|
Name |
Accession |
Description |
Interval |
E-value |
| ndhD |
CHL00011 |
NADH dehydrogenase subunit 4 |
91-573 |
0e+00 |
|
NADH dehydrogenase subunit 4
Pssm-ID: 176954 [Multi-domain] Cd Length: 498 Bit Score: 958.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 91 TNYFPWLTIVVVFPIAAGSLIFLFPHRGNKVIRWYSISICLIDLLLTTYAFCYHFQLDDPLIQLTENYKWINFFDFYWRL 170
Cdd:CHL00011 1 MNYFPWLTIIVVLPIFAGSLIFFLPHRGNKVIRWYTLCICLLELLLTTYAFCYHFQLDDPLIQLKEDYKWINFFDFHWRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 171 GIDGLSIGPILLTGFITTLATLAAQPVTREYQLFYFLMLAMYSGQIGPFSSRDILLFFIMWELELIPVYILL-------- 242
Cdd:CHL00011 81 GIDGLSIGPILLTGFITTLATLAAWPVTRNSRLFYFLMLAMYSGQIGLFSSRDLLLFFIMWELELIPVYLLLsmwggkkr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 243 ------FILYTAGGSVFLLMGILGIGLYGSNEPTLNFETLTNQSYPVALEIILYTAFLIAFAVKSPIIPLHTWLPDTHGE 316
Cdd:CHL00011 161 lysatkFILYTAGGSIFLLIGVLGMGLYGSNEPTLNFETLANQSYPVALEILFYIGFLIAYAVKLPIIPLHTWLPDTHGE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 317 AHYSTCMLLAGILLKMGAYGLVRINMELFSHAHSIFCPWLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIILGI 396
Cdd:CHL00011 241 AHYSTCMLLAGILLKMGAYGLIRINMELLPHAHSIFSPWLVIVGAIQIIYAASTSLGQRNLKKRIAYSSVSHMGFIIIGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 397 GSISDTGLNGAILQIISHGFIGAALFFLAGTSYDRLRLLYLDEMGGMAIPMPKIFTIFTILSMASLALPGMSGFVAELIV 476
Cdd:CHL00011 321 GSITDTGLNGAILQIISHGFIGAALFFLAGTSYDRIRLVYLDEMGGIAIPMPKIFTMFSSFSMASLALPGMSGFVAELIV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 477 FFGIITSQKYLFMMKILITFVTAIGMILTPIYLLSILRQMFYGYKFFNTPNSYFFDSGPRELFISISILIPVIGIGIYPD 556
Cdd:CHL00011 401 FFGIITSQKYLLMPKILITFVMAIGMILTPIYLLSMLRQMFYGYKLFNVPNSYFFDSGPRELFISICILLPVIGIGIYPD 480
|
490
....*....|....*..
gi 355505216 557 FIFSFSVDKVEAILANF 573
Cdd:CHL00011 481 FVLSLSVDKVEAILSNY 497
|
|
| PRK02546 |
PRK02546 |
NAD(P)H-quinone oxidoreductase subunit 4; Provisional |
90-555 |
0e+00 |
|
NAD(P)H-quinone oxidoreductase subunit 4; Provisional
Pssm-ID: 235050 [Multi-domain] Cd Length: 525 Bit Score: 564.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 90 MTNYFPWLTIVVVFPIAAGSLIFLFPHRGN-KVIRWYSISICLIDLLLTTYAFCYHFQLDDPLIQLTENYKWINFFDFYW 168
Cdd:PRK02546 2 NLANFPWLTTIILFPIVAALLIPFIPDKGDgKTVRWYALIVGLIDFLITVYAFYTGYDFSNPGLQLVESYSWLPQLGLTW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 169 RLGIDGLSIGPILLTGFITTLATLAAQPVTREYQLFYFLMLAMYSGQIGPFSSRDILLFFIMWELELIPVYILL------ 242
Cdd:PRK02546 82 SVGADGLSMPLILLTGFITTLAVLAAWPVTFKPKLFYFLMLAMYGGQIAVFAVQDMLLFFLAWELELIPVYLLLaiwggk 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 243 --------FILYTAGGSVFLLMGILGIGLYGSNePTLNFETLTNQSYPVALEIILYTAFLIAFAVKSPIIPLHTWLPDTH 314
Cdd:PRK02546 162 krqyaatkFILYTAGSSLFILLAALAMAFYGDT-PTFDMTALAAKDFGLGFQLLCYAGLLIAYGVKLPIVPLHTWLPDAH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 315 GEAHYSTCMLLAGILLKMGAYGLVRINMELFSHAHSIFCPWLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIIL 394
Cdd:PRK02546 241 GEATAPVHMLLAGILLKMGGYALLRMNAGMLPDAHAQFAPLLIVLGVVNIIYAALTSFAQRNLKRKIAYSSISHMGFVLI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 395 GIGSISDTGLNGAILQIISHGFIGAALFFLAGTSYDRLRLLYLDEMGGMAIPMPKIFTIFTILSMASLALPGMSGFVAEL 474
Cdd:PRK02546 321 GIGSFTDLGTSGAMLQMISHGLIGASLFFLVGATYDRTHTLMLDEMGGVGQKMRKMFAMWTACSLASLALPGMSGFVAEL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 475 IVFFGIITSQKYLFMMKILITFVTAIGMILTPIYLLSILRQMFYGYKFFN-TPNSYFFDSGPRELFISISILIPVIGIGI 553
Cdd:PRK02546 401 MVFVGFATSDAYTLPFRVVVVFLAAVGVILTPIYLLSMLREIFFGPENKElVSHEKLVDAEPREVFIIACLLVPIIGIGL 480
|
..
gi 355505216 554 YP 555
Cdd:PRK02546 481 YP 482
|
|
| PRK12561 |
PRK12561 |
NAD(P)H-quinone oxidoreductase subunit 4; Provisional |
119-555 |
0e+00 |
|
NAD(P)H-quinone oxidoreductase subunit 4; Provisional
Pssm-ID: 237137 [Multi-domain] Cd Length: 504 Bit Score: 556.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 119 NKVIRWYSISICLIDLLLTTYAFCYHFQLDDPLIQLTENYKWINFFDFYWRLGIDGLSIGPILLTGFITTLATLAAQPVT 198
Cdd:PRK12561 4 GKTVRWYALGVGLADFALMCYVFWQHYDPSSSSLQLVERYAWLPQIGLEWSLGVDGLSMPLVLLSGLITTLSIFASWKVT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 199 REYQLFYFLMLAMYSGQIGPFSSRDILLFFIMWELELIPVYILL--------------FILYTAGGSVFLLMGILGIGLY 264
Cdd:PRK12561 84 RKPRLFYFLMLVLYSAQIGVFLAQDLLLFFLMWELELVPVYLLIsiwggqkrlyaatkFILYTALASIFILVAGLALALS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 265 GSNePTLNFETLTNQSYPVALEIILYTAFLIAFAVKSPIIPLHTWLPDTHGEAHYSTCMLLAGILLKMGAYGLVRINMEL 344
Cdd:PRK12561 164 GDT-FTFDLAELGAKSYPLALELLLYAGFLIAFGVKLPIFPLHTWLPDAHGEASAPVSMILAGVLLKMGGYALIRFNVQM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 345 FSHAHSIFCPWLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIILGIGSISDTGLNGAILQIISHGFIGAALFFL 424
Cdd:PRK12561 243 LPDAHVYFAPALAILGVVNIIYGALNAFAQDNVKRRLAYSSVSHMGFVLLGIAAFTDLGISGAMLQMISHGLIAAALFFL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 425 AGTSYDRLRLLYLDEMGGMAIPMPKIFTIFTILSMASLALPGMSGFVAELIVFFGIITSQKYLFMMKILITFVTAIGMIL 504
Cdd:PRK12561 323 TGVTYERTHTLSIPNMGGLAKVMPKTFALFTASSMASLALPGMSGFVSELTVFLGITSSDVYSSTFRTITILLAAVGLIL 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 355505216 505 TPIYLLSILRQMFYGYKFFNTP-NSYFFDSGPRELFISISILIPVIGIGIYP 555
Cdd:PRK12561 403 TPIYLLSMLRRVFYGPRSELLPaLAVVEDAKPRELFIALSLLVPIIGIGFYP 454
|
|
| NuoM |
COG1008 |
NADH:ubiquinone oxidoreductase subunit 4 (chain M) [Energy production and conversion]; NADH: ... |
94-573 |
1.12e-162 |
|
NADH:ubiquinone oxidoreductase subunit 4 (chain M) [Energy production and conversion]; NADH:ubiquinone oxidoreductase subunit 4 (chain M) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440632 [Multi-domain] Cd Length: 488 Bit Score: 472.64 E-value: 1.12e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 94 FPWLTIVVVFPIAAGSLIFLFPHRGNKVIRWYSISICLIDLLLTTYAFcYHFQLDDPLIQLTENYKWINFFDFYWRLGID 173
Cdd:COG1008 3 MPLLSLLILLPLLGALLLLLLPRRNARLARWVALAVSLLTLLLSLYLL-AGFDPGTGGFQFVESYPWIPSLGISYHLGVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 174 GLSIGPILLTGFITTLATLAAQPVTREYQ-LFYFLMLAMYSGQIGPFSSRDILLFFIMWELELIPVYILL---------- 242
Cdd:COG1008 82 GISLPLVLLTALLTPLAILASWNEIKKRPkLYYALLLLLEAGMIGVFLALDLFLFYVFWELMLIPMYFLIgiwggerriy 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 243 ----FILYTAGGSVFLLMGILGIGLYgSNEPTLNFETLTNQSYPVALEIILYTAFLIAFAVKSPIIPLHTWLPDTHGEAH 318
Cdd:COG1008 162 aaikFFLYTLAGSLLMLVAILALYFL-AGALTFDIAELAAAPLPLTAQLLLFLAFFIAFAVKVPMFPFHTWLPDAHVEAP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 319 YSTCMLLAGILLKMGAYGLVRINMELFSHAHSIFCPWLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIILGIGS 398
Cdd:COG1008 241 TAGSVLLAGVLLKMGGYGLLRFALPLFPEASAYFAPLLAALGVIGIIYGALVALAQTDLKRLIAYSSVSHMGFVLLGIFA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 399 ISDTGLNGAILQIISHGFIGAALFFLAGTSYDRLRLLYLDEMGGMAIPMPKIFTIFTILSMASLALPGMSGFVAELIVFF 478
Cdd:COG1008 321 LNPLGLQGAVLQMVSHGLITAALFLLVGVLYDRTHTRDIADLGGLAKRMPVLAALFLLAALASLGLPGTSGFVGEFLVLL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 479 GIITSQkylfmmkILITFVTAIGMILTPIYLLSILRQMFYGYkfFNTPNSYFFDSGPRELFISISILIPVIGIGIYPDFI 558
Cdd:COG1008 401 GAFQVN-------PWLAILAALGLILTAAYLLWMYQRVFFGP--LKEELAELPDLNPRELAVLAPLAALILLLGLYPQPL 471
|
490
....*....|....*
gi 355505216 559 FSFSVDKVEAILANF 573
Cdd:COG1008 472 LDLIEPSVEALLARV 486
|
|
| NDH_I_M |
TIGR01972 |
proton-translocating NADH-quinone oxidoreductase, chain M; This model describes the 13th ... |
97-573 |
9.09e-135 |
|
proton-translocating NADH-quinone oxidoreductase, chain M; This model describes the 13th (based on E. coli) structural gene, M, of bacterial NADH dehydrogenase I, as well as chain 4 of the corresponding mitochondrial complex I and of the chloroplast NAD(P)H dehydrogenase complex. [Energy metabolism, Electron transport]
Pssm-ID: 273903 [Multi-domain] Cd Length: 481 Bit Score: 400.85 E-value: 9.09e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 97 LTIVVVFPIAAGSLIFLFPHRGNKVIRWYSISICLIDLLLTTYAFcYHFQLDDPLIQLTENYKWINFFDFYWRLGIDGLS 176
Cdd:TIGR01972 1 LSLLIFLPLIGALLILLLPSNKDGKARWIALVVALATLLLSLLLL-FQFDPTGSGFQFTEDIPWIPALGISYHLGVDGIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 177 IGPILLTGFITTLATLAAQPVTREYQ-LFYFLMLAMYSGQIGPFSSRDILLFFIMWELELIPVYILL------------- 242
Cdd:TIGR01972 80 LLLVLLTALLTLLAILASWESIQKRVkEFYALLLLLEAGVIGVFLALDLFLFYVFWEAMLIPMYLLIgvwggpnriyaam 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 243 -FILYTAGGSVFLLMGIlgIGLYGSNEPTLNFETLTNQSYPVALEIILYTAFLIAFAVKSPIIPLHTWLPDTHGEAHYST 321
Cdd:TIGR01972 160 kFFLYTLAGSLLMLLAI--LGLYFLGGGTFDLLELLNLPLPFGVQTWLFLAFFIAFAVKVPLFPLHTWLPDAHVEAPTAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 322 CMLLAGILLKMGAYGLVRINMELFSHAHSIFCPWLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIILGIGSISD 401
Cdd:TIGR01972 238 SVILAGVLLKMGTYGFLRFNLPLFPDASLYFAPVLAALGVIAIIYGALIALAQTDIKRLIAYSSISHMGFVLLGIFSFNE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 402 TGLNGAILQIISHGFIGAALFFLAGTSYDRLRLLYLDEMGGMAIPMPKIFTIFTILSMASLALPGMSGFVAELIVFFGIi 481
Cdd:TIGR01972 318 LGISGAVFQMISHGLITAALFLLVGVLYERAHTRDIAKYGGLANKMPVLAAFFMLFAMASLGLPGTSGFVGEFLILLGS- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 482 tsqkylFMMKILITFVTAIGMILTPIYLLSILRQMFYGyKFFNTPNSYFFDSGPRELFISISILIPVIGIGIYPDFIFSF 561
Cdd:TIGR01972 397 ------FKVNPVVAFLAALGIVLAAAYMLTLYKRVFFG-ELSNPEVAEFPDLNGREIAVLAPLVVLILFLGLYPNPLLDL 469
|
490
....*....|..
gi 355505216 562 SVDKVEAILANF 573
Cdd:TIGR01972 470 TEPSVNNLLSQV 481
|
|
| PRK05846 |
PRK05846 |
NADH:ubiquinone oxidoreductase subunit M; Reviewed |
94-573 |
1.14e-131 |
|
NADH:ubiquinone oxidoreductase subunit M; Reviewed
Pssm-ID: 235622 [Multi-domain] Cd Length: 497 Bit Score: 393.80 E-value: 1.14e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 94 FPWLTIVVVFPIAAGSLIFLFPHRGNKVIRWYSISICLIDLLLTTYAFCyHFQLDDPLIQLTENYKWINFFDFYWRLGID 173
Cdd:PRK05846 3 WPLLSLLIFLPLIGGLLVLLTERFGARLARWIALIGTLLTLLLSLVLWI-GFDSSNAGFQFVEKHPWIPRFGISYHLGVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 174 GLSIGPILLTGFITTLATLAAQPVTREYQLFYF-LMLAMYSGQIGPFSSRDILLFFIMWELELIPVYILL---------- 242
Cdd:PRK05846 82 GISLLLVVLTALLTPLAVLASWEEIKKRVKFYMaALLWLEGGVIGVFAALDLLLFYVFFEAMLIPMYFLIgvwggknriy 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 243 ----FILYTAGGSVFLLMGILGIGLYGSNEP-TLNFETLTNQSYPVALEIILYTAFLIAFAVKSPIIPLHTWLPDTHGEA 317
Cdd:PRK05846 162 aatkFFLYTLLGSLLMLVAIIYLVVVYYNATgTFDIADLLNLPLPPGVQYWLFLAFFIAFAVKMPMFPLHTWLPDAHVQA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 318 HYSTCMLLAGILLKMGAYGLVRINMELFSHAHSIFCPWLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIILGIG 397
Cdd:PRK05846 242 PTAGSVLLAGILLKMGAYGLLRFSLPLFPDASHEFAPIIITLGVIAIIYGALVALAQTDIKKLIAYSSISHMGFVTLGIF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 398 SISDTGLNGAILQIISHGFIGAALFFLAGTSYDRLRLLYLDEMGGMAIPMPKIFTIFTILSMASLALPGMSGFVAELIVF 477
Cdd:PRK05846 322 AGNQLGIQGAIFQMISHGLSSAALFLLVGVLYDRLHTRDIADYGGLAKVMPVLAAFFLFFAMASLGLPGTSGFVGEFLIL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 478 FGiitsqkyLFMMKILITFVTAIGMILTPIYLLSILRQMFYGYKffNTPNSYFFDSGPRELFISISILIPVIGIGIYPDF 557
Cdd:PRK05846 402 LG-------SFQVNPVIAFIATTGLILAAVYSLWLYQRVMFGPV--KNEVAKLKDLNGRELLILLPLVALLLLLGVYPKP 472
|
490
....*....|....*.
gi 355505216 558 IFSFSVDKVEAILANF 573
Cdd:PRK05846 473 LLDVIHPSVENLLQWV 488
|
|
| PRK06473 |
PRK06473 |
NADH-quinone oxidoreductase subunit M; |
97-551 |
5.20e-83 |
|
NADH-quinone oxidoreductase subunit M;
Pssm-ID: 235810 [Multi-domain] Cd Length: 500 Bit Score: 268.11 E-value: 5.20e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 97 LTIVVVFPIAAGSLIFLFPHRGN-KVIRWYSISICLIDLLLTTyAFCYHFQLDDPLIQLTENYKWINFFDFYWRLGIDGL 175
Cdd:PRK06473 2 LSALIWIPLLGAILIGFWPSGINgKLARSVALVIASVLLLLSL-VLAFQFDPGNPNQQFTEFIPWIDSLGLSYHLGVDGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 176 SIGPILLTGFITTLATLAAQPVTREYQLFYFLMLAMYSGQIGPFSSRDILLFFIMWELELIPVYILL------------- 242
Cdd:PRK06473 81 SLPLLVLNSLLTLIAIYSSDESIQRPRFYYSLLLLLNAGVSGAFLAQDLLLFFLFYELELIPLYLLIaiwggqrrgyaat 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 243 -FILYTAGGSVFLLMGILGIGlYGSNEPTLNFETLTNQSYPVALEIILYTAFLIAFAVKSPIIPLHTWLPDTHGEAHYST 321
Cdd:PRK06473 161 kFLLYTAISGILILVSFLGLV-WLSGASSFDYEPLRSHTLPLSTQLLLLAPILVGFGIKIPLVPFHTWLPDAHVEASTPV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 322 CMLLAGILLKMGAYGLVRINMELFSHAHSIFCPWLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIILGIGSISD 401
Cdd:PRK06473 240 SVLLAGVLLKLGTYGLLRFGVGLFPEAWVYLAPWLATWAVVSVLYGASCAIAQKDMKKMVAYSSIGHMGYILLAAAAATP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 402 TGLNGAILQIISHGFIGAALFFLAGTSYDRLRLLYLDEMGGMAIP---MPKIFTIFTILSMASLALPGMSGFVAELIVF- 477
Cdd:PRK06473 320 LSILAAVFQMISHGLISALLFLLVGVVYKKTGSRDVDVLRGLLNPergLPITGSLMILGVMASAGIPGMVGFIAEFLVFr 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 355505216 478 --FGIITSQKYLFMmkilitfvtaIGMILTPIYLLSILRQMFYGY---KFFNTPNSYFFDSGPRelfISISILIPVIGI 551
Cdd:PRK06473 400 gsFPIFPVQTLLCM----------IGTGLTAVYFLLLVNRVFFGRltaELSNLPRVLWSERLPA---LVLAVLIVVLGI 465
|
|
| PRK07363 |
PRK07363 |
NADH-quinone oxidoreductase subunit M; |
97-479 |
1.06e-71 |
|
NADH-quinone oxidoreductase subunit M;
Pssm-ID: 180945 [Multi-domain] Cd Length: 501 Bit Score: 238.46 E-value: 1.06e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 97 LTIVVVFPIAAGSLIFLFPhRGNKVIRWYSISICLIDLLLTTYAFC-YHFQLDDPLIQLTENYKWINFFDFYWRLGIDGL 175
Cdd:PRK07363 2 LSVLLWLPILGAIIIGFFP-GNLPSARLRQITLVFAVLVLAWSLFLlTQFDLSDPGMQFQEYLPWNEPLGLSYSLGVDGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 176 SIGPILLTGFITTLATLAAQPVTREYQLFYFLMLAMYSGQIGPFSSRDILLFFIMWELELIPVYILL------------- 242
Cdd:PRK07363 81 SLPLLVLNSLLTWIAIYSIGENTERPRLYYSLILLINGGIAGALLAQNLLLFFLFYELELIPFYLLIaiwggekrgyasi 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 243 -FILYTAGGSVFLLMGILGIGLYgSNEPTLNFETLTNQSYPVALEIILYTAFLIAFAVKSPIIPLHTWLPDTHGEAHYST 321
Cdd:PRK07363 161 kFLIYTAVSGLLVLAAFLGIVWL-SGSTSFDYDAISTQNLSLNTQLILLTGLLLGFGIKIPLVPLHTWLPDAYTEASPAV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 322 CMLLAGILLKMGAYGLVRINMELFSHAHSIFCPWLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIILGIGSISD 401
Cdd:PRK07363 240 AILLGGVLAKLGTYGLLRFGLQLFPQTWSLVAPGLAIIGTISVIYGALSAIAQKDIKRMVAYSSIGHMGYILVAAAAGTQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 402 TGLNGAILQIISHGFIGAALFFLAGTSYDRLRLLYLDEMGGMAIP---MPKIFTIFTILSMASLALPGMSGFVAELIVFF 478
Cdd:PRK07363 320 LSLLGAVAQMISHGLILALLFHLVGIVERKVGTRDLDVLNGLMNPirgLPLTSALLVLAGMASAGIPGLVGFVAEFIVFQ 399
|
.
gi 355505216 479 G 479
Cdd:PRK07363 400 G 400
|
|
| HyfB |
COG0651 |
Formate hydrogenlyase subunit 3/Multisubunit Na+/H+ antiporter, MnhD subunit [Energy ... |
96-503 |
3.17e-64 |
|
Formate hydrogenlyase subunit 3/Multisubunit Na+/H+ antiporter, MnhD subunit [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 440416 [Multi-domain] Cd Length: 430 Bit Score: 216.55 E-value: 3.17e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 96 WLTIVVVFPIAAGSLIFLFPHRGnKVIRWYSISICLIDLLLTTYAFCYHFQLDDPLIQLTEnykWINFFDFYwrLGIDGL 175
Cdd:COG0651 4 LLILPVLLPLLAAALLLLLGRRR-RLQRALSLLASLALLALALALLLQVLAGGPLVYALGG---WPAPFGIV--LVADRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 176 SIGPILLTGFITTLATLAAQPVTREYQ---LFYFLMLAMYSGQIGPFSSRDILLFFIMWELELIPVYILL---------- 242
Cdd:COG0651 78 SALFLLLTALVALAVLLYSIGYMRHERrgrRFYPLFLLLLAGMNGAFLTGDLFNLFVFFEVMLLASYGLValggtkealr 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 243 ----FILYTAGGSVFLLMGIlgIGLYGSNePTLNFETLTN--QSYPVALEIILYTAFLIAFAVKSPIIPLHTWLPDTHGE 316
Cdd:COG0651 158 aglkYLILNLVGSALFLLGV--GLLYGAT-GTLNMADLAArlAELDPGLLLAAFALLLVGFGIKAALFPLHFWLPDAYPA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 317 AHYSTCMLLAGILLKMGAYGLVRINMELFSHAHSIFC-PWLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIILG 395
Cdd:COG0651 235 APSPVSALLSGLLTKVGVYAILRVLTLLFGADPALFLgTLLLVLGLLTMLVGALGALAQRDLKRLLAYSSVSQIGYILLG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 396 IGSISDTGLNGAILQIISHGFIGAALFFLAGTSYDRLRLLYLDEMGGMAIPMPKIFTIFTILSMASLALPGMSGFVAELI 475
Cdd:COG0651 315 LGLGTPLGLAGALFHLLNHALAKALLFLAAGAIERATGTRDLDKLGGLGKRMPLTAAAFLIGALALAGLPPLSGFVSKWL 394
|
410 420
....*....|....*....|....*....
gi 355505216 476 VFFGIITSQKYLFMMKILIT-FVTAIGMI 503
Cdd:COG0651 395 LLQAALEAGAWLLAAVLLLSsLLTLAYFV 423
|
|
| psaC |
CHL00065 |
photosystem I subunit VII |
1-81 |
1.00e-63 |
|
photosystem I subunit VII
Pssm-ID: 177005 [Multi-domain] Cd Length: 81 Bit Score: 203.07 E-value: 1.00e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 1 MSHSVKIYDTCIGCTQCVRACPTDVLEMIPWDGCKAKQIASAPRTEDCVGCKRCESACPTDFLSVRVYLGPETTRSMARA 80
Cdd:CHL00065 1 MSHSVKIYDTCIGCTQCVRACPTDVLEMIPWDGCKAKQIASAPRTEDCVGCKRCESACPTDFLSVRVYLGHETTRSMGLA 80
|
.
