|
Name |
Accession |
Description |
Interval |
E-value |
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
53-941 |
0e+00 |
|
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other related proteins. The Salmonella enterica tetrathionate reductase catalyses the reduction of trithionate but not sulfur or thiosulfate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239159 [Multi-domain] Cd Length: 735 Bit Score: 1045.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 53 FSSCLGCNVRCGIVARVVKYgdVEVIERIEGNPYHVYNRAVSFDKQIKRYAPlPYNTPVKEALEKWSGTLCPRGADGIHY 132
Cdd:cd02758 1 YSSCLGCWTQCGIRVRVDKE--TGKVLRIAGNPYHPLNTAPSLPYNTPLKES-LYLSLVGENGLKARATACARGNAGLQY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 133 VYDPYRVLKPLKRAGPRGSGKWKAITWEQLINEVVNGGVIEETGERLPGlkeffaygklkeagfedpnailsemkidvdn 212
Cdd:cd02758 78 LYDPYRVLQPLKRVGPRGSGKWKPISWEQLIEEVVEGGDLFGEGHVEGL------------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 213 imkvardpnktyddlikaieefkakwsqrlgeKGLKLEDLLIDPDRPDLGTKANMVMYLRGRGQGHTdYFSQRWI-YAFG 291
Cdd:cd02758 127 --------------------------------KAIRDLDTPIDPDHPDLGPKANQLLYTFGRDEGRT-PFIKRFAnQAFG 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 292 SVNWTRHTSACQLGYYAGNSIWA----GYHDIQADPIGAKVIIGAGWSMGRVHPGA-TGQGLMIERACEGELKLYYVNPV 366
Cdd:cd02758 174 TVNFGGHGSYCGLSYRAGNGALMndldGYPHVKPDFDNAEFALFIGTSPAQAGNPFkRQARRLAEARTEGNFKYVVVDPV 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 367 APRTT--CNGNIIWIPVKPGEDAALAFAVIRWLIENKRYNEEFLSIPNRDSAKKLGYPVNTNATWLVITegerfgeflka 444
Cdd:cd02758 254 LPNTTsaAGENIRWVPIKPGGDGALAMAMIRWIIENERYNAEYLSIPSKEAAKAAGEPSWTNATHLVIT----------- 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 445 rdvgiedsdkpvvwtgerfatydsvdkadlyyvgkvtlpsgetVTVKTAFMIVRDEAFSKSFEDWLAIASpyerntpefa 524
Cdd:cd02758 323 -------------------------------------------VRVKSALQLLKEEAFSYSLEEYAEICG---------- 349
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 525 DYVKKIEQMAKDFADAApKAATTLHRGVGMHPNGEYIVWAYRTIDTLVGNFHRMGGLLARAAHTAYENYVYNVG-RSGFG 603
Cdd:cd02758 350 VPEAKIIELAKEFTSHG-RAAAVVHHGGTMHSNGFYNAYAIRMLNALIGNLNWKGGLLMSGGGFADNSAGPRYDfKKFFG 428
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 604 EPVRWGPPIDRHRYAYENTLEYWLRVKkalkegkswdeAVKAAFPTKRPWYPHTPEeSYTEIFAGIAEGYPYRIGALILF 683
Cdd:cd02758 429 EVKPWGVPIDRSKKAYEKTSEYKRKVA-----------AGENPYPAKRPWYPLTPE-LYTEVIASAAEGYPYKLKALILW 496
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 684 YANPVLATNYGVK-FIEVLKDPAKLPLFIVITTTINETALYADYIVPDTTYLETGTMGIQYLYatsgSVTLAESWRSPVI 762
Cdd:cd02758 497 MANPVYGAPGLVKqVEEKLKDPKKLPLFIAIDAFINETSAYADYIVPDTTYYESWGFSTPWGG----VPTKASTARWPVI 572
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 763 MPLTQRisdCPNGHPRYasFWEFFIDTAKALGMPGHGDKAIPGVKgkkyeGKWFSMHCEWEYILRVFANAALDAKDkglI 842
Cdd:cd02758 573 APLTEK---TANGHPVS--MESFLIDLAKALGLPGFGPNAIKDGQ-----GNKFPLNRAEDYYLRVAANIAYDGKA---P 639
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 843 PEDVPEEEVKFVEENYPIAQFRDILPPDEWKYVAYGLARGGVFTKYEESFDERGIskrRVPGRGTLYLWSEEVAKTRNNV 922
Cdd:cd02758 640 VPDASEEELKLTGVNRPIPALKRTLKPEEWRKVAYILARGGRFAPYEESYDGDNL---RNRWGKTLQIWNEKLAKSRNSV 716
|
890
....*....|....*....
gi 18159972 923 TGEKFWGGPKYFPIATYAP 941
Cdd:cd02758 717 TGEYFSGCPTYYPPRFADG 735
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
1-1050 |
0e+00 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 583.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 1 MTSRRAYLKAIAAAATLGIALWGYWPVVDKIIKPKRTPYG----PDPQFG------------------TNVRYVFSSCLG 58
Cdd:PRK14991 2 DKTRRQLLKGGLAAGGLAAFAAGYSDTAKRAAKGLLNGTSgkptRDRIHGnsltpeyrvdaqgqlqpnPQQRVANTQCLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 59 CNVRCGIVARVVKYGDvEVIeRIEGNPYHvynrAVSFDKqikryaPLPYNTPVKEALEKWSG--------TLCPRGADGI 130
Cdd:PRK14991 82 CWTQCGVRVRVDNATN-KIL-RIAGNPYH----PLSTDH------HIDMSTPVKEAFESLSGesglegrsTACARGNAML 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 131 HYVYDPYRVLKPLKRAGPRGSGKWKAITWEQLINEVVNGGvieetgerlpglkEFFAYGKLkeagfedpnailsemkidv 210
Cdd:PRK14991 150 EQLDSPYRVLQPLKRVGKRGSGKWQRISFEQLVEEVVEGG-------------DLFGEGHV------------------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 211 dnimkvardpnktydDLIKAIEEFKAkwsqrlgekglkledlLIDPDRPDLGTKANMVMYLRGRGQGHTDYFSQRWIYAF 290
Cdd:PRK14991 198 ---------------DGLRAIRDLDT----------------PIDAKNPEYGPKANQLLVTNASDEGRDAFIKRFAFNSF 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 291 GSVNWTRHTSACQLGYYAGNSiwAGYHDIQADPIG------AKVIIGAGWSmgrvhPGATG-----QGLMIERA-CEGEL 358
Cdd:PRK14991 247 GTRNFGNHGSYCGLAYRAGSG--ALMGDLDKNPHVkpdwdnVEFALFIGTS-----PAQSGnpfkrQARQLANArTRGNF 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 359 KLYYVNPVAPRTT---CNGNIIWIPVKPGEDAALAFAVIRWLIENKRYNEEFLSIPNRDSAKKLGYPVNTNATWLVITEG 435
Cdd:PRK14991 320 EYVVVAPALPLSSslaAGDNNRWLPIRPGTDSALAMGMIRWIIDNQRYNADYLAQPGVAAMQAAGEASWTNATHLVIADP 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 436 E--RFGEFLKARDVGI-------EDSDKPVVW---TGErFATYDSVDKADLYYVGKVTLPSGETVTVKTAFMIVRDEAFS 503
Cdd:PRK14991 400 GhpRYGQFLRASDLGLpfegearGDGEDTLVVdaaDGE-LVPATQAQPARLFVEQYVTLADGQRVRVKSSLQLLKEAARK 478
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 504 KSFEDWLAIASpyernTPEfadyvKKIEQMAKDFADAAPKAATTLHRGVgMHPNGEYIVWAYRTIDTLVGNFHRMGGLLA 583
Cdd:PRK14991 479 LSLAEYSEQCG-----VPE-----AQIIALAEEFTSHGRKAAVISHGGT-MSGNGFYNAWAIMMLNALIGNLNLKGGVVV 547
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 584 RAAhtayenyvynvGRSGFGEPVRW------------GPPIDRHRYAYENTLEYwlRVKKalkegkswdEAVKAAFPTKR 651
Cdd:PRK14991 548 GGG-----------KFPGFGDGPRYnlasfagkvkpkGVSLSRSKFPYEKSSEY--RRKV---------EAGQSPYPAKA 605
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 652 PWYPHTPEESyTEIFAGIAEGYPYRIGALILFYANPVlatnYGVKFI-----EVLKDPAKLPLFIVITTTINETALYADY 726
Cdd:PRK14991 606 PWYPFVAGLL-TEMLTAALEGYPYPLKAWINHMSNPI----YGVPGLravieEKLKDPKKLPLFISIDAFINETTALADY 680
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 727 IVPDTTYLETGTMGIQYlyatSGSVTLAESWRSPVIMPLTQRISDcpnGHPryASFWEFFIDTAKALGMPGHGDKAIpgv 806
Cdd:PRK14991 681 IVPDTHTYESWGFTAPW----GGVPTKASTARWPVVEPRTAKTAD---GQP--VCMESFLIAVAKRLQLPGFGDNAI--- 748
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 807 kgKKYEGKWFSMHCEWEYILRVFANAALDAKdkglipEDVPE---EEVKF--VEENYPIAQFRdiLPPDEWKYVAYGLAR 881
Cdd:PRK14991 749 --KDAQGNTHPLNRAEDFYLRGAANIAYLGK------TPVADasdEDIALtgVSRILPALQAT--LKPDEVRRVAFIYAR 818
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 882 GGVFTKYEESFDERGISKRRvpgRGTLYLWSEEVAKTRNNVTGEKFWGGPKYFPiatyapavPAFqkADewlhGTPLRQL 961
Cdd:PRK14991 819 GGRFAPAESAYDEERMGNRW---KKPLQIWNEDVAAARHSMTGERYSGCPTWYP--------PRL--AD----GTPLREQ 881
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 962 YPEKEWPFILILYTGPL---YTKHRSQfyywIKQVVPENFVLINPEDAAKLGVETGDVIKVETPVGAFEAPAVVEPAVAP 1038
Cdd:PRK14991 882 FPESQWPLLLISFKSNLmssMSIASPR----LRQVKPANPVALNPQDAARLGIQHGDRVRISTPGGSVVAQASVLNGVMP 957
|
1130
....*....|..
