|
Name |
Accession |
Description |
Interval |
E-value |
| NuoG |
TIGR01973 |
NADH-quinone oxidoreductase, chain G; This model represents the G subunit (one of 14: A->N) of ... |
4-651 |
0e+00 |
|
NADH-quinone oxidoreductase, chain G; This model represents the G subunit (one of 14: A->N) of the NADH-quinone oxidoreductase complex I which generally couples NADH and ubiquinone oxidation/reduction in bacteria and mammalian mitochondria while translocating protons, but may act on NADPH and/or plastoquinone in cyanobacteria and plant chloroplasts. This model excludes related subunits from formate dehydrogenase complexes. [Energy metabolism, Electron transport]
Pssm-ID: 273904 [Multi-domain] Cd Length: 602 Bit Score: 807.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 4 IHVDGKELEVDGADNLLQACLSLGLDIPYFCWHPALGSVGACRQCAVKQYTDEndtrgRIVMSCMTPATDGSWISIEDEE 83
Cdd:TIGR01973 1 IFIDGKELEVPKGTTVLQACLSAGIEIPRFCYHEKLSIAGNCRMCLVEVEKFP-----KPVASCATPVTDGMKISTNSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 84 AKVFRASVVEWLMTNHPHDCPVCEEGGHCHLQDMTVMTGHNERRYRFTKRTHQNQQLGPFISHEMNRCIACYRCVRFYKD 163
Cdd:TIGR01973 76 VKKAREGVMEFLLINHPLDCPICDQGGECDLQDQAVMYGSDRSRFREKKRTVENKYLGPLIKTEMTRCIHCTRCVRFANE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 164 YAGGTDLGVFGAHDNVYFGRVEDGTLESEFSGNLTEVCPTGVFTDKTHSERYnRKWDMQFSPSICHGCSSGCNISPGERY 243
Cdd:TIGR01973 156 VAGVEDLGVIGRGNNVEIGTYEGKTLESELSGNLIDICPVGALTSKPYAFKA-RPWELKSTPSICVHDSVGCNIRVDERN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 244 GELRRIENRFNGSVNQYFLCDRGRFGYGYVNREDRPRQPLLADG----AKLSLDEALDKAAD-LLRGRNIVGIGSPRASL 318
Cdd:TIGR01973 235 GEIMRILPRENDEINEEWLCDKGRFGYDGLNRQDRLTKPLLRNQegnlLEVSWAEALAIAAEkLKASSRIGGIAGPRSSL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 319 ESNYALRELV---GAEHFYSGIEAGELERIRLVLQVLNDSPLpvpnmRDIEDHDAIFVLGEDLTQTAARVALSLRQSVKG 395
Cdd:TIGR01973 315 EELFALKKLVrklGSENFDLRIRNYEFESADLRANYLFNTTL-----ADIEEADLVLLVGADLRQEAPLLNLRLRKAVKK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 396 KAeDMADAMRVQPWLDAAVKNIgqhalNPLFIASLTATKLDDIAeecVHAAPDdlarigfavahaldasapavegldaea 475
Cdd:TIGR01973 390 GG-AKVALIGIEKWNLTYPANT-----NLVFHPGLSPKKLDDIA---SGAHSD--------------------------- 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 476 aelakrIADALLAAKRPLIIAG----TSLGSKALIEAAANIAKALKLREKN-GSISLIVPEANSLGLAMLGGES--LDAA 548
Cdd:TIGR01973 434 ------IAAALKAAKKPLIIVGdsaiSHLDGAALISAAANIAKVIKVRRKEwNGLNILSSGANSVGLLDLGGEStgLDAA 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 549 LQavtDGSADAIVVLENDLYTRTDSAKVDAALNAAKVVIVADHQKTATSDRAHLVLPAASFAEGDGTLVSQEGRAQRFFQ 628
Cdd:TIGR01973 508 LN---LGAADALFLLGADLERALDKTARDALSKADAFIIYQGHHGTETAEKADVILPGAAFTEKSGTYVNLEGRAQRFEQ 584
|
650 660
....*....|....*....|...
gi 1330194573 629 VFDPKYmdasiLVHEGWRWLHAL 651
Cdd:TIGR01973 585 AVKPPG-----EAREDWRILRAL 602
|
|
| 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 ... |
225-669 |
0e+00 |
|
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: 563.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 225 PSICHGCSSGCNISPGERYGELRRIENRFNGSVNQYFLCDRGRFGYGYVNREDRPRQPLLADGA---KLSLDEALDKAAD 301
Cdd:cd02771 1 PSICHHCSVGCNISLGERYGELRRVENRYNGAVNHYFLCDRGRFGYGYVNSRDRLTQPLIRRGGtlvPVSWNEALDVAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 302 LLRGRN--IVGIGSPRASLESNYALRELVGAehfYSGIEAGELERIRLVLQVLNDSPLPVPNMRDIEDHDAIFVLGEDLT 379
Cdd:cd02771 81 RLKEAKdkVGGIGSPRASNESNYALQKLVGA---VLGTNNVDHRARRLIAEILRNGPIYIPSLRDIESADAVLVLGEDLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 380 QTAARVALSLRQSVKGKAEDMADAMRVQPWLDAAVKNIGQHALNPLFIASLTATKLDDIAEECVHAAPDDLARIGFAVAH 459
Cdd:cd02771 158 QTAPRIALALRQAARRKAVELAALSGIPKWQDAAVRNIAQGAKSPLFIVNALATRLDDIAAESIRASPGGQARLGAALAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 460 ALDASAPAVEGLDAEaaELAKRIADALLAAKRPLIIAGTSLGSKALIEAAANIAKALKLREKNGSISLIVPEANSLGLAM 539
Cdd:cd02771 238 AVDASAAGVSGLAPK--EKAARIAARLTGAKKPLIVSGTLSGSLELIKAAANLAKALKRRGENAGLTLAVEEGNSPGLLL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 540 LGGE------SLDAALQAVTDGSADAIVVLENDLYTRTDSAKVDAALNAAKVVIVADHQKTATSDRAHLVLPAASFAEGD 613
Cdd:cd02771 316 LGGHvtepglDLDGALAALEDGSADALIVLGNDLYRSAPERRVEAALDAAEFVVVLDHFLTETAERADVVLPAASFAEKS 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1330194573 614 GTLVSQEGRAQRFFQVFDPKYMDAsilvHEGWRWLHALRATLLNQ--PIDWTQLDHVT 669
Cdd:cd02771 396 GTFVNYEGRAQRFFKAYDDPAGDA----RSDWRWLHALAAKLGGKlvPSDAAILDEII 449
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
1-678 |
0e+00 |
|
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440657 [Multi-domain] Cd Length: 453 Bit Score: 541.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 1 MATIHVDGKELEVDGADNLLQACLSLGLDIPYFCWHPALGSVGACRQCAVKQytdenDTRGRIVMSCMTPATDGSWISIE 80
Cdd:COG1034 1 MVTITIDGKEVEVPKGTTVLQAAEKAGIEIPRFCYHPKLSIAGACRMCLVEV-----EGAPKPVASCATPVTDGMVVKTD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 81 DEEAKVFRASVVEWLMTNHPHDCPVCEEGGHCHLQDMTVMTGHNERRYRFTKRTHQNQQLGPFISHEMNRCIACYRCVRF 160