gi 355505216 81 F 81
Cdd:CHL00065 81 Y 81
|
|
| PS_I_psaC |
TIGR03048 |
photosystem I iron-sulfur protein PsaC; Members of this family are PsaC, an essential ... |
2-81 |
1.70e-61 |
|
photosystem I iron-sulfur protein PsaC; Members of this family are PsaC, an essential component of photosystem I (PS-I) reaction center in Cyanobacteria and chloroplasts. This small protein, about 80 amino acids in length, contains two copies of the ferredoxin-like 4Fe-4S binding site (pfam00037) and therefore eight conserved Cys residues. This protein is also called photosystem I subunit VII. [Energy metabolism, Photosynthesis]
Pssm-ID: 132092 [Multi-domain] Cd Length: 80 Bit Score: 197.43 E-value: 1.70e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 2 SHSVKIYDTCIGCTQCVRACPTDVLEMIPWDGCKAKQIASAPRTEDCVGCKRCESACPTDFLSVRVYLGPETTRSMARAF 81
Cdd:TIGR03048 1 AHSVKIYDTCIGCTQCVRACPTDVLEMVPWDGCKAGQIASAPRTEDCVGCKRCESACPTDFLSVRVYLGAETTRSMGLAY 80
|
|
| ND4 |
MTH00204 |
NADH dehydrogenase subunit 4; Provisional |
96-558 |
8.34e-58 |
|
NADH dehydrogenase subunit 4; Provisional
Pssm-ID: 164750 [Multi-domain] Cd Length: 485 Bit Score: 201.06 E-value: 8.34e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 96 WLTIVVVFPIAAGSLIFLFPHRGNKVIRWYSISICLIDLLLTTYAFCYHFQldDPLIQLTENYKWI--NFFDFYWR---L 170
Cdd:MTH00204 2 GLSLIFLILFMGIINVMGVPRENSVKLKKRALEWSLAILFSTLVLWGAFDG--EGQFQFINLIEWIisPTLNFQWGplvF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 171 GIDGLSIGPILLTGFITTLATLAAQPVTRE-YQLFYFLMLAMYSGQIGPFSSRDILLFFIMWELELIPVYILL------- 242
Cdd:MTH00204 80 AVDGVSLFFILLTTLLIPICILISWKSIKFlFKEFLLCLLFLEVLLIGVFSVLDLLLFYILFEGILIPMFLLIgiwgsre 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 243 --------FILYTAGGSVFLLMGILGIGlygSNEPTLNFETLTNQSYPVALEIILYTAFLIAFAVKSPIIPLHTWLPDTH 314
Cdd:MTH00204 160 ekvrasyyFFFYTFAGSVFMLLGIFQLY---SITGTTDYQILLNIKLPLSIQKWLLVGFFLSLAVKIPQIPFHIWLPQAH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 315 GEAHYSTCMLLAGILLKMGAYGLVRINMELFSHAHSIFCPWLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIIL 394
Cdd:MTH00204 237 VEAPVAGSVILAGILLKLGGYGFLRFSWPLFPAASEYFAPLIVMLSVIAVIYGSLTTCRQVDFKRLIAYSSVAHMGLVPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 395 GIGSISDTGLNGAILQIISHGFIGAALFFLAGTSYDRLRLLYLDEMGGMAIPMPKIFTIFTILSMASLALPGMSGFVAEl 474
Cdd:MTH00204 317 GLFTHTIEGLVAAVFLMLAHGFVSSALFIAVTFLYERHHTRLIKYYRGLTLTMPLFVIIMLVLSLANMGFPLSCNFVGE- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 475 ivFFGIITSQKYLFMMKILITFvtaiGMILTPIYLLSILRQMFYGYkffntPNSYFF---DSGPRELFISISILIPVIGI 551
Cdd:MTH00204 396 --FFSLLAAFEYSLGLGVLVTS----GMVWSAAYSLYLYNRISFGG-----GSNYLLfsrDLNRRELLAILPLIIAIFLL 464
|
....*..
gi 355505216 552 GIYPDFI 558
Cdd:MTH00204 465 GIVPFII 471
|
|
| PLN00071 |
PLN00071 |
photosystem I subunit VII; Provisional |
1-81 |
2.23e-57 |
|
photosystem I subunit VII; Provisional
Pssm-ID: 177700 [Multi-domain] Cd Length: 81 Bit Score: 186.69 E-value: 2.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 1 MSHSVKIYDTCIGCTQCVRACPTDVLEMIPWDGCKAKQIASAPRTEDCVGCKRCESACPTDFLSVRVYLGPETTRSMARA 80
Cdd:PLN00071 1 MSHPVKIYDTCIGCTQCVRACPTDVLEMIPWDGCKAKQIASAPRTEDCVGCKRCESACPTDFLSVRVYLGHETTRSIGLA 80
|
.
gi 355505216 81 F 81
Cdd:PLN00071 81 Y 81
|
|
| ND4 |
MTH00217 |
NADH dehydrogenase subunit 4; Provisional |
97-558 |
5.49e-50 |
|
NADH dehydrogenase subunit 4; Provisional
Pssm-ID: 214462 [Multi-domain] Cd Length: 482 Bit Score: 179.48 E-value: 5.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 97 LTIVVVFPIAAGSLIFLFPHrgNKVIRWYSISICLIDLLLTTYAFCYHFQLDDPLIQLTENYKWINFFDFYWR---LGID 173
Cdd:MTH00217 2 LELVFILPLIGILHLLIIPR--DNIVRLKKIALEWSLLTLTATILLWASFDGEGQFQAIKKFEWIPGIEPVFGpvvFAVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 174 GLSIGPILLTGFITTLATL----AAQPVTREYQLFYFLMLAMYsgqIGPFSSRDILLFFIMWELELIPVYILL------- 242
Cdd:MTH00217 80 GISIFFLILTALLTPICILiswnSIKFLIKEFLLCLLVIEILL---MGVFTILDLVGFYILFEGILIPMFLIIgiwgsre 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 243 --------FILYTAGGSVFLLMGIlgIGLYgSNEPTLNFETLTNQSYPVALEIILYTAFLIAFAVKSPIIPLHTWLPDTH 314
Cdd:MTH00217 157 ekvqasyyFFFYTFIGSVFMLLGI--FTLY-SYAGTTDYQALCCLKIEKELQYFIFLGFFLSLAIKIPKIPFHIWLPQAH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 315 GEAHYSTCMLLAGILLKMGAYGLVRINMELFSHAHSIFCPWLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIIL 394
Cdd:MTH00217 234 VEAPVAGSVILAGVLLKLGGYGFIRFSWPLLPEASEYFSPLIQTLSLLAIIYGSLTTCRQVDLKRIIAYSSVAHMGLVTL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 395 GIGSISDTGLNGAILQIISHGFIGAALFFLAGTSYDRLRLLYLDEMGGMAIPMPKIFTIFTILSMASLALPGMSGFVAEl 474
Cdd:MTH00217 314 GIFSHTIQGLVAAIFLMLAHGLVSSALFIAVTFLYERHHTRLIKYYRGMVITMPLFGILMLLLVLANASIPLSCNFVGE- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 475 ivFFGIITSQKYLFMMKILitfvTAIGMILTPIYLLSIlrqmfYGYKFFNTPNSYFF---DSGPRELFISISILIPVIGI 551
Cdd:MTH00217 393 --FLSLLAAFEYSYIVGVL----ASLGMVLSAGYSIYL-----YNRVCFGAPSKYLYfsrDLNRREFYVLLPLVFLIYLM 461
|
....*..
gi 355505216 552 GIYPDFI 558
Cdd:MTH00217 462 GIFPFII 468
|
|
| ND4 |
MTH00206 |
NADH dehydrogenase subunit 4; Provisional |
110-558 |
5.75e-47 |
|
NADH dehydrogenase subunit 4; Provisional
Pssm-ID: 214458 [Multi-domain] Cd Length: 450 Bit Score: 170.51 E-value: 5.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 110 LIFLFPHRGNKVIRWYSISICLIDLLLTTYAFCYHfqlddpliQLTENYKWINFFDFywrLGIDGLSIGPILLT------ 183
Cdd:MTH00206 6 LIMLLLMTILSKKKWLWRSTTFFSFLIALLFLLWF--------KWSSEVGWSFSNLY---LSYDPLSSPLVILScwllpl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 184 GFITTLATLAAQPVTREyQLFYFLMLAMYSGQIGPFSSRDILLFFIMWELELIPVYILL---------------FILYTA 248
Cdd:MTH00206 75 MFLASQNHMKNEPINRQ-RIYITLLIVLQLFLILFFSSSNLLLFYILFEASLIPTLLLItrwgnqkerlnagyyFLFYTL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 249 GGSVFLLMGILGIGLYGSNEPTLNFETLTNQSYpvaLEIILYTAFLIAFAVKSPIIPLHTWLPDTHGEAHYSTCMLLAGI 328
Cdd:MTH00206 154 IGSLPLLIALLFLQNSLGSLSLYILYFSKLTTW---NNNLWWLACILAFLVKLPLYGVHLWLPKAHVEAPVAGSMVLAGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 329 LLKMGAYGLVRINMELFSHAHSIFCPwLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIILGIGSISDTGLNGAI 408
Cdd:MTH00206 231 LLKLGGYGMMRIILILGPSTKLSSYF-FIILGLWGSIMTSSICLRQTDLKSLIAYSSVSHMSLVTAGILSGSPWGFKGAL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 409 LQIISHGFIGAALFFLAGTSYDRL--RLLYLdeMGGMAIPMPKIFTIFTILSMASLALPGMSGFVAELIVFFGIITSQKY 486
Cdd:MTH00206 310 LLMIAHGLVSSALFCLANLLYERShtRTILG--NRGLQMILPLLSFWWLLFFLANLGLPPFPNLFGELLIITSLFSWSNF 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 355505216 487 LFmmkilitFVTAIGMILTPIYLLSILRQMFYGYKFFNTPNSYFfdSGPRELFISISILIPVIGIGIYPDFI 558
Cdd:MTH00206 388 TL-------PLLGLGFLFTAIYSLYMFVMTQHGKTPNHLLSLSP--SSTREHLLLFLHLFPVILLILNPNLI 450
|
|
| PRK08375 |
PRK08375 |
putative monovalent cation/H+ antiporter subunit D; Reviewed |
170-562 |
7.38e-46 |
|
putative monovalent cation/H+ antiporter subunit D; Reviewed
Pssm-ID: 236251 [Multi-domain] Cd Length: 487 Bit Score: 168.52 E-value: 7.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 170 LGIDGLSIGPILLTGFITTLATLAAQPVTREYQ-LFYFLMLAMYSGQIGPFSSRDILLFFIMWELELIPVYILL------ 242
Cdd:PRK08375 73 LRADSLSALFLLVTSILAIAALLYAIGYGEHRQtRFYALFLLLLAGLLGALLTADLFNLFVFLEIMSLSSYALVamggdr 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 243 --------FILYTAGGSVFLLMGIlgIGLYGSNEpTLNFETLTNQSYPVALEIILYTAFLIAFAVKSPIIPLHTWLPDTH 314
Cdd:PRK08375 153 ralaaarkYLIVGLIGSTFLLIGV--GLLYGVTG-TLNMADLAGALAENPTVVTAFGFVLLALALKAAVFPLHTWLPRAY 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 315 GEAHYSTCMLLAGILLKMGAYGLVRINMELFSHAHSIFCPW---LMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGF 391
Cdd:PRK08375 230 PAAPPVVTALLSGLVTKVAVYALIRIYFTVFGGDFRFALGLgwlLAVLALLSMLVGSLAALGQDDVKRVLAYSTVSQMGY 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 392 IILGIGSISDTGLNGAILQIISHGFIGAALFFLAGTSYDRLRLLYLDEMGGMAIPMPKIFTIFTILSMASLALPGMSGFV 471
Cdd:PRK08375 310 ILLGLALLTPLALAAGLLHLLHHALMKGALFLAAGAIEVTYGTRRLSELSGLGRRMPLTAAAFAVASLSLIGVPPTSGFV 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 472 AELIVFFGIITSQKYLFMMKILitfvtaIGMILTPIYLLSILRQMFYGyKFFNTPNSYFFDSGPRELFISISILIPVIGI 551
Cdd:PRK08375 390 SKWYLVVGAVEAGQWLVLAVLL------ASSLLALLYFLRIWYRAFFG-PPPPGSEAPKQEAPLGMLAPSLALALLSLLL 462
|
410
....*....|.
gi 355505216 552 GIYPDFIFSFS 562
Cdd:PRK08375 463 GIYAGPLLQLA 473
|
|
| ND4 |
MTH00044 |
NADH dehydrogenase subunit 4; Validated |
151-559 |
1.84e-43 |
|
NADH dehydrogenase subunit 4; Validated
Pssm-ID: 214411 [Multi-domain] Cd Length: 458 Bit Score: 161.30 E-value: 1.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 151 LIQLTENYKWINFFdfyWRLGIDGLSIGPILLTGFITTLATLAAQPVTREY-----QLFYFLMLAMYSGQIGPFSSRDIL 225
Cdd:MTH00044 41 LLNNHWSSSWHNLS---LSLATDSLSSPLIILSCWLAPLSLLASINHLSNNspnnqRTFISLIIIILTALIITFSSLELI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 226 LFFIMWELELIPVYILL---------------FILYTAGGSVFLLMGILGIGLYGSNEPTLNFETLTNQSYPVALEIILY 290
Cdd:MTH00044 118 LFYIAFETTLIPTLILItrwgaqkeriqaglyFLFYTLFGSLPLLISLIAIYSSSSSLSIPLSELNWLTSLSSNSSSIWW 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 291 TAFLIAFAVKSPIIPLHTWLPDTHGEAHYSTCMLLAGILLKMGAYGLVR-------INMELFSHAHSIFCPWLMILGSIq 363
Cdd:MTH00044 198 IFCILAFLVKMPIYGFHLWLPKAHVEAPVAGSMILAAILLKLGGYGLIRlinlfslPSANNISFILIVFCCWGALITSI- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 364 iiyaasTSFGQRNLKKRIAYSSVSHMGFIILGIGSISDTGLNGAILQIISHGFIGAALFFLAGTSYDRLRLLYLDEMGGM 443
Cdd:MTH00044 277 ------ICLRQTDLKALIAYSSVGHMSLVAAGIFSGTNWGINGALILMIAHGLVSSALFCLANILYERSGTRTLSITRGF 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 444 AIPMPKIFTIFTILSMASLALPGMSGFVAELIVFFGIITsqkylfmMKILITFVTAIGMILTPIYLLSILrQMFYGYKFF 523
Cdd:MTH00044 351 KLITPLLPLWWLIFCAANLGLPPLPNLIGELLIISSIIS-------WSILSFPIIGLATVFGAIYSLLIY-QLTNSGSFP 422
|
410 420 430
....*....|....*....|....*....|....*.
gi 355505216 524 NTpNSYFFDSGPRELFISISILIPVIGIGIYPDFIF 559
Cdd:MTH00044 423 SW-ISNVSPISSREHLLIFLHLLPLILIIINPNIIL 457
|
|
| ND4 |
MTH00150 |
NADH dehydrogenase subunit 4; Provisional |
170-499 |
1.90e-43 |
|
NADH dehydrogenase subunit 4; Provisional
Pssm-ID: 214435 [Multi-domain] Cd Length: 417 Bit Score: 160.00 E-value: 1.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 170 LGIDGLSIGPILLTGFITTLATLAAQP---VTREYQLFYFLMLAMYSGQIGPFSSRDILLFFIMWELELIPVYILLFI-- 244
Cdd:MTH00150 20 FSVDSMSSLLISLSLWISGLMMLASQKsvkLRNKSSSFSLLVLLLCLILVLAFSVSSLLMFYFFFEASLIPTLLLILGwg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 245 -------------LYTAGGSVFLLMGILGIGL-YGSNEPTLNFETLTNQSYPVALEIILYTAFLiafaVKSPIIPLHTWL 310
Cdd:MTH00150 100 yqperlqagmymmLYTVGASLPLLLVILWMSSsYGSSFMLLISSLRKLLSSMGLWGLLVFLAFL----VKLPMYPFHLWL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 311 PDTHGEAHYSTCMLLAGILLKMGAYGLVRINMeLFSHAHSIFCPWLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMG 390
Cdd:MTH00150 176 PKAHVEAPVAGSMILAGILLKLGGYGILRMMM-VFSLSSSSFSIFLISLSLWGGVLTSLICLRQSDVKSLIAYSSVGHMS 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 391 FIILGIGSISDTGLNGAILQIISHGFIGAALFFLAGTSYDRL--RLLYLdeMGGMAIPMPKIFTIFTILSMASLALPGMS 468
Cdd:MTH00150 255 LVLAGVLSNTSWGWVGALIMMVSHGFCSSGLFCLANYTYEKVhsRSLFL--SKGMLMLYPSLSLWWFLFCIINMAAPPSL 332
|
330 340 350
....*....|....*....|....*....|.
gi 355505216 469 GFVAELIVFFGIITSQKYLFMMKILITFVTA 499
Cdd:MTH00150 333 NLLSEIMIFPSLISYSPWFFVPLGLMVFLSG 363
|
|
| ND4 |
MTH00226 |
NADH dehydrogenase subunit 4; Provisional |
170-559 |
2.07e-42 |
|
NADH dehydrogenase subunit 4; Provisional
Pssm-ID: 214466 [Multi-domain] Cd Length: 505 Bit Score: 159.32 E-value: 2.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 170 LGIDGLSIGPILLTGFITTLATLAA-QPVTREYQLFYFLMLAMYSGQIGPFSSRDILLFFIMWELELIPVYILL------ 242
Cdd:MTH00226 98 FAVDGISIYFIILTGFIVPCSILISwHSVKYLTKSFLICMLILEFLLYAVFSVLDIFMFYILFEGVLIPMYLILgiwgsr 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 243 ---------FILYTAGGSVFLLMGILGI-GLYGsnepTLNFETLTNQSY--PVALEIILYTAFLIAFAVKSPIIPLHTWL 310
Cdd:MTH00226 178 eekmqaayyFFFYTLIGSVLMLLCLFSLyNIHG----TTDYLTLASCSHvvSEQTQKWIFLGIFLAMAVKIPIFPFHIWL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 311 PDTHGEAHYSTCMLLAGILLKMGAYGLVRINMELFSHAHSIFCPWLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMG 390
Cdd:MTH00226 254 PKAHVEAPVAGSVLLAGILLKLGGYGLVRLSWPILPLGAQNLAPAVIAMGIVGIVYGSFATCRQIDVKRLVAYSSVAHMG 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 391 FIILGIGSISDTGLNGAILQIISHGFIGAALFFLAGTSYDRLRLLYLDEMGGMAIPMPKIFTIFTILSMASLALPGMSGF 470
Cdd:MTH00226 334 LVSITLVTHDIIGLTGSIFIMLAHGIVSSLLFILVTILYDRHHTRLIKYYRGLSITMPIWGTIMIVTSLANVAVPPSGNF 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 471 VAElivFFGIITSqkylFMMKILITFVTAIGMILTPIYLLSILRQMFYGYKffNTPNSYFFDSGPRELFISISILIPVIG 550
Cdd:MTH00226 414 IGE---YLSILSS----FNWNPIIGVFVCSGVILSAVYSFYFANRVTFGAP--GNLITFARDVNRREFYITASMVFFAFL 484
|
....*....
gi 355505216 551 IGIYPDFIF 559
Cdd:MTH00226 485 IGIYPIFIL 493
|
|
| ND4 |
MTH00163 |
NADH dehydrogenase subunit 4; Provisional |
151-559 |
6.49e-42 |
|
NADH dehydrogenase subunit 4; Provisional
Pssm-ID: 214443 [Multi-domain] Cd Length: 445 Bit Score: 156.47 E-value: 6.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 151 LIQLTENYKWINFFDFYWRLGIDGLSIGPILLTGFITTLATLAAQPVTR---EYQLFYFLMLAMYSGQIGPFSSRDILLF 227
Cdd:MTH00163 33 FLFMLLFSLSFYFSNISYFFGLDLLSFGLILLSFWICMLMILSSESVYKknnYSNLFLFLILFLLIFLLLTFSSMNLLLF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 228 FIMWELELIPVYILLF---------------ILYTAGGSVFLLMGILgigLYGSNEPTLNFETLTNQSYpvaLEIILYTA 292
Cdd:MTH00163 113 YIFFESSLIPTLFLILgwgyqperlqagiylLFYTLFASLPLLVGIF---YLYNNSGSLSFFLLNFFGS---LNFLWYLS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 293 FLIAFAVKSPIIPLHTWLPDTHGEAHYSTCMLLAGILLKMGAYGLVRInMELFSHAHSIFCPWLMILGSIQIIYAASTSF 372
Cdd:MTH00163 187 MILAFLVKMPMFFVHLWLPKAHVEAPVSGSMILAGVLLKLGGYGLLRV-MSFFSKLGLKFNYIWISISLVGGVIVSLICL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 373 GQRNLKKRIAYSSVSHMGFIILGIGSISDTGLNGAILQIISHGFIGAALFFLAGTSYDRL--RLLYLDEmgGMAIPMPKI 450
Cdd:MTH00163 266 RQVDLKSLIAYSSVAHMGLVLGGLMTFSYWGLMGSLLMMIGHGLCSSGLFCLANIIYERLgsRSLLINK--GLLNFMPSM 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 451 FTIFTILSMASLALPGMSGFVAELIVFFGIITSQKYLFMMKILITFVTAigmiLTPIYLLSIlrqMFYGYKFFNTPNSYF 530
Cdd:MTH00163 344 SLWWFLLSSSNMAAPPSLNLLGEISLINSLISWSKLSMIFLMLLSFFSA----AYSLYLYSY---SQHGKYYSGLYSCSS 416
|
410 420
....*....|....*....|....*....
gi 355505216 531 FDSgpRELFISISILIPVIGIGIYPDFIF 559
Cdd:MTH00163 417 GKV--REYLLLFLHWLPLNLLILKSDLFM 443
|
|
| ND4 |
MTH00124 |
NADH dehydrogenase subunit 4; Provisional |
185-513 |
1.25e-41 |
|
NADH dehydrogenase subunit 4; Provisional
Pssm-ID: 214427 [Multi-domain] Cd Length: 457 Bit Score: 156.12 E-value: 1.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 185 FITTLATLaaQPvtreyqlfyFLMLAmysgqigpFSSRDILLFFIMWELELIPVYILL---------------FILYTAG 249
Cdd:MTH00124 95 FLTTLILL--QT---------FLILA--------FSATELTLFYIMFEATLIPTLILItrwgnqperlsagtyFLFYTLI 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 250 GSVFLLMGILGIGLYgSNEPTLNFETLTNQSYPVAL-EIILYTAFLIAFAVKSPIIPLHTWLPDTHGEAHYSTCMLLAGI 328
Cdd:MTH00124 156 SSLPLLIAILYLHNQ-TGTLSLPMLQLTHPTLTNSWtNLLLWLACLMAFMVKMPLYGLHLWLPKAHVEAPIAGSMVLAAI 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 329 LLKMGAYGLVRINMELFSHAHSIFCPwLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIILGIGSISDTGLNGAI 408
Cdd:MTH00124 235 LLKLGGYGIIRITLLLPPLSNTLHYP-FLTLALWGALMTSLICLRQTDLKSLIAYSSVSHMGLVIAATMIQTPWSLSGAM 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 409 LQIISHGFIGAALFFLAGTSYDRL--RLLYLdeMGGMAIPMPKIFTIFTILSMASLALPGMSGFVAELIvffgIITSqky 486
Cdd:MTH00124 314 ILMIAHGLTSSMLFCLANTNYERThsRTLLL--TRGLQLLLPLMTTWWLLANLTNMALPPTINLMGELT----IMTS--- 384
|
330 340
....*....|....*....|....*..
gi 355505216 487 LFMMKILITFVTAIGMILTPIYLLSIL 513
Cdd:MTH00124 385 LFNWSPTTIILTGLATLITASYTLYMF 411
|
|
| Proton_antipo_M |
pfam00361 |
Proton-conducting membrane transporter; This is a family of membrane transporters that ... |
221-495 |
1.36e-41 |
|
Proton-conducting membrane transporter; This is a family of membrane transporters that inlcudes some 7 of potentially 14-16 TM regions. In many instances the family forms part of complex I that catalyzes the transfer of two electrons from NADH to ubiquinone in a reaction that is associated with proton translocation across the membrane, and in this context is a combination predominantly of subunits 2, 4, 5, 14, L, M and N. In many bacterial species these proteins are probable stand-alone transporters not coupled with oxidoreduction. The family in total represents homologs across the phyla.
