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1886399248 672 QDGVKEGPVRVkpTARIRKDCVYIVHGFGHKAPLMRLAHGRGASDNYLqtrykLDPISG---GAGLRVNFVRLEKA 744
Cdd:PRK15488 691 SVGKEKGKALV--TPGIRPDTLFAYMGFGSKNKELTRATGKGIHCGNL-----LPHVTSpvsGTNVHTTGVTLSKA 759
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
44-611 |
4.24e-118 |
|
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: 364.32 E-value: 4.24e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 44 CEGCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRLCPRGQGAPQTTYDPDRLKRPLIRVegSQRGEGKYRVATWEEALDH 123
Cdd:cd02759 4 CPGCHSGCGVLVYVKDGKLVKVEGDPNHPTNKGRLCMRGLAAPEIVYHPDRLLYPLKRV--GERGENKWERISWDEALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 124 IAKKMLEIREKYGPEAIAF-FGHGTGDYWFVDFLPAAW----GSPNAAKpSVSLCTAPREVASQWVFGRPIGGHEPiDWE 198
Cdd:cd02759 82 IAEKLAEIKAEYGPESIATaVGTGRGTMWQDSLFWIRFvrlfGSPNLFL-SGESCYWPRDMAHALTTGFGLGYDEP-DWE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 199 NARYIVLIGHHIGEDTHNTQLQDFALALKNGAKVVVVDPRFSTAAAKAHRWLPIKPGTDTALLLAWIHVLIYEDLYDKEY 278
Cdd:cd02759 160 NPECIVLWGKNPLNSNLDLQGHWLVAAMKRGAKLIVVDPRLTWLAARADLWLPIRPGTDAALALGMLNVIINEGLYDKDF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 279 VAKYTVGFEELKAHVKDFTPEWAEKHTEIPAQVIREVAREMAAHKPRAVlpptrhnVWY--------GDDTYRVMALLYv 350
Cdd:cd02759 240 VENWCYGFEELAERVQEYTPEKVAEITGVPAEKIRKAARLYATAKPACI-------QWGlaidqqknGTQTSRAIAILR- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 351 nVLLGNYGRPGGfyiaqspylekyplpplplepaaggcsgpsggdhepegfkpradkgkffarstaiqeliepmITGEPY 430
Cdd:cd02759 312 -AITGNLDVPGG--------------------------------------------------------------NLLIPY 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 431 PIKGLFAYGINLFHSIPNVPRTKEALKNLDLYVAIDVLPQEHVMWADVILPEATYLERyDDFVLVAHKTPFIQLRTPAHE 510
Cdd:cd02759 329 PVKMLIVFGTNPLASYADTAPVLEALKALDFIVVVDLFMTPTAMLADIVLPVAMSLER-PGLRGGFEAENFVQLRQKAVE 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 511 PLFDTKPGWWIARELGLRLGLE--QYFPWKTieeyletrlqslgldletmkgmGTLVQRGKPwledwekegrlPFGTASG 588
Cdd:cd02759 408 PYGEAKSDYEIVLELGKRLGPEeaEYYKYEK----------------------GLLRPDGQP-----------GFNTPTG 454
|
570 580
....*....|....*....|...
gi 1886399248 589 KIELYCQRFKEAGHQPLPVFTPP 611
Cdd:cd02759 455 KVELYSTMLEELGYDPLPYYREP 477
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
51-746 |
1.79e-113 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 358.81 E-value: 1.79e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 51 CGIVAHAVGNRVYKVEGYEANPKSRGRLCPRGQGAPQTTYDPDRLKRPLIRvegsqrGEGKYRVATWEEALDHIAKKMLE 130
Cdd:COG3383 18 CGIDLEVKDGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVNSPDRLTTPLIR------RGGEFREVSWDEALDLVAERLRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 131 IREKYGPEAIAFFGHGTGD----YWFVDFLPAAWGSPNAAKPSvSLCTAPREVASQWVFGrpIGGHE-PI-DWENARYIV 204
Cdd:COG3383 92 IQAEHGPDAVAFYGSGQLTneenYLLQKLARGVLGTNNIDNNA-RLCMASAVAGLKQSFG--SDAPPnSYdDIEEADVIL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 205 LIGHHIGEdTH---NTQLQDfalALKNGAKVVVVDPRFSTAAAKAHRWLPIKPGTDTALLLAWIHVLIYEDLYDKEYVAK 281
Cdd:COG3383 169 VIGSNPAE-AHpvlARRIKK---AKKNGAKLIVVDPRRTETARLADLHLQIKPGTDLALLNGLLHVIIEEGLVDEDFIAE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 282 YTVGFEELKAHVKDFTPEWAEKHTEIPAQVIREVAREMAAHKPRAVL---PPTRHnvWYGDDTyrVMALLYVNVLLGNYG 358
Cdd:COG3383 245 RTEGFEELKASVAKYTPERVAEITGVPAEDIREAARLIAEAKRAMILwgmGVNQH--TQGTDN--VNAIINLALATGNIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 359 RPGGFYI-------AQspylekyplpplplepaaGGCSGPSGGDHEPeGFKPRADKG--KFFAR-----------STAIQ 418
Cdd:COG3383 321 RPGTGPFpltgqnnVQ------------------GGRDMGALPNVLP-GYRDVTDPEhrAKVADawgvpplpdkpGLTAV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 419 ELIEPMITGEpypIKGLFAYGINLFHSIPNVPRTKEALKNLDLYVAIDVLPQEHVMWADVILPEATYLE----------R 488
Cdd:COG3383 382 EMFDAIADGE---IKALWIIGENPAVSDPDANHVREALEKLEFLVVQDIFLTETAEYADVVLPAASWAEkdgtftnterR 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 489 yddfvlvahktpfIQLRTPAHEPLFDTKPGWWIARELGLRLGLEqyFPWKTIEE-YLETRLQSL---GLDLETMKGMGTL 564
Cdd:COG3383 459 -------------VQRVRKAVEPPGEARPDWEIIAELARRLGYG--FDYDSPEEvFDEIARLTPdysGISYERLEALGGV 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 565 V-------QRGKPWLEDWEkegrlpFGTASGKielycQRFKEAGHQPlpvftPPEEPPEGF-YRLLYGRSPV--HTFART 634
Cdd:COG3383 524 QwpcpsedHPGTPRLFTGR------FPTPDGK-----ARFVPVEYRP-----PAELPDEEYpLVLTTGRLLDqwHTGTRT 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 635 QNNWVLMEMDPENEVWIHKEEAKRLGLKEGDYVMLVNQDGvkEGPVRVKPTARIRKDCVYIvhgfghkaPlmrlAHGRGA 714
Cdd:COG3383 588 RRSPRLNKHAPEPFVEIHPEDAARLGIKDGDLVRVSSRRG--EVVLRARVTDRVRPGTVFM--------P----FHWGEG 653
|
730 740 750
....*....|....*....|....*....|..
gi 1886399248 715 SDNYLqTRYKLDPISGGAGLRVNFVRLEKAER 746
Cdd:COG3383 654 AANAL-TNDALDPVSKQPEYKACAVRVEKVAE 684
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
43-741 |
4.39e-105 |
|
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate dehydrogenase alpha chains found mainly archaea but also in alpha and gamma proteobacteria and a small number of gram positive bacteria. The alpha chain contains domains for molybdopterin dinucleotide binding and molybdopterin oxidoreductase (pfam01568 and pfam00384, respectively). The holo-enzyme also contains beta and gamma subunits. The enzyme catalyzes the oxidation of formate (produced from pyruvate during anaerobic growth) to carbon dioxide with the concomitant release of two electrons and two protons. The enzyme's purpose is to allow growth on formate in some circumstances and, in the case of FdhH in gamma proteobacteria, to pass electrons to hydrogenase (by which process acid is neutralized). This model is well-defined, with only a single fragmentary sequence falling between trusted and noise. The alpha subunit of a version of nitrate reductase is closely related.
Pssm-ID: 130652 [Multi-domain] Cd Length: 671 Bit Score: 336.75 E-value: 4.39e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 43 ICEGCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRLCPRGQGAPQTTYDPDRLKRPLIRVEGsqrgegKYRVATWEEALD 122
Cdd:TIGR01591 2 VCPYCGVGCSLNLVVKDGKIVRVEPYQGHKANRGHLCVKGYFAWEFINSKDRLTTPLIREGD------KFREVSWDEAIS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 123 HIAKKMLEIREKYGPEAIAFFGHGTG----DYWFVDFLPAAWGSpNAAKPSVSLCTAPREVASQWVFGRPIGGHEPIDWE 198
Cdd:TIGR01591 76 YIAEKLKEIKEKYGPDSIGFIGSSRGtneeNYLLQKLARAVIGT-NNVDNCARVCHGPSVAGLKQTVGIGAMSNTISEIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 199 NARYIVLIGHHIGEdTHNTQLQDFALALKNGAKVVVVDPRFSTAAAKAHRWLPIKPGTDTALLLAWIHVLIYEDLYDKEY 278
Cdd:TIGR01591 155 NADLIVIIGYNPAE-SHPVVAQYLKNAKRNGAKIIVIDPRKTETAKIADLHIPLKPGTDIALLNAMANVIIEEGLYDKAF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 279 VAKYTVGFEELKAHVKDFTPEWAEKHTEIPAQVIREVAREMAAHKPRAV---LPPTRHNvwYGDDTyrVMALLYVNVLLG 355
Cdd:TIGR01591 234 IEKRTEGFEEFREIVKGYTPEYVEDITGVPADLIREAARMYAKAGSAAIlwgMGVTQHS--QGVET--VMALINLAMLTG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 356 NYGRPGGfyiAQSPYlekyplppLPLEPAAGGCSGPSgGDHEPEGFKPRADKG--KFFA-----------RSTAIQELIE 422
Cdd:TIGR01591 310 NIGKPGG---GVNPL--------RGQNNVQGACDMGA-LPDFLPGYQPVSDEEvrEKFAkawgvvklpaePGLRIPEMID 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 423 PMITGEpypIKGLFAYGINLFHSIPNVPRTKEALKNLDLYVAIDVLPQEHVMWADVILPEATYLERYDDFVLVAHKtpfI 502
Cdd:TIGR01591 378 AAADGD---VKALYIMGEDPLQSDPNTSKVRKALEKLELLVVQDIFMTETAKYADVVLPAAAWLEKEGTFTNAERR---I 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 503 QLRTPAHEPLFDTKPGWWIARELGLRLGLEQYF--PWKTIEEYLETRLQSLGLDLETMKGMGTLvqRGKPWLEDWEKEGR 580
Cdd:TIGR01591 452 QRFFKAVEPKGESKPDWEIIQELANALGLDWNYnhPQEIMDEIRELTPLFAGLTYERLDELGSL--QWPCNDSDASPTSY 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 581 L---PFGTASGKIELYcqrfkeaghqPLPVFTPPEEP-PEGFYRLLYGR--SPVHTFARTQNNWVLMEMDPENEVWIHKE 654
Cdd:TIGR01591 530 LykdKFATPDGKAKFI----------PLEWVAPIEEPdDEYPLILTTGRvlTHYNVGEMTRRVAGLRRLSPEPYVEINTE 599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 655 EAKRLGLKEGDYVMLVNQDGvkEGPVRVKPTARIRKDCVYIvhgfghkaPLmrlaHGRGASDNYLQTRYkLDPISGGAGL 734
Cdd:TIGR01591 600 DAKKLGIKDGDLVKVKSRRG--EITLRAKVSDRVNKGAIYI--------TM----HFWDGAVNNLTTDD-LDPISGTPEY 664
|
....*..
