|
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: 656.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 40 VYQICEGCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRVCPRGQGMPQTTYDPDRLKRPLIRVEgsQRGEGKYRVATWEE 119
Cdd:cd02755 1 VPSICEMCSSRCGILARVEDGRVVKIDGNPLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRVG--ERGEGKFREASWDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 120 ALDYVAKRMMKLKEEYGPEAIAFFGHGTGDSWFVDFLPAAWGSPNAAKPSvAICTAPRETAAQWVFgRPIGGHEPIDWEN 199
Cdd:cd02755 79 ALQYIASKLKEIKEQHGPESVLFGGHGGCYSPFFKHFAAAFGSPNIFSHE-STCLASKNLAWKLVI-DSFGGEVNPDFEN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 200 ARYIVLIGHHIGEDTHNTQLQDFALALKRGAKVVVVDPRFSTAAAKAHLWLPIKPGTDTALLLAWIHVLIYEDLYDKEYV 279
Cdd:cd02755 157 ARYIILFGRNLAEAIIVVDARRLMKALENGAKVVVVDPRFSELASKADEWIPIKPGTDLAFVLALIHVLISENLYDAAFV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 280 AKYTTGFEELKTHVKDFTPEWAEKHTEIPAEIIRQVAREMAAHKPQAVLPPTRHTVWYGDDTYRMMALYYVNVLLGNYGR 359
Cdd:cd02755 237 EKYTNGFELLKAHVKPYTPEWAAQITDIPADTIRRIAREFAAAAPHAVVDPGWRGTFYSNSFQTRRAIAIINALLGNIDK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 360 KGGFYIAQSPYlekyptpplplepaaggcsgpaggnhepegfkpradkgkffarttaiqeliepmitgePYPIKGLFAYG 439
Cdd:cd02755 317 RGGLYYAGSAK----------------------------------------------------------PYPIKALFIYR 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 440 INLFHSIPNVPRTKEALKKLDLYVAIDVLPQEHVMWADVILPEATYLERYDDLVAVAHKTPFIQLRVPAHEPLFDTKPGW 519
Cdd:cd02755 339 TNPFHSMPDRARLIKALKNLDLVVAIDILPSDTALYADVILPEATYLERDEPFSDKGGPAPAVATRQRAIEPLYDTRPGW 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 520 WIARELGIRLGLgeffpwqtieeyldtrlqsigfdletlkgmgtlvqkgkpwledwekegrlpFGTPSGKIELYCQAFKK 599
Cdd:cd02755 419 DILKELARRLGL---------------------------------------------------FGTPSGKIELYSPILAK 447
|
....*..
gi 2075248272 600 AGHQPLP 606
Cdd:cd02755 448 AGYDPLP 454
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
18-745 |
0e+00 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 628.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 18 ALRGSGPAKALKAPWYRQEVKSVYQICEGCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRVCPRGQGMPQTTYDPDRLKR 97
Cdd:COG0243 2 SLRDFKAAGAGAAALEAAGTKTVKTTCPGCGVGCGLGVKVEDGRVVRVRGDPDHPVNRGRLCAKGAALDERLYSPDRLTY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 98 PLIRVegSQRGEGKYRVATWEEALDYVAKRMMKLKEEYGPEAIAFFGHG-------TGDSWFVDFLPAAWGSPNAAKPSv 170
Cdd:COG0243 82 PMKRV--GPRGSGKFERISWDEALDLIAEKLKAIIDEYGPEAVAFYTSGgsagrlsNEAAYLAQRFARALGTNNLDDNS- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 171 AICTAPRETAAQWVFGRPIGGHEPIDWENARYIVLIGHHIGEdTHNTQLQDF-ALALKRGAKVVVVDPRFSTAAAKAHLW 249
Cdd:COG0243 159 RLCHESAVAGLPRTFGSDKGTVSYEDLEHADLIVLWGSNPAE-NHPRLLRRLrEAAKKRGAKIVVIDPRRTETAAIADEW 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 250 LPIKPGTDTALLLAWIHVLIYEDLYDKEYVAKYTTGFEELKTHVKDFTPEWAEKHTEIPAEIIRQVAREMAAHKPQAVLP 329
Cdd:COG0243 238 LPIRPGTDAALLLALAHVLIEEGLYDRDFLARHTVGFDELAAYVAAYTPEWAAEITGVPAEDIRELAREFATAKPAVILW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 330 ---PTRHTvwYGDDTYRMMALyyVNVLLGNYGRKGGFYiaqspylekyptpplplepaaggCSGPAggnhepegfkprad 406
Cdd:COG0243 318 gmgLQQHS--NGTQTVRAIAN--LALLTGNIGKPGGGP-----------------------FSLTG-------------- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 407 kgkffarttaiqeliEPMITGEPYPIKGLFAYGINLFHSIPNVPRTKEALKKLDLYVAIDVLPQEHVMWADVILPEATYL 486
Cdd:COG0243 357 ---------------EAILDGKPYPIKALWVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARYADIVLPATTWL 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 487 ERYDDLVAVAHktPFIQLRVPAHEPLFDTKPGWWIARELGIRLGLGEFFPWQ-TIEEYLDTRLQS---IGFDLETLKGMG 562
Cdd:COG0243 422 ERDDIVTNSED--RRVHLSRPAVEPPGEARSDWEIFAELAKRLGFEEAFPWGrTEEDYLRELLEAtrgRGITFEELREKG 499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 563 TL---VQKGKPWLEDWekegrlPFGTPSGKIELYCQAFKkagHQPLPVFTPPEEPPP-----GFYRLLYGRSPVHTFART 634
Cdd:COG0243 500 PVqlpVPPEPAFRNDG------PFPTPSGKAEFYSETLA---LPPLPRYAPPYEGAEpldaeYPLRLITGRSRDQWHSTT 570
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 635 QNNWVLMEMDPENEVWIHREEARRLGLKDGDYVILENQNGVREGPVRVkaTERIRKDCVYLVHGFGHKAplmkvAHGRGA 714
Cdd:COG0243 571 YNNPRLREIGPRPVVEINPEDAAALGIKDGDLVRVESDRGEVLARAKV--TEGIRPGVVFAPHGWWYEP-----ADDKGG 643
|
730 740 750
....*....|....*....|....*....|.
gi 2075248272 715 SDNYLqTRYKLDPISGGAGLRVNFVKLEKAE 745
Cdd:COG0243 644 NVNVL-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: 559.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 1 MQRREFLK----------LSTLAAGALALRGSGPAKAlkapwyrqEVKSVYQICEGCFWRCGIVAHAVGNRVYKVEGYEA 70
Cdd:PRK15488 3 LSRRDFLKgagagcaacaLGSLLPGALAANEIAQLKG--------KTKLTPSICEMCSTRCPIEARVVNGKNVFIQGNPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 71 NPKSRGRVCPRGQGMPQTTYDPDRLKRPLIRVegSQRGEGKYRVATWEEALDYVAKRMMKLKEEYGPEAIAFFGH-GTGD 149
Cdd:PRK15488 75 AKSFGTKVCARGGSGHSLLYDPQRIVKPLKRV--GERGEGKWQEISWDEAYQEIAAKLNAIKQQHGPESVAFSSKsGSLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 150 SWFVDFlPAAWGSPNAAKpSVAICTAPRETAAQWVFGRPIGghepIDWENARYIVLIGHHIGE-----DTHntQLQDFAL 224
Cdd:PRK15488 153 SHLFHL-ATAFGSPNTFT-HASTCPAGYAIAAKVMFGGKLK----RDLANSKYIINFGHNLYEginmsDTR--GLMTAQM 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 225 alKRGAKVVVVDPRFSTAAAKAHLWLPIKPGTDTALLLAWIHVLIYEDLYDKEYVAKYTTGFEELKTHVKDFTPEWAEKH 304
Cdd:PRK15488 225 --EKGAKLVVFEPRFSVVASKADEWHAIRPGTDLAVVLALCHVLIEENLYDKAFVERYTSGFEELAASVKEYTPEWAEAI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 305 TEIPAEIIRQVAREMAAHKPQAVLPPTrHTVWYGDDTYRMM-ALYYVNVLLGNYGRKGGFYIAQSPylEKYPTpplplep 383
Cdd:PRK15488 303 SDVPADDIRRIARELAAAAPHAIVDFG-HRATFTPEEFDMRrAIFAANVLLGNIERKGGLYFGKNA--SVYNK------- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 384 AAGGCSGPAGGNHEPEGFK----PRAD----KGKFFARTTAI-QELIEPMITGEPYPIKGLFAYGINLFHSIPNVPRTKE 454
Cdd:PRK15488 373 LAGEKVAPTLAKPGVKGMPkptaKRIDlvgeQFKYIAAGGGVvQSIIDATLTQKPYQIKGWVMSRHNPMQTVTDRADVVK 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 455 ALKKLDLYVAIDVLPQEHVMWADVILPEATYLERYDDLVAVAHKTPFIQLRVPAHEPLFDTKPGWWIARELGIRLGLGEF 534
Cdd:PRK15488 453 ALKKLDLVVVCDVYLSESAAYADVVLPESTYLERDEEISDKSGKNPAYALRQRVVEPIGDTKPSWQIFKELGEKMGLGQY 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 535 FPWQTIEEYldtRLQSIGFD---LETLKGMGtLVQKGKPWL---------------------EDWEKEGRLPFGTPSGKI 590
Cdd:PRK15488 533 YPWQDMETL---QLYQVNGDhalLKELKKKG-YVSFGVPLLlrepkmvakfvarypnakavdEDGTYGSQLKFKTPSGKI 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 591 ELYCQAFKKA-------GHQPLPVFTPPEepppgfYRLLYGRSPVHTFARTQNNWVLMEMDPENEVWIHREEARRLGLKD 663
Cdd:PRK15488 609 ELFSAKLEALapgygvpRYRDVALKKEDE------LYFIQGKVAVHTNGATQNVPLLANLMSDNAVWIHPQTAGKLGIKN 682
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 664 GDYVILENQNGVREGPVRVkaTERIRKDCVYLVHGFGHKAPLMKVAHGRGASDNYLqtrykLDPISG---GAGLRVNFVK 740
Cdd:PRK15488 683 GDEIRLENSVGKEKGKALV--TPGIRPDTLFAYMGFGSKNKELTRATGKGIHCGNL-----LPHVTSpvsGTNVHTTGVT 755
|
....
gi 2075248272 741 LEKA 744
Cdd:PRK15488 756 LSKA 759
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
44-611 |
1.09e-116 |
|
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: 360.47 E-value: 1.09e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 44 CEGCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRVCPRGQGMPQTTYDPDRLKRPLIRVegSQRGEGKYRVATWEEALDY 123
Cdd:cd02759 4 CPGCHSGCGVLVYVKDGKLVKVEGDPNHPTNKGRLCMRGLAAPEIVYHPDRLLYPLKRV--GERGENKWERISWDEALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 124 VAKRMMKLKEEYGPEAIAF-FGHGTGDSWFVDFLPAAW----GSPNAAKpSVAICTAPRETAAQWVFGRPIGGHEPiDWE 198
Cdd:cd02759 82 IAEKLAEIKAEYGPESIATaVGTGRGTMWQDSLFWIRFvrlfGSPNLFL-SGESCYWPRDMAHALTTGFGLGYDEP-DWE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 199 NARYIVLIGHHIGEDTHNTQLQDFALALKRGAKVVVVDPRFSTAAAKAHLWLPIKPGTDTALLLAWIHVLIYEDLYDKEY 278
Cdd:cd02759 160 NPECIVLWGKNPLNSNLDLQGHWLVAAMKRGAKLIVVDPRLTWLAARADLWLPIRPGTDAALALGMLNVIINEGLYDKDF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 279 VAKYTTGFEELKTHVKDFTPEWAEKHTEIPAEIIRQVAREMAAHKPQAVlpptrhtVWYG--DDTYRMM----ALYYVNV 352
Cdd:cd02759 240 VENWCYGFEELAERVQEYTPEKVAEITGVPAEKIRKAARLYATAKPACI-------QWGLaiDQQKNGTqtsrAIAILRA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 353 LLGNYGRKGGfyiaqspylekyptpplplepaaggcsgpaggnhepegfkpradkgkffarttaiqeliepmITGEPYPI 432
Cdd:cd02759 313 ITGNLDVPGG--------------------------------------------------------------NLLIPYPV 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 433 KGLFAYGINLFHSIPNVPRTKEALKKLDLYVAIDVLPQEHVMWADVILPEATYLERyDDLVAVAHKTPFIQLRVPAHEPL 512
Cdd:cd02759 331 KMLIVFGTNPLASYADTAPVLEALKALDFIVVVDLFMTPTAMLADIVLPVAMSLER-PGLRGGFEAENFVQLRQKAVEPY 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 513 FDTKPGWWIARELGIRLGLGEFfpwqTIEEYLDtrlqsigfdletlkgmGTLVQKGKPwledwekegrlPFGTPSGKIEL 592
Cdd:cd02759 410 GEAKSDYEIVLELGKRLGPEEA----EYYKYEK----------------GLLRPDGQP-----------GFNTPTGKVEL 458
|
570
....*....|....*....