gi 18159972 1039 GVIMVPYGMGRW 1050
Cdd:PRK14991 958 GVIAIEHGYGHR 969
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
46-1049 |
1.01e-62 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 227.03 E-value: 1.01e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 46 GTNVRYVFSSCLGCNVRCGIVARVVKygdvEVIERIEGNPYHVYNRavsfdkqikryaplpyntpvkealekwsGTLCPR 125
Cdd:COG0243 18 AAGTKTVKTTCPGCGVGCGLGVKVED----GRVVRVRGDPDHPVNR----------------------------GRLCAK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 126 GADGIHYVYDPYRVLKPLKRAGPRGSGKWKAITWEQLINEVvnggvieetGERLPGLKEffAYGklkeagfedPNAILse 205
Cdd:COG0243 66 GAALDERLYSPDRLTYPMKRVGPRGSGKFERISWDEALDLI---------AEKLKAIID--EYG---------PEAVA-- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 206 mkidvdnimkvardpnktyddlikaieefkakwsqrlgekglkledllidpdrpdlgtkanmvMYLRGRGQGHT----DY 281
Cdd:COG0243 124 ---------------------------------------------------------------FYTSGGSAGRLsneaAY 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 282 FSQRWIYAFGSVNWTRHTSAC----QLGYYA--GNSIWAG-YHDIQAdpigAKVIIGAGWSMGRVHPGATGQglMIERAC 354
Cdd:COG0243 141 LAQRFARALGTNNLDDNSRLChesaVAGLPRtfGSDKGTVsYEDLEH----ADLIVLWGSNPAENHPRLLRR--LREAAK 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 355 EGELKLYYVNPVAPRTTCNGNIiWIPVKPGEDAALAFAVIRWLIENKRYNEEFLsipnrdsakklgypvntnATWlviTE 434
Cdd:COG0243 215 KRGAKIVVIDPRRTETAAIADE-WLPIRPGTDAALLLALAHVLIEEGLYDRDFL------------------ARH---TV 272
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 435 GerfgeflkardvgiedsdkpvvwtgerfatydsvdkadlyyvgkvtlpsgetvtvktafmivrdeafsksFEDWLAIAS 514
Cdd:COG0243 273 G----------------------------------------------------------------------FDELAAYVA 282
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 515 PYernTPEFA------DyVKKIEQMAKDFAdAAPKAATTLHRGVGMHPNGEYIVWAYRTIDTLVGNFHRMGGLLARAAHT 588
Cdd:COG0243 283 AY---TPEWAaeitgvP-AEDIRELAREFA-TAKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGGPFSLTGE 357
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 589 Ayenyvynvgrsgfgepvrwgppidrhryayentleywlrvkkalkegkswdeavkaafptkrpwyphtpeesyteifag 668
Cdd:COG0243 358 A------------------------------------------------------------------------------- 358
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 669 IAEGYPYRIGALILFYANPVLATNYGVKFIEVLKdpaKLPLFIVITTTINETALYADYIVPDTTYLE----TGTMGIQYL 744
Cdd:COG0243 359 ILDGKPYPIKALWVYGGNPAVSAPDTNRVREALR---KLDFVVVIDTFLTETARYADIVLPATTWLErddiVTNSEDRRV 435
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 745 yatsgsvtlaeSWRSPVIMPLTQRISDcpnghpryasfWEFFIDTAKALGMpghgdkaipgvkgkkyegkwfsmhcewey 824
Cdd:COG0243 436 -----------HLSRPAVEPPGEARSD-----------WEIFAELAKRLGF----------------------------- 464
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 825 ilrvfanaaldakdKGLIPEDVPEEEVkfveenypiaqFRDILPPdewkyvayglARGGVFTkYEEsFDERGISKRRVPG 904
Cdd:COG0243 465 --------------EEAFPWGRTEEDY-----------LRELLEA----------TRGRGIT-FEE-LREKGPVQLPVPP 507
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 905 rGTLYLWseevaktrnnvtgEKFWGGP--KY--FPIATYAPAVPAFQKADEWLHGtplrqlyPEKEWPFILIlyTGPLYT 980
Cdd:COG0243 508 -EPAFRN-------------DGPFPTPsgKAefYSETLALPPLPRYAPPYEGAEP-------LDAEYPLRLI--TGRSRD 564
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18159972 981 KHRSQFYY--WIKQVVPENFVLINPEDAAKLGVETGDVIKVETPVGAFEAPAVVEPAVAPGVIMVPYGMGR 1049
Cdd:COG0243 565 QWHSTTYNnpRLREIGPRPVVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTEGIRPGVVFAPHGWWY 635
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
967-1159 |
5.66e-53 |
|
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: 181.72 E-value: 5.66e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 967 WPFILILYTgPLYTKHRSQFYYWIKQVVPENFVLINPEDAAKLGVETGDVIKVETPVGAFEAPAVVEPAVAPGVIMVPYG 1046
Cdd:cd02780 1 YPFILVTFK-SNLNSHRSANAPWLKEIKPENPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRPGVVAIEHG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 1047 MGRWADTVVVKPKyfelkdarakslidelpdkveipedavnpvkhlpdvvkkllftkspaeyYEKGLAVDKWRFNGVTPN 1126
Cdd:cd02780 80 YGHWAYGAVASTI-------------------------------------------------DGKDLPGDAWRGAGVNIN 110
|
170 180 190
....*....|....*....|....*....|...