gi 1886399248 735 RVNFVRL 741
Cdd:TIGR01591 665 KYTAVRI 671
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
43-529 |
5.33e-104 |
|
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: 323.90 E-value: 5.33e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 43 ICEGCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRLCPRGQGAPQTTYDPDRLKRPLIRVEGSqrgeGKYRVATWEEALD 122
Cdd:cd00368 3 VCPFCGVGCGILVYVKDGKVVRIEGDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGGR----GKFVPISWDEALD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 123 HIAKKMLEIREKYGPEAIAFFGHGTGD----YWFVDFLpAAWGSPNAAkPSVSLCTAPREVASQWvFGRPIGGHEPIDWE 198
Cdd:cd00368 79 EIAEKLKEIREKYGPDAIAFYGGGGASneeaYLLQKLL-RALGSNNVD-SHARLCHASAVAALKA-FGGGAPTNTLADIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 199 NARYIVLIGHHIGEdTHNTQLQDFALALKNGAKVVVVDPRFSTAAAKAHRWLPIKPGTDTALLLAwihvliyedlydkey 278
Cdd:cd00368 156 NADLILLWGSNPAE-THPVLAARLRRAKKRGAKLIVIDPRRTETAAKADEWLPIRPGTDAALALA--------------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 279 vakytvgfeelkahvkdftpEWAEKHTEIPAQVIREVAREMAAHKPRAVL---PPTRHnvWYGDDTYRVMALLyvNVLLG 355
Cdd:cd00368 220 --------------------EWAAEITGVPAETIRALAREFAAAKRAVILwgmGLTQH--TNGTQNVRAIANL--AALTG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 356 NYGRPGgfyiaqspylekyplpplplepaaggcsgpsggdhepegfkpradkgkffarstaiqeliepmitgepypikGL 435
Cdd:cd00368 276 NIGRPG------------------------------------------------------------------------GG 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 436 FAYGINLFHSIPNVPRTKEALKNLDLYVAIDVLPQEHVMWADVILPEATYLERYDDFVlvaHKTPFIQLRTPAHEPLFDT 515
Cdd:cd00368 284 LGPGGNPLVSAPDANRVRAALKKLDFVVVIDIFMTETAAYADVVLPAATYLEKEGTYT---NTEGRVQLFRQAVEPPGEA 360
|
490
....*....|....
gi 1886399248 516 KPGWWIARELGLRL 529
Cdd:cd00368 361 RSDWEILRELAKRL 374
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
47-606 |
6.11e-96 |
|
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: 307.25 E-value: 6.11e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 47 CFWRCGIVAHAVGNRVYKVEGYEANPKSRGRLCPRGQGAPQTTYDPDRLKRPLIRVEgsqRGEGKYRVATWEEALDHIAK 126
Cdd:cd02766 8 CPDTCSLLVTVEDGRIVRVEGDPAHPYTRGFICAKGARYVERVYSPDRLLTPLKRVG---RKGGQWERISWDEALDTIAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 127 KMLEIREKYGPEAIA---FFG-HGTGDYWFVDFLPAAWGSPNAAKpsvSLCTAPREVASQWVFGRpIGGHEPIDWENARY 202
Cdd:cd02766 85 KLKEIKAEYGPESILpysYAGtMGLLQRAARGRFFHALGASELRG---TICSGAGIEAQKYDFGA-SLGNDPEDMVNADL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 203 IVLIGhhigEDTHNTQLQDFAL---ALKNGAKVVVVDPRFSTAAAKAHRWLPIKPGTDTALLLAWIHVLIYEDLYDKEYV 279
Cdd:cd02766 161 IVIWG----INPAATNIHLMRIiqeARKRGAKVVVIDPYRTATAARADLHIQIRPGTDGALALGVAKVLFREGLYDRDFL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 280 AKYTVGFEELKAHVKDFTPEWAEKHTEIPAQVIREVAREMAAHKP---RAVLPPTRHNvwYGDDTYRVMALLyvNVLLGN 356
Cdd:cd02766 237 ARHTEGFEELKAHLETYTPEWAAEITGVSAEEIEELARLYGEAKPpsiRLGYGMQRYR--NGGQNVRAIDAL--PALTGN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 357 YGRPGGfyiaqspylekyplpplplepaaggcsgpsggdhepegfkpradkGKFFARSTAiqeliepmitgepyPIKGLF 436
Cdd:cd02766 313 IGVPGG---------------------------------------------GAFYSNSGP--------------PVKALW 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 437 AYGINLFHSIPNVPRTKEALKNLDLYVA-IDVLPQEHVMWADVILPEATYLERYDdfVLVAHKTPFIQLRTPAHEPLFDT 515
Cdd:cd02766 334 VYNSNPVAQAPDSNKVRKGLAREDLFVVvHDQFMTDTARYADIVLPATTFLEHED--VYASYWHYYLQYNEPAIPPPGEA 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 516 KPGWWIARELGLRLGLEQYFPWKTIEEYLE-----TRLQSLGLDLETMKGMGTLVQRGKPWledwekEGRLpFGTASGKI 590
Cdd:cd02766 412 RSNTEIFRELAKRLGFGEPPFEESDEEWLDqaldgTGLPLEGIDLERLLGPRKAGFPLVAW------EDRG-FPTPSGKF 484
|
570
....*....|....*.
gi 1886399248 591 ELYCQRFKEAGHQPLP 606
Cdd:cd02766 485 EFYSERAAKRGLPPLP 500
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
43-604 |
2.91e-91 |
|
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: 295.50 E-value: 2.91e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 43 ICEGCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRLCPRGQGAPQTTYDPDRLKRPLIRV--EGSQRGEGKYRVATWEEA 120
Cdd:cd02757 5 TCQGCTAWCGLQAYVEDGRVTKVEGNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRTnpRKGRDVDPKFVPISWDEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 121 LDHIAKKMLEIREKYGPEAIAFF----GHGTGDywFVDFLPAAWGSPNAAKPSvSLCTAPREVASQWVFGRPigGHEPID 196
Cdd:cd02757 85 LDTIADKIRALRKENEPHKIMLHrgryGHNNSI--LYGRFTKMIGSPNNISHS-SVCAESEKFGRYYTEGGW--DYNSYD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 197 WENARYIVLIGH-HIGEDTHNTQLQDFALALKNGAKVVVVDPRFSTAAAKAHRWLPIKPGTDTALLLAWIHVLIYEDLYD 275
Cdd:cd02757 160 YANAKYILFFGAdPLESNRQNPHAQRIWGGKMDQAKVVVVDPRLSNTAAKADEWLPIKPGEDGALALAIAHVILTEGLWD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 276 KEYVA----------------------KYTVGF-EELKAHVKDFTPEWAEKHTEIPAQVIREVAREMAAHKPRAVL---- 328
Cdd:cd02757 240 KDFVGdfvdgknyfkagetvdeesfkeKSTEGLvKWWNLELKDYTPEWAAKISGIPAETIERVAREFATAAPAAAAftwr 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 329 PPTRHNvwYGddTYRVMALLYVNVLLGNYGRPGGfyiaqspylekyplpplplepaaggcsgpsggdhepegfkpradkg 408
Cdd:cd02757 320 GATMQN--RG--SYNSMACHALNGLVGSIDSKGG---------------------------------------------- 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 409 kffarstaiqeLIEPMITGEpypIKGLFAYGINLFHSIPNVPRTKEALKNLDLYVAIDVLPQEHVMWADVILPEATYLER 488
Cdd:cd02757 350 -----------LCPNMGVPK---IKVYFTYLDNPVFSNPDGMSWEEALAKIPFHVHLSPFMSETTYFADIVLPDGHHFER 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 489 YDDFVLVAHKTPFIQLRTPAHEPLFDTKPGWWIARELGLRL------GLEQYFPWKtieeyletrlqslGLDLETMKGMG 562
Cdd:cd02757 416 WDVMSQENNLHPWLSIRQPVVKSLGEVREETEILIELAKKLdpkgsdGMKRYAPGQ-------------FKDPETGKNNR 482
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1886399248 563 tlvqrgkpwledWEKEgrLPFGTASGKIELYCQRFKEAGHQP 604
Cdd:cd02757 483 ------------WEFE--NVFPTETGKFEFYSETLKKYLQNH 510
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
49-615 |
6.21e-90 |
|
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: 294.91 E-value: 6.21e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 49 WRCGIVAHAVGNRVYKVEGYEANPKsrgRLCPRGQGAPQTTYDPDRLKRPLIRVE--------GSQRGEGKY-RVaTWEE 119
Cdd:cd02751 5 HWGPFKAHVKDGVIVRVEPDDTDQP---RPCPRGRSVRDRVYSPDRIKYPMKRVGwlgngpgsRELRGEGEFvRI-SWDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 120 ALDHIAKKMLEIREKYGPEAIaFFGHGTGDYWF--------VDFLPAAWGSPNAAKPSVSlcTAPREVASQWVFGRPIGG 191
Cdd:cd02751 81 ALDLVASELKRIREKYGNEAI-FGGSYGWASAGrlhhaqslLHRFLNLIGGYLGSYGTYS--TGAAQVILPHVVGSDEVY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 192 HEPIDW----ENARYIVLIGH--------HIGEDTHNtQLQDFALALKNGAKVVVVDPRFS-TAAAKAHRWLPIKPGTDT 258
Cdd:cd02751 158 EQGTSWddiaEHSDLVVLFGAnplktrqgGGGGPDHG-SYYYLKQAKDAGVRFICIDPRYTdTAAVLAAEWIPIRPGTDV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 259 ALLLAWIHVLIYEDLYDKEYVAKYTVGFEELKAHV---KDF---TPEWAEKHTEIPAQVIREVAREMAAhKPRAVL---P 329
Cdd:cd02751 237 ALMLAMAHTLITEDLHDQAFLARYTVGFDEFKDYLlgeSDGvpkTPEWAAEITGVPAETIRALAREIAS-KRTMIAqgwG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 330 PTRHNvwYGDDTYRVMALLyvNVLLGNYGRPG---GFYIAQSPYlekyplpplplepaAGGCSGPSGGDHEPEGFKPRAD 406
Cdd:cd02751 316 LQRAH--HGEQPAWMLVTL--AAMLGQIGLPGggfGFGYGYSNG--------------GGPPRGGAGGPGLPQGKNPVKD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 407 KGKFFARSTAIQELIEPM--ITGEP-YP-IKGLFAYGINLFHSIPNVPRTKEALKNLDLYVAIDVLPQEHVMWADVILPE 482
Cdd:cd02751 378 SIPVARIADALLNPGKEFtaNGKLKtYPdIKMIYWAGGNPLHHHQDLNRLIKALRKDETIVVHDIFWTASARYADIVLPA 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 483 ATYLERYDdfvLVAHKT---PFIQLRTPAHEPLFDTKPGWWIARELGLRLGLEQYFPW-KTIEEYLE-----TRLQSLGL 553
Cdd:cd02751 458 TTSLERND---IGLTGNysnRYLIAMKQAVEPLGEARSDYEIFAELAKRLGVEEEFTEgRDEMEWLEhlyeeTRAKAAGP 534
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1886399248 554 -----DLETMKGMGTLV--QRGKPWL------EDWEKEgrlPFGTASGKIELYCQRFKEAGH---QPLPVFTPPEEPP 615
Cdd:cd02751 535 gpelpSFEEFWEKGIVRvpAAPKPFVafadfrEDPEAN---PLGTPSGKIEIYSETLADFGYddcPGHPTWIEPWEGL 609
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
47-615 |
4.79e-89 |
|
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: 292.69 E-value: 4.79e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 47 CFWRCGIVAHAVGNRVYKVEGYEANPKSRG----RLCPRGQGAPQTTYDPDRLKRPLIRVegSQRGEGKYRVATWEEALD 122
Cdd:cd02770 8 CGGRCPLKAHVKDGVITRIETDDTGDDDPGfhqiRACLRGRSQRKRVYNPDRLKYPMKRV--GKRGEGKFVRISWDEALD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 123 HIAKKMLEIREKYGPEAIaFFGHGTGDYWFV-------DFLPAAWGSPNAAKPSVSlcTAPREVASQWVFGRPIGGHEPI 195
Cdd:cd02770 86 TIASELKRIIEKYGNEAI-YVNYGTGTYGGVpagrgaiARLLNLTGGYLNYYGTYS--WAQITTATPYTYGAAASGSSLD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 196 DWENARYIVLIGHHIGEDTHNTQLQ--DFALALKNGAKVVVVDPRFS-TAAAKAHRWLPIKPGTDTALLLAWIHVLIYED 272
Cdd:cd02770 163 DLKDSKLVVLFGHNPAETRMGGGGStyYYLQAKKAGAKFIVIDPRYTdTAVTLADEWIPIRPGTDAALVAAMAYVMITEN 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 273 LYDKEYVAKYTVGFEE--------LKAHVKDF-----------TPEWAEKHTEIPAQVIREVAREMAAHKPRAVLP---P 330
Cdd:cd02770 243 LHDQAFLDRYCVGFDAehlpegapPNESYKDYvlgtgydgtpkTPEWASEITGVPAETIRRLAREIATTKPAAILQgwgP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 331 TRHNvwYGDDTYRVMALLyvNVLLGNYGRPG---GFYIAQSPYlekyplpplplepaagGCSGPSGGDHepegfkPRADK 407
Cdd:cd02770 323 QRHA--NGEQAARAIMML--AAMTGNVGIPGgntGARPGGSAY----------------NGAGLPAGKN------PVKTS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 408 GKFFARSTAIQ--ELIEPMITGEP------YPIKGLFAYGIN-LFHSIPNVPRTKEALKNLD----LYVAIDVLPQEHVM 474
Cdd:cd02770 377 IPCFMWTDAIErgEEMTADDGGVKgadklkSNIKMIWNYAGNtLINQHSDDNNTTRALLDDEskceFIVVIDNFMTPSAR 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 475 WADVILPEATYLERYdDFVLVAHKTP--FIQLRTPAHEPLFDTKPGWWIARELGLRLGLE-QYFPWKTIEEYLE-----T 546
Cdd:cd02770 457 YADILLPDTTELERE-DIVLTSNAGMmeYLIYSQKAIEPLYECKSDYEICAELAKRLGVEdQFTEGKTEQEWLEelygqT 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 547 RLQSLGLD-LETMKGMGT-LVQRGKPW--LEDWEKE-GRLPFGTASGKIELYCQR------FKEAGHQ--PLPVFTPPEE 613
Cdd:cd02770 536 RAKEPGLPtYEEFREKGIyRVPRALPFvaFEDFREDpENNPLKTPSGKIEIYSKAladmakTLPEGDEipAIPKYVPAWE 615
|
..