Pssm-ID: 425636 [Multi-domain] Cd Length: 291 Bit Score: 151.70 E-value: 1.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 221 SRDILLFFIMWELELIPVYIL---------------LFILYTAGGSVFLLMGILGIGLYGSnepTLNFETLTNQSYPVAL 285
Cdd:pfam00361 1 ANDLLLMYLGWEAVLLPSYLLigywgksprsseagmKYFLLTLLGSSILLFGISLMYNYTG---TLSFDELSKALTGGLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 286 EI---ILYTAFLIAFAVKSPIIPLHTWLPDTHGEAHYSTCMLLAGILLKMGAYGLVRINMeLFSHAHSIFCPWLMILGSI 362
Cdd:pfam00361 78 SSgllLLFLLILVGFLFKSAQVPFHTWLPDAYEGAPTPVSALLAATLVKAGGYGLIRRSL-LYLPSSPFIQQILLILAII 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 363 QIIYAASTSFGQRNLKKRIAYSSVSHMGFIILGIGSISDTGLNGAILQIISHGFIGAALFFLAG-TSYDRLRLLYLDEMG 441
Cdd:pfam00361 157 SMLLGSLAALVQTDIKRLLAYSSISHMGYMLIALGAGTIYGIQAAIFHLLTHGLFSAGLFLCAGsVIYRRVHTRNIRDYG 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 355505216 442 GMAIPMPKIFTIFTILSMASLALPGMSGFVAELIVFFGIITSQKYLFMMKILIT 495
Cdd:pfam00361 237 GLAKTMPILALVFLVAMLSLAGLPPTAGFLGKFLILAAAVAASWIFLVLAGVVG 290
|
|
| ND4 |
MTH00068 |
NADH dehydrogenase subunit 4; Provisional |
170-510 |
9.14e-40 |
|
NADH dehydrogenase subunit 4; Provisional
Pssm-ID: 214417 [Multi-domain] Cd Length: 458 Bit Score: 150.84 E-value: 9.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 170 LGIDGLSIGPILLTGFITTLATLAAQ------PVTReyQLFYFLMLAMYS-GQIGPFSSRDILLFFIMWELELIPVYILL 242
Cdd:MTH00068 56 FGIDQISSPLLILTCWLLPLMILASQnhlknePINR--QRTYISMLIILQlTLILAFSATELILFYIFFEATLIPTLIII 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 243 ---------------FILYTAGGSVFLLMGILGI-GLYGSNEPTLnFETLTNQSYPVALEIILYTAFLIAFAVKSPIIPL 306
Cdd:MTH00068 134 trwgnqeerlnagtyFLFYTLAGSLPLLIALLILqNSLGSLSLIL-LELMSPMQLMTYTNKIWWLACLLAFMVKMPLYGL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 307 HTWLPDTHGEAHYSTCMLLAGILLKMGAYGLVRINMELFSHAHSIFCPwLMILGSIQIIYAASTSFGQRNLKKRIAYSSV 386
Cdd:MTH00068 213 HLWLPKAHVEAPIAGSMILAAVLLKLGGYGILRISILLTPLSKELSYP-FIILALWGVLMTSLICLRQTDLKSLIAYSSV 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 387 SHMGFIILGIGSISDTGLNGAILQIISHGFIGAALFFLAGTSYDRL--RLLYLdeMGGMAIPMPKIFTIFTILSMASLAL 464
Cdd:MTH00068 292 SHMGLVIAAALIQTPWSFSGAIILMISHGLTSSALFCLANTNYERThsRTLLL--LRGAQTILPLMATWWLLSNLSNMAL 369
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 355505216 465 PGMSGFVAELIvffgIITSqkyLFMMKILITFVTAIGMILTPIYLL 510
Cdd:MTH00068 370 PPSPNLWGELT----IMVS---LFNWSNWTILITGLGTLITAAYTL 408
|
|
| ND4 |
MTH00127 |
NADH dehydrogenase subunit 4; Provisional |
170-513 |
4.76e-37 |
|
NADH dehydrogenase subunit 4; Provisional
Pssm-ID: 177186 [Multi-domain] Cd Length: 459 Bit Score: 143.17 E-value: 4.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 170 LGIDGLSIGPILLTGFITTLATLAAQ------PVTREyQLFYFLMLAMYSGQIGPFSSRDILLFFIMWELELIPVYILL- 242
Cdd:MTH00127 57 MATDPLSTPLLVLTCWLLPLMILASQnhtapePINRQ-RMYITLLTSLQIFLILAFGATEIIMFYVMFEATLIPTLIIIt 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 243 --------------FILYTAGGSVFLLMGILgigLYGSNEPTLNFETLtNQSYPVAL----EIILYTAFLIAFAVKSPII 304
Cdd:MTH00127 136 rwgnqterlnagtyFLFYTLAGSLPLLVALL---LLQNSTGTLSMLTL-QYSQPLQLsswaDKLWWAGCLLAFLVKMPLY 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 305 PLHTWLPDTHGEAHYSTCMLLAGILLKMGAYGLVRINMELFSHAHSIFCPWlMILGSIQIIYAASTSFGQRNLKKRIAYS 384
Cdd:MTH00127 212 GVHLWLPKAHVEAPIAGSMVLAAVLLKLGGYGMMRMMVMLDPLTKELSYPF-IILALWGIIMTGSICLRQTDLKSLIAYS 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 385 SVSHMGFIILGIGSISDTGLNGAILQIISHGFIGAALFFLAGTSYDRLRLLYLDEMGGMAIPMPKIFTIFTILSMASLAL 464
Cdd:MTH00127 291 SVSHMGLVAGGILIQTPWGFTGALILMIAHGLTSSALFCLANTNYERTHSRTMLLARGLQMILPLMATWWFIASLANLAL 370
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 355505216 465 PGMSGFVAELIvffgIITSqkyLFMMKILITFVTAIGMILTPIYLLSIL 513
Cdd:MTH00127 371 PPLPNLMGELM----IITS---LFNWSPWTLALTGLGTLITAGYSLYMF 412
|
|
| PRK12667 |
PRK12667 |
putative monovalent cation/H+ antiporter subunit D; Reviewed |
99-500 |
3.05e-36 |
|
putative monovalent cation/H+ antiporter subunit D; Reviewed
Pssm-ID: 237167 [Multi-domain] Cd Length: 520 Bit Score: 142.03 E-value: 3.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 99 IVVVFPIAAgSLIFLFPHRGNKVIRWYSISICLIDLLLTTYAFCYHFQLDDPLIQLtenykwinFFDFYWRLGI----DG 174
Cdd:PRK12667 12 LLVLFAFLL-PLLSILLKGNRKIQKIYALLVSLITLILSILLFIQVYSSNKPIVYL--------FGGWPAPIGIvyevDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 175 LSIGPILLTGFITTLATLAAQPVTREYQL---FYFLMLAMYSGQIGPFSSRDILLFFIMWELELIPVYILLFILYTAGGS 251
Cdd:PRK12667 83 LGALLGLLTALVMFLILIYSYWYLEHESGpewYYTLLLGLEAGMLGILLTGDAFNLFVMLEVLSISAYGLVAYYRDRGDA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 252 V-----FLLMGILG--------IGLYGSNEpTLNFETLTNQS--------------YPVALEIILyTAFLIAFAVKSPII 304
Cdd:PRK12667 163 VeaaikYALIGAVGttlyflalAFLYATFG-TLNMADLSAKIrglsfpltgglagnPPLALGVAL-ALALWAFTIKAAIF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 305 PLHTWLPDTHGEAHYSTCMLLAGILLKMGAYGLVRINMELFSHAHS------IFCPWLMILGSIQIIYAASTSFGQRNLK 378
Cdd:PRK12667 241 PNHFWLPDAHPAAPSPVSAMLSGLVVNVGAYAIIRFLYTIFGISPSlidfraALSPILIILGAVSAIIGALMMVVQKDVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 379 KRIAYSSVSHMGFIILGIGSISDTGLNGAILQIISHGFIGAALFFLAGTSYDRLRLLYLDEMGGMAIPMPKIFTIFTILS 458
Cdd:PRK12667 321 RLLAYSTISHMGYIFMGIGIGTQLGLAAALFHIINHAIAKSLLFLASGVFIHAAGTRDIDELAGLGRKMPIASFAFLIGA 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 355505216 459 MASLALPGMSGFVAELIVFFGIITSQKYLFMMKILITFVTAI 500
Cdd:PRK12667 401 LSLVGIPPLNGFFSKLLLFNALLESGFYLPALVLLIASAISL 442
|
|
| ND4 |
MTH00014 |
NADH dehydrogenase subunit 4; Validated |
134-499 |
1.51e-34 |
|
NADH dehydrogenase subunit 4; Validated
Pssm-ID: 214399 [Multi-domain] Cd Length: 452 Bit Score: 136.02 E-value: 1.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 134 LLLTTYAFCYHFQLDDPLIQLTENykwinffdfywrLGIDGLSIGPILLTGFITTLATLAAQPV---TREYQLFYFLMLA 210
Cdd:MTH00014 31 LLLSLFTLLNLYPMSAPYSMFTES------------LSSDMLSAPLITLTLWITALMILASFKIfqnNKAPKTFMTNILI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 211 MYSGQIGPFSSRDILLFFIMWELELIPVYILLF---------------ILYTAGGSVFLLMGILGIGLYGSNEPTLNFET 275
Cdd:MTH00014 99 LNLILLLTFSASNLLMFYIFFEASLIPTLFLILgwgyqperlqasfylMIYTVTASLPLLMSILLIFYTNNSLSMLMSSM 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 276 LTNQSYPVALEIILYtafLIAFAVKSPIIPLHTWLPDTHGEAHYSTCMLLAGILLKMGAYGLVRINmELFSHAHSIFCPW 355
Cdd:MTH00014 179 EPPSIYLMNLWWLIT---ILAFMVKMPLYTVHLWLPKAHVEAPVAGSMILAGILLKLGGYGLLRMS-SLFMHINKSLSAP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 356 LMilgSIQIIYAASTSF---GQRNLKKRIAYSSVSHMGFIILGIGSISDTGLNGAILQIISHGFIGAALFFLAGTSYD-- 430
Cdd:MTH00014 255 FS---SISLVGAVITSLiciRQPDLKSLIAYSSVGHMGLMTAGIMSNTSWGWQGALAMMIAHGLCSSALFALANMTYEtt 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 355505216 431 RLRLLYLdeMGGMAIPMPKIFTIFTILSMASLALPGMSGFVAELIVFFGIITSQKYLFMMKILITFVTA 499
Cdd:MTH00014 332 HTRSLFL--TKGLLSLFPTMTMWWFLLSAANMAAPPSINLLSEIMLLTSILSSSLSTAILLAITSFLAA 398
|
|
| ND4 |
MTH00205 |
NADH dehydrogenase subunit 4; Provisional |
158-500 |
2.53e-33 |
|
NADH dehydrogenase subunit 4; Provisional
Pssm-ID: 214457 [Multi-domain] Cd Length: 448 Bit Score: 132.41 E-value: 2.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 158 YKWINFFDFYwrlgiDGLSIGPILLTGFITTLATLAAQPV---TREYQLFYFLMLAMYSGQIGPFSSRDILLFFIMWELE 234
Cdd:MTH00205 46 TSFISSSFSF-----DSLSLPLIMLSFWISLLMVLASYKVfksNKNSKLFTVSVIMLLLILILSFSVDNLLLFYITFEAS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 235 LIPVYILL---------------FILYTAGGSVFLLMGILGIGlygSNEPTLNFETLTNQSYPVALEIILYTAFLIAFAV 299
Cdd:MTH00205 121 LIPTLILIlgwgyqperlqasmyMMMYTLCASLPLLIGLFFLN---SLNFSLSMFFNFPLNFSDFYLFLYWIFLMLAFLV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 300 KSPIIPLHTWLPDTHGEAHYSTCMLLAGILLKMGAYGLVRINMELFshahSIFCPWLMILGSIQIIYAASTSF---GQRN 376
Cdd:MTH00205 198 KLPMYFVHLWLPKAHVEAPVSGSMILAGVLLKLGGYGLIRITSMLY----KLNSNFSELFFSISLWGGVMTGMiclRQVD 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 377 LKKRIAYSSVSHMGFIILGIGSISDTGLNGAILQIISHGFIGAALFFLAGTSYDRLRLLYLDEMGGMAIPMPKIFTIFTI 456
Cdd:MTH00205 274 LKSLIAYSSVGHMGLMVVGVFSNTSWGMNGAIIMMVAHGLCSSGMFALANVNYERTNSRSMLMNKGVLNTFPFLVLMWFL 353
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 355505216 457 LSMASLALPGMSGFVAELIVFFGIITSQKYLFMMKILITFVTAI 500
Cdd:MTH00205 354 LISCNMAAPPSLNLASEILLIMSLLSSSKISGIPLSLISFLSGA 397
|
|
| PRK08668 |
PRK08668 |
NADH dehydrogenase subunit M; Validated |
181-561 |
5.78e-33 |
|
NADH dehydrogenase subunit M; Validated
Pssm-ID: 236332 [Multi-domain] Cd Length: 610 Bit Score: 133.58 E-value: 5.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 181 LLTGFITTLATLAAQPVTREYQLFYFLMlaMYSGQIGPFSSRDILLFFIMWELELIPVYILLF----------ILYTAGG 250
Cdd:PRK08668 79 LLVIFSVAFFMVSEKTKNDAYFNMFALM--SLAGVLGVFLANDLLTLYIFWEIMTFSSFMMVPmgkkesrkasLKYFVLS 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 251 SVFLLMGILGIGLYGSNEPTLNFETLTNQ-----SYPVALEIILytaFLIAFAV-KSPIIPLHTWLPDTHGEAHYSTCML 324
Cdd:PRK08668 157 AIGAYAMLYAIFLIYAKTGTFDFADISQGlindtSTGFALIVFL---FLLAFGVaKAGIFPLHVWAPDAYSEAPQSFSAV 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 325 LAGILLKMGAYGL-----VRINMELFS-----HAHSIFCPWLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIIL 394
Cdd:PRK08668 234 LSGQLSKLGAYGFllvlyVLPGTKLFSefgtyRGVPLFNYILAWLGNISIIVGTLMAILQEDIKKLIAYSSVANGGYILV 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 395 GIGSISDTGLNGAILQIISHGFIGAALFFLAGTSYDRLRLLYLDEMGGMAIPMPKIFTI--FTILSMAslALPGMSGFVA 472
Cdd:PRK08668 314 GLGLGTSLGFAGGLFHVFNHALFKGLFFLIFAAVIYRTGTTKISEMGGLIEKMPFTFAMylVAIISLA--GIPPMSGFAS 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 473 ELIVFFGIITsqKYLFmmkiLITFVTAIGMILTPIYLLSILRQMFYGYKffnTPNSYFFDSGPRELFISISIL-IPVIGI 551
Cdd:PRK08668 392 KWLIFEALIS--KGMP----ITAFMAFFGSIGSFLYVFRPLAGVFLGQL---PSDHKDVKEAPLPMLIPMAILvLLNVVF 462
|
410
....*....|
gi 355505216 552 GIYPDFIFSF 561
Cdd:PRK08668 463 GVAPGLVLQE 472
|
|
| PRK08376 |
PRK08376 |
putative monovalent cation/H+ antiporter subunit D; Reviewed |
204-558 |
3.62e-30 |
|
putative monovalent cation/H+ antiporter subunit D; Reviewed
Pssm-ID: 236252 [Multi-domain] Cd Length: 521 Bit Score: 124.44 E-value: 3.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 204 FYFLMLAMYSGQIGPFSSRDILLFFIMWELELIPVYILLF------------ILYTAGGSVFLLMGILGIGLYGSNEPTL 271
Cdd:PRK08376 123 YYTLILLLELGMLGMAITGDLFNFFVFLEIMSIASYALVAfrndtweaieagIKYMFVGSLASSMVLLGIALLYGQYGTL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 272 NFETLTN--QSYPVALEIILYTAFLIAFAVKSPIIPLHTWLPDTHGEAHYS-TCMLLagILLKMGAYGLVRINMELFS-H 347
Cdd:PRK08376 203 NMAYLAVkmSENPTVVAKIALALFIAGLAMKSGAVPVHMWLPDAYPAAPSSiSAMLL--VIKQAGLYALARVLFSIYGpA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 348 AHSIFCPWLM-ILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIILGIG------------SISDTGLNGAILQIISH 414
Cdd:PRK08376 281 INLATVGWVIiILGCLTMFVGVAMAVVQKDVKRLLAYHSVSQIGYMLLGLGvglaalgdpamaSYGEIALAGGIYHIVNH 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 415 GFIGAALFFLAGTSYDRLRLLYLDEMGGMAIPMPKIFTIFTILSMASLALPGMSGFVAELIVFfgiitsqKYLFMMKILI 494
Cdd:PRK08376 361 ALYKALLFLTAGAVIYETGTRNLNELGGLARTMPKTTIAFLIGAAAIVGLPPFNGFASKWLIY-------ESSALFNPIL 433
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 355505216 495 TFVTAIGMILTPIYLLSILRQMFYGYKffnTPNSYFFDSGPRELFISISIL-IPVIGIGIYPDFI 558
Cdd:PRK08376 434 GVIAMIGSVLTLASFVKVFHTAFFGPP---SEKVMNVKEPPKPMLVPMLILaIAIIGMGLFPWQI 495
|
|
| ND4 |
MTH00110 |
NADH dehydrogenase subunit 4; Provisional |
173-513 |
7.24e-30 |
|
NADH dehydrogenase subunit 4; Provisional
Pssm-ID: 177172 [Multi-domain] Cd Length: 459 Bit Score: 122.69 E-value: 7.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 173 DGLSIGPILLTGFITTLATLAAQ------PVTREyQLFYFLMLAMYSGQIGPFSSRDILLFFIMWELELIPVYI------ 240
Cdd:MTH00110 59 DSLSTPLLILTTWLLPLMLMASQhhlskePLTRK-KLYITMLILLQLFLIMTFTATELIMFYILFEATLIPTLIiitrwg 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 241 ---------LLFILYTAGGSVFLLMGILGIGlygSNEPTLNFETLTNQSYPVALE---IILYTAFLIAFAVKSPIIPLHT 308
Cdd:MTH00110 138 nqterlnagLYFLFYTLVGSLPLLVALLYIQ---NNLGSLNFLLLQLWAQPLPNSwsnNLLWLACMMAFMVKMPLYGLHL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 309 WLPDTHGEAHYSTCMLLAGILLKMGAYGLVRINMELFSHAHSIFCPWLMiLGSIQIIYAASTSFGQRNLKKRIAYSSVSH 388
Cdd:MTH00110 215 WLPKAHVEAPIAGSMVLAAILLKLGGYGMMRITIILNPLTEFMAYPFLM-LSLWGMIMTSSICLRQTDLKSLIAYSSVSH 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 389 MGFIILGIGSISDTGLNGAILQIISHGFIGAALFFLAGTSYDRL--RLLYLDEmgGMAIPMPKIFTIFTILSMASLALPG 466
Cdd:MTH00110 294 MALVIVAILIQTPWSFMGATALMIAHGLTSSMLFCLANSNYERIhsRTMILAR--GLQTLLPLMATWWLLASLTNLALPP 371
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 355505216 467 MSGFVAELIVffgIITSQKYLFMMKILitfvTAIGMILTPIYLLSIL 513
Cdd:MTH00110 372 TINLIGELFV---IMSSFSWSNITIIL----MGLNMLITALYSLYML 411
|
|
| PRK12663 |
PRK12663 |
Na+/H+ antiporter subunit D; |
96-570 |
1.68e-27 |
|
Na+/H+ antiporter subunit D;
Pssm-ID: 237163 [Multi-domain] Cd Length: 497 Bit Score: 116.20 E-value: 1.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 96 WLTIV-VVFPIAAGSLIFLFPHRgNKVIRWYSIsICLIDLLLTTYAFCYHFQLDDPLIqltenykwINFFDFYWRLGI-- 172
Cdd:PRK12663 4 NLLILpMLLPLLCGLVLVFLRNR-DRLQRYLAI-GTLTILTLISLALLIYVQRHGPIT--------LDFGGWLPPFGIqf 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 173 --DGLSIGPILLTGFITTLATLAA----QPVTREYQLFYFLMLAMySGQIGPFSSRDILLFFIMWELELIPVYILLfily 246
Cdd:PRK12663 74 tgDSLSALMVTTASFVATAIMAYGfgdiEHSGRRYGFPPFILLLM-AGVIGSFLTGDLFNLYVWFEVMLIASFVLI---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 247 TAGGSVFLLMG---------------ILGIGLYGSNEPTLNFETLT---NQSYPVALEIILYTAFLIAFAVKSPIIPLHt 308
Cdd:PRK12663 149 TLGQEREQLRGaikyvvlnligswlfLLGIGLLYGTFGTLNMAHIAmrlNDMGDTATLTTIALLFLLAFGMKAALFPFM- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 309 WLPDTHGEAHYSTCMLLAGILLKMGAYGLVRINMELFSHAHSIFCPWLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSH 388
Cdd:PRK12663 228 WLPAAYHTPNTEVAALFAALLTKVGIYALIRVFTLLFPQERELLHPLLATMAAITMVIGALGALAYKDIRRIAGYQVISS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 389 MGFIILGIGSISDTGLNGAILQIISHGFIGAALFFLAGTSYDRLRLLYLDEMGGMAIPMPKIFTIFTILSMASLALPGMS 468
Cdd:PRK12663 308 IGFILLGLALGTPAGINGAIFYLVHDMVVKTALFLIAGSLVRLTGYRSLQYLGGLYRKEPLFGALFLILIFAIGGLPPFS 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 469 GFVAELIVFFGIITSQKYLFMMKILITfvtaigMILTPIYLLSILRQMFYGYkffNTPNSYFFDSGPRELFISISILI-P 547
Cdd:PRK12663 388 GFWGKVLLVQGALDNGAYILLALMLIT------SLITMYSLFRIFFLAYWGD---KDGEEVNFKPIPLYRKLPLSILAvV 458
|
490 500
....*....|....*....|...
gi 355505216 548 VIGIGIYPDFIFSFSVDKVEAIL 570
Cdd:PRK12663 459 VIAMGIAAEPLLNLTQDAAEGLL 481
|
|
| NuoL |
COG1009 |
Membrane H+-translocase/NADH:ubiquinone oxidoreductase subunit 5 (chain L)/Multisubunit Na+/H+ ... |
96-519 |
1.31e-26 |
|
Membrane H+-translocase/NADH:ubiquinone oxidoreductase subunit 5 (chain L)/Multisubunit Na+/H+ antiporter, MnhA subunit [Energy production and conversion]; Membrane H+-translocase/NADH:ubiquinone oxidoreductase subunit 5 (chain L)/Multisubunit Na+/H+ antiporter, MnhA subunit is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440633 [Multi-domain] Cd Length: 608 Bit Score: 114.09 E-value: 1.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 96 WLTIVVVFPIAAGSLIFLFPHR-GNKVIRWYSISICLIDLLLTTYAFcYHFQLDDPLIQLtenYKWINF--FDFYWRLGI 172
Cdd:COG1009 3 LLWLIPLLPLLGALLAGLLGRRlGRRAAGWLAALAPLAAFVLSLLLF-PAVLGGEVVVEL---YTWIPVgsLGLDFGFRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 173 DGLSIGPILLTGFITTLATLAA-------QPVTREYQLFYFLMLAMysgqIGPFSSRDILLFFIMWELELIPVYILL--- 242
Cdd:COG1009 79 DGLSLLMLLLVTGVGLLVHIYSigymsgdPGLARFFAYLLLFMAAM----LGLVLSDNLLLLFVFWELVGLCSYLLIgfw 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 243 -------------FILyTAGGSVFLLMGILGIGLYGSnepTLNFETLTNQSyPVALEIILYTAFLIAFAV----KSPIIP 305
Cdd:COG1009 155 yekpsarraarkaFLV-TRVGDLGLLLGILLLGAIAG---TLNFSELLAAA-PTILSSPLLTLILLLLLLgafgKSAQFP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 306 LHTWLPDTHgEA--------HYSTcMLLAGILLkmgaygLVRINmELFSHAHSIFcPWLMILGSIQIIYAASTSFGQRNL 377
Cdd:COG1009 230 LHFWLPDAM-EGptpvsallHAAT-MVKAGVYL------LARLS-PLFALSPVWL-TVVAIIGAITALFAALIALAQTDI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 378 KKRIAYSSVSHMGFIILGIGSisdTGLNGAILQIISHGFIGAALFFLAGT------SYDrlrllyLDEMGGMAIPMPKIF 451
Cdd:COG1009 300 KRVLAYSTVSQLGYMFLALGV---GAYVAALFHLLTHAFFKALLFLGAGSvihatgTRD------IRKMGGLRKKMPITA 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 452 TIFTI--LSMAslALPGMSGFVAELIVFFGIITSQKYlfmmKILITFVTAIGMILTPIYLLSILRQMFYG 519
Cdd:COG1009 371 ITFLIgaLSLA--GIPPFAGFFSKEAILEAALEAGGL----GPLLLAVALLGAFLTAFYSFRLFFLVFFG 434
|
|
| NuoN |
COG1007 |
NADH:ubiquinone oxidoreductase subunit 2 (chain N) [Energy production and conversion]; NADH: ... |
96-561 |
4.27e-26 |
|
NADH:ubiquinone oxidoreductase subunit 2 (chain N) [Energy production and conversion]; NADH:ubiquinone oxidoreductase subunit 2 (chain N) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440631 [Multi-domain] Cd Length: 473 Bit Score: 111.36 E-value: 4.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 96 WLTIVVVFPIAAGSLIFLF-----PHRGNKVIRWYSISICLIDLLLTTYAFCYHFQlddpliqltenykwINFFDFYWrl 170
Cdd:COG1007 4 LLALLPEIILLLGALVLLLldlflPRRSRRLLAGLALLGLLLALALLLLALGGGTG--------------TAFGGMFV-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 171 gIDGLSIGPILLTGFITTLATLAAQPVTREYQL----FYFLMLAMYSGQIGPFSSRDILLFFIMWELELIPVYILL---- 242
Cdd:COG1007 68 -VDGFALFFKLLILLAALLVLLLSRDYLERRGLlrgeFYALLLFATLGMMLMASANDLLTLFLGLELLSLSLYVLVafrr 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 243 -----------FILYTAGGSVFLLMGI-LGIGLYGSneptLNFETLTNQ-SYPVALEIILYTAF---LIAFAVKSPIIPL 306
Cdd:COG1007 147 ddrrsseaalkYFLLGALSSGFLLYGIsLLYGATGS----LNLAGIAAAlAAGGANSPLLLLGLvlvLAGLAFKLSAVPF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 307 HTWLPDTHGEAHYSTCMLLAGILlKMGAYG-LVRINMELFSHAHSIFCPWLMILGSIQIIYAASTSFGQRNLKKRIAYSS 385
Cdd:COG1007 223 HMWTPDVYEGAPTPVTAFLATAP-KIAAFAaLLRLLVEAFPGLAADWQLLLAVLAVLSMTVGNLAALAQTNVKRMLAYSS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 386 VSHMGFIILGIGSISDTGLNGAILQIISHGFIGAALF-FLAGTSYDRLRLLYLDEMGGMAIPMPKIFTIFTILsMASLA- 463
Cdd:COG1007 302 IAHAGYLLLGLAAGTPLGVSAALFYLLAYLFMNLGAFaVILLLSRKGGEAEEIEDLAGLARRSPLLALAMTIF-LLSLAg 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 464 LPGMSGFVAELIVFFGIITSQKYlfmmkilitFVTAIGMILTPI---YLLSILRQMfygykFFNTPNSYFFDSGPRELFI 540
Cdd:COG1007 381 IPPTAGFFGKFYVFSAAVEAGLY---------WLAVIAVLNSVIsayYYLRVVKAM-----YFDEPEEEAPISAPPGLRV 446
|
490 500
....*....|....*....|..
