|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
1-924 |
0e+00 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 1656.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 1 MNRRDFIKNTAIASAASVAGLSVPSS---MLGAQEEDWKWDKAVCRFCGTGCGIMIARKDGKIVATKGDPAAPVNRGLNC 77
Cdd:PRK13532 3 LSRRDFMKANAAAAAAAAAGLSLPAVanaVVGSAQTAIKWDKAPCRFCGTGCGVLVGTKDGRVVATQGDPDAPVNRGLNC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 78 IKGYFNAKIMYGEDRLVMPLLRMNeKGEFDKKGKFQQVSWQRAFDEMEKQFKKAYNELGVTGIGIFGSGQYTIQEGYAAL 157
Cdd:PRK13532 83 IKGYFLSKIMYGKDRLTQPLLRMK-DGKYDKEGEFTPVSWDQAFDVMAEKFKKALKEKGPTAVGMFGSGQWTIWEGYAAS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 158 KLAKAGFRTNNIDPNARHCMASAVVGFMQTFGVDEPSGCYDDIELTDTIITWGANMAEMHPILWSRVSDRKLSNLDkVKV 237
Cdd:PRK13532 162 KLMKAGFRSNNIDPNARHCMASAVVGFMRTFGIDEPMGCYDDIEAADAFVLWGSNMAEMHPILWSRVTDRRLSNPD-VKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 238 VNLSTFSNRTSNIADIEIIFKPNTDLAIWNYIAREIVYNHPeaMDMKFIKDHCVFATGYADIGYGMRnnPNHPKFKESek 317
Cdd:PRK13532 241 AVLSTFEHRSFELADNGIIFTPQTDLAILNYIANYIIQNNA--VNWDFVNKHTNFRKGATDIGYGLR--PTHPLEKAA-- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 318 dtvekenvitlddeeatslsylgvkagdkfemKHQGVADKNWEISFDEFKKGLAPYTLEYTARVAkGDDNEsledfkkKL 397
Cdd:PRK13532 315 --------------------------------KNPGTAGKSEPISFEEFKKFVAPYTLEKTAKMS-GVPKE-------QL 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 398 QELANLYIEKNRKVVSFWTMGFNQHTRGSWVNEQAYMVHFLLGKQAKPGSGAFSLTGQPSACGTAREVGTFSHRLPADMV 477
Cdd:PRK13532 355 EQLAKLYADPNRKVVSFWTMGFNQHTRGVWANNLVYNIHLLTGKISTPGNGPFSLTGQPSACGTAREVGTFSHRLPADMV 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 478 VANPKHREISEKIWKVPAKTINPKPGSPYLNIMRDLEDGKIKFAWVQVNNPWQNTANANH-WIAAAREMDNFIVVSDCYP 556
Cdd:PRK13532 435 VTNPKHREIAEKIWKLPEGTIPPKPGYHAVAQDRMLKDGKLNAYWVMCNNNMQAGPNINEeRLPGWRNPDNFIVVSDPYP 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 557 GISAKVADLILPSAMIYEKWGAYGNAERRTQHWKQQVLPVGAAMSDTWQILEFAKRFKLKEVWKEQKVdnkltlpsvlee 636
Cdd:PRK13532 515 TVSALAADLILPTAMWVEKEGAYGNAERRTQFWRQQVKAPGEAKSDLWQLVEFSKRFKTEEVWPEELL------------ 582
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 637 aKAMGYSEDDTLFDVLFANKEAKSFnPNDAIAKGFDNTDVKgderkiqgsdgkeftGYGFFVQKYLWEEYRKFGLGHGHD 716
Cdd:PRK13532 583 -AKKPEYRGKTLYDVLFANGQVDKF-PLSELAEGYLNDEAK---------------HFGFYVQKGLFEEYASFGRGHGHD 645
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 717 LADFDTYHKVRGLRWPVVNGKETQWRFNTKFDYYAKKaapNSDFAFYGDFnkmltngdliapkdekehsiKNKAKIFFRP 796
Cdd:PRK13532 646 LAPFDTYHKVRGLRWPVVDGKETLWRYREGYDPYVKA---GEGFKFYGKP--------------------DGKAVIFALP 702
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 797 FMKAPERPSKEYPFWLATGRVLEHWHSGTMTMRVPELYRAVPEALCYMSEKDGEKLGLNQGDLVWVESRRGKVKARVDMR 876
Cdd:PRK13532 703 YEPPAESPDEEYDLWLSTGRVLEHWHTGSMTRRVPELYRAFPEAVCFMHPEDAKARGLRRGDEVKVVSRRGEVKSRVETR 782
|
890 900 910 920
....*....|....*....|....*....|....*....|....*...
gi 218562408 877 GRNKPPVGLVYVPWFDENVYINKVTLDATCPLSKQTDFKKCAVKIYKA 924
Cdd:PRK13532 783 GRNKPPRGLVFVPFFDAAQLINKLTLDATDPLSKQTDFKKCAVKIEKV 830
|
|
| NAPA |
TIGR01706 |
periplasmic nitrate reductase, large subunit; This model represents the large subunit of a ... |
1-924 |
0e+00 |
|
periplasmic nitrate reductase, large subunit; This model represents the large subunit of a family of nitrate reductases found in proteobacteria which are localized to the periplasm. This subunit binds molybdopterin and contains a twin-arginine motif at the N-terminus. The protein associates with NapB, a soluble heme-containing protein and NapC, a membrane-bound cytochrome c. The periplasmic nitrate reductases are not involved in the assimilation of nitrogen, and are not directly involved in the formation of electrochemical gradients (i.e. respiration) either. Rather, the purpose of this enzyme is either dissimilatory (i.e. to dispose of excess reductive equivalents) or indirectly respiratory by virtue of the consumption of electrons derived from NADH via the proton translocating NADH dehydrogenase. The enzymes from Alicagenes eutrophus and Paracoccus pantotrophus have been characterized. In E. coli (as well as other organisms) this gene is part of a large nitrate reduction operon (napFDAGHBC). [Energy metabolism, Aerobic, Energy metabolism, Electron transport, Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 273766 [Multi-domain] Cd Length: 830 Bit Score: 1567.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 1 MNRRDFIKNTAIASAASVAGLSVP---SSMLGAQEE-DWKWDKAVCRFCGTGCGIMIARKDGKIVATKGDPAAPVNRGLN 76
Cdd:TIGR01706 2 ISRRDFIKATAIASAASVAGLSLPaqaANMVGGQEEtAIKWDKAPCRFCGTGCGVMVGVKDGRVVATQGDPAAPVNRGLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 77 CIKGYFNAKIMYGEDRLVMPLLRMNEkGEFDKKGKFQQVSWQRAFDEMEKQFKKAYNELGVTGIGIFGSGQYTIQEGYAA 156
Cdd:TIGR01706 82 CIKGYFLSKIMYGQDRLTQPLLRMKD-GKYDKDGEFTPVSWDQAFDEMEEQFKRALKEKGPTAIGMFGSGQWTIWEGYAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 157 LKLAKAGFRTNNIDPNARHCMASAVVGFMQTFGVDEPSGCYDDIELTDTIITWGANMAEMHPILWSRVSDRKLSNlDKVK 236
Cdd:TIGR01706 161 LKLMKAGFRSNNIDPNARHCMASAVVGFMRTFGMDEPMGCYDDFEAADAFVLWGSNMAEMHPILWTRVTDRRLSH-PKVK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 237 VVNLSTFSNRTSNIADIEIIFKPNTDLAIWNYIAREIVYNHpeAMDMKFIKDHCVFATGYADIGYGMRnnPNHPKFKESE 316
Cdd:TIGR01706 240 VVVLSTFTHRSFDLADIGIIFKPQTDLAILNYIANYIIQNN--AVNMDFVNKHTVFKTGATDIGYGLR--PDHPLEKAAK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 317 kdtvekenviTLDDEEATSLSYlgvkagdkfemkhqgvadknweisFDEFKKGLAPYTLEYTARVAKGDdnesledfKKK 396
Cdd:TIGR01706 316 ----------NADDPAATSLST------------------------FEEFKKFVAPYTLEKTSELSGVP--------KAK 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 397 LQELANLYIEKNRKVVSFWTMGFNQHTRGSWVNEQAYMVHFLLGKQAKPGSGAFSLTGQPSACGTAREVGTFSHRLPADM 476
Cdd:TIGR01706 354 LEQLAELYADPNRKVMSLWTMGFNQHTRGVWANNMVYNLHLLTGKIATPGNSPFSLTGQPSACGTAREVGTFSHRLPADM 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 477 VVANPKHREISEKIWKVPAKTINPKPGSPYLNIMRDLEDGKIKFAWVQVNNPWQNTANAN-HWIAAAREMDNFIVVSDCY 555
Cdd:TIGR01706 434 VVTNPKHREIAEKIWKIPAGTIPEKPGLHAVAQDRALKDGKLNFYWVQVNNNMQAGPNINeERLPGYRNPDNFIVVSDAY 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 556 PGISAKVADLILPSAMIYEKWGAYGNAERRTQHWKQQVLPVGAAMSDTWQILEFAKRFKLKEVWKEQKVDNKLTLPsvle 635
Cdd:TIGR01706 514 PTVTALAADLILPSAMWVEKEGAYGNAERRTQVWHQQVLAPGEARSDLWQLVEFSKRFKTEEVWPEELLAKKPEYR---- 589
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 636 eakamgyseDDTLFDVLFANKEAKSFNPNDAIAKgfdntdvkgderkiqgSDGKEFTGYGFFVQKYLWEEYRKFGLGHGH 715
Cdd:TIGR01706 590 ---------GKTLYDVLFANGEVDKFPLSEANAK----------------SLNAESTAFGFYVQKGLFEEYAKFGRGHGH 644
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 716 DLADFDTYHKVRGLRWPVVNGKETQWRFNTKFDYYAKKAApnsDFAFYGDFnkmltngdliapkdekehsiKNKAKIFFR 795
Cdd:TIGR01706 645 DLAPFDTYHKVRGLRWPVVNGKETQWRYREGSDPYVKAGA---GFQFYGNP--------------------DGKAVIFAL 701
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 796 PFMKAPERPSKEYPFWLATGRVLEHWHSGTMTMRVPELYRAVPEALCYMSEKDGEKLGLNQGDLVWVESRRGKVKARVDM 875
Cdd:TIGR01706 702 PYEPPAERPDEEYPLWLVTGRVLEHWHSGSMTRRVPELYRAFPEALCFMHPEDAKALGLRRGDEVWVVSRRGEVRSRVET 781
|
890 900 910 920
....*....|....*....|....*....|....*....|....*....