Cdd:COG1034 76 SPKVKKARKGVMEFLLINHPLDCPICDQGGECDLQDQAMEYGVDESRYEEEKRTVPKKDLGPLILLDMNRCILCTRCVRF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 161 YKDYAGGTDLGVFGAHDNVYFGRVEDGTLESEFSGNLTEVCPTGVFTDKTHSErYNRKWDMQFSPSICHGCSSGCNISPG 240
Cdd:COG1034 156 CDEIAGDPELGVIGRGEHSEIGTYLGKPLDSEFSGNCIDVCPVGALTSKPFRF-KARPWELKKTPSICPHCSVGCNIRVD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 241 ERYGELRRIENRFNGSVNQYFLCDRGRFGYGYVNREDRPRQPLLADGAKL---SLDEALDKAADllrgrnivgigspras 317
Cdd:COG1034 235 VRGGKVYRVLPRENEAVNEEWLCDKGRFGYDGLNSPDRLTRPLVRKDGELveaSWEEALAAAAE---------------- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 318 lesnyALRELVGAEHFYSGIEAGELERIRLVLQVLNDSPLpvpnmrdiedhDAIFVLGEDLtqtaarvalslrqsvkgka 397
Cdd:COG1034 299 -----GLKALKKAENSVGAALLGALPDAAAILEAAEAGKL-----------KALVLLGADP------------------- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 398 edmadamrvqpwldaavknigqhalnplfiasltatklddiaeecvhaapddlarigfavahaldasapavEGLDAEAAe 477
Cdd:COG1034 344 -----------------------------------------------------------------------YDLDPAAA- 351
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 478 lakriadallaakrpliiagtslgskalieaaaniakalklrekngsislivpeanslglamlggesldaalqavtdgsa 557
Cdd:COG1034 --------------------------------------------------------------------------------
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 558 daivvlendlytrtdsakvDAALNAAKVVIVADHQKTATSDRAHLVLPAASFAEGDGTLVSQEGRAQRFFQVFDPKYMda 637
Cdd:COG1034 352 -------------------LAALAKADFVVVLDHFGSATAERADVVLPAAAFAEKSGTFVNLEGRVQRFNAAVPPPGE-- 410
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1330194573 638 silVHEGWRWLHALrATLLNQPIDWTQLDHVTAAAAAAAPQ 678
Cdd:COG1034 411 ---ARPDWRVLRAL-ANALGAGLPYDSLEEVRAELAAEAPA 447
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
1-631 |
1.05e-55 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 206.72 E-value: 1.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 1 MATIHVDGKELEVDGADNLLQACLSLGLDIPYFCWHPALGSVGACRQCAVkqytdenDTRG--RIVMSCMTPATDGSWIS 78
Cdd:PRK07860 4 LVTLTIDGVEVSVPKGTLVIRAAELLGIQIPRFCDHPLLDPVGACRQCLV-------EVEGqrKPQASCTTTVTDGMVVK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 79 IED--EEAKVFRASVVEWLMTNHPHDCPVCEEGGHCHLQDMTVMTGHNERRYRFTKRTHQNqqlgPF-ISHEM----NRC 151
Cdd:PRK07860 77 TQLtsPVADKAQHGVMELLLINHPLDCPVCDKGGECPLQNQAMSNGRAESRFTDVKRTFPK----PInISTQVlldrERC 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 152 IACYRCVRFYKDYAGG--TDLGVFGAHDNVyfGRVEDGTLESEFSGNLTEVCPTGVFTDKTHSERyNRKWDMQFSPSICH 229
Cdd:PRK07860 153 VLCARCTRFSDQIAGDpfIDLQERGALQQV--GIYEGEPFQSYFSGNTVQICPVGALTGAAYRFR-ARPFDLVSTPSVCE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 230 GCSSGCNISPGERYGELRRienRFNGS---VNQYFLCDRGRFGYGYVNREDRPRQPLL--ADGA--KLSLDEALDKAADL 302
Cdd:PRK07860 230 HCASGCAQRTDHRRGKVLR---RLAGDdpeVNEEWNCDKGRWAFTYATQPDRITTPLVrdEDGElePASWSEALAVAARG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 303 L---RGRNIVGIGSpRASLESNYAlrelvgaehfYSGIEageleriRLVLQVlNDSplpvpnmrdieDHDAIFVLGEDLT 379
Cdd:PRK07860 307 LaaaRGRVGVLVGG-RLTVEDAYA----------YAKFA-------RVALGT-NDI-----------DFRARPHSAEEAD 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 380 QTAARVALslrqsvKGKAEDMAD---AMRV-----QPWLDAAV------KNIGQHALNPLFIASLTATKLDDIAEECVHA 445
Cdd:PRK07860 357 FLAARVAG------RGLGVTYADlekAPAVllvgfEPEEESPIvflrlrKAARKHGLKVYSIAPFATRGLEKMGGTLLRT 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 446 AP-------DDLARIGFAVAHALDAS---------APAVEGLDAEAAELAKRIADALL-----AAKRPLIIAGT--SL-- 500
Cdd:PRK07860 431 APggeaaalDALATGAPDVAELLRTPgavilvgerLATVPGALSAAARLADATGARLAwvprrAGERGALEAGAlpTLlp 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 501 GSKALIEAAANIAkalkLREKNGSISLivPEANslglamlgGESLDAALQAVTDGSADAIVVLENDLYTRTDSAKVDAAL 580
Cdd:PRK07860 511 GGRPVADPAARAE----VAAAWGVDEL--PAAP--------GRDTAGILAAAAAGELGALLVGGVEPADLPDPAAALAAL 576
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1330194573 581 NAAKVVIVADHQKTATSDRAHLVLPAASFAEGDGTLVSQEGRAQRFFQVFD 631
Cdd:PRK07860 577 DAAGFVVSLELRHSAVTERADVVLPVAPVAEKAGTFLNWEGRLRPFEAALR 627
|
|
| MopB_CT_NDH-1_NuoG2-N7 |
cd02788 |
MopB_CT_NDH-1_NuoG2-N7: C-terminal region of the NuoG-like subunit (of the variant with a ... |
806-901 |
9.95e-25 |
|
MopB_CT_NDH-1_NuoG2-N7: C-terminal region of the NuoG-like subunit (of the variant with a [4Fe-4S] cluster, N7) of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1) found in various bacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain, is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Unique to this group, compared to the other prokaryotic and eukaryotic groups in this domain protein family (NADH-Q-OR-NuoG2), is an N-terminal [4Fe-4S] cluster (N7/N1c) present in the second domain and a C-terminal region (this CD) homologous to the formate dehydrogenase C-terminal molybdopterin_binding (MopB) region.
Pssm-ID: 239189 [Multi-domain] Cd Length: 96 Bit Score: 98.92 E-value: 9.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 806 WQVVPFFHLFGSEETSSKAAPVQERIPAAYVSVAKSEADRLGVNDGALLSVNVAGKTLRLPLRIDEELGAGLVALP--KG 883
Cdd:cd02788 1 WQLVPYYHLFGSEELSQRSPVIAERAPAPYARLSPADAARLGLADGDLVEFSLGDGTLTLPVQISKYLPAGVVGLPlgAG 80
|
90
....*....|....*...