gi 355505216 541 SISIL-IPVIGIGIYPDFIFSF 561
Cdd:COG1007 447 ALVIAaLLVLLLGIFPGPLLDL 468
|
|
| PRK07234 |
PRK07234 |
putative monovalent cation/H+ antiporter subunit D; Reviewed |
90-487 |
1.85e-25 |
|
putative monovalent cation/H+ antiporter subunit D; Reviewed
Pssm-ID: 235978 [Multi-domain] Cd Length: 470 Bit Score: 109.66 E-value: 1.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 90 MTNYFPwltIVVVFPIAAGSLIFLFPhrgnKVIRWYSISICLIDLLlttYAFCYHFQLDDPLIQLTENYKWInffdfywr 169
Cdd:PRK07234 1 MTSLTP---VWIALPFLLGFAIYLLP----KLDRNLALGMAIVSAV---YALGLVASMVPLELTLLDNFGVT-------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 170 LGIDGLSIGPILLTGFITTLATLAAQPVTREYqlFYFLMLAMYSGQIG-PFSSRDILLFFIMWELELIPVYILL------ 242
Cdd:PRK07234 63 LRADALSGYFILTNALVTLAVIFYCWESAKTR--FFYAQLLILHGSVNaAFVCADLISLYVALEVLSIATFLLVayprtd 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 243 --------FILYTAGGSVFLLMGIlgIGLYGSNEpTLNFETLTNQSyPVALEIILytaflIAFAVKSPIIPLHTWLPDTH 314
Cdd:PRK07234 141 raiwvglrYLFYSNVAMLFYLIGA--VLVYQANG-TFAFSGLATAD-PEAFALIA-----LGLLVKGGIFVSGLWLPLTH 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 315 GEAHYSTCMLLAGILLKMGAYGLVRInmelfSHAHSIFCPWLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIIL 394
Cdd:PRK07234 212 SEAEPPVSALLSGVVVKAGVFPLVRC-----ALDVPGLDLIVRIFGVGTALLGVLFALLEKDLKRMLAFSTISQLGFILA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 395 GigsisdtGLNGAILQiISHGFIGAALFFLAGTSYDRLRLLYLDEMGGMAIPMPkiftiftiLSMASLA---LPGMSGFV 471
Cdd:PRK07234 287 A-------PLVGGLYA-LAHGLVKSTLFLCAGALPSRNFTELISQMLGIGKWIP--------LTMASFSiagFPLLAGFV 350
|
410
....*....|....*.
gi 355505216 472 AELIVFFGIITSQKYL 487
Cdd:PRK07234 351 SKVLTLKNLLPWQAIA 366
|
|
| PRK06521 |
PRK06521 |
hydrogenase 4 subunit B; Validated |
95-473 |
3.24e-24 |
|
hydrogenase 4 subunit B; Validated
Pssm-ID: 235820 [Multi-domain] Cd Length: 667 Bit Score: 107.28 E-value: 3.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 95 PWLTIVVVFPIAAGSLIFLFPHRGNKVIRWYSISICLIDLLLTTYAFCYHFQLDDPLIQLTENYKWINFfdfywRLGIDG 174
Cdd:PRK06521 6 QLLLLSLLLYLALGLAGLLLLRRPRLAIRLSGPTGLLGGLLGLASGLTALFAGPTLAAVLPLGLPFLPF-----HLRLDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 175 LSIGPILLTGFITTLATLAAQPVTREYQ--------LFYFLMLAmysGQIGPFSSRDILLFFIMWELELIPVYIL----- 241
Cdd:PRK06521 81 LSAFFLLVISLLGAAASLYSLGYFREYEgkgpgamgFFYNLFLA---SMVLVLLADDAFSFLVAWETMSLSSWFLvianh 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 242 ----------LFILYTAGGSVFLLmgiLGIGLYGSNEPTLNFETLTNQSYPVALEIIlytAFLIA---FAVKSPIIPLHT 308
Cdd:PRK06521 158 reaeirragfLYLLMAHAGALAIL---LAFGLLARESGSYDFAAMRAAHLSPFWASL---VFLLAlfgFGAKAGLVPLHV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 309 WLPDTHGEA--HYSTcmLLAGILLKMGAYGLVRINMELFSHAHSIFCPWLMILGSIQ----IIYAAStsfgQRNLKKRIA 382
Cdd:PRK06521 232 WLPRAHPAApsHVSA--LMSGVMLKVAIYGILRVVFDLLGAPGWWWGVLVLALGAISavlgVLYALA----EHDLKRLLA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 383 YSSVSHMGFIILGIG-----------SISDTGLNGAILQIISHGFIGAALFFLAGTSYDRLRLLYLDEMGGMAIPMPKIF 451
Cdd:PRK06521 306 YSTIENIGIIFVGLGlamvfiaygmpLLAALALTAALYHLLNHALFKSLLFLGAGAVLHATGTRDMEKLGGLIRRMPWTA 385
|
410 420
....*....|....*....|..
gi 355505216 452 TIFTILSMASLALPGMSGFVAE 473
Cdd:PRK06521 386 WAFLIGCLAISALPPLNGFVSE 407
|
|
| PRK06458 |
PRK06458 |
hydrogenase 4 subunit F; Validated |
97-503 |
4.98e-24 |
|
hydrogenase 4 subunit F; Validated
Pssm-ID: 235805 [Multi-domain] Cd Length: 490 Bit Score: 105.40 E-value: 4.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 97 LTIVVVFPIAAGSLIFLFPHRGnkVIRWYSISICLIDLLLTtyAFCYHFQLDDPliqltenykwiNFFDFYWRLGIDGLS 176
Cdd:PRK06458 7 FALLLLIPLLASLLLFALRKRR--LVATLNVLGITLTLILA--LWLVFTVPDAG-----------EIFAAGLWFFIDDLN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 177 IGPILLTGFITTLATLAAQPVTRE------------------YQLFYFLM-LAMYSGQIGpfssrdillffIMW-ELELI 236
Cdd:PRK06458 72 VFFLALIGVVGFLTSLYSIGYMRHevehgelspvtlrlyygmYQLFLFTMlLALTSNNLG-----------LMWvAIEAT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 237 PV-YILLFILYTAGGSV------FLLMGI-LGIGLYGSNEPTLNFETLTNQ-----------SYPVALE-IILYTAF--- 293
Cdd:PRK06458 141 TLsSALLVGIYRTRASLeaawkyIIICSVgVAFALFGTILVYANAATVMGDgemailwtellKHASLLDpTLMKLAFvfl 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 294 LIAFAVKSPIIPLHTWLPDTHGEAHYSTCMLLAGILLKMGAYGLVRINMELFSHAHSIFC-PWLMILGSIQIIYAASTSF 372
Cdd:PRK06458 221 LIGFGTKVGLFPMHAWLPDAHSEAPSPVSALLSGVLLNVALYAVLRYYILIDAAIGSDFPgRLLLIFGLLSVLVAAFFLL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 373 GQRNLKKRIAYSSVSHMGFIILGIGSISDTGLNGAILQIISHGFIGAALFFLAGTSYDRLRLLYLDEMGGMAIPMPKIFT 452
Cdd:PRK06458 301 RQRDIKRLFAYSSIEHMGLIAFALGIGGPLGIFAALLHMLNHSLTKSAIFFASGNVLQKYGTRDINVIRGLLKVSPLTGW 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 355505216 453 IFTILSMASLALPGMSGFVAELIVFFGIITSQKYLFMMKILITFVTAIGMI 503
Cdd:PRK06458 381 GLMLGALAIAGMPPFGVFISEFLILTAGLARGPLLIAILLLLLLTLAFAAL 431
|
|
| PRK06589 |
PRK06589 |
putative monovalent cation/H+ antiporter subunit D; Reviewed |
158-552 |
6.95e-24 |
|
putative monovalent cation/H+ antiporter subunit D; Reviewed
Pssm-ID: 235835 [Multi-domain] Cd Length: 489 Bit Score: 105.28 E-value: 6.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 158 YKWINFFDFYWRLGIDGLSIGPILLTGFIT------TLATLAAQPVTREYQLFYFLMLAMYSGQIGPFSSrDILLFFIMW 231
Cdd:PRK06589 67 FELMDFGNYSIGLHLEPLGLIFLLLIGFLWicallyTPKYLAINNIDSSSRFLFFFNLTILIGVLIALSS-DLFTMFVCY 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 232 ELELIPVYIL---------LFILYTAGGSVF---LLMGILGIGLYGSNEPTLNFETLTNQSYPVALEIILYTAFLIAfav 299
Cdd:PRK06589 146 ELLTISTAFLightrnnisLSGGYKYLKILMisaLLLFLPAVILIYTKTGNLDFVSGGLFSKNQSIILLLMFIYGIA--- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 300 KSPIIPLHTWLPdTHGEAHYSTCMLL-AGILLKMGAYGLVRINMELF--SHAHSIFC--PWLMILGSIQIIYAASTSFGQ 374
Cdd:PRK06589 223 KTAIFPVHSWLP-AAMVAHYPVSALLhAVIVVKTGLFCIYKILLYIFglSYLQRIFAefNWLIFIPIVSIFYSSLKALKT 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 375 RNLKKRIAYSSVSHMGFIILGIGSISDTGLNGAILQIISHGFIGAALFFLAGTSYDRLRLLYLDEMGGMAIPMPKIFTIF 454
Cdd:PRK06589 302 DNIKKILAYSTISQLSLALLSAFILTPKALGAAILHLVSHSFAKICLFYSMGSIYSLKKEDQVDKLHGTSKSFPLISFII 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 455 TILSMASLALPGMSGFVAELIVFFGIitSQKYLFMMKILITFVTAIGMILTPIYLLSILrqmFYGYKFFNTPNSYFFDSG 534
Cdd:PRK06589 382 SISSLSLIGIPIFSGFISKFLILLAA--SEQNQPWLSIIVMLVVIASSILSALYLLKIL---SSIYKPSLSENSFITKSL 456
|
410
....*....|....*...
gi 355505216 535 PRELFISISILIPVIGIG 552
Cdd:PRK06589 457 PYLMQISVITCCCALTLF 474
|
|
| PRK07691 |
PRK07691 |
putative monovalent cation/H+ antiporter subunit D; Reviewed |
173-570 |
9.02e-24 |
|
putative monovalent cation/H+ antiporter subunit D; Reviewed
Pssm-ID: 181085 [Multi-domain] Cd Length: 496 Bit Score: 104.65 E-value: 9.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 173 DGLSIGPILLTGFITTLATLAAQP---VTREYQLFYFLMLAMYSGQIGPFSSRDILLFFIMWELELIPVYILL------- 242
Cdd:PRK07691 76 DMFAALLVLTSSIITFLVILYSFQtigIERERYYYYPSVLFMLAGVNGAFLTGDIFNLFVFFEVMLMASYVLIviggtki 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 243 -------FILYTAGGSVFLLMGIlgiGLYGSNEPTLNFETLTNQSYPVALE-----IILYTAFLIAFAVKSPIIPLHTWL 310
Cdd:PRK07691 156 qlresikYVLINVVSSAFFVVAV---AILYSVVGTLNMADISVKIAELSAGqtgliTVVAILFLFVFATKAGLFPLYFWL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 311 PDTHGEAHYSTCMLLAGILLKMGAYGLVRINMELFSHAHSIFCPWLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMG 390
Cdd:PRK07691 233 PGSYYAPPIAIAALFGALLTKVGVYAIARTFTLFFSHDTSFTHYLILILALLTIIFGVIGAVAYFDIKKIIIYNIMIAVG 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 391 FIILGIGSISDTGLNGAILQIISHGFIGAALFFLAGTSYDRLRLLYLDEMGGMAIPMPKIFTIFTIlSMASLA-LPGMSG 469
Cdd:PRK07691 313 VILVGVAMMTESGMIGAIYYLIHDMIVKAALFLLIGIMIKITGTTDLKKMGGLIKRYPVLGWMFFI-AALSLAgIPPLSG 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 470 FVAELIVFFGIITSQKYLFMMKILITFVtaigmiltpIYLLSILRQMFYGykFFNTPNSYFFDSGP---RELFISISILI 546
Cdd:PRK07691 392 FYGKFFIVEGTFEAGFYVSGIIVLLSSL---------LVLYSVIKIFLKG--FWGEPKGYDLNNKVpvkKLLLPAVVLVA 460
|
410 420
....*....|....*....|....
gi 355505216 547 PVIGIGIYPDFIFSFSVDKVEAIL 570
Cdd:PRK07691 461 ITILYGLGAEPLYPYVKQAAETLY 484
|
|
| PRK08676 |
PRK08676 |
hydrogenase membrane subunit; Validated |
163-483 |
2.46e-23 |
|
hydrogenase membrane subunit; Validated
Pssm-ID: 181537 [Multi-domain] Cd Length: 485 Bit Score: 103.30 E-value: 2.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 163 FFDFYWRLGIDGLSIGPILLTGFITTLATLAAQPVT-----------REYQLFYFLMLAMYSGQIGPFSSRDILLFFIMW 231
Cdd:PRK08676 52 YFMESRYLFIDHLGIFVVLIASVVFILAALYARGYVdhllsngeldpENLKVFYLGFNLLLSVITFAFFSDNLALFWIFA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 232 ELELIPVYILLFIL-----------YTAGGSVFLLMGILG-IGLY-----GSNEPTLNFETLTNQS--YPVALEIILYTA 292
Cdd:PRK08676 132 ELTTVFSAMLIAILsarenidaalkYIFIASTAMIFAFIGlIFLFsltrqALGTGTLNWTELAAHAslLSPSVLGASFLF 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 293 FLIAFAVKSPIIPLHTWLPDTHGEAHYSTCMLLAGILLKMGAYGLVRINMELF-SHAHSIFCPWLMILGSIQIIYAASTS 371
Cdd:PRK08676 212 IFIGFLAKSGLVPFHTWLPAAYAKAPSVVSALLSGTVLNIGIYGILRLSALLRqSGAAEQFSNVLIGLGIFSIAVAAFSM 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 372 FGQRNLKKRIAYSSVSHMGFIILGIGSISDTGLNGAILQIISHGFIGAALFFLAGTSYDRLRLLYLDEMGGMAIPMPkiF 451
Cdd:PRK08676 292 LSQRNLKKLIAFSSIEHMGLMLLGIGIGTPLALFWMLFHMLAHSLVKSGLFFSAGILHRQYRSDRFDRIFDVFRLQP--V 369
|
330 340 350
....*....|....*....|....*....|..
gi 355505216 452 TIFTILsMASLALPGMSGFVAELIVFFGIITS 483
Cdd:PRK08676 370 AAWGVI-LGSAAIIGMPPFPLFLSKFFILLQL 400
|
|
| PRK08377 |
PRK08377 |
NADH dehydrogenase subunit N; Validated |
98-559 |
8.66e-22 |
|
NADH dehydrogenase subunit N; Validated
Pssm-ID: 181406 [Multi-domain] Cd Length: 494 Bit Score: 98.69 E-value: 8.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 98 TIVVVFPIAAGSLIFLFPHRGNKVIRWYSISICLIDLLLTTYAFCYHFQLDDPLIQLTENYKWinffdfywRLGIDgLSI 177
Cdd:PRK08377 6 SLLIALPLISAFFVPVIKGIGKSAVRYYLILITLLQTGIAGWVFMEVYTTGKPIIIMAGGWKP--------PVGIN-LYI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 178 GP--------ILLTGFITTLATLAA---QPVTREYQLFYFLMLamysGQIGPFSSRDILLFFIMWELELIPVYILL---- 242
Cdd:PRK08377 77 GPfaalfvliIAIVSFIMSIFSLKAvevEPIDKYAMLFLLLML----GATGMIATGDIFNLFVFMEITAITAYALTaynk 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 243 ----------FILYTAGGSVFLLMGILGIglYGSNEpTLN---FETLTNQSYPVALEIILyTAFLIAFAVKSPIIPLHTW 309
Cdd:PRK08377 153 tgeaaeasmkYIVLGGIGSSFFLIGVALI--YGATG-TLNmahIAQLAGTIDPTVAQVGL-ALLIFGLAVEAELFPLNAW 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 310 LPDTHGEAHYSTCMLLAGILLKMGAYGLVRINMELF-SHAHSIFCPWLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSH 388
Cdd:PRK08377 229 APDAYQAAPHPITVMFSAFVVKAGLYAMARILYLMQnANGWSSVLKLVIIMATLTVFFAELSALRQKNVKRMIAYSSIGQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 389 MGFIILGIGSISDTGLNGAILQIISHGFIGAALFFLAGTSYDRLRLLYLDEMGGMAIPMPKIFTIFTILSMASLALPGMS 468
Cdd:PRK08377 309 VGMIALALALGTQAGVDAGVFHMINHAIVKALLFLAVGYVGITLGGTEIEKFEGLGKRMPLTALALTIGALSTVGIPLFN 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 469 GFVAELIVFFGIItSQKYLFMMkILITFVTaigmILTPIYLLSILRQMFYGYKFFNTPNSYFFDsgprelFISISILIPV 548
Cdd:PRK08377 389 VFWSKFRIILAGL-SAGYTWPV-ALVLGAS----VVEAVYYFRLIHTMWFKGEGERIRENAAIG------IILLLLAALI 456
|
490
....*....|.
gi 355505216 549 IGIGIYPDFIF 559
Cdd:PRK08377 457 VVIGIYPTPFW 467
|
|
| PRK12662 |
PRK12662 |
putative monovalent cation/H+ antiporter subunit D; Reviewed |
170-518 |
9.15e-22 |
|
putative monovalent cation/H+ antiporter subunit D; Reviewed
Pssm-ID: 183662 [Multi-domain] Cd Length: 492 Bit Score: 98.65 E-value: 9.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 170 LGIDGLSIGPILLTGFITTLATL-AAQPVTREYQL-----FYFLMLAMYSGQIGPFSSRDILLFFIMWELELIPVYILL- 242
Cdd:PRK12662 72 LRVDILSATMLVLVNFIAVMSVLyGIYPNRKEISVnkipsFYSAFLLCLGGLLGILVSNDVFNIYVFLEISSISSYVLVa 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 243 --------------FILYTAGGSVFLLmgilGIGLYGSNEPTLNFETLTNQSYPVALEIILYTAFLIAF---AVKSPIIP 305
Cdd:PRK12662 152 mgrdkkalvaafeyLIIGTIGATFYLI----GIGFLYAITGTLNMGDMFLIIQDLPTNRAIQIGVLFIMvglFIKAALFP 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 306 LHTWLPDTHGEAHYSTCMLLAGILLKMGAYGLVRINMELFsHAHSIFCPW-----LMILGSIQIIYAASTSFGQRNLKKR 380
Cdd:PRK12662 228 FHKWLIQAYSEAPSFISVFFSGTSTKVMIYLIIRIVYDVF-KANFVFTTLpfnnvFMILAALAIVFGSVLAILSKDIKRI 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 381 IAYSSVSHMGFIILGIGSISDTGLNGAILQIISHGFIGAALFFLAGTSYDRLRLLYLDEMGGMAIPMPKIFTIFTILSMA 460
Cdd:PRK12662 307 FAYSSISHIGYIILAVSLNTYYGLAAAVAYIVNHSIVKSALFMVSGSISYHFGTTKLEDCLNLWKSMPKITLAFVLLSLS 386
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 355505216 461 SLALPGMSGFVAELIVFFGIITSQKYLFMmkilitFVTAIGMILTPIYLLSILRQMFY 518
Cdd:PRK12662 387 LIGMPPTSGFVAKWYILDAFIKSNAWIGL------VVLLVGSGLSVIYVWKIVEALYF 438
|
|
| PRK08667 |
PRK08667 |
hydrogenase membrane subunit; Validated |
205-483 |
7.12e-21 |
|
hydrogenase membrane subunit; Validated
Pssm-ID: 236331 [Multi-domain] Cd Length: 644 Bit Score: 96.72 E-value: 7.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 205 YFLMLAMYSGqigPFSSRDILLFFIMWELELIPVYILLFILYTAGGSvfllmgilgiglygsneptlnFEtLTNQSYPVA 284
Cdd:PRK08667 148 FFLVMNDYQE---EETQRAGIFYFVMTQLSTVFLMLGIIVLFIQTGS---------------------FE-LSPLGASAG 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 285 LEIILYTAFLIAFAVKSPIIPLHTWLPDTHGEAHYSTCMLLAGILLKMGAYGLVRINMELFShAHSIFCPWLMILGSIQI 364
Cdd:PRK08667 203 ILSLVFLLLFLGFGIKAGIIPFHKWLPYAHPASPSNVSALMSGVMLKVAVYGLVRFLMDVLS-PELWWGVLILLAGSISA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 365 IYAASTSFGQRNLKKRIAYSSVSHMGFIILGIG-----------SISDTGLNGAILQIISHGFIGAALFFLAGTSYDRLR 433
Cdd:PRK08667 282 LLGVIYALKEHDLKGLLAYSSIENIGIILMGIGlyvifgvygldTLALLALGGALFHSLNHALFKSLLFLTAGSVVHATG 361
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 355505216 434 LLYLDEMGGMAIPMPKIFTIFTILSMASLALPGMSGFVAELIVFFGIITS 483
Cdd:PRK08667 362 TRNIEKMGGLVKLMPYTSALFLVGAVSIAALPPFNGFASELLLYESFFQS 411
|
|
| PRK05777 |
PRK05777 |
NADH-quinone oxidoreductase subunit NuoN; |
99-561 |
6.55e-20 |
|
NADH-quinone oxidoreductase subunit NuoN;
Pssm-ID: 235603 [Multi-domain] Cd Length: 476 Bit Score: 92.96 E-value: 6.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 99 IVVVFPIAAGSLIFLFphRGNKVIRWYSISICLIDLLLTTYAFCYHfqlddpliqltenykWINFFDFYWRLGIDGLSIg 178
Cdd:PRK05777 15 LILLGAAVVLLLIDAF--VRRHSRRATLAVLALLLALVALLFVLGA---------------AGGGTAFGGMLVVDGFAL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 179 piLLTGFITtLATLAAQPVTREYQL------FYFLMLAMYSGQIGPFSSRDILLFFIMWELELIPVYILL---------- 242
Cdd:PRK05777 77 --FLKGLIL-LASLLALLLARPYLEdrgrgeFYLLVLFALLGMMVMVSANDLLTLFLGLELLSLPLYALAalrrdrrrsl 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 243 ------FILyTAGGSVFLLMGILGIglYGSNEpTLNFETLT---NQSYPVALEIILYTAFLIA-FAVKSPIIPLHTWLPD 312
Cdd:PRK05777 154 eaaikyFVL-GALASGFLLYGMSLL--YGATG-SLSFAGIAkalADGSGNSLLLLFGLVFLLVgLAFKLSAVPFHMWTPD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 313 THGEAHYSTCMLLAGILlKMGAYG-LVRINMELFSHAHSIFCPWLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGF 391
Cdd:PRK05777 230 VYEGAPTPVTAFLATAP-KIAAFAvLLRLLVVAFGGLSEDWQQVLAIIAIASMLVGNLAALSQTNIKRLLAYSSIAHAGY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 392 IILGIGSISDTGLNGAILQIISHGFIGAALF-FLAGTSYDRLRLLYLDEMGGMAIPMPKIFTIFTILsMASLA-LPGMSG 469
Cdd:PRK05777 309 LLVGLAAGTAEGYSAVLFYLLAYLFMTLGAFgVISLLRRKGGEAESISDFAGLSKRSPLLAAVMTIF-MLSLAgIPPTAG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 470 FVAELIVFFGIITSQkylfmmkilITFVTAIGMILTPI---YLLSILRQMFygykFFNTPNSYFFDSGPRELFISISIL- 545
Cdd:PRK05777 388 FWGKFYVFEAAVEAG---------LWWLAVIGVLNSAIgafYYLRVIKLMY----FDEPPRDAPVNWPLSAGGAVLSVSa 454
|
490
....*....|....*.
gi 355505216 546 IPVIGIGIYPDFIFSF 561
Cdd:PRK05777 455 LLVLVLGIFPQPLLDL 470
|
|
| PRK12665 |
PRK12665 |
putative monovalent cation/H+ antiporter subunit D; Reviewed |
282-477 |
1.57e-19 |
|
putative monovalent cation/H+ antiporter subunit D; Reviewed
Pssm-ID: 237165 [Multi-domain] Cd Length: 521 Bit Score: 91.95 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 282 PVALEIILYTAFLIAFAVKSPIIPLHTWLPDTHGEAHYSTCMLLAGILLKMGAYGLVRINMELFSHaHSIFCPwLMILGS 361
Cdd:PRK12665 204 PSGTRTALFAVLLVAFGIKAAVFPLSFWLPDSYPTAPAPVTAVFAGLLTKVGVYAIIRTHTLLFPG-GGLDTL-LMVVAL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 362 IQIIYAASTSFGQRNLKKRIAYSSVSHMGFIILGIGSISDTGLNGAILQIISHGFIGAALFFLAGTSYDRLRLLYLDEMG 441
Cdd:PRK12665 282 LTMVVGILGAIAQSDIKRLLSFTLVSHIGYMVFGIALSTVAGLSGAIYYVAHHITVQTTLFLVVGLIERQAGSSSLRRLG 361
|
170 180 190
....*....|....*....|....*....|....*.