gi 218562408 876 RGRNKPPVGLVYVPWFDENVYINKVTLDATCPLSKQTDFKKCAVKIYKA 924
Cdd:TIGR01706 782 RGRNKPPRGLVFVPWFDASQLINKVTLDATDPLSKQTDFKKCAVKIYKV 830
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
39-750 |
0e+00 |
|
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: 670.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 39 KAVCRFCGTGCGIMIARKDGKIVATKGDPAAPVNRGLNCIKGYFNAKIMYGEDRLVMPLLRMNekgefdkKGKFQQVSWQ 118
Cdd:cd02754 1 KTTCPYCGVGCGVEIGVKDGKVVAVRGDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLLRRN-------GGELVPVSWD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 119 RAFDEMEKQFKKAYNELGVTGIGIFGSGQYTIQEGYAALKLAKAGFRTNNIDPNARHCMASAVVGFMQTFGVDEPSGCYD 198
Cdd:cd02754 74 EALDLIAERFKAIQAEYGPDSVAFYGSGQLLTEEYYAANKLAKGGLGTNNIDTNSRLCMASAVAGYKRSFGADGPPGSYD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 199 DIELTDTIITWGANMAEMHPILWSRVSDRKLSNlDKVKVVNLSTFSNRTSNIADIEIIFKPNTDLAIWNYIAREIVYNhp 278
Cdd:cd02754 154 DIEHADCFFLIGSNMAECHPILFRRLLDRKKAN-PGAKIIVVDPRRTRTADIADLHLPIRPGTDLALLNGLLHVLIEE-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 279 EAMDMKFIKDHCVFatgyadigygmrnnpnhpkfkesekdtvekenvitlddeeatslsylgvkagdkfemkhqgvadkn 358
Cdd:cd02754 231 GLIDRDFIDAHTEG------------------------------------------------------------------ 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 359 weisFDEFKKGLAPYTLEYTARVAKGDdnesledfKKKLQELANLYIEKnRKVVSFWTMGFNQHTRGSWVNEQAYMVHFL 438
Cdd:cd02754 245 ----FEELKAFVADYTPEKVAEITGVP--------EADIREAARLFGEA-RKVMSLWTMGVNQSTQGTAANNAIINLHLA 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 439 LGKQAKPGSGAFSLTGQPSAcGTAREVGTFSHRLPADMVVANPKHREISEKIWKVPAKTINPKPGSPYLNIMRDLEDGKI 518
Cdd:cd02754 312 TGKIGRPGSGPFSLTGQPNA-MGGREVGGLANLLPGHRSVNNPEHRAEVAKFWGVPEGTIPPKPGLHAVEMFEAIEDGEI 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 519 KFAWVQVNNPWQNTANANHWIaAAREMDNFIVVSDCYP-GISAKVADLILPSAMIYEKWGAYGNAERRTQHWKQQVLPVG 597
Cdd:cd02754 391 KALWVMCTNPAVSLPNANRVR-EALERLEFVVVQDAFAdTETAEYADLVLPAASWGEKEGTMTNSERRVSLLRAAVEPPG 469
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 598 AAMSDTWQILEFAKRfklkevwkeqkvdnkltlpsvleeakaMGYSEddtlfdvlfankeaksfnpndaiakGFDNTDvk 677
Cdd:cd02754 470 EARPDWWILADVARR---------------------------LGFGE-------------------------LFPYTS-- 495
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 218562408 678 gderkiqgsdgkeftgygffvQKYLWEEYRKFGLGHGHDLADFdTYHKVR--GLRWPVVNG-KETQWRFNTKFDYY 750
Cdd:cd02754 496 ---------------------PEEVFEEYRRLSRGRGADLSGL-SYERLRdgGVQWPCPDGpPEGTRRLFEDGRFP 549
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
36-924 |
1.50e-177 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 530.23 E-value: 1.50e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 36 KWDKAVCRFCGTGCGIMIARKDGKIVATKGDPAAPVNRGLNCIKGYFNAKIMYGEDRLVMPLLRmnekgefdKKGKFQQV 115
Cdd:COG3383 5 KKVKTVCPYCGVGCGIDLEVKDGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVNSPDRLTTPLIR--------RGGEFREV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 116 SWQRAFDEMEKQFKKAYNELGVTGIGIFGSGQYTIQEGYAALKLAKAGFRTNNIDPNARHCMASAVVGFMQTFGVDEPSG 195
Cdd:COG3383 77 SWDEALDLVAERLREIQAEHGPDAVAFYGSGQLTNEENYLLQKLARGVLGTNNIDNNARLCMASAVAGLKQSFGSDAPPN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 196 CYDDIELTDTIITWGANMAEMHPILWSRVSDRKLSNldkVKVVNLSTFSNRTSNIADIEIIFKPNTDLAIWNYIAREIVY 275
Cdd:COG3383 157 SYDDIEEADVILVIGSNPAEAHPVLARRIKKAKKNG---AKLIVVDPRRTETARLADLHLQIKPGTDLALLNGLLHVIIE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 276 NhpEAMDMKFIKDHCVfatgyadigygmrnnpnhpkfkesekdtvekenvitlddeeatslsylgvkagdkfemkhqgva 355
Cdd:COG3383 234 E--GLVDEDFIAERTE---------------------------------------------------------------- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 356 dknweiSFDEFKKGLAPYTLEYTARVAkGDDNESLEdfkkklqELANLYIEKNRkVVSFWTMGFNQHTRGSWVNEQAYMV 435
Cdd:COG3383 248 ------GFEELKASVAKYTPERVAEIT-GVPAEDIR-------EAARLIAEAKR-AMILWGMGVNQHTQGTDNVNAIINL 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 436 HFLLGKQAKPGSGAFSLTGQPSACGtAREVGTFSHRLPADMVVANPKHREISEKIWKVPAktINPKPGSPYLNIMRDLED 515
Cdd:COG3383 313 ALATGNIGRPGTGPFPLTGQNNVQG-GRDMGALPNVLPGYRDVTDPEHRAKVADAWGVPP--LPDKPGLTAVEMFDAIAD 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 516 GKIKFAWVQVNNPWQNTANANHWIAAAREMDnFIVVSDCYPGISAKVADLILPSAMIYEKWGAYGNAERRTQHWKQQVLP 595
Cdd:COG3383 390 GEIKALWIIGENPAVSDPDANHVREALEKLE-FLVVQDIFLTETAEYADVVLPAASWAEKDGTFTNTERRVQRVRKAVEP 468
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 596 VGAAMSDTWQILEFAKRfklkevwkeqkvdnkltlpsvleeakaMGYseddtlfdvlfankeakSFNPNDAiakgfdnTD 675
Cdd:COG3383 469 PGEARPDWEIIAELARR---------------------------LGY-----------------GFDYDSP-------EE 497
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 676 VkgderkiqgsdgkeftgygffvqkylWEEYRKfgLGHGHDLADFDTYHKVRGLRWPVvngketqwrfntkfdyyAKKAA 755
Cdd:COG3383 498 V--------------------------FDEIAR--LTPDYSGISYERLEALGGVQWPC-----------------PSEDH 532
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 756 PNSDFAFYGDFNKmlTNGdliapkdekehsiknKAKIFFRPFMKAPERPSKEYPFWLATGRVLEHWHSGTMTMRVPELYR 835
Cdd:COG3383 533 PGTPRLFTGRFPT--PDG---------------KARFVPVEYRPPAELPDEEYPLVLTTGRLLDQWHTGTRTRRSPRLNK 595
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 836 AVPEALCYMSEKDGEKLGLNQGDLVWVESRRGKVKARVDMRGRNKPpvGLVYVPWFDENVYINKVTLDATCPLSKQTDFK 915
Cdd:COG3383 596 HAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGEVVLRARVTDRVRP--GTVFMPFHWGEGAANALTNDALDPVSKQPEYK 673
|
....*....
gi 218562408 916 KCAVKIYKA 924
Cdd:COG3383 674 ACAVRVEKV 682
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
1-924 |
2.68e-159 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 482.81 E-value: 2.68e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 1 MNRRDFiKNTAIASAAsvaglsvpssmlgAQEEDWKWDKAVCRFCGTGCGIMIARKDGKIVATKGDPAAPVNRGLNCIKG 80
Cdd:COG0243 1 MSLRDF-KAAGAGAAA-------------LEAAGTKTVKTTCPGCGVGCGLGVKVEDGRVVRVRGDPDHPVNRGRLCAKG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 81 YFNAKIMYGEDRLVMPLLRMNEKGEfdkkGKFQQVSWQRAFDEMEKQFKKAYNELGVTGIGIFGSG----QYTIQEGYAA 156
Cdd:COG0243 67 AALDERLYSPDRLTYPMKRVGPRGS----GKFERISWDEALDLIAEKLKAIIDEYGPEAVAFYTSGgsagRLSNEAAYLA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 157 LKLAKAgFRTNNIDPNARHCMASAVVGFMQTFGVDEPSGCYDDIELTDTIITWGANMAEMHPILWSRVSDRKLSNldKVK 236
Cdd:COG0243 143 QRFARA-LGTNNLDDNSRLCHESAVAGLPRTFGSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREAAKKR--GAK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 237 VVNLSTFSNRTSNIADIEIIFKPNTDLAIWNYIAREIVYNhpEAMDMKFIKDHCVfatGyadigygmrnnpnhpkfkese 316
Cdd:COG0243 220 IVVIDPRRTETAAIADEWLPIRPGTDAALLLALAHVLIEE--GLYDRDFLARHTV---G--------------------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 317 kdtvekenvitlddeeatslsylgvkagdkfemkhqgvadknweisFDEFKKGLAPYTLEYTARVAkGDDnesledfKKK 396
Cdd:COG0243 274 ----------------------------------------------FDELAAYVAAYTPEWAAEIT-GVP-------AED 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 397 LQELANLYIeKNRKVVSFWTMGFNQHTRGSWVNEQAYMVHFLLGKQAKPGSGAFSLTGqpsacgtarevgtfshrlpaDM 476
Cdd:COG0243 300 IRELAREFA-TAKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGGPFSLTG--------------------EA 358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 477 vvanpkhreisekiwkvpaktinpkpgspylniMRDLEDGKIKFAWVQVNNPWQNTANANHWIAAAREMDnFIVVSDCYP 556
Cdd:COG0243 359 ---------------------------------ILDGKPYPIKALWVYGGNPAVSAPDTNRVREALRKLD-FVVVIDTFL 404
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 557 GISAKVADLILPSAMIYEKWGAYGNAE-RRTQHWKQQVLPVGAAMSDTWQILEFAKRFKLKEVWKEqkvdnkltlpsvle 635
Cdd:COG0243 405 TETARYADIVLPATTWLERDDIVTNSEdRRVHLSRPAVEPPGEARSDWEIFAELAKRLGFEEAFPW-------------- 470
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 636 eakamGYSEDDtlfdvlfankeaksfnpndaiakgfdntdvkgderkiqgsdgkeftgygffvqkyLWEEYRKFGLGHGh 715
Cdd:COG0243 471 -----GRTEED-------------------------------------------------------YLRELLEATRGRG- 489
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 716 dlADFDTYHKVRGLRWPVVngKETQWRFNTKFDYYAKKAAPNSDFAFYGDFNKmltngdliapkdekehsiknkakiFFR 795
Cdd:COG0243 490 --ITFEELREKGPVQLPVP--PEPAFRNDGPFPTPSGKAEFYSETLALPPLPR------------------------YAP 541
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 796 PFMKAPErPSKEYPFWLATGRVLEHWHSgtMTMRVPELYRAVPEALCYMSEKDGEKLGLNQGDLVWVESRRGKVKARVDM 875
Cdd:COG0243 542 PYEGAEP-LDAEYPLRLITGRSRDQWHS--TTYNNPRLREIGPRPVVEINPEDAAALGIKDGDLVRVESDRGEVLARAKV 618
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*.
gi 218562408 876 RGRNKPpvGLVYVPWF-------DENVYINKVTLDATCPLSKQTDFKKCAVKIYKA 924
Cdd:COG0243 619 TEGIRP--GVVFAPHGwwyepadDKGGNVNVLTPDATDPLSGTPAFKSVPVRVEKA 672
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
41-921 |
2.96e-109 |
|
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate dehydrogenase alpha chains found mainly archaea but also in alpha and gamma proteobacteria and a small number of gram positive bacteria. The alpha chain contains domains for molybdopterin dinucleotide binding and molybdopterin oxidoreductase (pfam01568 and pfam00384, respectively). The holo-enzyme also contains beta and gamma subunits. The enzyme catalyzes the oxidation of formate (produced from pyruvate during anaerobic growth) to carbon dioxide with the concomitant release of two electrons and two protons. The enzyme's purpose is to allow growth on formate in some circumstances and, in the case of FdhH in gamma proteobacteria, to pass electrons to hydrogenase (by which process acid is neutralized). This model is well-defined, with only a single fragmentary sequence falling between trusted and noise. The alpha subunit of a version of nitrate reductase is closely related.
Pssm-ID: 130652 [Multi-domain] Cd Length: 671 Bit Score: 351.77 E-value: 2.96e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 41 VCRFCGTGCGIMIARKDGKIVATKGDPAAPVNRGLNCIKGYFNAKIMYGEDRLVMPLLRmnekgefdKKGKFQQVSWQRA 120
Cdd:TIGR01591 2 VCPYCGVGCSLNLVVKDGKIVRVEPYQGHKANRGHLCVKGYFAWEFINSKDRLTTPLIR--------EGDKFREVSWDEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 121 FDEMEKQFKKAYNELGVTGIGIFGSGQYTIQEGYAALKLAKAGFRTNNIDPNARHCMASAVVGFMQTFGVDEPSGCYDDI 200
Cdd:TIGR01591 74 ISYIAEKLKEIKEKYGPDSIGFIGSSRGTNEENYLLQKLARAVIGTNNVDNCARVCHGPSVAGLKQTVGIGAMSNTISEI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 201 ELTDTIITWGANMAEMHPILWSRVSDRKLSNldkVKVVNLSTFSNRTSNIADIEIIFKPNTDLAIWNYIAREIVYNHPEa 280
Cdd:TIGR01591 154 ENADLIVIIGYNPAESHPVVAQYLKNAKRNG---AKIIVIDPRKTETAKIADLHIPLKPGTDIALLNAMANVIIEEGLY- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 281 mDMKFIKDHCVfatgyadigygmrnnpnhpkfkesekdtvekenvitlddeeatslsylgvkagdkfemkhqgvadknwe 360
Cdd:TIGR01591 230 -DKAFIEKRTE--------------------------------------------------------------------- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 361 iSFDEFKKGLAPYTLEYTARVAKGDdnesledfKKKLQELANLYIEKNRKVVSfWTMGFNQHTRGSWVNEQAYMVHFLLG 440
Cdd:TIGR01591 240 -GFEEFREIVKGYTPEYVEDITGVP--------ADLIREAARMYAKAGSAAIL-WGMGVTQHSQGVETVMALINLAMLTG 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 441 KQAKPGSGAFSLTGQPSACGTArEVGTFSHRLPADMVVANPKHREISEKIWKVpaKTINPKPGSPYLNIMRDLEDGKIKF 520
Cdd:TIGR01591 310 NIGKPGGGVNPLRGQNNVQGAC-DMGALPDFLPGYQPVSDEEVREKFAKAWGV--VKLPAEPGLRIPEMIDAAADGDVKA 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 521 AWVQVNNPWQNTANANHWIAAAREMDnFIVVSDCYPGISAKVADLILPSAMIYEKWGAYGNAERRTQHWKQQVLPVGAAM 600
Cdd:TIGR01591 387 LYIMGEDPLQSDPNTSKVRKALEKLE-LLVVQDIFMTETAKYADVVLPAAAWLEKEGTFTNAERRIQRFFKAVEPKGESK 465
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 601 SDtWQILEfakrfklkevwkeqkvdnkltlpsvlEEAKAMGYseddtlfdvlfankeakSFNPNDAiakgfdntdvkgde 680
Cdd:TIGR01591 466 PD-WEIIQ--------------------------ELANALGL-----------------DWNYNHP-------------- 487
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 681 rkiqgsdgkeftgygffvqKYLWEEYRKfgLGHGHDLADFDTYHKVRGLRWPVV--NGKETQWRFNTKFDYYAKKAapns 758
Cdd:TIGR01591 488 -------------------QEIMDEIRE--LTPLFAGLTYERLDELGSLQWPCNdsDASPTSYLYKDKFATPDGKA---- 542
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 759 dfafygdfnkmltngdliapkdekehsiknkakIFFRPFMKAP-ERPSKEYPFWLATGRVLEHWHSGTMTMRVPELYRAV 837
Cdd:TIGR01591 543 ---------------------------------KFIPLEWVAPiEEPDDEYPLILTTGRVLTHYNVGEMTRRVAGLRRLS 589
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 838 PEALCYMSEKDGEKLGLNQGDLVWVESRRGKVKARVDMRGRNKPPVGLVYVPWFDENVyiNKVTLDATCPLSKQTDFKKC 917
Cdd:TIGR01591 590 PEPYVEINTEDAKKLGIKDGDLVKVKSRRGEITLRAKVSDRVNKGAIYITMHFWDGAV--NNLTTDDLDPISGTPEYKYT 667
|
....
