|
Name |
Accession |
Description |
Interval |
E-value |
| arsenite_ox_L |
TIGR02693 |
arsenite oxidase, large subunit; This model represents the large subunit of an arsenite ... |
9-841 |
0e+00 |
|
arsenite oxidase, large subunit; This model represents the large subunit of an arsenite oxidase complex. The small subunit is a Rieske protein. Homologs to both large and small subunits that score in the gray zone between the set trusted and noise bit score cutoffs for the respective models are found in Aeropyrum pernix K1 and in Sulfolobus tokodaii str. 7. This enzyme acts in energy metabolim by arsenite oxidation, rather than detoxification by reduction of arsenate to arsenite prior to export. [Energy metabolism, Electron transport]
Pssm-ID: 274261 [Multi-domain] Cd Length: 806 Bit Score: 1419.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 9 RLPIPPKNAKVYNQVCQYCTVGCGYKVYVWPVGEEGGVKPEQNAFGLDLSTPQPPLAGQSYTETMHAVTVGRDGRQYNVV 88
Cdd:TIGR02693 1 RLPIPPANAKKHNVTCHFCIVGCGYHVYTWPINKEGGTDPQQNAFGLDLSEQQQPESDAWYTPSMYNVVKQRDGRDVNVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 89 IVPAKDSPINRGNYSIRGGTNALTVWSLDRGTQDRLTYPLLRVGDQFQAITWQDALTLMGLLIKGIRDRDGNDDnIAVKC 168
Cdd:TIGR02693 81 IKPDKECVVNSGLGSVRGGRMAETSFSEDRNTQDRLTYPLVWRGDQMQPTSWDDALDLVARLTKKIVDEKGEDD-IIVSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 169 FDHGGSGQGFEDNYAAGKLFFAALSVKHIAIHNRPAYNSEVWGSRERGVHELNYTYEDARLADTIVLWGANSYETATVFY 248
Cdd:TIGR02693 160 FDHGGAGGGFENTWGTGKLYFEAMKVKNIRIHNRPAYNSEVHGTREMGVGELNNCYEDAELADTIVAVGTNAYETQTNYF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 249 VEHMLPNIQGATVAEKQQAFdPGEPAEPGYLIVIDPRKTSSYTVAAQVAPDRVMLLRPNLGTDYILANAIARAVWEKGYY 328
Cdd:TIGR02693 240 LNHWLPNLRGETLGKKKQLF-PGEPHEPGRIIIVDPRRTVSVNAAEQTAADRVLHLAINSGTDLALFNALFTYVADKGWV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 329 DMAYLQARTDMTLFEEyKAKSLKLSvpydefMAQAERITGVSRAEIEKAADWIAKPKAGRFKRRTLTIYEKGIIWNMKNY 408
Cdd:TIGR02693 319 DRDFIDKSGHLSSFED-AVKGCRMS------IAEAARITGVSAAQIIKAAEWIGKPKAGGKRRRTMFGYEKGIIWGNDNY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 409 DQVAAIVQLAVLTHNIGRPGTGCGRQGGHQEGYVRPPAptpgsIYRGGPPVNVDKFLIEGKGKFYWVIANDPYLSTPNNQ 488
Cdd:TIGR02693 392 RTNGALVNLALATGNIGRPGTGCVRLGGHQEGYVRPPD-----AHVGGPAAYVDQLLIGGKGGVHHIWGCDHYKTTLNAQ 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 489 VFRKRIHERTEKLTKALGAGGEpGTIQERAQKILDILYQdpDALFLVVQDIYMTETARDAHLILPAAGWGEANETSINCn 568
Cdd:TIGR02693 467 EFRRVYKKRTDMVKDAMSAAPY-GDREEMVNAIVDAINQ--GGLFAVNVDIYPTKIGEAAHLILPAATSGEMNLTSMNG- 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 569 SRLLRLYEKFMDPPGEAKPDWEIFKWVGLRIAELYRAEGKFEEAKKFEfGKNWKTDEDVFLAGAEEFRDNTVseEDEAVL 648
Cdd:TIGR02693 543 ERRMRLTEKFMDPPGQAMPDCLIAARLANTMERVYTAEGKVEYAKQFK-GFDWKTEEDAFMDGYNKNRDNTV--EDEAAH 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 649 EAENYKGVTYKLLKELGQKGIQTPVRRDPKtGKLVGTVRRYTYR-FGTEDGKFKWYgTDDWEGYPAEVAKYLEpgmaEKY 727
Cdd:TIGR02693 620 GGENYKFVTYELLSAMGTNGFQEPATRFTD-GKIEGTQRLYTDGvFSTDDGKARFM-DAPWRGLPAPGKQQQK----DKH 693
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 728 PFWVTTGRAQTIWQTAYHDRHLPEKALALPLPYVEVNPEDAKRLGLKSGDLVEVYNEEGNGTFLVYVTDAVKPGTLFLVM 807
Cdd:TIGR02693 694 KFWINNGRANVVWQSAYHDQENDFVMDRFPLPYIEMNPEDAAELGLKEGDLVEVYNDAGATQAMAYPTPTAKPGETFMLF 773
|
810 820 830
....*....|....*....|....*....|....
gi 55773483 808 YHWRGTSNSLVTGYTDpKTTIPWYKGTRANLRKV 841
Cdd:TIGR02693 774 GFPTGVQGNVTTAGTD-ELIIPNYKGTWGNIRKI 806
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
8-711 |
0e+00 |
|
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: 1146.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 8 DRLPIPPKNAKVYNQVCQYCTVGCGYKVYVWPVGEEGGVKPEQNAFGLDLSTPQPPLAGQSYTETMHAVTVGRDGRQYNV 87
Cdd:cd02756 1 DRVPLPPVNAERYNVTCHFCIVGCGYHVYVWPVGEEGGPSPGQNAIGYDLVDQVPPLNLQWYPKTMHYVVVTQDGREVYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 88 VIVPAKDSPINRGNYSIRGGTNALTVWSLDR-GTQDRLTYPLLRVGDQFQAITWQDALTLMGLLIKGIRDRDGNDDNIAV 166
Cdd:cd02756 81 VIVPDKECPVNSGNYSTRGGTNAERIWSPDNrVGETRLTTPLVRRGGQLQPTTWDDAIDLVARVIKGILDKDGNDDAVFA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 167 KCFDHGGSGQGFEDNYAAGKLFFAALSVKHIAIHNRPAYNSEVWGSRERGVHELNYTYEDARLADTIVLWGANSYETATV 246
Cdd:cd02756 161 SRFDHGGGGGGFENNWGVGKFFFMALQTPFVRIHNRPAYNSEVHATREMGVGELNNSYEDARLADTIVLWGNNPYETQTV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 247 FYVEHMLPNIQGATVAEKQQAFDPGEPAEPGYLIVIDPRKTSSYTVAAQVA-PDRVMLLRPNLGTDYILANAIARAVWEk 325
Cdd:cd02756 241 YFLNHWLPNLRGATVSEKQQWFPPGEPVPPGRIIVVDPRRTETVHAAEAAAgKDRVLHLQVNPGTDTALANAIARYIYE- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 326 gyydmaylqartdmtlfeeykakslklsvPYDEFMAQAERITGVSRAEIEKAADWIAKPKAGRFKRRTLTIYEKGIIWNM 405
Cdd:cd02756 320 -----------------------------SLDEVLAEAEQITGVPRAQIEKAADWIAKPKEGGYRKRVMFEYEKGIIWGN 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 406 KNYDQVAAIVQLAVLTHNIGRPGTGCGRQGGHQEGYVRPPAPTPGSIYRGGPPVNVDKFLIEGKGKFYWVIANDPYLSTP 485
Cdd:cd02756 371 DNYRPIYSLVNLAIITGNIGRPGTGCVRQGGHQEGYVRPPPPPPPWYPQYQYAPYIDQLLISGKGKVLWVIGCDPYKTTP 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 486 NNQVFRKRIHERTEKLTKALGAGGEPGTIQERAQKILDILYQDPDALFLVVQDIYMTETARDAHLILPAAGWGEANETSI 565
Cdd:cd02756 451 NAQRLRETINHRSKLVTDAVEAALYAGTYDREAMVCLIGDAIQPGGLFIVVQDIYPTKLAEDAHVILPAAANGEMNETSM 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 566 NCNSRLLRLYEKFMDPPGEAKPDWEIFKWVGLRIAELYRAEGKFEEAKKFEFGKNWKTDEDVFLAGAEEFRDNTVSEEDE 645
Cdd:cd02756 531 NGHERRLRLYEKFMDPPGEAMPDWWIAAMIANRIYELYQEEGKGGSAQYQFFGFIWKTEEDNFMDGSQEFADGGEFSEDY 610
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55773483 646 AVLEAENYKGVTYKLLKELGQKGIQTPVRRDPKTGKLVGTVRRYTYRFGTEDGKFKWYGTDDWEGY 711
Cdd:cd02756 611 YVLGQERYEGVTYNRLKAVGVNGIQLPVTTDTVTKILVTNVLRTEGVFDTEDGKAYVIDLAPWPGL 676
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
23-843 |
1.08e-140 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 432.77 E-value: 1.08e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 23 VCQYCTVGCGYKVYVwpvgeeggvkpeqnafgldlstpqpplagqsytetmhavtvgRDGRQynVVIVPAKDSPINRGNY 102
Cdd:COG3383 10 VCPYCGVGCGIDLEV------------------------------------------KDGKI--VKVEGDPDHPVNRGRL 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 103 SIRGGTNALTVwsldrGTQDRLTYPLLRVGDQFQAITWQDALTLMGLLIKGIRDRDGNDdniAVKCFdhgGSGQGF-EDN 181
Cdd:COG3383 46 CVKGRFGFEFV-----NSPDRLTTPLIRRGGEFREVSWDEALDLVAERLREIQAEHGPD---AVAFY---GSGQLTnEEN 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 182 YAAGKLFFAALSVKHIAIHNRPAYNSEVWGSRER-GVHELNYTYEDARLADTIVLWGANSYETATVFYvEHMLpniqgat 260
Cdd:COG3383 115 YLLQKLARGVLGTNNIDNNARLCMASAVAGLKQSfGSDAPPNSYDDIEEADVILVIGSNPAEAHPVLA-RRIK------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 261 vaekqQAFDPGepaepGYLIVIDPRKTSSytvaAQVApDRVMLLRPnlGTDYILANAIARAVWEKGYYDMAYLQARTDmt 340
Cdd:COG3383 187 -----KAKKNG-----AKLIVVDPRRTET----ARLA-DLHLQIKP--GTDLALLNGLLHVIIEEGLVDEDFIAERTE-- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 341 LFEEYKAKSLKLSVpydefmAQAERITGVSRAEIEKAADWIAKPKagrfkrRTLTIYEKGIIWNMKNYDQVAAIVQLAVL 420
Cdd:COG3383 248 GFEELKASVAKYTP------ERVAEITGVPAEDIREAARLIAEAK------RAMILWGMGVNQHTQGTDNVNAIINLALA 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 421 THNIGRPGTGCGR-------QG------------GHQEG-------------YVRPPAPTPGSiyrggPPVNVDKFLIEG 468
Cdd:COG3383 316 TGNIGRPGTGPFPltgqnnvQGgrdmgalpnvlpGYRDVtdpehrakvadawGVPPLPDKPGL-----TAVEMFDAIADG 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 469 KGKFYWVIANDPYLSTPNnqvfRKRIHERTEKLTkalgaggepgtiqeraqkildilyqdpdalFLVVQDIYMTETARDA 548
Cdd:COG3383 391 EIKALWIIGENPAVSDPD----ANHVREALEKLE------------------------------FLVVQDIFLTETAEYA 436
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 549 HLILPAAGWGEANETSINCNSRLLRLYeKFMDPPGEAKPDWEIfkwvglrIAELyraegkfeeAKKFEFGKNWKTDEDVF 628
Cdd:COG3383 437 DVVLPAASWAEKDGTFTNTERRVQRVR-KAVEPPGEARPDWEI-------IAEL---------ARRLGYGFDYDSPEEVF 499