gi 2075248272 593 YCQAFKKAGHQPLPVFTPP 611
Cdd:cd02759 459 YSTMLEELGYDPLPYYREP 477
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
51-745 |
1.64e-108 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 346.10 E-value: 1.64e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 51 CGIVAHAVGNRVYKVEGYEANPKSRGRVCPRGQGMPQTTYDPDRLKRPLIRvegsqrGEGKYRVATWEEALDYVAKRMMK 130
Cdd:COG3383 18 CGIDLEVKDGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVNSPDRLTTPLIR------RGGEFREVSWDEALDLVAERLRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 131 LKEEYGPEAIAFFGHGTG---DSW-FVDFLPAAWGSPN---AAKpsvaICTAPRETAAQWVFGrpIGGHE-PI-DWENAR 201
Cdd:COG3383 92 IQAEHGPDAVAFYGSGQLtneENYlLQKLARGVLGTNNidnNAR----LCMASAVAGLKQSFG--SDAPPnSYdDIEEAD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 202 YIVLIGHHIGEdTH---NTQLQDfalALKRGAKVVVVDPRFSTAAAKAHLWLPIKPGTDTALLLAWIHVLIYEDLYDKEY 278
Cdd:COG3383 166 VILVIGSNPAE-AHpvlARRIKK---AKKNGAKLIVVDPRRTETARLADLHLQIKPGTDLALLNGLLHVIIEEGLVDEDF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 279 VAKYTTGFEELKTHVKDFTPEWAEKHTEIPAEIIRQVAREMAAHKPQAVL---PPTRHTVwyGDDTyrMMALYYVNVLLG 355
Cdd:COG3383 242 IAERTEGFEELKASVAKYTPERVAEITGVPAEDIREAARLIAEAKRAMILwgmGVNQHTQ--GTDN--VNAIINLALATG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 356 NYGRKGgfyiaqspylekypTPPLPLEP---AAGGCSGPAGGNHEPeGFKPRADKG--KFFART-----------TAIQE 419
Cdd:COG3383 318 NIGRPG--------------TGPFPLTGqnnVQGGRDMGALPNVLP-GYRDVTDPEhrAKVADAwgvpplpdkpgLTAVE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 420 LIEPMITGEpypIKGLFAYGINLFHSIPNVPRTKEALKKLDLYVAIDVLPQEHVMWADVILPEATYLE----------Ry 489
Cdd:COG3383 383 MFDAIADGE---IKALWIIGENPAVSDPDANHVREALEKLEFLVVQDIFLTETAEYADVVLPAASWAEkdgtftnterR- 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 490 ddlvavahktpfIQLRVPAHEPLFDTKPGWWIARELGIRLGLGefFPWQTIEEYLD--TRLQSI--GFDLETLKGMGTlV 565
Cdd:COG3383 459 ------------VQRVRKAVEPPGEARPDWEIIAELARRLGYG--FDYDSPEEVFDeiARLTPDysGISYERLEALGG-V 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 566 QKGKPWlEDWEKEGRL---PFGTPSGKIELYcqafkkaghqPLPVFTPPEEPPPGF-YRLLYGRSPV--HTFARTQNNWV 639
Cdd:COG3383 524 QWPCPS-EDHPGTPRLftgRFPTPDGKARFV----------PVEYRPPAELPDEEYpLVLTTGRLLDqwHTGTRTRRSPR 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 640 LMEMDPENEVWIHREEARRLGLKDGDYVILENQNGvrEGPVRVKATERIRKDCVYLvhgfghkaPlmkvAHGRGASDNYL 719
Cdd:COG3383 593 LNKHAPEPFVEIHPEDAARLGIKDGDLVRVSSRRG--EVVLRARVTDRVRPGTVFM--------P----FHWGEGAANAL 658
|
730 740
....*....|....*....|....*.
gi 2075248272 720 qTRYKLDPISGGAGLRVNFVKLEKAE 745
Cdd:COG3383 659 -TNDALDPVSKQPEYKACAVRVEKVA 683
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
43-529 |
3.80e-100 |
|
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: 313.88 E-value: 3.80e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 43 ICEGCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRVCPRGQGMPQTTYDPDRLKRPLIRVEGSqrgeGKYRVATWEEALD 122
Cdd:cd00368 3 VCPFCGVGCGILVYVKDGKVVRIEGDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGGR----GKFVPISWDEALD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 123 YVAKRMMKLKEEYGPEAIAFFGHGTGD---SWFVDFLPAAWGSPNAAkPSVAICTAPRETAAQWvFGRPIGGHEPIDWEN 199
Cdd:cd00368 79 EIAEKLKEIREKYGPDAIAFYGGGGASneeAYLLQKLLRALGSNNVD-SHARLCHASAVAALKA-FGGGAPTNTLADIEN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 200 ARYIVLIGHHIGEdTHNTQLQDFALALKRGAKVVVVDPRFSTAAAKAHLWLPIKPGTDTALLLAwihvliyedlydkeyv 279
Cdd:cd00368 157 ADLILLWGSNPAE-THPVLAARLRRAKKRGAKLIVIDPRRTETAAKADEWLPIRPGTDAALALA---------------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 280 akyttgfeelkthvkdftpEWAEKHTEIPAEIIRQVAREMAAHKPQAVL---PPTRHTvwYGDDTYRMMALyyVNVLLGN 356
Cdd:cd00368 220 -------------------EWAAEITGVPAETIRALAREFAAAKRAVILwgmGLTQHT--NGTQNVRAIAN--LAALTGN 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 357 YGRKGgfyiaqspylekyptpplplepaaggcsgpaggnhepegfkpradkgkffarttaiqeliepmitgepypikGLF 436
Cdd:cd00368 277 IGRPG------------------------------------------------------------------------GGL 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 437 AYGINLFHSIPNVPRTKEALKKLDLYVAIDVLPQEHVMWADVILPEATYLERYDDLVavaHKTPFIQLRVPAHEPLFDTK 516
Cdd:cd00368 285 GPGGNPLVSAPDANRVRAALKKLDFVVVIDIFMTETAAYADVVLPAATYLEKEGTYT---NTEGRVQLFRQAVEPPGEAR 361
|
490
....*....|...
gi 2075248272 517 PGWWIARELGIRL 529
Cdd:cd00368 362 SDWEILRELAKRL 374
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
43-741 |
1.88e-99 |
|
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: 321.72 E-value: 1.88e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 43 ICEGCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRVCPRGQGMPQTTYDPDRLKRPLIRVEGsqrgegKYRVATWEEALD 122
Cdd:TIGR01591 2 VCPYCGVGCSLNLVVKDGKIVRVEPYQGHKANRGHLCVKGYFAWEFINSKDRLTTPLIREGD------KFREVSWDEAIS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 123 YVAKRMMKLKEEYGPEAIAFFG--HGTGDSWFV--DFLPAAWGSpNAAKPSVAICTAPRETAAQWVFGRPIGGHEPIDWE 198
Cdd:TIGR01591 76 YIAEKLKEIKEKYGPDSIGFIGssRGTNEENYLlqKLARAVIGT-NNVDNCARVCHGPSVAGLKQTVGIGAMSNTISEIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 199 NARYIVLIGHHIGEdTHNTQLQDFALALKRGAKVVVVDPRFSTAAAKAHLWLPIKPGTDTALLLAWIHVLIYEDLYDKEY 278
Cdd:TIGR01591 155 NADLIVIIGYNPAE-SHPVVAQYLKNAKRNGAKIIVIDPRKTETAKIADLHIPLKPGTDIALLNAMANVIIEEGLYDKAF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 279 VAKYTTGFEELKTHVKDFTPEWAEKHTEIPAEIIRQVAREMAAHKPQAV---LPPTRHTvwYGDDTyrMMALYYVNVLLG 355
Cdd:TIGR01591 234 IEKRTEGFEEFREIVKGYTPEYVEDITGVPADLIREAARMYAKAGSAAIlwgMGVTQHS--QGVET--VMALINLAMLTG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 356 NYGRKGGfyiaqspylekyptpplPLEPAAG-----GCSGPAGGNHEPEGFKPRADKG--KFFART-----------TAI 417
Cdd:TIGR01591 310 NIGKPGG-----------------GVNPLRGqnnvqGACDMGALPDFLPGYQPVSDEEvrEKFAKAwgvvklpaepgLRI 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 418 QELIEPMITGEpypIKGLFAYGINLFHSIPNVPRTKEALKKLDLYVAIDVLPQEHVMWADVILPEATYLERyDDLVAVAH 497
Cdd:TIGR01591 373 PEMIDAAADGD---VKALYIMGEDPLQSDPNTSKVRKALEKLELLVVQDIFMTETAKYADVVLPAAAWLEK-EGTFTNAE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 498 KTpfIQLRVPAHEPLFDTKPGWWIARELGIRLGLGEFF--PWQTIEEYLDTRLQSIGFDLETLKGMGTLvqKGKPWLEDW 575
Cdd:TIGR01591 449 RR--IQRFFKAVEPKGESKPDWEIIQELANALGLDWNYnhPQEIMDEIRELTPLFAGLTYERLDELGSL--QWPCNDSDA 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 576 EKEGRL---PFGTPSGKIELYcqafkkaghqPLPVFTPPEEPPPGF-YRLLYGR--SPVHTFARTQNNWVLMEMDPENEV 649
Cdd:TIGR01591 525 SPTSYLykdKFATPDGKAKFI----------PLEWVAPIEEPDDEYpLILTTGRvlTHYNVGEMTRRVAGLRRLSPEPYV 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 650 WIHREEARRLGLKDGDYVILENQNGvrEGPVRVKATERIRKDCVYlvhgfghkAPLmkvaHGRGASDNYLQTRYkLDPIS 729
Cdd:TIGR01591 595 EINTEDAKKLGIKDGDLVKVKSRRG--EITLRAKVSDRVNKGAIY--------ITM----HFWDGAVNNLTTDD-LDPIS 659
|
730
....*....|..
gi 2075248272 730 GGAGLRVNFVKL 741
Cdd:TIGR01591 660 GTPEYKYTAVRI 671
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
47-606 |
8.43e-93 |
|
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: 299.16 E-value: 8.43e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 47 CFWRCGIVAHAVGNRVYKVEGYEANPKSRGRVCPRGQGMPQTTYDPDRLKRPLIRVEgsqRGEGKYRVATWEEALDYVAK 126
Cdd:cd02766 8 CPDTCSLLVTVEDGRIVRVEGDPAHPYTRGFICAKGARYVERVYSPDRLLTPLKRVG---RKGGQWERISWDEALDTIAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 127 RMMKLKEEYGPEAIA------FFGHGTGDSwfVDFLPAAWGSPNAAKPsvaICTAPRETAAQWVFGRpIGGHEPIDWENA 200
Cdd:cd02766 85 KLKEIKAEYGPESILpysyagTMGLLQRAA--RGRFFHALGASELRGT---ICSGAGIEAQKYDFGA-SLGNDPEDMVNA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 201 RYIVLIGhhigEDTHNTQLQDFAL---ALKRGAKVVVVDPRFSTAAAKAHLWLPIKPGTDTALLLAWIHVLIYEDLYDKE 277
Cdd:cd02766 159 DLIVIWG----INPAATNIHLMRIiqeARKRGAKVVVIDPYRTATAARADLHIQIRPGTDGALALGVAKVLFREGLYDRD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 278 YVAKYTTGFEELKTHVKDFTPEWAEKHTEIPAEIIRQVAREMAAHKPQAV---LPPTRHTvwYGDDTYRMMALyyVNVLL 354
Cdd:cd02766 235 FLARHTEGFEELKAHLETYTPEWAAEITGVSAEEIEELARLYGEAKPPSIrlgYGMQRYR--NGGQNVRAIDA--LPALT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 355 GNYGRKGG--FYiaqspylekyptpplplepaaggcsgpagGNHEPegfkpradkgkffarttaiqeliepmitgepyPI 432
Cdd:cd02766 311 GNIGVPGGgaFY-----------------------------SNSGP--------------------------------PV 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 433 KGLFAYGINLFHSIPNVPRTKEAL-KKLDLYVAIDVLPQEHVMWADVILPEATYLERYDDLVAVAHktPFIQLRVPAHEP 511
Cdd:cd02766 330 KALWVYNSNPVAQAPDSNKVRKGLaREDLFVVVHDQFMTDTARYADIVLPATTFLEHEDVYASYWH--YYLQYNEPAIPP 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 512 LFDTKPGWWIARELGIRLGLGEFF----PWQTIEEYLD-TRLQSIGFDLETLKGMGTLVQKGKPWledwekEGRLpFGTP 586
Cdd:cd02766 408 PGEARSNTEIFRELAKRLGFGEPPfeesDEEWLDQALDgTGLPLEGIDLERLLGPRKAGFPLVAW------EDRG-FPTP 480
|
570 580
....*....|....*....|
gi 2075248272 587 SGKIELYCQAFKKAGHQPLP 606
Cdd:cd02766 481 SGKFEFYSERAAKRGLPPLP 500
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
43-604 |
5.64e-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: 294.73 E-value: 5.64e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 43 ICEGCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRVCPRGQGMPQTTYDPDRLKRPLIRV--EGSQRGEGKYRVATWEEA 120
Cdd:cd02757 5 TCQGCTAWCGLQAYVEDGRVTKVEGNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRTnpRKGRDVDPKFVPISWDEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 121 LDYVAKRMMKLKEEYGPEAIAFF-GHGTGD-SWFVDFLPAAWGSPNAAKPSvAICTAPRETAAQWVFGRPigGHEPIDWE 198
Cdd:cd02757 85 LDTIADKIRALRKENEPHKIMLHrGRYGHNnSILYGRFTKMIGSPNNISHS-SVCAESEKFGRYYTEGGW--DYNSYDYA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 199 NARYIVLIGH-HIGEDTHNTQLQDFALALKRGAKVVVVDPRFSTAAAKAHLWLPIKPGTDTALLLAWIHVLIYEDLYDKE 277
Cdd:cd02757 162 NAKYILFFGAdPLESNRQNPHAQRIWGGKMDQAKVVVVDPRLSNTAAKADEWLPIKPGEDGALALAIAHVILTEGLWDKD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 278 YVAKYTTG--------------FEE---------LKTHVKDFTPEWAEKHTEIPAEIIRQVAREMAAHKPqavlPPTRHT 334
Cdd:cd02757 242 FVGDFVDGknyfkagetvdeesFKEksteglvkwWNLELKDYTPEWAAKISGIPAETIERVAREFATAAP----AAAAFT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 335 vWYG-----DDTYRMMALYYVNVLLGNYGRKGGfyiaqspylekyptpplplepaaggcsgpaggnhepegfkpradkgk 409
Cdd:cd02757 318 -WRGatmqnRGSYNSMACHALNGLVGSIDSKGG----------------------------------------------- 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 410 ffarttaiqeLIEPMITGEpypIKGLFAYGINLFHSIPNVPRTKEALKKLDLYVAIDVLPQEHVMWADVILPEATYLERY 489
Cdd:cd02757 350 ----------LCPNMGVPK---IKVYFTYLDNPVFSNPDGMSWEEALAKIPFHVHLSPFMSETTYFADIVLPDGHHFERW 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 490 DDLVAVAHKTPFIQLRVPAHEPLFDTKPGWWIARELGIRL-GLGEFFPWQTI-EEYLDTrlqsigfdlETLKGMGtlvqk 567
Cdd:cd02757 417 DVMSQENNLHPWLSIRQPVVKSLGEVREETEILIELAKKLdPKGSDGMKRYApGQFKDP---------ETGKNNR----- 482
|
570 580 590
....*....|....*....|....*....|....*..