gi 1330194573 884 LAGIPPAIfgLTVDGLQE 901
Cdd:cd02788 81 FPGAPVAE--QTVVKLAA 96
|
|
| NADH-G_4Fe-4S_3 |
smart00929 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
88-128 |
9.39e-17 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 214918 [Multi-domain] Cd Length: 41 Bit Score: 74.54 E-value: 9.39e-17
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1330194573 88 RASVVEWLMTNHPHDCPVCEEGGHCHLQDMTVMTGHNERRY 128
Cdd:smart00929 1 RKTILELLLANHPLDCPVCDKNGECELQDLAYELGVDEQRY 41
|
|
| NADH-G_4Fe-4S_3 |
pfam10588 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
88-127 |
1.76e-15 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 463159 [Multi-domain] Cd Length: 40 Bit Score: 70.94 E-value: 1.76e-15
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1330194573 88 RASVVEWLMTNHPHDCPVCEEGGHCHLQDMTVMTGHNERR 127
Cdd:pfam10588 1 RKTILELLLSNHPLDCPTCDKNGNCELQDLAYELGVDEVR 40
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NuoG |
TIGR01973 |
NADH-quinone oxidoreductase, chain G; This model represents the G subunit (one of 14: A->N) of ... |
4-651 |
0e+00 |
|
NADH-quinone oxidoreductase, chain G; This model represents the G subunit (one of 14: A->N) of the NADH-quinone oxidoreductase complex I which generally couples NADH and ubiquinone oxidation/reduction in bacteria and mammalian mitochondria while translocating protons, but may act on NADPH and/or plastoquinone in cyanobacteria and plant chloroplasts. This model excludes related subunits from formate dehydrogenase complexes. [Energy metabolism, Electron transport]
Pssm-ID: 273904 [Multi-domain] Cd Length: 602 Bit Score: 807.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 4 IHVDGKELEVDGADNLLQACLSLGLDIPYFCWHPALGSVGACRQCAVKQYTDEndtrgRIVMSCMTPATDGSWISIEDEE 83
Cdd:TIGR01973 1 IFIDGKELEVPKGTTVLQACLSAGIEIPRFCYHEKLSIAGNCRMCLVEVEKFP-----KPVASCATPVTDGMKISTNSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 84 AKVFRASVVEWLMTNHPHDCPVCEEGGHCHLQDMTVMTGHNERRYRFTKRTHQNQQLGPFISHEMNRCIACYRCVRFYKD 163
Cdd:TIGR01973 76 VKKAREGVMEFLLINHPLDCPICDQGGECDLQDQAVMYGSDRSRFREKKRTVENKYLGPLIKTEMTRCIHCTRCVRFANE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 164 YAGGTDLGVFGAHDNVYFGRVEDGTLESEFSGNLTEVCPTGVFTDKTHSERYnRKWDMQFSPSICHGCSSGCNISPGERY 243
Cdd:TIGR01973 156 VAGVEDLGVIGRGNNVEIGTYEGKTLESELSGNLIDICPVGALTSKPYAFKA-RPWELKSTPSICVHDSVGCNIRVDERN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 244 GELRRIENRFNGSVNQYFLCDRGRFGYGYVNREDRPRQPLLADG----AKLSLDEALDKAAD-LLRGRNIVGIGSPRASL 318
Cdd:TIGR01973 235 GEIMRILPRENDEINEEWLCDKGRFGYDGLNRQDRLTKPLLRNQegnlLEVSWAEALAIAAEkLKASSRIGGIAGPRSSL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 319 ESNYALRELV---GAEHFYSGIEAGELERIRLVLQVLNDSPLpvpnmRDIEDHDAIFVLGEDLTQTAARVALSLRQSVKG 395
Cdd:TIGR01973 315 EELFALKKLVrklGSENFDLRIRNYEFESADLRANYLFNTTL-----ADIEEADLVLLVGADLRQEAPLLNLRLRKAVKK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 396 KAeDMADAMRVQPWLDAAVKNIgqhalNPLFIASLTATKLDDIAeecVHAAPDdlarigfavahaldasapavegldaea 475
Cdd:TIGR01973 390 GG-AKVALIGIEKWNLTYPANT-----NLVFHPGLSPKKLDDIA---SGAHSD--------------------------- 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 476 aelakrIADALLAAKRPLIIAG----TSLGSKALIEAAANIAKALKLREKN-GSISLIVPEANSLGLAMLGGES--LDAA 548
Cdd:TIGR01973 434 ------IAAALKAAKKPLIIVGdsaiSHLDGAALISAAANIAKVIKVRRKEwNGLNILSSGANSVGLLDLGGEStgLDAA 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 549 LQavtDGSADAIVVLENDLYTRTDSAKVDAALNAAKVVIVADHQKTATSDRAHLVLPAASFAEGDGTLVSQEGRAQRFFQ 628
Cdd:TIGR01973 508 LN---LGAADALFLLGADLERALDKTARDALSKADAFIIYQGHHGTETAEKADVILPGAAFTEKSGTYVNLEGRAQRFEQ 584
|
650 660
....*....|....*....|...
gi 1330194573 629 VFDPKYmdasiLVHEGWRWLHAL 651
Cdd:TIGR01973 585 AVKPPG-----EAREDWRILRAL 602
|
|
| 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 ... |
225-669 |
0e+00 |
|
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: 563.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 225 PSICHGCSSGCNISPGERYGELRRIENRFNGSVNQYFLCDRGRFGYGYVNREDRPRQPLLADGA---KLSLDEALDKAAD 301
Cdd:cd02771 1 PSICHHCSVGCNISLGERYGELRRVENRYNGAVNHYFLCDRGRFGYGYVNSRDRLTQPLIRRGGtlvPVSWNEALDVAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 302 LLRGRN--IVGIGSPRASLESNYALRELVGAehfYSGIEAGELERIRLVLQVLNDSPLPVPNMRDIEDHDAIFVLGEDLT 379
Cdd:cd02771 81 RLKEAKdkVGGIGSPRASNESNYALQKLVGA---VLGTNNVDHRARRLIAEILRNGPIYIPSLRDIESADAVLVLGEDLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 380 QTAARVALSLRQSVKGKAEDMADAMRVQPWLDAAVKNIGQHALNPLFIASLTATKLDDIAEECVHAAPDDLARIGFAVAH 459
Cdd:cd02771 158 QTAPRIALALRQAARRKAVELAALSGIPKWQDAAVRNIAQGAKSPLFIVNALATRLDDIAAESIRASPGGQARLGAALAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 460 ALDASAPAVEGLDAEaaELAKRIADALLAAKRPLIIAGTSLGSKALIEAAANIAKALKLREKNGSISLIVPEANSLGLAM 539
Cdd:cd02771 238 AVDASAAGVSGLAPK--EKAARIAARLTGAKKPLIVSGTLSGSLELIKAAANLAKALKRRGENAGLTLAVEEGNSPGLLL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 540 LGGE------SLDAALQAVTDGSADAIVVLENDLYTRTDSAKVDAALNAAKVVIVADHQKTATSDRAHLVLPAASFAEGD 613
Cdd:cd02771 316 LGGHvtepglDLDGALAALEDGSADALIVLGNDLYRSAPERRVEAALDAAEFVVVLDHFLTETAERADVVLPAASFAEKS 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1330194573 614 GTLVSQEGRAQRFFQVFDPKYMDAsilvHEGWRWLHALRATLLNQ--PIDWTQLDHVT 669
Cdd:cd02771 396 GTFVNYEGRAQRFFKAYDDPAGDA----RSDWRWLHALAAKLGGKlvPSDAAILDEII 449
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
1-678 |
0e+00 |
|
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440657 [Multi-domain] Cd Length: 453 Bit Score: 541.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 1 MATIHVDGKELEVDGADNLLQACLSLGLDIPYFCWHPALGSVGACRQCAVKQytdenDTRGRIVMSCMTPATDGSWISIE 80
Cdd:COG1034 1 MVTITIDGKEVEVPKGTTVLQAAEKAGIEIPRFCYHPKLSIAGACRMCLVEV-----EGAPKPVASCATPVTDGMVVKTD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 81 DEEAKVFRASVVEWLMTNHPHDCPVCEEGGHCHLQDMTVMTGHNERRYRFTKRTHQNQQLGPFISHEMNRCIACYRCVRF 160
Cdd:COG1034 76 SPKVKKARKGVMEFLLINHPLDCPICDQGGECDLQDQAMEYGVDESRYEEEKRTVPKKDLGPLILLDMNRCILCTRCVRF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 161 YKDYAGGTDLGVFGAHDNVYFGRVEDGTLESEFSGNLTEVCPTGVFTDKTHSErYNRKWDMQFSPSICHGCSSGCNISPG 240
Cdd:COG1034 156 CDEIAGDPELGVIGRGEHSEIGTYLGKPLDSEFSGNCIDVCPVGALTSKPFRF-KARPWELKKTPSICPHCSVGCNIRVD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 241 ERYGELRRIENRFNGSVNQYFLCDRGRFGYGYVNREDRPRQPLLADGAKL---SLDEALDKAADllrgrnivgigspras 317