gi 1886399248 614 PP 615
Cdd:cd02770 616 GP 617
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
43-589 |
1.10e-86 |
|
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: 283.34 E-value: 1.10e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 43 ICEGCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRLCPRGQGAPQTTYDPDRLKRPLIRVEGsqrgegKYRVATWEEALD 122
Cdd:cd02753 3 VCPYCGVGCGLELWVKDNKIVGVEPVKGHPVNRGKLCVKGRFGFDFVNSKDRLTKPLIRKNG------KFVEASWDEALS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 123 HIAKKMLEIREKYGPEAIAFFGHGTG----DYWFVDFLPAAWGSPN---AAKpsvsLCTAPREVASQWVFGrpIGGH-EP 194
Cdd:cd02753 77 LVASRLKEIKDKYGPDAIAFFGSAKCtneeNYLFQKLARAVGGTNNvdhCAR----LCHSPTVAGLAETLG--SGAMtNS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 195 I-DWENARYIVLIGHHIGEdTH---NTQLQDfalALKNGAKVVVVDPRFSTAAAKAHRWLPIKPGTDTALLLAWIHVLIY 270
Cdd:cd02753 151 IaDIEEADVILVIGSNTTE-AHpviARRIKR---AKRNGAKLIVADPRRTELARFADLHLQLRPGTDVALLNAMAHVIIE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 271 EDLYDKEYVAKYTVGFEELKAHVKDFTPEWAEKHTEIPAQVIREVAREMAAHKPRAVLpptrhnvwYG-------DDTYR 343
Cdd:cd02753 227 EGLYDEEFIEERTEGFEELKEIVEKYTPEYAERITGVPAEDIREAARMYATAKSAAIL--------WGmgvtqhsHGTDN 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 344 VMALLYVNVLLGNYGRPG-GFYiaqspylekyplpplplepaaggcsgPSGGDHEPEGfkpRADKGKFfarstaiqelie 422
Cdd:cd02753 299 VMALSNLALLTGNIGRPGtGVN--------------------------PLRGQNNVQG---ACDMGAL------------ 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 423 PMItgepYP--IKGLFAYGINLFHSIPNVPRTKEALKNLDLYVAIDVLPQEHVMWADVILPEATYLERYDDFVLVAHKtp 500
Cdd:cd02753 338 PNV----LPgyVKALYIMGENPALSDPNTNHVRKALESLEFLVVQDIFLTETAELADVVLPAASFAEKDGTFTNTERR-- 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 501 fIQLRTPAHEPLFDTKPGWWIARELGLRLGLE-QYFPWKTI-EEYLETRLQSLGLDLETMKGMGTL-------VQRGKPW 571
Cdd:cd02753 412 -VQRVRKAVEPPGEARPDWEIIQELANRLGYPgFYSHPEEIfDEIARLTPQYAGISYERLERPGGLqwpcpdeDHPGTPI 490
|
570
....*....|....*...
gi 1886399248 572 LEDWEkegrlpFGTASGK 589
Cdd:cd02753 491 LHTER------FATPDGK 502
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
46-611 |
1.42e-84 |
|
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: 279.36 E-value: 1.42e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 46 GCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRLCPRGQGAPQTTYDPDRLKRPLIRVegSQRGEGKYRVATWEEALDHIA 125
Cdd:cd02765 7 NCGGRCPLKCHVRDGKIVKVEPNEWPDKTYKRGCTRGLSHLQRVYSPDRLKYPMKRV--GERGEGKFERITWDEALDTIA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 126 KKMLEIREKYGPEAIAFFgHGTGDYWFVDFLPAAW---GSPNAAKPSVSLCTAP--REVASQwVFGRPigGHEPIDWENA 200
Cdd:cd02765 85 DKLTEAKREYGGKSILWM-SSSGDGAILSYLRLALlggGLQDALTYGIDTGVGQgfNRVTGG-GFMPP--TNEITDWVNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 201 RYIVLIGHHIGEdTHNTQLQDFALALKNGAKVVVVDPRFSTAAAKAHRWLPIKPGTDTALLLAWIHVLIYEDLYDKEYVA 280
Cdd:cd02765 161 KTIIIWGSNILE-TQFQDAEFFLDARENGAKIVVIDPVYSTTAAKADQWVPIRPGTDPALALGMINYILEHNWYDEAFLK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 281 KYT--------------------------------------------------------------VGFEELKAHVKDFTP 298
Cdd:cd02765 240 SNTsapflvredngtllrqadvtatpaedgyvvwdtnsdspepvaatninpalegeytingvkvhTVLTALREQAASYPP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 299 EWAEKHTEIPAQVIREVAREMAAHKPRAVLP---PTRhnVWYGDDTYRVMALLyvNVLLGNYGRPGgfyiaqspylekyp 375
Cdd:cd02765 320 KAAAEICGLEEAIIETLAEWYATGKPSGIWGfggVDR--YYHSHVFGRTAAIL--AALTGNIGRVG-------------- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 376 lpplplepaaGGCSGpsggdhepegfkpradkgkffarstaiqeliepmitgepypIKGLFAYGINLFHSIPNVPRTKEA 455
Cdd:cd02765 382 ----------GGVGQ-----------------------------------------IKFMYFMGSNFLGNQPDRDRWLKV 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 456 LKNLDLYVAIDVLPQEHVMWADVILPEATYLERYDDFVLVAHKtPFIQLRTPAHEPLFDTKPGWWIARELGLRLGLEQYF 535
Cdd:cd02765 411 MKNLDFIVVVDIFHTPTVRYADIVLPAAHWFEVEDLLVRYTTH-PHVLLQQKAIEPLFESKSDFEIEKGLAERLGLGDYF 489
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 536 PwKTIEEYLETRLQS-----LGLDLETMKGMGTLVQRGKPWLEDWEKEGRlPFGTASGKIELYCQRFKEAgHQPLPVFTP 610
Cdd:cd02765 490 P-KTPEDYVRAFMNSddpalDGITWEALKEEGIIMRLATPEDPYVAYLDQ-KFGTPSGKLEFYNEAAPEL-EEALPLPEE 566
|
.
gi 1886399248 611 P 611
Cdd:cd02765 567 P 567
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
51-589 |
1.87e-81 |
|
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: 271.02 E-value: 1.87e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 51 CGIVAHAVGNRVYKVEGYEANPKSRGRLCPRGQGAPQTTYDPDRLKRPLIRVEGsqrgeGKYRVATWEEALDHIAKKMLE 130
Cdd:cd02754 11 CGVEIGVKDGKVVAVRGDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLLRRNG-----GELVPVSWDEALDLIAERFKA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 131 IREKYGPEAIAFFGHG---TGDYWFVD-FLPAAWGSPNAaKPSVSLCTAPREVASQWVFG--RPIGGHEpiDWENARYIV 204
Cdd:cd02754 86 IQAEYGPDSVAFYGSGqllTEEYYAANkLAKGGLGTNNI-DTNSRLCMASAVAGYKRSFGadGPPGSYD--DIEHADCFF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 205 LIGHHIGEdTHNTQLQDFALALKN--GAKVVVVDPRFSTAAAKAHRWLPIKPGTDTALLLAWIHVLIYEDLYDKEYVAKY 282
Cdd:cd02754 163 LIGSNMAE-CHPILFRRLLDRKKAnpGAKIIVVDPRRTRTADIADLHLPIRPGTDLALLNGLLHVLIEEGLIDRDFIDAH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 283 TVGFEELKAHVKDFTPEWAEKHTEIPAQVIREVAREMaAHKPRAVLPPTR------HNVWygddtyRVMALLYVNVLLGN 356
Cdd:cd02754 242 TEGFEELKAFVADYTPEKVAEITGVPEADIREAARLF-GEARKVMSLWTMgvnqstQGTA------ANNAIINLHLATGK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 357 YGRPGG--FYIAQSPylekyplpplplePAAGG--CSGPS---GGDHEPEGFKPRADKGKF---------FARSTAIQEL 420
Cdd:cd02754 315 IGRPGSgpFSLTGQP-------------NAMGGreVGGLAnllPGHRSVNNPEHRAEVAKFwgvpegtipPKPGLHAVEM 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 421 IEPMITGEpypIKGLFAYGINLFHSIPNVPRTKEALKNLDLYVAIDV-LPQEHVMWADVILPEATYLERyDDFVLVAHKT 499
Cdd:cd02754 382 FEAIEDGE---IKALWVMCTNPAVSLPNANRVREALERLEFVVVQDAfADTETAEYADLVLPAASWGEK-EGTMTNSERR 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 500 pfIQLRTPAHEPLFDTKPGWWIARELGLRLGLEQYFPWKTIEE-YLETRLQSLGLDLEtMKGM--GTLVQRGKPW---LE 573
Cdd:cd02754 458 --VSLLRAAVEPPGEARPDWWILADVARRLGFGELFPYTSPEEvFEEYRRLSRGRGAD-LSGLsyERLRDGGVQWpcpDG 534
|
570 580
....*....|....*....|
gi 1886399248 574 DWEKEGRL----PFGTASGK 589
Cdd:cd02754 535 PPEGTRRLfedgRFPTPDGR 554
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
69-562 |
2.00e-75 |
|
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: 251.47 E-value: 2.00e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 69 EANPksRGrlCPRGQGAPQTTYDPDRLKRPLIRVEgsQRGEGKYRVATWEEALDHIAKKMLEIREKYGPEAIAFFGH--G 146
Cdd:cd02750 45 DYNP--RG--CQRGASFSWYLYSPDRVKYPLKRVG--ARGEGKWKRISWDEALELIADAIIDTIKKYGPDRVIGFSPipA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 147 TGdywfvdflPAAWGSP-------NAAKPSVSLCTAPREVASQWVFGRPIGGHEPIDWENARYIVLIGHHIGEdthnTQL 219
Cdd:cd02750 119 MS--------MVSYAAGsrfasliGGVSLSFYDWYGDLPPGSPQTWGEQTDVPESADWYNADYIIMWGSNVPV----TRT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 220 QD---FALALKNGAKVVVVDPRFSTAAAKAHRWLPIKPGTDTALLLAWIHVLIYEDLYDKEYVAKYTvgfeELKAHVkdF 296
Cdd:cd02750 187 PDahfLTEARYNGAKVVVVSPDYSPSAKHADLWVPIKPGTDAALALAMAHVIIKEKLYDEDYLKEYT----DLPFLV--Y 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 297 TPEWAEKHTEIPAQVIREVAREMAAHKPRAVLPPTRHNVWY-GDDTYRVMALLYvnVLLGNYGRPGGfyiaqspylekyp 375
Cdd:cd02750 261 TPAWQEAITGVPRETVIRLAREFATNGRSMIIVGAGINHWYhGDLCYRALILLL--ALTGNEGKNGG------------- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 376 lpplplepaaggcsgpsGGDHepegfkpradkgkffarstaiqeliepmITGEPypiKGLFAYGINLFHS-------IPN 448
Cdd:cd02750 326 -----------------GWAH----------------------------YVGQP---RVLFVWRGNLFGSsgkgheyFED 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 449 VPRTKealknLDLYVAIDVLPQEHVMWADVILPEATYLERYDDFVLVAHktPFIQLRTPAHEPLFDTKPGWWIARELGLR 528
Cdd:cd02750 358 APEGK-----LDLIVDLDFRMDSTALYSDIVLPAATWYEKHDLSTTDMH--PFIHPFSPAVDPLWEAKSDWEIFKALAKK 430
|
490 500 510
....*....|....*....|....*....|....