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 629 lagaeefrdntvseeDEAVLEAENYKGVTYKLLKELGqkGIQTPVRrdpkTGKLVGTVRRYTYRFGTEDGKFKWYGTDdW 708
Cdd:COG3383 500 ---------------DEIARLTPDYSGISYERLEALG--GVQWPCP----SEDHPGTPRLFTGRFPTPDGKARFVPVE-Y 557
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 709 EGyPAEVAkylepgmAEKYPFWVTTGRAQTIWQTAYHDRHLPEKALALPLPYVEVNPEDAKRLGLKSGDLVEVYNEEGNG 788
Cdd:COG3383 558 RP-PAELP-------DEEYPLVLTTGRLLDQWHTGTRTRRSPRLNKHAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGEV 629
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*
gi 55773483 789 TFLVYVTDAVKPGTLFLVMYHWRGTSNSLVTGYTDPKTTIPWYKGTRANLRKVAG 843
Cdd:COG3383 630 VLRARVTDRVRPGTVFMPFHWGEGAANALTNDALDPVSKQPEYKACAVRVEKVAE 684
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
10-843 |
2.51e-124 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 389.97 E-value: 2.51e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 10 LPIPPKNAKVYNQVCQYCTVGCGYKVYVwpvgeeggvkpeqnafgldlstpqpplagqsytetmhavtvgRDGRqynVV- 88
Cdd:COG0243 14 AALEAAGTKTVKTTCPGCGVGCGLGVKV------------------------------------------EDGR---VVr 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 89 IVPAKDSPINRGNYSIRGGTNALTVWSldrgtQDRLTYPLLRVG----DQFQAITWQDALTLMGLLIKGIRDRDGNDdni 164
Cdd:COG0243 49 VRGDPDHPVNRGRLCAKGAALDERLYS-----PDRLTYPMKRVGprgsGKFERISWDEALDLIAEKLKAIIDEYGPE--- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 165 AVKCFDHGGSGQGF--EDNYAAGKlFFAALSVKHIAIHNRPAYNSEVWGSRE-RGVHELNYTYEDARLADTIVLWGANSY 241
Cdd:COG0243 121 AVAFYTSGGSAGRLsnEAAYLAQR-FARALGTNNLDDNSRLCHESAVAGLPRtFGSDKGTVSYEDLEHADLIVLWGSNPA 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 242 ETATvfyveHMLPNIQGAtvAEKQQAfdpgepaepgYLIVIDPRKTSSytvaAQVApDRVMLLRPnlGTDYILANAIARA 321
Cdd:COG0243 200 ENHP-----RLLRRLREA--AKKRGA----------KIVVIDPRRTET----AAIA-DEWLPIRP--GTDAALLLALAHV 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 322 VWEKGYYDMAYLQARTDMtlFEEYKAkslkLSVPYDefMAQAERITGVSRAEIEKAADWIAKpkagrfKRRTLTIYEKGI 401
Cdd:COG0243 256 LIEEGLYDRDFLARHTVG--FDELAA----YVAAYT--PEWAAEITGVPAEDIRELAREFAT------AKPAVILWGMGL 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 402 IWNMKNYDQVAAIVQLAVLTHNIGRPGTGCGRQGGHqegyvrppaptpgSIYRGGPPvnvdkfliegKGKFYWVIANDPY 481
Cdd:COG0243 322 QQHSNGTQTVRAIANLALLTGNIGKPGGGPFSLTGE-------------AILDGKPY----------PIKALWVYGGNPA 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 482 LSTPNnqvfrkriherTEKLTKALgaggepgtiqeraqkildilyQDPDalFLVVQDIYMTETARDAHLILPAAGWGEAN 561
Cdd:COG0243 379 VSAPD-----------TNRVREAL---------------------RKLD--FVVVIDTFLTETARYADIVLPATTWLERD 424
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 562 ETSINCNSRLLRLYEKFMDPPGEAKPDWEIFkwvglriAELyraegkfeeAKKFEFGK---NWKTDEDVFlagaeefrdn 638
Cdd:COG0243 425 DIVTNSEDRRVHLSRPAVEPPGEARSDWEIF-------AEL---------AKRLGFEEafpWGRTEEDYL---------- 478
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 639 tvseedEAVLEAENYKGVTYKLLKELGqkGIQTPVRRDPKTgklvgtvrRYTYRFGTEDGKFKWYgtDDWEGYPAeVAKY 718
Cdd:COG0243 479 ------RELLEATRGRGITFEELREKG--PVQLPVPPEPAF--------RNDGPFPTPSGKAEFY--SETLALPP-LPRY 539
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 719 LEP-----GMAEKYPFWVTTGRAQTIWQTAYHdrHLPEKALALPLPYVEVNPEDAKRLGLKSGDLVEVYNEEGNGTFLVY 793
Cdd:COG0243 540 APPyegaePLDAEYPLRLITGRSRDQWHSTTY--NNPRLREIGPRPVVEINPEDAAALGIKDGDLVRVESDRGEVLARAK 617
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 55773483 794 VTDAVKPGTLFLVMYHWR-------GTSNSLVTGYTDPKTTIPWYKGTRANLRKVAG 843
Cdd:COG0243 618 VTEGIRPGVVFAPHGWWYepaddkgGNVNVLTPDATDPLSGTPAFKSVPVRVEKAAA 674
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
23-699 |
2.66e-76 |
|
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: 259.08 E-value: 2.66e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 23 VCQYCTVGCGYKVYVwpvgeeggvkpeqnafgldlstpqpplagqsytetmhavtvgRDGRQynVVIVPAKDSPINRGNY 102
Cdd:cd02754 3 TCPYCGVGCGVEIGV------------------------------------------KDGKV--VAVRGDPEHPVNRGRL 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 103 SIRGGTNALTVwsldrGTQDRLTYPLLRV-GDQFQAITWQDALTLMGLLIKGIRDRDGNDdniAVKCFdhgGSGQGF-ED 180
Cdd:cd02754 39 CIKGLNLHKTL-----NGPERLTRPLLRRnGGELVPVSWDEALDLIAERFKAIQAEYGPD---SVAFY---GSGQLLtEE 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 181 NYAAGKLFFAALSVKHIAIHNRPAYNSEVWG-SRERGVHELNYTYEDARLADTIVLWGANSYETATVFYvehmlpniqgA 259
Cdd:cd02754 108 YYAANKLAKGGLGTNNIDTNSRLCMASAVAGyKRSFGADGPPGSYDDIEHADCFFLIGSNMAECHPILF----------R 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 260 TVAEKQQAFDPGEpaepgyLIVIDPRKTSSytvaAQVApDRVMLLRPnlGTDYILANAIARAVWEKGYYDMAYLQARTDm 339
Cdd:cd02754 178 RLLDRKKANPGAK------IIVVDPRRTRT----ADIA-DLHLPIRP--GTDLALLNGLLHVLIEEGLIDRDFIDAHTE- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 340 tLFEEYKAKSLKLSVPYdefmaqAERITGVSRAEIEKAADWIAKPkagrfkRRTLTIYEKGIIWNMKNYDQVAAIVQLAV 419
Cdd:cd02754 244 -GFEELKAFVADYTPEK------VAEITGVPEADIREAARLFGEA------RKVMSLWTMGVNQSTQGTAANNAIINLHL 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 420 LTHNIGRPGTG-------CGRQGGHQEGY--VRPPAPT------------------PGSIYRGGPP--VNVDKFLIEGKG 470
Cdd:cd02754 311 ATGKIGRPGSGpfsltgqPNAMGGREVGGlaNLLPGHRsvnnpehraevakfwgvpEGTIPPKPGLhaVEMFEAIEDGEI 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 471 KFYWVIANDPYLSTPNNQvfrkRIHERTEKLTkalgaggepgtiqeraqkildilyqdpdalFLVVQDIY-MTETARDAH 549
Cdd:cd02754 391 KALWVMCTNPAVSLPNAN----RVREALERLE------------------------------FVVVQDAFaDTETAEYAD 436
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 550 LILPAAGWGEANETSINCNSRLLRLyEKFMDPPGEAKPDWEIFkwvglriAELYRAEGKFEeakkfefGKNWKTDEDVFl 629
Cdd:cd02754 437 LVLPAASWGEKEGTMTNSERRVSLL-RAAVEPPGEARPDWWIL-------ADVARRLGFGE-------LFPYTSPEEVF- 500
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55773483 630 agaEEFRdnTVSEEDEAvleaeNYKGVTYKLLKelgQKGIQTPVRRDPKTgklvGTVRRYT-YRFGTEDGK 699
Cdd:cd02754 501 ---EEYR--RLSRGRGA-----DLSGLSYERLR---DGGVQWPCPDGPPE----GTRRLFEdGRFPTPDGR 554
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
23-599 |
5.59e-72 |
|
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: 241.46 E-value: 5.59e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 23 VCQYCTVGCGYKVYVwpvgeeggvkpeqnafgldlstpqpplagqsytetmhavtvgRDGRQynVVIVPAKDSPINRGNY 102
Cdd:cd00368 3 VCPFCGVGCGILVYV------------------------------------------KDGKV--VRIEGDPNHPVNEGRL 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 103 SIRGGTNALTVWSldrgtQDRLTYPLLRVG--DQFQAITWQDALTLMGLLIKGIRDRDGNDdNIAVkcfdHGGSGQGFED 180
Cdd:cd00368 39 CDKGRAGLDGLYS-----PDRLKYPLIRVGgrGKFVPISWDEALDEIAEKLKEIREKYGPD-AIAF----YGGGGASNEE 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 181 NYAAGKLFFAALSVkHIAIHNRPAYNSEVWGSRERGVHELNYTYEDARLADTIVLWGANSYETATVFYveHMLpniqgat 260
Cdd:cd00368 109 AYLLQKLLRALGSN-NVDSHARLCHASAVAALKAFGGGAPTNTLADIENADLILLWGSNPAETHPVLA--ARL------- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 261 vaekQQAFDPGepaepGYLIVIDPRKTSSYTVAAQVAPdrvmlLRPnlGTDYILANAiaravwekgyydmaylqartdmt 340
Cdd:cd00368 179 ----RRAKKRG-----AKLIVIDPRRTETAAKADEWLP-----IRP--GTDAALALA----------------------- 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 341 lfeeykakslklsvpydefmAQAERITGVSRAEIEKAADWIAKPKagrfkrRTLTIYEKGIIWNMKNYDQVAAIVQLAVL 420
Cdd:cd00368 220 --------------------EWAAEITGVPAETIRALAREFAAAK------RAVILWGMGLTQHTNGTQNVRAIANLAAL 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 421 THNIGRPGTGCGRqgghqegyvrppaptpgsiyrggppvnvdkfliegkgkfywviANDPYLSTPNNQVFRKrihertek 500
Cdd:cd00368 274 TGNIGRPGGGLGP-------------------------------------------GGNPLVSAPDANRVRA-------- 302
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 501 ltkalgaggepgtiqerAQKILDilyqdpdalFLVVQDIYMTETARDAHLILPAAGWGEANETSINCNSRLLRLyEKFMD 580
Cdd:cd00368 303 -----------------ALKKLD---------FVVVIDIFMTETAAYADVVLPAATYLEKEGTYTNTEGRVQLF-RQAVE 355
|
570
....*....|....*....