Cdd:COG1034 235 VRGGKVYRVLPRENEAVNEEWLCDKGRFGYDGLNSPDRLTRPLVRKDGELveaSWEEALAAAAE---------------- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 318 lesnyALRELVGAEHFYSGIEAGELERIRLVLQVLNDSPLpvpnmrdiedhDAIFVLGEDLtqtaarvalslrqsvkgka 397
Cdd:COG1034 299 -----GLKALKKAENSVGAALLGALPDAAAILEAAEAGKL-----------KALVLLGADP------------------- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 398 edmadamrvqpwldaavknigqhalnplfiasltatklddiaeecvhaapddlarigfavahaldasapavEGLDAEAAe 477
Cdd:COG1034 344 -----------------------------------------------------------------------YDLDPAAA- 351
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 478 lakriadallaakrpliiagtslgskalieaaaniakalklrekngsislivpeanslglamlggesldaalqavtdgsa 557
Cdd:COG1034 --------------------------------------------------------------------------------
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 558 daivvlendlytrtdsakvDAALNAAKVVIVADHQKTATSDRAHLVLPAASFAEGDGTLVSQEGRAQRFFQVFDPKYMda 637
Cdd:COG1034 352 -------------------LAALAKADFVVVLDHFGSATAERADVVLPAAAFAEKSGTFVNLEGRVQRFNAAVPPPGE-- 410
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1330194573 638 silVHEGWRWLHALrATLLNQPIDWTQLDHVTAAAAAAAPQ 678
Cdd:COG1034 411 ---ARPDWRVLRAL-ANALGAGLPYDSLEEVRAELAAEAPA 447
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
225-655 |
9.12e-109 |
|
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: 340.41 E-value: 9.12e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 225 PSICHGCSSGCNISPGERYGELRRIENRFNGSVNQYFLCDRGRFGYGYVNREDRPRQPLLADGAKL---SLDEALDKAAD 301
Cdd:cd02768 1 ESIDVHDALGSNIRVDVRGGEVMRILPRENEAINEEWISDKGRFGYDGLNSRQRLTQPLIKKGGKLvpvSWEEALKTVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 302 LLRGRN---IVGIGSPRASLESNYALRELVGAEhfysGIEAGELERIRLVLQVLND---SPLPVPNMRDIEDHDAIFVLG 375
Cdd:cd02768 81 GLKAVKgdkIGGIAGPRADLESLFLLKKLLNKL----GSNNIDHRLRQSDLPADNRlrgNYLFNTSIAEIEEADAVLLIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 376 EDLTQTAARVALSLRQSVKGKAedmadamrvqpwldaavknigqhalNPLFIASLTATKLddIAEECVHAAPddlarIGF 455
Cdd:cd02768 157 SNLRKEAPLLNARLRKAVKKKG-------------------------AKIAVIGPKDTDL--IADLTYPVSP-----LGA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 456 AVAHALDASAPAVEgldaeaaelaKRIADALLAAKRPLIIAGTSL---GSKALIEAAANIAKALKlreKNGSISLIVPEA 532
Cdd:cd02768 205 SLATLLDIAEGKHL----------KPFAKSLKKAKKPLIILGSSAlrkDGAAILKALANLAAKLG---TGAGLWNGLNVL 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 533 NSLGLAmLGGESLDAALQAVTDGSADAIVVLENDLYTRTDSAKVdaALNAAKVVIVADHQKTATSDRAHLVLPAASFAEG 612
Cdd:cd02768 272 NSVGAR-LGGAGLDAGLALLEPGKAKLLLLGEDELDRSNPPAAV--ALAAADAFVVYQGHHGDTGAQADVILPAAAFTEK 348
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1330194573 613 DGTLVSQEGRAQRFFQVFDPKYMdasilVHEGWRWLHALRATL 655
Cdd:cd02768 349 SGTYVNTEGRVQRFKKAVSPPGD-----AREDWKILRALSNLL 386
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
1-631 |
1.05e-55 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 206.72 E-value: 1.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 1 MATIHVDGKELEVDGADNLLQACLSLGLDIPYFCWHPALGSVGACRQCAVkqytdenDTRG--RIVMSCMTPATDGSWIS 78
Cdd:PRK07860 4 LVTLTIDGVEVSVPKGTLVIRAAELLGIQIPRFCDHPLLDPVGACRQCLV-------EVEGqrKPQASCTTTVTDGMVVK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 79 IED--EEAKVFRASVVEWLMTNHPHDCPVCEEGGHCHLQDMTVMTGHNERRYRFTKRTHQNqqlgPF-ISHEM----NRC 151
Cdd:PRK07860 77 TQLtsPVADKAQHGVMELLLINHPLDCPVCDKGGECPLQNQAMSNGRAESRFTDVKRTFPK----PInISTQVlldrERC 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 152 IACYRCVRFYKDYAGG--TDLGVFGAHDNVyfGRVEDGTLESEFSGNLTEVCPTGVFTDKTHSERyNRKWDMQFSPSICH 229
Cdd:PRK07860 153 VLCARCTRFSDQIAGDpfIDLQERGALQQV--GIYEGEPFQSYFSGNTVQICPVGALTGAAYRFR-ARPFDLVSTPSVCE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 230 GCSSGCNISPGERYGELRRienRFNGS---VNQYFLCDRGRFGYGYVNREDRPRQPLL--ADGA--KLSLDEALDKAADL 302
Cdd:PRK07860 230 HCASGCAQRTDHRRGKVLR---RLAGDdpeVNEEWNCDKGRWAFTYATQPDRITTPLVrdEDGElePASWSEALAVAARG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 303 L---RGRNIVGIGSpRASLESNYAlrelvgaehfYSGIEageleriRLVLQVlNDSplpvpnmrdieDHDAIFVLGEDLT 379
Cdd:PRK07860 307 LaaaRGRVGVLVGG-RLTVEDAYA----------YAKFA-------RVALGT-NDI-----------DFRARPHSAEEAD 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 380 QTAARVALslrqsvKGKAEDMAD---AMRV-----QPWLDAAV------KNIGQHALNPLFIASLTATKLDDIAEECVHA 445
Cdd:PRK07860 357 FLAARVAG------RGLGVTYADlekAPAVllvgfEPEEESPIvflrlrKAARKHGLKVYSIAPFATRGLEKMGGTLLRT 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 446 AP-------DDLARIGFAVAHALDAS---------APAVEGLDAEAAELAKRIADALL-----AAKRPLIIAGT--SL-- 500
Cdd:PRK07860 431 APggeaaalDALATGAPDVAELLRTPgavilvgerLATVPGALSAAARLADATGARLAwvprrAGERGALEAGAlpTLlp 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 501 GSKALIEAAANIAkalkLREKNGSISLivPEANslglamlgGESLDAALQAVTDGSADAIVVLENDLYTRTDSAKVDAAL 580
Cdd:PRK07860 511 GGRPVADPAARAE----VAAAWGVDEL--PAAP--------GRDTAGILAAAAAGELGALLVGGVEPADLPDPAAALAAL 576
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1330194573 581 NAAKVVIVADHQKTATSDRAHLVLPAASFAEGDGTLVSQEGRAQRFFQVFD 631
Cdd:PRK07860 577 DAAGFVVSLELRHSAVTERADVVLPVAPVAEKAGTFLNWEGRLRPFEAALR 627
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
225-651 |
2.18e-49 |
|
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: 179.06 E-value: 2.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 225 PSICHGCSSGCNISPGERYGELRRIENRFNGSVNQYFLCDRGRFGYGYVNREDRPRQPLLADGAK-----LSLDEALDKA 299
Cdd:cd00368 1 PSVCPFCGVGCGILVYVKDGKVVRIEGDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGGRgkfvpISWDEALDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 300 ADLLR-------GRNIVGIGSPRASLESNYALREL--------VGAEHFYSGIEAGelerirlVLQVLNDSPLPVPNMRD 364
Cdd:cd00368 81 AEKLKeirekygPDAIAFYGGGGASNEEAYLLQKLlralgsnnVDSHARLCHASAV-------AALKAFGGGAPTNTLAD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 365 IEDHDAIFVLGEDLTQTAARVALSLRQSVKGKAedmadamrvqpwldaavKNIgqhALNPLFiaSLTATKLDdiaeecVH 444
Cdd:cd00368 154 IENADLILLWGSNPAETHPVLAARLRRAKKRGA-----------------KLI---VIDPRR--TETAAKAD------EW 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 445 AAPddlaRIG--FAVAHALDASapAVEGLDAEA-AELAKRIAdallAAKRPLIIAGTSL----GSKALIEAAANIAKALK 517
Cdd:cd00368 206 LPI----RPGtdAALALAEWAA--EITGVPAETiRALAREFA----AAKRAVILWGMGLtqhtNGTQNVRAIANLAALTG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 518 LREKNGsislivpeanslGLAMLGGesldaalqavtdgsadaivvleNDLYTRTDSAKVDAALNAAKVVIVADHQKTATS 597
Cdd:cd00368 276 NIGRPG------------GGLGPGG----------------------NPLVSAPDANRVRAALKKLDFVVVIDIFMTETA 321