gi 355505216 442 GMAIPMPKIFTIFTILSMASLALPGMSGFVAELIVF 477
Cdd:PRK12665 362 GLAKASPLLAVLFFVPALNLGGIPPFSGFIGKVALL 397
|
|
| PRK12668 |
PRK12668 |
Na(+)/H(+) antiporter subunit D; |
105-472 |
2.14e-17 |
|
Na(+)/H(+) antiporter subunit D;
Pssm-ID: 237168 [Multi-domain] Cd Length: 581 Bit Score: 85.33 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 105 IAAGSLIFLFPHRgnkVIRWYSISICLIDLLLttyafcyhfqlddpLIQLTE-NYKWINFFDFYWRLG-IDGLSIGPILL 182
Cdd:PRK12668 13 IAGALLVPFLPGR---ARKALLLLAPVLAVLA--------------VLTVPEgTYLTVTFLGFDLVLGrVDKLSRVFGLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 183 TGFITTLATLAAQPVTREYQLfyflMLAMY--SGQIGPFSSRDILLFFIMWELELIPVYILL---------------FIL 245
Cdd:PRK12668 76 FGIMAFIGVIYALHVKDPGQH----VAALLyvGSALGAVFAGDLLTLFVFWELMAFTSTFLVwargtkaavragfryLLV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 246 YTAGGsVFLLMGILgigLYGSNEPTLNFETLTNQSYPVALEIilytafLIAFAVKSPIIPLHTWLPDTHGEAHYSTCMLL 325
Cdd:PRK12668 152 HVLGG-VLLLAGIL---LHYAETGSFAFGAIAGLGGTAAWLI------LIGFGVNAAFPPLHAWLPDAYPEATVTGSVFL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 326 AGILLKMGAYGLVRinmeLFSHAHsifcpWLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIILGIGSISDTGLN 405
Cdd:PRK12668 222 SAFTTKTAVYALAR----AFPGTE-----LLIYIGAAMAVYGVFFALLENDLRRLLSYHIVSQVGYMVAGIGIGTALAIN 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 355505216 406 GAILQIISHGFIGAALFFLAGTSYDRLRLLYLDEMGGMAIPMPKIFTIFTILSMASLALPGMSGFVA 472
Cdd:PRK12668 293 GAVAHAFNHILYKGLLFMSAGAVLYRTGTEKLTELGGLYRSMPLTALFCLVGALSISAFPLFSGFVS 359
|
|
| PRK12650 |
PRK12650 |
DUF4040 family protein; |
204-471 |
2.57e-17 |
|
DUF4040 family protein;
Pssm-ID: 237158 [Multi-domain] Cd Length: 962 Bit Score: 85.86 E-value: 2.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 204 FYFLMLAMYSGQIGPFSSRDILLFFIMWELELIPVYILL-------------FILYTAGGSVFLLMGiLGIGLYGSNEPT 270
Cdd:PRK12650 112 FYLLMTAFMAAMLLLVLADDVVVLFVAWELVSLASFFLIarsgsggeagsirTLILTFFGGLTLLAA-VAIAATQTGTTS 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 271 LNfETLTNQSY---PVALEIIlytAFLIAFAV--KSPIIPLHTWLPDTHGEAHYSTCMLLAGILLKMGAYGLVRinmelF 345
Cdd:PRK12650 191 LS-GILHSDVWaekPGLTTVV---AVLIAVAAftKSAQFPFHFWLPEAMAAITPVSAFLHAAAVVKAGIYLLLR-----F 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 346 SHAHSIFCPW---LMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIILGIGSISDTGLNGAILQIISHGFIGAALF 422
Cdd:PRK12650 262 SPVFHDVAVWnwlLIIVGMITALMGAVFAVQKTDLKKLTAYSTVSQLGWIVATIGVGTPFALTAAVVHTLAHALFKSSLF 341
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 355505216 423 FLAGT------SYDRLRLlyldemGGMAIPMPKIFTIFTI--LSMAslALPGMSGFV 471
Cdd:PRK12650 342 MLIGVvdhqagTRDIRRL------GSLWRRMPFTFVSVTIaaLSMA--AVPPLFGFV 390
|
|
| ND4 |
MTH00094 |
NADH dehydrogenase subunit 4; Provisional |
293-531 |
2.79e-17 |
|
NADH dehydrogenase subunit 4; Provisional
Pssm-ID: 177157 [Multi-domain] Cd Length: 403 Bit Score: 84.19 E-value: 2.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 293 FLIAFAVKSPIIPLHTWLPDTHGEAHYSTCMLLAGILLKMGAYGLVRInmeLFSHAHSIFCPWlMILGSIQIIYAASTSF 372
Cdd:MTH00094 157 LSLSFMMKFPVYFLHLWLPKAHVEAPTTASMLLAGLLLKLGTAGFLRI---LGSLNFVYNNFW-IIFSLLGMILSSFCCV 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 373 GQRNLKKRIAYSSVSHMGFIILGIGSISDTGLNGAILQIISHGFIGAALFFLAGTSY--DRLRLLYLdeMGGMAIPMPKI 450
Cdd:MTH00094 233 FQSDSKSLAAYSSVTHMSFLLLSLVYMSMSGKLSGLMMMLAHGYTSTLMFYLIGEFYhiSKSRLIYF--MNSFFSSSMFF 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 451 FTIFTILSMASLALPGMSGFVAELIVFFGIITSQKYLFMMKILItfvtaigMILTPIYLLSILRQMFYGYKFFNTPNSYF 530
Cdd:MTH00094 311 GLIFSLVFLSNSGVPPSLSFFSEFLIISNSFMKNKFSFFFIFFY-------FLVSFYYSLFLIVSSFMGKKFSNFNNFNV 383
|
.
gi 355505216 531 F 531
Cdd:MTH00094 384 G 384
|
|
| PRK12647 |
PRK12647 |
putative monovalent cation/H+ antiporter subunit A; Reviewed |
154-475 |
4.83e-17 |
|
putative monovalent cation/H+ antiporter subunit A; Reviewed
Pssm-ID: 237156 [Multi-domain] Cd Length: 761 Bit Score: 84.59 E-value: 4.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 154 LTENYKWINFFDFYWRLGIDGLSIGPILLTGFITTLATLAAQPVTREYQ---LFYFLMLAMYSGQIGPFSSRDILLFFIM 230
Cdd:PRK12647 44 VRGGYAWVPSLGVNLSFLLDGLSLTFALLITGIGTLIVLYAGGYLKGHPdlgRFYSYILLFMASMLGLVLSDNLITLFVF 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 231 WELELIPVYILL---------------FILYTAGGSVFLLMGILGIG-LYGSNEPT--LNFETLTNQS--YPVALEIILY 290
Cdd:PRK12647 124 WELTSITSFLLIgfnhereaarraalqALLVTGGGGLALLAGLILLGnVTGTYSLSelLASGDVIREHplYLAILLLVLG 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 291 TAFliafaVKSPIIPLHTWLPD-----THGEAH-YSTCMLLAGIllkmgaYGLVRINMELFSHAhsifcPWLMIL---GS 361
Cdd:PRK12647 204 GAF-----TKSAQFPFHFWLPNameapTPVSAYlHSATMVKAGI------YLLARLNPVLGGTP-----LWQTILplfGG 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 362 IQIIYAASTSFGQRNLKKRIAYSSVSHMGFIILGIGSISDTGLNGAILQIISHGFIGAALFFLAGT------SYDRLRLl 435
Cdd:PRK12647 268 LTMLTGALLAVRQTDLKLILAYSTVSALGTLVMLLGLGSELAIKAAVLFLVAHSLYKGALFMVAGIidhetgTRDITKL- 346
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 355505216 436 yldemGGMAIPMPKIFtIFTILSMASLA-LPGMSGFVA-ELI 475
Cdd:PRK12647 347 -----GGLRRAMPITA-AAALLAALSMAgLPPLFGFLAkELI 382
|
|
| NDH_I_N |
TIGR01770 |
proton-translocating NADH-quinone oxidoreductase, chain N; This model describes the 14th ... |
204-559 |
2.10e-16 |
|
proton-translocating NADH-quinone oxidoreductase, chain N; This model describes the 14th (based on E. coli) structural gene, N, of bacterial and chloroplast energy-transducing NADH (or NADPH) dehydrogenases. This model does not describe any subunit of the mitochondrial complex I (for which the subunit composition is very different), nor NADH dehydrogenases that are not coupled to ion transport. The Enzyme Commission designation 1.6.5.3, for NADH dehydrogenase (ubiquinone), is applied broadly, perhaps unfortunately, even if the quinone is menaquinone (Thermus, Mycobacterium) or plastoquinone (chloroplast). For chloroplast members, the name NADH-plastoquinone oxidoreductase is used for the complex and this protein is designated as subunit 2 or B. This model also includes a subunit of a related complex in the archaeal methanogen, Methanosarcina mazei, in which F420H2 replaces NADH and 2-hydroxyphenazine replaces the quinone. [Energy metabolism, Electron transport]
Pssm-ID: 273795 [Multi-domain] Cd Length: 468 Bit Score: 81.92 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 204 FYFLMLAMYSGQIGPFSSRDILLFFIMWELELIPVYILL----------------FILyTAGGSVFLLMGILGIglYGSN 267
Cdd:TIGR01770 104 FYILLLFALLGIFLLVSSNDLLSIYLGLELQSLCFYVLAglkrksrfsteaglkyFIL-GAFSSGLLLFGISLI--YGFT 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 268 EpTLNFETLTNQSYPVALEIILYTA----FLIAFAVKSPIIPLHTWLPDTHGEAHYSTCMLLAGILLKMGAYGLVRINME 343
Cdd:TIGR01770 181 G-SLNFEDLLLFLSNGMLNISLLLLgivlILVGLLFKLSAVPFHMWVPDVYEGAPTPVTAFFSIVPKIAIFAVFLRLFLY 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 344 LFSHAHSIFCPWLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIILGIGSISDTGLNGAILQIISHGFIGAALF- 422
Cdd:TIGR01770 260 ILFGFSEAWQIFLAIIAFLSMLIGNFGALAQKKVKRLLAYSSISHVGYILIGLLAGTLEGIKAVLFYIFIYALMSLGAFg 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 423 -FLAGTSYDRLRLLYLDEMGGMAIPMPKIFTIFTILsMASLA-LPGMSGFVAELIVFFGIItsQKYLFMMKILITFVTAI 500
Cdd:TIGR01770 340 vLSLLRSYKDEWIEYISDFAGLFKTNPILAILILIF-MFSLAgIPPLAGFFGKFYVFFALL--KSGLYWLAVIAVLTSVI 416
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 355505216 501 GMiltpIYLLSILRQMfygykFFNTPNSYFFDSGPR--ELFISISILIPVIGIGIYPDFIF 559
Cdd:TIGR01770 417 GA----FYYLRVVKVM-----YFDKPERRIPSNPQSkaQSLLLSISALFILFLGLFPSLIL 468
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
9-75 |
2.44e-16 |
|
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440758 [Multi-domain] Cd Length: 66 Bit Score: 73.63 E-value: 2.44e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 355505216 9 DTCIGCTQCVRACPTDVLEMIPWDGCKAKQIasapRTEDCVGCKRCESACPTDFLSVRVYLGPETTR 75
Cdd:COG1143 2 DKCIGCGLCVRVCPVDAITIEDGEPGKVYVI----DPDKCIGCGLCVEVCPTGAISMTPFELAVEDR 64
|
|
| PRK06525 |
PRK06525 |
hydrogenase 4 subunit D; Validated |
196-479 |
2.75e-16 |
|
hydrogenase 4 subunit D; Validated
Pssm-ID: 180606 [Multi-domain] Cd Length: 479 Bit Score: 81.56 E-value: 2.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 196 PVTREYQLFYFLMLAMYSGQIGPFSSRDILLFFIMWELELIPVYILlfILYT-------AGGSVFLLMGILGIGLYGSNE 268
Cdd:PRK06525 107 PVHEGTGRYYAFLLLFIGAMAGLVYSSTLLGLLLFFEITGLCSWAL--ISYYqspkalrSALKALLITHIGSLGLYLAAA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 269 ----PTLNFETLTNQSYPVALEIILYTAFLIAFAVKSPIIPLHTWLPDTHGEAHYSTCMLLAGILLKMGAYGLVRINMEL 344
Cdd:PRK06525 185 tlflQTGTFALSALSGLHGSLKYLVFLGILFAAWGKSAQLPFYSWLPDAMEAPTPASAYLHAASMVKVGVYIFARAIQSM 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 345 FSHAHSIFcpWLM-ILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIILGIG-SI--SDTGLNGAILQIISHGFIGAA 420
Cdd:PRK06525 265 GPIPHVIG--YVGaVMAIVTLLYGFLMYLPQQDMKRLLAYSTITQLGYMFFGLSlAIlgSRLALEGSIAYIFNHAFAKSL 342
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 355505216 421 LFFLAGTSYDRLRLLYLDEMGGMAIPMPKIFTIFTILSMASLALPGMSGFVAELIVFFG 479
Cdd:PRK06525 343 FFLVAGALSYSCGTRLLPRLRGVLKKLPLVGVGFCVAALAITGVPPFNGFFSKFPIFAA 401
|
|
| PreA |
COG1146 |
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
7-61 |
3.24e-16 |
|
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];
Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 73.20 E-value: 3.24e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 355505216 7 IYDTCIGCTQCVRACPTDVLEMIPwDGCKAKQIasapRTEDCVGCKRCESACPTD 61
Cdd:COG1146 6 DTDKCIGCGACVEVCPVDVLELDE-EGKKALVI----NPEECIGCGACELVCPVG 55
|
|
| PRK08042 |
PRK08042 |
formate hydrogenlyase subunit 3; Reviewed |
247-526 |
4.56e-16 |
|
formate hydrogenlyase subunit 3; Reviewed
Pssm-ID: 181206 [Multi-domain] Cd Length: 593 Bit Score: 81.41 E-value: 4.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 247 TAGGSVFLLMGILGIGL-----------YGsnepTLNFETLTNQSYPVALEIILYTAFLIAFAVKSPIIPLHTWLPDTHG 315
Cdd:PRK08042 133 SKEGKLWFALGRLGTLLlaiacwllwqrYG----TLDLRLLDMRMQQLPLGSDIWLLGVIGFGLLAGIIPLHGWVPQAHA 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 316 EAHYSTCMLLAGILLKMGAYGLVRINmeLFSHAHSIFCP-WLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIIL 394
Cdd:PRK08042 209 NASAPAAALFSTVVMKIGLLGILTLS--LLGGNAPLWWGvALLVLGMITAFVGGLYALMEHNIQRLLAYHTLENIGIILL 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 395 GIGS-----------ISDTGLNGAILQIISHGFIGAALFFLAGTSYDRLRLLYLDEMGGMAIPMPKIFTIFTILSMASLA 463
Cdd:PRK08042 287 GLGAgvtgialeqpaLIALGLVGGLYHLLNHSLFKSVLFLGAGSVWFRTGHRDIEKLGGIGKKMPVISIAMLVGLMAMAA 366
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 355505216 464 LPGMSGFVAELIV---FFGIitSQKYLFMMKILITFVtAIGMILTPIYLLSILRQMfYGYKFFNTP 526
Cdd:PRK08042 367 LPPLNGFAGEWVIyqsFFKL--SNSGAFVARLLGPLL-AVGLAITGALAVMCMAKV-YGVTFLGAP 428
|
|
| PRK12646 |
PRK12646 |
DUF4040 family protein; |
119-519 |
1.38e-15 |
|
DUF4040 family protein;
Pssm-ID: 183646 [Multi-domain] Cd Length: 800 Bit Score: 80.18 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 119 NKVIRWYSISICLIDLLLTTYAFCYHFQLDDPLIQLTENYKWINFFDFYWRLGIDGLSIGPILLTGFITTLATL-AAQPV 197
Cdd:PRK12646 23 RRALAKYAGYIALVAPIISSIYFLIQIPSVAKLQYLSTSIPWMKTLDINLDLRLDGLSLMFSLIISLIGIAVFFyATQYL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 198 TREY----QLFYFLMLAMYSgQIGPFSSRDILLFFIMWELELIPVYILLFILYTAG---------------GSVFLLMGI 258
Cdd:PRK12646 103 SSRKdnlpRFYFYLTLFMFS-MIGIVLSDNTILMYVFWELTSVSSFLLISYWYNNGdsqfgaiqsfmitvfGGLALLVGF 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 259 lgIGLYgSNEPTLNFETLTNQSYPVA---LEIILYTAFLIAFAVKSPIIPLHTWLPDTHGEAHYSTCMLLAGILLKMGAY 335
Cdd:PRK12646 182 --IMLY-IMTGTNNITEILGQADHIKnhgLFIPMIFMFLLGAFTKSAQFPFHIWLPRAMAAPTPVSAYLHSATMVKAGIF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 336 GLVRINMELFSHAHSIFCpwLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIILGIG--------------SISD 401
Cdd:PRK12646 259 LLFRFTPLLGLSNMYIYI--VTFVGLITMLFGSITALKQWDLKGILAYSTISQLGMIMAMVGigggyaqhqqdaiaSIYV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 402 TGLNGAILQIISHGFIGAALFFLAGTSYDRLRLLYLDEMGGMAIPMPKIFTIFTILSMASLALPGMSGFVAELIVFFGII 481
Cdd:PRK12646 337 FVLFAALFHLMNHAIFKCALFMGVGIIDHEAGTRDIRILSGMRQLFPKMNLVMTIAALSMAGVPFLNGFLSKEMFLDALT 416
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 355505216 482 TS---QKYLFMMKILITFVTAIGMILTPIYLLSILRQMFYG 519
Cdd:PRK12646 417 QTgqlSQFSLISMIIIVFIGVIASIFTFTYALYMVKEVFWG 457
|
|
| ND5 |
MTH00032 |
NADH dehydrogenase subunit 5; Provisional |
128-477 |
3.34e-15 |
|
NADH dehydrogenase subunit 5; Provisional
Pssm-ID: 214407 [Multi-domain] Cd Length: 669 Bit Score: 78.85 E-value: 3.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 128 SICLIDLLLTTYAFCYHFQLDDPLIQLtENYKWINFFDFYWRLGI--DGLSIGPILLTGFITTLATLAAQPVTRE----- 200
Cdd:MTH00032 33 TICMGSSTLIALFLAYEVLINDAVVHI-ELYKWIESEIFITHIGLlyDTLSVTMLLVISSISTLVHIYSTSYMSDdphvp 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 201 -----YQLFYFLMLAMysgqigpFSSRDILLFFIMWELELIPVYILLF---------------ILYTAGGSVFLLMGI-- 258
Cdd:MTH00032 112 rflcyLSLFTFLMMVL-------VTSDNYLQLFIGWEGVGVCSYLLVAfwttriqankaaikaIVVNRVGDVGVILGMvl 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 259 ------------LGIGLYGSNEPTLNFETLTNQSYPVALEIILYTAFLIAFAVKSPIIPLHTWLPDTHGEAHYSTCMLLA 326
Cdd:MTH00032 185 iyktigsldfltFNGGSVGSGIMDRGYYGGGAYESPLAPFAIIGILLLIGCIGKSAQLGLHTWLPDAMEGPTPVSALIHA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 327 GILLKMGAYGLVRiNMELFSHAhSIFCPWLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIILGIGsiSDTGLNG 406
Cdd:MTH00032 265 ATMVTAGVFLMIR-SFPLFEKA-PLTLLIITIFGALTAFFAATVGLVQNDLKKVIAYSTCSQLGYMVLIIG--IEGSHNV 340
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 355505216 407 AILQIISHGFIGAALFFLAGTSYDRLRLLYLD--EMGGMAIPMPKIFTIFTILSMASLALPGMSGFVAELIVF 477
Cdd:MTH00032 341 GLFHLVNHAFFKALLFLSAGSVIHSTTVDEQDmrKMGGLIHSIPFTYTMMLIGSFSIMGLPYLTGFYSKDLIL 413
|
|
| NDH_I_L |
TIGR01974 |
proton-translocating NADH-quinone oxidoreductase, chain L; This model describes the 12th ... |
97-519 |
4.68e-14 |
|
proton-translocating NADH-quinone oxidoreductase, chain L; This model describes the 12th (based on E. coli) structural gene, L, of bacterial NADH dehydrogenase I, as well as chain 5 of the corresponding mitochondrial complex I and subunit 5 (or F) of the chloroplast NAD(P)H-plastoquinone dehydrogenase complex. [Energy metabolism, Electron transport]
Pssm-ID: 273905 [Multi-domain] Cd Length: 609 Bit Score: 75.01 E-value: 4.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 97 LTIVVVFPIAaGSLIFLFPHR--GNKVIRWYSISICLIDLLLTTYAFCyHFQLDDPLIQLTEN-YKWINF--FDFYWRLG 171
Cdd:TIGR01974 3 IFLIVFLPLI-GFLIAGLFGRriGERVSGIIGIGSVGLSAALSAFVFV-DFFLNGEGEAFTQSlFPWISVggFQVDFGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 172 IDGLSIGPILLTGFITTLATL------AAQPVTREY----QLFYFLMLAMysgqigpFSSRDILLFFIMWELELIPVYIL 241
Cdd:TIGR01974 81 LDGLSLTMLVVVTGVGSLVHIysigymAHDEGYSRFfaylNLFTFSMLML-------VLADNFLQLFFGWEGVGLCSYLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 242 L----------------FILyTAGGSVFLLMGILGIGLYGSnepTLNFETLTNQSYPVALEIILYTAFLIAFAV--KSPI 303
Cdd:TIGR01974 154 IgfwykkpsannaaikaFVV-NRVGDFGLLLGIFLIFWYFG---TLNFQEVFALAPGAFFSALTLICLLLFIGAmgKSAQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 304 IPLHTWLPD-----THGEA--HYSTcMLLAGILLkmgaygLVRINmELFSHAHSIFCpWLMILGSIQIIYAASTSFGQRN 376
Cdd:TIGR01974 230 LPLHTWLPDamegpTPVSAliHAAT-MVTAGVYL------VARTS-PLFELSPTALY-LVTIIGAITALFAATVALVQND 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 377 LKKRIAYSSVSHMG--FIILGIGsisdtGLNGAILQIISHGFIGAALFFLAGT----SYDRLRLLYldeMGGMAIPMPKI 450
Cdd:TIGR01974 301 IKRILAYSTMSQLGymFLALGVG-----AYAAAIFHLMTHAFFKALLFLGAGSvihaMHHEQDIRK---MGGLRKKMPVT 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 355505216 451 FTIFTILSMASLALPGMSGFVAELIVFFGIITSQKYLFMMKILItfvtaIGMILTPIYLLSILRQMFYG 519
Cdd:TIGR01974 373 YITFLIGSLALIGFPGFAGFFSKDLILEAAFASGTHSFLFVAGL-----IGAFLTAFYSFRLIFMVFHG 436
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
3-72 |
1.20e-13 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 67.81 E-value: 1.20e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 355505216 3 HSVKIYDTCIGCTQCVRACPTDVLEMIPWDGCKAKQIASA-PRTEDCVGCKRCESACPTDFLSVRVYLGPE 72
Cdd:cd10549 34 GPEIDEDKCVFCGACVEVCPTGAIELTPEGKEYVPKEKEAeIDEEKCIGCGLCVKVCPVDAITLEDELEIV 104
|
|
| PRK12666 |
PRK12666 |
putative monovalent cation/H+ antiporter subunit D; Reviewed |
294-477 |
3.55e-13 |
|
putative monovalent cation/H+ antiporter subunit D; Reviewed
Pssm-ID: 237166 [Multi-domain] Cd Length: 528 Bit Score: 72.19 E-value: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 294 LIAFAVKSPIIPLHTWLPDTHGEAHYSTCMLLAgILLKMGAYGLVRINMELFSHA----HSIFCPWLMILGSIQIIYAAS 369
Cdd:PRK12666 217 LVVFLIKAAMWPLNFWLPPAYAAASAPVAALFA-IMTKVGIYAILRLSTLLFGPEagasAGFGQDWLLPGGLATLAFGAI 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 370 TSFGQRNLKKRIAYSSVSHMGFIILGIGSISDTGLNGAILQIISHGFIGAALFFLA-------GTSYDRL---RLLYLDE 439
Cdd:PRK12666 296 GVLAAQRLRRLAAYLVLVSSGTLLAAIGLGNPAATAAALYYLVHSTLAAAALFLLAdlverqrGAAADRLavtPELYDLD 375
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 355505216 440 MG-----GMAIPMPKIF--TIFTILSMASLALPGMSGFVAELIVF 477
Cdd:PRK12666 376 EEeeeevGVAIPATMALlgLLFFICALALAGLPPLSGFLGKFALL 420
|
|
| Fer4_7 |
pfam12838 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
11-61 |
1.13e-12 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 463724 [Multi-domain] Cd Length: 51 Bit Score: 62.54 E-value: 1.13e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 355505216 11 CIGCTQCVRACPTDVLEMIPWDGCKAKQIASApRTEDCVGCKRCESACPTD 61
Cdd:pfam12838 1 CIGCGACVAACPVGAITLDEVGEKKGTKTVVI-DPERCVGCGACVAVCPTG 50
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
5-61 |
6.69e-12 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 62.80 E-value: 6.69e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 355505216 5 VKIYDTCIGCTQCVRACPTDVLEMIPwdgCKAKQIASAPRTEDCVGCKRCESACPTD 61
Cdd:cd10549 2 KYDPEKCIGCGICVKACPTDAIELGP---NGAIARGPEIDEDKCVFCGACVEVCPTG 55
|
|
| COG1149 |
COG1149 |
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
8-61 |
1.37e-11 |
|
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];
Pssm-ID: 440763 [Multi-domain] Cd Length: 68 Bit Score: 60.13 E-value: 1.37e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 355505216 8 YDTCIGCTQCVRACPTDVLEMipwDGCKAKQIasapRTEDCVGCKRCESACPTD 61
Cdd:COG1149 10 EEKCIGCGLCVEVCPEGAIKL---DDGGAPVV----DPDLCTGCGACVGVCPTG 56
|
|
| PRK12649 |
PRK12649 |
putative monovalent cation/H+ antiporter subunit A; Reviewed |
92-521 |
2.53e-11 |
|
putative monovalent cation/H+ antiporter subunit A; Reviewed
Pssm-ID: 183649 [Multi-domain] Cd Length: 789 Bit Score: 66.39 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 92 NYFPWLTIVVVFPIAAGSLIFLFPHRGNKVIRWYSISICLIDLLLTTYAFCYHFQLDdpliQLTENYKWINFFDFYWRLG 171
Cdd:PRK12649 2 DSFNAIVLAIFLPFILAWTVPVLEKVLKQRIGWFAAAIAFTSFALIAQVAPEVIHGT----IITGSISWLPSAGVEFSIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 172 IDGLS---------IGPILLT---GFITTLATLaaqpvTREYQLFYFLMLAMysgqIGPFSSRDILLFFIMWELELIPVY 239
Cdd:PRK12649 78 ADGLAvligliasgIGVIIMSysnGYMSHKEDL-----PRYYQYLLLFMGSM----IGMVFSGNTIQLFIFWELTSITSF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 240 ILL---------------FILYTAGGSVFLLMGILGIG-LYGSNE--PTLNFETLTNQSYPVALEIILYTAFLIAFAVKS 301
Cdd:PRK12649 149 MLIgywrhrpesvygatkSLLITAGGGLFMFAGFLLLHvITGTYDiaTILQDSELIENIKGHPLFLITLILIFIGAAAKS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 302 PIIPLHTWLPDTHGEAHYSTCMLLAGILLKMGAYGLVRInmelfshaHSIFC---PWLMIL---GSIQIIYAASTSFGQR 375
Cdd:PRK12649 229 AQGPFYIWLPNAMEAPTPVSAFLHSATMVKAGVYLVARI--------HPIFSgteAWFILVsgtGMITMVLAGFLAFRQT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 376 NLKKRIAYSSVSHMGFIILGIGSIS----DTGLNGAILQIISHGFIGAALFFLAGTSYDRLRLLYLDEMGGMAIPMPKIF 451
Cdd:PRK12649 301 DIKAILAYSTISQLAYLMTMYGYTTyhepGLGVAAATFHLLNHATFKACLFLVAGIVAHEAATRDIRKLGGLRKEMPITF 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 355505216 452 TIFTILSMASLALPGMSGFVAELIVFFGIITSQKYL-FMMKILITFVTAIGMILTPIYLLSILRQMFYGYK 521
Cdd:PRK12649 381 IVASIAALAMAGIPPLNGFLSKEMFYETSVEMGALIgGPFTIIIPAVAVLGGVFTFAYSIKLIDGIFLGER 451
|
|
| PsaC |
COG5703 |
Photosystem I reaction center iron-sulfur center subunit VII, PsaC [Energy production and ... |
1-65 |
4.41e-11 |
|
Photosystem I reaction center iron-sulfur center subunit VII, PsaC [Energy production and conversion]; Photosystem I reaction center iron-sulfur center subunit VII, PsaC is part of the Pathway/BioSystem: Photosystem I
Pssm-ID: 444413 [Multi-domain] Cd Length: 82 Bit Score: 59.07 E-value: 4.41e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 355505216 1 MSHSVKIYDTCIGCTQCVRACPTDVLEMIPWDGCKAKQIASAPRTEDCVGCKRCESACPTDFLSV 65
Cdd:COG5703 1 MSHSVKIYDTCIGCTQCVRACPTDVLEMVPWDGCKAGQIAASPRTEDCVGCKRCETACPTDFLSI 65
|
|
| PRK12644 |
PRK12644 |
putative monovalent cation/H+ antiporter subunit A; Reviewed |
210-508 |
5.00e-11 |
|
putative monovalent cation/H+ antiporter subunit A; Reviewed
Pssm-ID: 237154 [Multi-domain] Cd Length: 965 Bit Score: 65.72 E-value: 5.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 210 AMYsgqiGPFSSRDILLFFIMWELELIPVYILL----------------FILYTAGGsvfLLMgILGIGLYGSNEPTLNF 273
Cdd:PRK12644 118 AMF----GLVTSDNLLLLYVFWELTTVLSFLLIghyaeraasrraalqaLLVTTAGG---LAM-LVGIIILGQAAGTYRL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 274 ETLTNQSYPVALEIILYTAFLIAFAVKSPIIPLHTWLPDTHGEAHYSTCMLLAGILLKMGAYGLVRinmelFSHAHSIFC 353
Cdd:PRK12644 190 SELLADPPTGPAVSVAVVLILVGALSKSAIVPFHFWLPGAMAAPTPVSAYLHAAAMVKAGIYLVAR-----LAPGFADVP 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 354 PW---LMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIIL--GIGSiSDTGLNGAILqIISHGFIGAALFFL---- 424
Cdd:PRK12644 265 VWrptVLVLGLATMLLGGWRALRQHDLKLILAYGTVSQLGFLTVlvGIGT-RDAALAGLAM-LLAHALFKAALFLVvgii 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 425 ---AGTSyDrlrllyLDEMGGMAIPMPKIFtIFTILSMASLA-LPGMSGFVAELIVFFGIITSQkYLFMMKILITFVTAI 500
Cdd:PRK12644 343 dhsTGTR-D------IRKLSGLGRRQPVLA-VVAALAAASMAgLPPLLGFVAKEAALEAVLHDG-ALGPAGPVVLAGIVL 413
|
....*...