gi 2075248272 568 gkpwledWEKEgrLPFGTPSGKIELYCQAFKKAGHQP 604
Cdd:cd02757 483 -------WEFE--NVFPTETGKFEFYSETLKKYLQNH 510
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
49-615 |
1.47e-88 |
|
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: 291.05 E-value: 1.47e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 49 WRCGIVAHAVGNRVYKVEGYEANPKsrgRVCPRGQGMPQTTYDPDRLKRPLIRVE--------GSQRGEGKY-RVaTWEE 119
Cdd:cd02751 5 HWGPFKAHVKDGVIVRVEPDDTDQP---RPCPRGRSVRDRVYSPDRIKYPMKRVGwlgngpgsRELRGEGEFvRI-SWDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 120 ALDYVAKRMMKLKEEYGPEAIaFFGHGTGDSWFVDFLP---------------AAWGSPNAAkpsvaictapretAAQWV 184
Cdd:cd02751 81 ALDLVASELKRIREKYGNEAI-FGGSYGWASAGRLHHAqsllhrflnliggylGSYGTYSTG-------------AAQVI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 185 FGRPIGGHEPI----DW----ENARYIVLIGH--------HIGEDTHNtQLQDFALALKRGAKVVVVDPRFS-TAAAKAH 247
Cdd:cd02751 147 LPHVVGSDEVYeqgtSWddiaEHSDLVVLFGAnplktrqgGGGGPDHG-SYYYLKQAKDAGVRFICIDPRYTdTAAVLAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 248 LWLPIKPGTDTALLLAWIHVLIYEDLYDKEYVAKYTTGFEELKTHV---KDF---TPEWAEKHTEIPAEIIRQVAREMAA 321
Cdd:cd02751 226 EWIPIRPGTDVALMLAMAHTLITEDLHDQAFLARYTVGFDEFKDYLlgeSDGvpkTPEWAAEITGVPAETIRALAREIAS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 322 HKPQ--AVLPPTRHTvwYGDDTYRM-MALYYvnvLLGNYGRKG---GFYIAQSPYlekyptpplplepaAGGCSGPAGGN 395
Cdd:cd02751 306 KRTMiaQGWGLQRAH--HGEQPAWMlVTLAA---MLGQIGLPGggfGFGYGYSNG--------------GGPPRGGAGGP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 396 HEPEGFKPRADKGKFFARTTAIQELIEPM--ITGEP-YP-IKGLFAYGINLFHSIPNVPRTKEALKKLDLYVAIDVLPQE 471
Cdd:cd02751 367 GLPQGKNPVKDSIPVARIADALLNPGKEFtaNGKLKtYPdIKMIYWAGGNPLHHHQDLNRLIKALRKDETIVVHDIFWTA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 472 HVMWADVILPEATYLERYDDLVAVAHKTPFIQLRVPAHEPLFDTKPGWWIARELGIRLGLGEFFP-----WQTIEE-YLD 545
Cdd:cd02751 447 SARYADIVLPATTSLERNDIGLTGNYSNRYLIAMKQAVEPLGEARSDYEIFAELAKRLGVEEEFTegrdeMEWLEHlYEE 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 546 TRLQSIGF-----DLETLKGMGTLV--QKGKPWL------EDWEKEgrlPFGTPSGKIELYCQAFKKAGH---QPLPVFT 609
Cdd:cd02751 527 TRAKAAGPgpelpSFEEFWEKGIVRvpAAPKPFVafadfrEDPEAN---PLGTPSGKIEIYSETLADFGYddcPGHPTWI 603
|
....*.
gi 2075248272 610 PPEEPP 615
Cdd:cd02751 604 EPWEGL 609
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
47-615 |
4.01e-87 |
|
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: 287.68 E-value: 4.01e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 47 CFWRCGIVAHAVGNRVYKVEGYEANPKSRG----RVCPRGQGMPQTTYDPDRLKRPLIRVegSQRGEGKYRVATWEEALD 122
Cdd:cd02770 8 CGGRCPLKAHVKDGVITRIETDDTGDDDPGfhqiRACLRGRSQRKRVYNPDRLKYPMKRV--GKRGEGKFVRISWDEALD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 123 YVAKRMMKLKEEYGPEAIaFFGHGTGDSWFV-------DFLPAAWGSPNAAKPSVAicTAPRETAAQWVFGRPIGGHEPI 195
Cdd:cd02770 86 TIASELKRIIEKYGNEAI-YVNYGTGTYGGVpagrgaiARLLNLTGGYLNYYGTYS--WAQITTATPYTYGAAASGSSLD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 196 DWENARYIVLIGHHIGEDTHNTQLQ--DFALALKRGAKVVVVDPRFS-TAAAKAHLWLPIKPGTDTALLLAWIHVLIYED 272
Cdd:cd02770 163 DLKDSKLVVLFGHNPAETRMGGGGStyYYLQAKKAGAKFIVIDPRYTdTAVTLADEWIPIRPGTDAALVAAMAYVMITEN 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 273 LYDKEYVAKYTTGFEE--------LKTHVKDF-----------TPEWAEKHTEIPAEIIRQVAREMAAHKPQAVLP---P 330
Cdd:cd02770 243 LHDQAFLDRYCVGFDAehlpegapPNESYKDYvlgtgydgtpkTPEWASEITGVPAETIRRLAREIATTKPAAILQgwgP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 331 TRHTvwYGDDTYRMMALyyVNVLLGNYGRKGGFYIAqSPYLEKYPTPPLPlepaaggcsgpAGGNhepegfkPRADKGKF 410
Cdd:cd02770 323 QRHA--NGEQAARAIMM--LAAMTGNVGIPGGNTGA-RPGGSAYNGAGLP-----------AGKN-------PVKTSIPC 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 411 FARTTAIQ---ELIEPMITGEPY-----PIKGLFAYGIN-LFHSIPNVPRTKEAL----KKLDLYVAIDVLPQEHVMWAD 477
Cdd:cd02770 380 FMWTDAIErgeEMTADDGGVKGAdklksNIKMIWNYAGNtLINQHSDDNNTTRALlddeSKCEFIVVIDNFMTPSARYAD 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 478 VILPEATYLERYDDLV-AVAHKTPFIQLRVPAHEPLFDTKPGWWIARELGIRLGLGEFFPW-QTIEEYLD-----TRLQS 550
Cdd:cd02770 460 ILLPDTTELEREDIVLtSNAGMMEYLIYSQKAIEPLYECKSDYEICAELAKRLGVEDQFTEgKTEQEWLEelygqTRAKE 539
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2075248272 551 IGFD-LETLKGMG---TLVQKGKPWLEDWEKE-GRLPFGTPSGKIELYCQA------FKKAGHQ--PLPVFTPPEEPP 615
Cdd:cd02770 540 PGLPtYEEFREKGiyrVPRALPFVAFEDFREDpENNPLKTPSGKIEIYSKAladmakTLPEGDEipAIPKYVPAWEGP 617
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
43-589 |
4.35e-83 |
|
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: 273.71 E-value: 4.35e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 43 ICEGCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRVCPRGQGMPQTTYDPDRLKRPLIRVEGsqrgegKYRVATWEEALD 122
Cdd:cd02753 3 VCPYCGVGCGLELWVKDNKIVGVEPVKGHPVNRGKLCVKGRFGFDFVNSKDRLTKPLIRKNG------KFVEASWDEALS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 123 YVAKRMMKLKEEYGPEAIAFFG--HGTGDSWFV--DFLPAAWGSPN---AAKpsvaICTAPRETAAQWVFGrpIGGH-EP 194
Cdd:cd02753 77 LVASRLKEIKDKYGPDAIAFFGsaKCTNEENYLfqKLARAVGGTNNvdhCAR----LCHSPTVAGLAETLG--SGAMtNS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 195 I-DWENARYIVLIGHHIGEdTH---NTQLQDfalALKRGAKVVVVDPRFSTAAAKAHLWLPIKPGTDTALLLAWIHVLIY 270
Cdd:cd02753 151 IaDIEEADVILVIGSNTTE-AHpviARRIKR---AKRNGAKLIVADPRRTELARFADLHLQLRPGTDVALLNAMAHVIIE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 271 EDLYDKEYVAKYTTGFEELKTHVKDFTPEWAEKHTEIPAEIIRQVAREMAAHKPQAVL---PPTRHTVwyGDDTyrMMAL 347
Cdd:cd02753 227 EGLYDEEFIEERTEGFEELKEIVEKYTPEYAERITGVPAEDIREAARMYATAKSAAILwgmGVTQHSH--GTDN--VMAL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 348 YYVNVLLGNYGRKGgfyiaqspylekypTPPLPLE---PAAGGCsgpaggnhepegfkpraDKGKFfarttaiqeliePM 424
Cdd:cd02753 303 SNLALLTGNIGRPG--------------TGVNPLRgqnNVQGAC-----------------DMGAL------------PN 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 425 ItgepYP--IKGLFAYGINLFHSIPNVPRTKEALKKLDLYVAIDVLPQEHVMWADVILPEATYLERyDDLVAVAHKTpfI 502
Cdd:cd02753 340 V----LPgyVKALYIMGENPALSDPNTNHVRKALESLEFLVVQDIFLTETAELADVVLPAASFAEK-DGTFTNTERR--V 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 503 QLRVPAHEPLFDTKPGWWIARELGIRLGLGEFFpwQTIEEYLD--TRL--QSIGFDLETLKGMGTL-------VQKGKPW 571
Cdd:cd02753 413 QRVRKAVEPPGEARPDWEIIQELANRLGYPGFY--SHPEEIFDeiARLtpQYAGISYERLERPGGLqwpcpdeDHPGTPI 490
|
570
....*....|....*...
gi 2075248272 572 LEDWEkegrlpFGTPSGK 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 |
1.07e-80 |
|
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: 268.96 E-value: 1.07e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 46 GCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRVCPRGQGMPQTTYDPDRLKRPLIRVegSQRGEGKYRVATWEEALDYVA 125
Cdd:cd02765 7 NCGGRCPLKCHVRDGKIVKVEPNEWPDKTYKRGCTRGLSHLQRVYSPDRLKYPMKRV--GERGEGKFERITWDEALDTIA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 126 KRMMKLKEEYGPEAIAFFgHGTGDSWFVDFLPAAwgSPNAAKPsVAICTAPRETAAQWV-----FGRPIGGHEPIDWENA 200
Cdd:cd02765 85 DKLTEAKREYGGKSILWM-SSSGDGAILSYLRLA--LLGGGLQ-DALTYGIDTGVGQGFnrvtgGGFMPPTNEITDWVNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 201 RYIVLIGHHIGEdTHNTQLQDFALALKRGAKVVVVDPRFSTAAAKAHLWLPIKPGTDTALLLAWIHVLIYEDLYDKEYVA 280
Cdd:cd02765 161 KTIIIWGSNILE-TQFQDAEFFLDARENGAKIVVIDPVYSTTAAKADQWVPIRPGTDPALALGMINYILEHNWYDEAFLK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 281 KYT--------------------------------------------------------------TGFEELKTHVKDFTP 298
Cdd:cd02765 240 SNTsapflvredngtllrqadvtatpaedgyvvwdtnsdspepvaatninpalegeytingvkvhTVLTALREQAASYPP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 299 EWAEKHTEIPAEIIRQVAREMAAHKPQAVLP---PTRhtVWYGDDTYRMMALyyVNVLLGNYGRKGGFyIAQspylekyp 375
Cdd:cd02765 320 KAAAEICGLEEAIIETLAEWYATGKPSGIWGfggVDR--YYHSHVFGRTAAI--LAALTGNIGRVGGG-VGQ-------- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 376 tpplplepaaggcsgpaggnhepegfkpradkgkffarttaiqeliepmitgepypIKGLFAYGINLFHSIPNVPRTKEA 455
Cdd:cd02765 387 --------------------------------------------------------IKFMYFMGSNFLGNQPDRDRWLKV 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 456 LKKLDLYVAIDVLPQEHVMWADVILPEATYLERYDDLVAVAHKtPFIQLRVPAHEPLFDTKPGWWIARELGIRLGLGEFF 535
Cdd:cd02765 411 MKNLDFIVVVDIFHTPTVRYADIVLPAAHWFEVEDLLVRYTTH-PHVLLQQKAIEPLFESKSDFEIEKGLAERLGLGDYF 489
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 536 PwQTIEEYLDTRLQS-----IGFDLETLKGMGTLVQKGKPWLEDWEKEGRlPFGTPSGKIELYCQAFKKAgHQPLPVFTP 610
Cdd:cd02765 490 P-KTPEDYVRAFMNSddpalDGITWEALKEEGIIMRLATPEDPYVAYLDQ-KFGTPSGKLEFYNEAAPEL-EEALPLPEE 566
|
.