gi 55773483 581 PPGEAKPDWEIFKWVGLRI 599
Cdd:cd00368 356 PPGEARSDWEILRELAKRL 374
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
23-706 |
7.76e-71 |
|
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: 242.50 E-value: 7.76e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 23 VCQYCTVGCGYKVYVwpvgeeggvkpeqnafgldlstpqpplagqsytetmhavtvgRDGRQynVVIVPAKDSPINRGNY 102
Cdd:cd02753 3 VCPYCGVGCGLELWV------------------------------------------KDNKI--VGVEPVKGHPVNRGKL 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 103 SIRG--GTNALTVWsldrgtqDRLTYPLLRVGDQFQAITWQDALTLMGLLIKGIRDRDGNDdniAVKCFdhgGSGQGF-E 179
Cdd:cd02753 39 CVKGrfGFDFVNSK-------DRLTKPLIRKNGKFVEASWDEALSLVASRLKEIKDKYGPD---AIAFF---GSAKCTnE 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 180 DNYAAGKLFFAAL---SVKHIAihnRPAYNSEVWGSRERgvheLNY-----TYEDARLADTIVLWGANSYETATVFYVEH 251
Cdd:cd02753 106 ENYLFQKLARAVGgtnNVDHCA---RLCHSPTVAGLAET----LGSgamtnSIADIEEADVILVIGSNTTEAHPVIARRI 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 252 MLPNIQGAtvaekqqafdpgepaepgYLIVIDPRKTSSYTVAAqvapdrvMLLRPNLGTDYILANAIARAVWEKGYYDMA 331
Cdd:cd02753 179 KRAKRNGA------------------KLIVADPRRTELARFAD-------LHLQLRPGTDVALLNAMAHVIIEEGLYDEE 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 332 YLQARTdmTLFEEYKAKSLKLSVPYdefmaqAERITGVSRAEIEKAADWIAKpkagrfKRRTLTIYEKGIIWNMKNYDQV 411
Cdd:cd02753 234 FIEERT--EGFEELKEIVEKYTPEY------AERITGVPAEDIREAARMYAT------AKSAAILWGMGVTQHSHGTDNV 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 412 AAIVQLAVLTHNIGRPGTGCGRQGGH---QegyvrppaptpGSIYRGGPPVNVDKFLiegkgKFYWVIANDPYLSTPNnq 488
Cdd:cd02753 300 MALSNLALLTGNIGRPGTGVNPLRGQnnvQ-----------GACDMGALPNVLPGYV-----KALYIMGENPALSDPN-- 361
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 489 vfrkriherTEKLTKALGAggepgtiqeraqkiLDilyqdpdalFLVVQDIYMTETARDAHLILPAAGWGEANETSINCN 568
Cdd:cd02753 362 ---------TNHVRKALES--------------LE---------FLVVQDIFLTETAELADVVLPAASFAEKDGTFTNTE 409
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 569 SRLLRLYeKFMDPPGEAKPDWEIfkwvglrIAELYRAEGkfeeakkfeFGKNWKTDEDVFlagaeefrdntvseeDEAVL 648
Cdd:cd02753 410 RRVQRVR-KAVEPPGEARPDWEI-------IQELANRLG---------YPGFYSHPEEIF---------------DEIAR 457
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 649 EAENYKGVTYKLLKELGqkGIQTPVR--RDPKTGKLvgtvrrYTYRFGTEDGKFKWYGTD 706
Cdd:cd02753 458 LTPQYAGISYERLERPG--GLQWPCPdeDHPGTPIL------HTERFATPDGKARFMPVE 509
|
|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
727-841 |
3.78e-64 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase (Arsenite-Ox) and related proteins. Arsenite oxidase oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin.
Pssm-ID: 239180 [Multi-domain] Cd Length: 115 Bit Score: 210.39 E-value: 3.78e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 727 YPFWVTTGRAQTIWQTAYHDRHLPEKALALPLPYVEVNPEDAKRLGLKSGDLVEVYNEEGNGTFLVYVTDAVKPGTLFLV 806
Cdd:cd02779 1 YKYWVNNGRANIIWQTAYHDQNNSEIAERVPLPYIEVNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKPGQTFML 80
|
90 100 110
....*....|....*....|....*....|....*
gi 55773483 807 MYHWRGTSNSLVTGYTDPKTTIPWYKGTRANLRKV 841
Cdd:cd02779 81 MAHPRPGANGLVTPYVDPETIIPYYKGTWANIRKI 115
|
|
| Rieske_3 |
pfam18465 |
Rieske 3Fe-4S; This domain is comprised of the iron-sulphur cluster and Rieske subunit found ... |
24-120 |
4.37e-51 |
|
Rieske 3Fe-4S; This domain is comprised of the iron-sulphur cluster and Rieske subunit found in the large subunit of arsenite oxidase. Arsenite oxidase is a 100 kDa molybdenum- and iron-sulfur-containing protein located on the outer surface of the inner membrane of Gram-negative organizms. The large subunit of arsenite oxidase is similar to other members of the dimethylsulfoxide (DMSO) reductase family of molybdenum enzymes. The large subunit of arsenite oxidase is divided into four domains, with domain I binding the [3Fe-4S] cluster. Domain I, consists of three antiparallel beta sheets and six helices. The [3Fe-4S] cluster is coordinated by the motif Cys21-X2-Cys24-X3-Cys28 near the interface with domains III and IV. A large, flattened funnel-like cavity bounded by domains I, II, and III leads to the molybdenum center pfam00384 located near the center of the molecule.
Pssm-ID: 465779 [Multi-domain] Cd Length: 96 Bit Score: 173.69 E-value: 4.37e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 24 CQYCTVGCGYKVYVWPVGEEGGVKPEQNAFGLDLSTPQPPLAGQSYTETMHAVtVGRDGRQYNVVIVPAKDSPINRGNYS 103
Cdd:pfam18465 1 CHYCIVGCGYKVYTWPVGKQGGPAPSQNAFGVDLSKQQPPLSGAWYAPSMHNV-VTQNGRDVNIVIKPDKDCVVNSGLSS 79
|
90
....*....|....*..
gi 55773483 104 IRGGTNALTVWSLDRGT 120
Cdd:pfam18465 80 IRGGRMAEKLYSPDTPT 96
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
122-703 |
3.19e-35 |
|
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: 140.85 E-value: 3.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 122 DRLTYPLLRVGD---QFQAITWQDALTLMGLLIKGIRDRDGnddniAVKCFDHGGSGQGFEDNYAAGKLFFAALSVKHIA 198
Cdd:cd02766 54 DRLLTPLKRVGRkggQWERISWDEALDTIAAKLKEIKAEYG-----PESILPYSYAGTMGLLQRAARGRFFHALGASELR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 199 ihnrpayNSEVWGSRERGvheLNYTY--------EDARLADTIVLWGANSyeTATvfyvehmlpNIQGATVAekQQAFDP 270
Cdd:cd02766 129 -------GTICSGAGIEA---QKYDFgaslgndpEDMVNADLIVIWGINP--AAT---------NIHLMRII--QEARKR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 271 GEPaepgyLIVIDPRKTSSytvAAQVapDRVMLLRPnlGTDYILANAIARAVWEKGYYDMAYLQARTDMtlFEEYKAKSL 350
Cdd:cd02766 186 GAK-----VVVIDPYRTAT---AARA--DLHIQIRP--GTDGALALGVAKVLFREGLYDRDFLARHTEG--FEELKAHLE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 351 KLSVpydefmAQAERITGVSRAEIEKAADWIAKPKagrfkrRTLTIyekgIIWNMKNY----DQVAAIVQLAVLTHNIGR 426
Cdd:cd02766 252 TYTP------EWAAEITGVSAEEIEELARLYGEAK------PPSIR----LGYGMQRYrnggQNVRAIDALPALTGNIGV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 427 PGTGCgrqgghqegyvrppaptpgsIY-RGGPPVnvdkfliegkgKFYWVIANDPYLSTPNnqvfrkriherTEKLTKAL 505
Cdd:cd02766 316 PGGGA--------------------FYsNSGPPV-----------KALWVYNSNPVAQAPD-----------SNKVRKGL 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 506 gaggepgtiqERaqkildilyqdpDALFLVVQDIYMTETARDAHLILPAAGWGEANETSINCNSRLLRLYEKFMDPPGEA 585
Cdd:cd02766 354 ----------AR------------EDLFVVVHDQFMTDTARYADIVLPATTFLEHEDVYASYWHYYLQYNEPAIPPPGEA 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 586 KPDWEIFKwvglriaELyraegkfeeAKKFEFgknwktdedvflaGAEEFRDNtvseeDEAVLEAEnykgvtykLLKELG 665
Cdd:cd02766 412 RSNTEIFR-------EL---------AKRLGF-------------GEPPFEES-----DEEWLDQA--------LDGTGL 449
|
570 580 590
....*....|....*....|....*....|....*...
gi 55773483 666 QKGIQTPVRRDPKTGKLVGTVRRYTYRFGTEDGKFKWY 703
Cdd:cd02766 450 PLEGIDLERLLGPRKAGFPLVAWEDRGFPTPSGKFEFY 487
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
122-605 |
7.10e-34 |
|
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: 137.53 E-value: 7.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 122 DRLTYPLLRVGDQFQAITWQDALTLMGLLIKGIRDRDGNdDNIAVkcfdHGGSGQGfedNYAAGKLFFAALsVKHIAIHN 201
Cdd:cd02762 53 DRLRTPMRRRGGSFEEIDWDEAFDEIAERLRAIRARHGG-DAVGV----YGGNPQA---HTHAGGAYSPAL-LKALGTSN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 202 RpAYNS-------EVWGSRERGvHELNYTYEDARLADTIVLWGANSYETatvfyveHMLPNIQGATVAEKQQAFDPGepa 274
Cdd:cd02762 124 Y-FSAAtadqkpgHFWSGLMFG-HPGLHPVPDIDRTDYLLILGANPLQS-------NGSLRTAPDRVLRLKAAKDRG--- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 275 epGYLIVIDPRKTSSytvaAQVApDRVMLLRPnlGTDYILANAIARAVWEKGYYDMAYLQARTDMtlFEEYKAKSLKLSV 354
Cdd:cd02762 192 --GSLVVIDPRRTET----AKLA-DEHLFVRP--GTDAWLLAAMLAVLLAEGLTDRRFLAEHCDG--LDEVRAALAEFTP 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 355 pydEFMAQAeriTGVSRAEIEKAA-DWIAKPKAGRFKR--------RTLTIYEKGIIWnmknydqvaaivqlaVLTHNIG 425
Cdd:cd02762 261 ---EAYAPR---CGVPAETIRRLArEFAAAPSAAVYGRlgvqtqlfGTLCSWLVKLLN---------------LLTGNLD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 426 RPGT---------GCGRQGGHQEGYVRPPAPTPGS-IYRGGPPVNV--DKFLIEGKGKF--YWVIANDPYLSTPNnqvfr 491
Cdd:cd02762 320 RPGGamfttpaldLVGQTSGRTIGRGEWRSRVSGLpEIAGELPVNVlaEEILTDGPGRIraMIVVAGNPVLSAPD----- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 492 kriherTEKLTKALGAggepgtiqeraqkiLDilyqdpdalFLVVQDIYMTETARDAHLILPAAGWGEANE-TSINCN-- 568
Cdd:cd02762 395 ------GARLEAALGG--------------LE---------FMVSVDVYMTETTRHADYILPPASQLEKPHaTFFNLEfp 445
|
490 500 510
....*....|....*....|....*....|....*..