gi 218562408 918 AVKI 921
Cdd:TIGR01591 668 AVRI 671
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
39-621 |
1.35e-76 |
|
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: 259.45 E-value: 1.35e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 39 KAVCRFCGTGCGIMIARKDGKIVATKGDPAAPVNRGLNCIKGYFNAKIMYGEDRLVMPLLRmnekgefdKKGKFQQVSWQ 118
Cdd:cd02753 1 KTVCPYCGVGCGLELWVKDNKIVGVEPVKGHPVNRGKLCVKGRFGFDFVNSKDRLTKPLIR--------KNGKFVEASWD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 119 RAFDEMEKQFKKAYNELGVTGIGIFGSGQYTIQEGYAALKLAKAGFRTNNIDPNARHCMASAVVGFMQTFGVDEPSGCYD 198
Cdd:cd02753 73 EALSLVASRLKEIKDKYGPDAIAFFGSAKCTNEENYLFQKLARAVGGTNNVDHCARLCHSPTVAGLAETLGSGAMTNSIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 199 DIELTDTIITWGANMAEMHPILWSRVSDRKLsNLDKVKVVNLStfSNRTSNIADIEIIFKPNTDLAIWNYIAREIVYNhp 278
Cdd:cd02753 153 DIEEADVILVIGSNTTEAHPVIARRIKRAKR-NGAKLIVADPR--RTELARFADLHLQLRPGTDVALLNAMAHVIIEE-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 279 EAMDMKFIKDHCvfatgyadigygmrnnpnhpkfkesekdtvekENvitlddeeatslsylgvkagdkfemkhqgvadkn 358
Cdd:cd02753 228 GLYDEEFIEERT--------------------------------EG---------------------------------- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 359 weisFDEFKKGLAPYTLEYTARVAKGDdnesledfKKKLQELANLYIEKNRKVVsFWTMGFNQHTRGSwvneqaYMVH-- 436
Cdd:cd02753 242 ----FEELKEIVEKYTPEYAERITGVP--------AEDIREAARMYATAKSAAI-LWGMGVTQHSHGT------DNVMal 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 437 ----FLLGKQAKPGSGAFSLTGQPSACGtAREVGTFSHRLPadmvvanpkhreisekiwkvpaktinpkpgspylnimrd 512
Cdd:cd02753 303 snlaLLTGNIGRPGTGVNPLRGQNNVQG-ACDMGALPNVLP--------------------------------------- 342
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 513 ledGKIKFAWVQVNNPWQNTANANHWIAAAREMDnFIVVSDCYPGISAKVADLILPSAMIYEKWGAYGNAERRTQHWKQQ 592
Cdd:cd02753 343 ---GYVKALYIMGENPALSDPNTNHVRKALESLE-FLVVQDIFLTETAELADVVLPAASFAEKDGTFTNTERRVQRVRKA 418
|
570 580 590
....*....|....*....|....*....|....*.
gi 218562408 593 VLPVGAAMSDTWQILEFAKR-------FKLKEVWKE 621
Cdd:cd02753 419 VEPPGEARPDWEIIQELANRlgypgfySHPEEIFDE 454
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
39-613 |
1.91e-75 |
|
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: 251.86 E-value: 1.91e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 39 KAVCRFCGTGCGIMIARKDGKIVATKGDPAAPVNRGLNCIKGYFNAKIMYGEDRLVMPLLRMNekgefdKKGKFQQVSWQ 118
Cdd:cd00368 1 PSVCPFCGVGCGILVYVKDGKVVRIEGDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVG------GRGKFVPISWD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 119 RAFDEMEKQFKKAYNELGVTGIGIFGSGQYTIQEGYAALKLAkAGFRTNNIDPNARHCMASAVVGfMQTFGVDEPSGCYD 198
Cdd:cd00368 75 EALDEIAEKLKEIREKYGPDAIAFYGGGGASNEEAYLLQKLL-RALGSNNVDSHARLCHASAVAA-LKAFGGGAPTNTLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 199 DIELTDTIITWGANMAEMHPILWSRVSDRKLSNldkVKVVNLSTFSNRTSNIADIEIIFKPNTDLAIWNyiareivynhp 278
Cdd:cd00368 153 DIENADLILLWGSNPAETHPVLAARLRRAKKRG---AKLIVIDPRRTETAAKADEWLPIRPGTDAALAL----------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 279 eamdmkfikdhcvfatgyadigygmrnnpnhpkfkesekdtvekenvitlddeeatslsylgvkagdkfemkhqgvadkn 358
Cdd:cd00368 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 359 weisfdefkkglapytLEYTARVAkGDDnesledfKKKLQELANLYIeKNRKVVSFWTMGFNQHTRGSWVNEQAYMVHFL 438
Cdd:cd00368 219 ----------------AEWAAEIT-GVP-------AETIRALAREFA-AAKRAVILWGMGLTQHTNGTQNVRAIANLAAL 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 439 LGKQAKPGSGAFSltgqpsacgtarevgtfshrlpadmvvanpkhreisekiwkvpaktinpkpgspylnimrdledgki 518
Cdd:cd00368 274 TGNIGRPGGGLGP------------------------------------------------------------------- 286
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 519 kfawvqVNNPWQNTANANHWIAAAREMDnFIVVSDCYPGISAKVADLILPSAMIYEKWGAYGNAERRTQHWKQQVLPVGA 598
Cdd:cd00368 287 ------GGNPLVSAPDANRVRAALKKLD-FVVVIDIFMTETAAYADVVLPAATYLEKEGTYTNTEGRVQLFRQAVEPPGE 359
|
570
....*....|....*
gi 218562408 599 AMSDTWQILEFAKRF 613
Cdd:cd00368 360 ARSDWEILRELAKRL 374
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
807-924 |
2.68e-51 |
|
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: 175.84 E-value: 2.68e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 807 EYPFWLATGRVLEHWHSGTMTMRVPELYRAVPEALCYMSEKDGEKLGLNQGDLVWVESRRGKVKARVDMRGRnkPPVGLV 886
Cdd:cd02791 2 EYPLWLNTGRVRDQWHTMTRTGRVPRLNAHVPEPYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDR--VRPGEV 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 218562408 887 YVPWFDENVY-----INKVTLDATCPLSKQTDFKKCAVKIYKA 924
Cdd:cd02791 80 FVPMHWGDQFgrsgrVNALTLDATDPVSGQPEFKHCAVRIEKV 122
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
806-923 |
1.99e-46 |
|
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: 161.91 E-value: 1.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 806 KEYPFWLATGRVLEHWHSGTMTMRVPELYRAVPEALCYMSEKDGEKLGLNQGDLVWVESRRGKVKARVDMRGRNKPpvGL 885
Cdd:cd00508 1 EEYPLVLTTGRLLEHWHTGTMTRRSPRLAALAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRP--GT 78
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 218562408 886 VYVPWFDENVY----INKVTLDATCPLSKQTDFKKCAVKIYK 923
Cdd:cd00508 79 VFMPFHWGGEVsggaANALTNDALDPVSGQPEFKACAVRIEK 120
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
92-612 |
5.16e-44 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 163.34 E-value: 5.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 92 RLVMPLLRMNEkgefdkkGKFQQVSWQRAFDEMEKQFKKAYNELGVTGIGI-FGSGQYTIQEGYAALK-LAKA--GFRTN 167
Cdd:pfam00384 1 RLKYPMVRRGD-------GKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAInGGSGGLTDVESLYALKkLLNRlgSKNGN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 168 NIDPNARHCMASAvvgfmQTFGVDEPSG-----CYDDIELTDTIITWGANMAEMHPILWSRVSDRKLSNldKVKVVNLST 242
Cdd:pfam00384 74 TEDHNGDLCTAAA-----AAFGSDLRSNylfnsSIADIENADLILLIGTNPREEAPILNARIRKAALKG--KAKVIVIGP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 243 FSNRTSNIADIEIifKPNTDLAIWNYIAreivynHPeamdmkFIKdhcvfatgyadigygmrnnpnhpkfkesekdtvek 322
Cdd:pfam00384 147 RLDLTYADEHLGI--KPGTDLALALAGA------HV------FIK----------------------------------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 323 envitlddeeatslsylgvkagdkfemkhqgvadknweisfdEFKKGlapytleytarvakgddneslEDFKKklqelan 402
Cdd:pfam00384 178 ------------------------------------------ELKKD---------------------KDFAP------- 187
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 403 lyieknrKVVSFWTMGFNQHTRGSWVNEQAYMVHFLLGKQAKPGSGAFSLTgqpSACGTAREVGtfshrlpadmvvanpk 482
Cdd:pfam00384 188 -------KPIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLN---ILQGAASPVG---------------- 241
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 483 hreisekiwkvpAKTINPKPGSPYLNIMRDLEDGKIKFAWVQVNNPWQNTANANHWIAAAREMDNFiVVSDCYPGIS-AK 561
Cdd:pfam00384 242 ------------ALDLGLVPGIKSVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLF-VVYDGHHGDKtAK 308
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 218562408 562 VADLILPSAMIYEKWGAYGNAERRTQHWKQQVLPVGAAMSDtWQIL-EFAKR 612
Cdd:pfam00384 309 YADVILPAAAYTEKNGTYVNTEGRVQSTKQAVPPPGEARED-WKILrALSEV 359
|
|
| formate-DH-alph |
TIGR01553 |
formate dehydrogenase-N alpha subunit; This model describes a subset of formate dehydrogenase ... |
1-890 |
4.93e-42 |
|
formate dehydrogenase-N alpha subunit; This model describes a subset of formate dehydrogenase alpha chains found mainly in proteobacteria but also in Aquifex. The alpha chain contains domains for molybdopterin dinucleotide binding and molybdopterin oxidoreductase (pfam01568 and pfam00384, respectively). The holo-enzyme also contains beta and gamma subunits of 32 and 20 kDa. The enzyme catalyzes the oxidation of formate (produced from pyruvate during anaerobic growth) to carbon dioxide with the concomitant release of two electrons and two protons. The electrons are utilized mainly in the nitrate respiration by nitrate reductase. In E. coli and Salmonella, there are two forms of the formate dehydrogenase, one induced by nitrate which is strictly anaerobic (fdn), and one incuced during the transition from aerobic to anaerobic growth (fdo). This subunit is one of only three proteins in E. coli which contain selenocysteine. This model is well-defined, with a large, unpopulated trusted/noise gap. [Energy metabolism, Anaerobic, Energy metabolism, Electron transport]
Pssm-ID: 273689 [Multi-domain] Cd Length: 1009 Bit Score: 166.62 E-value: 4.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 1 MNRRDFIKNTAI-ASAASVAGLSVPSSMLGAQEEDWKWDKA-----VCRFCGTGCGIMI-------ARKDGKIVATKGDP 67
Cdd:TIGR01553 2 ISRRAFLKLTAGgATLSAFGGLGFDLAPAKAQARALKTVDAkqttsVCCYCSVSCGLLVyssshtgDNKTNRAIHVEGDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 68 AAPVNRGLNCIKGYFNAKIMYGEDRLVMPLLRMnekgefDKKGKFQQVSWQRAFDEMEKQFKKAYNELGVT--------- 138
Cdd:TIGR01553 82 DHPINRGSLCPKGASTWDLVNNERRPANPLYRA------PGSDQWEEISWDWAIDTIARRVKDTRDATFVTkdakgqvvn 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 139 ---GIGIFGSGQYTIQEGYAALKLAKAgFRTNNIDPNARHCMASAVVGFMQTFGVDEPSGCYDDIELTDTIITWGANMAE 215
Cdd:TIGR01553 156 rcdGIASVGSSAMDNEECWLYQKWLRS-LGLFYIEHQARIUHSPTVASLAPSFGRGAMTNNWVDIKNSDLILVMGGNPAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 216 MHPILWSRVSDRKLSNldkVKVVNLSTFSNRTSNIADIEIIFKPNTDLAIWNYIAREIVYNHpeamdmKFIKDHCVFATG 295
Cdd:TIGR01553 235 NHPIGFKWAIRAKKKG---AKIIHIDPRFNRTATVADLYAPIRSGSDIAFLNGMIKYILEKE------LYQKEYVVNYTN 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 296 YADI---GYGMRN------NPNHPKFKESEKDTVEKENVITLDDEEatslsylgvkagdkfeMKHQgvadknwEISFDEF 366
Cdd:TIGR01553 306 ASFIvgeGFAFEDglfagyNKETRKYDKSKWGYEFDENGNPKRDET----------------LKHP-------RCVFNIL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 367 KKGLAPYTLEYTARVAkgddNESLEDFKKKLQELANLYIeKNRKVVSFWTMGFNQHTRGSWVNEQAYMVHFLLGKQAKPG 446
Cdd:TIGR01553 363 KEHYSRYTPEKVSAIC----GTPKELFLKVYEEYCKTGK-PNKAMTILYALGWTQHSVGTQNIRAMSINQLLLGNIGVPG 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 447 SGAFSLTGQPSACGTArEVGTFSHRLPADMVVANPKHREISEKIWKVPAKTINP-------------------------- 500
Cdd:TIGR01553 438 GGINALRGHSNVQGST-DHGLLMHILPGYLGTPRASIPTYEQYTKKFTPVSKDPqsanywsnfpkffasyiksmwgdaat 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 501 -----------KPG---SPYLNIMRDLEDGKIKFAWVQVNNPWQNTANANHWIAAAREMDnFIVVSDCY----------P 556
Cdd:TIGR01553 517 nengwaydylpKGEdgyDSWLTLFDDMFQGKIKGFFAWGQNPLNSGPNSNKTREALTKLK-WMVVMDPFdnetgsfwrgP 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 557 GISAKVAD---LILPSAMIYEKWGAYGNAERRTQ-HWKQqVLPVGAAMSDTWQILEFAKRFK--------------LKEV 618
Cdd:TIGR01553 596 GMDPKEIKtevFFLPTAVFIEKEGSISNSGRWMQwRYKG-PDPPGNAIPDGDIIVELAKRVQelyakeggklaepvTKLK 674
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 619 WKEQKVDNkltlPSVLEEAKAM-GYSEDDtlFDV------------LFANKEAK------------SFNPNDAIAKGFDN 673
Cdd:TIGR01553 675 WDYWVPDH----PDAHEIAKEInGYALKD--FKVgdveykkgqqiaTFGHLRDDgsttsgcwlytgSYTEKGNMAARRDK 748
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 674 TDVKGderkiQGSdgkeFTGYGFfvqkyLWEEYRKFGLGHGHDLADFDTYHKVRGL-RWpvvNGKETQWrFNTKFDYYAK 752
Cdd:TIGR01553 749 SDPAG-----LGL----YPGWTW-----AWPANRRVLYNRASVDLNGKPWDPERALvEW---NAAEKKW-VGDIPDYPPT 810
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 753 kAAPNSDF-AFYgdfnkMLTNG--DLIAPKDEK-----EHSIKNKAKIFFRPF-MKAPERPS--------------KEYP 809
Cdd:TIGR01553 811 -APPEKGKgAFI-----MKPEGygRLFAPGKREdgplpEHYEPMESPVITNPFhPNVLHNPTalhyktdekavgdpKRYP 884
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 810 FWLATGRVLEHWHsgTMTMRVPELYRAVPEALCYMSEKDGEKLGLNQGDLVWVESRRGKVKARVDMRGRNKP------PV 883
Cdd:TIGR01553 885 FVATTYRLTEHWH--TWTRNTPWLLEAEPQMFCEISEELATEKGIQNGDKVILESVRGKIWAKAIVTKRIKPlaiqgqQV 962
|
....*..