gi 355505216 501 GMILTPIY 508
Cdd:PRK12644 414 GSILTVAY 421
|
|
| ND5 |
MTH00208 |
NADH dehydrogenase subunit 5; Provisional |
220-426 |
6.50e-11 |
|
NADH dehydrogenase subunit 5; Provisional
Pssm-ID: 177251 [Multi-domain] Cd Length: 628 Bit Score: 64.99 E-value: 6.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 220 SSRDILLFFIMWEleliPVYILLFIL-------------------YTAGGSVFLLMgILGIGLYGSNEPTLNFETLTNQS 280
Cdd:MTH00208 156 SSNNLFLLFIGWE----GVGFLSFLLiswwttrndanssalqaviYNRIGDIGIIL-FLSLSLINFNSWNLNEILSLNNS 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 281 YPVALEIILYTAfLIAFAVKSPIIPLHTWLPD-----THGEA--HYSTcMLLAGILLkmgaygLVRINmELFSHaHSIFC 353
Cdd:MTH00208 231 NSFLINILLFGI-LLAAAGKSAQFGLHPWLPAamegpTPVSAllHSST-MVVAGVFL------LIRTS-PLISN-SPWFL 300
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 355505216 354 PWLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIILGIgsisdtGLNG---AILQIISHGFIGAALFFLAG 426
Cdd:MTH00208 301 SLCLILGSLTALFAASTAISQHDIKKIIAYSTTSQLGLMVVAI------GLNQpnlALFHICTHAFFKAMLFLCSG 370
|
|
| NapF |
COG1145 |
Ferredoxin [Energy production and conversion]; |
5-65 |
7.66e-11 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440760 [Multi-domain] Cd Length: 238 Bit Score: 62.43 E-value: 7.66e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 355505216 5 VKIYDTCIGCTQCVRACPTDVLEMIpwDGCKAKQIasapRTEDCVGCKRCESACPTDFLSV 65
Cdd:COG1145 178 VIDAEKCIGCGLCVKVCPTGAIRLK--DGKPQIVV----DPDKCIGCGACVKVCPVGAISL 232
|
|
| ND5 |
MTH00020 |
NADH dehydrogenase subunit 5; Reviewed |
128-470 |
1.42e-10 |
|
NADH dehydrogenase subunit 5; Reviewed
Pssm-ID: 214400 [Multi-domain] Cd Length: 610 Bit Score: 63.94 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 128 SICLIDLLLTTYAFCYHFQLDDPLIQLtENYKWIN--FFDFYWRLGIDGLSIGPILLTGFITTLATLAAQPVTRE----- 200
Cdd:MTH00020 33 SSCLIISLSWSFLIFYEILFNSSTTYI-KLWRWLDsdLLTVYFGLQFDGLVAIMLLVVTTVSTLVHIFSTAYMRGdphip 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 201 -----YQLFYFLMLAMysgqigpFSSRDILLFFIMWELELIPVYILLFILYT---------------AGGSVFLLMGILG 260
Cdd:MTH00020 112 rfmsyLSLFTFLMVVL-------VTSDNYLQLFIGWEGVGLCSYLLINFWLTrieankaaikamlvnRVGDIGLLLAMFL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 261 I-GLYGSneptLNFETLTNQSYPVALEIILYTAFLIAFAV--KSPIIPLHTWLPDTHGEAHYSTCMLLAGILLKMGAYGL 337
Cdd:MTH00020 185 LwDRFGS----LDFSSVFNMVVSAPSSDITLICLFLFIGAvgKSAQLGLHTWLPDAMEGPTPVSALIHAATMVTAGVFLL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 338 VRINmELFSHAHSIFCPwLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIILGIG-SISDTGLngaiLQIISHGF 416
Cdd:MTH00020 261 IRSS-PLFEQAPLALII-VTIVGSLTVFFAATVGLVQNDLKKVIAYSTCSQLGYMVVACGlSHYSISL----FHLMNHAF 334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 355505216 417 IGAALFFLAGTSYDRLrllyLDE-----MGGMAIPMPKIFTIFTILSMASLALPGMSGF 470
Cdd:MTH00020 335 FKALLFLSAGSVIHAL----SDEqdmrkMGGLISFLPLTYIFFLIGSLSLMGFPYLTGF 389
|
|
| NuoI |
TIGR01971 |
NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of ... |
9-72 |
1.45e-10 |
|
NADH-quinone oxidoreductase, chain I; This model represents the I 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, but may act on NADPH and/or plastoquinone in cyanobacteria and plant chloroplasts. This model excludes "I" subunits from the closely related F420H2 dehydrogenase and formate hydrogenlyase complexes. [Energy metabolism, Electron transport]
Pssm-ID: 273902 [Multi-domain] Cd Length: 122 Bit Score: 58.97 E-value: 1.45e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 355505216 9 DTCIGCTQCVRACPTDVLEMIPWDGCKAKQIASAPR--TEDCVGCKRCESACPTDFLsvrvYLGPE 72
Cdd:TIGR01971 43 EKCIGCTLCAAVCPADAIRVVPAEGEDGKRRLKFYEinFGRCIFCGLCEEACPTDAI----VLTPE 104
|
|
| COG2768 |
COG2768 |
Uncharacterized Fe-S cluster protein [Function unknown]; |
5-80 |
1.47e-10 |
|
Uncharacterized Fe-S cluster protein [Function unknown];
Pssm-ID: 442050 [Multi-domain] Cd Length: 74 Bit Score: 57.43 E-value: 1.47e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 355505216 5 VKIYDTCIGCTQCVRACPTDVLEMIPwdgcKAKQIasapRTEDCVGCKRCESACPTDFLSVRVYLGPETTRSMARA 80
Cdd:COG2768 7 YVDEEKCIGCGACVKVCPVGAISIED----GKAVI----DPEKCIGCGACIEVCPVGAIKIEWEEDEEFQEKMAEY 74
|
|
| RnfB |
COG2878 |
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ... |
9-61 |
3.33e-10 |
|
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase
Pssm-ID: 442125 [Multi-domain] Cd Length: 254 Bit Score: 60.78 E-value: 3.33e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 355505216 9 DTCIGCTQCVRACPTDVLEMIPwdgckaKQIAsaprT---EDCVGCKRCESACPTD 61
Cdd:COG2878 137 YGCIGCGDCIKACPFDAIVGAA------KGMH----TvdeDKCTGCGLCVEACPVD 182
|
|
| PRK07118 |
PRK07118 |
Fe-S cluster domain-containing protein; |
8-65 |
6.10e-10 |
|
Fe-S cluster domain-containing protein;
Pssm-ID: 235941 [Multi-domain] Cd Length: 280 Bit Score: 60.33 E-value: 6.10e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 8 YDTCIGCTQCVRACPTDVLEMIPwdgcKAKQIASAPRTED------------CVGCKRCESACPTDFLSV 65
Cdd:PRK07118 167 EDKCTGCGACVKACPRNVIELIP----KSARVFVACNSKDkgkavkkvcevgCIGCGKCVKACPAGAITM 232
|
|
| Fer4_21 |
pfam14697 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
9-61 |
1.54e-09 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 434137 [Multi-domain] Cd Length: 59 Bit Score: 53.82 E-value: 1.54e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 355505216 9 DTCIGCTQCVRACPTDVLEMIPWDGckaKQIAsAPRTEDCVGCKRCESACPTD 61
Cdd:pfam14697 6 DTCIGCGKCYIACPDTSHQAIVGDG---KRHH-TVIEDECTGCNLCVSVCPVD 54
|
|
| Fer4_9 |
pfam13187 |
4Fe-4S dicluster domain; |
11-63 |
2.30e-09 |
|
4Fe-4S dicluster domain;
Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 53.33 E-value: 2.30e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 355505216 11 CIGCTQCVRACPTDVLEMipwdGCKAKQIASAPRTEDCVGCKRCESACPTDFL 63
Cdd:pfam13187 2 CTGCGACVAACPAGAIVP----DLVGQTIRGDIAGLACIGCGACVDACPRGAI 50
|
|
| DsrA |
COG2221 |
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ... |
9-61 |
2.74e-09 |
|
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];
Pssm-ID: 441823 [Multi-domain] Cd Length: 69 Bit Score: 53.52 E-value: 2.74e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 355505216 9 DTCIGCTQCVRACPTDVLEmipWDGCKAKQIAsaprtEDCVGCKRCESACPTD 61
Cdd:COG2221 15 EKCIGCGLCVAVCPTGAIS---LDDGKLVIDE-----EKCIGCGACIRVCPTG 59
|
|
| PRK12648 |
PRK12648 |
putative monovalent cation/H+ antiporter subunit A; Reviewed |
97-519 |
3.14e-09 |
|
putative monovalent cation/H+ antiporter subunit A; Reviewed
Pssm-ID: 237157 [Multi-domain] Cd Length: 948 Bit Score: 59.82 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 97 LTIVVVFPIAAGSLIFLFPHRGNKVIRWYSISICLIDLLLTtyAFCYHFQLDDPLIQLTenYKWINFFDFYWRLGIDGLS 176
Cdd:PRK12648 3 LLLLVLLPFLGALLAALLPRNARNAEAWLAGLVALAALVLL--ALLYPAVAAGEVIRAE--IEWLPALGLNLSLRLDGLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 177 IgpiLLTGFITTLATL----------AAQPVTREYQLFYFLMLAMysgqIGPFSSRDILLFFIMWELELIPVYILlfILY 246
Cdd:PRK12648 79 W---LFALLILGIGLLvvlyaryylsPADPVPRFFSFLLLFMGAM----LGIVLSGNLILLVVFWELTSLSSFLL--IGY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 247 -----------------TAGGSVFLLMGILGIG-LYGSNEPT--LNFETLTNQS--YPVALEIILYTAFliafaVKSPII 304
Cdd:PRK12648 150 whhradarrgarmaltvTGAGGLALLAGVLLLGhIVGSYDLDvvLAAGDLIRAHplYPPALVLILLGAF-----TKSAQF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 305 PLHTWLPdtHGEA---------HYSTcMLLAGILLkmgaygLVRinmelFSHAHSIFCPWLMILGS---IQIIYAASTSF 372
Cdd:PRK12648 225 PFHFWLP--HAMAaptpvsaylHSAT-MVKAGVFL------LAR-----LWPVLAGTEEWFWIVGGaglITLLLGAYFAL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 373 GQRNLKKRIAYSSVSHMGFIILGIGSISDTGLNGAILQIISHGFIGAALFFLAG-----TSYDRLRLLyldemGGMAIPM 447
Cdd:PRK12648 291 FQHDLKGLLAYSTISHLGLITLLLGLGSPLAAVAAIFHIINHATFKASLFMAAGiidheTGTRDMRRL-----SGLRRLM 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 355505216 448 PKIFTIFTILSMASLALPGMSGFVA-ELivFFGIITSQKYLFMMKILITFVTAIGMILTPIYLLSILRQMFYG 519
Cdd:PRK12648 366 PITATLAMVAAAAMAGVPLLNGFLSkEM--FFAETLDTHLLGSLDWLLPVAATLAGAFSVAYSLRFIHDVFFG 436
|
|
| PorD |
COG1144 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ... |
7-61 |
4.64e-09 |
|
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440759 [Multi-domain] Cd Length: 84 Bit Score: 53.52 E-value: 4.64e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 355505216 7 IYDTCIGCTQCVRACPTDVlemIPWDGCKAKQIAsaprTEDCVGCKRCESACPTD 61
Cdd:COG1144 28 DEDKCIGCGLCWIVCPDGA---IRVDDGKYYGID----YDYCKGCGICAEVCPVK 75
|
|
| IorA |
COG4231 |
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ... |
1-61 |
5.67e-09 |
|
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];
Pssm-ID: 443375 [Multi-domain] Cd Length: 76 Bit Score: 52.74 E-value: 5.67e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 355505216 1 MSHSVkIYDTCIGCTQCVRACPTDVLEMIPWdgcKAKqIasapRTEDCVGCKRCESACPTD 61
Cdd:COG4231 15 MRYVI-DEDKCTGCGACVKVCPADAIEEGDG---KAV-I----DPDLCIGCGSCVQVCPVD 66
|
|
| PRK06590 |
PRK06590 |
NADH:ubiquinone oxidoreductase subunit L; Reviewed |
90-470 |
1.88e-08 |
|
NADH:ubiquinone oxidoreductase subunit L; Reviewed
Pssm-ID: 235836 [Multi-domain] Cd Length: 624 Bit Score: 57.09 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 90 MTNYfpwLTIVVVFPIAAGSLIFLFPHR-GNKVIRWYSISICLIDLLLTTYAFCYHFQLDDPLIQLTeNYKWINF--FDF 166
Cdd:PRK06590 1 MMNL---LWLIVLLPLIGALILGLFGRRiGEKWAHLVGTGLVGLSALLSLVVFFDFLLGGGRAFSQT-LWTWISVgdFDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 167 YWRLGIDGLSIgpiLLTGFITTLATL---------AAQPVTREY----QLFYF--LMLAMysgqigpfsSRDILLFFIMW 231
Cdd:PRK06590 77 DFGLRVDGLSA---TMLVVVTGVSFLvhiysigymAHDEGYRRFfaylNLFTFsmLMLVL---------SDNLLQLFFGW 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 232 ELELIPVYILL----------------FILyTAGGSVFLLMGILGIGLY-GSneptLNFETLTNQSYPVALE---IILYT 291
Cdd:PRK06590 145 EGVGLCSYLLIgfwykkpsagaaamkaFIV-NRVGDVGLALGIFLLFAEfGS----LNYDEVFAAAPQFFGLgwsALTLI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 292 AFL--IAFAVKSPIIPLHTWLPD-----THGEA--HYSTcMLLAGILLkmgaygLVRINmELFSHAHSIFCpWLMILGSI 362
Cdd:PRK06590 220 CLLlfIGAMGKSAQFPLHTWLPDamegpTPVSAliHAAT-MVTAGVYL------VARMS-PLFELSPEALL-FVAIVGAV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 363 QIIYAASTSFGQRNLKKRIAYSSVSHMGFIILGIGSIsdtGLNGAILQIISHGFIGAALFFLAG-----TSYDrlrllyL 437
Cdd:PRK06590 291 TALFAAFIGLVQTDIKRVLAYSTMSQLGYMFLALGVG---AYAAAIFHLMTHAFFKALLFLGAGsvihaMHHE------Q 361
|
410 420 430
....*....|....*....|....*....|....*
gi 355505216 438 D--EMGGMAIPMPKIFTIFTILSMASLALPGMSGF 470
Cdd:PRK06590 362 DirKMGGLRKKMPVTYATFLIGTLALIGIPPFAGF 396
|
|
| ND5 |
MTH00211 |
NADH dehydrogenase subunit 5; Provisional |
244-525 |
3.16e-08 |
|
NADH dehydrogenase subunit 5; Provisional
Pssm-ID: 214459 [Multi-domain] Cd Length: 597 Bit Score: 56.50 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 244 ILYTAGGSVFLLMGIlGIGLYGSNEPTLNFETLTNQSypvalEIILYTAFLIAFAVKSPIIPLHTWLPDTHgEA------ 317
Cdd:MTH00211 167 VIYNRIGDIGLLLSM-VWLLLNLNSWEISQLFILNLD-----LTLFLLGLLLAAMGKSAQFGFHPWLPSAM-EGptpvsa 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 318 --HYSTcMLLAGILLKMGAYGLVRINMELFShahsifcpWLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIILG 395
Cdd:MTH00211 240 llHSST-MVVAGVFLLIRLSPLFQNNQLILG--------AVLLLGALTMLFGALCALTQNDIKKIVAFSTTSQLGLMMVT 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 396 IgsisdtGLNG---AILQIISHGFIGAALFFLAGTS-YDRLRLLYLDEMGGMAIPMPKIFTIFTILSMASLALPGMSGFV 471
Cdd:MTH00211 311 L------GLNQpqlAFLHICTHAFFKAMLFMCSGSIiHGLNNEQDIRKMGGLSKNLPFTSSCLFLGSLALMGFPFLSGFF 384
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 355505216 472 AELIVFFGIITSQKYLFMMkilitFVTAIGMILTPIYLLSILRQMFYGYKFFNT 525
Cdd:MTH00211 385 SKDLILESMNGSYLNAWAL-----LLTLLATSLTAAYSFRLIFLSLGGYPRFLS 433
|
|
| ND5 |
MTH00210 |
NADH dehydrogenase subunit 5; Provisional |
264-470 |
3.18e-08 |
|
NADH dehydrogenase subunit 5; Provisional
Pssm-ID: 177253 [Multi-domain] Cd Length: 616 Bit Score: 56.55 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 264 YGSNEPTLNFETLTNQSYPVALEIILYTAFLIAFAvKSPIIPLHTWLPDTHGEAHYSTCMLLAGILLKMGAYGLVRiNME 343
Cdd:MTH00210 189 FGTLEFSTISSLLVTNINKESLTIICLLLFIGAVG-KSAQLGLHTWLPDAMEGPTPVSALIHAATMVTAGVFLIIR-SGP 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 344 LFSHAhSIFCPWLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIILGIGsISdtGLNGAILQIISHGFIGAALFF 423
Cdd:MTH00210 267 LFEGS-PLALTIVTILGALTAFFAATVGVVQNDLKKVIAYSTCSQLGYMVMVCG-IS--NYSTSLFHLMNHAFFKALLFL 342
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 355505216 424 LAGTSYDRLRllylDE-----MGGMAIPMPKIFTIFTILSMASLALPGMSGF 470
Cdd:MTH00210 343 SAGSVIHAVS----DEqdmrkMGGLIKSIPFTYVMILIGSLSLMGFPYLTGF 390
|
|
| ND5 |
MTH00004 |
NADH dehydrogenase subunit 5; Validated |
258-470 |
5.57e-08 |
|
NADH dehydrogenase subunit 5; Validated
Pssm-ID: 214398 [Multi-domain] Cd Length: 602 Bit Score: 55.56 E-value: 5.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 258 ILGIGLYGSNEPTLNF-ETLTNQSYPvaleIILYTAFLIAFAVKSPIIPLHTWLPD-----THGEA--HYSTcMLLAGIL 329
Cdd:MTH00004 183 ILSMAWLAMTLNTWEIqQLFSPTQTP----TLPLLGLILAATGKSAQFGLHPWLPAamegpTPVSAllHSST-MVVAGIF 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 330 LkmgaygLVRIN--MELFSHAHSIfCpwlMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIILGIgsisdtGLNG- 406
Cdd:MTH00004 258 L------LIRTHplLQNNQTALTI-C---LCLGALTTLFAATCALTQNDIKKIIAFSTSSQLGLMMVTI------GLNQp 321
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 355505216 407 --AILQIISHGFIGAALFFLAGTSYDRLRllylDE-----MGGMAIPMPKIFTIFTILSMASLALPGMSGF 470
Cdd:MTH00004 322 qlAFLHISTHAFFKAMLFLCSGSIIHNLN----NEqdirkMGGLQKTLPITSSCLTIGNLALMGTPFLSGF 388
|
|
| PRK07390 |
PRK07390 |
NAD(P)H-quinone oxidoreductase subunit F; Validated |
250-519 |
1.00e-07 |
|
NAD(P)H-quinone oxidoreductase subunit F; Validated
Pssm-ID: 236008 [Multi-domain] Cd Length: 613 Bit Score: 54.92 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 250 GSVFLLMGILGIGLYGsnePTLNFETLTNQSYPVALEIIlyTAFLIAFAV------KSPIIPLHTWLpDTHGEAHYSTCM 323
Cdd:PRK07390 183 GDLLLLMGVVALSPLA---GTLNFSDLAAWAATANLDPL--TATLLGLALiagptgKCAQFPLHLWL-DEAMEGPNPASI 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 324 LLAGILLKMGAYGLVRInMELFSHahsifCPW----LMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIILGIGsi 399
Cdd:PRK07390 257 LRNSVVVATGAWVLIKL-QPVLAL-----SPValtvLIVIGTVTAIGASLVAIAQIDIKRALSYSTSAYLGLVFIAVG-- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 400 sdTGLNGAILQII-SHGFIGAALFFLAGT------SYDrlrllyLDEMGGMAIPMPKIFTIFTILSMASLALPGMSGFVA 472
Cdd:PRK07390 329 --LQQPDIALLLLlTHAIAKALLFMSVGSiilttiTQD------LTELGGLWSRMPATTLAFLVGSAGLVALLPLGGFWA 400
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 355505216 473 ELIVFFGIITSQKYLFMMKILITFVTAIGmiltpiyLLSILRQMFYG 519
Cdd:PRK07390 401 LLRLADGLWAVSPWLVGVLLLVNALTAFN-------LTRVFRLVFLG 440
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
5-59 |
1.01e-07 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 404174 [Multi-domain] Cd Length: 56 Bit Score: 48.79 E-value: 1.01e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 355505216 5 VKIYDTCIGCTQCVRACPTDvlemIPWDGCKAKQIASAPR---TEDCVGCKRCESACP 59
Cdd:pfam13237 3 VIDPDKCIGCGRCTAACPAG----LTRVGAIVERLEGEAVrigVWKCIGCGACVEACP 56
|
|
| oorD |
PRK09626 |
2-oxoglutarate-acceptor oxidoreductase subunit OorD; Reviewed |
11-62 |
1.05e-07 |
|
2-oxoglutarate-acceptor oxidoreductase subunit OorD; Reviewed
Pssm-ID: 236597 [Multi-domain] Cd Length: 103 Bit Score: 50.10 E-value: 1.05e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 355505216 11 CIGCTQCVRACPTDVLEMIPWDGCKAKQIASAPRTEDCVGCKRCESACPtDF 62
Cdd:PRK09626 18 CKACDICVSVCPAGVLAMRIDPHAVLGKMIKVVHPESCIGCRECELHCP-DF 68
|
|
| PRK12664 |
PRK12664 |
putative monovalent cation/H+ antiporter subunit D; Reviewed |
285-498 |
1.11e-07 |
|
putative monovalent cation/H+ antiporter subunit D; Reviewed
Pssm-ID: 237164 [Multi-domain] Cd Length: 527 Bit Score: 54.74 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 285 LEIILYTAFLIAFAVKSPIIPLHTWLPDTHGEAHYSTCMLLAGILLKMGAYGLVRinmeLFSHAhsifcPWLMILGSIQI 364
Cdd:PRK12664 142 YTGYCKLLFMLGLLINCACFPASSWVVDAYPAASNFGIIVLSLFTTKVAALVLLL----FFSGE-----EILLFLGIITA 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 365 IYAASTSFGQRNLKKRIAYSSVSHMGFIILGIG--SISDTGLNGAILQIISHGFIGAALFFLAGTSYDRLRLLYLDEMGG 442
Cdd:PRK12664 213 IYGIIFASLEQNIRRLLCYNVVGQMGLLIIAIGfsGSSGVAIGILILQIVLSVVYQTLLFMVADSVINRTRKFNLNRVGG 292
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 355505216 443 M-AIPMPKIFTIFTILSMAslALPGMSGFVAELIVFFGIITSQ------KYLFMMKILITFVT 498
Cdd:PRK12664 293 LfKMSLEAMCCIIAILNMG--AFPGTAGFVSKSLITHSIDTAGltlvlyKKLFLICSLLLFAS 353
|
|
| ND2 |
MTH00196 |
NADH dehydrogenase subunit 2; Provisional |
243-523 |
1.45e-07 |
|
NADH dehydrogenase subunit 2; Provisional
Pssm-ID: 214453 [Multi-domain] Cd Length: 365 Bit Score: 53.88 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 243 FILYTAGGSVFLLMGILGIGLYGSNE-PTLNFETLTNQSYPVALEIILYTAFLIAFAVKSPIIPLHTWLPDTHGEAHYST 321