gi 18159972 1127 VAEMADPSLGGWPLLSWLGAAQAYFDTPARIVK 1159
Cdd:cd02780 111 DIGLVDPSRGGWSLVDWVGGAAARYDTPVKIEK 143
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
52-735 |
1.27e-32 |
|
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: 134.10 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 52 VFSSCLGCNVRCGIVARVvkygDVEVIERIEGNPYHVYNRavsfdkqikryaplpyntpvkealekwsGTLCPRGADGIH 131
Cdd:cd02757 2 VPSTCQGCTAWCGLQAYV----EDGRVTKVEGNPLHPGSR----------------------------GRLCAKGHLGLQ 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 132 YVYDPYRVLKPLKRAGPRG----SGKWKAITWEQLINEVVnggvieetgerlpglkeffaygklkeagfedpnailsemk 207
Cdd:cd02757 50 QVYDPDRILYPMKRTNPRKgrdvDPKFVPISWDEALDTIA---------------------------------------- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 208 idvdnimkvardpnktyDDLIKAIEEfkakwsqrlgekglkledllidpDRPdlgtkaNMVMYLRGRGQGHTDYFSQRWI 287
Cdd:cd02757 90 -----------------DKIRALRKE-----------------------NEP------HKIMLHRGRYGHNNSILYGRFT 123
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 288 YAFGSVNWTRHTSACQLGYYAGNSIWAGYHDI-QADPIGAKVIIGAGWS---MGRVHPGAtgqglmiERACEGELKLYYV 363
Cdd:cd02757 124 KMIGSPNNISHSSVCAESEKFGRYYTEGGWDYnSYDYANAKYILFFGADpleSNRQNPHA-------QRIWGGKMDQAKV 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 364 NPVAPR--TTCNGNIIWIPVKPGEDAALAFAVIRWLIENKRYNEEFLsipnrdsakklgypvntnatwlvitegerfgef 441
Cdd:cd02757 197 VVVDPRlsNTAAKADEWLPIKPGEDGALALAIAHVILTEGLWDKDFV--------------------------------- 243
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 442 lkardvgiedsdkpvvwtgerfatYDSVDkadlyyvGKVTLPSGETVTVKTAfmivrDEAFSKSFEDWLAIAspYERNTP 521
Cdd:cd02757 244 ------------------------GDFVD-------GKNYFKAGETVDEESF-----KEKSTEGLVKWWNLE--LKDYTP 285
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 522 EFADYV-----KKIEQMAKDFADAAPKAATTLHRGVGMHPNGEYIVWAYRTIDTLVGNFHRMGGLLaraahtayenyvyn 596
Cdd:cd02757 286 EWAAKIsgipaETIERVAREFATAAPAAAAFTWRGATMQNRGSYNSMACHALNGLVGSIDSKGGLC-------------- 351
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 597 vgrsgfgePVRWGPPIDRHryayentLEYWLRVKKALKEGKSWDEAVkaafptkrpwyphtpeesyteifagiaegypyr 676
Cdd:cd02757 352 --------PNMGVPKIKVY-------FTYLDNPVFSNPDGMSWEEAL--------------------------------- 383
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 18159972 677 igalilfyanpvlatnygvkfievlkdpAKLPLFIVITTTINETALYADYIVPDTTYLE 735
Cdd:cd02757 384 ----------------------------AKIPFHVHLSPFMSETTYFADIVLPDGHHFE 414
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
54-793 |
2.00e-29 |
|
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: 121.67 E-value: 2.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 54 SSCLGCNVRCGIVARVvKYGdveVIERIEGNPYHVYNRavsfdkqikryaplpyntpvkealekwsGTLCPRGADGIHYV 133
Cdd:cd00368 2 SVCPFCGVGCGILVYV-KDG---KVVRIEGDPNHPVNE----------------------------GRLCDKGRAGLDGL 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 134 YDPYRVLKPLKRAGPRgsGKWKAITWEQLINEVVNggvieetgerlpglkeffaygKLKEAgfedpnailsemkidvdni 213
Cdd:cd00368 50 YSPDRLKYPLIRVGGR--GKFVPISWDEALDEIAE---------------------KLKEI------------------- 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 214 mKVARDPNKtyddlikaieefkakwsqrlgekglkledllidpdrpdlgtkanmVMYLRGRGQGHTD-YFSQRWIYAFGS 292
Cdd:cd00368 88 -REKYGPDA---------------------------------------------IAFYGGGGASNEEaYLLQKLLRALGS 121
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 293 VNWTRHTSACQLGYYAGNSIWAGYHDI--QADPIGAKVIIGAGWSMGRVHPgatGQGLMIERACEGELKLYYVNPVAPRT 370
Cdd:cd00368 122 NNVDSHARLCHASAVAALKAFGGGAPTntLADIENADLILLWGSNPAETHP---VLAARLRRAKKRGAKLIVIDPRRTET 198
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 371 TCNGNiIWIPVKPGEDAALAFAvirwlienkryneeflsipnrdsakklgypvntnatwlvitegerfgeflkardvgie 450
Cdd:cd00368 199 AAKAD-EWLPIRPGTDAALALA---------------------------------------------------------- 219
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 451 dsDKPVVWTGerfatydsVDKADlyyvgkvtlpsgetvtvktafmivrdeafsksfedwlaiaspyerntpefadyvkkI 530
Cdd:cd00368 220 --EWAAEITG--------VPAET--------------------------------------------------------I 233
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 531 EQMAKDFAdAAPKAATTLHRGVGMHPNGEYIVWAYRTIDTLVGNFHRMGGLLARAahtayenyvynvgrsgfgepvrwgp 610
Cdd:cd00368 234 RALAREFA-AAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGPG------------------------- 287
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 611 pidrhryayentleywlrvkkalkegkswdeavkaafptkrpwyphtpeesyteifagiaegypyrigalilfyANPVLA 690
Cdd:cd00368 288 --------------------------------------------------------------------------GNPLVS 293
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 691 TNYGVKFIEVLKdpaKLPLFIVITTTINETALYADYIVPDTTYLEtgtmgiqylyaTSGSVTLAE---SWRSPVIMPLTQ 767
Cdd:cd00368 294 APDANRVRAALK---KLDFVVVIDIFMTETAAYADVVLPAATYLE-----------KEGTYTNTEgrvQLFRQAVEPPGE 359
|
730 740
....*....|....*....|....*.
gi 18159972 768 RISDcpnghpryasfWEFFIDTAKAL 793
Cdd:cd00368 360 ARSD-----------WEILRELAKRL 374
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
52-735 |
8.04e-29 |
|
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: 121.25 E-value: 8.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 52 VFSSCLGCNVRCGIVARVVkygDVEVIeRIEGNPYHVYNRavsfdkqikryaplpyntpvkealekwsGTLCPRGADGIH 131
Cdd:cd02755 1 VPSICEMCSSRCGILARVE---DGRVV-KIDGNPLSPLSR----------------------------GKLCARGNAGIQ 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 132 YVYDPYRVLKPLKRAGPRGSGKWKAITWEQLINEVvnggvieetGERLPGLKEffAYGklkeagfedPNAILsemkidvd 211
Cdd:cd02755 49 LLYDPDRLKKPLIRVGERGEGKFREASWDEALQYI---------ASKLKEIKE--QHG---------PESVL-------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 212 nimkvardpnktyddlikaieefkakWSqrlgekglkledllidpdrpdlgtkanmvmylrGRGQGHTDYFsQRWIYAFG 291
Cdd:cd02755 101 --------------------------FG---------------------------------GHGGCYSPFF-KHFAAAFG 120
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 292 SVNWTRHTSACQLGYY-AGNSIWAGYH-DIQADPIGAKVIIGAGWSM--GRVHPGATGQGLMIERACegelKLYYVNPVA 367
Cdd:cd02755 121 SPNIFSHESTCLASKNlAWKLVIDSFGgEVNPDFENARYIILFGRNLaeAIIVVDARRLMKALENGA----KVVVVDPRF 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 368 PRTTCNGNiIWIPVKPGEDAALAFAVIRWLIENKRYNEEFLSipnrdsakklgypvntnatwlvitegerfgeflkardv 447
Cdd:cd02755 197 SELASKAD-EWIPIKPGTDLAFVLALIHVLISENLYDAAFVE-------------------------------------- 237
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 448 giedsdkpvvwtgerfatydsvdkadlYYVgkvtlpsgetvtvkTAFMIVRDEafsksfedwlaiASPYernTPEFADYV 527
Cdd:cd02755 238 ---------------------------KYT--------------NGFELLKAH------------VKPY---TPEWAAQI 261
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 528 -----KKIEQMAKDFADAAPKA-ATTLHRGVGMHpNGEYIVWAYRTIDTLVGNFHRMGGLLARAAHtayenyvynvgrsg 601
Cdd:cd02755 262 tdipaDTIRRIAREFAAAAPHAvVDPGWRGTFYS-NSFQTRRAIAIINALLGNIDKRGGLYYAGSA-------------- 326
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 602 fgepvrwgppidrhryayentleywlrvkkalkegkswdeavkaafptkrpwyphtpeesyteifagiaegYPYRIGALI 681
Cdd:cd02755 327 -----------------------------------------------------------------------KPYPIKALF 335
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 18159972 682 LFYANPVLATNYGVKFIEVLKdpaKLPLFIVITTTINETALYADYIVPDTTYLE 735