gi 1886399248 529 lgleqyFPWKTIeeyleTRLQSLGLDLETMKGMG 562
Cdd:cd02750 431 ------VPWRTL-----TGRQQFYLDHDWFLELG 453
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
41-555 |
4.79e-73 |
|
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: 247.70 E-value: 4.79e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 41 YQICEGCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRLCPRGQGAPQTTYDPDRLKRPLIRVEGSqrgegkYRVATWEEA 120
Cdd:cd02762 1 KRACILCEANCGLVVTVEDGRVASIRGDPDDPLSKGYICPKAAALGDYQNDPDRLRTPMRRRGGS------FEEIDWDEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 121 LDHIAKKMLEIREKYGPEAIAFFGHGTGDYWFV-----DFLPAAWGSPNAAKPSvSLCTAPREVASQWVFGRPIGGHEPi 195
Cdd:cd02762 75 FDEIAERLRAIRARHGGDAVGVYGGNPQAHTHAggaysPALLKALGTSNYFSAA-TADQKPGHFWSGLMFGHPGLHPVP- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 196 DWENARYIVLIGHH-----------IGEDTHNTQLQDfalalkNGAKVVVVDPRFSTAAAKAHRWLPIKPGTDTALLLAW 264
Cdd:cd02762 153 DIDRTDYLLILGANplqsngslrtaPDRVLRLKAAKD------RGGSLVVIDPRRTETAKLADEHLFVRPGTDAWLLAAM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 265 IHVLIYEDLYDKEYVAKYTVGFEELKAHVKDFTPEWAEKHTEIPAQVIREVAREMAAHKPRAVlpptrhnvwYGD----- 339
Cdd:cd02762 227 LAVLLAEGLTDRRFLAEHCDGLDEVRAALAEFTPEAYAPRCGVPAETIRRLAREFAAAPSAAV---------YGRlgvqt 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 340 ------DTYRVMALlyvNVLLGNYGRPGGfYIAQSPYLEKyplpplplepaaggcSGPSGGDHEPEGFKPRADKGKFFAR 413
Cdd:cd02762 298 qlfgtlCSWLVKLL---NLLTGNLDRPGG-AMFTTPALDL---------------VGQTSGRTIGRGEWRSRVSGLPEIA 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 414 S---TAIqeLIEPMITGEPYPIKGLFAYGINLFHSIPNVPRTKEALKNLDLYVAIDVLPQEHVMWADVILPEATYLER-- 488
Cdd:cd02762 359 GelpVNV--LAEEILTDGPGRIRAMIVVAGNPVLSAPDGARLEAALGGLEFMVSVDVYMTETTRHADYILPPASQLEKph 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1886399248 489 YDDFVLVAHKTPFiQLRTPAHEPLFDTKPGWWIARELG------LRLGL--EQYFPWKTIEEYLETRlqsLGLDL 555
Cdd:cd02762 437 ATFFNLEFPRNAF-RYRRPLFPPPPGTLPEWEILARLVealdavLRAGFygERAGGTLLLAALLERP---SGVDL 507
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
1-743 |
6.01e-68 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 239.93 E-value: 6.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 1 MQRREFLKLSALGVGAMA--------LRGSGPAKALkAPWYAQEvKSVYQICE-GCFWRCGIVAHAVGNRVYKVE----- 66
Cdd:PRK14990 14 VSRRGLVKTTAIGGLAMAssaltlpfSRIAHAVDSA-IPTKSDE-KVIWSACTvNCGSRCPLRMHVVDGEIKYVEtdntg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 67 --GYEANPKSRGrlCPRGQGAPQTTYDPDRLKRPLIRVegSQRGEGKYRVATWEEALDHIAKKMLEIREKYGPEAIaFFG 144
Cdd:PRK14990 92 ddNYDGLHQVRA--CLRGRSMRRRVYNPDRLKYPMKRV--GARGEGKFERISWEEAYDIIATNMQRLIKEYGNESI-YLN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 145 HGTGDywFVDFLPAAWGSPNAAKPSVSLCT----------APREVAS--QWVFGRPIGGHEPIDWENARYIVLIGHHIGE 212
Cdd:PRK14990 167 YGTGT--LGGTMTRSWPPGNTLVARLMNCCggylnhygdySSAQIAEglNYTYGGWADGNSPSDIENSKLVVLFGNNPGE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 213 DTHNTQLQDFALA---LKNGAKVVVVDPRFS-TAAAKAHRWLPIKPGTDTALLLAWIHVLIYEDLYDKEYVAKYTVGFEE 288
Cdd:PRK14990 245 TRMSGGGVTYYLEqarQKSNARMIIIDPRYTdTGAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQPFLDKYCVGYDE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 289 --------LKAHVKDF-----------TPEWAEKHTEIPAQVIREVAREMAAHKPRAVLP---PTRHNvwYGDDTYRVMA 346
Cdd:PRK14990 325 ktlpasapKNGHYKAYilgegpdgvakTPEWASQITGVPADKIIKLAREIGSTKPAFISQgwgPQRHA--NGEIATRAIS 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 347 LLyvNVLLGNYGRPGGFYIAQSpylekyplpplplepaaGGCSGPSggDHEPEGFKPRADKGKFFARSTAIQE-----LI 421
Cdd:PRK14990 403 ML--AILTGNVGINGGNSGARE-----------------GSYSLPF--VRMPTLENPIQTSISMFMWTDAIERgpemtAL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 422 EPMITGE---PYPIKGLFAYGIN-LFHSIPNVPRTKEAL---KNLDLYVAIDVLPQEHVMWADVILPEATYLERYdDFVL 494
Cdd:PRK14990 462 RDGVRGKdklDVPIKMIWNYAGNcLINQHSEINRTHEILqddKKCELIVVIDCHMTSSAKYADILLPDCTASEQM-DFAL 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 495 VAH--KTPFIQLRTPAHEPLFDTKPGWWIARELGLRLGLEQYFP-WKTIEEYL-----ETRLQSLGL-DLETMKGMGTLV 565
Cdd:PRK14990 541 DAScgNMSYVIFNDQVIKPRFECKTIYEMTSELAKRLGVEQQFTeGRTQEEWMrhlyaQSREAIPELpTFEEFRKQGIFK 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 566 QRG--------KPWLEDWEKEgrlPFGTASGKIELYCQRFKEAGH----------QPLPVFTPPEE----PPEGFYRL-- 621
Cdd:PRK14990 621 KRDpqghhvayKAFREDPQAN---PLTTPSGKIEIYSQALADIAAtwelpegdviDPLPIYTPGFEsyqdPLNKQYPLql 697
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 622 --LYGRSPVHTfarTQNNWVLMEMDPENEVWIHKEEAKRLGLKEGDYVMLVNQDGvkEGPVRVKPTARIRKDCVYIVHGF 699
Cdd:PRK14990 698 tgFHYKSRVHS---TYGNVDVLKAACRQEMWINPLDAQKRGINNGDKVRIFNDRG--EVHIEAKVTPRMMPGVVALGEGA 772
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 1886399248 700 GHKAPLMRLahGRGASDNYLQTRyKLDPISGGAGLRVNFVRLEK 743
Cdd:PRK14990 773 WYDPDAKRV--DKGGCINVLTTQ-RPSPLAKGNPSHTNLVQVEK 813
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
41-531 |
7.49e-65 |
|
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: 228.56 E-value: 7.49e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 41 YQICEGCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRLCPRGQGAPQTTYDPDRLKRPLIRVEgsQRGEGKYRVATWEEA 120
Cdd:cd02763 1 TTTCYMCACRCGIRVHLRDGKVRYIKGNPDHPLNKGVICAKGSSGIMKQYSPARLTKPLLRKG--PRGSGQFEEIEWEEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 121 LDHIAKKMLEIREKyGPEAIAFFghgTG-------DYWFVdflpAAWGSPNAAKPSvSLCTAPREVA-------SQWVFG 186
Cdd:cd02763 79 FSIATKRLKAARAT-DPKKFAFF---TGrdqmqalTGWFA----GQFGTPNYAAHG-GFCSVNMAAGglysiggSFWEFG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 187 RPigghepiDWENARYIVLIGhhIGEDTHNTQLQDFALALKN-GAKVVVVDPRFSTAAAKAHRWLPIKPGTDTALLLAWI 265
Cdd:cd02763 150 GP-------DLEHTKYFMMIG--VAEDHHSNPFKIGIQKLKRrGGKFVAVNPVRTGYAAIADEWVPIKPGTDGAFILALA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 266 HVLIYEDLYDKEYVAKYTvgfeelKAHV-KDFTPEWAEKHTEIPAQVIREVAREMA--AHKPRAVLPPTRHNVW------ 336
Cdd:cd02763 221 HELLKAGLIDWEFLKRYT------NAAElVDYTPEWVEKITGIPADTIRRIAKELGvtARDQPIELPIAWTDVWgrkhek 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 337 ------------------YGDDTYRVMALLYvnVLLGNYGRPGGF--------YIAQSPYLEKYPLPPLPLEPAAGGCSG 390
Cdd:cd02763 295 itgrpvsfhamrgiaahsNGFQTIRALFVLM--MLLGTIDRPGGFrhkppyprHIPPLPKPPKIPSADKPFTPLYGPPLG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 391 -PSGGDH---EPEGFKPRADKGKFFARSTAIQELIEPMIT----GEPYPIKGLFAYGINL-FHSIPNVPRTKEALKNLD- 460
Cdd:cd02763 373 wPASPDDllvDEDGNPLRIDKAYSWEYPLAAHGCMQNVITnawrGDPYPIDTLMIYMANMaWNSSMNTPEVREMLTDKDa 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 461 -------LYVAIDVLPQEHVMWADVILPEATYLERYDDFVLVAHKT-----PFIQLRTPAHEPLFDTKPGWWIARELGLR 528
Cdd:cd02763 453 sgnykipFIIVCDAFYSEMVAFADLVLPDTTYLERHDAMSLLDRPIseadgPVDAIRVPIVEPKGDVKPFQEVLIELGTR 532
|
...
gi 1886399248 529 LGL 531
Cdd:cd02763 533 LGL 535
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
61-615 |
1.14e-51 |
|
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: 190.17 E-value: 1.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 61 RVYKVEGYEANPKSRgrlcPRGQGAPQTTYDPDRLKRPLIRVE---------GSQRGEGKY-RVaTWEEALDHIAKKMLE 130
Cdd:cd02769 17 RIVGVRPFEEDPDPS----PLLDGVPDAVYSPTRIKYPMVRRGwlekgpgsdRSLRGKEEFvRV-SWDEALDLVAAELKR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 131 IREKYGPEAIafFGHGTGdywfvdflpaaWGSPNAAKPSVSL------CT--APREV------ASQWVFGRPIGGHEPID 196
Cdd:cd02769 92 VRKTYGNEAI--FGGSYG-----------WSSAGRFHHAQSLlhrflnLAggYVGSVgdystgAAQVILPHVVGSMEVYT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 197 -----W----ENARYIVLIGhhiGEDTHNTQLQDFAL----------ALKN-GAKVVVVDP-RFSTAAAKAHRWLPIKPG 255
Cdd:cd02769 159 eqqtsWpviaEHTELVVAFG---ADPLKNAQIAWGGIpdhqaysylkALKDrGIRFISISPlRDDTAAELGAEWIAIRPG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 256 TDTALLLAWIHVLIYEDLYDKEYVAKYTVGFEELKAHV---KD---FTPEWAEKHTEIPAQVIREVAREMAAHKpravlp 329
Cdd:cd02769 236 TDVALMLALAHTLVTEGLHDKAFLARYTVGFDKFLPYLlgeSDgvpKTPEWAAAICGIPAETIRELARRFASKR------ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 330 pTRHNV-W------YGDDTYrvMALLYVNVLLGNYGRPGGFYIAQSPYLekyplpplplePAAGGCSGPSGGDHEPEGFK 402
Cdd:cd02769 310 -TMIMAgWslqrahHGEQPH--WMAVTLAAMLGQIGLPGGGFGFGYHYS-----------NGGGPPRGAAPPPALPQGRN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 403 PRADkgkFFARSTAIQELIEPmitGEP---------YP-IKglFAY--GINLFHSIPNVPRTKEALKNLDLYVAIDVLPQ 470
Cdd:cd02769 376 PVSS---FIPVARIADMLLNP---GKPfdyngkkltYPdIK--LVYwaGGNPFHHHQDLNRLIRAWQKPETVIVHEPFWT 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 471 EHVMWADVILPEATYLERyDDFVlVAHKTPFIQLRTPAHEPLFDTKPGWWIARELGLRLGLEQYFP-------W-KTIee 542
Cdd:cd02769 448 ATARHADIVLPATTSLER-NDIG-GSGDNRYIVAMKQVVEPVGEARDDYDIFADLAERLGVEEQFTegrdemeWlRHL-- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 543 YLETRLQSLGLDLEtMKGMGTLVQRGKPWLEDWEKE-GRL----------PFGTASGKIELYCQR---FKEAGHQPLPVF 608
Cdd:cd02769 524 YEESRAQAAARGVE-MPSFDEFWAQGYVELPIPEADfVRLadfredpeanPLGTPSGRIEIFSETiagFGYDDCPGHPTW 602
|
....*..