gi 2075248272 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 |
3.54e-79 |
|
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: 264.86 E-value: 3.54e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 51 CGIVAHAVGNRVYKVEGYEANPKSRGRVCPRGQGMPQTTYDPDRLKRPLIRVEGsqrgeGKYRVATWEEALDYVAKRMMK 130
Cdd:cd02754 11 CGVEIGVKDGKVVAVRGDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLLRRNG-----GELVPVSWDEALDLIAERFKA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 131 LKEEYGPEAIAFFGHG---TGDSWFVD-FLPAAWGSPNaAKPSVAICTAPRETAAQWVFG--RPIGGHEpiDWENARYIV 204
Cdd:cd02754 86 IQAEYGPDSVAFYGSGqllTEEYYAANkLAKGGLGTNN-IDTNSRLCMASAVAGYKRSFGadGPPGSYD--DIEHADCFF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 205 LIGHHIGEdTHNTQLQDFALALK--RGAKVVVVDPRFSTAAAKAHLWLPIKPGTDTALLLAWIHVLIYEDLYDKEYVAKY 282
Cdd:cd02754 163 LIGSNMAE-CHPILFRRLLDRKKanPGAKIIVVDPRRTRTADIADLHLPIRPGTDLALLNGLLHVLIEEGLIDRDFIDAH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 283 TTGFEELKTHVKDFTPEWAEKHTEIPAEIIRQVAREMAahKPQAVLpptrhTVW--------YGDDTYRmmALYYVNVLL 354
Cdd:cd02754 242 TEGFEELKAFVADYTPEKVAEITGVPEADIREAARLFG--EARKVM-----SLWtmgvnqstQGTAANN--AIINLHLAT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 355 GNYGRKGgfyiaqspylekypTPPLPL--EPAAGG---CSG----PAGGNHEPEGfKPRADKGKF---------FARTTA 416
Cdd:cd02754 313 GKIGRPG--------------SGPFSLtgQPNAMGgreVGGlanlLPGHRSVNNP-EHRAEVAKFwgvpegtipPKPGLH 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 417 IQELIEPMITGEpypIKGLFAYGINLFHSIPNVPRTKEALKKLDLYVAIDV-LPQEHVMWADVILPEATYLERyDDLVAV 495
Cdd:cd02754 378 AVEMFEAIEDGE---IKALWVMCTNPAVSLPNANRVREALERLEFVVVQDAfADTETAEYADLVLPAASWGEK-EGTMTN 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 496 AHKTpfIQLRVPAHEPLFDTKPGWWIARELGIRLGLGEFFPWQTIEEYLD-------TRLQSI-GFDLETLKGMGTL--V 565
Cdd:cd02754 454 SERR--VSLLRAAVEPPGEARPDWWILADVARRLGFGELFPYTSPEEVFEeyrrlsrGRGADLsGLSYERLRDGGVQwpC 531
|
570 580
....*....|....*....|....*...
gi 2075248272 566 QKGKPwledwEKEGRL----PFGTPSGK 589
Cdd:cd02754 532 PDGPP-----EGTRRLfedgRFPTPDGR 554
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
41-526 |
9.70e-76 |
|
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: 255.01 E-value: 9.70e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 41 YQICEGCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRVCPRGQGMPQTTYDPDRLKRPLIRVEGSqrgegkYRVATWEEA 120
Cdd:cd02762 1 KRACILCEANCGLVVTVEDGRVASIRGDPDDPLSKGYICPKAAALGDYQNDPDRLRTPMRRRGGS------FEEIDWDEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 121 LDYVAKRMMKLKEEYGPEAIAFF-----GHGTGDSWFVDFLPAAWGSPNAAKPSVAIcTAPRETAAQWVFGRPIGGHEPi 195
Cdd:cd02762 75 FDEIAERLRAIRARHGGDAVGVYggnpqAHTHAGGAYSPALLKALGTSNYFSAATAD-QKPGHFWSGLMFGHPGLHPVP- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 196 DWENARYIVLIGHH-----------IGEDTHNTQLQDfalalkRGAKVVVVDPRFSTAAAKAHLWLPIKPGTDTALLLAW 264
Cdd:cd02762 153 DIDRTDYLLILGANplqsngslrtaPDRVLRLKAAKD------RGGSLVVIDPRRTETAKLADEHLFVRPGTDAWLLAAM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 265 IHVLIYEDLYDKEYVAKYTTGFEELKTHVKDFTPEWAEKHTEIPAEIIRQVAREMAAHKPQAVlpptrhtvwYGD----- 339
Cdd:cd02762 227 LAVLLAEGLTDRRFLAEHCDGLDEVRAALAEFTPEAYAPRCGVPAETIRRLAREFAAAPSAAV---------YGRlgvqt 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 340 ---DTYRMMALYYVNVLLGNYGRKGGfyiaqspylEKYPTPPLPLEPAAGGCSGPAGGNHEPEGFKPRAdKGKFFARTTA 416
Cdd:cd02762 298 qlfGTLCSWLVKLLNLLTGNLDRPGG---------AMFTTPALDLVGQTSGRTIGRGEWRSRVSGLPEI-AGELPVNVLA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 417 iqeliEPMITGEPYPIKGLFAYGINLFHSIPNVPRTKEALKKLDLYVAIDVLPQEHVMWADVILPEATYLER--YD--DL 492
Cdd:cd02762 368 -----EEILTDGPGRIRAMIVVAGNPVLSAPDGARLEAALGGLEFMVSVDVYMTETTRHADYILPPASQLEKphATffNL 442
|
490 500 510
....*....|....*....|....*....|....
gi 2075248272 493 VAVAHktpFIQLRVPAHEPLFDTKPGWWIARELG 526
Cdd:cd02762 443 EFPRN---AFRYRRPLFPPPPGTLPEWEILARLV 473
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
69-545 |
1.28e-71 |
|
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: 241.45 E-value: 1.28e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 69 EANPksRGrvCPRGQGMPQTTYDPDRLKRPLIRVEgsQRGEGKYRVATWEEALDYVAKRMMKLKEEYGPEAIAFFGHGTG 148
Cdd:cd02750 45 DYNP--RG--CQRGASFSWYLYSPDRVKYPLKRVG--ARGEGKWKRISWDEALELIADAIIDTIKKYGPDRVIGFSPIPA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 149 DSwfvdflPAAWGSP-------NAAKPSVAICTAPRETAAQWVFGRPIGGHEPIDWENARYIVLIGHHIGEdthnTQLQD 221
Cdd:cd02750 119 MS------MVSYAAGsrfasliGGVSLSFYDWYGDLPPGSPQTWGEQTDVPESADWYNADYIIMWGSNVPV----TRTPD 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 222 ---FALALKRGAKVVVVDPRFSTAAAKAHLWLPIKPGTDTALLLAWIHVLIYEDLYDKEYVAKYTtgfeELKTHVkdFTP 298
Cdd:cd02750 189 ahfLTEARYNGAKVVVVSPDYSPSAKHADLWVPIKPGTDAALALAMAHVIIKEKLYDEDYLKEYT----DLPFLV--YTP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 299 EWAEKHTEIPAEIIRQVAREMAAHKPQAVL--PPTRHtvWY-GDDTYRMMALyyVNVLLGNYGRKGGfyiaqspylekyp 375
Cdd:cd02750 263 AWQEAITGVPRETVIRLAREFATNGRSMIIvgAGINH--WYhGDLCYRALIL--LLALTGNEGKNGG------------- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 376 tpplplepaaggcsgpaGGNHepegfkpradkgkffarttaiqeliepmITGEPypiKGLFAYGINLFHS-------IPN 448
Cdd:cd02750 326 -----------------GWAH----------------------------YVGQP---RVLFVWRGNLFGSsgkgheyFED 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 449 VPrtkeaLKKLDLYVAIDVLPQEHVMWADVILPEATYLERYDDLVAVAHktPFIQLRVPAHEPLFDTKPGWWIARELGIR 528
Cdd:cd02750 358 AP-----EGKLDLIVDLDFRMDSTALYSDIVLPAATWYEKHDLSTTDMH--PFIHPFSPAVDPLWEAKSDWEIFKALAKK 430
|
490 500
....*....|....*....|.
gi 2075248272 529 lglgefFPWQT----IEEYLD 545
Cdd:cd02750 431 ------VPWRTltgrQQFYLD 445
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
1-743 |
3.11e-71 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 249.18 E-value: 3.11e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 1 MQRREFLKlsTLAAGALALRGSgpakALKAPWYR------------QEVKSVYQICE-GCFWRCGIVAHAVGNRVYKVE- 66
Cdd:PRK14990 14 VSRRGLVK--TTAIGGLAMASS----ALTLPFSRiahavdsaiptkSDEKVIWSACTvNCGSRCPLRMHVVDGEIKYVEt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 67 ------GYEAnpKSRGRVCPRGQGMPQTTYDPDRLKRPLIRVegSQRGEGKYRVATWEEALDYVAKRMMKLKEEYGPEAI 140
Cdd:PRK14990 88 dntgddNYDG--LHQVRACLRGRSMRRRVYNPDRLKYPMKRV--GARGEGKFERISWEEAYDIIATNMQRLIKEYGNESI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 141 aFFGHGTGDswFVDFLPAAWGSPNAAKPSVAIC------------TAPRETAAQWVFGRPIGGHEPIDWENARYIVLIGH 208
Cdd:PRK14990 164 -YLNYGTGT--LGGTMTRSWPPGNTLVARLMNCcggylnhygdysSAQIAEGLNYTYGGWADGNSPSDIENSKLVVLFGN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 209 HIGEDTHNTQLQDFALALKR---GAKVVVVDPRFS-TAAAKAHLWLPIKPGTDTALLLAWIHVLIYEDLYDKEYVAKYTT 284
Cdd:PRK14990 241 NPGETRMSGGGVTYYLEQARqksNARMIIIDPRYTdTGAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQPFLDKYCV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 285 GFEElKT---------HVKDF-----------TPEWAEKHTEIPAEIIRQVAREMAAHKPQAVLP---PTRHTvwYGDDT 341
Cdd:PRK14990 321 GYDE-KTlpasapkngHYKAYilgegpdgvakTPEWASQITGVPADKIIKLAREIGSTKPAFISQgwgPQRHA--NGEIA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 342 YRMMALyyVNVLLGNYGRKGGFYIAQS-----PYlEKYPTPPLPLEPAAggcsgpaggnhepegfkpradkgKFFARTTA 416
Cdd:PRK14990 398 TRAISM--LAILTGNVGINGGNSGAREgsyslPF-VRMPTLENPIQTSI-----------------------SMFMWTDA 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 417 IQE-----LIEPMITGE---PYPIKGLFAYGIN-LFHSIPNVPRTKEAL---KKLDLYVAIDVLPQEHVMWADVILPEAT 484
Cdd:PRK14990 452 IERgpemtALRDGVRGKdklDVPIKMIWNYAGNcLINQHSEINRTHEILqddKKCELIVVIDCHMTSSAKYADILLPDCT 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 485 YLERYD-DLVAVAHKTPFIQLRVPAHEPLFDTKPGWWIARELGIRLGLGE-FFPWQTIEEYL----DTRLQSIGF--DLE 556
Cdd:PRK14990 532 ASEQMDfALDASCGNMSYVIFNDQVIKPRFECKTIYEMTSELAKRLGVEQqFTEGRTQEEWMrhlyAQSREAIPElpTFE 611
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 557 TLKGMGTLVQKG--------KPWLEDWEKEgrlPFGTPSGKIELYCQAFKKAGH----------QPLPVFTPPEE----P 614
Cdd:PRK14990 612 EFRKQGIFKKRDpqghhvayKAFREDPQAN---PLTTPSGKIEIYSQALADIAAtwelpegdviDPLPIYTPGFEsyqdP 688
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 615 PPGFYRL----LYGRSPVHTfarTQNNWVLMEMDPENEVWIHREEARRLGLKDGDYVILENQNGvrEGPVRVKATERIRK 690
Cdd:PRK14990 689 LNKQYPLqltgFHYKSRVHS---TYGNVDVLKAACRQEMWINPLDAQKRGINNGDKVRIFNDRG--EVHIEAKVTPRMMP 763
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 2075248272 691 DCVYLVHGFGHKAPLMKVahGRGASDNYLQTRyKLDPISGGAGLRVNFVKLEK 743
Cdd:PRK14990 764 GVVALGEGAWYDPDAKRV--DKGGCINVLTTQ-RPSPLAKGNPSHTNLVQVEK 813
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
41-534 |
1.93e-69 |
|
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: 241.27 E-value: 1.93e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 41 YQICEGCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRVCPRGQGMPQTTYDPDRLKRPLIRVEgsQRGEGKYRVATWEEA 120
Cdd:cd02763 1 TTTCYMCACRCGIRVHLRDGKVRYIKGNPDHPLNKGVICAKGSSGIMKQYSPARLTKPLLRKG--PRGSGQFEEIEWEEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 121 LDYVAKRMMKLKEEyGPEAIAFFghgTG-------DSWFVdflpAAWGSPNAAKPSvAICTAPRETA-------AQWVFG 186
Cdd:cd02763 79 FSIATKRLKAARAT-DPKKFAFF---TGrdqmqalTGWFA----GQFGTPNYAAHG-GFCSVNMAAGglysiggSFWEFG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 187 RPigghepiDWENARYIVLIGhhIGEDTHNTQLQDFALALKR-GAKVVVVDPRFSTAAAKAHLWLPIKPGTDTALLLAWI 265
Cdd:cd02763 150 GP-------DLEHTKYFMMIG--VAEDHHSNPFKIGIQKLKRrGGKFVAVNPVRTGYAAIADEWVPIKPGTDGAFILALA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 266 HVLIYEDLYDKEYVAKYTTGFEelkthVKDFTPEWAEKHTEIPAEIIRQVAREMA-AHKPQAVLPPTRHTVWYGDDTYRM 344
Cdd:cd02763 221 HELLKAGLIDWEFLKRYTNAAE-----LVDYTPEWVEKITGIPADTIRRIAKELGvTARDQPIELPIAWTDVWGRKHEKI 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 345 M-----------------------ALYYVNVLLGNYGRKGGFyIAQSPY---LEKYPTPP------LPLEPAAGGCSG-P 391
Cdd:cd02763 296 TgrpvsfhamrgiaahsngfqtirALFVLMMLLGTIDRPGGF-RHKPPYprhIPPLPKPPkipsadKPFTPLYGPPLGwP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 392 AGGNH---EPEGFKPRADKGKFFARTTAIQELIEPMIT----GEPYPIKGLFAYGINL-FHSIPNVPRTKEALK------ 457
Cdd:cd02763 375 ASPDDllvDEDGNPLRIDKAYSWEYPLAAHGCMQNVITnawrGDPYPIDTLMIYMANMaWNSSMNTPEVREMLTdkdasg 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 458 --KLDLYVAIDVLPQEHVMWADVILPEATYLERYDDL------VAVAhKTPFIQLRVPAHEPLFDTKPGWWIARELGIRL 529
Cdd:cd02763 455 nyKIPFIIVCDAFYSEMVAFADLVLPDTTYLERHDAMslldrpISEA-DGPVDAIRVPIVEPKGDVKPFQEVLIELGTRL 533
|
....*
gi 2075248272 530 GLGEF 534
Cdd:cd02763 534 GLPGF 538