gi 218562408 884 GLVYVPW 890
Cdd:TIGR01553 963 HMIGIPI 969
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
39-614 |
2.48e-37 |
|
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: 149.47 E-value: 2.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 39 KAVCRFCGTGCGIMIARKDGKIVATKGDPAAPVNRGLNCIKGYFNAKIMYGEDRLVMPLLRMNekgefdKKGKFQQVSWQ 118
Cdd:cd02752 1 RTICPYCSVGCGLIAYVQNGVWVHQEGDPDHPVNRGSLCPKGAALRDFVHSPKRLKYPMYRAP------GSGKWEEISWD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 119 RAFDEMEKQFKK-------AYNELGVT-----GIGIFGSGQYTIQEGYAALKLAKAgFRTNNIDPNARHCMASAVVGFMQ 186
Cdd:cd02752 75 EALDEIARKMKDirdasfvEKNAAGVVvnrpdSIAFLGSAKLSNEECYLIRKFARA-LGTNNLDHQARIUHSPTVAGLAN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 187 TFGVDEPSGCYDDIELTDTIITWGANMAEMHPILWSRVSDRKLSNLDKVKVVNlSTFsNRTSNIADIEIIFKPNTDLAiw 266
Cdd:cd02752 154 TFGRGAMTNSWNDIKNADVILVMGGNPAEAHPVSFKWILEAKEKNGAKLIVVD-PRF-TRTAAKADLYVPIRSGTDIA-- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 267 nyiareivynhpeamdmkFIkdhcvfatgyadigYGMrnnpnhpkfkesekdtvekenvitlddeeatslsylgvkagdk 346
Cdd:cd02752 230 ------------------FL--------------GGM------------------------------------------- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 347 feMKHqgvadknweisfdefkkgLAPYTLEYTARVAkgddNESLEDFKKKLQELANlYIEKNRKVVSFWTMGFNQHTRGS 426
Cdd:cd02752 235 --INY------------------IIRYTPEEVEDIC----GVPKEDFLKVAEMFAA-TGRPDKPGTILYAMGWTQHTVGS 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 427 WVNEQAYMVHFLLGKQAKPGSGAFSLTGQPSACGtAREVGTFSHRLPADMvvanpkhreisekiwkvpaKTINPKPGSPY 506
Cdd:cd02752 290 QNIRAMCILQLLLGNIGVAGGGVNALRGHSNVQG-ATDLGLLSHNLPGYL-------------------GGQNPNSSFPN 349
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 507 LNIMRDLEDgkiKFAWVQVNNPWQNTANANhWIAAAreMDNfivvsdcypgISAKVADLILPSAMIYEKWGAYGNAERRT 586
Cdd:cd02752 350 ANKVRRALD---KLDWLVVIDPFPTETAAF-WKNPG--MDP----------KSIQTEVFLLPAACQYEKEGSITNSGRWL 413
|
570 580
....*....|....*....|....*....
gi 218562408 587 QhWKQQVL-PVGAAMSDTWQILEFAKRFK 614
Cdd:cd02752 414 Q-WRYKVVePPGEAKSDGDILVELAKRLG 441
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
39-617 |
3.54e-32 |
|
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: 131.27 E-value: 3.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 39 KAVCRFCGTGCGIMIARKDGKIVATKGDPAAPVNRGLNCIKGYFNAKIMYGEDRLVMPLLRMNEKGEfdkkGKFQQVSWQ 118
Cdd:cd02759 1 KGTCPGCHSGCGVLVYVKDGKLVKVEGDPNHPTNKGRLCMRGLAAPEIVYHPDRLLYPLKRVGERGE----NKWERISWD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 119 RAFDEMEKQFKKAYNELGVTGIGI-FGSGQYTiqeGYAALKLAKAGFRTNNIdPNARHCMASAVVGFMQTFGVDEPSGC- 196
Cdd:cd02759 77 EALDEIAEKLAEIKAEYGPESIATaVGTGRGT---MWQDSLFWIRFVRLFGS-PNLFLSGESCYWPRDMAHALTTGFGLg 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 197 YDDIEL--TDTIITWGANMAEMHPIL-WSRVSD-RKLSNldKVKVV--NLSTFSNRtsniADIEIIFKPNTD----LAIW 266
Cdd:cd02759 153 YDEPDWenPECIVLWGKNPLNSNLDLqGHWLVAaMKRGA--KLIVVdpRLTWLAAR----ADLWLPIRPGTDaalaLGML 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 267 NYIAREIVYNHpeamdmkfikdhcvfatgyadigygmrnnpnhpkfkesekDTVEkenvitlddeeatslsylgvkagdk 346
Cdd:cd02759 227 NVIINEGLYDK----------------------------------------DFVE------------------------- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 347 femkhqgvadkNWEISFDEFKKGLAPYTLEYTARVAkGDDNEsledfkkKLQELANLYIeknrkvvsfwtmgfnqhtrgs 426
Cdd:cd02759 242 -----------NWCYGFEELAERVQEYTPEKVAEIT-GVPAE-------KIRKAARLYA--------------------- 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 427 wvneqaymvhfllgkQAKPGSGAFSLTGQ--PSACGTAREVgtfshrlpADMVvanpkhreisekiwkvpAKTIN-PKPG 503
Cdd:cd02759 282 ---------------TAKPACIQWGLAIDqqKNGTQTSRAI--------AILR-----------------AITGNlDVPG 321
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 504 S----PYlnimrdledgKIKFAWVQVNNPWQNTANANHWIAAAREMDnFIVVSDCYPGISAKVADLILPSAMIYEKWGAY 579
Cdd:cd02759 322 GnlliPY----------PVKMLIVFGTNPLASYADTAPVLEALKALD-FIVVVDLFMTPTAMLADIVLPVAMSLERPGLR 390
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 218562408 580 GNAERRTQHWKQQ--VLPVGAAMSDTWQILEFAKRFKLKE 617
Cdd:cd02759 391 GGFEAENFVQLRQkaVEPYGEAKSDYEIVLELGKRLGPEE 430
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
806-923 |
1.25e-31 |
|
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: 119.27 E-value: 1.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 806 KEYPFWLATGRVLEHWHSGTMTMRVPELYRAVPEALCYMSEKDGEKLGLNQGDLVWVESRRGKV--KARVDmrgrNKPPV 883
Cdd:cd02790 1 EEYPLVLTTGRVLYHYHTGTMTRRAEGLDAIAPEEYVEINPEDAKRLGIEDGEKVRVSSRRGSVevRARVT----DRVPE 76
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 218562408 884 GLVYVP--WFDENVyiNKVTLDATCPLSKQTDFKKCAVKIYK 923
Cdd:cd02790 77 GVVFMPfhFAEAAA--NLLTNAALDPVAKIPEFKVCAVRVEK 116
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
40-617 |
7.95e-31 |
|
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: 127.75 E-value: 7.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 40 AVC-RFCGTGCGIMIARKDGKIVATKGDPAAPVNRGLNCIKGYFNAKIMYGEDRLVMPLLRMNEKGefdkkGKFQQVSWQ 118
Cdd:cd02766 2 SVCpLDCPDTCSLLVTVEDGRIVRVEGDPAHPYTRGFICAKGARYVERVYSPDRLLTPLKRVGRKG-----GQWERISWD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 119 RAFDEMEKQFKKAYNELGVTGI-GIFGSGQYTIQEGYAALKLAKAGFRTNNIDPnarHCMASAVVGFMQTFGvDEPSGCY 197
Cdd:cd02766 77 EALDTIAAKLKEIKAEYGPESIlPYSYAGTMGLLQRAARGRFFHALGASELRGT---ICSGAGIEAQKYDFG-ASLGNDP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 198 DDIELTDTIITWGANMAEMHPILWSRVSDRKLSNldkVKVVNLSTFSNRTSNIADIEIIFKPNTDLAIWNYIAREIVYNh 277
Cdd:cd02766 153 EDMVNADLIVIWGINPAATNIHLMRIIQEARKRG---AKVVVIDPYRTATAARADLHIQIRPGTDGALALGVAKVLFRE- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 278 pEAMDMKFIkdhcvfatgyadigygmrnnpnhpkfkesekdtvekenvitlddeeatslsylgvkagdkfemkhqgvadK 357
Cdd:cd02766 229 -GLYDRDFL----------------------------------------------------------------------A 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 358 NWEISFDEFKKGLAPYTLEYTARVAkgddNESLEDFKkklqELANLYIEKNRkvVSFWtMGFN-QHTRGSWVNEQAYM-V 435
Cdd:cd02766 238 RHTEGFEELKAHLETYTPEWAAEIT----GVSAEEIE----ELARLYGEAKP--PSIR-LGYGmQRYRNGGQNVRAIDaL 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 436 HFLLGKQAKPGSGAFSLTGQPsacgtarevgtfshrlpadmvvanpkhreisekiwkvpaktinpkpgspylnimrdled 515
Cdd:cd02766 307 PALTGNIGVPGGGAFYSNSGP----------------------------------------------------------- 327
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 516 gKIKFAWVQVNNPWQNTANANHWIAAAREMDNFIVVSDCYPGISAKVADLILPSAMIYEKW---GAYGnaerrtQHW--- 589
Cdd:cd02766 328 -PVKALWVYNSNPVAQAPDSNKVRKGLAREDLFVVVHDQFMTDTARYADIVLPATTFLEHEdvyASYW------HYYlqy 400
|
570 580
....*....|....*....|....*....
gi 218562408 590 -KQQVLPVGAAMSDTWQILEFAKRFKLKE 617
Cdd:cd02766 401 nEPAIPPPGEARSNTEIFRELAKRLGFGE 429
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
41-612 |
4.37e-27 |
|
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: 115.86 E-value: 4.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 41 VCRFCGTGCGIMIARKDGKIVATKGDPAAPVNRGLNCIKGYFNAKIMYGEDRLVMPLLRMNEKGEfdkkGKFQQVSWQRA 120
Cdd:cd02755 4 ICEMCSSRCGILARVEDGRVVKIDGNPLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRVGERGE----GKFREASWDEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 121 FDEMEKQFKKAYNELGVTGIGIFGSGqyTIQEGYaaLKLAKAGFRTNNIDPNARHCMASAVVGFMQTFGVDEPSGcYDDI 200
Cdd:cd02755 80 LQYIASKLKEIKEQHGPESVLFGGHG--GCYSPF--FKHFAAAFGSPNIFSHESTCLASKNLAWKLVIDSFGGEV-NPDF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 201 ELTDTIITWGANMAEmhPILWSRVSDRKLSNLDKVKVVNLSTFSNRTSNIADIEIIFKPNTD----LAIWNYIAREIVYn 276
Cdd:cd02755 155 ENARYIILFGRNLAE--AIIVVDARRLMKALENGAKVVVVDPRFSELASKADEWIPIKPGTDlafvLALIHVLISENLY- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 277 hpeamDMKFIKDHCvfatgyadigYGmrnnpnhpkfkesekdtvekenvitlddeeatslsylgvkagdkfemkhqgvad 356
Cdd:cd02755 232 -----DAAFVEKYT----------NG------------------------------------------------------ 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 357 knweisFDEFKKGLAPYTLEYTARVAKGDdnesledfKKKLQELANLYIEKNRK-VVSFWTMG-FNQHTRGSWvnEQAYM 434
Cdd:cd02755 243 ------FELLKAHVKPYTPEWAAQITDIP--------ADTIRRIAREFAAAAPHaVVDPGWRGtFYSNSFQTR--RAIAI 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 435 VHFLLGKQAKPGSgafsltgqpsacgtarevgtfshrlpadmvvanpkhreisekiWkVPAKTInpkpgSPYlnimrdle 514
Cdd:cd02755 307 INALLGNIDKRGG-------------------------------------------L-YYAGSA-----KPY-------- 329
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 515 dgKIKFAWVQVNNPWQNTANANHWIAAAREMDnFIVVSDCYPGISAKVADLILPSAMIYEK----WGAYGNAERRTQhwK 590
Cdd:cd02755 330 --PIKALFIYRTNPFHSMPDRARLIKALKNLD-LVVAIDILPSDTALYADVILPEATYLERdepfSDKGGPAPAVAT--R 404
|
570 580
....*....|....*....|...