gi 1886399248 609 TPPEEPP 615
Cdd:cd02769 603 LEPAEWL 609
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
41-535 |
7.59e-51 |
|
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: 189.86 E-value: 7.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 41 YQICEGCFWRCGIVAHaVGNRVYKVEGYEANP------------------------------KSRGRLCPRGQGAPQTTY 90
Cdd:cd02758 1 YSSCLGCWTQCGIRVR-VDKETGKVLRIAGNPyhplntapslpyntplkeslylslvgenglKARATACARGNAGLQYLY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 91 DPDRLKRPLIRVegSQRGEGKYRVATWEEALDHIAK----------------KMLEI-----REKYGPEA--IAF-FGHG 146
Cdd:cd02758 80 DPYRVLQPLKRV--GPRGSGKWKPISWEQLIEEVVEggdlfgeghveglkaiRDLDTpidpdHPDLGPKAnqLLYtFGRD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 147 TGDYWFVD-FLPAAWGSPNAAKPSvSLCTAPREVASQWVFGRPIGGHEPI-DWENARYIVLIGHHIGEDTHNTQLQDFAL 224
Cdd:cd02758 158 EGRTPFIKrFANQAFGTVNFGGHG-SYCGLSYRAGNGALMNDLDGYPHVKpDFDNAEFALFIGTSPAQAGNPFKRQARRL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 225 ALK---NGAKVVVVDPRFS---TAAAKAHRWLPIKPGTDTALLLAWIHVLIYEDLYDKEY-------------------- 278
Cdd:cd02758 237 AEArteGNFKYVVVDPVLPnttSAAGENIRWVPIKPGGDGALAMAMIRWIIENERYNAEYlsipskeaakaagepswtna 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 279 ---VAKYTV--GFEELKAHVKDFT-PEWAEkHTEIPAQVIREVAREMAAHKPRAVLpPTRHNVWYGDDTYRVMALLYVNV 352
Cdd:cd02758 317 thlVITVRVksALQLLKEEAFSYSlEEYAE-ICGVPEAKIIELAKEFTSHGRAAAV-VHHGGTMHSNGFYNAYAIRMLNA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 353 LLGNYGRPGGFYIAQSPYLEKYPLPPLPLEPAAGGC--SGPSGGDHEP-----EGFKPRADKGK---------FFARSTA 416
Cdd:cd02758 395 LIGNLNWKGGLLMSGGGFADNSAGPRYDFKKFFGEVkpWGVPIDRSKKayektSEYKRKVAAGEnpypakrpwYPLTPEL 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 417 IQELIEPMITGEPYPIKGLFAYGINLFHSIPN-VPRTKEALKN---LDLYVAIDVLPQEHVMWADVILPEATYLER---- 488
Cdd:cd02758 475 YTEVIASAAEGYPYKLKALILWMANPVYGAPGlVKQVEEKLKDpkkLPLFIAIDAFINETSAYADYIVPDTTYYESwgfs 554
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1886399248 489 --YDDFVLVAHktpfiQLRTPAHEPLFDTKPGwwiarelGLRLGLEQYF 535
Cdd:cd02758 555 tpWGGVPTKAS-----TARWPVIAPLTEKTAN-------GHPVSMESFL 591
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
619-743 |
3.26e-48 |
|
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: 166.30 E-value: 3.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 619 YRLLYGRSPVHTFARTQNNWVLMEMDPENEVWIHKEEAKRLGLKEGDYVMLVNQDGVKEGPVRVKPTarIRKDCVYIVHG 698
Cdd:cd02778 2 FRLIYGKSPVHTHGHTANNPLLHELTPENTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEG--IRPDTVFMPHG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1886399248 699 FGHKAPLMRLAHGRGASDNYLqTRYKLDPISGGAGLRVNFVRLEK 743
Cdd:cd02778 80 FGHWAPALSRAYGGGVNDNNL-LPGSTEPVSGGAGLQEFTVTVRK 123
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
43-603 |
1.15e-46 |
|
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: 176.44 E-value: 1.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 43 ICEGCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRLCPRGQGAPQTTYDPDRLKRPLIRVEGSqrgeGKYRVATWEEALD 122
Cdd:cd02752 3 ICPYCSVGCGLIAYVQNGVWVHQEGDPDHPVNRGSLCPKGAALRDFVHSPKRLKYPMYRAPGS----GKWEEISWDEALD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 123 HIAKKMLEIREK------------YGPEAIAFFGHGTGD----YWFVDFLpAAWGSpNAAKPSVSLCTAPREVASQWVFG 186
Cdd:cd02752 79 EIARKMKDIRDAsfveknaagvvvNRPDSIAFLGSAKLSneecYLIRKFA-RALGT-NNLDHQARIUHSPTVAGLANTFG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 187 RPIGGHEPIDWENARYIVLIGHHIGEDtHNTQLQDFALAL-KNGAKVVVVDPRFSTAAAKAHRWLPIKPGTDTALLLAWI 265
Cdd:cd02752 157 RGAMTNSWNDIKNADVILVMGGNPAEA-HPVSFKWILEAKeKNGAKLIVVDPRFTRTAAKADLYVPIRSGTDIAFLGGMI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 266 HvliyedlydkeYVAKYtvgfeelkahvkdfTPEWAEKHTEIPAQVIREVAREMAAH----KPRAV---LPPTRHNVwyG 338
Cdd:cd02752 236 N-----------YIIRY--------------TPEEVEDICGVPKEDFLKVAEMFAATgrpdKPGTIlyaMGWTQHTV--G 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 339 DDTYRVMALLyvNVLLGNYGRPGGfyiaqspylekyplpplpLEPAAGGCSGPSGGdhepegfkprADKGKFFarstaiq 418
Cdd:cd02752 289 SQNIRAMCIL--QLLLGNIGVAGG------------------GVNALRGHSNVQGA----------TDLGLLS------- 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 419 eliepmitgepypiKGLFAY--GINLFHSIPNVPRTKEALKNLDLYVAIDVLPQE-HVMWAD------------VILPEA 483
Cdd:cd02752 332 --------------HNLPGYlgGQNPNSSFPNANKVRRALDKLDWLVVIDPFPTEtAAFWKNpgmdpksiqtevFLLPAA 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 484 TYLERYDDFVLVAHktpFIQLRTPAHEPLFDTKPGWWIARELGLRLG-LEQYFPWKTIEEYLE--------------TRL 548
Cdd:cd02752 398 CQYEKEGSITNSGR---WLQWRYKVVEPPGEAKSDGDILVELAKRLGfLYEKEGGAFPEPITKwnygygdeptpeeiARE 474
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1886399248 549 QSLGL--DLETMKGMGTLVQRGKPWLEdwEKEGRLPFGTASGKiELYCQRFKEAGHQ 603
Cdd:cd02752 475 INGGAltDGYTGQSPERLKAHGQNVHT--FDTLRDDGSTACGC-WIYSGSYTEEGRM 528
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
94-526 |
1.48e-45 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 166.81 E-value: 1.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 94 RLKRPLIRvegsqRGEGKYRVATWEEALDHIAKKMLEIREKYGPEAIAFFGhGTGDYWFVDFLPAA------WGSPNAA- 166
Cdd:pfam00384 1 RLKYPMVR-----RGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAING-GSGGLTDVESLYALkkllnrLGSKNGNt 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 167 -KPSVSLCTAPREVA-SQWVFGRpIGGHEPIDWENARYIVLIGHHIGEdTH---NTQLqdFALALKNGAKVVVVDPRFSt 241
Cdd:pfam00384 75 eDHNGDLCTAAAAAFgSDLRSNY-LFNSSIADIENADLILLIGTNPRE-EApilNARI--RKAALKGKAKVIVIGPRLD- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 242 aAAKAHRWLPIKPGTDTALLLAWIHVLIYEDLYDkeyvakytvgfeelkahvKDFTPewaekhteipaqvirevaremaa 321
Cdd:pfam00384 150 -LTYADEHLGIKPGTDLALALAGAHVFIKELKKD------------------KDFAP----------------------- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 322 hKPrAVLPPTRHNVWY-GDDTYRvmALLYVNVLLGNYGRPGG----FYIAQSpylekyplpplplepaaGGCSGpSGGDh 396
Cdd:pfam00384 188 -KP-IIIVGAGVLQRQdGEAIFR--AIANLADLTGNIGRPGGgwngLNILQG-----------------AASPV-GALD- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 397 epEGFKPRadkgkffarstaiQELIEPMITGEPYPIKGLFAYGINLFHSIPNVPRTKEALKNLDLYVAIDVLPQEH-VMW 475
Cdd:pfam00384 245 --LGLVPG-------------IKSVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFVVYDGHHGDKtAKY 309
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1886399248 476 ADVILPEATYLERYDDFVLVAHKtpfIQLRTPAHEPLFDTKPGWWIARELG 526
Cdd:pfam00384 310 ADVILPAAAYTEKNGTYVNTEGR---VQSTKQAVPPPGEAREDWKILRALS 357
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
1-674 |
5.15e-39 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 155.21 E-value: 5.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 1 MQRREFLKlSALGVGAMALRGSG---PAKALKAPWYAQEVKSVYQIcEGCFWRcGIVAHAVGNRVYKVEGYE--ANPksr 75
Cdd:PRK15102 1 ASRRRFLK-GLGGLSAAGMLGPSlltPRSALAAQAAAAETTKEWIL-TGSHWG-AFRAKVKNGRFVEAKPFEldKYP--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 76 grlCPRGQGAPQTTYDPDRLKRPLIRVE---------GSQRGEGKYRVATWEEALDHIAKKMLEIREKYGPEAI------ 140
Cdd:PRK15102 75 ---TKMINGIKGHVYNPSRIRYPMVRLDwlrkrhksdTSQRGDNRFVRVSWDEALDLFYEELERVQKTYGPSALhtgqtg 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 141 ----------------AFFGHGT-----GDYwfvdflpaawgSPNAAK---PSVSLCTaprEVASQwvfgrpiGGHEPID 196
Cdd:PRK15102 152 wqstgqfhsatghmqrAIGMHGNsvgtvGDY-----------STGAGQvilPYVLGST---EVYEQ-------GTSWPLI 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 197 WENARYIVLIGH------HIG--EDTHNT--QLQDFALALKNGA-KVVVVDPRFStaaaKAHRWLP-----IKPGTDTAL 260
Cdd:PRK15102 211 LENSKTIVLWGSdpvknlQVGwnCETHESyaYLAQLKEKVAKGEiNVISIDPVVT----KTQNYLGcehlyVNPQTDVPL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 261 LLAWIHVLIYEDLYDKEYVAKYTVGFEELKAHV---KD---FTPEWAEKHTEIPAQVIREVAREMAAHKPRAVLPPTRHN 334
Cdd:PRK15102 287 MLALAHTLYSENLYDKKFIDNYCLGFEQFLPYLlgeKDgvpKTPEWAEKICGIDAETIRELARQMAKGRTQIIAGWCIQR 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 335 VWYGDDTYRVMALLyvNVLLGNYGRPGGFYiaqsPYLEKYPLPPLPLEPAAGGCSGPSGGDhepEGFKPRADKGKFFARS 414
Cdd:PRK15102 367 QQHGEQPYWMGAVL--AAMLGQIGLPGGGI----SYGHHYSGIGVPSSGGAIPGGFPGNLD---TGQKPKHDNSDYKGYS 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 415 TAI------QELIEPMIT----GEP--YP-IKGLFAYGINLFHSIPNVPRTKEALKNLDLYVAIDVLPQEHVMWADVILP 481
Cdd:PRK15102 438 STIpvarfiDAILEPGKTinwnGKKvtLPpLKMMIFSGTNPWHRHQDRNRMKEAFRKLETVVAIDNQWTATCRFADIVLP 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 482 EATYLERYDDFVLVAHKTPFIQLRTPAHEPLFDTKPGWWIARELGLRLGLEQYFP-------WktIEE-YLETRLQSLGL 553
Cdd:PRK15102 518 ACTQFERNDIDQYGSYSNRGIIAMKKVVEPLFESRSDFDIFRELCRRFGREKEYTrgmdemgW--LKRlYQECKQQNKGK 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 554 ----DLETMKGMG-TLVQRGKPWL--EDWEKEGRL-PFGTASGKIELYCQRFKEAGH---QPLPVFTPPEEPPEG----- 617
Cdd:PRK15102 596 fhmpEFDEFWKKGyVEFGEGQPWVrhADFREDPELnPLGTPSGLIEIYSRKIADMGYddcQGHPMWFEKIERSHGgpgsd 675
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 618 -----------------------FYRLLY---GRSPvhtfartqnnwvlmemdpeneVWIHKEEAKRLGLKEGDYVMLVN 671
Cdd:PRK15102 676 kyplwlqsvhpdkrlhsqlceseELRETYtvqGREP---------------------VYINPQDAKARGIKDGDVVRVFN 734
|
...