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1330194573 598 DRAHLVLPAASFAEGDGTLVSQEGRAQRFFQVFDPKYMdasilVHEGWRWLHAL 651
Cdd:cd00368 322 AYADVVLPAATYLEKEGTYTNTEGRVQLFRQAVEPPGE-----ARSDWEILREL 370
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
221-881 |
1.81e-36 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 147.34 E-value: 1.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 221 MQFSPSICHGCSSGCNISPGERYGELRRIENRFNGSVNQYFLCDRGRFGYGYVNREDRPRQPLLADGAKL---SLDEALD 297
Cdd:COG3383 4 MKKVKTVCPYCGVGCGIDLEVKDGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVNSPDRLTTPLIRRGGEFrevSWDEALD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 298 KAADLLR------GRN-IVGIGSPRASLESNYAL----RELVGAEHFYSgieageleRIRL--------VLQVLNDSPLP 358
Cdd:COG3383 84 LVAERLReiqaehGPDaVAFYGSGQLTNEENYLLqklaRGVLGTNNIDN--------NARLcmasavagLKQSFGSDAPP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 359 VPnMRDIEDHDAIFVLGEDLTQTAARVALSLRQSVKGKAE------------DMADA-MRVQPWLDAAVKN------IGQ 419
Cdd:COG3383 156 NS-YDDIEEADVILVIGSNPAEAHPVLARRIKKAKKNGAKlivvdprrtetaRLADLhLQIKPGTDLALLNgllhviIEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 420 HALNPLFIASLTaTKLDDIAEECVHAAPDDLARIgfavahaldasapavEGLDAEAAElakRIADALLAAKRPLIIagTS 499
Cdd:COG3383 235 GLVDEDFIAERT-EGFEELKASVAKYTPERVAEI---------------TGVPAEDIR---EAARLIAEAKRAMIL--WG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 500 LG------SKALIEAAANIAKALKL--REKNGSISLiVPEANSLGLAMLG------------------------------ 541
Cdd:COG3383 294 MGvnqhtqGTDNVNAIINLALATGNigRPGTGPFPL-TGQNNVQGGRDMGalpnvlpgyrdvtdpehrakvadawgvppl 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 542 ----GESLDAALQAVTDGSADAIVVL-ENDLYTRTDSAKVDAALNAAKVVIVADHQKTATSDRAHLVLPAASFAEGDGTL 616
Cdd:COG3383 373 pdkpGLTAVEMFDAIADGEIKALWIIgENPAVSDPDANHVREALEKLEFLVVQDIFLTETAEYADVVLPAASWAEKDGTF 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 617 VSQEGRAQRFFQVFDPKYMdasilVHEGWRWLHALrATLLNQPIDWTqldhvtaaaaaaapqlarivdaAPSAAFRIkgm 696
Cdd:COG3383 453 TNTERRVQRVRKAVEPPGE-----ARPDWEIIAEL-ARRLGYGFDYD----------------------SPEEVFDE--- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 697 kLAREPLRYSGRT--AMRADISVHEP-RTPQDNDTAFAFSmEGYSGSVEPRQQVPFAWSPGWNSPqawnkfqdevgghir 773
Cdd:COG3383 502 -IARLTPDYSGISyeRLEALGGVQWPcPSEDHPGTPRLFT-GRFPTPDGKARFVPVEYRPPAELP--------------- 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 774 agDPGTRLIESTGDSLnwfasvprpfnpaqgtwqvvpffHLFGSEETSSKAAPVQERIPAAYVSVAKSEADRLGVNDGAL 853
Cdd:COG3383 565 --DEEYPLVLTTGRLL-----------------------DQWHTGTRTRRSPRLNKHAPEPFVEIHPEDAARLGIKDGDL 619
|
730 740
....*....|....*....|....*...
gi 1330194573 854 LSVNVAGKTLRLPLRIDEELGAGLVALP 881
Cdd:COG3383 620 VRVSSRRGEVVLRARVTDRVRPGTVFMP 647
|
|
| PTZ00305 |
PTZ00305 |
NADH:ubiquinone oxidoreductase; Provisional |
2-204 |
9.28e-31 |
|
NADH:ubiquinone oxidoreductase; Provisional
Pssm-ID: 140326 [Multi-domain] Cd Length: 297 Bit Score: 123.22 E-value: 9.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 2 ATIHVDGKELEV-DGADNLLQACLSLGLDIPYFCWHPALGSVGACRQCAVKQYTDENdtrgrIVMSCMTPATDGSWISIE 80
Cdd:PTZ00305 69 AIMFVNKRPVEIiPQEENLLEVLEREGIRVPKFCYHPILSVAGNCRMCLVQVDGTQN-----LVVSCATVALPGMSIITD 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 81 DEEAKVFRASVVEWLMTNHPHDCPVCEEGGHCHLQDMTVMTGHNERRYRFTKRTHQNQQLGPFISHEMNRCIACYRCVRF 160
Cdd:PTZ00305 144 SRLVRDAREGNVELILINHPNDCPICEQATNCDLQNVSMNYGTDIPRYKEDKRAVQDFYFDPQTRVVLNRCIHCTRCVRF 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1330194573 161 YKDYAGGTDLGVFGAHdnvyfGRVEDGT----LESEFSGNL--TEVCPTG 204
Cdd:PTZ00305 224 LNEHAQDFNLGMIGRG-----GLSEISTfldeLEVKTDNNMpvSQLCPVG 268
|
|
| PRK08493 |
PRK08493 |
NADH-quinone oxidoreductase subunit G; |
1-540 |
6.18e-30 |
|
NADH-quinone oxidoreductase subunit G;
Pssm-ID: 236277 [Multi-domain] Cd Length: 819 Bit Score: 127.51 E-value: 6.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 1 MATIHVDGKELEVDGADNLLQACLSLGLDIPYFCWHPALGSVGACRQCAVkqytdenDTRGRIVMSCMTPATDGSWI--- 77
Cdd:PRK08493 1 MITITINGKECEAQEGEYILNVARRNGIFIPAICYLSGCSPTLACRLCMV-------EADGKRVYSCNTKAKEGMNIltn 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 78 --SIEDEeakvfRASVVEWLMTNHPHDCPVCEEGGHCHLQDMTVMTGHNERRYRfTKRTHQNQQLGPFISHEMNRCIACY 155
Cdd:PRK08493 74 tpNLMDE-----RNAIMQTYDVNHPLECGVCDKSGECELQNFTHEMGVNHQPYA-IKDTHKPHKHWGKINYDPSLCIVCE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 156 RCVRFYKDYAGGTDLGVF--GAH--DNVY-------------------FGRVEDGTLESEFSGNLTEVCPTGVFTDKTHS 212
Cdd:PRK08493 148 RCVTVCKDKIGESALKTVprGLDapDKSFkesmpkdayavwskkqkslIGPVGGETLDCSFCGECIAVCPVGALSSSDFQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 213 ERYNrKWDMQFSPSICHGCSSGCNI-------SPGERYGELRRIENRFngsvnqYF--LCDRGRFGYGYVNREDRPRQpl 283
Cdd:PRK08493 228 YTSN-AWELKKIPATCPHCSDCCLIyydvkhsSILNQESKIYRVSNDF------YFnpLCGAGRFAFDFQNEADKDEK-- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 284 ladgaklsldeALDKAADLLRGRNIVGIGSpRASLESNYALrELVGAEHFYSGI--EAGELER-IRLVLQVLNDSPLpvP 360
Cdd:PRK08493 299 -----------AFKEAVEAFKEAKAIKFNS-FITNEEALIL-QRLKKKFGLKLIneEALKFQQfLKVFSEVSGKSYS--A 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 361 NMRDIEDHDAIFVLGEDLTQTAARVALSLRQSV---KGKA---EDMADamrvqPWLDAAVKNIGQHALNPLFIASLTATK 434
Cdd:PRK08493 364 NLEDIKTSDFVVVAGSALKTDNPLLRYAINNALkmnKASGlyfHPIKD-----NVIANLSKNFFCITHEVGAEEIILYFL 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 435 LDDIAEECvhAAPDDLAriGFAVAHALDASAPAVEGLDAEAAELAK---------------------------------- 480
Cdd:PRK08493 439 LKKFLEEE--AILKSLE--EFKQSIVKEAALSILEEIREKVLEQAEqgcenqeevkkevpkkvkkipevdtyllleelgi 514
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330194573 481 ------RIADALLAAKRPLIIAGTSLGSKaliEAAANIAKALKLREKNGSISLIV--PEANSLGLAML 540
Cdd:PRK08493 515 neetyeKLEALLAKKNNFTLVVGEDLYAH---KNAKNLAKLLGLIQKYTAFKVILipPSTNTLGVALI 579
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
225-651 |
1.04e-27 |
|
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: 116.68 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 225 PSICHGCSSGCNISPGERYGELRRIENRFNGSVNQYFLCDRGRFGYGYVNREDRPRQPLLADGAK---LSLDEALDKAAD 301
Cdd:cd02772 1 KSVSPHDALGSNLVVHVKNNKVMRVVPRENEAINECWLSDRDRFSYEGLNSEDRLTKPMIKKDGQwqeVDWETALEYVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 302 LLR------GRNIVG-IGSPRASLESNYALRELVgaehfySGIEAGELE-RIRLVLQVLNDSPLPVPNM----RDIEDHD 369
Cdd:cd02772 81 GLSaiikkhGADQIGaLASPHSTLEELYLLQKLA------RGLGSDNIDhRLRQSDFRDDAKASGAPWLgmpiAEISELD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 370 AIFVLGEDLTQTAARVALSLRQSVKGKAEdmadamrvqpwldaavknigQHALNPL---FIASLTATKLddiaeecvhAA 446