Cdd:cd02755 336 IYRTNPFHSMPDRARLIKALK---NLDLVVAIDILPSDTALYADVILPEATYLE 386
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
48-1049 |
2.83e-27 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 119.39 E-value: 2.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 48 NVRYVFSSCLGCNVRCGIVARVVKYGDVevieRIEGNPYhvynrAVSFdkqikryaplpyntpvkealekwSGTLCPRGA 127
Cdd:PRK15488 40 KTKLTPSICEMCSTRCPIEARVVNGKNV----FIQGNPK-----AKSF-----------------------GTKVCARGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 128 DGIHYVYDPYRVLKPLKRAGPRGSGKWKAITWEQlinevvnggvieetgerlpglkeffaygklkeagfedpnailsemk 207
Cdd:PRK15488 88 SGHSLLYDPQRIVKPLKRVGERGEGKWQEISWDE---------------------------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 208 idvdnimkvardpnkTYDDLIKAIEEFKAKWSqrlgekglkledllidpdrpdlgtkANMVMYLRGRGQGHTDYFSqrWI 287
Cdd:PRK15488 122 ---------------AYQEIAAKLNAIKQQHG-------------------------PESVAFSSKSGSLSSHLFH--LA 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 288 YAFGSVNWTRHTSACQLGY-YAGNSIWAGyhDIQADPIGAKVIIGAGWSM--GRVHPGATGqglMIERACEGELKLYYVN 364
Cdd:PRK15488 160 TAFGSPNTFTHASTCPAGYaIAAKVMFGG--KLKRDLANSKYIINFGHNLyeGINMSDTRG---LMTAQMEKGAKLVVFE 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 365 P----VAPRTTcngniIWIPVKPGEDAALAFAVIRWLIENKRYNEEFlsipnrdsakklgypvntnatwlvitegerfge 440
Cdd:PRK15488 235 PrfsvVASKAD-----EWHAIRPGTDLAVVLALCHVLIEENLYDKAF--------------------------------- 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 441 flkardvgiedsdkpvvwtgerfatydsVDKadlYYVGkvtlpsgetvtvktafmivrdeafsksFEDWLAIASPYernT 520
Cdd:PRK15488 277 ----------------------------VER---YTSG---------------------------FEELAASVKEY---T 295
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 521 PEFADYV-----KKIEQMAKDFADAAPKA-------ATTLHRGVGMHPngeyivwAYRTIDTLVGNFHRMGGL-LARAAH 587
Cdd:PRK15488 296 PEWAEAIsdvpaDDIRRIARELAAAAPHAivdfghrATFTPEEFDMRR-------AIFAANVLLGNIERKGGLyFGKNAS 368
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 588 T----AYENYVYNVGRSGF-GEPVRWGPPIDR--HRYAYENTleywlrvkkalKEGkswdeavkaafptkrpwyphtpee 660
Cdd:PRK15488 369 VynklAGEKVAPTLAKPGVkGMPKPTAKRIDLvgEQFKYIAA-----------GGG------------------------ 413
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 661 SYTEIFAGIAEGYPYRIGALILFYANPVLATNYGVKFIEVLKdpaKLPLFIVITTTINETALYADYIVPDTTYLETGTmG 740
Cdd:PRK15488 414 VVQSIIDATLTQKPYQIKGWVMSRHNPMQTVTDRADVVKALK---KLDLVVVCDVYLSESAAYADVVLPESTYLERDE-E 489
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 741 IQylyatsgsvtlAESWRSPVIMpLTQRISDcPNGHPRYAsfWEFFIDTAKALGMpghgdkaipgvkgkkyeGKWFSmhc 820
Cdd:PRK15488 490 IS-----------DKSGKNPAYA-LRQRVVE-PIGDTKPS--WQIFKELGEKMGL-----------------GQYYP--- 534
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 821 eWEYI-----LRVFANAALDA--KDKGLIPEDVP----EEEV--KFVEEnYPIAQFRDilppdewkyvayglarggvftk 887
Cdd:PRK15488 535 -WQDMetlqlYQVNGDHALLKelKKKGYVSFGVPlllrEPKMvaKFVAR-YPNAKAVD---------------------- 590
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 888 yEESFDERGISKRRVPGRGTLYLWS-EEVAKTRnnvtgekfwGGPKYFPIATyapavpafQKADEwlhgtplrqLYpeke 966
Cdd:PRK15488 591 -EDGTYGSQLKFKTPSGKIELFSAKlEALAPGY---------GVPRYRDVAL--------KKEDE---------LY---- 639
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 967 wpfiLILYTGPLYTKHRSQFYYWIKQVVPENFVLINPEDAAKLGVETGDVIKVETPVGAFEAPAVVEPAVAPGVIMVPYG 1046
Cdd:PRK15488 640 ----FIQGKVAVHTNGATQNVPLLANLMSDNAVWIHPQTAGKLGIKNGDEIRLENSVGKEKGKALVTPGIRPDTLFAYMG 715
|
...
gi 18159972 1047 MGR 1049
Cdd:PRK15488 716 FGS 718
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
49-1055 |
3.05e-21 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 99.96 E-value: 3.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 49 VRYVFSSCLGCNVRCGIVARVvkygDVEVIERIEGNPYHVYNRavsfdkqikryaplpyntpvkealekwsGTLCPRGAD 128
Cdd:COG3383 4 MKKVKTVCPYCGVGCGIDLEV----KDGKIVKVEGDPDHPVNR----------------------------GRLCVKGRF 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 129 GIHYVYDPYRVLKPLKRAGprgsGKWKAITWEQLINEVVnggvieetgERLPGLKEffAYGKlkeagfeDPNAILSEmki 208
Cdd:COG3383 52 GFEFVNSPDRLTTPLIRRG----GEFREVSWDEALDLVA---------ERLREIQA--EHGP-------DAVAFYGS--- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 209 dvdnimkvARDPNktyddlikaiEEfkakwsqrlgekglkledllidpdrpdlgtkanmvMYLRG---RGqghtdyfsqr 285
Cdd:COG3383 107 --------GQLTN----------EE-----------------------------------NYLLQklaRG---------- 123
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 286 wiyAFGSVNW---TR--HTSACQ-----LGYYAG-NSiwagYHDIqadpIGAKVIIGAGWSMGRVHPGAtgqGLMIERAC 354
Cdd:COG3383 124 ---VLGTNNIdnnARlcMASAVAglkqsFGSDAPpNS----YDDI----EEADVILVIGSNPAEAHPVL---ARRIKKAK 189
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 355 EGELKLYYVNPVapRT-TCNGNIIWIPVKPGEDAALAFAVIRWLIENKRYNEEFlsIPNRdsakklgypvntnatwlviT 433
Cdd:COG3383 190 KNGAKLIVVDPR--RTeTARLADLHLQIKPGTDLALLNGLLHVIIEEGLVDEDF--IAER-------------------T 246
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 434 EGerFGEFLKArdvgIEDsdkpvvWTGERFATYDSVDKADlyyvgkvtlpsgetvtvktafmivrdeafsksfedwlaia 513
Cdd:COG3383 247 EG--FEELKAS----VAK------YTPERVAEITGVPAED---------------------------------------- 274
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 514 spyerntpefadyvkkIEQMAKDFAdAAPKAATTLHRGVGMHPNGEYIVWAyrtidtlVGNFHRMGGllaraahtayeny 593
Cdd:COG3383 275 ----------------IREAARLIA-EAKRAMILWGMGVNQHTQGTDNVNA-------IINLALATG------------- 317
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 594 vyNVGRSGFG-EPVR----------WGppidrhryAYENTLEYWLRVKkalkegkswDEAVKAAFptKRPWY----PHTP 658
Cdd:COG3383 318 --NIGRPGTGpFPLTgqnnvqggrdMG--------ALPNVLPGYRDVT---------DPEHRAKV--ADAWGvpplPDKP 376
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 659 EESYTEIFAGIAEGypyRIGALILFYANPVL-ATNYGvKFIEVLKdpaKLPLFIVITTTINETALYADYIVPDTTYLETg 737
Cdd:COG3383 377 GLTAVEMFDAIADG---EIKALWIIGENPAVsDPDAN-HVREALE---KLEFLVVQDIFLTETAEYADVVLPAASWAEK- 448
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 738 tmgiqylyatSGSVTLAE---SWRSPVIMPLTQRISDcpnghpryasfWEFFIDTAKALGmpghgdkaipgvkgkkyegk 814
Cdd:COG3383 449 ----------DGTFTNTErrvQRVRKAVEPPGEARPD-----------WEIIAELARRLG-------------------- 487
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 815 wfsmhCEWEYilrvfanaaldaKDkgliPEDVPEEevkfveenypIAQfrdilppdewkyvayglarggvftkyeESFDE 894
Cdd:COG3383 488 -----YGFDY------------DS----PEEVFDE----------IAR---------------------------LTPDY 509
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 895 RGISKRRVPGRGTLYlWSeevaktrnnVTGEKFWGGPKYFPIATYAPAVPAFQKADEWlhgTPLRQLyPEKEWPFILIly 974
Cdd:COG3383 510 SGISYERLEALGGVQ-WP---------CPSEDHPGTPRLFTGRFPTPDGKARFVPVEY---RPPAEL-PDEEYPLVLT-- 573
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 975 TGPLY----TKHRSQFYYWIKQVVPENFVLINPEDAAKLGVETGDVIKVETPVGAFEAPAVVEPAVAPGVIMVPYgmgRW 1050
Cdd:COG3383 574 TGRLLdqwhTGTRTRRSPRLNKHAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGEVVLRARVTDRVRPGTVFMPF---HW 650
|
....*
gi 18159972 1051 ADTVV 1055
Cdd:COG3383 651 GEGAA 655
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
989-1052 |
3.55e-20 |
|
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site. This hierarchy is of the conserved MopB_CT domain present in many, but not all, MopB homologs.