Cdd:MTH00196 50 FVLGALSSGLFLFGCALLCGTTGGLHlSYINLVLNSGQSFSSVSVPIGYLLIIVALLFKLSVAPFHMWAPDVYEGAPTKT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 322 CMLLAgILLKMGAYG-LVRINMELfshahsifcPWLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIILGIGSIS 400
Cdd:MTH00196 130 TALLA-IVPKLGIFSiLVSIGLNV---------NILLIGGLFSLFVGAIGALNQTKIKRLLAYSGIGHMGFVLWGIEIGS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 401 DTGLNGAILQIISHGFIGAALFFLAGTSYDRLRLLYLDEMGGMAIPMPKIFTIFTILSMAslALPGMSGFVAELIVFFGI 480
Cdd:MTH00196 200 FESIQASLVYLFIYIIMSICVFSIILALNVYKNLIIEFSGLSRRLPILAITLALTFLSIA--GIPPLVGFLGKWLILLSG 277
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 355505216 481 ITSQKYLFMMKILITFVTAIGmiltpiYLLSILRQMFYGYKFF 523
Cdd:MTH00196 278 VVYQYYLIFLLAVFCSVIAGV------YYVRIVKILFFQANSF 314
|
|
| PRK08348 |
PRK08348 |
NADH-plastoquinone oxidoreductase subunit; Provisional |
9-64 |
1.50e-07 |
|
NADH-plastoquinone oxidoreductase subunit; Provisional
Pssm-ID: 181399 [Multi-domain] Cd Length: 120 Bit Score: 50.22 E-value: 1.50e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 355505216 9 DTCIGCTQCVRACPTDVLEMIPwdgcKAKQIASAprTEDCVGCKRCESACPTDFLS 64
Cdd:PRK08348 42 DKCVGCRMCVTVCPAGVFVYLP----EIRKVALW--TGRCVFCGQCVDVCPTGALQ 91
|
|
| RnfB |
COG2878 |
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ... |
3-60 |
1.62e-07 |
|
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase
Pssm-ID: 442125 [Multi-domain] Cd Length: 254 Bit Score: 52.69 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 3 HSVkIYDTCIGCTQCVRACPTDVLEMIP---------WD---------GCKAKQIASAPR--------------TEDCVG 50
Cdd:COG2878 162 HTV-DEDKCTGCGLCVEACPVDCIEMVPvsptvvvssWDkgkavrkvvGCIGLCCKKCCPaaaitvnnlaaiidYKKCTC 240
|
90
....*....|
gi 355505216 51 CKRCESACPT 60
Cdd:COG2878 241 CGCCEKCCPT 250
|
|
| PRK08764 |
PRK08764 |
Rnf electron transport complex subunit RnfB; |
11-66 |
1.63e-07 |
|
Rnf electron transport complex subunit RnfB;
Pssm-ID: 181550 [Multi-domain] Cd Length: 135 Bit Score: 50.69 E-value: 1.63e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 355505216 11 CIGCTQCVRACPTDVLEmipwDGCKAKQIASAPRtedCVGCKRCESACPTDFLSVR 66
Cdd:PRK08764 87 CIGCTKCIQACPVDAIV----GGAKHMHTVIAPL---CTGCELCVPACPVDCIELH 135
|
|
| ND4 |
MTH00062 |
NADH dehydrogenase subunit 4; Provisional |
206-504 |
1.89e-07 |
|
NADH dehydrogenase subunit 4; Provisional
Pssm-ID: 214413 [Multi-domain] Cd Length: 417 Bit Score: 53.39 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 206 FLMLAMYSGqIGPFSSRDILLFFIMWELELIPVYILL---------------FILYTAGGSVFLLMGILGIGLygsNEPT 270
Cdd:MTH00062 76 FLFLSLIFS-ILCFCVNNSLLFWFFYELSIIPLLYLLfsespyserylaswyFLGYLLLTSLPLLLCLLYLSL---VNGS 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 271 LNFetlTNQSYPVALEIILYTAFLIAFAVKSPIIPLHTWLPDTHGEAHYSTCMLLAGILLKMGAYGLVRINMELFSHAHS 350
Cdd:MTH00062 152 FNF---SDWGSDDSVSLIVYYVLSFMFITKVPLFPFHTWLPIVHAEASSPVSIFLSGYIMKLGLLGVYRFCGFIFSGSFL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 351 IFCPWLMILGSIQIIYAASTSFGQRNLkkriAYSSVSHMGFIILGIGSISDTGLNGAILQIISHGFIGAALFFLAGTSYD 430
Cdd:MTH00062 229 GYLFLCCLFSVFFLITACSELDGKRWL----AFLSLSHILVPVLGLFVGDWSSINLSFFYCLGHGLSAGLVFLLLWCFYE 304
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 355505216 431 ----RLRLLYLDEMGGMAIPMpkIFTIFTILSMASlaLPGMSGFVAELIVFFGIITSQKYLFMMKILITFVTAIGMIL 504
Cdd:MTH00062 305 vsgsRNWVLLKSGINGSLVLR--VIVVFSFLSLCS--FPPTIQFFCEVFLVSSSFGVLVYLLFWCFYLFFGGLVPLIL 378
|
|
| PRK12387 |
PRK12387 |
formate hydrogenlyase complex iron-sulfur subunit; Provisional |
8-60 |
3.59e-07 |
|
formate hydrogenlyase complex iron-sulfur subunit; Provisional
Pssm-ID: 183492 [Multi-domain] Cd Length: 180 Bit Score: 50.42 E-value: 3.59e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 355505216 8 YDTCIGCTQCVRACPTDVLEMiPWD---GCKAKQIaSAPRtedCVGCKRCESACPT 60
Cdd:PRK12387 37 PQQCIGCAACVNACPSNALTV-ETDlatGELAWEF-NLGR---CIFCGRCEEVCPT 87
|
|
| rnfB |
TIGR01944 |
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ... |
9-67 |
3.76e-07 |
|
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the B subunit. [Energy metabolism, Electron transport]
Pssm-ID: 273887 [Multi-domain] Cd Length: 165 Bit Score: 50.18 E-value: 3.76e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 355505216 9 DTCIGCTQCVRACPTDVlemipwdgckakqIASAPR------TEDCVGCKRCESACPTDFLSVRV 67
Cdd:TIGR01944 113 DNCIGCTKCIQACPVDA-------------IVGAAKamhtviADECTGCDLCVEPCPTDCIEMIP 164
|
|
| PRK12645 |
PRK12645 |
monovalent cation/H+ antiporter subunit A; Reviewed |
284-558 |
3.80e-07 |
|
monovalent cation/H+ antiporter subunit A; Reviewed
Pssm-ID: 237155 [Multi-domain] Cd Length: 800 Bit Score: 53.01 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 284 ALEIILYTAFliafaVKSPIIPLHTWLPD-----THGEAH-YSTCMLLAGILLKMGAYGLVRINMELFshahsifcpWL- 356
Cdd:PRK12645 212 AMILILLGAF-----TKSAQFPFYIWLPDameapTPVSAYlHSATMVKAGIYLVARFTPIFAGSQVWF---------WTv 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 357 MILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFII--LGIGSIS-----------DTGLNGAILQIISHGFIGAALFF 423
Cdd:PRK12645 278 TLVGLITLFWGSLNAVKQTDLKGILAFSTVSQLGLIMslLGIGAASlhyqgddskiyAAAITAAIFHLINHATFKGSLFM 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 424 LAG-----TSYDRLRLLyldemGGMAIPMPKIFTIFTI--LSMAslALPGMSGFVAELIVFFGIITSQKYLFM----MKI 492
Cdd:PRK12645 358 IVGivdheTGTRDIRKL-----GGLMTIMPITFTIALIgaLSMA--GLPPFNGFLSKEMFFESMLNATEANLFsldtWGV 430
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 355505216 493 LITFVTAIGMILTPIYLLSILRQMFYG-YKFFNTPNSyffdsgPRE----LFISISIL-IPVIGIGIYPDFI 558
Cdd:PRK12645 431 LFPVIAWVASVFTFVYSIIFIFKTFFGkYKPEQLPKK------AHEapigMLISPIILaSLVVVFGLFPNIL 496
|
|
| ND2 |
MTH00200 |
NADH dehydrogenase subunit 2; Provisional |
243-561 |
4.88e-07 |
|
NADH dehydrogenase subunit 2; Provisional
Pssm-ID: 177246 [Multi-domain] Cd Length: 347 Bit Score: 51.89 E-value: 4.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 243 FILYTAGGSVFLLMGILgiglygsneptlNFETLTNQSYPVALEIILYTAFLIAFAVKSPIIPLHTWLPDTHGEAHYSTC 322
Cdd:MTH00200 60 FIIQATASALLLFGGLL------------NAWTSGQWGISEMLGPLSETLILLALALKLGLAPGHFWVPDVLQGLSLQTG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 323 MLLAGILLKMGAYGLVRINMELFSHAhsifcpwLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIILGIGSISDT 402
Cdd:MTH00200 128 LILSTWQKLAPFALLIQLAPALNSNI-------LLLLGLLSVLVGGWGGLNQTQLRKILAYSSIAHLGWLLSGLVYSPNL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 403 GLNGAILQIISHGFIGAALFFLAGTSYDRLRllyldeMGGMAIPMPKIFTIFTILSMAslALPGMSGFvaelivFFGIIT 482
Cdd:MTH00200 201 ALLYLLLYVIITLTVFLLLNLLNSTKINSLS------SSKTKNPILSMLLGLTLLSLG--GLPPLTGF------FPKWLI 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 483 SQkylFMMKILITFVTAIGMILTPIYLLSILRqMFYGYKFFNTPNSYFFDSGPRE-----LFISISILIPVIGIGIYPDF 557
Cdd:MTH00200 267 LQ---ELSKQGLFIYATILLLGSLLSLFFYLR-LSYLTLLTLSPNQINMMSSWRTksnsnLLVGLLLLLSILGLPLTPQL 342
|
....
gi 355505216 558 IFSF 561
Cdd:MTH00200 343 LFLF 346
|
|
| ND5 |
MTH00066 |
NADH dehydrogenase subunit 5; Provisional |
286-470 |
7.35e-07 |
|
NADH dehydrogenase subunit 5; Provisional
Pssm-ID: 214416 [Multi-domain] Cd Length: 598 Bit Score: 52.22 E-value: 7.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 286 EIILYTAFLIAFAVKSPIIPLHTWLPD-----THGEA--HYSTcMLLAGILLkmgaygLVRINmELFSHAHSIfcpwLMI 358
Cdd:MTH00066 206 STLPLLGLILAAAGKSAQFGLHPWLPAamegpTPVSAllHSST-MVVAGIFL------LIRFH-PLLENNQTA----LTI 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 359 ---LGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIILGIgsisdtGLNG---AILQIISHGFIGAALFFLAGTSYDRL 432
Cdd:MTH00066 274 clcLGALTTLFTAACALTQNDIKKIVAFSTSSQLGLMMVTI------GLNQpqlAFFHICTHAFFKAMLFLCSGSIIHSL 347
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 355505216 433 RllylDE-----MGGMAIPMPKIFTIFTILSMASLALPGMSGF 470
Cdd:MTH00066 348 N----DEqdirkMGGLQKALPITTSCLTIGSLALTGTPFLAGF 386
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
11-80 |
7.93e-07 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 50.95 E-value: 7.93e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 355505216 11 CIGCTQCVRACPTDVlemipwdgckakqIASAPR------TEDCVGCKRCESACPTDFLSVRVYLGPET---TRSMARA 80
Cdd:PRK06991 87 CIGCTLCMQACPVDA-------------IVGAPKqmhtvlADLCTGCDLCVPPCPVDCIDMVPVTGERTgwdAWSQAQA 152
|
|
| PRK05113 |
PRK05113 |
electron transport complex protein RnfB; Provisional |
9-61 |
9.44e-07 |
|
electron transport complex protein RnfB; Provisional
Pssm-ID: 235347 [Multi-domain] Cd Length: 191 Bit Score: 49.56 E-value: 9.44e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 355505216 9 DTCIGCTQCVRACPTDVlemipwdgckakqIASAPR------TEDCVGCKRCESACPTD 61
Cdd:PRK05113 114 DNCIGCTKCIQACPVDA-------------IVGATKamhtviSDLCTGCDLCVAPCPTD 159
|
|
| PRK07376 |
PRK07376 |
NADH-quinone oxidoreductase subunit L; |
254-470 |
1.22e-06 |
|
NADH-quinone oxidoreductase subunit L;
Pssm-ID: 236005 [Multi-domain] Cd Length: 673 Bit Score: 51.56 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 254 LLMGILGI----GLYGSNEPTLNFETLTNQ-SYPVALEIILYTAFLIAFAVKSPIIPLHTWLPD-----THGEA--HYST 321
Cdd:PRK07376 189 LLLGILGLfwatGSFDFDGIADRLSELVSSgAVSGWLALLLCILVFLGPMAKSAQFPLHVWLPDamegpTPISAliHAAT 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 322 cMLLAGILLKMGAYglvrinmELFSHAhsifcPWLM----ILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIILGIG 397
Cdd:PRK07376 269 -MVAAGVFLVARMY-------PVFEQF-----PAVMtviaWTGAITAFLGASIALTQNDIKKGLAYSTISQLGYMVMAMG 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 398 SisdtGLNGA-ILQIISHGFIGAALFFLAGT---------------SYDrLRLlyldeMGGMAIPMPKIFTIFTILSMAS 461
Cdd:PRK07376 336 C----GAYSAgLFHLMTHAYFKAMLFLGSGSvihgmeevvghdpvlAQD-MRL-----MGGLRKYMPITAITFLIGCLAI 405
|
....*....
gi 355505216 462 LALPGMSGF 470
Cdd:PRK07376 406 SGIPPFAGF 414
|
|
| DMSOR_beta_like |
cd16373 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
9-60 |
1.63e-06 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319895 [Multi-domain] Cd Length: 154 Bit Score: 48.02 E-value: 1.63e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 355505216 9 DTCI------GCTQCVRACPTDVLEMIPWDGCKAKQIasapRTEDCVGCKRCESACPT 60
Cdd:cd16373 91 DRCLawqggtDCGVCVEACPTEAIAIVLEDDVLRPVV----DEDKCVGCGLCEYVCPV 144
|
|
| ND2 |
MTH00144 |
NADH dehydrogenase subunit 2; Provisional |
204-533 |
1.95e-06 |
|
NADH dehydrogenase subunit 2; Provisional
Pssm-ID: 214432 [Multi-domain] Cd Length: 328 Bit Score: 49.88 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 204 FYFLMLaMYSGQIGPFSSRDILLFFIMWELELIPVYILLFILYT--------------AGGSVFLLMGILgIGLYGSNEP 269
Cdd:MTH00144 7 LLFLFL-MVMGTLLSLSSSHWLGVWVGLEINLIGFLPLLVYKKKssesesvvkyfiiqSLGSSLLIFGSL-IMYNLSFSW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 270 tlnfetltnqsypvaleiILYTAFLIAFAVKSPIIPLHTWLPDTHGEAHYSTCMLLAGI--LLKMGAYGLVRINMELFSH 347
Cdd:MTH00144 85 ------------------FSMSLLLLGLCLKLGLFPFHFWVPSVMAGLSWLSCFLLLTWqkVAPLFLLSNFLDLYWLAYL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 348 ahsifcpwLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIILGIGSISDTGLNGAILQIISHGFIgaaLFFLAGT 427
Cdd:MTH00144 147 --------LCVISVLSALVGSIGGLNQTQVRALLAYSSISHTGWMLVAILHGSWLMWMYFLIYIVSSGFL---FFSLWSG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 428 SYDRLRLLYldemGGMAIPMPKIFTIFTILSMAslALPGMSGFVAELIVFFGiitsqkYLFMMKILITFVTAIGMILTPI 507
Cdd:MTH00144 216 DSGSMKDLG----SLKPSYKTGLSIISLLLSLG--GLPPFLGFCSKLLVLIS------SMESSPLLLILLLLLGSLISLF 283
|
330 340
....*....|....*....|....*..
gi 355505216 508 YLLSILRQMF-YGYKFFNTPNSYFFDS 533
Cdd:MTH00144 284 FYLSVFFSSFlSSSKSKKSNSSKVLNS 310
|
|
| ND5 |
MTH00207 |
NADH dehydrogenase subunit 5; Provisional |
250-508 |
2.02e-06 |
|
NADH dehydrogenase subunit 5; Provisional
Pssm-ID: 164753 [Multi-domain] Cd Length: 572 Bit Score: 50.53 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 250 GSVFLLMGIlGIGLYGSNEPTLNFeTLTNQSYPVALEIIlytaflIAFAVKSPIIPLHTWLPDTHGEAHYSTCMLLAGIL 329
Cdd:MTH00207 150 GDVMLLLSI-GWTLNQGHWSITNM-WQTDMNNYIALSIM------IAAMTKSAQMPFSSWLPAAMAAPTPVSALVHSSTL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 330 LKMGAYGLVRINMelFSHAHSIFCPWLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFII--LGIGSIsdtglNGA 407
Cdd:MTH00207 222 VTAGVFLLIRFYP--FLSSTYWFNPALLLTASLTMLMAGLSAMTECDMKKIIALSTLSQLGVMMasLGLGMP-----KLA 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 408 ILQIISHGFIGAALFFLAGT-------SYDrlrllyLDEMGGMAIPMPKIFTIFTILSMASLALPGMSGF-----VAELI 475
Cdd:MTH00207 295 LFHLITHALFKALLFVCAGSlihshhhSQD------LRTMGNLTNQMPLTTSCLLIANLALCGSPFLSGFyskdlILESS 368
|
250 260 270
....*....|....*....|....*....|...
gi 355505216 476 VFFGIITSQKYLFMMKILITFVTAIGMILTPIY 508
Cdd:MTH00207 369 LFYPHNSLMILMIFLATALTAAYSTRFTLAVLW 401
|
|
| ND2 |
MTH00199 |
NADH dehydrogenase subunit 2; Provisional |
295-499 |
2.71e-06 |
|
NADH dehydrogenase subunit 2; Provisional
Pssm-ID: 177245 [Multi-domain] Cd Length: 460 Bit Score: 50.02 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 295 IAFAVKSPIIPLHTWLPDTHGEAHYSTCMLLAgILLKMGAYG-LVRINMELfshahsifcPWLMILGSIQIIYAASTSFG 373
Cdd:MTH00199 198 ISLLFKLSAAPFHMWAPDVYEGAPTITTALLA-TVPKIGVFSiLVQIGPVT---------NVVLICAVLSIIYGAIGALN 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 374 QRNLKKRIAYSSVSHMGFIILGIGSISDTGLNGAILQIISHGFIGAALFFLAGTSydRLRLLYLDEMGGMAIPMPKIFTI 453
Cdd:MTH00199 268 QTKIKRLLAYSGIGHMGFILFGVAIGSFESIQASLIYMIIYVIMSICSFSIILSL--KLTKGLIVEVSGLSRKNPVIALT 345
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 355505216 454 FTILSMASLALPGMSGFVAELIVFFGIITSQKYLFMMKILITFVTA 499
Cdd:MTH00199 346 LALTFLSIAGIPPLAGFLSKWLILLSGVSSGYYLICIIAVLSSVIA 391
|
|
| Fer4_8 |
pfam13183 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
11-61 |
5.08e-06 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 433017 [Multi-domain] Cd Length: 64 Bit Score: 44.22 E-value: 5.08e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 355505216 11 CIGCTQCVRACP----TDVLEMIPWDGCKAKQIASAPRTED-------CVGCKRCESACPTD 61
Cdd:pfam13183 2 CIRCGACLAACPvylvTGGRFPGDPRGGAAALLGRLEALEGlaeglwlCTLCGACTEVCPVG 63
|
|
| NapF_like |
cd10564 |
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ... |
11-66 |
5.25e-06 |
|
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319886 [Multi-domain] Cd Length: 139 Bit Score: 46.08 E-value: 5.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 11 CIGCTQCVRACPTDVL---EMIPW-------DGCKAKQ---------------IASAPR----------TEDCVGCKRCE 55
Cdd:cd10564 47 CTFCGACAEACPEGALdpaREAPWplraeigDSCLALQgvecrscqdacptqaIRFRPRlggialpeldADACTGCGACV 126
|
90
....*....|.
gi 355505216 56 SACPTDFLSVR 66
Cdd:cd10564 127 SVCPVGAITLT 137
|
|
| DMSOR_beta_like |
cd16373 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
10-60 |
5.98e-06 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319895 [Multi-domain] Cd Length: 154 Bit Score: 46.48 E-value: 5.98e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 355505216 10 TCIGCTQCVRACPTDVLEMIPWDGcKAKQIAS---APRTEDCV-GCKRCESACPT 60
Cdd:cd16373 15 LCIRCGLCVEACPTGVIQPAGLED-GLEGGRTpylDPREGPCDlCCDACVEVCPT 68
|
|
| DMSOR_beta-like |
cd04410 |
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ... |
10-61 |
6.71e-06 |
|
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319870 [Multi-domain] Cd Length: 136 Bit Score: 45.84 E-value: 6.71e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 355505216 10 TCIGCTQ--CVRACPTDVLEMIPwDGckAKQIasapRTEDCVGCKRCESACPTD 61
Cdd:cd04410 49 SCMHCEDppCVKACPTGAIYKDE-DG--IVLI----DEDKCIGCGSCVEACPYG 95
|
|
| PRK05888 |
PRK05888 |
NADH-quinone oxidoreductase subunit NuoI; |
11-61 |
7.90e-06 |
|
NADH-quinone oxidoreductase subunit NuoI;
Pssm-ID: 235637 [Multi-domain] Cd Length: 164 Bit Score: 46.41 E-value: 7.90e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 355505216 11 CIGCTQCVRACPTDVLEMIpwdgckakqiaSAPRTED-------------CVGCKRCESACPTD 61
Cdd:PRK05888 60 CIACKLCAAICPADAITIE-----------AAEREDGrrrttrydinfgrCIFCGFCEEACPTD 112
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
11-66 |
9.60e-06 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 48.10 E-value: 9.60e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 355505216 11 CIGCTQCVRACPTDVLEMipwDGCKAKQIAsaprtEDCVGCKRCESACPTDFLSVR 66
Cdd:COG4624 93 CKNCYPCVRACPVKAIKV---DDGKAEIDE-----EKCISCGQCVAVCPFGAITEK 140
|
|
| ACS_1 |
cd01916 |
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ... |
9-69 |
1.00e-05 |
|
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and methanogenic organisms and is responsible for the synthesis and breakdown of acetyl-CoA. ACS forms a heterotetramer with carbon monoxide dehydrogenase (CODH) consisting of two ACS and two CODH subunits. CODH reduces carbon dioxide to carbon monoxide and ACS then synthesizes acetyl-CoA from carbon monoxide, CoA, and a methyl group donated by another protein (CoFeSP). ACS has three structural domains, an N-terminal rossman fold domain with a helical region at its N-terminus which interacts with CODH, and two alpha + beta fold domains. A Ni-Fe-S center referred to as the A-cluster is located in the C-terminal domain. A large cavity exists between the three domains which may bind CoA.