gi 55773483 569 SRLLRLYEKFMDPPGEAKPDWEIFKWVGLRIAELYRA 605
Cdd:cd02762 446 RNAFRYRRPLFPPPPGTLPEWEILARLVEALDAVLRA 482
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
75-786 |
5.66e-32 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 133.87 E-value: 5.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 75 AVTVG-RDGRqynvvIVPAK---DSPINRGNYSIRGGTNALTVWSldrgtQDRLTYPLLRVGD-------QFQAITWQDA 143
Cdd:PRK13532 55 GVLVGtKDGR-----VVATQgdpDAPVNRGLNCIKGYFLSKIMYG-----KDRLTQPLLRMKDgkydkegEFTPVSWDQA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 144 LTLMGLLIKGIRDRDGNDdniAVKCFdhgGSGQG--FEdNYAAGKLFFAALSVKHIAIHNRPAYNSEVWG-SRERGVHEL 220
Cdd:PRK13532 125 FDVMAEKFKKALKEKGPT---AVGMF---GSGQWtiWE-GYAASKLMKAGFRSNNIDPNARHCMASAVVGfMRTFGIDEP 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 221 NYTYEDARLADTIVLWGANSYEtatvfyvehMLPnIQGATVAEKQQAFdpgepaePGYLIVIdprkTSSYTVAAQVAPDR 300
Cdd:PRK13532 198 MGCYDDIEAADAFVLWGSNMAE---------MHP-ILWSRVTDRRLSN-------PDVKVAV----LSTFEHRSFELADN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 301 VMLLRPNlgTDYILANAIAR------AV-WE---------KGYYDMAY-------LQ----------ARTDMTlFEEYKa 347
Cdd:PRK13532 257 GIIFTPQ--TDLAILNYIANyiiqnnAVnWDfvnkhtnfrKGATDIGYglrpthpLEkaaknpgtagKSEPIS-FEEFK- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 348 kslKLSVPYDefMAQAERITGVSRAEIEKAADWIAKPkagrfKRRTLTIYEKGI------IW--NMknydqvaaIVQLAV 419
Cdd:PRK13532 333 ---KFVAPYT--LEKTAKMSGVPKEQLEQLAKLYADP-----NRKVVSFWTMGFnqhtrgVWanNL--------VYNIHL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 420 LTHNIGRPGTG----------CG--RQGG---HqegyvRPPA-------------------------PTPGSiyrggPPV 459
Cdd:PRK13532 395 LTGKISTPGNGpfsltgqpsaCGtaREVGtfsH-----RLPAdmvvtnpkhreiaekiwklpegtipPKPGY-----HAV 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 460 NVDKFLIEGKGKFYWVIANDPYLSTPNNQvfrkriHERTekltkalgaggePGtiqeraqkildilYQDPDAlFLVVQDI 539
Cdd:PRK13532 465 AQDRMLKDGKLNAYWVMCNNNMQAGPNIN------EERL------------PG-------------WRNPDN-FIVVSDP 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 540 YMTETARDAHLILPAAGWGEaNETSINCNSRLLRLYEKFMDPPGEAKPD-WEIfkwvglriaelyraegkfeeakkFEFG 618
Cdd:PRK13532 513 YPTVSALAADLILPTAMWVE-KEGAYGNAERRTQFWRQQVKAPGEAKSDlWQL-----------------------VEFS 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 619 KNWKTDE---DVFLAGAEEFRDNTVSE-----------------EDEAVLEAENY-----KGvtykLLKELGQ------- 666
Cdd:PRK13532 569 KRFKTEEvwpEELLAKKPEYRGKTLYDvlfangqvdkfplselaEGYLNDEAKHFgfyvqKG----LFEEYASfgrghgh 644
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 667 -----------KGIQTPVRRDPKTgklvgtvrRYTYRFGT-----EDGKFKWYGTDD------WEGY--PAEVAKylepg 722
Cdd:PRK13532 645 dlapfdtyhkvRGLRWPVVDGKET--------LWRYREGYdpyvkAGEGFKFYGKPDgkavifALPYepPAESPD----- 711
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55773483 723 maEKYPFWVTTGRAQTIWQTAYHDRHLPEKALALPLPYVEVNPEDAKRLGLKSGDLVEVYNEEG 786
Cdd:PRK13532 712 --EEYDLWLSTGRVLEHWHTGSMTRRVPELYRAFPEAVCFMHPEDAKARGLRRGDEVKVVSRRG 773
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
80-610 |
2.28e-30 |
|
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: 125.49 E-value: 2.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 80 RDGRqyNVVIVPAKDSPINRGNYSIRGGTNALTVWSldrgtQDRLTYPLLRVGD----QFQAITWQDALTLMGLLIKGIR 155
Cdd:cd02755 19 EDGR--VVKIDGNPLSPLSRGKLCARGNAGIQLLYD-----PDRLKKPLIRVGErgegKFREASWDEALQYIASKLKEIK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 156 DRDGNDdniAVKCFDHGGSGQGFEdnyaagKLFFAALSVKHIAIHNRPAYNSE--VWGSRERGVH-ELNYTYEDARLadt 232
Cdd:cd02755 92 EQHGPE---SVLFGGHGGCYSPFF------KHFAAAFGSPNIFSHESTCLASKnlAWKLVIDSFGgEVNPDFENARY--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 233 IVLWGANSYEtATVFyvehmlPNIQGATVAEKQQAfdpgepaepgYLIVIDPRktssYTVAAQVApDRVMLLRPnlGTDY 312
Cdd:cd02755 160 IILFGRNLAE-AIIV------VDARRLMKALENGA----------KVVVVDPR----FSELASKA-DEWIPIKP--GTDL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 313 ILANAIARAVWEKGYYDMAYLQARTDMtlFEEYKAKSLKLSVpydefmAQAERITGVSRAEIEKAADWIA--KPKAgrfk 390
Cdd:cd02755 216 AFVLALIHVLISENLYDAAFVEKYTNG--FELLKAHVKPYTP------EWAAQITDIPADTIRRIAREFAaaAPHA---- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 391 rrtltIYEKG--IIWNMKNYDQVAAIVQLAVLTHNIGRPGtgcgrqgghqeGYVRPPAPTPGSIyrggppvnvdkflieg 468
Cdd:cd02755 284 -----VVDPGwrGTFYSNSFQTRRAIAIINALLGNIDKRG-----------GLYYAGSAKPYPI---------------- 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 469 kgKFYWVIANDPYLSTPNnqvfrkriherTEKLTKALgaggepgtiqeraqKILDilyqdpdalFLVVQDIYMTETARDA 548
Cdd:cd02755 332 --KALFIYRTNPFHSMPD-----------RARLIKAL--------------KNLD---------LVVAIDILPSDTALYA 375
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55773483 549 HLILPAAGWGEANE----TSINCNSRLLRLyeKFMDPPGEAKPDWEIFKWVGLRIAELYRAEGKFE 610
Cdd:cd02755 376 DVILPEATYLERDEpfsdKGGPAPAVATRQ--RAIEPLYDTRPGWDILKELARRLGLFGTPSGKIE 439
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
123-593 |
2.78e-29 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 120.20 E-value: 2.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 123 RLTYPLLRVGD-QFQAITWQDALTLMGLLIKGIRDrDGNDDNIAVKcfdhGGSGQGFE-DNYAAGKLFFAALSVKHIAIH 200
Cdd:pfam00384 1 RLKYPMVRRGDgKFVRVSWDEALDLIAKKLKRIIK-KYGPDAIAIN----GGSGGLTDvESLYALKKLLNRLGSKNGNTE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 201 NR----PAYNSEVWGSRERGVHELNYTYEDARLADTIVLWGANSYETATVFYvehmlpniqgatVAEKQQAFDPGEPaep 276
Cdd:pfam00384 76 DHngdlCTAAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILN------------ARIRKAALKGKAK--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 277 gyLIVIDPRKTSSYTVAaqvapdrvmLLRPNLGTDYILANAIARAVWEKGYYDmaylqartdmtlfeeykakslklsvpy 356
Cdd:pfam00384 141 --VIVIGPRLDLTYADE---------HLGIKPGTDLALALAGAHVFIKELKKD--------------------------- 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 357 defmaqaeritgvsraeiekaadwiaKPkagrFKRRTLTIYEKGIIwNMKNYDQV-AAIVQLAVLTHNIGRPGTGCGRQG 435
Cdd:pfam00384 183 --------------------------KD----FAPKPIIIVGAGVL-QRQDGEAIfRAIANLADLTGNIGRPGGGWNGLN 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 436 GHQeGYVRPPAPTPGSIYRGGPPVNVDKFLIEGKGKFYWVIANDPYLSTPNNQvfrkriherteKLTKALgaggepgtiq 515
Cdd:pfam00384 232 ILQ-GAASPVGALDLGLVPGIKSVEMINAIKKGGIKVLYLLGNNPFVTHADEN-----------RVVKAL---------- 289
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55773483 516 eraqkildilyQDPDAlfLVVQDIYM-TETARDAHLILPAAGWGEANETSINcNSRLLRLYEKFMDPPGEAKPDWEIFK 593
Cdd:pfam00384 290 -----------QKLDL--FVVYDGHHgDKTAKYADVILPAAAYTEKNGTYVN-TEGRVQSTKQAVPPPGEAREDWKILR 354
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
121-613 |
7.04e-29 |
|
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: 122.72 E-value: 7.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 121 QDRLTYPLLRVG--------------DQFQAITWQDALTLMGLLIKGIRDRDGNDdniAVkcFDHGGSGQGFEDNYAAGK 186
Cdd:cd02751 45 PDRIKYPMKRVGwlgngpgsrelrgeGEFVRISWDEALDLVASELKRIREKYGNE---AI--FGGSYGWASAGRLHHAQS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 187 LFFAALS-----VKHI------AIHNRPAYnseVWGSRErgVHELNYTYED-ARLADTIVLWGANSYETATVfyvehmlp 254
Cdd:cd02751 120 LLHRFLNliggyLGSYgtystgAAQVILPH---VVGSDE--VYEQGTSWDDiAEHSDLVVLFGANPLKTRQG-------- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 255 niqGATVAEKQQAFDPGEPAEPGY-LIVIDPRKTSSytvaAQVAPDRVMLLRPnlGTDYILANAIARAVWEKGYYDMAYL 333
Cdd:cd02751 187 ---GGGGPDHGSYYYLKQAKDAGVrFICIDPRYTDT----AAVLAAEWIPIRP--GTDVALMLAMAHTLITEDLHDQAFL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 334 QARTdmTLFEEYKAKSLKLS--VPYDEfmAQAERITGVSRAEIEKAADWIAKpkagrfkRRTLTIYEKGIIwNMKNYDQV 411