gi 1886399248 672 QDG 674
Cdd:PRK15102 735 DRG 737
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
44-534 |
9.78e-37 |
|
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: 147.81 E-value: 9.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 44 CEGCFWRCGIVAHAVGNRVykVEGYEANPK------SRGRLCPRGQGAPQTTYDPDRLKRPLIRV---EGSQRGEGkYRV 114
Cdd:cd02760 4 CYNCVAGPDFMAVKVVDGV--ATEIEPNFAaedihpARGRVCVKAYGLVQKTYNPNRVLQPMKRTnpkKGRNEDPG-FVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 115 ATWEEALDHIAKKMLEIREKYG------PEAIAFFGHG--TGDYW--FVDFLpAAWGSPNAAKPSVSL--CTAPREVASQ 182
Cdd:cd02760 81 ISWDEALDLVAAKLRRVREKGLldekglPRLAATFGHGgtPAMYMgtFPAFL-AAWGPIDFSFGSGQGvkCVHSEHLYGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 183 -WVFGRPIGGhepiDWENARYIVLIGHHIGEDTHNTQLQDFALALKNGAKVVVVDPRFSTAAAKAHRWLPIKPGTDTALL 261
Cdd:cd02760 160 fWHRAFTVAA----DTPLANYVISFGSNVEASGGPCAVTRHADARVRGYKRVQVEPHLSVTGACSAEWVPIRPKTDPAFM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 262 LAWIHVLIYE---DLYDKEYV-----AKYTVG------------------------------------------------ 285
Cdd:cd02760 236 FAMIHVMVHEqglGKLDVPFLrdrtsSPYLVGpdglylrdaatgkplvwdersgravpfdtrgavpavagdfavdgavsv 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 286 -----------------FEELKAHVKDFTPEWAEKHTEIPAQVIREVAREMA----------------AHKPRAV-LPPT 331
Cdd:cd02760 316 daddetaihqgvegttaFTMLVEHMRKYTPEWAESICDVPAATIRRIAREFLenasigstievdgvtlPYRPVAVtLGKS 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 332 RHNVWygDDTYRVMALLYVNVLLGNYGRPG-------------------------GFYIAQSPYLEKYPLPPLPLEPAAG 386
Cdd:cd02760 396 VNNGW--GAFECCWARTLLATLVGALEVPGgtlgttvrlnrphddrlasvkpgedGFMAQGFNPTDKEHWVVKPTGRNAH 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 387 GCSGPSGGDHE-PEGFKPRaDKGKFFARSTAIQELIEPmitgePYPIKGLFAYGINLFHSIPNVPRTKEALKNLDLYVAI 465
Cdd:cd02760 474 RTLVPIVGNSAwSQALGPT-QLAWMFLREVPLDWKFEL-----PTLPDVWFNYRTNPAISFWDTATLVDNIAKFPFTVSF 547
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1886399248 466 DVLPQEHVMWADVILPEATYLERYDdfVLVAHKTPFIQ---------LRTPAHEPLFDTKPGWWIARELGLRLGL-EQY 534
Cdd:cd02760 548 AYTEDETNWMADVLLPEATDLESLQ--MIKVGGTKFVEqfwehrgvvLRQPAVEPQGEARDFTWISTELAKRTGLlADY 624
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
3-537 |
1.16e-29 |
|
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: 124.14 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 3 RREFLKLSALGVGAMALRGSGPAKALKAPW-----------YAQEVKSVYQICEGCfwrcGIVAHAVGNRVYKVEGYEAN 71
Cdd:cd02764 1 RRGFLKLMGASLAMASAAACRYPVEKIVPYviwpenivpgeTVYYATSLVPAGEGQ----GVLVKTVDGRPIKIEGNPDH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 72 PKSRGRLCPRGQGAPQTTYDPDRLKRPLIRVEGSQRGEgkyrvATWEEALDHIAKKMLEIREKY----------GP---E 138
Cdd:cd02764 77 PASLGGTSARAQASVLSLYDPDRAQGPLRRGIDGAYVA-----SDWADFDAKVAEQLKAVKDGGklavlsgnvnSPtteA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 139 AIAFF-GHGTGDYWFVdflpaaWgSPNAAKPSVSlctaprevASQWVFGRPigGHEPIDWENARYIV-----LIGHHIGE 212
Cdd:cd02764 152 LIGDFlKKYPGAKHVV------Y-DPLSAEDVNE--------AWQASFGKD--VVPGYDFDKAEVIVsidadFLGSWISA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 213 DTHNtqlQDFA-----LALKNGAKVVVVDPRFSTAAAKAHRWLPIKPGTDTALLLAWIHVLIyedlyDKEYVAKYTVGFE 287
Cdd:cd02764 215 IRHR---HDFAakrrlGAEEPMSRLVAAESVYTLTGANADVRLAIRPSQEKAFALGLAHKLI-----KKGAGSSLPDFFR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 288 ELKAhvkDFTPEWAEKHTEIPAQVIREVAREMAAHKPRAVLPPTRHNVWYGDDTyrVMALLYVNVLLGNYGRpggfyiaq 367
Cdd:cd02764 287 ALNL---AFKPAKVAELTVDLDKALAALAKALAAAGKSLVVAGSELSQTAGADT--QVAVNALNSLLGNDGK-------- 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 368 spylekyplpplPLEPAAGGCSGPSGGDHepegfkpradkgkffarstAIQELIEPMITGEpypIKGLFAYGINLFHSIP 447
Cdd:cd02764 354 ------------TVDHARPIKGGELGNQQ-------------------DLKALASRINAGK---VSALLVYDVNPVYDLP 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 448 NVPRTKEALKNLDLYVAIDVLPQEHVMWADVILPEATYLERYDDFVLVAhktPFIQLRTPAHEPLFDTKPGW-----WIA 522
Cdd:cd02764 400 QGLGFAKALEKVPLSVSFGDRLDETAMLCDWVAPMSHGLESWGDAETPD---GTYSICQPVIAPLFDTRSAQeslllALG 476
|
570
....*....|....*
gi 1886399248 523 RELGLRLGLEQYFPW 537
Cdd:cd02764 477 GSLGGYEKLRRYTSW 491
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
94-488 |
2.14e-26 |
|
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: 114.71 E-value: 2.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 94 RLKRPLIRvegsQRGEGKYRVATWEEALDHIAKKMLEIRekygPEAIAFF--GHGTGDYWFVDFLPA-AWGS---PNAAK 167
Cdd:cd02767 64 RLTYPMRY----DAGSDHYRPISWDEAFAEIAARLRALD----PDRAAFYtsGRASNEAAYLYQLFArAYGTnnlPDCSN 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 168 psvsLCTAPREVASQWVFGRPIGGHEPIDWENARYIVLIGHHIGEDtHNTQLQDFALALKNGAKVVVVDP-------RF- 239
Cdd:cd02767 136 ----MCHEPSSVGLKKSIGVGKGTVSLEDFEHTDLIFFIGQNPGTN-HPRMLHYLREAKKRGGKIIVINPlrepgleRFa 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 240 -----STAAAK----AHRWLPIKPGTDTALLLAWIHVLIYED-----LYDKEYVAKYTVGFEELKAHVKDFtpEWA--EK 303
Cdd:cd02767 211 npqnpESMLTGgtkiADEYFQVRIGGDIALLNGMAKHLIERDdepgnVLDHDFIAEHTSGFEEYVAALRAL--SWDeiER 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 304 HTEIPAQVIREVAReMAAHKPRAVLpptrhnVW--------YGDDTYRVMallyVNVLL--GNYGRPGgfyiaqspylek 373
Cdd:cd02767 289 ASGLSREEIEAFAA-MYAKSERVVF------VWgmgitqhaHGVDNVRAI----VNLALlrGNIGRPG------------ 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 374 yplpplplepaAGGCS--GPSG--GDHE--------PE---------GFKPRADKGkffaRSTAiqELIEPMITGEpypI 432
Cdd:cd02767 346 -----------AGLMPirGHSNvqGDRTmgitekpfPEfldaleevfGFTPPRDPG----LDTV--EAIEAALEGK---V 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1886399248 433 KGLFAYGINLFHSIPNVPRTKEALKNLDLYVAID-VLPQEHVMWADV--ILPEATYLER 488
Cdd:cd02767 406 KAFISLGGNFAEAMPDPAATEEALRRLDLTVHVAtKLNRSHLVHGEEalILPCLGRTEI 464
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
629-735 |
2.70e-19 |
|
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site. This hierarchy is of the conserved MopB_CT domain present in many, but not all, MopB homologs.
Pssm-ID: 239176 [Multi-domain] Cd Length: 101 Bit Score: 83.52 E-value: 2.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 629 HTFARTQNNWvLMEMDPENEVWIHKEEAKRLGLKEGDYVMLVNQDGVKEGPVRVkpTARIRKDCVYIVHGFGHKaplmrl 708
Cdd:cd02775 6 HSGTRTRNPW-LRELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKV--TDGVPPGVVFLPHGWGHR------ 76
|
90 100
....*....|....*....|....*..
gi 1886399248 709 aHGRGASDNYLqTRYKLDPISGGAGLR 735
Cdd:cd02775 77 -GGRGGNANVL-TPDALDPPSGGPAYK 101
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
1-328 |
7.34e-18 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 88.42 E-value: 7.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 1 MQRREFLKLSALGVGAMALRGSGPAKALKAPWYAQ-EVKSVYQICEGCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRLC 79
Cdd:PRK13532 3 LSRRDFMKANAAAAAAAAAGLSLPAVANAVVGSAQtAIKWDKAPCRFCGTGCGVLVGTKDGRVVATQGDPDAPVNRGLNC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 80 PRGQGAPQTTYDPDRLKRPLIRV-EGSQRGEGKYRVATWEEALDHIAKKMLEIREKYGPEAIAFFGHGTGDYW----FVD 154
Cdd:PRK13532 83 IKGYFLSKIMYGKDRLTQPLLRMkDGKYDKEGEFTPVSWDQAFDVMAEKFKKALKEKGPTAVGMFGSGQWTIWegyaASK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 155 FLPAAWGSpNAAKPSVSLCTAPREVAsqwvFGRPIGGHEPI----DWENARYIVLIGHHIGEdTHN---TQLQDFALAlK 227
Cdd:PRK13532 163 LMKAGFRS-NNIDPNARHCMASAVVG----FMRTFGIDEPMgcydDIEAADAFVLWGSNMAE-MHPilwSRVTDRRLS-N 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 228 NGAKVVVVdprfSTAaakAHRW-----LPI--KPGTDTALLLAWIHVLIYEDLYDKEYVAKYTV---------------- 284
Cdd:PRK13532 236 PDVKVAVL----STF---EHRSfeladNGIifTPQTDLAILNYIANYIIQNNAVNWDFVNKHTNfrkgatdigyglrpth 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1886399248 285 ------------------GFEELKAHVKDFTPEWAEKHTEIPAQVIREVArEMAAHKPRAVL 328
Cdd:PRK13532 309 plekaaknpgtagksepiSFEEFKKFVAPYTLEKTAKMSGVPKEQLEQLA-KLYADPNRKVV 369
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
619-736 |
5.37e-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: 74.23 E-value: 5.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 619 YRLLYGRSPVHTFARTQNNWVLMEMDPENE-VWIHKEEAKRLGLKEGDYVMLVNQDGVKEGPVRVkpTARIRKDCVYIVH 697
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKPEPEvVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKV--TDRVRPGVVFMPF 78
|
90 100 110
....*....|....*....|....*....|....*....
gi 1886399248 698 GFGHKAplmrlahgRGASDNYLqTRYKLDPISGGAGLRV 736
Cdd:pfam01568 79 GWWYEP--------RGGNANAL-TDDATDPLSGGPEFKT 108
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
37-91 |
1.54e-14 |
|
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is found in a number of reductase/dehydrogenase families, which include the periplasmic nitrate reductase precursor and the formate dehydrogenase alpha chain.