Cdd:cd02772 155 RVLVIGSNLRKEHPLLAQRLRQAVKKGAK--------------------LSAINPAdddFLFPLSGKAI---------VA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 447 PDDLARIGFAVAHAL---DASAPAVEGLDAEAAELAKRIADALLAAKRPLIIagtsLGSKAL--IEAAANIAKALKLREK 521
Cdd:cd02772 206 PSALANALAQVAKALaeeKGLAVPDEDAKVEASEEARKIAASLVSAERAAVF----LGNLAQnhPQAATLRALAQEIAKL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 522 NGSISLIVPE-ANSLGLAMLG---GESLDAALQAVTDGSADAIVVLENDLYTRTDSAKVDAALNAAKVVIVADHQKTATS 597
Cdd:cd02772 282 TGATLGVLGEgANSVGAYLAGalpHGGLNAAAMLEQPRKAYLLLNVEPELDCANPAQALAALNQAEFVVALSAFASAALL 361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1330194573 598 DRAHLVLPAASFAEGDGTLVSQEGRAQRFFQVFDPkYMDAsilvHEGWRWLHAL 651
Cdd:cd02772 362 DYADVLLPIAPFTETSGTFVNLEGRVQSFKGVVKP-LGEA----RPAWKVLRVL 410
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
225-632 |
1.53e-27 |
|
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: 117.70 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 225 PSICHGCSSGCNISPGERYGELRRIENRFNGSVNQYFLCDRGRFGYGYVNREDRPRQPLLADGAKL---SLDEALDKAAD 301
Cdd:cd02753 1 KTVCPYCGVGCGLELWVKDNKIVGVEPVKGHPVNRGKLCVKGRFGFDFVNSKDRLTKPLIRKNGKFveaSWDEALSLVAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 302 LLR------GRN-IVGIGSPRASLESNYALRELVGAehfysgieAGELERI----RL--------VLQVLNDSPLPVPnM 362
Cdd:cd02753 81 RLKeikdkyGPDaIAFFGSAKCTNEENYLFQKLARA--------VGGTNNVdhcaRLchsptvagLAETLGSGAMTNS-I 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 363 RDIEDHDAIFVLGEDLTQTAARVALSLRQSVKGKAE---------DMADA----MRVQPWLDAAVKN------IGQHALN 423
Cdd:cd02753 152 ADIEEADVILVIGSNTTEAHPVIARRIKRAKRNGAKlivadprrtELARFadlhLQLRPGTDVALLNamahviIEEGLYD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 424 PLFIASLTaTKLDDIAEECVHAAPDDLARIgfavahaldasapavEGLDAEA-AELAKRIADallaAKRPLIIAGTSL-- 500
Cdd:cd02753 232 EEFIEERT-EGFEELKEIVEKYTPEYAERI---------------TGVPAEDiREAARMYAT----AKSAAILWGMGVtq 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 501 ------GSKALIEAAA---NIAK----ALKLREKNgsislivpeaNSLGLAMLGgesldaALQAVTDGSADAIVVL-END 566
Cdd:cd02753 292 hshgtdNVMALSNLALltgNIGRpgtgVNPLRGQN----------NVQGACDMG------ALPNVLPGYVKALYIMgENP 355
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1330194573 567 LYTRTDSAKVDAALNAAKVVIVADHQKTATSDRAHLVLPAASFAEGDGTLVSQEGRAQRFFQVFDP 632
Cdd:cd02753 356 ALSDPNTNHVRKALESLEFLVVQDIFLTETAELADVVLPAASFAEKDGTFTNTERRVQRVRKAVEP 421
|
|
| PRK07569 |
PRK07569 |
bidirectional hydrogenase complex protein HoxU; Validated |
3-204 |
1.35e-26 |
|
bidirectional hydrogenase complex protein HoxU; Validated
Pssm-ID: 181037 [Multi-domain] Cd Length: 234 Bit Score: 108.97 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 3 TIHVDGKELEVDGADNLLQACLSLGLDIPYFCWHPALGSVGACRQCAVkqytdENDTRGRIVMSCMTPATDGSWISIEDE 82
Cdd:PRK07569 5 TLTIDDQLVSAREGETLLEAAREAGIPIPTLCHLDGLSDVGACRLCLV-----EIEGSNKLLPACVTPVAEGMVVQTNTP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 83 EAKVFRASVVEWLMTNHPHDCPVCEEGGHCHLQDMTVMTG--HNERRYRFTKRTHQnqqlgpfISHEM-----NRCIACY 155
Cdd:PRK07569 80 RLQEYRRMIVELLFAEGNHVCAVCVANGNCELQDLAIEVGmdHVRFPYLFPRRPVD-------ISHPRfgidhNRCVLCT 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1330194573 156 RCVRFYKDYAGGT--DLGVFGAHDNVyfgrVED-----GTLESEFS-GNLTEVCPTG 204
Cdd:PRK07569 153 RCVRVCDEIEGAHtwDVAGRGAKSRV----ITDlnqpwGTSETCTScGKCVQACPTG 205
|
|
| MopB_CT_NDH-1_NuoG2-N7 |
cd02788 |
MopB_CT_NDH-1_NuoG2-N7: C-terminal region of the NuoG-like subunit (of the variant with a ... |
806-901 |
9.95e-25 |
|
MopB_CT_NDH-1_NuoG2-N7: C-terminal region of the NuoG-like subunit (of the variant with a [4Fe-4S] cluster, N7) of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1) found in various bacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain, is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Unique to this group, compared to the other prokaryotic and eukaryotic groups in this domain protein family (NADH-Q-OR-NuoG2), is an N-terminal [4Fe-4S] cluster (N7/N1c) present in the second domain and a C-terminal region (this CD) homologous to the formate dehydrogenase C-terminal molybdopterin_binding (MopB) region.
Pssm-ID: 239189 [Multi-domain] Cd Length: 96 Bit Score: 98.92 E-value: 9.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 806 WQVVPFFHLFGSEETSSKAAPVQERIPAAYVSVAKSEADRLGVNDGALLSVNVAGKTLRLPLRIDEELGAGLVALP--KG 883
Cdd:cd02788 1 WQLVPYYHLFGSEELSQRSPVIAERAPAPYARLSPADAARLGLADGDLVEFSLGDGTLTLPVQISKYLPAGVVGLPlgAG 80
|
90
....*....|....*...
gi 1330194573 884 LAGIPPAIfgLTVDGLQE 901
Cdd:cd02788 81 FPGAPVAE--QTVVKLAA 96
|
|
| NADH-G_4Fe-4S_3 |
smart00929 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
88-128 |
9.39e-17 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 214918 [Multi-domain] Cd Length: 41 Bit Score: 74.54 E-value: 9.39e-17
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1330194573 88 RASVVEWLMTNHPHDCPVCEEGGHCHLQDMTVMTGHNERRY 128
Cdd:smart00929 1 RKTILELLLANHPLDCPVCDKNGECELQDLAYELGVDEQRY 41
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
234-625 |
1.50e-15 |
|
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: 79.62 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 234 GCNISPGERYGELRRIENRFNGSVNQYFLCDRGRFGYGYVNREdRPRQPLLADGAKL---SLDEALDKAADLLRGRN--- 307
Cdd:cd02773 10 GSNIRVDTRGGEVMRILPRLNEDINEEWISDKTRFAYDGLKRQ-RLDKPYIRKNGKLkpaTWEEALAAIAKALKGVKpde 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 308 IVGIGSPRASLESNYALRELV---GAEHFYSGIEAGELERIRLVLQVLNDSplpvpnMRDIEDHDAIFVLGEDLTQTAAR 384
Cdd:cd02773 89 IAAIAGDLADVESMVALKDLLnklGSENLACEQDGPDLPADLRSNYLFNTT------IAGIEEADAVLLVGTNPRFEAPV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 385 VALSLRQSVKGKaedmadamrvqpwlDAAVKNIGQhalnplfiasltatklddiaeecvhaaPDDLArigFAVAHaLDAS 464
Cdd:cd02773 163 LNARIRKAWLHG--------------GLKVGVIGP---------------------------PVDLT---YDYDH-LGTD 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 465 APAVEGLDAEAAELAKriadALLAAKRPLIIAGTS-LGSK---ALIEAAANIAKALK-LREKNGSISLIVPEANSLGLAM 539
Cdd:cd02773 198 AKTLQDIASGKHPFSK----ALKDAKKPMIIVGSGaLARKdgaAILAAVAKLAKKNGvVREGWNGFNVLHRAASRVGALD 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 540 LGGESLDAALqaVTDGSADAIVVLENDLYTRTDSAKvdaalnAAKVVIVADHQKTATSdRAHLVLPAASFAEGDGTLVSQ 619
Cdd:cd02773 274 LGFVPGAGAI--RKSGPPKVLYLLGADEIDITPIPK------DAFVVYQGHHGDRGAQ-IADVILPGAAYTEKSGTYVNT 344
|
....*.