gi 218562408 591 QQVLPVGAAMSDTWQIL-EFAKR 612
Cdd:cd02755 405 QRAIEPLYDTRPGWDILkELARR 427
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
806-923 |
2.16e-26 |
|
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: 104.61 E-value: 2.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 806 KEYPFWLATGRVLEHWHSGTMTMRVPELYRAVPEALCYMSEKDGEKLGLNQGDLVWVESRRGKVKARVDMRGRNKPPVgl 885
Cdd:cd02792 1 EEFPLVLTTGRLTEHFHGGNMTRNSPYLAELQPEMFVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHE-- 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 218562408 886 VYVPW---FDENVY---INKVTLDATCPLSKQTDFKKCAVKIYK 923
Cdd:cd02792 79 VGIPYhwgGMGLVIgdsANTLTPYVGDPNTQTPEYKAFLVNIEK 122
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
810-918 |
3.61e-25 |
|
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: 100.81 E-value: 3.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 810 FWLATGRVLEHWHSGTMTMRVPELYRAVPEAlCYMSEKDGEKLGLNQGDLVWVESRRGKVKARVDMRGRNKPpvGLVYVP 889
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKPEPEV-VEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRP--GVVFMP 77
|
90 100 110
....*....|....*....|....*....|...
gi 218562408 890 --WFDENVY--INKVTLDATCPLSKQTDFKKCA 918
Cdd:pfam01568 78 fgWWYEPRGgnANALTDDATDPLSGGPEFKTCA 110
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
1-642 |
2.01e-24 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 109.76 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 1 MNRRDFIKNTAIASAASVAGLSVPSSmLGAQEEDW-----KWDKAVCRFCGTGCGIMIARKDGKIVATKGDPAAPVNRGL 75
Cdd:PRK15488 3 LSRRDFLKGAGAGCAACALGSLLPGA-LAANEIAQlkgktKLTPSICEMCSTRCPIEARVVNGKNVFIQGNPKAKSFGTK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 76 NCIKGYFNAKIMYGEDRLVMPLLRMNEKGEfdkkGKFQQVSWQRAFDEMEKQFKKAYNELGVTGIgIFG--SGQytiQEG 153
Cdd:PRK15488 82 VCARGGSGHSLLYDPQRIVKPLKRVGERGE----GKWQEISWDEAYQEIAAKLNAIKQQHGPESV-AFSskSGS---LSS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 154 YaALKLAKAgFRTNNIDPNARHCMASAVVGFMQTFGVDEPSgcydDIELTDTIITWGANMAEmhpilWSRVSD-RKLSNL 232
Cdd:PRK15488 154 H-LFHLATA-FGSPNTFTHASTCPAGYAIAAKVMFGGKLKR----DLANSKYIINFGHNLYE-----GINMSDtRGLMTA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 233 DKVKVVNLSTFSNRTSNIAD-------IeiifKPNTD----LAIWNYIAREIVYnhpeamDMKFIKDHCvfaTGYadigy 301
Cdd:PRK15488 223 QMEKGAKLVVFEPRFSVVASkadewhaI----RPGTDlavvLALCHVLIEENLY------DKAFVERYT---SGF----- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 302 gmrnnpnhPKFKESEKD-TVEKENVITlddeeatslsylGVKAGDKFEMKHQ-------GVADKNWEISF--DEFKKGLA 371
Cdd:PRK15488 285 --------EELAASVKEyTPEWAEAIS------------DVPADDIRRIARElaaaaphAIVDFGHRATFtpEEFDMRRA 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 372 PYTLeytarvakgddNESLEDFKKKlqelANLYIEKNRKVvsfwtmgFNQhtrgswvneqaymvhfLLGKQ-----AKPG 446
Cdd:PRK15488 345 IFAA-----------NVLLGNIERK----GGLYFGKNASV-------YNK----------------LAGEKvaptlAKPG 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 447 SGAFSltgQPSAcgtarevgtfsHRLpaDMVvaNPKHREISEK---IWKVPAKTINPKpgsPYlnimrdledgKIKfAWV 523
Cdd:PRK15488 387 VKGMP---KPTA-----------KRI--DLV--GEQFKYIAAGggvVQSIIDATLTQK---PY----------QIK-GWV 434
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 524 QV-NNPWQNTANANHWIAAAREMDnFIVVSDCYPGISAKVADLILPSAMIYE----------KWGAYGnaerrtqhWKQQ 592
Cdd:PRK15488 435 MSrHNPMQTVTDRADVVKALKKLD-LVVVCDVYLSESAAYADVVLPESTYLErdeeisdksgKNPAYA--------LRQR 505
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 593 VL-PVGAAmSDTWQIL-EFAKRFKLK--------EVWKEQKVDNKltlPSVLEEAKAMGY 642
Cdd:PRK15488 506 VVePIGDT-KPSWQIFkELGEKMGLGqyypwqdmETLQLYQVNGD---HALLKELKKKGY 561
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
45-625 |
7.34e-23 |
|
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: 104.10 E-value: 7.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 45 CGTGCGIMIARKDGKIVATK-GDPAAP-VNRGlnCIKGYFNAKIMYGEDRLVMPLLRMNEKGEfdkkGKFQQVSWQRAFD 122
Cdd:cd02765 8 CGGRCPLKCHVRDGKIVKVEpNEWPDKtYKRG--CTRGLSHLQRVYSPDRLKYPMKRVGERGE----GKFERITWDEALD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 123 EMEKQFKKAYNELGVTGIGIF-GSGQYTIQeGYAALKLAKAGFRTN---NIDPNARHCMaSAVVGFMQTFGVDEPsgcyD 198
Cdd:cd02765 82 TIADKLTEAKREYGGKSILWMsSSGDGAIL-SYLRLALLGGGLQDAltyGIDTGVGQGF-NRVTGGGFMPPTNEI----T 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 199 DIELTDTIITWGANMAEMHP-----ILWSRVSDRKLSNLDKVkvvnlstFSNrTSNIADIEIIFKPNTD----LAIWNYI 269
Cdd:cd02765 156 DWVNAKTIIIWGSNILETQFqdaefFLDARENGAKIVVIDPV-------YST-TAAKADQWVPIRPGTDpalaLGMINYI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 270 AREIVYNHPeamdmkfikdhcvFATGYADIGYGMRNNPNHPKFKESEKDTVEKENVITLDDEEATSLSY--LGVKAGDKF 347
Cdd:cd02765 228 LEHNWYDEA-------------FLKSNTSAPFLVREDNGTLLRQADVTATPAEDGYVVWDTNSDSPEPVaaTNINPALEG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 348 EMKHQGVADKNweiSFDEFKKGLAPYTLEYTArvakgdDNESLEDfkKKLQELANLYIekNRKVVSFWTMGFNQHTRGSW 427
Cdd:cd02765 295 EYTINGVKVHT---VLTALREQAASYPPKAAA------EICGLEE--AIIETLAEWYA--TGKPSGIWGFGGVDRYYHSH 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 428 VNEQAY-MVHFLLGKQAKPGSGAfsltgqpsacgtarevgtfshrlpadmvvanpkhreisekiwkvpaktinpkpgspy 506
Cdd:cd02765 362 VFGRTAaILAALTGNIGRVGGGV--------------------------------------------------------- 384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 507 lnimrdledGKIKFAWVQVNNPWQNTANANHWIAAAREMDnFIVVSDCYPGISAKVADLILPSAMIYEKWGAYGNAERRT 586
Cdd:cd02765 385 ---------GQIKFMYFMGSNFLGNQPDRDRWLKVMKNLD-FIVVVDIFHTPTVRYADIVLPAAHWFEVEDLLVRYTTHP 454
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 218562408 587 QHWKQQ--VLPVGAAMSDTWQILEFAKRFKLKEVWKEQKVD 625
Cdd:cd02765 455 HVLLQQkaIEPLFESKSDFEIEKGLAERLGLGDYFPKTPED 495
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
817-915 |
7.15e-22 |
|
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site. This hierarchy is of the conserved MopB_CT domain present in many, but not all, MopB homologs.
Pssm-ID: 239176 [Multi-domain] Cd Length: 101 Bit Score: 91.23 E-value: 7.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 817 VLEHWHSGTMTmRVPELYRAVPEALCYMSEKDGEKLGLNQGDLVWVESRRGKVKARVDMRGRnkPPVGLVYVP-----WF 891
Cdd:cd02775 1 LRDHFHSGTRT-RNPWLRELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDG--VPPGVVFLPhgwghRG 77
|
90 100
....*....|....*....|....
gi 218562408 892 DENVYINKVTLDATCPLSKQTDFK 915
Cdd:cd02775 78 GRGGNANVLTPDALDPPSGGPAYK 101
|
|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
35-89 |
1.77e-21 |
|
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for which the structure is known. This first domain (residues 1 to 60) of PDB:1aa6 is an Fe4S4 cluster just below the protein surface.
Pssm-ID: 428168 [Multi-domain] Cd Length: 55 Bit Score: 88.50 E-value: 1.77e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 218562408 35 WKWDKAVCRFCGTGCGIMIARKDGKIVATKGDPAAPVNRGLNCIKGYFNAKIMYG 89
Cdd:pfam04879 1 MKVVKTICPYCGVGCGLEVHVKDGKIVKVEGDPDHPVNEGRLCVKGRFGYERVYN 55
|
|
| 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 ... |
39-224 |
8.59e-19 |
|
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: 90.53 E-value: 8.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 39 KAVCRFCGTGCGIMIARKDGKIVATKGDPAAPVNRGLNCIKGYFNAKIMYGEDRLVMPLLRmnekgefdKKGKFQQVSWQ 118
Cdd:cd02771 1 PSICHHCSVGCNISLGERYGELRRVENRYNGAVNHYFLCDRGRFGYGYVNSRDRLTQPLIR--------RGGTLVPVSWN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 119 RAFDEMEKQFKKAynelgVTGIGIFGSGQYTIQEGYAALKLAKAGFRTNNIDPNARhcmaSAVVGFMQTFGVDEPSgcYD 198
Cdd:cd02771 73 EALDVAAARLKEA-----KDKVGGIGSPRASNESNYALQKLVGAVLGTNNVDHRAR----RLIAEILRNGPIYIPS--LR 141
|
170 180
....*....|....*....|....*.
gi 218562408 199 DIELTDTIITWGANMAEMHPILWSRV 224
Cdd:cd02771 142 DIESADAVLVLGEDLTQTAPRIALAL 167
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
49-642 |
1.28e-18 |
|
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: 90.75 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 49 CGIMIAR-KDGKIVATKGDPAAPVNrglNCIKGYFNAKIMYGEDRLVMPLLRMN--EKGEFDK----KGKFQQVSWQRAF 121
Cdd:cd02751 6 WGPFKAHvKDGVIVRVEPDDTDQPR---PCPRGRSVRDRVYSPDRIKYPMKRVGwlGNGPGSRelrgEGEFVRISWDEAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 122 DEMEKQFKKAYNELGVTGI-GIFGSGQYTIQEGYA--ALK--LAKAGFRTNNIDPnarHCMASAVVGFMQTFGVDEPSGC 196
Cdd:cd02751 83 DLVASELKRIREKYGNEAIfGGSYGWASAGRLHHAqsLLHrfLNLIGGYLGSYGT---YSTGAAQVILPHVVGSDEVYEQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 197 Y---DDI-ELTDTIITWGANMAEMHPILWSRVSDRKLSNLDK-----VKVVNLSTFSNRTSNIADIE-IIFKPNTDLAIW 266
Cdd:cd02751 160 GtswDDIaEHSDLVVLFGANPLKTRQGGGGGPDHGSYYYLKQakdagVRFICIDPRYTDTAAVLAAEwIPIRPGTDVALM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 267 NYIAREIVYNHPEamDMKFIKDHCVfatgyadiGYGmrnnpnhpKFKES---EKDTVEKenvitlDDEEATSLSylGVKA 343
Cdd:cd02751 240 LAMAHTLITEDLH--DQAFLARYTV--------GFD--------EFKDYllgESDGVPK------TPEWAAEIT--GVPA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 344 GdkfemkhqgvadknweisfdefkkglapytleytarvakgddnesledfkkKLQELANLYIEKNRKVVSFWtmGFNQHT 423
Cdd:cd02751 294 E---------------------------------------------------TIRALAREIASKRTMIAQGW--GLQRAH 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 424 RGswvnEQAY----MVHFLLGKQAKPGSGaFSLTGQPSACGTAREVGTFSHRLPAdmvVANPKHREISEKIWkvpAKTIN 499
Cdd:cd02751 321 HG----EQPAwmlvTLAAMLGQIGLPGGG-FGFGYGYSNGGGPPRGGAGGPGLPQ---GKNPVKDSIPVARI---ADALL 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 500 pKPGSPYLNIMRDLEDGKIKFAWVQVNNPWQNTANANHWIAAAREmDNFIVVSDCYPGISAKVADLILPSAMIYEKW--G 577
Cdd:cd02751 390 -NPGKEFTANGKLKTYPDIKMIYWAGGNPLHHHQDLNRLIKALRK-DETIVVHDIFWTASARYADIVLPATTSLERNdiG 467
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 578 AYGNAERRTQ-HWKQQVLPVGAAMSDTWQILEFAKRF-----------------KLKEVWKEQKVDNKLTLPSvLEEAKA 639
Cdd:cd02751 468 LTGNYSNRYLiAMKQAVEPLGEARSDYEIFAELAKRLgveeeftegrdemewleHLYEETRAKAAGPGPELPS-FEEFWE 546
|
...