Pssm-ID: 239176 [Multi-domain] Cd Length: 101 Bit Score: 86.60 E-value: 3.55e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18159972 989 WIKQVVPENFVLINPEDAAKLGVETGDVIKVETPVGAFEAPAVVEPAVAPGVIMVPYGMGRWAD 1052
Cdd:cd02775 15 WLRELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGHRGG 78
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
55-408 |
2.70e-18 |
|
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: 89.29 E-value: 2.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 55 SCLGCNVRCGIVArVVKYGDVEvieRIEGNPYHVYNRavsfdkqikryaplpyntpvkealekwsGTLCPRGADGIHYVY 134
Cdd:cd02759 3 TCPGCHSGCGVLV-YVKDGKLV---KVEGDPNHPTNK----------------------------GRLCMRGLAAPEIVY 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 135 DPYRVLKPLKRAGPRGSGKWKAITWEQLINEVvnggvieetGERLPGLKEffAYGklkeagfedPNAIlsemkidvdnim 214
Cdd:cd02759 51 HPDRLLYPLKRVGERGENKWERISWDEALDEI---------AEKLAEIKA--EYG---------PESI------------ 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 215 kvardpnktyddlikaieefkAKWSqrlgekglkledllidpdrpdlGTkanmvmylrGRGQG-HTDYFSQRWIYAFGSV 293
Cdd:cd02759 99 ---------------------ATAV----------------------GT---------GRGTMwQDSLFWIRFVRLFGSP 126
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 294 NWTRHTSACQLGYYAGNSIWAGYHDI--QADPIGAKVII--GAGWSMGRVHPGATGQGLMIERACegelKLYYVNP---- 365
Cdd:cd02759 127 NLFLSGESCYWPRDMAHALTTGFGLGydEPDWENPECIVlwGKNPLNSNLDLQGHWLVAAMKRGA----KLIVVDPrltw 202
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 18159972 366 VAPRTTcngniIWIPVKPGEDAALAFAVIRWLIENKRYNEEFL 408
Cdd:cd02759 203 LAARAD-----LWLPIRPGTDAALALGMLNVIINEGLYDKDFV 240
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
54-764 |
9.81e-16 |
|
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), and other related proteins. The phenylacetyl-CoA:acceptor oxidoreductase has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239161 [Multi-domain] Cd Length: 760 Bit Score: 82.33 E-value: 9.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 54 SSCLGCNVRCGIVARVVKYGdveVIERIEGNPyhvynravsfdkqikryaplpyntpVKEALEKWSGTLCPRGADGIHYV 133
Cdd:cd02760 2 TYCYNCVAGPDFMAVKVVDG---VATEIEPNF-------------------------AAEDIHPARGRVCVKAYGLVQKT 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 134 YDPYRVLKPLKRAGPRgSGK-----WKAITWEQLINEVVnggvieetgERLPGLKEffaYGKLKEAGFEDPNAILSEmki 208
Cdd:cd02760 54 YNPNRVLQPMKRTNPK-KGRnedpgFVPISWDEALDLVA---------AKLRRVRE---KGLLDEKGLPRLAATFGH--- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 209 dvdnimkvardpNKTYDDLIKAIEEFKAKWsqrlgekglkledllidpdrpdlGTkANMVMylrGRGQGHTDYFSQRWIY 288
Cdd:cd02760 118 ------------GGTPAMYMGTFPAFLAAW-----------------------GP-IDFSF---GSGQGVKCVHSEHLYG 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 289 AFGSVNWTrhtsacqlgyYAGNSIWAGYhdiqADPIGAKVIIGAGWSMGRVHPGATGQGLmieracegelKLYYVNP-VA 367
Cdd:cd02760 159 EFWHRAFT----------VAADTPLANY----VISFGSNVEASGGPCAVTRHADARVRGY----------KRVQVEPhLS 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 368 PRTTCNGNiiWIPVKPGEDAALAFAVIRWLIENK---RYNEEFLsipnRDsakklgypvNTNATWLVITEGerfgefLKA 444
Cdd:cd02760 215 VTGACSAE--WVPIRPKTDPAFMFAMIHVMVHEQglgKLDVPFL----RD---------RTSSPYLVGPDG------LYL 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 445 RDvgiEDSDKPVVW-----TGERFATYDSVD--KADLYYVGKVT-LPSGET-----VTVKTAFMIVRDEafsksfedwla 511
Cdd:cd02760 274 RD---AATGKPLVWdersgRAVPFDTRGAVPavAGDFAVDGAVSvDADDETaihqgVEGTTAFTMLVEH----------- 339
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 512 iaspYERNTPEFADYV-----KKIEQMAKDFADAAP---------------KAATTLHRGVGMHPNGEYIVWAYRTIDTL 571
Cdd:cd02760 340 ----MRKYTPEWAESIcdvpaATIRRIAREFLENASigstievdgvtlpyrPVAVTLGKSVNNGWGAFECCWARTLLATL 415
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 572 VGNFHRMGGLLAR--AAHTAYEN---YVYnVGRSGFGEPVRWgpPIDRHRYAYENTLEYWLRVKKALKEGKSWDEavkAA 646
Cdd:cd02760 416 VGALEVPGGTLGTtvRLNRPHDDrlaSVK-PGEDGFMAQGFN--PTDKEHWVVKPTGRNAHRTLVPIVGNSAWSQ---AL 489
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 647 FPTKRPWYphtpeeSYTEIFAGIAEGYPYRIGALILFYANPVLATnygVKFIEVLKDPAKLPLFIVITTTINETALYADY 726
Cdd:cd02760 490 GPTQLAWM------FLREVPLDWKFELPTLPDVWFNYRTNPAISF---WDTATLVDNIAKFPFTVSFAYTEDETNWMADV 560
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 18159972 727 IVPDTTYLETGTMgiQYLYATSGSVTLAESW----RSPVIMP 764
Cdd:cd02760 561 LLPEATDLESLQM--IKVGGTKFVEQFWEHRgvvlRQPAVEP 600
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
122-580 |
1.53e-15 |
|
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: 81.37 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 122 LCPRGADGIHYVYDPYRVLKPLKRAGPRGSGKWKAITWEQLINEVvnggvieetGERLPGLKEffAYGKlKEAGFedpna 201
Cdd:cd02765 39 GCTRGLSHLQRVYSPDRLKYPMKRVGERGEGKFERITWDEALDTI---------ADKLTEAKR--EYGG-KSILW----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 202 ilsemkidvdnimkvardpnktyddLIKAIEEFKAKWsQRLGEKGLKLEDllidpdrpDLGTKANMvmylrGRGQGhtdy 281
Cdd:cd02765 102 -------------------------MSSSGDGAILSY-LRLALLGGGLQD--------ALTYGIDT-----GVGQG---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 282 fsQRWIYAFGSVnwtrhtsacqlgyYAGNSIwagyhdiqADPIGAKVIIGAGWSMGRVHpgaTGQGLMIERACEGELKLY 361
Cdd:cd02765 139 --FNRVTGGGFM-------------PPTNEI--------TDWVNAKTIIIWGSNILETQ---FQDAEFFLDARENGAKIV 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 362 YVNPVAPRTTCNGNIiWIPVKPGEDAALAFAVIRWLIENKRYNEEFLsipnrdsaKKlgypvNTNATWLViteGERFGEF 441
Cdd:cd02765 193 VIDPVYSTTAAKADQ-WVPIRPGTDPALALGMINYILEHNWYDEAFL--------KS-----NTSAPFLV---REDNGTL 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 442 LKARDVGIEDSDKP-VVWTGERfATYDSVDKADLYYV--GKVTLpsgETVTVKTAFMIVRDEAfsKSFEDWLAIaspyER 518
Cdd:cd02765 256 LRQADVTATPAEDGyVVWDTNS-DSPEPVAATNINPAleGEYTI---NGVKVHTVLTALREQA--ASYPPKAAA----EI 325
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18159972 519 NTPEFADyvkkIEQMAKDFADAAPKAATTLHrGVGMHPNGEYIVWAYRTIDTLVGNFHRMGG 580
Cdd:cd02765 326 CGLEEAI----IETLAEWYATGKPSGIWGFG-GVDRYYHSHVFGRTAAILAALTGNIGRVGG 382
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
971-1046 |
2.61e-15 |
|
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: 73.08 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 971 LILYTGPLYTKHRSQFYY----WIKQVVPEnFVLINPEDAAKLGVETGDVIKVETPVGAFEAPAVVEPAVAPGVIMVPYG 1046
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTrrvlRLAKPEPE-VVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFG 79
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
54-797 |
9.12e-15 |
|
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239164 [Multi-domain] Cd Length: 679 Bit Score: 79.11 E-value: 9.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 54 SSCLGCNVRCGIvaRV-VKYGDVEVIErieGNPYHVYNRavsfdkqikryaplpyntpvkealekwsGTLCPRGADGIHY 132
Cdd:cd02763 2 TTCYMCACRCGI--RVhLRDGKVRYIK---GNPDHPLNK----------------------------GVICAKGSSGIMK 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 133 VYDPYRVLKPLKRAGPRGSGKWKAITWEQlinevvnggVIEETGERLPGLKeffaygklkeagfedpnailsemkidvdn 212
Cdd:cd02763 49 QYSPARLTKPLLRKGPRGSGQFEEIEWEE---------AFSIATKRLKAAR----------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 213 imkvARDPNKtyddlikaieefkakwsqrlgekglkledllidpdrpdlgtkanmVMYLRGRGQGHTdyFSQRWIYAFGS 292
Cdd:cd02763 91 ----ATDPKK---------------------------------------------FAFFTGRDQMQA--LTGWFAGQFGT 119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 293 VNWTRHTSACQLGYYAGnsiwagyhdiqadpiGAKVIIGAGWSMGRVHPGATGQGLMIERACE----------GELK--- 359
Cdd:cd02763 120 PNYAAHGGFCSVNMAAG---------------GLYSIGGSFWEFGGPDLEHTKYFMMIGVAEDhhsnpfkigiQKLKrrg 184
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 360 --LYYVNPVapRTTCNGnII--WIPVKPGEDAALAFAVIRWLIENKRYNEEFLsipnrdsakkLGYpvnTNATWLVITEG 435
Cdd:cd02763 185 gkFVAVNPV--RTGYAA-IAdeWVPIKPGTDGAFILALAHELLKAGLIDWEFL----------KRY---TNAAELVDYTP 248
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 436 ErfgeflkardvgiedsdkpvvwtgerfatydsvdkadlyYVGKVTLPSGETVTVKTAFMIVrdEAFSKSFEdwLAIASp 515
Cdd:cd02763 249 E---------------------------------------WVEKITGIPADTIRRIAKELGV--TARDQPIE--LPIAW- 284
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 516 yernTPEFADYVKKIEqmakdfadAAPKAATTLhRGVGMHPNGEYIVWAYRTIDTLVGNFHRMGGLLARA---------A 586
Cdd:cd02763 285 ----TDVWGRKHEKIT--------GRPVSFHAM-RGIAAHSNGFQTIRALFVLMMLLGTIDRPGGFRHKPpyprhipplP 351
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 587 HTAYENYVYNVGRSGFGEPVRW-GPPIDRHRYAYENTleywLRVKKALkegkSWDeavkaafptkrpwYPHTPEESYTEI 665
Cdd:cd02763 352 KPPKIPSADKPFTPLYGPPLGWpASPDDLLVDEDGNP----LRIDKAY----SWE-------------YPLAAHGCMQNV 410
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 666 FAGIAEGYPYRIGALILFYANpvLATNYGVKFIEVL-----KDPA---KLPLFIVITTTINETALYADYIVPDTTYLETG 737
Cdd:cd02763 411 ITNAWRGDPYPIDTLMIYMAN--MAWNSSMNTPEVRemltdKDASgnyKIPFIIVCDAFYSEMVAFADLVLPDTTYLERH 488
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18159972 738 ---TMGIQYLYATSGSVtlaESWRSPVIMPLtqriSDCpnghpryASFWEFFIDTAKALGMPG 797
Cdd:cd02763 489 damSLLDRPISEADGPV---DAIRVPIVEPK----GDV-------KPFQEVLIELGTRLGLPG 537
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
54-166 |
2.00e-13 |
|
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: 74.74 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 54 SSCLGCNVRCGIVArvvkYGDVEVIERIEGNPYHVYNRavsfdkqikryaplpyntpvkealekwsGTLCPRGADGIHYV 133
Cdd:cd02752 2 TICPYCSVGCGLIA----YVQNGVWVHQEGDPDHPVNR----------------------------GSLCPKGAALRDFV 49
|
90 100 110
....*....|....*....|....*....|...