Cdd:cd02751 258 ARYT--VGFDEFKDYLLGESdgVPKTP--EWAAEITGVPAETIRALAREIAS-------KRTMIAQGWGLQ-RAHHGEQP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 412 A-AIVQLAVLTHNIGRPGTGCGRQGGHQEGYVRPPAPTPGSIYRGGP-PVnvdKFLIEGkgkFYWV--IANDPYLSTPNN 487
Cdd:cd02751 326 AwMLVTLAAMLGQIGLPGGGFGFGYGYSNGGGPPRGGAGGPGLPQGKnPV---KDSIPV---ARIAdaLLNPGKEFTANG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 488 QVFRK-RIHertekltKALGAGGEPgTIQERAQKILDILYQDPDalFLVVQDIYMTETARDAHLILPAAGWGEAN--ETS 564
Cdd:cd02751 400 KLKTYpDIK-------MIYWAGGNP-LHHHQDLNRLIKALRKDE--TIVVHDIFWTASARYADIVLPATTSLERNdiGLT 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 55773483 565 INCNSRLLRLYEKFMDPPGEAKPDWEIFKWVGLR--IAELYrAEGKFEEAK 613
Cdd:cd02751 470 GNYSNRYLIAMKQAVEPLGEARSDYEIFAELAKRlgVEEEF-TEGRDEMEW 519
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
122-612 |
1.79e-27 |
|
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: 118.58 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 122 DRLTYPLLRVG----DQFQAITWQDALTLMGLLIKGIRDRDGNDdniAVkcFDHGGSG---QGFEDNYAAGKLFfaALSV 194
Cdd:cd02770 58 DRLKYPMKRVGkrgeGKFVRISWDEALDTIASELKRIIEKYGNE---AI--YVNYGTGtygGVPAGRGAIARLL--NLTG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 195 KHIAIhnrpaYNSEVWGSRERGVhelNYTYEDA-------RLADT--IVLWGANSYET-----ATVFYVEHMLPNiqGAT 260
Cdd:cd02770 131 GYLNY-----YGTYSWAQITTAT---PYTYGAAasgssldDLKDSklVVLFGHNPAETrmgggGSTYYYLQAKKA--GAK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 261 VaekqqafdpgepaepgylIVIDPRktssYTVAAQVAPDRVMLLRPnlGTDYILANAIARAVWEKGYYDMAYLQART--- 337
Cdd:cd02770 201 F------------------IVIDPR----YTDTAVTLADEWIPIRP--GTDAALVAAMAYVMITENLHDQAFLDRYCvgf 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 338 -DMTLFEEYKAK-SLK---LSVPYDEFM---AQAERITGVSRAEIEKAADWIAKPKA-----GRFKRRTltiyekgiiwn 404
Cdd:cd02770 257 dAEHLPEGAPPNeSYKdyvLGTGYDGTPktpEWASEITGVPAETIRRLAREIATTKPaailqGWGPQRH----------- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 405 mKNYDQVA-AIVQLAVLTHNIGRPGTG-CGRQGGHQEGYVRPPA---PTPGSIyrggpPVnvdkfliegkgkFYWV--IA 477
Cdd:cd02770 326 -ANGEQAArAIMMLAAMTGNVGIPGGNtGARPGGSAYNGAGLPAgknPVKTSI-----PC------------FMWTdaIE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 478 NDPYLSTpnnqvfRKRIHERTEKLT---KALGAGGEPGTIQERAQ--KILDILYQDPD-ALFLVVQDIYMTETARDAHLI 551
Cdd:cd02770 388 RGEEMTA------DDGGVKGADKLKsniKMIWNYAGNTLINQHSDdnNTTRALLDDESkCEFIVVIDNFMTPSARYADIL 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55773483 552 LPAAGWGEAN---ETSINCNSRLLRLYEKFMDPPGEAKPDWEIFKWVGLRI-AELYRAEGKFEEA 612
Cdd:cd02770 462 LPDTTELEREdivLTSNAGMMEYLIYSQKAIEPLYECKSDYEICAELAKRLgVEDQFTEGKTEQE 526
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
94-611 |
2.43e-27 |
|
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: 116.64 E-value: 2.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 94 DSPINRGNYSIRGGTNALTVWSldrgtQDRLTYPLLRVGDQ----FQAITWQDALTLMGLLIKGIRDRDGnDDNIAvkcF 169
Cdd:cd02759 30 NHPTNKGRLCMRGLAAPEIVYH-----PDRLLYPLKRVGERgenkWERISWDEALDEIAEKLAEIKAEYG-PESIA---T 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 170 DHG-GSGQGFEDNYAAGKLFFAALSVKHI-AIHNrpAYNSEVWGSRERGVHELNYTYEDARLADTIVLWGANSYETATVF 247
Cdd:cd02759 101 AVGtGRGTMWQDSLFWIRFVRLFGSPNLFlSGES--CYWPRDMAHALTTGFGLGYDEPDWENPECIVLWGKNPLNSNLDL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 248 yvehmlpniQGATVAEKQQAfdpGEPaepgyLIVIDPRKTSSYTVAAQVAPdrvmlLRPnlGTDYILANAIARAVWEKGY 327
Cdd:cd02759 179 ---------QGHWLVAAMKR---GAK-----LIVVDPRLTWLAARADLWLP-----IRP--GTDAALALGMLNVIINEGL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 328 YDMAYLQARTDMtlFEEYKAKSLKLSVpydefmAQAERITGVSRAEIEKAADWIAKPKAGrfkrrtlTIYEKGIIWNMKN 407
Cdd:cd02759 235 YDKDFVENWCYG--FEELAERVQEYTP------EKVAEITGVPAEKIRKAARLYATAKPA-------CIQWGLAIDQQKN 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 408 YDQ-VAAIVQLAVLTHNIGRPGTGcgrqgghqegyvrppaptpgsiyRGGP-PVnvdkfliegkgKFYWVIANDPYLSTP 485
Cdd:cd02759 300 GTQtSRAIAILRAITGNLDVPGGN-----------------------LLIPyPV-----------KMLIVFGTNPLASYA 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 486 NNQvfrkrihertekltkalgaggepgtIQERAQKILDilyqdpdalFLVVQDIYMTETARDAHLILPAAGWGEANETSI 565
Cdd:cd02759 346 DTA-------------------------PVLEALKALD---------FIVVVDLFMTPTAMLADIVLPVAMSLERPGLRG 391
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 55773483 566 NCNSR-LLRLYEKFMDPPGEAKPDWEIFKWVGLRIAELYRAEGKFEE 611
Cdd:cd02759 392 GFEAEnFVQLRQKAVEPYGEAKSDYEIVLELGKRLGPEEAEYYKYEK 438
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
80-703 |
3.02e-27 |
|
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: 117.58 E-value: 3.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 80 RDGRqynVVIVPAKDSPINR-GNYSIRGGTNALTVWSldrgtQDRLTYPLLRVGD----QFQAITWQDALTLMGLLIKGI 154
Cdd:cd02765 19 RDGK---IVKVEPNEWPDKTyKRGCTRGLSHLQRVYS-----PDRLKYPMKRVGErgegKFERITWDEALDTIADKLTEA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 155 RDRDGNDdNIAVkcfdHGGSGQGFEDNYAAGKLFFAALsvkHIAI-----HNRPAYNSEVWGS-RERGVHELNytyeDAR 228
Cdd:cd02765 91 KREYGGK-SILW----MSSSGDGAILSYLRLALLGGGL---QDALtygidTGVGQGFNRVTGGgFMPPTNEIT----DWV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 229 LADTIVLWGANsyetatvfyvehmlpnIQGATVAEKQQAFDPGEPAEPgyLIVIDPRKTSSYTVAAQVAPdrvmlLRPnl 308
Cdd:cd02765 159 NAKTIIIWGSN----------------ILETQFQDAEFFLDARENGAK--IVVIDPVYSTTAAKADQWVP-----IRP-- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 309 GTDYILANAIARAVWEKGYYDMAYLQART-----------------------------------------DMT-----LF 342
Cdd:cd02765 214 GTDPALALGMINYILEHNWYDEAFLKSNTsapflvredngtllrqadvtatpaedgyvvwdtnsdspepvAATninpaLE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 343 EEYKAKSLKLSVPYDEFMAQAER--------ITGVSRAEIEKAADWIAKPKAGrfkrrtlTIYEKGIIWNMKNYD---QV 411
Cdd:cd02765 294 GEYTINGVKVHTVLTALREQAASyppkaaaeICGLEEAIIETLAEWYATGKPS-------GIWGFGGVDRYYHSHvfgRT 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 412 AAIvqLAVLTHNIGRPGTGCGRQgghqegyvrppaptpgsiyrggppvnvdkfliegkgKFYWVIANdpylSTPNNQVFR 491
Cdd:cd02765 367 AAI--LAALTGNIGRVGGGVGQI------------------------------------KFMYFMGS----NFLGNQPDR 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 492 KRIHERTEKLTkalgaggepgtiqeraqkildilyqdpdalFLVVQDIYMTETARDAHLILPAAGWGEANE---TSINCN 568
Cdd:cd02765 405 DRWLKVMKNLD------------------------------FIVVVDIFHTPTVRYADIVLPAAHWFEVEDllvRYTTHP 454
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 569 SRLLRlyEKFMDPPGEAKPDWEIFKWVglriaelyraegkfeeAKKFEFGKNW-KTDEDVFlagaeefrDNTVSEEDEAv 647
Cdd:cd02765 455 HVLLQ--QKAIEPLFESKSDFEIEKGL----------------AERLGLGDYFpKTPEDYV--------RAFMNSDDPA- 507
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 55773483 648 leaenYKGVTYKLLKELGqkgiqTPVRRDPKTGKLVGTVRRytyRFGTEDGKFKWY 703
Cdd:cd02765 508 -----LDGITWEALKEEG-----IIMRLATPEDPYVAYLDQ---KFGTPSGKLEFY 550
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
725-840 |
7.03e-27 |
|
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: 106.05 E-value: 7.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 725 EKYPFWVTTGRAQTIWQTAYHDRHLPEKALALPLPYVEVNPEDAKRLGLKSGDLVEVYNEEGNGTFLVYVTDAVKPGTLF 804
Cdd:cd00508 1 EEYPLVLTTGRLLEHWHTGTMTRRSPRLAALAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRPGTVF 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 55773483 805 LVMyHWRGTS-----NSLVTGYTDPKTTIPWYKGTRANLRK 840
Cdd:cd00508 81 MPF-HWGGEVsggaaNALTNDALDPVSGQPEFKACAVRIEK 120
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
23-626 |
5.46e-23 |
|
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: 104.79 E-value: 5.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 23 VCQYCTVGCGYKVYVwpvgeeggvkpeqnafgldlstpqpplagqsytetmhavtvgRDGRQYNVVIVPakDSPINRGNY 102