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
61-615 |
5.85e-52 |
|
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: 190.94 E-value: 5.85e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 61 RVYKVEGYEANPKSRgrvcPRGQGMPQTTYDPDRLKRPLIRVE---------GSQRGEGKY-RVaTWEEALDYVAKRMMK 130
Cdd:cd02769 17 RIVGVRPFEEDPDPS----PLLDGVPDAVYSPTRIKYPMVRRGwlekgpgsdRSLRGKEEFvRV-SWDEALDLVAAELKR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 131 LKEEYGPEAIafFGHGTGdswfvdflpaaWGSP--------------NAAKPSVAICTAPRETAAQWVFGRPIGGHEPID 196
Cdd:cd02769 92 VRKTYGNEAI--FGGSYG-----------WSSAgrfhhaqsllhrflNLAGGYVGSVGDYSTGAAQVILPHVVGSMEVYT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 197 -----W----ENARYIVLIGhhiGEDTHNTQLQDFAL----------ALK-RGAKVVVVDP-RFSTAAAKAHLWLPIKPG 255
Cdd:cd02769 159 eqqtsWpviaEHTELVVAFG---ADPLKNAQIAWGGIpdhqaysylkALKdRGIRFISISPlRDDTAAELGAEWIAIRPG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 256 TDTALLLAWIHVLIYEDLYDKEYVAKYTTGFEELKTHV---KD---FTPEWAEKHTEIPAEIIRQVAREMAAHKPQAVlp 329
Cdd:cd02769 236 TDVALMLALAHTLVTEGLHDKAFLARYTVGFDKFLPYLlgeSDgvpKTPEWAAAICGIPAETIRELARRFASKRTMIM-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 330 ptrhTVW------YGDDTYRMMAlyyvnVL---LGNYGRKGGFYIAQSPYLEkyptpplplepAAGGCSGPAGGNHEPEG 400
Cdd:cd02769 314 ----AGWslqrahHGEQPHWMAV-----TLaamLGQIGLPGGGFGFGYHYSN-----------GGGPPRGAAPPPALPQG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 401 FKPRADkgkFF--ARttaIQELIE-PmitGEP---------YP-IKglFAY--GINLFHSIPNVPRTKEALKKLDLYVAI 465
Cdd:cd02769 374 RNPVSS---FIpvAR---IADMLLnP---GKPfdyngkkltYPdIK--LVYwaGGNPFHHHQDLNRLIRAWQKPETVIVH 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 466 DVLPQEHVMWADVILPEATYLERyDDLvAVAHKTPFIqlrVPAH---EPLFDTKPGWWIARELGIRLGLGEFFP------ 536
Cdd:cd02769 443 EPFWTATARHADIVLPATTSLER-NDI-GGSGDNRYI---VAMKqvvEPVGEARDDYDIFADLAERLGVEEQFTegrdem 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 537 -WQTiEEYLDTRLQSIGFDLEtLKGMGTLVQKGKPWLEDWEKE-GRL----------PFGTPSGKIELYCQ---AFKKAG 601
Cdd:cd02769 518 eWLR-HLYEESRAQAAARGVE-MPSFDEFWAQGYVELPIPEADfVRLadfredpeanPLGTPSGRIEIFSEtiaGFGYDD 595
|
650
....*....|....
gi 2075248272 602 HQPLPVFTPPEEPP 615
Cdd:cd02769 596 CPGHPTWLEPAEWL 609
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
41-534 |
1.81e-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: 191.79 E-value: 1.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 41 YQICEGCFWRCGIVAHaVGNRVYKVEGYEANP------------------------------KSRGRVCPRGQGMPQTTY 90
Cdd:cd02758 1 YSSCLGCWTQCGIRVR-VDKETGKVLRIAGNPyhplntapslpyntplkeslylslvgenglKARATACARGNAGLQYLY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 91 DPDRLKRPLIRVegSQRGEGKYRVATWEEALDYVAK-------------RMMKLKE--------EYGPEA--IAF-FGHG 146
Cdd:cd02758 80 DPYRVLQPLKRV--GPRGSGKWKPISWEQLIEEVVEggdlfgeghveglKAIRDLDtpidpdhpDLGPKAnqLLYtFGRD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 147 TGDSWFVD-FLPAAWGSPNAAKPSvAICTAPRETAAQWVFGRPIGGHEPI-DWENARYIVLIGHHIGEDTHNTQLQDFAL 224
Cdd:cd02758 158 EGRTPFIKrFANQAFGTVNFGGHG-SYCGLSYRAGNGALMNDLDGYPHVKpDFDNAEFALFIGTSPAQAGNPFKRQARRL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 225 ALKR---GAKVVVVDPRFS---TAAAKAHLWLPIKPGTDTALLLAWIHVLIYEDLYDKEYVA------------------ 280
Cdd:cd02758 237 AEARtegNFKYVVVDPVLPnttSAAGENIRWVPIKPGGDGALAMAMIRWIIENERYNAEYLSipskeaakaagepswtna 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 281 -------KYTTGFEELKTHVKDFT-PEWAEkHTEIPAEIIRQVAREMAAHKPQAVLpPTRHTVWYGDDTYRMMALYYVNV 352
Cdd:cd02758 317 thlvitvRVKSALQLLKEEAFSYSlEEYAE-ICGVPEAKIIELAKEFTSHGRAAAV-VHHGGTMHSNGFYNAYAIRMLNA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 353 LLGNYGRKGGFYIAQSPYleKYPT-PPLPLEPAAGGCSGPAGGNHEPEG--------FKPRADKGK---------FFART 414
Cdd:cd02758 395 LIGNLNWKGGLLMSGGGF--ADNSaGPRYDFKKFFGEVKPWGVPIDRSKkayektseYKRKVAAGEnpypakrpwYPLTP 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 415 TAIQELIEPMITGEPYPIKGLFAYGINLFHSIPN-VPRTKEALK---KLDLYVAIDVLPQEHVMWADVILPEATYLER-- 488
Cdd:cd02758 473 ELYTEVIASAAEGYPYKLKALILWMANPVYGAPGlVKQVEEKLKdpkKLPLFIAIDAFINETSAYADYIVPDTTYYESwg 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 2075248272 489 ----YDDLVAVAHktpfiQLRVPAHEPLFDTKPG------WWIARELGIRLGLGEF 534
Cdd:cd02758 553 fstpWGGVPTKAS-----TARWPVIAPLTEKTANghpvsmESFLIDLAKALGLPGF 603
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
619-743 |
4.83e-45 |
|
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: 157.44 E-value: 4.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 619 YRLLYGRSPVHTFARTQNNWVLMEMDPENEVWIHREEARRLGLKDGDYVILENQNGVREGPVRVkaTERIRKDCVYLVHG 698
Cdd:cd02778 2 FRLIYGKSPVHTHGHTANNPLLHELTPENTLWINPETAARLGIKDGDRVEVSSARGKVTGKARL--TEGIRPDTVFMPHG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2075248272 699 FGHKAPLMKVAHGRGASDNYLqTRYKLDPISGGAGLRVNFVKLEK 743
Cdd:cd02778 80 FGHWAPALSRAYGGGVNDNNL-LPGSTEPVSGGAGLQEFTVTVRK 123
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
94-526 |
2.56e-44 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 163.34 E-value: 2.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 94 RLKRPLIRvegsqRGEGKYRVATWEEALDYVAKRMMKLKEEYGPEAIAFFGhGTGD-----SWFV--DFLpAAWGSPNAA 166
Cdd:pfam00384 1 RLKYPMVR-----RGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAING-GSGGltdveSLYAlkKLL-NRLGSKNGN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 167 --KPSVAICTAPRETA-AQWVFGRpIGGHEPIDWENARYIVLIGHHIGEdTH---NTQLqdFALALKRGAKVVVVDPRFS 240
Cdd:pfam00384 74 teDHNGDLCTAAAAAFgSDLRSNY-LFNSSIADIENADLILLIGTNPRE-EApilNARI--RKAALKGKAKVIVIGPRLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 241 taAAKAHLWLPIKPGTDTALLLAWIHVLIYEDLYDKEYVAKyttgfeelkthvkdftpewaekhteipAEIIrqVAREMa 320
Cdd:pfam00384 150 --LTYADEHLGIKPGTDLALALAGAHVFIKELKKDKDFAPK---------------------------PIII--VGAGV- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 321 ahkpqavlppTRHTvwYGDDTYRMMALyyVNVLLGNYGRKGGfyiaqspylekyptpplplepaaggcsGPAGGNHEP-E 399
Cdd:pfam00384 198 ----------LQRQ--DGEAIFRAIAN--LADLTGNIGRPGG---------------------------GWNGLNILQgA 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 400 GFKPRADKGKFFARTTAIQELIEPMITGepypIKGLFAYGINLFHSIPNVPRTKEALKKLDLYVAIDVLPQEH-VMWADV 478
Cdd:pfam00384 237 ASPVGALDLGLVPGIKSVEMINAIKKGG----IKVLYLLGNNPFVTHADENRVVKALQKLDLFVVYDGHHGDKtAKYADV 312
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2075248272 479 ILPEATYLERYDDLVAVAHKtpfIQLRVPAHEPLFDTKPGWWIARELG 526
Cdd:pfam00384 313 ILPAAAYTEKNGTYVNTEGR---VQSTKQAVPPPGEAREDWKILRALS 357
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
43-530 |
6.02e-44 |
|
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: 168.73 E-value: 6.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 43 ICEGCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRVCPRGQGMPQTTYDPDRLKRPLIRVEGSqrgeGKYRVATWEEALD 122
Cdd:cd02752 3 ICPYCSVGCGLIAYVQNGVWVHQEGDPDHPVNRGSLCPKGAALRDFVHSPKRLKYPMYRAPGS----GKWEEISWDEALD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 123 YVAKRMMKLKEE------------YGPEAIAFFGHGTGD---SWFVDFLPAAWGSpNAAKPSVAICTAPRETAAQWVFGR 187
Cdd:cd02752 79 EIARKMKDIRDAsfveknaagvvvNRPDSIAFLGSAKLSneeCYLIRKFARALGT-NNLDHQARIUHSPTVAGLANTFGR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 188 PIGGHEPIDWENARYIVLIGHHIGEDtHNTQLQDFALAL-KRGAKVVVVDPRFSTAAAKAHLWLPIKPGTDTALLLAWIH 266
Cdd:cd02752 158 GAMTNSWNDIKNADVILVMGGNPAEA-HPVSFKWILEAKeKNGAKLIVVDPRFTRTAAKADLYVPIRSGTDIAFLGGMIN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 267 vliyedlydkeYVAKYttgfeelkthvkdfTPEWAEKHTEIPAEIIRQVAREMAAH----KPQAV---LPPTRHTVwyGD 339
Cdd:cd02752 237 -----------YIIRY--------------TPEEVEDICGVPKEDFLKVAEMFAATgrpdKPGTIlyaMGWTQHTV--GS 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 340 DTYRMMALyyVNVLLGNYGRKGGfyiaqspylekyptpplplepaaggcsgpaGGNhepegfkprADKGKffartTAIQE 419
Cdd:cd02752 290 QNIRAMCI--LQLLLGNIGVAGG------------------------------GVN---------ALRGH-----SNVQG 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 420 LIEPMITGEPYPikGLFAyGINLFHSIPNVPRTKEALKKLDLYVAIDVLPQE-HVMWAD------------VILPEATYL 486
Cdd:cd02752 324 ATDLGLLSHNLP--GYLG-GQNPNSSFPNANKVRRALDKLDWLVVIDPFPTEtAAFWKNpgmdpksiqtevFLLPAACQY 400
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2075248272 487 ERYDDLVAVAHktpFIQLRVPAHEPLFDTKPGWWIARELGIRLG 530
Cdd:cd02752 401 EKEGSITNSGR---WLQWRYKVVEPPGEAKSDGDILVELAKRLG 441
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
44-565 |
4.68e-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: 148.96 E-value: 4.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 44 CEGCFWRCGIVAHAVGNRVykVEGYEANPK------SRGRVCPRGQGMPQTTYDPDRLKRPLIRV---EGSQRGEGkYRV 114
Cdd:cd02760 4 CYNCVAGPDFMAVKVVDGV--ATEIEPNFAaedihpARGRVCVKAYGLVQKTYNPNRVLQPMKRTnpkKGRNEDPG-FVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 115 ATWEEALDYVAKRMMKLKE-----EYG-PEAIAFFGHGTGDSWFVDFLP---AAWGSPNAakpSVAICTAPRETAAQWVF 185
Cdd:cd02760 81 ISWDEALDLVAAKLRRVREkglldEKGlPRLAATFGHGGTPAMYMGTFPaflAAWGPIDF---SFGSGQGVKCVHSEHLY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 186 GRPIGGHEPI--DWENARYIVLIGHHIGEDTHNTQLQDFALALKRGAKVVVVDPRFSTAAAKAHLWLPIKPGTDTALLLA 263
Cdd:cd02760 158 GEFWHRAFTVaaDTPLANYVISFGSNVEASGGPCAVTRHADARVRGYKRVQVEPHLSVTGACSAEWVPIRPKTDPAFMFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 264 WIHVLIYE---DLYDKEY-------------------------------------------------------------- 278
Cdd:cd02760 238 MIHVMVHEqglGKLDVPFlrdrtsspylvgpdglylrdaatgkplvwdersgravpfdtrgavpavagdfavdgavsvda 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 279 --------VAKYTTGFEELKTHVKDFTPEWAEKHTEIPAEIIRQVAREMA----------------AHKPQAV-LPPTRH 333
Cdd:cd02760 318 ddetaihqGVEGTTAFTMLVEHMRKYTPEWAESICDVPAATIRRIAREFLenasigstievdgvtlPYRPVAVtLGKSVN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 334 TVWygDDTYRMMALYYVNVLLGN-------------------------YGRKGGFYIAQSPYLEKYPTPPLPLEPAAGGC 388
Cdd:cd02760 398 NGW--GAFECCWARTLLATLVGAlevpggtlgttvrlnrphddrlasvKPGEDGFMAQGFNPTDKEHWVVKPTGRNAHRT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 389 SGPAGGNHE-PEGFKPRaDKGKFFARTTAIQELIEPmitgePYPIKGLFAYGINLFHSIPNVPRTKEALKKLDLYVAIDV 467
Cdd:cd02760 476 LVPIVGNSAwSQALGPT-QLAWMFLREVPLDWKFEL-----PTLPDVWFNYRTNPAISFWDTATLVDNIAKFPFTVSFAY 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 468 LPQEHVMWADVILPEATYLERYDDLVAVAHKtpFIQ---------LRVPAHEPLFDTKPGWWIARELGIRLGLgeffpwq 538
Cdd:cd02760 550 TEDETNWMADVLLPEATDLESLQMIKVGGTK--FVEqfwehrgvvLRQPAVEPQGEARDFTWISTELAKRTGL------- 620
|
650 660
....*....|....*....|....*..