gi 218562408 640 MGY 642
Cdd:cd02751 547 KGI 549
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
37-616 |
2.33e-18 |
|
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: 89.42 E-value: 2.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 37 WDKAVCRFCGTGCGIMIARKDGKIVATKGDPAAPVNRGLNCIKGYFNAKIMYGEDRLVMPLLRMNEKGEFDKKGKFQQVS 116
Cdd:cd02757 1 WVPSTCQGCTAWCGLQAYVEDGRVTKVEGNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRTNPRKGRDVDPKFVPIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 117 WQRAFDEMEKQFKKAYNELGVTGIGIFgSGQYTIQEGYAALKLAKAGFRTNNIDPNARhCMASAVVGFMQT-FGVDEPSG 195
Cdd:cd02757 81 WDEALDTIADKIRALRKENEPHKIMLH-RGRYGHNNSILYGRFTKMIGSPNNISHSSV-CAESEKFGRYYTeGGWDYNSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 196 CYDDielTDTIITWGAN-MAEMHPI-LWSRVSDRKlsnLDKVKVVNLSTFSNRTSNIADIEIIFKPNTD----LAIWNYI 269
Cdd:cd02757 159 DYAN---AKYILFFGADpLESNRQNpHAQRIWGGK---MDQAKVVVVDPRLSNTAAKADEWLPIKPGEDgalaLAIAHVI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 270 AREIVYNHPeamdmkFIKDhcvFATGyadigygmrnnpnHPKFKESEkdtvekenviTLDDEEatslsylgvkagdkFEM 349
Cdd:cd02757 233 LTEGLWDKD------FVGD---FVDG-------------KNYFKAGE----------TVDEES--------------FKE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 350 KHQGVADKNWeisfdefKKGLAPYTLEYTARVAkGDDNESLEDFKKklqELANlyieKNRKVVSFWTMGFNQHTRGSWVN 429
Cdd:cd02757 267 KSTEGLVKWW-------NLELKDYTPEWAAKIS-GIPAETIERVAR---EFAT----AAPAAAAFTWRGATMQNRGSYNS 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 430 EQAYMVHFLLGKQAKPGsgafsltgqpsacgtarevGTFSHRlpadmvvanpkhreisekiwkvpaktinpkpGSPYLNI 509
Cdd:cd02757 332 MACHALNGLVGSIDSKG-------------------GLCPNM-------------------------------GVPKIKV 361
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 510 MrdledgkikFAWvqVNNP-WQNTANANHWIAAARemDNFIVVSDCYPGISAKVADLILPSAMIYEKWG---AYGNAERR 585
Cdd:cd02757 362 Y---------FTY--LDNPvFSNPDGMSWEEALAK--IPFHVHLSPFMSETTYFADIVLPDGHHFERWDvmsQENNLHPW 428
|
570 580 590
....*....|....*....|....*....|..
gi 218562408 586 TqHWKQQVL-PVGAAMSDTWQILEFAKRFKLK 616
Cdd:cd02757 429 L-SIRQPVVkSLGEVREETEILIELAKKLDPK 459
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
36-88 |
8.64e-16 |
|
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: 72.28 E-value: 8.64e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 218562408 36 KWDKAVCRFCGTGCGIMIARKDGKIVATKGDPAAPVNRGLNCIKGYFNAKIMY 88
Cdd:smart00926 2 KWVPTVCPLCGVGCGLLVEVKDGRVVRVRGDPDHPVNRGRLCPKGRAGLEQVY 54
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
42-607 |
1.27e-15 |
|
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: 80.90 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 42 CRFCGTGCGIMIARKDGKIVATKGDPAAPVNRGLNCIKGYFNAKIMYGEDRLVMPLLRmnekgefdKKGKFQQVSWQRAF 121
Cdd:cd02762 4 CILCEANCGLVVTVEDGRVASIRGDPDDPLSKGYICPKAAALGDYQNDPDRLRTPMRR--------RGGSFEEIDWDEAF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 122 DEMEKQFKKAYNELGVTGIGIF-GSGQYTIQEGYAALKLAKAGFRTNNidpnarHCMASAVVGFMQTFGVDEPSGCYD-- 198
Cdd:cd02762 76 DEIAERLRAIRARHGGDAVGVYgGNPQAHTHAGGAYSPALLKALGTSN------YFSAATADQKPGHFWSGLMFGHPGlh 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 199 ---DIELTDTIITWGANMAEMHPILWSrVSDRKLSNlDKVK-----VVNLSTFSNRTSNIADIEIIFKPNTDLAIWNYIA 270
Cdd:cd02762 150 pvpDIDRTDYLLILGANPLQSNGSLRT-APDRVLRL-KAAKdrggsLVVIDPRRTETAKLADEHLFVRPGTDAWLLAAML 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 271 reivynhpeamdmkfikdHCVFATGYADIGYgmrnnpnhpkfkesekdtvekenVITLDDeeatslsylgvkagdkfemk 350
Cdd:cd02762 228 ------------------AVLLAEGLTDRRF-----------------------LAEHCD-------------------- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 351 hqgvadknweiSFDEFKKGLAPYTLEYTARVAkGDDNESLEDFKKklqELANlyiekNRKVVSFWTMGFNQHTRG---SW 427
Cdd:cd02762 247 -----------GLDEVRAALAEFTPEAYAPRC-GVPAETIRRLAR---EFAA-----APSAAVYGRLGVQTQLFGtlcSW 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 428 VNEqayMVHFLLGKQAKPGsgafsltgqpsacgtarevGTFSHRLPADMVVAnPKHREISEKIWKVPAKTINPKPGSPYL 507
Cdd:cd02762 307 LVK---LLNLLTGNLDRPG-------------------GAMFTTPALDLVGQ-TSGRTIGRGEWRSRVSGLPEIAGELPV 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 508 N-----IMRDlEDGKIKFAWVQVNNPWQNTANANHWIAAAREMDnFIVVSDCYPGISAKVADLILPSAMIYEKW---GAY 579
Cdd:cd02762 364 NvlaeeILTD-GPGRIRAMIVVAGNPVLSAPDGARLEAALGGLE-FMVSVDVYMTETTRHADYILPPASQLEKPhatFFN 441
|
570 580
....*....|....*....|....*....
gi 218562408 580 GNAERRTQHWKQQVLPV-GAAMSDtWQIL 607
Cdd:cd02762 442 LEFPRNAFRYRRPLFPPpPGTLPE-WEIL 469
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
92-522 |
6.32e-14 |
|
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: 75.81 E-value: 6.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 92 RLVMPLLRmnEKGEfdkkGKFQQVSWQRAFDEMEKQFKKayneLGVTGIGIFGSGQYTIQEGYAALKLAKAgFRTNNIDP 171
Cdd:cd02767 64 RLTYPMRY--DAGS----DHYRPISWDEAFAEIAARLRA----LDPDRAAFYTSGRASNEAAYLYQLFARA-YGTNNLPD 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 172 NARHCMASAVVGFMQTFGVDEPSGCYDDIELTDTIITWGANMAEMHPilwsrvsdRKLSNLDKVK-------VVN----- 239
Cdd:cd02767 133 CSNMCHEPSSVGLKKSIGVGKGTVSLEDFEHTDLIFFIGQNPGTNHP--------RMLHYLREAKkrggkiiVINplrep 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 240 -LSTFSN---------RTSNIADIEIIFKPNTDLAIWNYIAREIVYNHPE---AMDMKFIKDHCVfatgyadigygmrnn 306
Cdd:cd02767 205 gLERFANpqnpesmltGGTKIADEYFQVRIGGDIALLNGMAKHLIERDDEpgnVLDHDFIAEHTS--------------- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 307 pNHPKFKESekdtvekenvitlddeeatslsylgvkagdkfemkhqgVADKNWEisfdefkkglapyTLEYTARVAKGDd 386
Cdd:cd02767 270 -GFEEYVAA--------------------------------------LRALSWD-------------EIERASGLSREE- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 387 nesledfkkkLQELANLYIEKNRKVVSfWTMGFNQHTRGsWVNEQAyMVHFLL--GKQAKPGSGAFSLTGQPSACGtARE 464
Cdd:cd02767 297 ----------IEAFAAMYAKSERVVFV-WGMGITQHAHG-VDNVRA-IVNLALlrGNIGRPGAGLMPIRGHSNVQG-DRT 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 218562408 465 VGtfshrlpadmVVANPKhREISEKIWKVPAKTINPKPGSPYLNIMRDLEDGKIKFAW 522
Cdd:cd02767 363 MG----------ITEKPF-PEFLDALEEVFGFTPPRDPGLDTVEAIEAALEGKVKAFI 409
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
45-662 |
1.16e-13 |
|
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: 75.05 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 45 CGTGCGIMIARKDGKIV------ATKGDPAAPVNRGlnCIKGYFNAKIMYGEDRLVMPLLRMNEKGEfdkkGKFQQVSWQ 118
Cdd:cd02770 8 CGGRCPLKAHVKDGVITrietddTGDDDPGFHQIRA--CLRGRSQRKRVYNPDRLKYPMKRVGKRGE----GKFVRISWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 119 RAFDEMEKQFKKAYNELGVTGIGI-FGSGQYtiqegYAALKLAKAGFRTNNIDPN--ARH---CMASAVVGFMQTFGVDE 192
Cdd:cd02770 82 EALDTIASELKRIIEKYGNEAIYVnYGTGTY-----GGVPAGRGAIARLLNLTGGylNYYgtySWAQITTATPYTYGAAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 193 PSGCYDDIELTDTIITWGANMAEMHPILWSRVSDRKLSNLDKVKVVNLS-TFSNRTSNIADIEIIFKPNTDLAIWNYIAR 271
Cdd:cd02770 157 SGSSLDDLKDSKLVVLFGHNPAETRMGGGGSTYYYLQAKKAGAKFIVIDpRYTDTAVTLADEWIPIRPGTDAALVAAMAY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 272 EIVYNHPeaMDMKFIKDHCVfatgyadiGYGMRNNPNHPKFKESEKDTVekenvitlddeeatslsyLGvkagdkfEMKH 351
Cdd:cd02770 237 VMITENL--HDQAFLDRYCV--------GFDAEHLPEGAPPNESYKDYV------------------LG-------TGYD 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 352 QGVADKNW--EISfdefkkGLAPYTLEYTARvakgddnesledfkkklqELANlyiEKNRKVVSFWtmGFNQHTRGswvn 429
Cdd:cd02770 282 GTPKTPEWasEIT------GVPAETIRRLAR------------------EIAT---TKPAAILQGW--GPQRHANG---- 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 430 EQA----YMVHFLLGKQAKPGSGAFSLTGQPSACGTAREVGTfshrlpadmvvaNPKHREISEKIWKVPAKTinpkpgSP 505
Cdd:cd02770 329 EQAaraiMMLAAMTGNVGIPGGNTGARPGGSAYNGAGLPAGK------------NPVKTSIPCFMWTDAIER------GE 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 506 YLNIMRDLEDGK------IKFAWVQVNNPWQNT----ANANHWIAAAREMDNFIVVSDCYPGISAKVADLILPSAMIYEK 575
Cdd:cd02770 391 EMTADDGGVKGAdklksnIKMIWNYAGNTLINQhsddNNTTRALLDDESKCEFIVVIDNFMTPSARYADILLPDTTELER 470
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 576 WG----AYGNAERRTQHWKQQVLPVGAAMSDTWQILEFAKR---------FKLKEVWKE----QKVDNKLTLPSvLEEAK 638
Cdd:cd02770 471 EDivltSNAGMMEYLIYSQKAIEPLYECKSDYEICAELAKRlgvedqfteGKTEQEWLEelygQTRAKEPGLPT-YEEFR 549
|
650 660
....*....|....*....|....*....