Cdd:cd02752 3 ICPYCSVGCGLIAYV------------------------------------------QNGVWVHQEGDP--DHPVNRGSL 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 103 SIRGGTnaltVWSLDRGtQDRLTYPLLRVG--DQFQAITWQDALTLMGLLIKGIRDRDGNDDNIAVKCFDH-------GG 173
Cdd:cd02752 39 CPKGAA----LRDFVHS-PKRLKYPMYRAPgsGKWEEISWDEALDEIARKMKDIRDASFVEKNAAGVVVNRpdsiaflGS 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 174 SGQGFEDNYAAGKlFFAALSVKHIAIHNRPAYNSEVWGSRER-GVHELNYTYEDARLADTIVLWGANSYETATVFYvEHM 252
Cdd:cd02752 114 AKLSNEECYLIRK-FARALGTNNLDHQARIUHSPTVAGLANTfGRGAMTNSWNDIKNADVILVMGGNPAEAHPVSF-KWI 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 253 L--PNIQGATvaekqqafdpgepaepgyLIVIDPRKTSSYTVAAQVAPdrvmlLRPnlGTDYILANAIaravwekgyydm 330
Cdd:cd02752 192 LeaKEKNGAK------------------LIVVDPRFTRTAAKADLYVP-----IRS--GTDIAFLGGM------------ 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 331 aylqartdmtlfeeykaksLKLSVPYDEFMaqAERITGVSRAEIEKAADWIAkpKAGRFKRRTLTIYEKGiiWNMKNYD- 409
Cdd:cd02752 235 -------------------INYIIRYTPEE--VEDICGVPKEDFLKVAEMFA--ATGRPDKPGTILYAMG--WTQHTVGs 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 410 ---QVAAIVQLavLTHNIGRPGTGCGRQGGHqegyvrppAPTPGSIYRGGPPVNVDKFLiegKGkfywviaNDPYLSTPN 486
Cdd:cd02752 290 qniRAMCILQL--LLGNIGVAGGGVNALRGH--------SNVQGATDLGLLSHNLPGYL---GG-------QNPNSSFPN 349
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 487 nqvfrkriherTEKLTKALGAggepgtiqeraqkiLDilyqdpdalFLVVQDIYMTETAR-------------DAHLILP 553
Cdd:cd02752 350 -----------ANKVRRALDK--------------LD---------WLVVIDPFPTETAAfwknpgmdpksiqTEVFLLP 395
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55773483 554 AAGWGEAnETSINCNSRLLRLYEKFMDPPGEAKPDWEIFKWVGLRIAELYRAEGkfeeAKKFEFGKNWKTDED 626
Cdd:cd02752 396 AACQYEK-EGSITNSGRWLQWRYKVVEPPGEAKSDGDILVELAKRLGFLYEKEG----GAFPEPITKWNYGYG 463
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
725-841 |
5.92e-23 |
|
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: 94.95 E-value: 5.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 725 EKYPFWVTTGRAQTIWQTAYHDRHLPEKALALPLPYVEVNPEDAKRLGLKSGDLVEVYNEEGNGTFLVYVTDAVKPGTLF 804
Cdd:cd02791 1 AEYPLWLNTGRVRDQWHTMTRTGRVPRLNAHVPEPYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPGEVF 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 55773483 805 LVMyHWRGTS------NSLVTGYTDPKTTIPWYKGTRANLRKV 841
Cdd:cd02791 81 VPM-HWGDQFgrsgrvNALTLDATDPVSGQPEFKHCAVRIEKV 122
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
729-834 |
2.83e-22 |
|
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: 92.34 E-value: 2.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 729 FWVTTGRAQTIWQTAYHDRHLPEKALALPlPYVEVNPEDAKRLGLKSGDLVEVYNEEGNGTFLVYVTDAVKPGTLFLVMY 808
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKPEP-EVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFG 79
|
90 100 110
....*....|....*....|....*....|
gi 55773483 809 HWR----GTSNSLVTGYTDPKTTIPWYKGT 834
Cdd:pfam01568 80 WWYeprgGNANALTDDATDPLSGGPEFKTC 109
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
725-840 |
4.43e-22 |
|
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: 92.29 E-value: 4.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 725 EKYPFWVTTGRAQTIWQTAYHDRHLPEKALALPLPYVEVNPEDAKRLGLKSGDLVEVYNEEGNGTFLVYVTDAVKPGTLF 804
Cdd:cd02792 1 EEFPLVLTTGRLTEHFHGGNMTRNSPYLAELQPEMFVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHEVG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 55773483 805 LVmYHW------RGTSNSLVTGYT-DPKTTIPWYKGTRANLRK 840
Cdd:cd02792 81 IP-YHWggmglvIGDSANTLTPYVgDPNTQTPEYKAFLVNIEK 122
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
122-635 |
3.80e-20 |
|
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: 94.31 E-value: 3.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 122 DRLTYPLLRVGDQ----FQAITWQDALTLMGLLIKGIRDRDGNDDNIAVKCFDHGGSGQgfednYAAGKLFFAALSVKHI 197
Cdd:cd02750 65 DRVKYPLKRVGARgegkWKRISWDEALELIADAIIDTIKKYGPDRVIGFSPIPAMSMVS-----YAAGSRFASLIGGVSL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 198 AIH----NRPAYNSEVWGsrergVHELNYTYEDARLADTIVLWGANSYETATVFYveHMLpniqgatvaekqqafdpgep 273
Cdd:cd02750 140 SFYdwygDLPPGSPQTWG-----EQTDVPESADWYNADYIIMWGSNVPVTRTPDA--HFL-------------------- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 274 AEPGY----LIVIDPRKTSSYTVAaqvapDRVMLLRPnlGTDYILANAIARAVWEKGYYDMAYLQARTDMTLFeeykaks 349
Cdd:cd02750 193 TEARYngakVVVVSPDYSPSAKHA-----DLWVPIKP--GTDAALALAMAHVIIKEKLYDEDYLKEYTDLPFL------- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 350 lkLSVPydefmAQAERITGVSRAEIEKAADWIAKPKagrfkrRTLTIYEKGiiwNMKNY--DQVA-AIVQLAVLTHNIGR 426
Cdd:cd02750 259 --VYTP-----AWQEAITGVPRETVIRLAREFATNG------RSMIIVGAG---INHWYhgDLCYrALILLLALTGNEGK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 427 PGTGCgrqgghqegyvrppaptpgSIYRGGPPVnvdkfliegkgkfYWVIANDPYLSTPNNQVFRKRIHERTEKLtkalg 506
Cdd:cd02750 323 NGGGW-------------------AHYVGQPRV-------------LFVWRGNLFGSSGKGHEYFEDAPEGKLDL----- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 507 aggepgtiqeraqkildilyqdpdalfLVVQDIYMTETARDAHLILPAAGWGEANETSINCNSRLLRLYEKFMDPPGEAK 586
Cdd:cd02750 366 ---------------------------IVDLDFRMDSTALYSDIVLPAATWYEKHDLSTTDMHPFIHPFSPAVDPLWEAK 418
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 55773483 587 PDWEIFKwvglriaelyraegkfEEAKKFEfgknWKT---------DEDVFLAGAEEF 635
Cdd:cd02750 419 SDWEIFK----------------ALAKKVP----WRTltgrqqfylDHDWFLELGETL 456
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
740-832 |
6.92e-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: 85.45 E-value: 6.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 740 WQTAYHDRhLPEKALALPLPYVEVNPEDAKRLGLKSGDLVEVYNEEGNGTFLVYVTDAVKPGTLFLVMYHWR-----GTS 814
Cdd:cd02775 5 FHSGTRTR-NPWLRELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGHrggrgGNA 83
|
90
....*....|....*...
gi 55773483 815 NSLVTGYTDPKTTIPWYK 832
Cdd:cd02775 84 NVLTPDALDPPSGGPAYK 101
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
725-832 |
3.71e-19 |
|
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: 83.83 E-value: 3.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 725 EKYPFWVTTGRaqTIWQtaYHDRHLPEKALAL----PLPYVEVNPEDAKRLGLKSGDLVEVYNEEGNGTFLVYVTDAVKP 800
Cdd:cd02790 1 EEYPLVLTTGR--VLYH--YHTGTMTRRAEGLdaiaPEEYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPE 76
|
90 100 110
....*....|....*....|....*....|..
gi 55773483 801 GTLFLVMYHWRGTSNSLVTGYTDPKTTIPWYK 832
Cdd:cd02790 77 GVVFMPFHFAEAAANLLTNAALDPVAKIPEFK 108
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
123-430 |
3.07e-16 |
|
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: 82.74 E-value: 3.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 123 RLTYPLLR--VGDQFQAITWQDALTLMGLLIKGIrdrdgnDDNIAVKCFdhggSGQGfeDNYAAgklFFAALSVKHIAIH 200
Cdd:cd02767 64 RLTYPMRYdaGSDHYRPISWDEAFAEIAARLRAL------DPDRAAFYT----SGRA--SNEAA---YLYQLFARAYGTN 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 201 NRP-AYN-----SEVWGSRERGVHELNYTYEDARLADTIVLWGANSYETATVFYveHMLPNI--QGATVAekqqAFDPGE 272
Cdd:cd02767 129 NLPdCSNmchepSSVGLKKSIGVGKGTVSLEDFEHTDLIFFIGQNPGTNHPRML--HYLREAkkRGGKII----VINPLR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 273 paEPG---YLIVIDPRK--TSSYTVAAQVapdrvmlLRPNLGTDYILANAIARAVWE-----KGYYDMAYLQARTdmTLF 342
Cdd:cd02767 203 --EPGlerFANPQNPESmlTGGTKIADEY-------FQVRIGGDIALLNGMAKHLIErddepGNVLDHDFIAEHT--SGF 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 343 EEYKAKSLKLSvpYDEFmaqaERITGVSRAEIEKAADWIAKPKAGRFkrrtltIYEKGIIWNMKNYDQVAAIVQLAVLTH 422
Cdd:cd02767 272 EEYVAALRALS--WDEI----ERASGLSREEIEAFAAMYAKSERVVF------VWGMGITQHAHGVDNVRAIVNLALLRG 339
|
....*...