gi 2075248272 539 tIEEYldTRLQSIGFDLETLKGMGTLV 565
Cdd:cd02760 621 -LADY--NAALNRGAGGAPLKGEGYDQ 644
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
1-674 |
8.59e-36 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 145.20 E-value: 8.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 1 MQRREFLKlSTLAAGALALRGSG---PAKALKAPWYRQEVKSVYQIcEGCFWRcGIVAHAVGNRVYKVEGYE--ANPksr 75
Cdd:PRK15102 1 ASRRRFLK-GLGGLSAAGMLGPSlltPRSALAAQAAAAETTKEWIL-TGSHWG-AFRAKVKNGRFVEAKPFEldKYP--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 76 grvCPRGQGMPQTTYDPDRLKRPLIRVE---------GSQRGEGKYRVATWEEALDYVAKRMMKLKEEYGPEAI------ 140
Cdd:PRK15102 75 ---TKMINGIKGHVYNPSRIRYPMVRLDwlrkrhksdTSQRGDNRFVRVSWDEALDLFYEELERVQKTYGPSALhtgqtg 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 141 ----------------AFFGHGTGDSWFVDFlpaawgSPNAAK---PSVAICTAPRETAAQWvfgrpigghePIDWENAR 201
Cdd:PRK15102 152 wqstgqfhsatghmqrAIGMHGNSVGTVGDY------STGAGQvilPYVLGSTEVYEQGTSW----------PLILENSK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 202 YIVLIGH------HIG--EDTHNT--QLQDFALALKRGA-KVVVVDPRFStaaaKAHLWLP-----IKPGTDTALLLAWI 265
Cdd:PRK15102 216 TIVLWGSdpvknlQVGwnCETHESyaYLAQLKEKVAKGEiNVISIDPVVT----KTQNYLGcehlyVNPQTDVPLMLALA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 266 HVLIYEDLYDKEYVAKYTTGFEELKTHV---KD---FTPEWAEKHTEIPAEIIRQVAREMAAHKPQAVLPPTRHTVWYGD 339
Cdd:PRK15102 292 HTLYSENLYDKKFIDNYCLGFEQFLPYLlgeKDgvpKTPEWAEKICGIDAETIRELARQMAKGRTQIIAGWCIQRQQHGE 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 340 DTYRMMALyyVNVLLGNYGRKGGFYiaqsPYLEKYPTPPLPlepaAGGCSGPAG--GNHEpEGFKPRADKGKF--FARTT 415
Cdd:PRK15102 372 QPYWMGAV--LAAMLGQIGLPGGGI----SYGHHYSGIGVP----SSGGAIPGGfpGNLD-TGQKPKHDNSDYkgYSSTI 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 416 AIQELIEPMItgEP------------YP-IKGLFAYGINLFHSIPNVPRTKEALKKLDLYVAIDVLPQEHVMWADVILPE 482
Cdd:PRK15102 441 PVARFIDAIL--EPgktinwngkkvtLPpLKMMIFSGTNPWHRHQDRNRMKEAFRKLETVVAIDNQWTATCRFADIVLPA 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 483 ATYLERYDDLVAVAHKTPFIQLRVPAHEPLFDTKPGWWIARELGIRLG--------LGEFfpwQTIEE-YLDTRLQSIG- 552
Cdd:PRK15102 519 CTQFERNDIDQYGSYSNRGIIAMKKVVEPLFESRSDFDIFRELCRRFGrekeytrgMDEM---GWLKRlYQECKQQNKGk 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 553 FDL---ETLKGMG-TLVQKGKPWL--EDWEKEGRL-PFGTPSGKIELYCQAFKKAGH---QPLPVFTPPEEPP---PGFY 619
Cdd:PRK15102 596 FHMpefDEFWKKGyVEFGEGQPWVrhADFREDPELnPLGTPSGLIEIYSRKIADMGYddcQGHPMWFEKIERShggPGSD 675
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2075248272 620 RLLYGRSPVHTFARTQNNwvLMEMDPENE---------VWIHREEARRLGLKDGDYVILENQNG 674
Cdd:PRK15102 676 KYPLWLQSVHPDKRLHSQ--LCESEELREtytvqgrepVYINPQDAKARGIKDGDVVRVFNDRG 737
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
3-535 |
2.64e-30 |
|
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: 126.06 E-value: 2.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 3 RREFLKLSTLAAGALALRGSGPAKALKAPW-----------YRQEVKSVYQICEGCfwrcGIVAHAVGNRVYKVEGYEAN 71
Cdd:cd02764 1 RRGFLKLMGASLAMASAAACRYPVEKIVPYviwpenivpgeTVYYATSLVPAGEGQ----GVLVKTVDGRPIKIEGNPDH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 72 PKSRGRVCPRGQGMPQTTYDPDRLKRPLIRVEGSQRGEgkyrvATWEEALDYVAKRMMKLKEEY----------GP---E 138
Cdd:cd02764 77 PASLGGTSARAQASVLSLYDPDRAQGPLRRGIDGAYVA-----SDWADFDAKVAEQLKAVKDGGklavlsgnvnSPtteA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 139 AIAFF-GHGTGDSWFVdflpaaWgSPNAAKPsvaictaPREtAAQWVFGRPigGHEPIDWENARYIV-----LIGHHIGE 212
Cdd:cd02764 152 LIGDFlKKYPGAKHVV------Y-DPLSAED-------VNE-AWQASFGKD--VVPGYDFDKAEVIVsidadFLGSWISA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 213 DTHNtqlQDFALALKRGA-----KVVVVDPRFSTAAAKAHLWLPIKPGTDTALLLAWIHVLIyedlyDKEYVAKYTTGFE 287
Cdd:cd02764 215 IRHR---HDFAAKRRLGAeepmsRLVAAESVYTLTGANADVRLAIRPSQEKAFALGLAHKLI-----KKGAGSSLPDFFR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 288 ELKThvkDFTPEWAEKHTEIPAEIIRQVAREMAAHKPQAVLPPTRHTVWYGDDTyrMMALYYVNVLLGNYGRKggfyiaq 367
Cdd:cd02764 287 ALNL---AFKPAKVAELTVDLDKALAALAKALAAAGKSLVVAGSELSQTAGADT--QVAVNALNSLLGNDGKT------- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 368 spylekyptpplpLEPAAGGCSGPAGGNHepegfkpradkgkffarttAIQELIEPMITGEpypIKGLFAYGINLFHSIP 447
Cdd:cd02764 355 -------------VDHARPIKGGELGNQQ-------------------DLKALASRINAGK---VSALLVYDVNPVYDLP 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 448 NVPRTKEALKKLDLYVAIDVLPQEHVMWADVILPEATYLERYDDLVAVAHKTPFIQlrvPAHEPLFDTKPgwwiARE--- 524
Cdd:cd02764 400 QGLGFAKALEKVPLSVSFGDRLDETAMLCDWVAPMSHGLESWGDAETPDGTYSICQ---PVIAPLFDTRS----AQEsll 472
|
570
....*....|...
gi 2075248272 525 --LGIRLGLGEFF 535
Cdd:cd02764 473 laLGGSLGGYEKL 485
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
94-589 |
1.68e-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: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 94 RLKRPLIRvegsQRGEGKYRVATWEEALDYVAKRMMKLKeeygPEAIAFF--GHGTGDSWFVDFLPA-AWGS---PNAAK 167
Cdd:cd02767 64 RLTYPMRY----DAGSDHYRPISWDEAFAEIAARLRALD----PDRAAFYtsGRASNEAAYLYQLFArAYGTnnlPDCSN 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 168 psvaICTAPRETAAQWVFGRPIGGHEPIDWENARYIVLIGHHIGEDtHNTQLQDFALALKRGAKVVVVDP-------RF- 239
Cdd:cd02767 136 ----MCHEPSSVGLKKSIGVGKGTVSLEDFEHTDLIFFIGQNPGTN-HPRMLHYLREAKKRGGKIIVINPlrepgleRFa 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 240 -----STAAAK----AHLWLPIKPGTDTALLLAWIHVLIYED-----LYDKEYVAKYTTGFEELKTHVKDFtpEWA--EK 303
Cdd:cd02767 211 npqnpESMLTGgtkiADEYFQVRIGGDIALLNGMAKHLIERDdepgnVLDHDFIAEHTSGFEEYVAALRAL--SWDeiER 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 304 HTEIPAEIIRQVAReMAAHKPQAV----LPPTRHTvwYGDDTYRMMalyyVNVLL--GNYGRKGgfyiaqspylekypTP 377
Cdd:cd02767 289 ASGLSREEIEAFAA-MYAKSERVVfvwgMGITQHA--HGVDNVRAI----VNLALlrGNIGRPG--------------AG 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 378 PLPLEpaagGCSGPAGG-------NHEPE---------GFKPRADKGkffaRTTAiqELIEPMITGEpypIKGLFAYGIN 441
Cdd:cd02767 348 LMPIR----GHSNVQGDrtmgiteKPFPEfldaleevfGFTPPRDPG----LDTV--EAIEAALEGK---VKAFISLGGN 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 442 LFHSIPNVPRTKEALKKLDLYVAID-VLPQEHVMWADV--ILPEATYLER-----------YDDLVAVAHKTpfIQLRVP 507
Cdd:cd02767 415 FAEAMPDPAATEEALRRLDLTVHVAtKLNRSHLVHGEEalILPCLGRTEIdmqaggaqavtVEDSMSMTHTS--RGRLKP 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 508 AHEPLFDtkPGWWIARELGIRLGlGEFFPWQTI-EEYLDTRLQSIGFDLETLKGMG-TLVQKGKPWLEDWEKEGRlpFGT 585
Cdd:cd02767 493 ASRVLLS--EEAIVAGIAGARLG-EAKPEWEILvEDYDRIRDEIAAVIYEGFADFNqRGDQPGGFHLPNGARERK--FNT 567
|
....
gi 2075248272 586 PSGK 589
Cdd:cd02767 568 PSGK 571
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
629-735 |
2.22e-20 |
|
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: 86.60 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 629 HTFARTQNNWvLMEMDPENEVWIHREEARRLGLKDGDYVILENQNGvrEGPVRVKATERIRKDCVYLVHGFGHKaplmkv 708
Cdd:cd02775 6 HSGTRTRNPW-LRELAPEPVVEINPEDAAALGIKDGDLVRVESRRG--SVVLRAKVTDGVPPGVVFLPHGWGHR------ 76
|
90 100
....*....|....*....|....*..
gi 2075248272 709 aHGRGASDNYLqTRYKLDPISGGAGLR 735
Cdd:cd02775 77 -GGRGGNANVL-TPDALDPPSGGPAYK 101
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
619-736 |
4.21e-18 |
|
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - containing oxidoreductases and tungsten formylmethanofuran dehydrogenase subunit d (FwdD) and molybdenum formylmethanofuran dehydrogenase subunit (FmdD); where the domain constitutes almost the entire subunit. The formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and has a molybdopterin dinucleotide cofactor. This domain corresponds to the C-terminal domain IV in dimethyl sulfoxide (DMSO)reductase which interacts with the 2-amino pyrimidone ring of both molybdopterin guanine dinucleotide molecules.