gi 18159972 134 YDPYRVLKPLKRAGprGSGKWKAITWEQLINEV 166
Cdd:cd02752 50 HSPKRLKYPMYRAP--GSGKWEEISWDEALDEI 80
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
965-1045 |
3.13e-13 |
|
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and other related proteins. Formate dehydrogenase H is a component of the anaerobic formate hydrogen lyase complex and catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. Formate dehydrogenase N (alpha subunit) is the major electron donor to the bacterial nitrate respiratory chain and nitrate reductases, Nap and Nas, catalyze the reduction of nitrate to nitrite. This CD (MopB_CT_Fdh-Nap-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 238282 [Multi-domain] Cd Length: 120 Bit Score: 67.53 E-value: 3.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 965 KEWPFILIlyTGplytkhRSQFYY----------WIKQVVPENFVLINPEDAAKLGVETGDVIKVETPVGAFEAPAVVEP 1034
Cdd:cd00508 1 EEYPLVLT--TG------RLLEHWhtgtmtrrspRLAALAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTD 72
|
90
....*....|.
gi 18159972 1035 AVAPGVIMVPY 1045
Cdd:cd00508 73 RVRPGTVFMPF 83
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
965-1045 |
1.17e-12 |
|
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: 65.72 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 965 KEWPFILIlyTGplytkhrSQFYYW-----------IKQVVPENFVLINPEDAAKLGVETGDVIKVETPVGAFEAPAVVE 1033
Cdd:cd02790 1 EEYPLVLT--TG-------RVLYHYhtgtmtrraegLDAIAPEEYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVT 71
|
90
....*....|..
gi 18159972 1034 PAVAPGVIMVPY 1045
Cdd:cd02790 72 DRVPEGVVFMPF 83
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
968-1051 |
1.93e-12 |
|
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: 65.37 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 968 PFILILYTGPLYTKHRSQFYYWIKQVVPENFVLINPEDAAKLGVETGDVIKVETPVGAFEAPAVVEPAVAPGVIMVPYGM 1047
Cdd:cd02778 1 EFRLIYGKSPVHTHGHTANNPLLHELTPENTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMPHGF 80
|
....
gi 18159972 1048 GRWA 1051
Cdd:cd02778 81 GHWA 84
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
989-1045 |
3.41e-12 |
|
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: 64.55 E-value: 3.41e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 18159972 989 WIKQVVPENFVLINPEDAAKLGVETGDVIKVETPVGAFEAPAVVEPAVAPGVIMVPY 1045
Cdd:cd02792 27 YLAELQPEMFVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHEVGIPY 83
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
967-1046 |
8.32e-12 |
|
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: 63.37 E-value: 8.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 967 WPFILIlytGPLYtKHR--SQFYY--WIKQVVPENF---VLINPEDAAKLGVETGDVIKVETPVGAFEAPAVVEPAVAPG 1039
Cdd:cd02777 1 YPLQLI---SPHP-KRRlhSQLDNvpWLREAYKVKGrepVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPG 76
|
....*..
gi 18159972 1040 VIMVPYG 1046
Cdd:cd02777 77 VVALPEG 83
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
88-408 |
1.59e-10 |
|
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: 65.03 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 88 VYNRAVSFDKQIKRYAPLPYNTPVKEALEkwsgtlCPRGADGIHYVYDPYRVLKPLKRAGPRGSGKWKAITWEQLINEVV 167
Cdd:cd02750 22 VKNGIVTREEQATDYPETPPDLPDYNPRG------CQRGASFSWYLYSPDRVKYPLKRVGARGEGKWKRISWDEALELIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 168 NGGV--IEETG-ERLPGLKEFFAYGKL-KEAGFEdpnaiLSEMkidvdnIMKVARDPNKTYDDLIKAieefkakWSQRLG 243
Cdd:cd02750 96 DAIIdtIKKYGpDRVIGFSPIPAMSMVsYAAGSR-----FASL------IGGVSLSFYDWYGDLPPG-------SPQTWG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 244 EKGLKLEDLlidpdrpdlgtkanmvmylrgrgqghtDYFSQRWIYAFGS-VNWTRHTSACQLgyyagnsIWAGYHdiqad 322
Cdd:cd02750 158 EQTDVPESA---------------------------DWYNADYIIMWGSnVPVTRTPDAHFL-------TEARYN----- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 323 piGAKVIIgagwsmgrVHPGatgqglmieracegelklyyVNPVAPRTTcngniIWIPVKPGEDAALAFAVIRWLIENKR 402
Cdd:cd02750 199 --GAKVVV--------VSPD--------------------YSPSAKHAD-----LWVPIKPGTDAALALAMAHVIIKEKL 243
|
....*.
gi 18159972 403 YNEEFL 408
Cdd:cd02750 244 YDEDYL 249
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
994-1050 |
1.71e-10 |
|
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: 59.51 E-value: 1.71e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 18159972 994 VPENFVLINPEDAAKLGVETGDVIKVETPVGAFEAPAVVEPAVAPGVIMVPYGMGRW 1050
Cdd:cd02791 32 VPEPYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPGEVFVPMHWGDQ 88
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
968-1046 |
2.19e-10 |
|
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239182 [Multi-domain] Cd Length: 130 Bit Score: 59.63 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 968 PFILILYTGplytkHRSQFYY--------WIKQVVPENFVLINPEDAAKLGVETGDVIKVETPVGAFEAPAVVEPAVAPG 1039
Cdd:cd02781 1 EYPLILTTG-----ARSYYYFhsehrqlpSLRELHPDPVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPG 75
|
....*..
gi 18159972 1040 VIMVPYG 1046
Cdd:cd02781 76 VVRAEHG 82
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
967-1046 |
8.30e-10 |
|
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: 57.69 E-value: 8.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 967 WPFILILYtgplYTKHR--SQFYY--WIKQVVPeNFVLINPEDAAKLGVETGDVIKVETPVGAFEAPAVVEPAVAPGVIM 1042
Cdd:cd02794 1 YPLQLIGW----HYKRRthSTFDNvpWLREAFP-QEVWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVVA 75
|
....
gi 18159972 1043 VPYG 1046
Cdd:cd02794 76 LPQG 79
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
966-1052 |
1.20e-09 |
|
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: 57.38 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 966 EWPFILILYTGpLYTKHrSQF--YYWIKQVVPENFVLINPEDAAKLGVETGDVIKVETPVGAFEAPAVVEPAVAPGVIMV 1043
Cdd:cd02785 1 KYPLACIQRHS-RFRVH-SQFsnVPWLLELQPEPRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGVVTA 78
|
....*....