Pssm-ID: 197994 [Multi-domain] Cd Length: 55 Bit Score: 68.43 E-value: 1.54e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1886399248 37 VKSVYQICEGCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRLCPRGQGAPQTTYD 91
Cdd:smart00926 1 EKWVPTVCPLCGVGCGLLVEVKDGRVVRVRGDPDHPVNRGRLCPKGRAGLEQVYS 55
|
|
| NarG |
COG5013 |
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and ... |
75-283 |
4.56e-14 |
|
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 444037 [Multi-domain] Cd Length: 1231 Bit Score: 76.40 E-value: 4.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 75 RGrlCPRGQGAPQTTYDPDRLKRPLIR-----------------VEG---------------SQRGEGKYRVATWEEALD 122
Cdd:COG5013 94 RG--CPRGASFSWYTYSPTRVKYPYVRgvllelwreararhgdpVEAwasivedpekrrrykSARGKGGFVRATWDEANE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 123 HIAKKMLEIREKYGPEAIAFFghgtgdywfvdflpaawgSPNAAKPSVSLCTAPR-------------------EVASQW 183
Cdd:COG5013 172 IIAAANVYTIKKYGPDRVAGF------------------SPIPAMSMVSYAAGARflsliggvmlsfydwyadlPPASPQ 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 184 VFGR----PigghEPIDWENARYIVLIGHHIGE----DTHNtqlqdFALALKNGAKVVVVDPRFSTAAAKAHRWLPIKPG 255
Cdd:COG5013 234 VWGEqtdvP----ESADWYNSGYLIMWGSNVPQtrtpDAHF-----MTEARYKGTKVVVVSPDYAENTKFADEWLPPKQG 304
|
250 260 270
....*....|....*....|....*....|....
gi 1886399248 256 TDTALLLAWIHVLIYEDLYDK------EYVAKYT 283
Cdd:COG5013 305 TDAALAMAMGHVILKEFHVDRqvpyftDYARRYT 338
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
75-702 |
1.39e-13 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 74.65 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 75 RGRLCPRGQGAPQTTYDPDRLKRPLIRVegSQRGEGKYRVATWEEALDHIAKK-----------MLEIRE---------- 133
Cdd:PRK14991 138 RSTACARGNAMLEQLDSPYRVLQPLKRV--GKRGSGKWQRISFEQLVEEVVEGgdlfgeghvdgLRAIRDldtpidaknp 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 134 KYGPEA----IAFFGHGTGDYWFVDFLPAAWGSPNAAKPSvSLCTAPREVASQWVFGR-PIGGHEPIDWENARYIVLIGH 208
Cdd:PRK14991 216 EYGPKAnqllVTNASDEGRDAFIKRFAFNSFGTRNFGNHG-SYCGLAYRAGSGALMGDlDKNPHVKPDWDNVEFALFIGT 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 209 HIGEDTHNTQLQDFALA---LKNGAKVVVVDPRF----STAAAKAHRWLPIKPGTDTALLLAWIHVLIYEDLYDKEYVAK 281
Cdd:PRK14991 295 SPAQSGNPFKRQARQLAnarTRGNFEYVVVAPALplssSLAAGDNNRWLPIRPGTDSALAMGMIRWIIDNQRYNADYLAQ 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 282 --------------------------------------YTVGFEELK-----------------AHVKDFTP-------- 298
Cdd:PRK14991 375 pgvaamqaageaswtnathlviadpghprygqflrasdLGLPFEGEArgdgedtlvvdaadgelVPATQAQParlfveqy 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 299 -------------------EWAEKHT--------EIPAQVIREVAREMAAHKPRAVLpPTRHNVWYGDDTYRVMALLYVN 351
Cdd:PRK14991 455 vtladgqrvrvksslqllkEAARKLSlaeyseqcGVPEAQIIALAEEFTSHGRKAAV-ISHGGTMSGNGFYNAWAIMMLN 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 352 VLLGNYGRPGGFYIaqspylekyplpplplepaaggcsgpSGGDHEPEGFKPRAD----------KGKFFARSTA----- 416
Cdd:PRK14991 534 ALIGNLNLKGGVVV--------------------------GGGKFPGFGDGPRYNlasfagkvkpKGVSLSRSKFpyeks 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 417 ---------------------------IQELIEPMITGEPYPIKGLFAYGINLFHSIPNV-PRTKEALKN---LDLYVAI 465
Cdd:PRK14991 588 seyrrkveagqspypakapwypfvaglLTEMLTAALEGYPYPLKAWINHMSNPIYGVPGLrAVIEEKLKDpkkLPLFISI 667
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 466 DVLPQEHVMWADVILPEATYLERYdDFVLVAHKTPF--IQLRTPAHEPLFD-TKPGWWIARE-----LGLRLGL------ 531
Cdd:PRK14991 668 DAFINETTALADYIVPDTHTYESW-GFTAPWGGVPTkaSTARWPVVEPRTAkTADGQPVCMEsfliaVAKRLQLpgfgdn 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 532 ---------------EQYF---------------PWKTIEEYLETRLQSLGLDL------ETMKGMGTLVQRG------- 568
Cdd:PRK14991 747 aikdaqgnthplnraEDFYlrgaaniaylgktpvADASDEDIALTGVSRILPALqatlkpDEVRRVAFIYARGgrfapae 826
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 569 KPWLEDWEKEG-RLPF-------GTA---------SGKIELYCQRFkeAGHQPLPVFTPPEEPPegfYRLLYGRSPVHTf 631
Cdd:PRK14991 827 SAYDEERMGNRwKKPLqiwnedvAAArhsmtgerySGCPTWYPPRL--ADGTPLREQFPESQWP---LLLISFKSNLMS- 900
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1886399248 632 ARTQNNWVLMEMDPENEVWIHKEEAKRLGLKEGDYVMLVNQDGVKEGPVRVKptARIRKDCVYIVHGFGHK 702
Cdd:PRK14991 901 SMSIASPRLRQVKPANPVALNPQDAARLGIQHGDRVRISTPGGSVVAQASVL--NGVMPGVIAIEHGYGHR 969
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
629-743 |
2.95e-13 |
|
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: 66.76 E-value: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 629 HTFARTQNNWVLMEMDPENEVWIHKEEAKRLGLKEGDYVMLVNQDGVKEGPVRVkpTARIRKDCVYIVHGFGHKAPlmrl 708
Cdd:cd00508 17 HTGTMTRRSPRLAALAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARV--TDRVRPGTVFMPFHWGGEVS---- 90
|
90 100 110
....*....|....*....|....*....|....*
gi 1886399248 709 ahgrGASDNYLqTRYKLDPISGGAGLRVNFVRLEK 743
Cdd:cd00508 91 ----GGAANAL-TNDALDPVSGQPEFKACAVRIEK 120
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
625-743 |
3.50e-13 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate reductase, subunit A, (TtrA); respiratory arsenate As(V) reductase, catalytic subunit (ArrA); and other related proteins.
Pssm-ID: 239181 [Multi-domain] Cd Length: 143 Bit Score: 67.32 E-value: 3.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 625 RSPVHTfARTQNNWVLMEMDPENEVWIHKEEAKRLGLKEGDYVMLVNQDGVKEGPVRVKPTarIRKDCVYIVHGFGHKAp 704
Cdd:cd02780 9 KSNLNS-HRSANAPWLKEIKPENPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEG--VRPGVVAIEHGYGHWA- 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1886399248 705 LMRLAHGR--------------------GASDNYLQTRYKLDPISGGAGLRVNFVRLEK 743
Cdd:cd02780 85 YGAVASTIdgkdlpgdawrgagvnindiGLVDPSRGGWSLVDWVGGAAARYDTPVKIEK 143
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
72-542 |
5.36e-13 |
|
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: 72.51 E-value: 5.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 72 PKSRGRLCPRGQGAPQTTYDPD------RLKRPLIRVEGSQRGegkyrvATWEEALDHIAKKMLEIREKYGPE-AIAF-- 142
Cdd:cd02756 89 PVNSGNYSTRGGTNAERIWSPDnrvgetRLTTPLVRRGGQLQP------TTWDDAIDLVARVIKGILDKDGNDdAVFAsr 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 143 FGHGTGDYWFVD------FLPAAWGSPNAA---KPSVSL-CTAPREVasqwvfGRPIGGHEPIDWENARYIVLIGHHIGE 212
Cdd:cd02756 163 FDHGGGGGGFENnwgvgkFFFMALQTPFVRihnRPAYNSeVHATREM------GVGELNNSYEDARLADTIVLWGNNPYE 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 213 DTHN-------TQLQDFALALKNGA----------KVVVVDPRFS-TAAAKAHRW-------LPIKPGTDTALLLAwIHV 267
Cdd:cd02756 237 TQTVyflnhwlPNLRGATVSEKQQWfppgepvppgRIIVVDPRRTeTVHAAEAAAgkdrvlhLQVNPGTDTALANA-IAR 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 268 LIYEDLydKEYVAKytvgfeelkahvkdftpewAEKHTEIPAQVIrEVAREMAA------HKPRAVLPPTRHNVWyGDDT 341
Cdd:cd02756 316 YIYESL--DEVLAE-------------------AEQITGVPRAQI-EKAADWIAkpkeggYRKRVMFEYEKGIIW-GNDN 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 342 YR-VMALLYVNVLLGNYGRPGgfyiaqspylekyplpplplepaaGGCsGPSGGDHEPEGFKPRADKGKFFARSTAI--- 417
Cdd:cd02756 373 YRpIYSLVNLAIITGNIGRPG------------------------TGC-VRQGGHQEGYVRPPPPPPPWYPQYQYAPyid 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 418 QELIEP------MITGEPY---PIKGLFAYGIN---------LFHSIPNVPRTKEALKNLDL---------YVAIDVLPQ 470
Cdd:cd02756 428 QLLISGkgkvlwVIGCDPYkttPNAQRLRETINhrsklvtdaVEAALYAGTYDREAMVCLIGdaiqpgglfIVVQDIYPT 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 471 EHVMWADVILPEATYLERYDDFVLVAHKTpfIQLRTPAHEPLFDTKPGWWIARELGLRL----------GLEQY----FP 536
Cdd:cd02756 508 KLAEDAHVILPAAANGEMNETSMNGHERR--LRLYEKFMDPPGEAMPDWWIAAMIANRIyelyqeegkgGSAQYqffgFI 585
|
....*.