gi 1330194573 620 EGRAQR 625
Cdd:cd02773 345 EGRVQQ 350
|
|
| NADH-G_4Fe-4S_3 |
pfam10588 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
88-127 |
1.76e-15 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 463159 [Multi-domain] Cd Length: 40 Bit Score: 70.94 E-value: 1.76e-15
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1330194573 88 RASVVEWLMTNHPHDCPVCEEGGHCHLQDMTVMTGHNERR 127
Cdd:pfam10588 1 RKTILELLLSNHPLDCPTCDKNGNCELQDLAYELGVDEVR 40
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
289-634 |
3.13e-15 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 78.21 E-value: 3.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 289 KLSLDEALDKAADLLRGRN---------IVGIGSPRASLESNYALREL---VGAEHFYSgieAGELERIRLVLQVLNDSP 356
Cdd:pfam00384 16 RVSWDEALDLIAKKLKRIIkkygpdaiaINGGSGGLTDVESLYALKKLlnrLGSKNGNT---EDHNGDLCTAAAAAFGSD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 357 LP-----VPNMRDIEDHDAIFVLGEDLTQTAARVALSLRQSVKGKaedmadamrvqpwlDAAVKNIGQhalnplfiaSLT 431
Cdd:pfam00384 93 LRsnylfNSSIADIENADLILLIGTNPREEAPILNARIRKAALKG--------------KAKVIVIGP---------RLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 432 ATklddiaeecvhaapddlarigFAVAHaLDASAPAVEGLdaeAAELAKRIADALLAAK----RPLIIAGTSL----GSK 503
Cdd:pfam00384 150 LT---------------------YADEH-LGIKPGTDLAL---ALAGAHVFIKELKKDKdfapKPIIIVGAGVlqrqDGE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 504 ALIEAAANIAKALKLREKNGSIS---LIVP-EANSLGLAMLG---GESLDAALQAVTDGSADAIVVL-ENDLYTRTDSAK 575
Cdd:pfam00384 205 AIFRAIANLADLTGNIGRPGGGWnglNILQgAASPVGALDLGlvpGIKSVEMINAIKKGGIKVLYLLgNNPFVTHADENR 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 576 VDAALNAAKVVIVAD-HQKTATSDRAHLVLPAASFAEGDGTLVSQEGRAQRFFQVFDPKY 634
Cdd:pfam00384 285 VVKALQKLDLFVVYDgHHGDKTAKYADVILPAAAYTEKNGTYVNTEGRVQSTKQAVPPPG 344
|
|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
221-275 |
7.37e-14 |
|
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: 66.55 E-value: 7.37e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1330194573 221 MQFSPSICHGCSSGCNISPGERYGELRRIENRFNGSVNQYFLCDRGRFGYGYVNR 275
Cdd:pfam04879 1 MKVVKTICPYCGVGCGLEVHVKDGKIVKVEGDPDHPVNEGRLCVKGRFGYERVYN 55
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
221-274 |
5.25e-13 |
|
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: 64.19 E-value: 5.25e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1330194573 221 MQFSPSICHGCSSGCNISPGERYGELRRIENRFNGSVNQYFLCDRGRFGYGYVN 274
Cdd:smart00926 1 EKWVPTVCPLCGVGCGLLVEVKDGRVVRVRGDPDHPVNRGRLCPKGRAGLEQVY 54
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
220-634 |
1.08e-12 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 71.80 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 220 DMQFSPSICHGCSSGCNISPGERYGELRRIENRFNGSVNQYFLCDRGRFGYGYVNREDRPRQPLLADGAK-------LSL 292
Cdd:COG0243 20 GTKTVKTTCPGCGVGCGLGVKVEDGRVVRVRGDPDHPVNRGRLCAKGAALDERLYSPDRLTYPMKRVGPRgsgkferISW 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 293 DEALDKAADLLR------GRNIVGIGS-----PRASLESNYALRELV---GAEHFYS-------GIEAGelerirlVLQV 351
Cdd:COG0243 100 DEALDLIAEKLKaiideyGPEAVAFYTsggsaGRLSNEAAYLAQRFAralGTNNLDDnsrlcheSAVAG-------LPRT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 352 LNDSPLPVPnMRDIEDHDAIFVLGEDLTQTAARVALSLRQSVKGK-------------AEDMADAmrvqpWL------DA 412
Cdd:COG0243 173 FGSDKGTVS-YEDLEHADLIVLWGSNPAENHPRLLRRLREAAKKRgakivvidprrteTAAIADE-----WLpirpgtDA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 413 AVKN------IGQHALNPLFIASLTaTKLDDIAEECVHAAPDDLARIgfavahaldaSapaveGLDAEA-AELAKRIAda 485
Cdd:COG0243 247 ALLLalahvlIEEGLYDRDFLARHT-VGFDELAAYVAAYTPEWAAEI----------T-----GVPAEDiRELAREFA-- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 486 llAAKRPLIIAGTSL-----GSKAlIEAAANIAkALKlreknGSISliVPEAnslGLAMLGGEsldaalqAVTDGS---A 557
Cdd:COG0243 309 --TAKPAVILWGMGLqqhsnGTQT-VRAIANLA-LLT-----GNIG--KPGG---GPFSLTGE-------AILDGKpypI 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1330194573 558 DAIVVLE-NDLYTRTDSAKVDAALNAAKVVIVADHQKTATSDRAHLVLPAASFAEGDGTLVSQE-GRAQRFFQVFDPKY 634
Cdd:COG0243 368 KALWVYGgNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARYADIVLPATTWLERDDIVTNSEdRRVHLSRPAVEPPG 446
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
3-74 |
7.80e-12 |
|
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.
Pssm-ID: 238126 [Multi-domain] Cd Length: 84 Bit Score: 62.03 E-value: 7.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 3 TIHVDGKELEVDGADNLLQACLSLGLDIPYFCWHpalgsvGACRQCAVK-----------QYTDENDTRGRIVMSCMTPA 71
Cdd:cd00207 4 NVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRA------GACGTCKVEvvegevdqsdpSLLDEEEAEGGYVLACQTRV 77
|
...
gi 1330194573 72 TDG 74
Cdd:cd00207 78 TDG 80
|
|
| Fer2_4 |
pfam13510 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
1-74 |
1.00e-10 |
|
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which a beta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated. This cluster appears within sarcosine oxidase proteins.
Pssm-ID: 433268 [Multi-domain] Cd Length: 82 Bit Score: 58.70 E-value: 1.00e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330194573 1 MATIHVDGKELEVDGADNLLQACLSLGLDIPYFCWHPA----LGSVGACRQCAVKQYTDENdtrgriVMSCMTPATDG 74
Cdd:pfam13510 3 PVTFTFDGRPVTAPEGDTIAAALLANGVRVPRSCKYGRprgiFCAMGECRNCLVEVDGVPN------VRACTTPVREG 74
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
1-107 |
1.10e-08 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 58.97 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 1 MATIH--VDGKELEVDGADNLLQACLSLGLDIPYFCWHPALGSVGACRQCAVkqytdENDTRGRIVMSCMTPATDGSWIS 78
Cdd:PRK12814 1 MNTISltINGRSVTAAPGTSILEAAASAGITIPTLCFHQELEATGSCWMCIV-----EIKGKNRFVPACSTAVSEGMVIE 75
|
90 100 110
....*....|....*....|....*....|.