gi 18159972 1044 PygMGRWAD 1052
Cdd:cd02785 79 E--QGWWSR 85
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
529-735 |
1.23e-09 |
|
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: 62.41 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 529 KIEQMAKDFAdAAPKAATTLHRGVGMHPNGEYIVWAYRTIDTLVGNFHRMGGLLAraaHTAYENYVYNVGRSGFGepvrw 608
Cdd:cd02762 273 TIRRLAREFA-AAPSAAVYGRLGVQTQLFGTLCSWLVKLLNLLTGNLDRPGGAMF---TTPALDLVGQTSGRTIG----- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 609 gppidrhryayentleywlrvkkalkeGKSWDEAVkAAFPTKRPWYPHT--PEESYTEifagiaegYPYRIGALILFYAN 686
Cdd:cd02762 344 ---------------------------RGEWRSRV-SGLPEIAGELPVNvlAEEILTD--------GPGRIRAMIVVAGN 387
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 18159972 687 PVLATNYGVKFIEVLkdpAKLPLFIVITTTINETALYADYIVPDTTYLE 735
Cdd:cd02762 388 PVLSAPDGARLEAAL---GGLEFMVSVDVYMTETTRHADYILPPASQLE 433
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
49-135 |
1.33e-09 |
|
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is found in a number of reductase/dehydrogenase families, which include the periplasmic nitrate reductase precursor and the formate dehydrogenase alpha chain.
Pssm-ID: 197994 [Multi-domain] Cd Length: 55 Bit Score: 54.95 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 49 VRYVFSSCLGCNVRCGIVARVVKygdvEVIERIEGNPYHVYNRavsfdkqikryaplpyntpvkealekwsGTLCPRGAD 128
Cdd:smart00926 1 EKWVPTVCPLCGVGCGLLVEVKD----GRVVRVRGDPDHPVNR----------------------------GRLCPKGRA 48
|
....*..
gi 18159972 129 GIHYVYD 135
Cdd:smart00926 49 GLEQVYS 55
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
999-1048 |
2.29e-08 |
|
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: 53.94 E-value: 2.29e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 18159972 999 VLINPEDAAKLGVETGDVIKVETPVGAFEAPAVVEPAVAPGVIMVPYGMG 1048
Cdd:cd02782 35 LRIHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMPGVVSLPHGWG 84
|
|
| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
999-1046 |
1.32e-07 |
|
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: 51.48 E-value: 1.32e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 18159972 999 VLINPEDAAKLGVETGDVIKVETPVGAFEAPAVVEPAVAPGVIMVPYG 1046
Cdd:cd02793 35 IRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPGVVQLPTG 82
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
63-167 |
1.79e-07 |
|
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: 55.33 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 63 CGIVARVvkygDVEVIERIEGNPYHVYNRavsfdkqikryaplpyntpvkealekwsGTLCPRGADGIHYVYDPYRVLKP 142
Cdd:cd02766 12 CSLLVTV----EDGRIVRVEGDPAHPYTR----------------------------GFICAKGARYVERVYSPDRLLTP 59
|
90 100
....*....|....*....|....*
gi 18159972 143 LKRAGPRGsGKWKAITWEQLINEVV 167
Cdd:cd02766 60 LKRVGRKG-GQWERISWDEALDTIA 83
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
995-1044 |
2.17e-07 |
|
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: 50.74 E-value: 2.17e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 18159972 995 PENFVLINPEDAAKLGVETGDVIKVETPVGAFEAPAVVEPAVAPGVIMVP 1044
Cdd:cd02786 29 GEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVVVAE 78
|
|
| 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 ... |
990-1048 |
4.71e-07 |
|
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: 48.85 E-value: 4.71e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 18159972 990 IKQVVPENFVLINPEDAAKLGVETGDVIKVETPVGAFEAPAVVEPAVAPGVIMVPYGMG 1048
Cdd:cd02788 22 IAERAPAPYARLSPADAARLGLADGDLVEFSLGDGTLTLPVQISKYLPAGVVGLPLGAG 80
|
|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
994-1054 |
5.05e-07 |
|
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: 49.38 E-value: 5.05e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18159972 994 VPENFVLINPEDAAKLGVETGDVIKVETPVGAFEAPAVVEPAVAPGVIMVPygMGRWADTV 1054
Cdd:cd02779 30 VPLPYIEVNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKPGQTFML--MAHPRPGA 88
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
123-166 |
1.11e-06 |
|
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: 52.71 E-value: 1.11e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 18159972 123 CPRGADGIHYVYDPYRVLKPLKRAGPRGSGKWKAITWEQLINEV 166
Cdd:cd02770 44 CLRGRSQRKRVYNPDRLKYPMKRVGKRGEGKFVRISWDEALDTI 87
|
|
| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
999-1043 |
5.00e-06 |
|
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. This CD (MopB_CT_Nitrate-R-NarG-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239177 [Multi-domain] Cd Length: 141 Bit Score: 47.37 E-value: 5.00e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 18159972 999 VLINPEDAAKLGVETGDVIKVETPVGAFEAPAVVEPAVAPGVIMV 1043
Cdd:cd02776 33 VWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTVFM 77
|
|
| MopB_CT_PHLH |
cd02784 |
The MopB_CT_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
996-1058 |
6.74e-06 |
|
The MopB_CT_PHLH CD includes a group of related uncharacterized putative hydrogenase-like homologs (PHLH) of molybdopterin binding proteins. This CD is of the PHLH region homologous to the conserved molybdopterin-binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239185 [Multi-domain] Cd Length: 137 Bit Score: 47.06 E-value: 6.74e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18159972 996 ENFVLINPEDAAKLGVETGDVIKVETPVGAFEAPAVVEPAVAPGVIMVPYGMGRWADTVVVKP 1058
Cdd:cd02784 37 DNAALVSPRTAEALGLLQGDVVRIRRGGRTIELPVWIQPGHAEGVVLLALGYGRTHAGKVGNG 99
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
123-1052 |
8.72e-06 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 50.03 E-value: 8.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 123 CPRGADGIHYVYDPYRVLKPLKRAGPRGSGKWKAITWEQLINevvnggVIEETGERLpglkeffaygkLKEAGFEdpNAI 202
Cdd:PRK14990 104 CLRGRSMRRRVYNPDRLKYPMKRVGARGEGKFERISWEEAYD------IIATNMQRL-----------IKEYGNE--SIY 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 203 LSEMKIDVDNIMKVARDPNKTyddLIkaieefkakwsqrlgekglkledllidpdrpdlgtkANMVMYLRGRGQGHTDYF 282
Cdd:PRK14990 165 LNYGTGTLGGTMTRSWPPGNT---LV------------------------------------ARLMNCCGGYLNHYGDYS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 283 SQRwiYAFGsVNWTRHtsacqlGYYAGNSiwagyhdiQADPIGAKVIIGAGWSMGRVHPGATGQGLMIERA-CEGELKLY 361
Cdd:PRK14990 206 SAQ--IAEG-LNYTYG------GWADGNS--------PSDIENSKLVVLFGNNPGETRMSGGGVTYYLEQArQKSNARMI 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 362 YVNPVAPRTTCNGNIIWIPVKPGEDAALAFAVirwlienkryneeflsipnrdsakklgypvntnaTWLVITEgerfgef 441
Cdd:PRK14990 269 IIDPRYTDTGAGREDEWIPIRPGTDAALVNGL----------------------------------AYVMITE------- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 442 lkardvgiedsdkpvvwtgerfatyDSVDKA--DLYYVG--KVTLPSGETVTVKTAFMIVRDEAfsksfeDWLAiaspye 517
Cdd:PRK14990 308 -------------------------NLVDQPflDKYCVGydEKTLPASAPKNGHYKAYILGEGP------DGVA------ 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 518 rNTPEFADYV-----KKIEQMAKDFADAAPkAATTLHRGVGMHPNGEYIVWAYRTIDTLVGNFHRMGGllaraahtayen 592
Cdd:PRK14990 351 -KTPEWASQItgvpaDKIIKLAREIGSTKP-AFISQGWGPQRHANGEIATRAISMLAILTGNVGINGG------------ 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 593 yvyNVG-RSGfgepvRWGPPIDRHRyAYENTLEYWLRVKKalkegksWDEAVKAAfptkrpwyphtPEesYTEIFAGIAE 671
Cdd:PRK14990 417 ---NSGaREG-----SYSLPFVRMP-TLENPIQTSISMFM-------WTDAIERG-----------PE--MTALRDGVRG 467
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 672 GYPYRIG-ALILFYANPVLATNYGV--KFIEVLKDPAKLPLFIVITTTINETALYADYIVPDTTYLETGTMGIQylyATS 748
Cdd:PRK14990 468 KDKLDVPiKMIWNYAGNCLINQHSEinRTHEILQDDKKCELIVVIDCHMTSSAKYADILLPDCTASEQMDFALD---ASC 544
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 749 GSVtlaeswrSPVIMPlTQRISdcpnghPRY--ASFWEFFIDTAKALgmpghgdkaipGVKGKKYEGKwfsMHCEWeyiL 826
Cdd:PRK14990 545 GNM-------SYVIFN-DQVIK------PRFecKTIYEMTSELAKRL-----------GVEQQFTEGR---TQEEW---M 593
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 827 RvfanaALDAKDKGLIPeDVPEEEvKFVEENypIAQFRDilppDEWKYVAYglarggvftkyeESFDERGISKRRVPGRG 906
Cdd:PRK14990 594 R-----HLYAQSREAIP-ELPTFE-EFRKQG--IFKKRD----PQGHHVAY------------KAFREDPQANPLTTPSG 648
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 907 TLYLWSEEVAKTRNNvtgekfWGGPK---YFPIATYAPAVPAFQKadewlhgtPLRQLYPekewpfilILYTGPLYtKHR 983
Cdd:PRK14990 649 KIEIYSQALADIAAT------WELPEgdvIDPLPIYTPGFESYQD--------PLNKQYP--------LQLTGFHY-KSR 705
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18159972 984 SQFYYWIKQVVP---ENFVLINPEDAAKLGVETGDVIKVETPVGAFEAPAVVEPAVAPGVIMVpyGMGRWAD 1052
Cdd:PRK14990 706 VHSTYGNVDVLKaacRQEMWINPLDAQKRGINNGDKVRIFNDRGEVHIEAKVTPRMMPGVVAL--GEGAWYD 775
|
|
| FwdD |
COG1153 |
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion]; |
1001-1055 |
1.20e-05 |
|
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion];
Pssm-ID: 440767 [Multi-domain] Cd Length: 127 Bit Score: 46.00 E-value: 1.20e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 18159972 1001 INPEDAAKLGVETGDVIKVETPVGAFEAPAVVEPAVAPGVIMVPygMGRWADTVV 1055
Cdd:COG1153 35 LNPEDMKKLGIKEGDKVKVTSEYGEVVVKAKESEDLHPGLVFIP--MGPWANAVV 87
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
660-765 |
4.13e-05 |
|
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like homologs (PHLH) of molybdopterin binding (MopB) proteins. This CD is of the PHLH region homologous to the catalytic molybdopterin-binding subunit of MopB homologs.