gi 55773483 423 NIGRPGTG 430
Cdd:cd02767 340 NIGRPGAG 347
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
123-807 |
6.53e-16 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 82.41 E-value: 6.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 123 RLTYPLLRVGD----QFQAITWQDALTLMGLLIKGIRDRDGnDDNIAVKCFDHGGSGQGFEDNYAAG--KLF-FAALSVK 195
Cdd:PRK15488 98 RIVKPLKRVGErgegKWQEISWDEAYQEIAAKLNAIKQQHG-PESVAFSSKSGSLSSHLFHLATAFGspNTFtHASTCPA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 196 HIAIHNRPAYNsevwGSRERGVHELNYtyedarladtIVLWGANSYETATVFYVEHMlpniqgATVAEKQQAfdpgepae 275
Cdd:PRK15488 177 GYAIAAKVMFG----GKLKRDLANSKY----------IINFGHNLYEGINMSDTRGL------MTAQMEKGA-------- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 276 pgYLIVIDPRktssYTVAAQVApDRVMLLRPnlGTDYILANAIARAVWEKGYYDMAYLQARTdmTLFEEYkAKSLKLSVP 355
Cdd:PRK15488 229 --KLVVFEPR----FSVVASKA-DEWHAIRP--GTDLAVVLALCHVLIEENLYDKAFVERYT--SGFEEL-AASVKEYTP 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 356 ydefmAQAERITGVSRAEIEKAADWIAK--PKA----GRfkRRTLTIYEkgiiwnmknYDQVAAIVQLAVLTHNIGRpgt 429
Cdd:PRK15488 297 -----EWAEAISDVPADDIRRIARELAAaaPHAivdfGH--RATFTPEE---------FDMRRAIFAANVLLGNIER--- 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 430 gcgrQGGhqegyvrppaptpgsIYRGGPPVNVDKFLIEGKGkfywviandPYLSTPNNQVFRK----RIHERTEKLTKAL 505
Cdd:PRK15488 358 ----KGG---------------LYFGKNASVYNKLAGEKVA---------PTLAKPGVKGMPKptakRIDLVGEQFKYIA 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 506 GAGGepgtiqeRAQKILD-ILYQDPDAL----------------------------FLVVQDIYMTETARDAHLILPAAG 556
Cdd:PRK15488 410 AGGG-------VVQSIIDaTLTQKPYQIkgwvmsrhnpmqtvtdradvvkalkkldLVVVCDVYLSESAAYADVVLPEST 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 557 WGEANEtSINCNSRLLRLY---EKFMDPPGEAKPDWEIFKWVG--LRIAELYraegkfeeakkfefgkNWKTDEDVFLAG 631
Cdd:PRK15488 483 YLERDE-EISDKSGKNPAYalrQRVVEPIGDTKPSWQIFKELGekMGLGQYY----------------PWQDMETLQLYQ 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 632 AeefrdntvsEEDEAVLEAENYKG-VTYK---LLKElgQKGIQTPVRRDPKTgKLVGtvRRYTY----RFGTEDGKFKWY 703
Cdd:PRK15488 546 V---------NGDHALLKELKKKGyVSFGvplLLRE--PKMVAKFVARYPNA-KAVD--EDGTYgsqlKFKTPSGKIELF 611
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 704 GTDDWEGYPAE-VAKYLEPGMAEKYPFWVTTGRaqTIWQTAYHDRHLPEKALALPLPYVEVNPEDAKRLGLKSGDLVEVY 782
Cdd:PRK15488 612 SAKLEALAPGYgVPRYRDVALKKEDELYFIQGK--VAVHTNGATQNVPLLANLMSDNAVWIHPQTAGKLGIKNGDEIRLE 689
|
730 740
....*....|....*....|....*
gi 55773483 783 NEEGNGTFLVYVTDAVKPGTLFLVM 807
Cdd:PRK15488 690 NSVGKEKGKALVTPGIRPDTLFAYM 714
|
|
| FwdD |
COG1153 |
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion]; |
731-848 |
8.76e-13 |
|
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion];
Pssm-ID: 440767 [Multi-domain] Cd Length: 127 Bit Score: 66.03 E-value: 8.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 731 VTTGRaqTIWQ--TAYHDRHLPE--KALAlplpYVEVNPEDAKRLGLKSGDLVEVYNEEGNGTFLVYVTDAVKPGTLFLV 806
Cdd:COG1153 5 LITGR--TIFQgvAIEGGKFSDEyfDACA----VCELNPEDMKKLGIKEGDKVKVTSEYGEVVVKAKESEDLHPGLVFIP 78
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 55773483 807 MYHWrgtSNSLVTGYTDPkTTIPWYKGTRANLRKVAGAIPSV 848
Cdd:COG1153 79 MGPW---ANAVVPPETHS-TGMPDFKGVPVEVEPTDEEVLSA 116
|
|
| 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 ... |
97-592 |
1.14e-12 |
|
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: 71.27 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 97 INRGNYSIRGGtnaltvWSLDRG--------TQDRLTYPLLRVGDQFQAITWQDALTLMGLLIKGIRDRdgnddniavkc 168
Cdd:cd02771 26 ENRYNGAVNHY------FLCDRGrfgygyvnSRDRLTQPLIRRGGTLVPVSWNEALDVAAARLKEAKDK----------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 169 fdHGGSGQG---FEDNYAAGKLFFAALSVKHIAIHNRPAYNSEVWGSRERGVhelnyTYEDARLADTIVLWGANSYETAT 245
Cdd:cd02771 89 --VGGIGSPrasNESNYALQKLVGAVLGTNNVDHRARRLIAEILRNGPIYIP-----SLRDIESADAVLVLGEDLTQTAP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 246 VfyVEHMLpnIQGATVAEKQQAFDPGEPAEPGYLIVIDPRKTSSYTVAAQVAPDRVMLLRPNL-----GTDYILANAIAR 320
Cdd:cd02771 162 R--IALAL--RQAARRKAVELAALSGIPKWQDAAVRNIAQGAKSPLFIVNALATRLDDIAAESiraspGGQARLGAALAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 321 AVwekgyydmaylqartdmtlfeeykakslklsvpydefmaQAERITGVSRAEIEKAADWIAKPKAGRfkrRTLtiyekg 400
Cdd:cd02771 238 AV---------------------------------------DASAAGVSGLAPKEKAARIAARLTGAK---KPL------ 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 401 IIW--NMKNYDQVAAIVQLAVLthnIGRPGTGCGRQGGHQEGYVrpPAPTPGSIYRGGPPVNVDKFL---IEGKGKFYWV 475
Cdd:cd02771 270 IVSgtLSGSLELIKAAANLAKA---LKRRGENAGLTLAVEEGNS--PGLLLLGGHVTEPGLDLDGALaalEDGSADALIV 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 476 IANDPYLSTPNNQVFRkrihertekltkALGAGGepgtiqeraqkildilyqdpdalFLVVQDIYMTETARDAHLILPAA 555
Cdd:cd02771 345 LGNDLYRSAPERRVEA------------ALDAAE-----------------------FVVVLDHFLTETAERADVVLPAA 389
|
490 500 510
....*....|....*....|....*....|....*..
gi 55773483 556 GWGEANETSINCNSRLLRLYEKFMDPPGEAKPDWEIF 592
Cdd:cd02771 390 SFAEKSGTFVNYEGRAQRFFKAYDDPAGDARSDWRWL 426
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
727-810 |
1.63e-12 |
|
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239182 [Multi-domain] Cd Length: 130 Bit Score: 65.41 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 727 YPFWVTTGrAQTIWQTAYHDRHLPEKALALPLPYVEVNPEDAKRLGLKSGDLVEVYNEEGNGTFLVYVTDAVKPGTLFLV 806
Cdd:cd02781 2 YPLILTTG-ARSYYYFHSEHRQLPSLRELHPDPVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVRAE 80
|
....
gi 55773483 807 MYHW 810
Cdd:cd02781 81 HGWW 84
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
123-613 |
6.73e-11 |
|
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: 65.75 E-value: 6.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 123 RLTYPLLRVG---------------DQFQAITWQDALTLMGLLIKGIRDRDGNDdniAVkcfdHGGSgqgfednY---AA 184
Cdd:cd02769 46 RIKYPMVRRGwlekgpgsdrslrgkEEFVRVSWDEALDLVAAELKRVRKTYGNE---AI----FGGS-------YgwsSA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 185 GKL---------FFAAL--SVKHI---AIHNRPAYNSEVWGSRErGVHELNYTYED-ARLADTIVLWGANSYETATVfyv 249
Cdd:cd02769 112 GRFhhaqsllhrFLNLAggYVGSVgdySTGAAQVILPHVVGSME-VYTEQQTSWPViAEHTELVVAFGADPLKNAQI--- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 250 ehmlpniqGATVAEKQQAFDP-GEPAEPGY-LIVIDPRKTS--SYTVAAQVAPdrvmllRPNlgTDYILANAIARAVWEK 325
Cdd:cd02769 188 --------AWGGIPDHQAYSYlKALKDRGIrFISISPLRDDtaAELGAEWIAI------RPG--TDVALMLALAHTLVTE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 326 GYYDMAYLQARTdmTLFEEYKAKSLKLS--VPYDEfmAQAERITGVSRAEIEKAADWIAkpkagrfKRRTLTIyekgIIW 403
Cdd:cd02769 252 GLHDKAFLARYT--VGFDKFLPYLLGESdgVPKTP--EWAAAICGIPAETIRELARRFA-------SKRTMIM----AGW 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 404 NMKNYD---QVA-AIVQLAVLTHNIGRPGTGCGRQGGHQEGYVRPPAPTPG-SIYRGGPPVN--------VDKFLIEGK- 469
Cdd:cd02769 317 SLQRAHhgeQPHwMAVTLAAMLGQIGLPGGGFGFGYHYSNGGGPPRGAAPPpALPQGRNPVSsfipvariADMLLNPGKp 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 470 ----GK---------FYWVIANdPYLStpnnqvfrkriHERTEKLTKALgaggepgtiqeraqkildilyQDPDAlfLVV 536
Cdd:cd02769 397 fdynGKkltypdiklVYWAGGN-PFHH-----------HQDLNRLIRAW---------------------QKPET--VIV 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55773483 537 QDIYMTETARDAHLILPAAGWGEANETSINCNSRLLRLYEKFMDPPGEAKPDWEIFKwvglRIAELYRAEGKFEEAK 613
Cdd:cd02769 442 HEPFWTATARHADIVLPATTSLERNDIGGSGDNRYIVAMKQVVEPVGEARDDYDIFA----DLAERLGVEEQFTEGR 514
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
727-815 |
6.08e-10 |
|
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: 57.29 E-value: 6.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 727 YPFWVTTGRAQTIWQTAYHDrhLPEKALALPLPYVEVNPEDAKRLGLKSGDLVEVYNEEGNGTFLVYVTDAVKPGTLFLV 806
Cdd:cd02786 1 YPLRLITPPAHNFLNSTFAN--LPELRAKEGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVVVAE 78
|
....*....
gi 55773483 807 MYHWRGTSN 815
Cdd:cd02786 79 GGWWREHSP 87
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
465-592 |
8.38e-10 |
|
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440657 [Multi-domain] Cd Length: 453 Bit Score: 61.78 E-value: 8.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 465 LIEGKGKFYWVIANDPYLSTPnnqvfrkrihertEKLTKALGAGGepgtiqeraqkildilyqdpdalFLVVQDIYMTET 544
Cdd:COG1034 328 AEAGKLKALVLLGADPYDLDP-------------AAALAALAKAD-----------------------FVVVLDHFGSAT 371
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 55773483 545 ARDAHLILPAAGWGEANETSINCNSRLLRlYEKFMDPPGEAKPDWEIF 592
Cdd:COG1034 372 AERADVVLPAAAFAEKSGTFVNLEGRVQR-FNAAVPPPGEARPDWRVL 418
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
760-840 |
2.85e-09 |
|
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: 55.74 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 760 YVEVNPEDAKRLGLKSGDLVEVYNEEGNGTFLVYVTDAVKPGTLFLVMY--HW----------RGTSNSLVTGYTDPKTT 827
Cdd:cd02778 31 TLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMPHGfgHWapalsrayggGVNDNNLLPGSTEPVSG 110
|
90
....*....|...