gi 1330194573 79 IEDEEAKVFRASVVEWLMTNHPHDC--PvCE 107
Cdd:PRK12814 76 TENAELHAMRRQSLERLIEQHCGDClgP-CE 105
|
|
| Fer2 |
pfam00111 |
2Fe-2S iron-sulfur cluster binding domain; |
4-72 |
1.23e-07 |
|
2Fe-2S iron-sulfur cluster binding domain;
Pssm-ID: 395061 [Multi-domain] Cd Length: 77 Bit Score: 49.83 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 4 IHVDGKELEVDGADN---LLQACLSLGLDIPYFCWHpalgsvGACRQCAVK---------QYTDENDTR--GRIVMSCMT 69
Cdd:pfam00111 1 VTINGKGVTIEVPDGettLLDAAEEAGIDIPYSCRG------GGCGTCAVKvlegedqsdQSFLEDDELaaGYVVLACQT 74
|
...
gi 1330194573 70 PAT 72
Cdd:pfam00111 75 YPK 77
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
225-632 |
4.52e-07 |
|
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. 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: 53.38 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 225 PSICHGCSSGCNISPGERYGELRRIENRFNGSVNQYFLCDRGRFGYGYVNREDRPRQPLL-ADGAKL---SLDEALDKAA 300
Cdd:cd02754 1 KTTCPYCGVGCGVEIGVKDGKVVAVRGDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLLrRNGGELvpvSWDEALDLIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 301 DLLR------GRNIVG-IGSPRASLESNYALRELVgaehfysgieageleriRLVLQVLNDSP----------------- 356
Cdd:cd02754 81 ERFKaiqaeyGPDSVAfYGSGQLLTEEYYAANKLA-----------------KGGLGTNNIDTnsrlcmasavagykrsf 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 357 ---LPVPNMRDIEDHDAIFVLGedlTQTA-------ARVALSLRQSVKGK----------AEDMADA-MRVQPWLDAAVK 415
Cdd:cd02754 144 gadGPPGSYDDIEHADCFFLIG---SNMAechpilfRRLLDRKKANPGAKiivvdprrtrTADIADLhLPIRPGTDLALL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 416 N------IGQHALNPLFIAS-----------LTATKLDDIAEECVhAAPDDLARIGFAVAHALDASAPAVEGLD--AEAA 476
Cdd:cd02754 221 NgllhvlIEEGLIDRDFIDAhtegfeelkafVADYTPEKVAEITG-VPEADIREAARLFGEARKVMSLWTMGVNqsTQGT 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 477 ELAKRIADALLAAKR-------PLIIAG--------------TSLGSKALIEAA---ANIAKALKLREKNgsislIVPEA 532
Cdd:cd02754 300 AANNAIINLHLATGKigrpgsgPFSLTGqpnamggrevgglaNLLPGHRSVNNPehrAEVAKFWGVPEGT-----IPPKP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 533 nslglamlgGESLDAALQAVTDGSADAI-VVLENDLYTRTDSAKVDAALNAAKVVIVAD-HQKTATSDRAHLVLPAASFA 610
Cdd:cd02754 375 ---------GLHAVEMFEAIEDGEIKALwVMCTNPAVSLPNANRVREALERLEFVVVQDaFADTETAEYADLVLPAASWG 445
|
490 500
....*....|....*....|..
gi 1330194573 611 EGDGTLVSQEGRAQRFFQVFDP 632
Cdd:cd02754 446 EKEGTMTNSERRVSLLRAAVEP 467
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
225-304 |
1.06e-05 |
|
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: 48.83 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 225 PSICHGCSSGCNISPGERYGELRRIENRFNGSVNQYFLCDRGRFGYGYVNREDRPRQPLLADGAK-------LSLDEALD 297
Cdd:cd02755 2 PSICEMCSSRCGILARVEDGRVVKIDGNPLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRVGERgegkfreASWDEALQ 81
|
....*..
gi 1330194573 298 KAADLLR 304
Cdd:cd02755 82 YIASKLK 88
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
225-304 |
5.31e-05 |
|
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: 46.66 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 225 PSICHGCSSGCNISPGERYGELRRIENRFNGSVNQYFLCDRGRFGYGYVNREDRPRQPLLADGAK-----------LSLD 293
Cdd:cd02757 3 PSTCQGCTAWCGLQAYVEDGRVTKVEGNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRTNPRkgrdvdpkfvpISWD 82
|
90
....*....|.
gi 1330194573 294 EALDKAADLLR 304
Cdd:cd02757 83 EALDTIADKIR 93
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
480-588 |
6.74e-05 |
|
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a 2-fold Rossman fold.
Pssm-ID: 425523 [Multi-domain] Cd Length: 137 Bit Score: 43.71 E-value: 6.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 480 KRIADALLAAKRPLIIAG----TSLGSKALIEAA--ANIAKALKLREKNgsislIVPEANSLGLAMLGGESLDAALQAVT 553
Cdd:pfam00205 2 EKAAELLKKAKRPVILAGggvrRSGASEELRELAekLGIPVVTTLMGKG-----AFPEDHPLYLGMLGMHGTPAANEALE 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1330194573 554 DgsADAIVVLENDLYTRTDSAKVDAALNAAKVVIV 588
Cdd:pfam00205 77 E--ADLVLAVGARFDDIRTTGKLPEFAPDAKIIHI 109
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
225-330 |
7.71e-05 |
|
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: 46.62 E-value: 7.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 225 PSICHGCSSGCNISPGERYGELRRIENRFNGSVNQYFLCDRGRFGYGYVNREDRPRQPL-LADGA----KLSLDEALDKA 299
Cdd:cd02752 1 RTICPYCSVGCGLIAYVQNGVWVHQEGDPDHPVNRGSLCPKGAALRDFVHSPKRLKYPMyRAPGSgkweEISWDEALDEI 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1330194573 300 ADLL---RGRNIVG----------------IGSPRASLESNYALRELVGA 330
Cdd:cd02752 81 ARKMkdiRDASFVEknaagvvvnrpdsiafLGSAKLSNEECYLIRKFARA 130
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
454-611 |
1.10e-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: 45.94 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 454 GFAVAHALDASAPAVEGLDAEAAELAKRIADALLAAKRPLIIAGTSLGSKALIEA-AANIAKALKLreknGSISLIVPEA 532
Cdd:cd02764 283 DFFRALNLAFKPAKVAELTVDLDKALAALAKALAAAGKSLVVAGSELSQTAGADTqVAVNALNSLL----GNDGKTVDHA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 533 N-SLGLAMLGGESLDAALQAVTDGSADAIVVLE-NDLYTRTDSAKVDAALNAAKVVIVADHQKTATSDRAHLVLPAASFA 610
Cdd:cd02764 359 RpIKGGELGNQQDLKALASRINAGKVSALLVYDvNPVYDLPQGLGFAKALEKVPLSVSFGDRLDETAMLCDWVAPMSHGL 438
|
.
gi 1330194573 611 E 611
Cdd:cd02764 439 E 439
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
455-617 |
6.52e-04 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 43.17 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 455 FAVAHALDASAPAVE---GLDAEAAELAkRIADALLAAKRPLIIAGTSLGSKALIEAAANIAKALKLRE-KNGSISLIVP 530
Cdd:PRK05858 167 FSMADDDGRPGALTElpaGPTPDPDALA-RAAGLLAEAQRPVIMAGTDVWWGHAEAALLRLAEELGIPVlMNGMGRGVVP 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 531 EANSLGLAMLGGESLdaalqavtdGSADAIVVLendlytrtdSAKVDAALN------AAKVVIVADhqktATSDRAHLVL 604
Cdd:PRK05858 246 ADHPLAFSRARGKAL---------GEADVVLVV---------GVPMDFRLGfgvfggTAQLVHVDD----APPQRAHHRP 303
|
170
....*....|...
gi 1330194573 605 PAASFAeGDGTLV 617
Cdd:PRK05858 304 VAAGLY-GDLSAI 315
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
437-588 |
2.15e-03 |
|
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439799 [Multi-domain] Cd Length: 548 Bit Score: 41.68 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330194573 437 DIAEECVHAAPDDLArigfavahaLDASAPAVEGldaeAAELAKRIADALLAAKRPLIIAG----TSLGSKALIEAA--A 510
Cdd:COG0028 163 DVQAAEAEEEPAPPE---------LRGYRPRPAP----DPEAIEEAAELLAAAKRPVILAGggarRAGAAEELRALAerL 229
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330194573 511 NIAKALKLREKNgsislIVPEANSLGLAMLGGESLDAALQAVTDgsADAIVVLENDLYTRTdSAKVDAALNAAKVVIV 588
Cdd:COG0028 230 GAPVVTTLMGKG-----AFPEDHPLYLGMLGMHGTPAANEALAE--ADLVLAVGARFDDRV-TGNWDEFAPDAKIIHI 299
|
|
| |