Pssm-ID: 239165 [Multi-domain] Cd Length: 524 Bit Score: 47.48 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 660 ESYTEIFAGIAEGypyRIGALILFYANPVLATNYGVKFIEVLKdpaKLPLFIVITTTINETALYADYIVPDTTYLET-GT 738
Cdd:cd02764 370 QDLKALASRINAG---KVSALLVYDVNPVYDLPQGLGFAKALE---KVPLSVSFGDRLDETAMLCDWVAPMSHGLESwGD 443
|
90 100
....*....|....*....|....*..
gi 18159972 739 MgiqylYATSGSVTLAEswrsPVIMPL 765
Cdd:cd02764 444 A-----ETPDGTYSICQ----PVIAPL 461
|
|
| MopB_CT_FmdC-FwdD |
cd02789 |
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran ... |
997-1058 |
4.74e-05 |
|
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: 43.57 E-value: 4.74e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18159972 997 NFVLINPEDAAKLGVETGDVIKVETPVGAFEAPAVVEPAVAPGVIMVPygMGRWADtVVVKP 1058
Cdd:cd02789 31 AYCEINPEDYKLLGKPEGDKVKVTSEFGEVVVFAKENEGVPEGMVFIP--MGPWAN-VVVDP 89
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
499-802 |
7.61e-04 |
|
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: 43.36 E-value: 7.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 499 DEAFSKS----FEDWLAIASPYernTPEFADYV-----KKIEQMAKDFADAAPkAATTLHRGVGMHPNGEYIVWAYRTID 569
Cdd:cd02753 231 DEEFIEErtegFEELKEIVEKY---TPEYAERItgvpaEDIREAARMYATAKS-AAILWGMGVTQHSHGTDNVMALSNLA 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 570 TLVGNfhrmggllaraahtayenyvynVGRSGFG-EPVRwGppidrhryayENTleywlrVKKALKEGkswdeavkaAFP 648
Cdd:cd02753 307 LLTGN----------------------IGRPGTGvNPLR-G----------QNN------VQGACDMG---------ALP 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 649 TkrpWYPhtpeesyteifagiaeGYpyrIGALILFYANPVLA---TNYGVKFIEvlkdpaKLPLFIVITTTINETALYAD 725
Cdd:cd02753 339 N---VLP----------------GY---VKALYIMGENPALSdpnTNHVRKALE------SLEFLVVQDIFLTETAELAD 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 726 YIVPDTTYLEtgtmgiqylyaTSGSVTLAE---SWRSPVIMPLTQRISDcpnghpryasfWEFFIDTAKALGMPGHGDKA 802
Cdd:cd02753 391 VVLPAASFAE-----------KDGTFTNTErrvQRVRKAVEPPGEARPD-----------WEIIQELANRLGYPGFYSHP 448
|
|
| CDC48_N |
smart01073 |
Cell division protein 48 (CDC48) N-terminal domain; This domain has a double psi-beta barrel ... |
997-1058 |
1.03e-03 |
|
Cell division protein 48 (CDC48) N-terminal domain; This domain has a double psi-beta barrel fold and includes VCP-like ATPase and N-ethylmaleimide sensitive fusion protein N-terminal domains. Both the VAT and NSF N-terminal functional domains consist of two structural domains of which this is at the N-terminus. The VAT-N domain found in AAA ATPases is a substrate 185-residue recognition domain.
Pssm-ID: 215012 [Multi-domain] Cd Length: 82 Bit Score: 39.13 E-value: 1.03e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 997 NFVLINPEDAAKLGVETGDVIKVETPVGAFeapAVVEPA---VAPGVIMVPYGMGRWA-----DTVVVKP 1058
Cdd:smart01073 15 GIARLSPEDMDELGLFPGDYVLITGKRRTV---AIVWPAypeDPGGIIRIDGVQRKNAgvsigDTVTVRK 81
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
120-166 |
1.13e-03 |
|
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: 42.97 E-value: 1.13e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 18159972 120 GTLCPRGADGIHYVYDPYRVLKPLKRAGprgsGKWKAITWEQLINEV 166
Cdd:cd02753 36 GKLCVKGRFGFDFVNSKDRLTKPLIRKN----GKFVEASWDEALSLV 78
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
999-1041 |
1.17e-03 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 43.12 E-value: 1.17e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 18159972 999 VLINPEDAAKLGVETGDVIKVETPVGAFEAPAVVEPAVAPGVI 1041
Cdd:PRK15102 712 VYINPQDAKARGIKDGDVVRVFNDRGQVLAGAVVSDRYPPGVI 754
|
|
| MopB_CT_ydeP |
cd02787 |
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial ... |
999-1045 |
1.30e-03 |
|
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239188 [Multi-domain] Cd Length: 112 Bit Score: 39.57 E-value: 1.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 18159972 999 VLINPEDAAKLGVETGDVIKVETPVGAFE-----APAVVEPAVAPGVIMVPY 1045
Cdd:cd02787 33 VFMNPDDIARLGLKAGDRVDLESAFGDGQgrivrGFRVVEYDIPRGCLAAYY 84
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
378-408 |
2.36e-03 |
|
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: 42.22 E-value: 2.36e-03
10 20 30
....*....|....*....|....*....|.
gi 18159972 378 WIPVKPGEDAALAFAVIRWLIENKRYNEEFL 408
Cdd:cd02751 227 WIPIRPGTDVALMLAMAHTLITEDLHDQAFL 257
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
123-166 |
3.61e-03 |
|
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: 41.45 E-value: 3.61e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 18159972 123 CPRGADGIHYVYDPYRVLKPLKRAGP----------RGSGKWKAITWEQLINEV 166
Cdd:cd02751 32 CPRGRSVRDRVYSPDRIKYPMKRVGWlgngpgsrelRGEGEFVRISWDEALDLV 85
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
351-408 |
5.68e-03 |
|
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: 40.71 E-value: 5.68e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 18159972 351 ERACEGELKLYYVNPVAPRTTCNGNIIWIPVKPGEDAALAFAVIRWLIENKRYNEEFL 408
Cdd:cd02769 202 KALKDRGIRFISISPLRDDTAAELGAEWIAIRPGTDVALMLALAHTLVTEGLHDKAFL 259
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
655-740 |
9.00e-03 |
|
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: 40.29 E-value: 9.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18159972 655 PHTPEESYTEIFAGIAEGypyRIGALILFYANPVLATNYGVKFIEVLKdpaKLPLFIVITTTI-NETALYADYIVPDTTY 733
Cdd:cd02754 371 PPKPGLHAVEMFEAIEDG---EIKALWVMCTNPAVSLPNANRVREALE---RLEFVVVQDAFAdTETAEYADLVLPAASW 444
|
....*...
gi 18159972 734 LE-TGTMG 740
Cdd:cd02754 445 GEkEGTMT 452
|
|
| |