Pssm-ID: 426328 [Multi-domain] Cd Length: 110 Bit Score: 80.40 E-value: 4.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 619 YRLLYGRSPVHTFARTQNNWVLMEMDPENE-VWIHREEARRLGLKDGDYVILENQNGVREGPVRVkaTERIRKDCVYLVH 697
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKPEPEvVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKV--TDRVRPGVVFMPF 78
|
90 100 110
....*....|....*....|....*....|....*....
gi 2075248272 698 GFGHKAplmkvahgRGASDNYLqTRYKLDPISGGAGLRV 736
Cdd:pfam01568 79 GWWYEP--------RGGNANAL-TDDATDPLSGGPEFKT 108
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
1-316 |
3.05e-16 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 83.02 E-value: 3.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 1 MQRREFLKLSTLAAGALALRGSGPAKAL-------------KAPwyrqevksvyqiCEGCFWRCGIVAHAVGNRVYKVEG 67
Cdd:PRK13532 3 LSRRDFMKANAAAAAAAAAGLSLPAVANavvgsaqtaikwdKAP------------CRFCGTGCGVLVGTKDGRVVATQG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 68 YEANPKSRGRVCPRGQGMPQTTYDPDRLKRPLIRV-EGSQRGEGKYRVATWEEALDYVAKRMMKLKEEYGPEAIAFFGHG 146
Cdd:PRK13532 71 DPDAPVNRGLNCIKGYFLSKIMYGKDRLTQPLLRMkDGKYDKEGEFTPVSWDQAFDVMAEKFKKALKEKGPTAVGMFGSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 147 TGDSW----FVDFLPAAWGSpNAAKPSVAICTApretAAQWVFGRPIGGHEPI----DWENARYIVLIGHHIGEdTHN-- 216
Cdd:PRK13532 151 QWTIWegyaASKLMKAGFRS-NNIDPNARHCMA----SAVVGFMRTFGIDEPMgcydDIEAADAFVLWGSNMAE-MHPil 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 217 -TQLQDFALAlKRGAKVVVVdprfSTAAAK----AHLWLPIKPGTDTALLLAWIHVLIYEDLYDKEYVAKYTT------- 284
Cdd:PRK13532 225 wSRVTDRRLS-NPDVKVAVL----STFEHRsfelADNGIIFTPQTDLAILNYIANYIIQNNAVNWDFVNKHTNfrkgatd 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2075248272 285 ---------------------------GFEELKTHVKDFTPEWAEKHTEIPAEIIRQVA 316
Cdd:PRK13532 300 igyglrpthplekaaknpgtagksepiSFEEFKKFVAPYTLEKTAKMSGVPKEQLEQLA 358
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
2-702 |
5.72e-16 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 82.35 E-value: 5.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 2 QRREFLKlSTLAAGALALRGSGPAKALK------------------------APWYR------------QEVKsvYQICE 45
Cdd:PRK14991 4 TRRQLLK-GGLAAGGLAAFAAGYSDTAKraakgllngtsgkptrdrihgnslTPEYRvdaqgqlqpnpqQRVA--NTQCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 46 GCFWRCGIVAHA--VGNRVYKVEGYEANPKS--------------------------RGRVCPRGQGMPQTTYDPDRLKR 97
Cdd:PRK14991 81 GCWTQCGVRVRVdnATNKILRIAGNPYHPLStdhhidmstpvkeafeslsgesglegRSTACARGNAMLEQLDSPYRVLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 98 PLIRVegSQRGEGKYRVATWEEALDYVAkrmmklkeeygpEAIAFFGHGTgdswfVDFLPAAWG--SP-NAAKPS----- 169
Cdd:PRK14991 161 PLKRV--GKRGSGKWQRISFEQLVEEVV------------EGGDLFGEGH-----VDGLRAIRDldTPiDAKNPEygpka 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 170 --VAICTAPRETA-------AQWVFG-RPIGGH-------------------------EPiDWENARYIVLIGHHIGEDT 214
Cdd:PRK14991 222 nqLLVTNASDEGRdafikrfAFNSFGtRNFGNHgsycglayragsgalmgdldknphvKP-DWDNVEFALFIGTSPAQSG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 215 HNTQLQDFALALKR---GAKVVVVDPRF----STAAAKAHLWLPIKPGTDTALLLAWIHVLIYEDLYDKEY--------- 278
Cdd:PRK14991 301 NPFKRQARQLANARtrgNFEYVVVAPALplssSLAAGDNNRWLPIRPGTDSALAMGMIRWIIDNQRYNADYlaqpgvaam 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 279 -------------------------------------------------VAKYTTG-------------FEELKTHVKDF 296
Cdd:PRK14991 381 qaageaswtnathlviadpghprygqflrasdlglpfegeargdgedtlVVDAADGelvpatqaqparlFVEQYVTLADG 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 297 TP-----------EWAEKHT--------EIPAEIIRQVAREMAAHKPQAVLPPTRHTVwYGDDTYRMMALYYVNVLLGNY 357
Cdd:PRK14991 461 QRvrvksslqllkEAARKLSlaeyseqcGVPEAQIIALAEEFTSHGRKAAVISHGGTM-SGNGFYNAWAIMMLNALIGNL 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 358 GRKGGFYIAQSPYLEKYPTPPLPLEPAAGGCsGPAGGN--------HEPEGFKPRADKGK---------FFARTTAIQEL 420
Cdd:PRK14991 540 NLKGGVVVGGGKFPGFGDGPRYNLASFAGKV-KPKGVSlsrskfpyEKSSEYRRKVEAGQspypakapwYPFVAGLLTEM 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 421 IEPMITGEPYPIKGLFAYGINLFHSIPNV-PRTKEALK---KLDLYVAIDVLPQEHVMWADVILPEATYLERYdDLVAVA 496
Cdd:PRK14991 619 LTAALEGYPYPLKAWINHMSNPIYGVPGLrAVIEEKLKdpkKLPLFISIDAFINETTALADYIVPDTHTYESW-GFTAPW 697
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 497 HKTPF--IQLRVPAHEPLFD-TKPGWWIARE-----LGIRLGL------------GEFFPWQTIEEYLDTRLQSIGFDLE 556
Cdd:PRK14991 698 GGVPTkaSTARWPVVEPRTAkTADGQPVCMEsfliaVAKRLQLpgfgdnaikdaqGNTHPLNRAEDFYLRGAANIAYLGK 777
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 557 T-----------LKG----MGTLVQKGKPwlEDWEKEGRLPfgTPSGKIELYCQAFKkaGHQPLPVFTPP-----EEPP- 615
Cdd:PRK14991 778 TpvadasdediaLTGvsriLPALQATLKP--DEVRRVAFIY--ARGGRFAPAESAYD--EERMGNRWKKPlqiwnEDVAa 851
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 616 -------------PGFY--RLLYGrSPVHTfARTQNNWVLMEMD--------------------PENEVWIHREEARRLG 660
Cdd:PRK14991 852 arhsmtgerysgcPTWYppRLADG-TPLRE-QFPESQWPLLLISfksnlmssmsiasprlrqvkPANPVALNPQDAARLG 929
|
970 980 990 1000
....*....|....*....|....*....|....*....|..
gi 2075248272 661 LKDGDYVILENQNGVREGPVRVKATerIRKDCVYLVHGFGHK 702
Cdd:PRK14991 930 IQHGDRVRISTPGGSVVAQASVLNG--VMPGVIAIEHGYGHR 969
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
72-542 |
4.35e-15 |
|
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: 79.06 E-value: 4.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 72 PKSRGRVCPRGQGMPQTTYDPD------RLKRPLIRVEGSQRGegkyrvATWEEALDYVAKRMMKLKEEYGPE-AIAF-- 142
Cdd:cd02756 89 PVNSGNYSTRGGTNAERIWSPDnrvgetRLTTPLVRRGGQLQP------TTWDDAIDLVARVIKGILDKDGNDdAVFAsr 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 143 FGHGTGDSWFVD------FLPAAWGSPNaakpsVAICTAPRETAAQWVfGRPIGGHEP----IDWENARYIVLIGHHIGE 212
Cdd:cd02756 163 FDHGGGGGGFENnwgvgkFFFMALQTPF-----VRIHNRPAYNSEVHA-TREMGVGELnnsyEDARLADTIVLWGNNPYE 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 213 DTHNTQLQDFALALkRGAKV------------------VVVDPRFS-TAAAKAH-------LWLPIKPGTDTALLLAwIH 266
Cdd:cd02756 237 TQTVYFLNHWLPNL-RGATVsekqqwfppgepvppgriIVVDPRRTeTVHAAEAaagkdrvLHLQVNPGTDTALANA-IA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 267 VLIYEDLydKEYVAKyttgfeelkthvkdftpewAEKHTEIPAEIIRQVAREMAAHK-----PQAVLPPTRHTVWyGDDT 341
Cdd:cd02756 315 RYIYESL--DEVLAE-------------------AEQITGVPRAQIEKAADWIAKPKeggyrKRVMFEYEKGIIW-GNDN 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 342 YRMM-ALYYVNVLLGNYGRKGGFYIAQSPYLEKYPTPPLPlepaaggcsGPagGNHEPEGFKPRAD------KGKFFArt 414
Cdd:cd02756 373 YRPIySLVNLAIITGNIGRPGTGCVRQGGHQEGYVRPPPP---------PP--PWYPQYQYAPYIDqllisgKGKVLW-- 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 415 taiqeliepMITGEPY---PIKGLFAYGIN---------LFHSIPNVPRTKEALKKLDL---------YVAIDVLPQEHV 473
Cdd:cd02756 440 ---------VIGCDPYkttPNAQRLRETINhrsklvtdaVEAALYAGTYDREAMVCLIGdaiqpgglfIVVQDIYPTKLA 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 474 MWADVILPEATYLERYDDLVAVAHKTpfIQLRVPAHEPLFDTKPGWWIARELGIRL-------GLGEF-------FPWQT 539
Cdd:cd02756 511 EDAHVILPAAANGEMNETSMNGHERR--LRLYEKFMDPPGEAMPDWWIAAMIANRIyelyqeeGKGGSaqyqffgFIWKT 588
|
...
gi 2075248272 540 IEE 542
Cdd:cd02756 589 EED 591
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
629-743 |
6.13e-15 |
|
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: 71.77 E-value: 6.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 629 HTFARTQNNWVLMEMDPENEVWIHREEARRLGLKDGDYVILENQNGvrEGPVRVKATERIRKDCVYLVHGFGHKAPlmkv 708
Cdd:cd00508 17 HTGTMTRRSPRLAALAPEPFVEIHPEDAARLGIKDGDLVRVSSRRG--SVVVRARVTDRVRPGTVFMPFHWGGEVS---- 90
|
90 100 110
....*....|....*....|....*....|....*
gi 2075248272 709 ahgrGASDNYLqTRYKLDPISGGAGLRVNFVKLEK 743
Cdd:cd00508 91 ----GGAANAL-TNDALDPVSGQPEFKACAVRIEK 120
|
|
| NarG |
COG5013 |
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and ... |
75-283 |
2.40e-14 |
|
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 444037 [Multi-domain] Cd Length: 1231 Bit Score: 77.17 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 75 RGrvCPRGQGMPQTTYDPDRLKRPLIR-----------------VEG---------------SQRGEGKYRVATWEEALD 122
Cdd:COG5013 94 RG--CPRGASFSWYTYSPTRVKYPYVRgvllelwreararhgdpVEAwasivedpekrrrykSARGKGGFVRATWDEANE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 123 YVAKRMMKLKEEYGPEAIAFF---------GHGTG---------------DsWFVDfLPAAwgSPNaakpsvaictapre 178
Cdd:COG5013 172 IIAAANVYTIKKYGPDRVAGFspipamsmvSYAAGarflsliggvmlsfyD-WYAD-LPPA--SPQ-------------- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 179 taaqwVFGR----PigghEPIDWENARYIVLIGHHIGE----DTHNtqlqdFALALKRGAKVVVVDPRFSTAAAKAHLWL 250
Cdd:COG5013 234 -----VWGEqtdvP----ESADWYNSGYLIMWGSNVPQtrtpDAHF-----MTEARYKGTKVVVVSPDYAENTKFADEWL 299
|
250 260 270
....*....|....*....|....*....|....*....