gi 1886399248 537 WKTIEE 542
Cdd:cd02756 586 WKTEED 591
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
31-259 |
1.66e-11 |
|
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440657 [Multi-domain] Cd Length: 453 Bit Score: 67.17 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 31 PWYAQEVKSvyqICEGCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRLCPRGQGAPQTTYDPDRLKRPLIRvegsqrGEG 110
Cdd:COG1034 212 PWELKKTPS---ICPHCSVGCNIRVDVRGGKVYRVLPRENEAVNEEWLCDKGRFGYDGLNSPDRLTRPLVR------KDG 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 111 KYRVATWEEALDHIAKKMLEIREKYGPEAIAFFGhgtgdywfvdflpaawGSPNAAKpsvslctAPREVASQWVFGRPIG 190
Cdd:COG1034 283 ELVEASWEEALAAAAEGLKALKKAENSVGAALLG----------------ALPDAAA-------ILEAAEAGKLKALVLL 339
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1886399248 191 GHEPIDWENARyivlighhigedthntqlqdFALALKNGAKVVVVDPRFSTAAAKAHRWLPIKPGTDTA 259
Cdd:COG1034 340 GADPYDLDPAA--------------------ALAALAKADFVVVLDHFGSATAERADVVLPAAAFAEKS 388
|
|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
38-91 |
7.27e-11 |
|
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: 58.07 E-value: 7.27e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1886399248 38 KSVYQICEGCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRLCPRGQGAPQTTYD 91
Cdd:pfam04879 2 KVVKTICPYCGVGCGLEVHVKDGKIVKVEGDPDHPVNEGRLCVKGRFGYERVYN 55
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
629-743 |
2.23e-10 |
|
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: 58.40 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 629 HTFARTQNNWVLMEMDPENEVWIHKEEAKRLGLKEGDYVMLVNQDGVKEGPVRVkpTARIRKDCVYIvhgfghkaPLmrl 708
Cdd:cd02790 17 HTGTMTRRAEGLDAIAPEEYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARV--TDRVPEGVVFM--------PF--- 83
|
90 100 110
....*....|....*....|....*....|....*
gi 1886399248 709 aHGRGASDNYLqTRYKLDPISGGAGLRVNFVRLEK 743
Cdd:cd02790 84 -HFAEAAANLL-TNAALDPVAKIPEFKVCAVRVEK 116
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
417-545 |
3.54e-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: 3.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 417 IQELIEPMITGepyPIKGLFAYGINLFHSIPNvpRTKEALKNLDLYVAIDVLPQEHVMWADVILPEATYLERYDDFVLVA 496
Cdd:COG1034 321 AAAILEAAEAG---KLKALVLLGADPYDLDPA--AALAALAKADFVVVLDHFGSATAERADVVLPAAAFAEKSGTFVNLE 395
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1886399248 497 HKtpfIQLRTPAHEPLFDTKPGWWIARELGLRLGLEqyFPWKTIEEYLE 545
Cdd:COG1034 396 GR---VQRFNAAVPPPGEARPDWRVLRALANALGAG--LPYDSLEEVRA 439
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
632-744 |
7.33e-09 |
|
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: 54.71 E-value: 7.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 632 ARTQNNWV-----LMEMDPENEVWIHKEEAKRLGLKEGDYVMLVNQDGVKEGPVRVKPTarIRKDCVYIVHGFGHKAPLM 706
Cdd:cd02782 13 LRSNNSWLhndprLVKGRNRCTLRIHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDD--MMPGVVSLPHGWGHDYPGV 90
|
90 100 110
....*....|....*....|....*....|....*....
gi 1886399248 707 RLAHGR-GASDNYLQTRYKLDPISGGAGLRVNFVRLEKA 744
Cdd:cd02782 91 SGAGSRpGVNVNDLTDDTQRDPLSGNAAHNGVPVRLARV 129
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
629-743 |
1.42e-08 |
|
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: 53.45 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 629 HTFARTQ----NNWVLMEMDPeNEVWIHKEEAKRLGLKEGDYVMLVNQDGVKEGPVRVkpTARIRKDCVYIVHGFGHKAp 704
Cdd:cd02794 9 HYKRRTHstfdNVPWLREAFP-QEVWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKV--TERIMPGVVALPQGAWYEP- 84
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1886399248 705 lmrLAHG--RGASDNYLqTRYKLDPISGGAGLRVNFVRLEK 743
Cdd:cd02794 85 ---DANGidKGGCINTL-TGLRPSPLAKGNPQHTNLVQVEK 121
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
629-743 |
2.69e-08 |
|
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: 52.61 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 629 HTFARTQNNWVLMEMDPENEVWIHKEEAKRLGLKEGDYVMLVNqdgvKEGPVRVKP--TARIRKDCVYIVHGFGHKAPlm 706
Cdd:cd02792 17 HGGNMTRNSPYLAELQPEMFVEISPELAAERGIKNGDMVWVSS----PRGKIKVKAlvTDRVKPHEVGIPYHWGGMGL-- 90
|
90 100 110
....*....|....*....|....*....|....*..
gi 1886399248 707 rlahGRGASDNYLqTRYKLDPISGGAGLRVNFVRLEK 743
Cdd:cd02792 91 ----VIGDSANTL-TPYVGDPNTQTPEYKAFLVNIEK 122
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
618-735 |
3.22e-07 |
|
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: 50.00 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 618 FYRLLYGRSPVHTfaRTQNNWV--LMEMDPENEVWIHKEEAKRLGLKEGDYVMLVNQDGvkegpvRVKPTAR----IRKD 691
Cdd:cd02781 4 LILTTGARSYYYF--HSEHRQLpsLRELHPDPVAEINPETAAKLGIADGDWVWVETPRG------RARQKARltpgIRPG 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1886399248 692 CVYIVHG--FGHKAPLMRLAHGRGASD-NYLQTRYKLDPISGGAGLR 735
Cdd:cd02781 76 VVRAEHGwwYPEREAGEPALGGVWESNaNALTSDDWNDPVSGSSPLR 122
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
90-320 |
4.70e-07 |
|
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1), found in beta- and gammaproteobacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239173 [Multi-domain] Cd Length: 414 Bit Score: 52.74 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 90 YDPDRLKRPLIRVEGsqrgegKYRVATWEEALDHIAKKMLEIREKYGPEAIAFFGHGTG---DYWFVDFLPAAWGSPN-- 164
Cdd:cd02772 50 NSEDRLTKPMIKKDG------QWQEVDWETALEYVAEGLSAIIKKHGADQIGALASPHStleELYLLQKLARGLGSDNid 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 165 ------AAKPSVSLCTAPrevasqWvFGRPIGghepiDWENARYIVLIGHHIGEDtH---NTQLQDfalALKNGAKVVVV 235
Cdd:cd02772 124 hrlrqsDFRDDAKASGAP------W-LGMPIA-----EISELDRVLVIGSNLRKE-HpllAQRLRQ---AVKKGAKLSAI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 236 -----DPRFS---TAAAKAHRWLPIKpgTDTALLLAWIHVLIYEDLYDK-EYVAKYTVGFEELKAH--VKDFTPEWAEKH 304
Cdd:cd02772 188 npaddDFLFPlsgKAIVAPSALANAL--AQVAKALAEEKGLAVPDEDAKvEASEEARKIAASLVSAerAAVFLGNLAQNH 265
|
250
....*....|....*.
gi 1886399248 305 TEipAQVIREVAREMA 320
Cdd:cd02772 266 PQ--AATLRALAQEIA 279
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
629-744 |
5.14e-06 |
|
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: 46.41 E-value: 5.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 629 HTFARTQNNWVLMEMDPENEVWIHKEEAKRLGLKEGDYVMLVNQDGVKEGPVRVkpTARIRKDCVYIVHGFGHkaplmrl 708
Cdd:cd02791 17 HTMTRTGRVPRLNAHVPEPYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRV--TDRVRPGEVFVPMHWGD------- 87
|
90 100 110
....*....|....*....|....*....|....*.
gi 1886399248 709 AHGRGASDNYLqTRYKLDPISGGAGLRVNFVRLEKA 744
Cdd:cd02791 88 QFGRSGRVNAL-TLDATDPVSGQPEFKHCAVRIEKV 122
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|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
43-240 |
9.78e-06 |
|
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: 48.43 E-value: 9.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 43 ICEGCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRLCPRGQGAPQTTYDPDRLKRPLIRvegsqrGEGKYRVATWEEALD 122
Cdd:cd02768 3 IDVHDALGSNIRVDVRGGEVMRILPRENEAINEEWISDKGRFGYDGLNSRQRLTQPLIK------KGGKLVPVSWEEALK 76
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 123 HIAKKMLEIRekygPEAIAFFGHGTGD----YWFVDFLpAAWGSPN----AAKPSVSLCTAPRevaSQWVFGRPIGGhep 194
Cdd:cd02768 77 TVAEGLKAVK----GDKIGGIAGPRADleslFLLKKLL-NKLGSNNidhrLRQSDLPADNRLR---GNYLFNTSIAE--- 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1886399248 195 IdwENARYIVLIGHHIgEDTH---NTQLQDfaLALKNGAKVVVVDPRFS 240
Cdd:cd02768 146 I--EEADAVLLIGSNL-RKEApllNARLRK--AVKKKGAKIAVIGPKDT 189
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| 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 ... |
43-136 |
1.10e-05 |
|
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: 48.54 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 43 ICEGCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRLCPRGQGAPQTTYDPDRLKRPLIrvegsqRGEGKYRVATWEEALD 122
Cdd:cd02771 3 ICHHCSVGCNISLGERYGELRRVENRYNGAVNHYFLCDRGRFGYGYVNSRDRLTQPLI------RRGGTLVPVSWNEALD 76
|
90
....*....|....
gi 1886399248 123 HIAKKMLEIREKYG 136
Cdd:cd02771 77 VAAARLKEAKDKVG 90
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
619-674 |
2.87e-04 |
|
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239186 [Multi-domain] Cd Length: 124 Bit Score: 41.20 E-value: 2.87e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1886399248 619 YRLLY----GRSPVH-TFArtqNNWVLMEMDPENEVWIHKEEAKRLGLKEGDYVMLVNQDG 674
Cdd:cd02785 2 YPLACiqrhSRFRVHsQFS---NVPWLLELQPEPRVKINPIDAAARGIAHGDLVEVYNDRG 59
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|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
647-698 |
5.79e-04 |
|
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: 40.65 E-value: 5.79e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1886399248 647 NEVWIHKEEAKRLGLKEGDYVMLVNQDGVKEGPVRVkpTARIRKDCVYIVHG 698
Cdd:cd02777 34 EPVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARV--TDRIMPGVVALPEG 83
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|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
94-261 |
9.47e-04 |
|
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone oxidoreductase/respiratory complex I/NADH dehydrogenase-1(NDH-1) of eukaryotes and the Nqo3/G subunit of alphaproteobacteria NDH-1. The NADH-quinone oxidoreductase is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The nad11 gene codes for the largest (75 kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Paracoccus denitrificans, this subunit is encoded by the nqo3 gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The Nad11/Nqo3 subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239174 [Multi-domain] Cd Length: 375 Bit Score: 42.25 E-value: 9.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 94 RLKRPLIRvegsqrGEGKYRVATWEEALDHIAKKmleIREKYGPE--AIAffghgtGDywFVDF--------LPAAWGSP 163
Cdd:cd02773 53 RLDKPYIR------KNGKLKPATWEEALAAIAKA---LKGVKPDEiaAIA------GD--LADVesmvalkdLLNKLGSE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886399248 164 NAAKPSVSLcTAPREVASQWVFGRPIGGhepidWENARYIVLIGHHIGED--THNTQLQDFALAlkNGAKVVVVDPRFST 241
Cdd:cd02773 116 NLACEQDGP-DLPADLRSNYLFNTTIAG-----IEEADAVLLVGTNPRFEapVLNARIRKAWLH--GGLKVGVIGPPVDL 187
|
170 180
....*....|....*....|
gi 1886399248 242 AAAKAHRwlpikpGTDTALL 261
Cdd:cd02773 188 TYDYDHL------GTDAKTL 201
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|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
630-704 |
3.24e-03 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase (Arsenite-Ox) and related proteins. Arsenite oxidase oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin.
Pssm-ID: 239180 [Multi-domain] Cd Length: 115 Bit Score: 38.21 E-value: 3.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1886399248 630 TFARTQNNWVLMEMDPENEVWIHKEEAKRLGLKEGDYVMLVNQDGvkEGPVRVKPTARIRKDCVYIVhgFGHKAP 704
Cdd:cd02779 16 TAYHDQNNSEIAERVPLPYIEVNPEDAKREGLKNGDLVEVYNDYG--STTAMAYVTNTVKPGQTFML--MAHPRP 86
|
|
| MopB_CT_ydeP |
cd02787 |
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial ... |
649-682 |
7.30e-03 |
|
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239188 [Multi-domain] Cd Length: 112 Bit Score: 36.87 E-value: 7.30e-03
10 20 30
....*....|....*....|....*....|....
gi 1886399248 649 VWIHKEEAKRLGLKEGDYVMLVNQDGvkEGPVRV 682
Cdd:cd02787 33 VFMNPDDIARLGLKAGDRVDLESAFG--DGQGRI 64
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