gi 218562408 639 AMG-----YSEDDTLFDVLFANKEAKSFN 662
Cdd:cd02770 550 EKGiyrvpRALPFVAFEDFREDPENNPLK 578
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
61-212 |
1.25e-13 |
|
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin. Arsenite oxidase is a heterodimeric enzyme containing a large and a small subunit. The large catalytic subunit harbors the molybdopterin cofactor and the [3Fe-4S] cluster; and the small subunit belongs to the structural class of the Rieske proteins. The small subunit is not included in this alignment. Members of MopB_Arsenite-Ox CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239157 [Multi-domain] Cd Length: 676 Bit Score: 74.83 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 61 VATKGDPAAPVNRGLNCIKGYFNAKIMY------GEDRLVMPLLRMNekgefdkkGKFQQVSWQRAFDEMEKQFKKAYNE 134
Cdd:cd02756 80 IVIVPDKECPVNSGNYSTRGGTNAERIWspdnrvGETRLTTPLVRRG--------GQLQPTTWDDAIDLVARVIKGILDK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 135 LGvTGIGIF------GSGQYTIQEGYAALKLAKAGFRTNNIDPNARHCMASAVVGFMQTfGVDEPSGCYDDIELTDTIIT 208
Cdd:cd02756 152 DG-NDDAVFasrfdhGGGGGGFENNWGVGKFFFMALQTPFVRIHNRPAYNSEVHATREM-GVGELNNSYEDARLADTIVL 229
|
....
gi 218562408 209 WGAN 212
Cdd:cd02756 230 WGNN 233
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
39-131 |
1.15e-12 |
|
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: 71.79 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 39 KAVCRFCGTGCGIMIARKDGKIVATKGDPAAPVNRGLNCIKGyfNAKIM--YGEDRLVMPLLRMNEKGefdkKGKFQQVS 116
Cdd:cd02763 1 TTTCYMCACRCGIRVHLRDGKVRYIKGNPDHPLNKGVICAKG--SSGIMkqYSPARLTKPLLRKGPRG----SGQFEEIE 74
|
90
....*....|....*
gi 218562408 117 WQRAFDEMEKQFKKA 131
Cdd:cd02763 75 WEEAFSIATKRLKAA 89
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
807-872 |
5.57e-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: 63.87 E-value: 5.57e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 218562408 807 EYPFWLATG-RVLEHWHSgtMTMRVPELYRAVPEALCYMSEKDGEKLGLNQGDLVWVESRRGKVKAR 872
Cdd:cd02781 1 EYPLILTTGaRSYYYFHS--EHRQLPSLRELHPDPVAEINPETAAKLGIADGDWVWVETPRGRARQK 65
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
1-575 |
6.82e-12 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 69.67 E-value: 6.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 1 MNRRDFIKNTAIAS-AASVAGLSVPSSMLGA---------QEEDWKWDKAVCRfCGTGCGIMIARKDGKIVATKGDPAAP 70
Cdd:PRK14990 14 VSRRGLVKTTAIGGlAMASSALTLPFSRIAHavdsaiptkSDEKVIWSACTVN-CGSRCPLRMHVVDGEIKYVETDNTGD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 71 VN-RGLN----CIKGYFNAKIMYGEDRLVMPLLRMNEKGEfdkkGKFQQVSWQRAFDEMEKQFKKAYNELGVTGIGI-FG 144
Cdd:PRK14990 93 DNyDGLHqvraCLRGRSMRRRVYNPDRLKYPMKRVGARGE----GKFERISWEEAYDIIATNMQRLIKEYGNESIYLnYG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 145 SGQY--TIQEGYAALKLAKAgfRTNN-----IDPNARHCMASAVVGFMQTFGVDEPSGCYDDIELTDTIITWGANMAEMH 217
Cdd:PRK14990 169 TGTLggTMTRSWPPGNTLVA--RLMNccggyLNHYGDYSSAQIAEGLNYTYGGWADGNSPSDIENSKLVVLFGNNPGETR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 218 ----PILWSRVSDRKLSNLdKVKVVNlSTFSNRTSNIADIEIIFKPNTDLAIWNYIAREIVYNHpeAMDMKFIKDHCVfa 293
Cdd:PRK14990 247 msggGVTYYLEQARQKSNA-RMIIID-PRYTDTGAGREDEWIPIRPGTDAALVNGLAYVMITEN--LVDQPFLDKYCV-- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 294 tgyadiGYGMRNNPNHPKFKESEKdtvekenvitlddeeatslSYLGVKAGDkfemkhqGVADknweisfdefkkglapy 373
Cdd:PRK14990 321 ------GYDEKTLPASAPKNGHYK-------------------AYILGEGPD-------GVAK----------------- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 374 TLEYTARVAkGDDNESLEDFKKKLQELANLYIEKNrkvvsfWtmGFNQHTRGSWVNEQAYMVHFLlgkqakpgSGAFSLT 453
Cdd:PRK14990 352 TPEWASQIT-GVPADKIIKLAREIGSTKPAFISQG------W--GPQRHANGEIATRAISMLAIL--------TGNVGIN 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 454 GQPSAcgtAREvGTFS---HRLPadmVVANPKHREISEKIWKVPAKTinpkpgSPYLNIMRDLEDGK------IKFAWVQ 524
Cdd:PRK14990 415 GGNSG---ARE-GSYSlpfVRMP---TLENPIQTSISMFMWTDAIER------GPEMTALRDGVRGKdkldvpIKMIWNY 481
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 218562408 525 VNNPWQNT---ANANHWIAAAREMDNFIVVSDCYPGISAKVADLILPSAMIYEK 575
Cdd:PRK14990 482 AGNCLINQhseINRTHEILQDDKKCELIVVIDCHMTSSAKYADILLPDCTASEQ 535
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
41-246 |
9.65e-12 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 68.82 E-value: 9.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 41 VCRFCGTGCGIMIARKDGKI---VATKgDPAapVNRGLNCIKGYFNAKIMYGEDRLVMPLLRmnekgefDKKGKFQQVSW 117
Cdd:PRK07860 227 VCEHCASGCAQRTDHRRGKVlrrLAGD-DPE--VNEEWNCDKGRWAFTYATQPDRITTPLVR-------DEDGELEPASW 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 118 QRAFDEMEKQFKKAYNELGV-TGigifgsGQYTIQEGYAALKLAKAGFRTNNIDPNAR-------HCMASAVVGfmQTFG 189
Cdd:PRK07860 297 SEALAVAARGLAAARGRVGVlVG------GRLTVEDAYAYAKFARVALGTNDIDFRARphsaeeaDFLAARVAG--RGLG 368
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 218562408 190 VDepsgcYDDIELTDTIITWGANMAEMHPILWSRVsdRKLSNLDKVKVVNLSTFSNR 246
Cdd:PRK07860 369 VT-----YADLEKAPAVLLVGFEPEEESPIVFLRL--RKAARKHGLKVYSIAPFATR 418
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
45-274 |
3.05e-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: 63.49 E-value: 3.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 45 CGTGCGIMIARKDGkIVATKGD----PAAPVN------RGlnCIKGYFNAKIMYGEDRLVMPLLRMNEKGEfdkkGKFQQ 114
Cdd:cd02750 12 CTGSCSWNVYVKNG-IVTREEQatdyPETPPDlpdynpRG--CQRGASFSWYLYSPDRVKYPLKRVGARGE----GKWKR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 115 VSWQRAFDEMEKQFK---KAYNELGVTGI-GIFGSGQYTIQEGYAALKLAkAGFRTNNIDPNARHCMASAvvgfmQTFGV 190
Cdd:cd02750 85 ISWDEALELIADAIIdtiKKYGPDRVIGFsPIPAMSMVSYAAGSRFASLI-GGVSLSFYDWYGDLPPGSP-----QTWGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 191 --DEPSgcYDDIELTDTIITWGANmaemhpILWSRVSDRKL---SNLDKVKVVNLSTFSNRTSNIADIEIIFKPNTDLAI 265
Cdd:cd02750 159 qtDVPE--SADWYNADYIIMWGSN------VPVTRTPDAHFlteARYNGAKVVVVSPDYSPSAKHADLWVPIKPGTDAAL 230
|
....*....
gi 218562408 266 WNYIAREIV 274
Cdd:cd02750 231 ALAMAHVII 239
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
39-264 |
5.39e-10 |
|
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: 62.30 E-value: 5.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 39 KAVCRFCGTGCGIMIARKDGKIVATKGDPAAPVNRGLNCIKGYFNAKIMYGEDRLVMPLLRMNekgefdkkGKFQQVSWQ 118
Cdd:cd02768 1 ESIDVHDALGSNIRVDVRGGEVMRILPRENEAINEEWISDKGRFGYDGLNSRQRLTQPLIKKG--------GKLVPVSWE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 119 RAFDEMEKQFKKAYNElgvtGIGIFGSGQYTIQEGYAALKLAKaGFRTNNIDPNARHCMASAVVGFMQTFGvdePSGCYD 198
Cdd:cd02768 73 EALKTVAEGLKAVKGD----KIGGIAGPRADLESLFLLKKLLN-KLGSNNIDHRLRQSDLPADNRLRGNYL---FNTSIA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 218562408 199 DIELTDTIITWGANMAEMHPILWSRVsdRKLSNLDKVKVVNLSTFSnrTSNIADIEIIFKPNTDLA 264
Cdd:cd02768 145 EIEEADAVLLIGSNLRKEAPLLNARL--RKAVKKKGAKIAVIGPKD--TDLIADLTYPVSPLGASL 206
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
50-665 |
6.22e-09 |
|
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: 59.58 E-value: 6.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 50 GIMIAR-KDGKIVATKGDPAAPVNRGLncIKGYFNAkiMYGEDRLVMPLLRMN--EKGEFDK-----KGKFQQVSWQRAF 121
Cdd:cd02769 7 GAFRARvKDGRIVGVRPFEEDPDPSPL--LDGVPDA--VYSPTRIKYPMVRRGwlEKGPGSDrslrgKEEFVRVSWDEAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 122 DEMEKQFKKAYNELGVTGIgiFGsGQYtiqeGY--------AALKLAKA-----GF--RTNNIDPNARHCMASAVVGFMQ 186
Cdd:cd02769 83 DLVAAELKRVRKTYGNEAI--FG-GSY----GWssagrfhhAQSLLHRFlnlagGYvgSVGDYSTGAAQVILPHVVGSME 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 187 TFGVDEPSgcYDDI-ELTDTIITWGANMAEMHPILWSRVSD-------RKLSNlDKVKVVNLSTFSNRTSNIADIE-IIF 257
Cdd:cd02769 156 VYTEQQTS--WPVIaEHTELVVAFGADPLKNAQIAWGGIPDhqaysylKALKD-RGIRFISISPLRDDTAAELGAEwIAI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 258 KPNTDLAIWNYIAREIVYNhpEAMDMKFIKDHCVfatgyadiGYgmrnnpnhPKFKE---SEKDTVEKenvitlDDEEAT 334
Cdd:cd02769 233 RPGTDVALMLALAHTLVTE--GLHDKAFLARYTV--------GF--------DKFLPyllGESDGVPK------TPEWAA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 335 SLSylGVKAGdkfemkhqgvadknweisfdefkkglapytleytarvakgddnesledfkkKLQELANLYIEKNRKVVSF 414
Cdd:cd02769 289 AIC--GIPAE---------------------------------------------------TIRELARRFASKRTMIMAG 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 415 WTMGFNQHtrgswvNEQAY-MVHFL---LGKQAKPGSGaFSLTGQPSACGTAREVGTFSHRLPADmvvANPkhreISEKI 490
Cdd:cd02769 316 WSLQRAHH------GEQPHwMAVTLaamLGQIGLPGGG-FGFGYHYSNGGGPPRGAAPPPALPQG---RNP----VSSFI 381
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 491 wkvPAKTINP---KPGSPYLNIMRDLEDGKIKFAWVQVNNPWQNTANANHWIAAAREMDNFIVvSDCYPGISAKVADLIL 567
Cdd:cd02769 382 ---PVARIADmllNPGKPFDYNGKKLTYPDIKLVYWAGGNPFHHHQDLNRLIRAWQKPETVIV-HEPFWTATARHADIVL 457
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 568 PSAMIYEK--WGAYGNaERRTQHWKQQVLPVGAAMSDtWQIL-EFAKRFKLKEVWKEQKvDNKLTLPSVLEEAKAMGYSE 644
Cdd:cd02769 458 PATTSLERndIGGSGD-NRYIVAMKQVVEPVGEARDD-YDIFaDLAERLGVEEQFTEGR-DEMEWLRHLYEESRAQAAAR 534
|
650 660
....*....|....*....|...
gi 218562408 645 DDTL--FDVLFANKEAKSFNPND 665
Cdd:cd02769 535 GVEMpsFDEFWAQGYVELPIPEA 557
|
|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
808-923 |
9.44e-09 |
|
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: 54.00 E-value: 9.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 808 YPFWLATGRVLEHWHSGTMTMRVPELYRAVPEALCYMSEKDGEKLGLNQGDLVWVESRRGKVKARVDMRGRNKPpvGLVY 887
Cdd:cd02779 1 YKYWVNNGRANIIWQTAYHDQNNSEIAERVPLPYIEVNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKP--GQTF 78
|
90 100 110
....*....|....*....|....*....|....*.