gi 55773483 828 IPWYKGTRANLRK 840
Cdd:cd02778 111 GAGLQEFTVTVRK 123
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
230-826 |
4.50e-09 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 60.07 E-value: 4.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 230 ADTIVLWGANSYEtatvfyvehmlpNIQGATVAEKQQAFdpgepaepGYL--------------IVIDP--RKTSSYTVA 293
Cdd:PRK15102 214 SKTIVLWGSDPVK------------NLQVGWNCETHESY--------AYLaqlkekvakgeinvISIDPvvTKTQNYLGC 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 294 AQVAPdrvmllrpNLGTDYILANAIARAVWEKGYYDMAYLQartDMTL-FEEYkakslklsVPYdeFMAQ---------- 362
Cdd:PRK15102 274 EHLYV--------NPQTDVPLMLALAHTLYSENLYDKKFID---NYCLgFEQF--------LPY--LLGEkdgvpktpew 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 363 AERITGVSRAEIEKAADWIAKpkagrfkRRTLTIYekG-IIWNMKNYDQVA-AIVQLAVLTHNIGRPGTGCGRqgGHQeg 440
Cdd:PRK15102 333 AEKICGIDAETIRELARQMAK-------GRTQIIA--GwCIQRQQHGEQPYwMGAVLAAMLGQIGLPGGGISY--GHH-- 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 441 YVRPPAPTPGSIYRGGPPVNVDkfliEG-KGKFywviandpylstpNNQVFRKriHERTEKLTKALGAGGEPG-TIQERA 518
Cdd:PRK15102 400 YSGIGVPSSGGAIPGGFPGNLD----TGqKPKH-------------DNSDYKG--YSSTIPVARFIDAILEPGkTINWNG 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 519 QKIL--DIL------------YQDPDALF--------LVVQDIYMTETARDAHLILPAAGWGEANETSI--NCNSRLLRL 574
Cdd:PRK15102 461 KKVTlpPLKmmifsgtnpwhrHQDRNRMKeafrkletVVAIDNQWTATCRFADIVLPACTQFERNDIDQygSYSNRGIIA 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 575 YEKFMDPPGEAKPDWEIFKWVGLR----------------IAELYrAEGKFEEAKKF---EFGKNWKTDEDVFLAGAEEF 635
Cdd:PRK15102 541 MKKVVEPLFESRSDFDIFRELCRRfgrekeytrgmdemgwLKRLY-QECKQQNKGKFhmpEFDEFWKKGYVEFGEGQPWV 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 636 RDNTVSEEDEavleaenykgvtyklLKELGqkgiqTPVrrdpktgklvGTVRRYTYRFGTedgkfkwYGTDDWEGYPAEV 715
Cdd:PRK15102 620 RHADFREDPE---------------LNPLG-----TPS----------GLIEIYSRKIAD-------MGYDDCQGHPMWF 662
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 716 AKyLE-----PGmAEKYPFWVttgraqtiwQTAYHDRHLPEK---ALALPLPY-------VEVNPEDAKRLGLKSGDLVE 780
Cdd:PRK15102 663 EK-IErshggPG-SDKYPLWL---------QSVHPDKRLHSQlceSEELRETYtvqgrepVYINPQDAKARGIKDGDVVR 731
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 55773483 781 VYNEEGNGTFLVYVTDAVKPGTLFLVMYHWRGTSNSLVTG----YTDPKT 826
Cdd:PRK15102 732 VFNDRGQVLAGAVVSDRYPPGVIRIHEGAWYGPDKGGEIGalctYGDPNT 781
|
|
| MopB_CT_FmdC-FwdD |
cd02789 |
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran ... |
731-833 |
8.13e-09 |
|
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran dehydrogenase (FmdC) and subunit D of tungsten formylmethanofuran dehydrogenase (FwdD), and other related proteins. Formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and some eubacteria. Members of this CD belong to the molybdopterin_binding superfamily of proteins. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239190 [Multi-domain] Cd Length: 106 Bit Score: 53.97 E-value: 8.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 731 VTTGRaqTIWQTAYHDRHLPEKALALPLPYVEVNPEDAKRLGLKSGDLVEVYNEegNGTFLVYV--TDAVKPGTLFLVMY 808
Cdd:cd02789 5 LNSGR--TIDQGRIIEGGNKLTYEVDACAYCEINPEDYKLLGKPEGDKVKVTSE--FGEVVVFAkeNEGVPEGMVFIPMG 80
|
90 100
....*....|....*....|....*
gi 55773483 809 HWrgtSNSLVTGYTDpKTTIPWYKG 833
Cdd:cd02789 81 PW---ANVVVDPYTD-STGSPIFKG 101
|
|
| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
759-810 |
5.79e-08 |
|
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. This CD (MopB_CT_Nitrate-R-NarG-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239177 [Multi-domain] Cd Length: 141 Bit Score: 52.38 E-value: 5.79e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 55773483 759 PYVEVNPEDAKRLGLKSGDLVEVYNEEGNGTFLVYVTDAVKPGTLFlvMYHW 810
Cdd:cd02776 31 PVVWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTVF--MYHA 80
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
726-803 |
1.92e-07 |
|
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: 50.44 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 726 KYPFWVTTGRAQtiWQTayHDRHLPEKAL--ALPLPYVEVNPEDAKRLGLKSGDLVEVYNEEGNGTFLVYVTDAVKPGTL 803
Cdd:cd02785 1 KYPLACIQRHSR--FRV--HSQFSNVPWLleLQPEPRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGVV 76
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
533-593 |
2.28e-07 |
|
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: 53.83 E-value: 2.28e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55773483 533 FLVVQDIYMTETARDAHLILPAAGWGEANETSINCNSRLLRLyEKFMDPPGEAKPDWEIFK 593
Cdd:cd02768 321 AFVVYQGHHGDTGAQADVILPAAAFTEKSGTYVNTEGRVQRF-KKAVSPPGDAREDWKILR 380
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| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
727-803 |
2.82e-07 |
|
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: 50.28 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 727 YPFWVTTgraqtiWQTAYHDR----HLPEKALALPLPYVE---VNPEDAKRLGLKSGDLVEVYNEEgnGTFL--VYVTDA 797
Cdd:cd02777 1 YPLQLIS------PHPKRRLHsqldNVPWLREAYKVKGREpvwINPLDAAARGIKDGDIVRVFNDR--GAVLagARVTDR 72
|
....*.
gi 55773483 798 VKPGTL 803
Cdd:cd02777 73 IMPGVV 78
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|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
94-428 |
3.80e-07 |
|
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: 53.60 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 94 DSPINRGNYSIRGgtnALTVWSL-DrgtQDRLTYPLLRVG--------DQFQAITWQDAL-TLMGLLIKGIRDRDGNDdn 163
Cdd:cd02757 32 LHPGSRGRLCAKG---HLGLQQVyD---PDRILYPMKRTNprkgrdvdPKFVPISWDEALdTIADKIRALRKENEPHK-- 103
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 164 IAVKcfdhggSGQGFEDNYAAGKLFFAALSVKHIAIHNRPAYNSEVWGsreRGVHELNYTYEDARLADT--IVLWGANSY 241
Cdd:cd02757 104 IMLH------RGRYGHNNSILYGRFTKMIGSPNNISHSSVCAESEKFG---RYYTEGGWDYNSYDYANAkyILFFGADPL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 242 ETAtvfyveHMLPNIQGATvaekqqafdpGEPAEPGYLIVIDPRKTSSYTVAaqvapDRVMLLRPnlGTDYILANAIARA 321
Cdd:cd02757 175 ESN------RQNPHAQRIW----------GGKMDQAKVVVVDPRLSNTAAKA-----DEWLPIKP--GEDGALALAIAHV 231
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250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 322 VWEKGYYDMAYLQARTDMT------------LFEEYKAKSL--KLSVPY-DEFMAQAERITGVSRAEIEKAADWIA--KP 384
Cdd:cd02757 232 ILTEGLWDKDFVGDFVDGKnyfkagetvdeeSFKEKSTEGLvkWWNLELkDYTPEWAAKISGIPAETIERVAREFAtaAP 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 55773483 385 KAGRFKRRTLTIYEKGIIWNMknydqvaAIVQLAVLTHNIGRPG 428
Cdd:cd02757 312 AAAAFTWRGATMQNRGSYNSM-------ACHALNGLVGSIDSKG 348
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| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
760-803 |
1.20e-06 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate reductase, subunit A, (TtrA); respiratory arsenate As(V) reductase, catalytic subunit (ArrA); and other related proteins.
Pssm-ID: 239181 [Multi-domain] Cd Length: 143 Bit Score: 48.83 E-value: 1.20e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 55773483 760 YVEVNPEDAKRLGLKSGDLVEVYNEEGNGTFLVYVTDAVKPGTL 803
Cdd:cd02780 31 PVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRPGVV 74
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| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
760-803 |
4.59e-06 |
|
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO.This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239194 [Multi-domain] Cd Length: 129 Bit Score: 46.86 E-value: 4.59e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 55773483 760 YVEVNPEDAKRLGLKSGDLVEVYNEEgnGTFL--VYVTDAVKPGTL 803
Cdd:cd02793 34 PIRINPADAAARGIADGDIVRVFNDR--GACLagAVVTDGIMPGVV 77
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|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
761-841 |
4.37e-05 |
|
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: 43.92 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 761 VEVNPEDAKRLGLKSGDLVEVYNEEGNGTFLVYVTDAVKPGTLFLVM---YHWRGTS----------NSLVTG-YTDPKT 826
Cdd:cd02782 35 LRIHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMPGVVSLPHgwgHDYPGVSgagsrpgvnvNDLTDDtQRDPLS 114
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90
....*....|....*
gi 55773483 827 TIPWYKGTRANLRKV 841
Cdd:cd02782 115 GNAAHNGVPVRLARV 129
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| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
763-803 |
4.64e-05 |
|
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: 43.82 E-value: 4.64e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 55773483 763 VNPEDAKRLGLKSGDLVEVYNEEGNGTFLVYVTDAVKPGTL 803
Cdd:cd02794 34 INPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVV 74
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| MopB_CT_ydeP |
cd02787 |
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial ... |
761-834 |
5.17e-05 |
|
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239188 [Multi-domain] Cd Length: 112 Bit Score: 43.42 E-value: 5.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 761 VEVNPEDAKRLGLKSGDLVEVYNEEGNGT-----FLVYVTDAVKPGTLFLvmyHWRGTsNSLVT-GYTDPKTTIPWYKGT 834
Cdd:cd02787 33 VFMNPDDIARLGLKAGDRVDLESAFGDGQgrivrGFRVVEYDIPRGCLAA---YYPEG-NVLVPlDHRDPQSKTPAYKSV 108
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| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
123-437 |
1.30e-04 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 45.81 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 123 RLTYPLL--RVGDQFQAITWQDALTLMGLLIKGIRDRDgnddniAVKCFDHGGSgqgfeDNYAAgklFFAALSVKHIAIH 200
Cdd:PRK09939 108 RLTQPLKydAVSDCYKPLSWQQAFDEIGARLQSYSDPN------QVEFYTSGRT-----SNEAA---FLYQLFAREYGSN 173
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 201 NRPAYN------SEVWGSRERGVHELNYTYEDARLADTIVLWGANSYETATvfyveHMLPNIQG-ATVAEKQQAFDPGE- 272
Cdd:PRK09939 174 NFPDCSnmchepTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHP-----RMLTSLRAlVKRGAKMIAINPLQe 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 273 --------PAEPGYLIVIDPRKTSSYTVAAQVAPDrvMLLRPNLGTDYILANAIARAVWEKGYYDMAYLQARTdmTLFEE 344
Cdd:PRK09939 249 rglerftaPQNPFEMLTNSETQLASAYYNVRIGGD--MALLKGMMRLLIERDDAASAAGRPSLLDDEFIQTHT--VGFDE 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 345 YKAKSLklsvpyDEFMAQAERITGVSRAEIEKAADWIAKPKagrfkrRTLTIYEKGIIWNMKNYDQVAAIVQLAVLTHNI 424
Cdd:PRK09939 325 LRRDVL------NSEWKDIERISGLSQTQIAELADAYAAAE------RTIICYGMGITQHEHGTQNVQQLVNLLLMKGNI 392
|
330
....*....|...
gi 55773483 425 GRPGTGCGRQGGH 437
Cdd:PRK09939 393 GKPGAGICPLRGH 405
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| MopB_CT_NDH-1_NuoG2-N7 |
cd02788 |
MopB_CT_NDH-1_NuoG2-N7: C-terminal region of the NuoG-like subunit (of the variant with a ... |
756-781 |
1.38e-04 |
|
MopB_CT_NDH-1_NuoG2-N7: C-terminal region of the NuoG-like subunit (of the variant 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, 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 and a C-terminal region (this CD) homologous to the formate dehydrogenase C-terminal molybdopterin_binding (MopB) region.
Pssm-ID: 239189 [Multi-domain] Cd Length: 96 Bit Score: 41.53 E-value: 1.38e-04
10 20
....*....|....*....|....*.
gi 55773483 756 LPLPYVEVNPEDAKRLGLKSGDLVEV 781
Cdd:cd02788 26 APAPYARLSPADAARLGLADGDLVEF 51
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|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
761-803 |
2.12e-04 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 44.99 E-value: 2.12e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 55773483 761 VEVNPEDAKRLGLKSGDLVEVYNEEGNGTFLVYVTDAVKPGTL 803
Cdd:PRK14991 918 VALNPQDAARLGIQHGDRVRISTPGGSVVAQASVLNGVMPGVI 960
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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 ... |
120-239 |
1.35e-03 |
|
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: 41.96 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55773483 120 TQDRLTYPLLRVGDQFQAITWQDALTLMGLLIKGIRdRDGNDDNIAVKCFDHGGSgqgfEDNYAAGKLfFAALSVKHIAi 199
Cdd:cd02772 51 SEDRLTKPMIKKDGQWQEVDWETALEYVAEGLSAII-KKHGADQIGALASPHSTL----EELYLLQKL-ARGLGSDNID- 123
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 55773483 200 hNRPAYNSEVWGSRERGVHELNYTYEDARLADTIVLWGAN 239
Cdd:cd02772 124 -HRLRQSDFRDDAKASGAPWLGMPIAEISELDRVLVIGSN 162
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