gi 2075248272 251 PIKPGTDTALLLAWIHVLIYEDLYDK------EYVAKYT 283
Cdd:COG5013 300 PPKQGTDAALAMAMGHVILKEFHVDRqvpyftDYARRYT 338
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
37-91 |
6.11e-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: 66.50 E-value: 6.11e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2075248272 37 VKSVYQICEGCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRVCPRGQGMPQTTYD 91
Cdd:smart00926 1 EKWVPTVCPLCGVGCGLLVEVKDGRVVRVRGDPDHPVNRGRLCPKGRAGLEQVYS 55
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
31-259 |
1.82e-12 |
|
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: 70.25 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 31 PWYRQEVKSvyqICEGCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRVCPRG----QGMpqttYDPDRLKRPLIRvegsq 106
Cdd:COG1034 212 PWELKKTPS---ICPHCSVGCNIRVDVRGGKVYRVLPRENEAVNEEWLCDKGrfgyDGL----NSPDRLTRPLVR----- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 107 rGEGKYRVATWEEALDYVAKRMMKLKEEYGPEAIAFFGhgtgdswfvdflpaawGSPNAAkpsvAICTAPRETAAQWVFg 186
Cdd:COG1034 280 -KDGELVEASWEEALAAAAEGLKALKKAENSVGAALLG----------------ALPDAA----AILEAAEAGKLKALV- 337
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2075248272 187 rpIGGHEPIDWENARyivlighhigedthntqlqdFALALKRGAKVVVVDPRFSTAAAKAHLWLPIKPGTDTA 259
Cdd:COG1034 338 --LLGADPYDLDPAA--------------------ALAALAKADFVVVLDHFGSATAERADVVLPAAAFAEKS 388
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
625-743 |
2.17e-12 |
|
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: 65.01 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 625 RSPVHTfARTQNNWVLMEMDPENEVWIHREEARRLGLKDGDYVILENQNGVREGPVRVkaTERIRKDCVYLVHGFGHKAp 704
Cdd:cd02780 9 KSNLNS-HRSANAPWLKEIKPENPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKV--TEGVRPGVVAIEHGYGHWA- 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2075248272 705 LMKVAHGR--------------------GASDNYLQTRYKLDPISGGAGLRVNFVKLEK 743
Cdd:cd02780 85 YGAVASTIdgkdlpgdawrgagvnindiGLVDPSRGGWSLVDWVGGAAARYDTPVKIEK 143
|
|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
38-91 |
2.61e-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: 59.23 E-value: 2.61e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2075248272 38 KSVYQICEGCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRVCPRGQGMPQTTYD 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 |
3.93e-11 |
|
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: 60.71 E-value: 3.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 629 HTFARTQNNWVLMEMDPENEVWIHREEARRLGLKDGDYVILENqngvREGPVRVKA--TERIRKDCVYLvhgfghkaPLm 706
Cdd:cd02790 17 HTGTMTRRAEGLDAIAPEEYVEINPEDAKRLGIEDGEKVRVSS----RRGSVEVRArvTDRVPEGVVFM--------PF- 83
|
90 100 110
....*....|....*....|....*....|....*..
gi 2075248272 707 kvaHGRGASDNYLqTRYKLDPISGGAGLRVNFVKLEK 743
Cdd:cd02790 84 ---HFAEAAANLL-TNAALDPVAKIPEFKVCAVRVEK 116
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
629-743 |
1.02e-10 |
|
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: 59.54 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 629 HTFARTQNNWVLMEMDPENEVWIHREEARRLGLKDGDYVILENqngvREGPVRVKA--TERIRKDCVYLVHGFGHKAPlm 706
Cdd:cd02792 17 HGGNMTRNSPYLAELQPEMFVEISPELAAERGIKNGDMVWVSS----PRGKIKVKAlvTDRVKPHEVGIPYHWGGMGL-- 90
|
90 100 110
....*....|....*....|....*....|....*..
gi 2075248272 707 kvahGRGASDNYLqTRYKLDPISGGAGLRVNFVKLEK 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 |
6.56e-10 |
|
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239182 [Multi-domain] Cd Length: 130 Bit Score: 57.70 E-value: 6.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 618 FYRLLYGRSPVHTfaRTQNNWV--LMEMDPENEVWIHREEARRLGLKDGDYVILENQNGvrEGPVRVKATERIRKDCVYL 695
Cdd:cd02781 4 LILTTGARSYYYF--HSEHRQLpsLRELHPDPVAEINPETAAKLGIADGDWVWVETPRG--RARQKARLTPGIRPGVVRA 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2075248272 696 VHG--FGHKAPLMKVAHGRGASD-NYLQTRYKLDPISGGAGLR 735
Cdd:cd02781 80 EHGwwYPEREAGEPALGGVWESNaNALTSDDWNDPVSGSSPLR 122
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
632-744 |
1.91e-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: 56.25 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 632 ARTQNNWV-----LMEMDPENEVWIHREEARRLGLKDGDYVILENQNGVREGPVRVkaTERIRKDCVYLVHGFGHKAPLM 706
Cdd:cd02782 13 LRSNNSWLhndprLVKGRNRCTLRIHPDDAAALGLADGDKVRVTSAAGSVEAEVEV--TDDMMPGVVSLPHGWGHDYPGV 90
|
90 100 110
....*....|....*....|....*....|....*....
gi 2075248272 707 KVAHGR-GASDNYLQTRYKLDPISGGAGLRVNFVKLEKA 744
Cdd:cd02782 91 SGAGSRpGVNVNDLTDDTQRDPLSGNAAHNGVPVRLARV 129
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
417-545 |
2.97e-09 |
|
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440657 [Multi-domain] Cd Length: 453 Bit Score: 59.85 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 417 IQELIEPMITGepyPIKGLFAYGINLFHSIPNvpRTKEALKKLDLYVAIDVLPQEHVMWADVILPEATYLERYDDLVAVA 496
Cdd:COG1034 321 AAAILEAAEAG---KLKALVLLGADPYDLDPA--AALAALAKADFVVVLDHFGSATAERADVVLPAAAFAEKSGTFVNLE 395
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2075248272 497 HKtpfIQLRVPAHEPLFDTKPGWWIARELGIRLGLGefFPWQTIEEYLD 545
Cdd:COG1034 396 GR---VQRFNAAVPPPGEARPDWRVLRALANALGAG--LPYDSLEEVRA 439
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
629-743 |
2.97e-09 |
|
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: 55.38 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 629 HTFARTQ----NNWVLMEMDPeNEVWIHREEARRLGLKDGDYVILENQNGVREGPVRVkaTERIRKDCVYLVHGFGHKAP 704
Cdd:cd02794 9 HYKRRTHstfdNVPWLREAFP-QEVWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKV--TERIMPGVVALPQGAWYEPD 85
|
90 100 110
....*....|....*....|....*....|....*....
gi 2075248272 705 LMKVAHgrGASDNYLqTRYKLDPISGGAGLRVNFVKLEK 743
Cdd:cd02794 86 ANGIDK--GGCINTL-TGLRPSPLAKGNPQHTNLVQVEK 121
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
629-744 |
1.65e-07 |
|
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. This CD (MopB_CT_Nitrate-R-Nap) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
Pssm-ID: 239192 [Multi-domain] Cd Length: 122 Bit Score: 50.65 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 629 HTFARTQNNWVLMEMDPENEVWIHREEARRLGLKDGDYVILENQNGVREGPVRVkaTERIRKDCVYLVHGFGhkaplmkV 708
Cdd:cd02791 17 HTMTRTGRVPRLNAHVPEPYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRV--TDRVRPGEVFVPMHWG-------D 87
|
90 100 110
....*....|....*....|....*....|....*.
gi 2075248272 709 AHGRGASDNYLqTRYKLDPISGGAGLRVNFVKLEKA 744
Cdd:cd02791 88 QFGRSGRVNAL-TLDATDPVSGQPEFKHCAVRIEKV 122
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|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
90-237 |
6.38e-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: 52.36 E-value: 6.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 90 YDPDRLKRPLIRVEGsqrgegKYRVATWEEALDYVAKRMMKLKEEYGPEAIAFFG--HGTGDSWFV-DFLPAAWGSPNaa 166
Cdd:cd02772 50 NSEDRLTKPMIKKDG------QWQEVDWETALEYVAEGLSAIIKKHGADQIGALAspHSTLEELYLlQKLARGLGSDN-- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 167 kpsvaICTAPRET---------AAQWvFGRPIGghepiDWENARYIVLIGHHIGEDtH---NTQLQDfalALKRGAKVVV 234
Cdd:cd02772 122 -----IDHRLRQSdfrddakasGAPW-LGMPIA-----EISELDRVLVIGSNLRKE-HpllAQRLRQ---AVKKGAKLSA 186
|
...
gi 2075248272 235 VDP 237
Cdd:cd02772 187 INP 189
|
|
| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
623-733 |
1.17e-06 |
|
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. This CD (MopB_CT_Nitrate-R-NarG-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239177 [Multi-domain] Cd Length: 141 Bit Score: 48.53 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 623 YGRSPVHTFARTqNNWVLMEMDPENEVWIHREEARRLGLKDGDYVILENQNGVREgpVRVKATERIRKDCVYLVHGFGH- 701
Cdd:cd02776 8 HGKWSIHSTYRD-NLLMLRLQRGGPVVWMNPKDAAELGIKDNDWVEVFNDNGVVV--ARAKVSPRIPRGTVFMYHAQERh 84
|
90 100 110
....*....|....*....|....*....|....*
gi 2075248272 702 -KAPLMKVAHGRGASDNYLqTRYKLDP--ISGGAG 733
Cdd:cd02776 85 vNVPGSKLTGKRGGIHNSV-TRVRIKPthLVGGYG 118
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
75-149 |
1.53e-05 |
|
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: 48.05 E-value: 1.53e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2075248272 75 RGRVCPRGqgmpqtTYDPDRLKRPLIRvegsqrGEGKYRVATWEEALDYVAKRMmklkEEYGPEAIAFFGHGTGD 149
Cdd:cd02768 41 KGRFGYDG------LNSRQRLTQPLIK------KGGKLVPVSWEEALKTVAEGL----KAVKGDKIGGIAGPRAD 99
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
647-698 |
2.79e-05 |
|
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: 44.11 E-value: 2.79e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2075248272 647 NEVWIHREEARRLGLKDGDYVILENQNGVREGPVRVkaTERIRKDCVYLVHG 698
Cdd:cd02777 34 EPVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARV--TDRIMPGVVALPEG 83
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|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
619-684 |
1.99e-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: 41.58 E-value: 1.99e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2075248272 619 YRLLY----GRSPVH-TFArtqNNWVLMEMDPENEVWIHREEARRLGLKDGDYVILENQngvrEGPVRVKA 684
Cdd:cd02785 2 YPLACiqrhSRFRVHsQFS---NVPWLLELQPEPRVKINPIDAAARGIAHGDLVEVYND----RGSVVCKA 65
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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 |
3.83e-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: 43.41 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 94 RLKRPLIRvegsqrGEGKYRVATWEEALDYVAKRMMKLKeeygPEAIAFFGHGTGD--SWFV--DFLpAAWGSPNAAKPS 169
Cdd:cd02773 53 RLDKPYIR------KNGKLKPATWEEALAAIAKALKGVK----PDEIAAIAGDLADveSMVAlkDLL-NKLGSENLACEQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 170 VAIcTAPRETAAQWVFGRPIGGhepidWENARYIVLIGHHIGED--THNTQLQDFALAlkRGAKVVVVDPRFSTAAAKAH 247
Cdd:cd02773 122 DGP-DLPADLRSNYLFNTTIAG-----IEEADAVLLVGTNPRFEapVLNARIRKAWLH--GGLKVGVIGPPVDLTYDYDH 193
|
170
....*....|....
gi 2075248272 248 LwlpikpGTDTALL 261
Cdd:cd02773 194 L------GTDAKTL 201
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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 ... |
43-133 |
6.89e-04 |
|
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: 42.76 E-value: 6.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 43 ICEGCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRVCPRGQGMPQTTYDPDRLKRPLIrvegsqRGEGKYRVATWEEALD 122
Cdd:cd02771 3 ICHHCSVGCNISLGERYGELRRVENRYNGAVNHYFLCDRGRFGYGYVNSRDRLTQPLI------RRGGTLVPVSWNEALD 76
|
90
....*....|.
gi 2075248272 123 YVAkrmMKLKE 133
Cdd:cd02771 77 VAA---ARLKE 84
|
|
| MopB_CT_2 |
cd02783 |
The MopB_CT_2 CD includes a group of related uncharacterized bacterial and archaeal ... |
634-687 |
1.51e-03 |
|
The MopB_CT_2 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239184 [Multi-domain] Cd Length: 156 Bit Score: 39.75 E-value: 1.51e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2075248272 634 TQNNWvLMEMDPENEVWIHREEARRLGLKDGDYVILENQNGVREGPVRVKATER 687
Cdd:cd02783 20 SQNAW-LRQIHTRNYLYMHPKTAKELGIKDGDWVWVESVNGRVKGQARFTETVE 72
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
630-739 |
1.90e-03 |
|
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239187 [Multi-domain] Cd Length: 116 Bit Score: 38.80 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075248272 630 TFARTQNnwvLMEMDPENEVWIHREEARRLGLKDGDYVILENQNGVREGPVRVkaTERIRKDCVYLVHGFGHKAplmkVA 709
Cdd:cd02786 17 TFANLPE---LRAKEGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKV--TDDVPPGVVVAEGGWWREH----SP 87
|
90 100 110
....*....|....*....|....*....|
gi 2075248272 710 HGRGAsdNYLqTRYKLDPISGGAGLRVNFV 739
Cdd:cd02786 88 DGRGV--NAL-TSARLTDLGGGSTFHDTRV 114
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