gi 218562408 888 VPWFDENVYINKVTLDATCPLSKQTDFKKCAVKIYK 923
Cdd:cd02779 79 MLMAHPRPGANGLVTPYVDPETIIPYYKGTWANIRK 114
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
87-224 |
2.91e-08 |
|
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: 56.98 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 87 MYGEDRLVMPLLRmnekgefdKKGKFQQVSWQRAFDEMEKQFKKAYNELGVTGIGIFGSGQYTIQEGYAALKLAkAGFRT 166
Cdd:cd02772 49 LNSEDRLTKPMIK--------KDGQWQEVDWETALEYVAEGLSAIIKKHGADQIGALASPHSTLEELYLLQKLA-RGLGS 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 218562408 167 NNIDPNARHCMASAVVgfmqTFGVDEPSGC-YDDIELTDTIITWGANMAEMHPILWSRV 224
Cdd:cd02772 120 DNIDHRLRQSDFRDDA----KASGAPWLGMpIAEISELDRVLVIGSNLRKEHPLLAQRL 174
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
809-873 |
7.08e-08 |
|
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: 51.89 E-value: 7.08e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 218562408 809 PFWLATGRVLehWHSGTMTMRVPELYRAVPEALCYMSEKDGEKLGLNQGDLVWVESRRGKVKARV 873
Cdd:cd02778 1 EFRLIYGKSP--VHTHGHTANNPLLHELTPENTLWINPETAARLGIKDGDRVEVSSARGKVTGKA 63
|
|
| FwdB |
COG1029 |
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion]; |
37-265 |
1.38e-07 |
|
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion];
Pssm-ID: 440652 [Multi-domain] Cd Length: 428 Bit Score: 54.85 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 37 WDKAVCRFCGTGCG-IMIARKDGKIVATKGDpaapvnrglnCIKGyfNAKIMY--GEDRLVMPLLRmnekgefdkkgkFQ 113
Cdd:COG1029 5 VKNVVCPFCGCLCDdLEVEVEGGKIVVVKNA----------CAIG--AAKFERavSDHRITSPRIR------------GK 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 114 QVSWQRAFDEMEKQFKKAYNELgvtgigIFGSGQYTIQEGYAALKLA-KAGfrtNNIDPNARHCMASAVVGfMQTFGVde 192
Cdd:COG1029 61 EVSLEEAIDKAAEILANAKRPL------IYGLSSTDCEAMRAGLALAeRVG---AVVDNTASVCHGPSLLA-LQDVGW-- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 193 pSGCyddiELT------DTIITWGANMAEMHPILWSRVS-------------DRKLSNLDKVKvvnlstfsNRTSNIADI 253
Cdd:COG1029 129 -PTC----TLGevknraDVIIYWGCNPVHAHPRHMSRYSvfprgfftpkgrkDRTVIVVDPRP--------TDTAKVADL 195
|
250
....*....|..
gi 218562408 254 EIIFKPNTDLAI 265
Cdd:COG1029 196 HLQVKPGRDYEV 207
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
42-130 |
4.40e-07 |
|
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: 53.82 E-value: 4.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 42 CRFCGTGCGIMIAR-KDGKIVATKGDPAAP---VNRGLNCIKGYFNAKIMYGEDRLVMPLLRMNEKGEFDKKGKFQQVSW 117
Cdd:cd02760 4 CYNCVAGPDFMAVKvVDGVATEIEPNFAAEdihPARGRVCVKAYGLVQKTYNPNRVLQPMKRTNPKKGRNEDPGFVPISW 83
|
90
....*....|...
gi 218562408 118 QRAFDEMEKQFKK 130
Cdd:cd02760 84 DEALDLVAAKLRR 96
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
1-291 |
1.95e-06 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 51.98 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 1 MNRRDFIKNTAIASAASVAGLSV--PSSMLGAQ------EEDWKWdkavcrfcgTGC---GIMIARKDGKIVATKgdpaa 69
Cdd:PRK15102 1 ASRRRFLKGLGGLSAAGMLGPSLltPRSALAAQaaaaetTKEWIL---------TGShwgAFRAKVKNGRFVEAK----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 70 PVNRG------LNCIKGyfnakIMYGEDRLVMPLLRMN-----EKGEFDKKG--KFQQVSWQRAFDEMekqfkkaYNELG 136
Cdd:PRK15102 67 PFELDkyptkmINGIKG-----HVYNPSRIRYPMVRLDwlrkrHKSDTSQRGdnRFVRVSWDEALDLF-------YEELE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 137 vtgigifgsgqyTIQEGYA--ALKLAKAGFRTNNIDPNARHCMASAVV---GFMQTFGvDEPSGCYDDI----------- 200
Cdd:PRK15102 135 ------------RVQKTYGpsALHTGQTGWQSTGQFHSATGHMQRAIGmhgNSVGTVG-DYSTGAGQVIlpyvlgstevy 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 201 ----------ELTDTIITWGANM---------AEMH------PILWSRVSDRklsnldKVKVVNLSTFSNRTSNIADIEI 255
Cdd:PRK15102 202 eqgtswplilENSKTIVLWGSDPvknlqvgwnCETHesyaylAQLKEKVAKG------EINVISIDPVVTKTQNYLGCEH 275
|
330 340 350
....*....|....*....|....*....|....*..
gi 218562408 256 IF-KPNTDLAIWNYIAREIVYNhpEAMDMKFIKDHCV 291
Cdd:PRK15102 276 LYvNPQTDVPLMLALAHTLYSE--NLYDKKFIDNYCL 310
|
|
| FwdD |
COG1153 |
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion]; |
840-924 |
1.97e-05 |
|
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion];
Pssm-ID: 440767 [Multi-domain] Cd Length: 127 Bit Score: 44.84 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 840 ALCYMSEKDGEKLGLNQGDLVWVESRRGKV--KARVDmrgrNKPPVGLVYVPwfdENVYINKVTLDATC----PlskqtD 913
Cdd:COG1153 31 AVCELNPEDMKKLGIKEGDKVKVTSEYGEVvvKAKES----EDLHPGLVFIP---MGPWANAVVPPETHstgmP-----D 98
|
90
....*....|.
gi 218562408 914 FKKCAVKIYKA 924
Cdd:COG1153 99 FKGVPVEVEPT 109
|
|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
41-262 |
5.78e-05 |
|
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, subunit B (FmdB/FwdB), 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 (MopB) superfamily of proteins.
Pssm-ID: 239162 [Multi-domain] Cd Length: 415 Bit Score: 46.56 E-value: 5.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 41 VCRFCGTGCG-IMIARKDGKIVATKgdPAapvnrglnCIKGyfNAKIMYGEDRLVMPLLRmnekgefdkkgkFQQVSWQR 119
Cdd:cd02761 3 VCPFCGLLCDdIEVEVEDNKITKVR--NA--------CRIG--AAKFARYERRITTPRID------------GKPVSLEE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 120 AFDEMEKQFKKAYNELgvtgigIFGSGQyTIQEGY-AALKLAKAgfrTNN-IDPNARHCMASAVVGfMQTFGVdePSGCY 197
Cdd:cd02761 59 AIEKAAEILKEAKRPL------FYGLGT-TVCEAQrAGIELAEK---LGAiIDHAASVCHGPNLLA-LQDSGW--PTTTL 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 218562408 198 DDIE-LTDTIITWGANMAEMHPILWSRVS-------------DRKLSNLDKVKvvnlstfsNRTSNIADIEIIFKPNTD 262
Cdd:cd02761 126 GEVKnRADVIVYWGTNPMHAHPRHMSRYSvfprgffreggreDRTLIVVDPRK--------SDTAKLADIHLQIDPGSD 196
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
546-607 |
9.31e-05 |
|
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone oxidoreductase/respiratory complex I/NADH dehydrogenase-1(NDH-1) of eukaryotes and the Nqo3/G subunit of alphaproteobacteria NDH-1. The NADH-quinone oxidoreductase is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The nad11 gene codes for the largest (75 kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Paracoccus denitrificans, this subunit is encoded by the nqo3 gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The Nad11/Nqo3 subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239174 [Multi-domain] Cd Length: 375 Bit Score: 45.72 E-value: 9.31e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 218562408 546 DNFIVvsdcYPG----ISAKVADLILPSAMIYEKWGAYGNAERRTQHWKQQVLPVGAAMSDtWQIL 607
Cdd:cd02773 308 DAFVV----YQGhhgdRGAQIADVILPGAAYTEKSGTYVNTEGRVQQTRKAVSPPGDARED-WKIL 368
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
3-274 |
1.67e-04 |
|
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: 45.17 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 3 RRDFIKNTAIASAASVAG-------LSVPSSMLGAQEEDWKWDKAVCRFC--GTGCGIMIARKDGKIVATKGDPAAPVNR 73
Cdd:cd02764 1 RRGFLKLMGASLAMASAAacrypveKIVPYVIWPENIVPGETVYYATSLVpaGEGQGVLVKTVDGRPIKIEGNPDHPASL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 74 GlnCIKGYFNAKI--MYGEDRLVMPLlrmneKGEFDkkGKFQQVSWQrAFDEMEKQFKKAYNELGVTGIGIFGSGQYTIQ 151
Cdd:cd02764 81 G--GTSARAQASVlsLYDPDRAQGPL-----RRGID--GAYVASDWA-DFDAKVAEQLKAVKDGGKLAVLSGNVNSPTTE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 152 EGYAALKLAKAGFRTNNIDPNARHCMASAvvgfMQT-FGVDEPSGcYDdIELTDTIITWGANMAE--MHPILWSR--VSD 226
Cdd:cd02764 151 ALIGDFLKKYPGAKHVVYDPLSAEDVNEA----WQAsFGKDVVPG-YD-FDKAEVIVSIDADFLGswISAIRHRHdfAAK 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 218562408 227 RKLS-NLDKVKVVNLSTFSNRTSNIADIEIIFKPNTDLAIWNYIAREIV 274
Cdd:cd02764 225 RRLGaEEPMSRLVAAESVYTLTGANADVRLAIRPSQEKAFALGLAHKLI 273
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
808-923 |
3.52e-04 |
|
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: 41.12 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 808 YPFWLATGRVLEHWHSGTMTmrVPELYRAVPEAlCYMSEKDGEKLGLNQGDLVWVESRRGKVKARVDMRGRNKPpvGLVY 887
Cdd:cd02794 1 YPLQLIGWHYKRRTHSTFDN--VPWLREAFPQE-VWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMP--GVVA 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 218562408 888 VP---WF-------DENVYINKVTLDATCPLSKQTDFKKCAVKIYK 923
Cdd:cd02794 76 LPqgaWYepdangiDKGGCINTLTGLRPSPLAKGNPQHTNLVQVEK 121
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
808-873 |
8.95e-04 |
|
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: 40.35 E-value: 8.95e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 218562408 808 YPFWLATGRVLEHWHSgtmTMRVPELYRAVPEALCYMSEKDGEKLGLNQGDLVWVESRRGKVKARV 873
Cdd:cd02780 1 YPFILVTFKSNLNSHR---SANAPWLKEIKPENPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKA 63
|
|
| MopB_CT_ydeP |
cd02787 |
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial ... |
834-921 |
3.17e-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: 38.41 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 834 YRAVP---EALcYMSEKDGEKLGLNQGDLVWVESRRGKVKARVDMRGRNKP---PVGLVYVPWFDENVYInkvTLDATCP 907
Cdd:cd02787 23 YRGVFgrrDVV-FMNPDDIARLGLKAGDRVDLESAFGDGQGRIVRGFRVVEydiPRGCLAAYYPEGNVLV---PLDHRDP 98
|
90
....*....|....
gi 218562408 908 LSKQTDFKKCAVKI 921
Cdd:cd02787 99 QSKTPAYKSVPVRL 112
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
807-889 |
3.33e-03 |
|
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: 38.53 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 807 EYPFWLATGRvlEHWHSG-TMTMRVPELYRAVPEALCYMSEKDGEKLGLNQGDLVWVESRRGKVKARVDMRGRNKPpvGL 885
Cdd:cd02782 1 DYPFLLLIGR--RHLRSNnSWLHNDPRLVKGRNRCTLRIHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMP--GV 76
|
....
gi 218562408 886 VYVP 889
Cdd:cd02782 77 VSLP 80
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
808-892 |
5.56e-03 |
|
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: 37.95 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562408 808 YPFWLAT----GRVlehwHSgtmTM-RVPELYRAVPEAL---CYMSEKDGEKLGLNQGDLVWVESRRGKVKARVDMRGRN 879
Cdd:cd02777 1 YPLQLISphpkRRL----HS---QLdNVPWLREAYKVKGrepVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRI 73
|
90
....*....|....*.
gi 218562408 880 KPpvGLVYVP---WFD 892
Cdd:cd02777 74 MP--GVVALPegaWYD 87
|
|
| MopB_CT_FmdC-FwdD |
cd02789 |
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran ... |
840-910 |
5.76e-03 |
|
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: 37.41 E-value: 5.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 218562408 840 ALCYMSEKDGEKLGLNQGDLVWVESRRGKVKARVDMRGRNkpPVGLVYVP---WfdENVYINKVTLDATCPLSK 910
Cdd:cd02789 31 AYCEINPEDYKLLGKPEGDKVKVTSEFGEVVVFAKENEGV--PEGMVFIPmgpW--ANVVVDPYTDSTGSPIFK 100
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
807-872 |
7.43e-03 |
|
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: 37.35 E-value: 7.43e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 218562408 807 EYPFWLATGRVLEHWHSgtMTMRVPELYRAVPEALCYMSEKDGEKLGLNQGDLVWVESRRGKVKAR 872
Cdd:cd02785 1 KYPLACIQRHSRFRVHS--QFSNVPWLLELQPEPRVKINPIDAAARGIAHGDLVEVYNDRGSVVCK 64
|
|
| FcbT1 |
COG4663 |
TRAP-type mannitol/chloroaromatic compound transport system, periplasmic component [Secondary ... |
1-36 |
7.85e-03 |
|
TRAP-type mannitol/chloroaromatic compound transport system, periplasmic component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443700 [Multi-domain] Cd Length: 356 Bit Score: 39.72 E-value: 7.85e-03
10 20 30
....*....|....*....|....*....|....*.
gi 218562408 1 MNRRDFIKNTAIASAASVAGLSVPSSMLGAQEEDWK 36
Cdd:COG4663 1 MKRRSFLKGAALGAAAAAAALAAPAIAQAQPTIRWR 36
|
|
| |