Pssm-ID: 238897 [Multi-domain] Cd Length: 731 Bit Score: 48.56 E-value: 1.00e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 355505216 9 DTCIGCTQCVRACPTD--VLEMIPwdgcKAKQ--IASAPRTED-CVGCKRCESACPTDFLSVRVYL 69
Cdd:cd01916 365 AKCTDCGWCTRACPNSlrIKEAME----AAKEgdFSGLADLFDqCVGCGRCEQECPKEIPIINMIE 426
|
|
| Fer4_17 |
pfam13534 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
11-62 |
1.19e-05 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 433287 [Multi-domain] Cd Length: 61 Bit Score: 43.22 E-value: 1.19e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 355505216 11 CIGCTQCVRACPT---------DVLEMIPWDGCKAKQIAsaPRTEDCVGCKRCESACPTDF 62
Cdd:pfam13534 2 CIQCGCCVDECPRyllngdepkKLMRAAYLGDLEELQAN--KVANLCSECGLCEYACPMGL 60
|
|
| DMSOR_beta-like |
cd04410 |
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ... |
5-61 |
1.41e-05 |
|
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319870 [Multi-domain] Cd Length: 136 Bit Score: 45.07 E-value: 1.41e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 355505216 5 VKIY-DTCIGCTQCVRACPTDVLEMIPWDGckakqiasapRTEDCVGCK---------RCESACPTD 61
Cdd:cd04410 75 VLIDeDKCIGCGSCVEACPYGAIVFDPEPG----------KAVKCDLCGdrldeglepACVKACPTG 131
|
|
| DMSOR_beta_like |
cd16367 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
5-63 |
1.46e-05 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319889 [Multi-domain] Cd Length: 138 Bit Score: 44.99 E-value: 1.46e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 355505216 5 VKIYDTCIGCTQCVRACPTDVLEMIPWDGCKAkqiasaprtedCVGC--KRCESACPTDFL 63
Cdd:cd16367 82 VVISDACCGCGNCASACPYGAIQMVRAVKCDL-----------CAGYagPACVSACPTGAA 131
|
|
| ND5 |
MTH00108 |
NADH dehydrogenase subunit 5; Provisional |
294-470 |
1.73e-05 |
|
NADH dehydrogenase subunit 5; Provisional
Pssm-ID: 177170 [Multi-domain] Cd Length: 602 Bit Score: 47.54 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 294 LIAFAVKSPIIPLHTWLPD-----THGEA--HYSTcMLLAGILLkmgaygLVRIN--MELFSHAHSIfcpwLMILGSIQI 364
Cdd:MTH00108 217 LLAATGKSAQFGLHPWLPSamegpTPVSAllHSST-MVVAGVFL------LIRFHplMENNKTIQTL----TLCLGAITT 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 365 IYAASTSFGQRNLKKRIAYSSVSHMGFIILGIGsISDTGLngAILQIISHGFIGAALFFLAGTSYDRLRllylDE----- 439
Cdd:MTH00108 286 LFTAICALTQNDIKKIVAFSTSSQLGLMMVTIG-INQPHL--AFLHICTHAFFKAMLFMCSGSIIHNLN----DEqdirk 358
|
170 180 190
....*....|....*....|....*....|....
gi 355505216 440 MGGMAIPMPkiFTIfTILSMASLALPGM---SGF 470
Cdd:MTH00108 359 MGGLFKTLP--FTS-TALIIGSLALTGMpflTGF 389
|
|
| PRK06459 |
PRK06459 |
hydrogenase 4 subunit B; Validated |
221-398 |
1.86e-05 |
|
hydrogenase 4 subunit B; Validated
Pssm-ID: 235806 [Multi-domain] Cd Length: 585 Bit Score: 47.48 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 221 SRDILLFFIMWELELIPVYILLFI---------LYTAGGSVFLLMGILGIGLYGSNEPTLNFETLTNQsypvaLEIILYT 291
Cdd:PRK06459 91 SDNYLLFLAGWEIMTIPSYVAIALtkknkrpafVFMAFGELSTVLILAGFAWAFIISGTTNFSYLPSP-----VPLILAS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 292 aflIAFAVKSPIIPLH--TWLPDTHGEAHYSTCMLLAGILLKMGAYGLVRINMELFSHAHSIFCPWLMILGSIQIIYAAS 369
Cdd:PRK06459 166 ---FGFIIKMGMMPFLvsEWLPIAHGNAPSNFSAILSATMTLMGVYGILKMTILTQTIPIGYFGLTILAIGAFSILFGAL 242
|
170 180
....*....|....*....|....*....
gi 355505216 370 TSFGQRNLKKRIAYSSVSHMGFIILGIGS 398
Cdd:PRK06459 243 YAYVSENVKGLLAFSTIENNGAILVALGL 271
|
|
| PRK06273 |
PRK06273 |
ferredoxin; Provisional |
9-59 |
2.54e-05 |
|
ferredoxin; Provisional
Pssm-ID: 235764 [Multi-domain] Cd Length: 165 Bit Score: 44.70 E-value: 2.54e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 355505216 9 DTCIGCTQCVRACPTDVLEMIPW------DGCKAKQIasaPR--TEDCVGCKRCESACP 59
Cdd:PRK06273 49 ELCIGCGGCANVCPTKAIEMIPVepvkitEGYVKTKI---PKidYEKCVYCLYCHDFCP 104
|
|
| DMSOR_beta_like |
cd16372 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
9-66 |
2.70e-05 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319894 [Multi-domain] Cd Length: 125 Bit Score: 43.86 E-value: 2.70e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 355505216 9 DTCIGCTQCVRACPTDVLemipwdgckaKQIASAPRTEDCVGCKRCESACPTDFLSVR 66
Cdd:cd16372 77 KLCVGCLMCVGFCPEGAM----------FKHEDYPEPFKCIACGICVKACPTGALELV 124
|
|
| HycB_like |
cd10554 |
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ... |
3-65 |
2.72e-05 |
|
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation.
Pssm-ID: 319876 [Multi-domain] Cd Length: 149 Bit Score: 44.56 E-value: 2.72e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 355505216 3 HSVKIY-DTCIGCTQCVRACPTDVLEMIPwDGCKAKQIASAPRTE----D-CVGCK---RCESACPTDFLSV 65
Cdd:cd10554 78 GVVQVDeERCIGCKLCVLACPFGAIEMAP-TTVPGVDWERGPRAVavkcDlCAGREggpACVEACPTKALTL 148
|
|
| HycB |
COG1142 |
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion]; |
10-59 |
3.17e-05 |
|
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
Pssm-ID: 440757 [Multi-domain] Cd Length: 138 Bit Score: 43.88 E-value: 3.17e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 355505216 10 TCIGCTQ--CVRACPTDVLEMIpwDGckAKQIasapRTEDCVGCKRCESACP 59
Cdd:COG1142 51 QCRHCEDapCAEVCPVGAITRD--DG--AVVV----DEEKCIGCGLCVLACP 94
|
|
| PhsB_like |
cd10553 |
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ... |
7-59 |
4.10e-05 |
|
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This family includes beta FeS subunits of anaerobic DMSO reductase (DMSOR) superfamily that have yet to be characterized. DMSOR consists of a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and the tungsten-containing formate dehydrogenase (FDH-T). Examples of heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319875 [Multi-domain] Cd Length: 146 Bit Score: 43.89 E-value: 4.10e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 355505216 7 IYDTCIGCTQ--CVRACPTDVLEMIPWDGckakqIAsAPRTEDCVGCKRCESACP 59
Cdd:cd10553 54 VYMSCFHCENpwCVKACPTGAMQKREKDG-----IV-YVDQELCIGCKACIEACP 102
|
|
| PRK09898 |
PRK09898 |
ferredoxin-like protein; |
9-76 |
4.39e-05 |
|
ferredoxin-like protein;
Pssm-ID: 182135 [Multi-domain] Cd Length: 208 Bit Score: 44.83 E-value: 4.39e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 9 DTCIGCT--QCVRACPTDVLEMIPWDGCKAKQiasaprTEDCVGCKRCESACPTDFLSVrvylGPETTRS 76
Cdd:PRK09898 121 DTCRQCKepQCMNVCPIGAITWQQKEGCITVD------HKRCIGCSACTTACPWMMATV----NTESKKS 180
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
8-32 |
4.64e-05 |
|
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440758 [Multi-domain] Cd Length: 66 Bit Score: 41.65 E-value: 4.64e-05
10 20
....*....|....*....|....*
gi 355505216 8 YDTCIGCTQCVRACPTDVLEMIPWD 32
Cdd:COG1143 34 PDKCIGCGLCVEVCPTGAISMTPFE 58
|
|
| PRK06277 |
PRK06277 |
energy conserving hydrogenase EhbF; |
244-475 |
4.78e-05 |
|
energy conserving hydrogenase EhbF;
Pssm-ID: 235767 [Multi-domain] Cd Length: 478 Bit Score: 46.18 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 244 ILYTAGGSVFLLmgilGIGLYGSNEPTLNFETLTNQSYPVALEIILYTAFL---IAFAVKSPIIPLHTWLPDTHGEAH-Y 319
Cdd:PRK06277 157 ILGNVAGSILLL----GIGFLLASTGTLNITDIHNALLVNPTSPVIYGGLLlliFGLLYGSGLPPFHTIKSDIYAKAKpF 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 320 STCMLLAGILLKMGAYGLVRINM----ELFSHAHSIfcpwLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIILG 395
Cdd:PRK06277 233 GSALLQTFSKFVLVALMLVIFKLfgglSYFPSAQGV----LIALSVLAMVFGVVMALLQTDYKRLLAYHAISQGGYVAAG 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 396 IGSISDTGLNGAILQIISHGFIGAALFFLAGTSYDRLRLLYLDEMGGMAIPMPKIFTIFTILSMASLALPGMSGFVAELI 475
Cdd:PRK06277 309 LALGTPLGIVAGIFHAINHVIYKSALFLGAGIVSYRTKTSNLRKLGGLLPVMPVVAFMVLCAKLAISGVPPFNGFQSKLM 388
|
|
| NapF_like |
cd10564 |
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ... |
9-64 |
6.49e-05 |
|
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319886 [Multi-domain] Cd Length: 139 Bit Score: 43.00 E-value: 6.49e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 355505216 9 DTCIGCTQCVRACPTDVLEMIpwDGCKAkQIasAPRTEDCVGCKRCESACPTDFLS 64
Cdd:cd10564 13 DLCTRCGDCVEACPEGIIVRG--DGGFP-EL--DFSRGECTFCGACAEACPEGALD 63
|
|
| HycB |
COG1142 |
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion]; |
7-65 |
6.97e-05 |
|
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
Pssm-ID: 440757 [Multi-domain] Cd Length: 138 Bit Score: 43.11 E-value: 6.97e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 355505216 7 IYDTCIGCTQCVRACPTDVLEMIPWdgcKAKQIASAprtedCVGCK------RCESACPTDFLSV 65
Cdd:COG1142 79 DEEKCIGCGLCVLACPFGAITMVGE---KSRAVAVK-----CDLCGgreggpACVEACPTGALRL 135
|
|
| ndhF |
CHL00025 |
NADH dehydrogenase subunit 5 |
254-426 |
7.44e-05 |
|
NADH dehydrogenase subunit 5
Pssm-ID: 214338 [Multi-domain] Cd Length: 741 Bit Score: 45.65 E-value: 7.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 254 LLMGILGigLY---GSNEPTLNFETLTN--QSYPVALEIILYTAFLI-AFAV-KSPIIPLHTWLPD-----THGEA--HY 319
Cdd:CHL00025 189 LLLGILG--FYwitGSFEFRDLFEIFNNliYNNEVNLLFATLCAFLLfLGPVaKSAQFPLHVWLPDamegpTPISAliHA 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 320 STcMLLAGILLkmgaygLVRInMELFshahsIFCPWLMIL----GSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIIL- 394
Cdd:CHL00025 267 AT-MVAAGIFL------VARL-LPLF-----IVIPYIMNLisliGIITALLGATLALAQKDIKRGLAYSTMSQLGYMMLa 333
|
170 180 190
....*....|....*....|....*....|...
gi 355505216 395 -GIGSISdtglnGAILQIISHGFIGAALFFLAG 426
Cdd:CHL00025 334 lGIGSYR-----AALFHLITHAYSKALLFLGSG 361
|
|
| ndhI |
CHL00014 |
NADH dehydrogenase subunit I |
8-64 |
7.78e-05 |
|
NADH dehydrogenase subunit I
Pssm-ID: 214334 [Multi-domain] Cd Length: 167 Bit Score: 43.59 E-value: 7.78e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 355505216 8 YDTCIGCTQCVRACPTDvLEMIPWD---GCKAKQIASapRTED---CVGCKRCESACPTDFLS 64
Cdd:CHL00014 58 FDKCIACEVCVRVCPID-LPVVDWKletDIRKKRLLN--YSIDfgvCIFCGNCVEYCPTNCLS 117
|
|
| HybA |
COG0437 |
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ... |
8-85 |
1.45e-04 |
|
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion];
Pssm-ID: 440206 [Multi-domain] Cd Length: 184 Bit Score: 43.01 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 8 YDTCIGCTQCVRACPTDVLEMIPWDGCKAKqiasaprtedCVGCK---------RCESACPTDflsVRVYLGPETTRSMA 78
Cdd:COG0437 89 YDKCIGCRYCVAACPYGAPRFNPETGVVEK----------CTFCAdrldegllpACVEACPTG---ALVFGDLDDPESEV 155
|
....*..
gi 355505216 79 RAFLAQV 85
Cdd:COG0437 156 SKRLAEL 162
|
|
| PorD |
COG1144 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ... |
7-30 |
1.47e-04 |
|
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440759 [Multi-domain] Cd Length: 84 Bit Score: 40.81 E-value: 1.47e-04
10 20
....*....|....*....|....
gi 355505216 7 IYDTCIGCTQCVRACPTDVLEMIP 30
Cdd:COG1144 58 DYDYCKGCGICAEVCPVKAIEMVP 81
|
|
| PRK08318 |
PRK08318 |
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
9-61 |
1.51e-04 |
|
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 44.55 E-value: 1.51e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 355505216 9 DTCIGCTQCVRACPTDVLEMIPWDGCKAKQIASapRTEDCVGCKRCESACPTD 61
Cdd:PRK08318 342 DKCIGCGRCYIACEDTSHQAIEWDEDGTRTPEV--IEEECVGCNLCAHVCPVE 392
|
|
| Fer |
COG1141 |
Ferredoxin [Energy production and conversion]; |
9-65 |
1.61e-04 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440756 [Multi-domain] Cd Length: 63 Bit Score: 39.86 E-value: 1.61e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 355505216 9 DTCIGCTQCVRACPtDVLEMIPWDGCKAKQIASAPRTEDCVgcKRCESACPTDFLSV 65
Cdd:COG1141 8 DTCIGCGLCVALAP-EVFELDDDGKAVVLDEEVPEELEEDV--REAADACPVGAITV 61
|
|
| PRK08222 |
PRK08222 |
hydrogenase 4 subunit H; Validated |
11-60 |
1.64e-04 |
|
hydrogenase 4 subunit H; Validated
Pssm-ID: 181301 [Multi-domain] Cd Length: 181 Bit Score: 42.82 E-value: 1.64e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 355505216 11 CIGCTQCVRACPTDVLEMipwdgckAKQIASAPRTED-----CVGCKRCESACPT 60
Cdd:PRK08222 40 CIACGACTCACPANALTI-------QTDDQQNSRTWQlylgrCIYCGRCEEVCPT 87
|
|
| rnfB |
TIGR01944 |
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ... |
2-30 |
2.27e-04 |
|
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the B subunit. [Energy metabolism, Electron transport]
Pssm-ID: 273887 [Multi-domain] Cd Length: 165 Bit Score: 42.09 E-value: 2.27e-04
10 20
....*....|....*....|....*....
gi 355505216 2 SHSVkIYDTCIGCTQCVRACPTDVLEMIP 30
Cdd:TIGR01944 137 MHTV-IADECTGCDLCVEPCPTDCIEMIP 164
|
|
| Fer4 |
pfam00037 |
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ... |
5-27 |
2.36e-04 |
|
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 459642 [Multi-domain] Cd Length: 24 Bit Score: 38.38 E-value: 2.36e-04
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
11-109 |
2.50e-04 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 43.97 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 11 CIGCTQCVRACPTDVLEMIPWDGCKAKQIASAPRTEDCVGCKR---CESACPTDFLSVRVYLGPETTRSMARAFLAQvyl 87
Cdd:PRK12769 87 CIGCKSCVVACPFGTMQIVLTPVAAGKVKATAHKCDLCAGRENgpaCVENCPADALQLVTEQALSGMAKSRRLRTAR--- 163
|
90 100
....*....|....*....|..
gi 355505216 88 ifmTNYFPWLTIVVVFPIAAGS 109
Cdd:PRK12769 164 ---QEHQPWHASTAAQEMPAMS 182
|
|
| PRK07118 |
PRK07118 |
Fe-S cluster domain-containing protein; |
11-60 |
2.74e-04 |
|
Fe-S cluster domain-containing protein;
Pssm-ID: 235941 [Multi-domain] Cd Length: 280 Bit Score: 43.00 E-value: 2.74e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 355505216 11 CIGCTQCVRACPTDVLEMipwDGCKAKQIasaprTEDCVGCKRCESACPT 60
Cdd:PRK07118 215 CIGCGKCVKACPAGAITM---ENNLAVID-----QEKCTSCGKCVEKCPT 256
|
|
| DMSOR_beta_like |
cd10550 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
8-65 |
2.87e-04 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319872 [Multi-domain] Cd Length: 130 Bit Score: 41.02 E-value: 2.87e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 355505216 8 YDTCIGCTQCVRACPTDVLEMIPWDG----CkakqiasaprteD-CVGCKRCESACPTDFLSV 65
Cdd:cd10550 79 EDKCIGCGMCVEACPFGAIRVDPETGkaikC------------DlCGGDPACVKVCPTGALEF 129
|
|
| ND5 |
MTH00137 |
NADH dehydrogenase subunit 5; Provisional |
306-470 |
2.91e-04 |
|
NADH dehydrogenase subunit 5; Provisional
Pssm-ID: 214428 [Multi-domain] Cd Length: 611 Bit Score: 43.67 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 306 LHTWLPD-----THGEA--HYSTcMLLAGILLkmgaygLVRIN--MELFSHAHSIfCPWLmilGSIQIIYAASTSFGQRN 376
Cdd:MTH00137 234 LHPWLPSamegpTPVSAllHSST-MVVAGIFL------LIRLSplMENNQTALTT-CLCL---GALTTLFTATCALTQND 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 377 LKKRIAYSSVSHMGFIILGIGsisdtgLNG---AILQIISHGFIGAALFFLAGTSYDRLRllylDE-----MGGMAIPMP 448
Cdd:MTH00137 303 IKKIVAFSTSSQLGLMMVTIG------LNQpqlAFLHICTHAFFKAMLFLCSGSIIHSLN----DEqdirkMGGLHHLTP 372
|
170 180
....*....|....*....|....*
gi 355505216 449 KIFTIFTIlsmASLALPGM---SGF 470
Cdd:MTH00137 373 FTSSCLTI---GSLALTGTpflAGF 394
|
|
| napG |
PRK09476 |
quinol dehydrogenase periplasmic component; Provisional |
10-63 |
2.97e-04 |
|
quinol dehydrogenase periplasmic component; Provisional
Pssm-ID: 236534 [Multi-domain] Cd Length: 254 Bit Score: 42.69 E-value: 2.97e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 355505216 10 TCIGCTQCVRACPTDVLEMIPW-DGCKAKQIASAPRTEDCVGCKR--CESACPTDFL 63
Cdd:PRK09476 60 ACIRCGLCVQACPYDTLKLATLaSGLSAGTPYFVARDIPCEMCEDipCVKACPSGAL 116
|
|
| RNAP_D |
cd07030 |
D subunit of Archaeal RNA polymerase; The D subunit of archaeal RNA polymerase (RNAP) is ... |
5-66 |
3.22e-04 |
|
D subunit of Archaeal RNA polymerase; The D subunit of archaeal RNA polymerase (RNAP) is involved in the assembly of RNAP subunits. RNAP is a large multi-subunit complex responsible for the synthesis of RNA. It is the principal enzyme of the transcription process, and is a final target in many regulatory pathways that control gene expression in all living cells. A single distinct RNAP complex is found in archaea, which may be responsible for the synthesis of all RNAs. The archaeal RNAP harbors homologues of all eukaryotic RNAP II subunits with two exceptions (RPB8 and RPB9). The 12 archaeal subunits are designated by letters and can be divided into three functional groups that are engaged in: (I) catalysis (A'/A", B'/B" or B); (II) assembly (L, N, D and P); and (III) auxiliary functions (F, E, H and K). The D subunit is equivalent to the RPB3 subunit of eukaryotic RNAP II. It contains two subdomains: one subdomain is similar the eukaryotic Rpb11/AC19/archaeal L subunit which is involved in dimerization, and the other is an inserted beta sheet subdomain. The assembly of the two largest archaeal RNAP subunits that provide most of the enzyme's catalytic functions depends on the presence of the archaeal D/L heterodimer.
Pssm-ID: 132908 [Multi-domain] Cd Length: 259 Bit Score: 42.64 E-value: 3.22e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 355505216 5 VKIYDTCIGCTQCVRACPTDVLEmipwdgcKAKQIASAPRTEDCVGCKRCESACPTDFLSVR 66
Cdd:cd07030 165 IEIDEDCDGCGKCVEECPRGVLE-------LEEGKVVVEDLEDCSLCKLCERACDAGAIRVG 219
|
|
| PRK08168 |
PRK08168 |
NADH-quinone oxidoreductase subunit L; |
292-472 |
3.57e-04 |
|
NADH-quinone oxidoreductase subunit L;
Pssm-ID: 236171 [Multi-domain] Cd Length: 516 Bit Score: 43.15 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 292 AFLIAFAV--KSPIIPLHTWLPDTHgEAHYSTCMLLAGILLKMGAYGLVRInMELFSHAHSifCPW-LMILGSIQIIYAA 368
Cdd:PRK08168 203 ALLLVLAVilKTAQLPVHGWLIQVM-EAPTPVSALLHAGVVNLGGFVLIRF-APLLEQAPP--ARWlLVLVGLATAVLAG 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 369 STSFGQRNLKKRIAYSSVSHMGFIILGIGsisdTGLNG-AILQIISHGFIGAALFFLAGTSYDRLRLLyldEMGGMAIPM 447
Cdd:PRK08168 279 LVMLTRISIKVRLAWSTVAQMGFMLLECG----LGLYElALLHLVAHSLYKAHAFLSASEAVRDTRLR---RLQGPQSAA 351
|
170 180
....*....|....*....|....*.
gi 355505216 448 PKIFTIFT-ILSMASLALPGMSGFVA 472
Cdd:PRK08168 352 GVVSLLLApLLSAALVLLLQSLLPLG 377
|
|
| PRK13795 |
PRK13795 |
hypothetical protein; Provisional |
11-59 |
3.59e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237510 [Multi-domain] Cd Length: 636 Bit Score: 43.44 E-value: 3.59e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 355505216 11 CIGCTQCVRACPTDVLEMipwDGCKAKqIASAPrtEDCVGCKRCESACP 59
Cdd:PRK13795 583 CVGCGVCVGACPTGAIRI---EEGKRK-ISVDE--EKCIHCGKCTEVCP 625
|
|
| ND2 |
MTH00041 |
NADH dehydrogenase subunit 2; Validated |
285-561 |
4.21e-04 |
|
NADH dehydrogenase subunit 2; Validated
Pssm-ID: 177116 [Multi-domain] Cd Length: 349 Bit Score: 42.61 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 285 LEIILYTAFLIAFAVKSPIIPLHTWLPDTHGEAHYSTCMLLAGILLKMGAYGLVRINMELFSHAhsifcpwLMILGSIQI 364
Cdd:MTH00041 90 LNTLSSIIITLALALKLGLAPCHFWFPDVLQGLPFLQGLIIATWQKIAPLILLISISNLLNSNI-------LILCGILSV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 365 IYAASTSFGQRNLKKRIAYSSVSHMGFIIlgigSISDTGLNGAILQIISHGFIGAALFFLAgtsyDRLRLLYLDEMGGMA 444
Cdd:MTH00041 163 LVGGWGGLNQTQTRKILAFSSIAHLGWII----ITSAYSPNASIIMFLIYIIINTSIFLIG----NNFSLSTLSHLNKLS 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 445 IPMPkIFTIFTILSMASLA-LPGMSGFVAELIvffgiitsqkylfmmkILITFVTAIGMILTPIYLL-SILRQMFYGYKF 522
Cdd:MTH00041 235 QLNP-ISAFLFILSILSLGgLPPLTGFLNKFI----------------SLYCLIQNNSILISIILIIgSLLSLFFYLRIS 297
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 355505216 523 FNT------PNSYFFDS-------GPRELFISISILIPVIGIGIYPDFIFSF 561
Cdd:MTH00041 298 FNTsltlfpQHSISLFSwrnsgniTVYGVILSILSSISILGLLLIPLFLSFL 349
|
|
| FDH-O_like |
cd10560 |
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ... |
9-77 |
4.37e-04 |
|
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes beta subunit of formate dehydrogenase family O (FDH-O), which is highly homologous to formate dehydrogenase N (FDH-N), a member of the DMSO reductase family. In E. coli three formate dehydrogenases are synthesized that are capable of oxidizing formate; Fdh-H, couples formate disproportionation to hydrogen and CO2, and is part of the cytoplasmically oriented formate hydrogenlyase complex, while FDH-N and FDH-O indicate their respective induction after growth with nitrate and oxygen. Little is known about FDH-O, although it shows formate oxidase activity during aerobic growth and is also synthesized during nitrate respiration, similar to FDH-N.
Pssm-ID: 319882 [Multi-domain] Cd Length: 225 Bit Score: 41.99 E-value: 4.37e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 355505216 9 DTCIGCTQ--CVRACPTDVLEMIPWDGCkakqiasAPRTEDCVGCKRCESACPtdFLSVRVylGPETTRSM 77
Cdd:cd10560 76 DVCKHCTDagCLEACPTGAIFRTEFGTV-------YIQPDICNGCGYCVAACP--FGVIDR--NEETGRAH 135
|
|
| DMSOR_beta_like |
cd16370 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
9-59 |
4.42e-04 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319892 [Multi-domain] Cd Length: 131 Bit Score: 40.33 E-value: 4.42e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 355505216 9 DTCIGCTQ--CVRACPTDVLEMIPWDGCKAKQiasaprtEDCVGCKRCESACP 59
Cdd:cd16370 51 VVCRACEDppCAEACPTGALEPRKGGGVVLDK-------EKCIGCGNCVKACI 96
|
|
| ND2 |
MTH00197 |
NADH dehydrogenase subunit 2; Provisional |
243-512 |
4.45e-04 |
|
NADH dehydrogenase subunit 2; Provisional
Pssm-ID: 177244 [Multi-domain] Cd Length: 323 Bit Score: 42.74 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 243 FILYTAGGSVFLLMGILGIglygsneptlnfetltnqSYPVALEIILYTAFLIAFAVKSPIIPLHTWLPDTHGEAHYSTC 322
Cdd:MTH00197 53 YFLFQEFGSALLLMGGSLS------------------FSNLYLSLLSVVLVILGLLLKLGAFPFHFWVPSVMESLSWFNC 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 323 MLLAgILLKMGAYGLVRINMELFShahsifcpWLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMGFIIlgigSISDT 402
Cdd:MTH00197 115 FLLA-TWQKLAPLLILAFNSSSFM--------GLLICSVLSSLIGGIGGMNQSNIRQLLAYSSIGHTGWML----MSLVY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 403 GLNGAILQIISHGFIGAALFFLagTSYDRLRLLYLDEMGGMAIPMPKIFTIFTILSMAslALPGMSGFVAELIVFFGIIT 482
Cdd:MTH00197 182 SPSIFMLYYLIYFVIMFMLFLF--LSKNNLSSLNQQYSNPESMSSNLVFLGLSFLSLG--GLPPLSGFFLKWLILTSLLS 257
|
250 260 270
....*....|....*....|....*....|
gi 355505216 483 SQKYlfmmkiLITFVTAIGMILTPIYLLSI 512
Cdd:MTH00197 258 SNIS------LITFMLILSTCFSLYYYLSL 281
|
|
| PRK07569 |
PRK07569 |
bidirectional hydrogenase complex protein HoxU; Validated |
11-60 |
4.54e-04 |
|
bidirectional hydrogenase complex protein HoxU; Validated
Pssm-ID: 181037 [Multi-domain] Cd Length: 234 Bit Score: 41.95 E-value: 4.54e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 355505216 11 CIGCTQCVRACptDVLEMI-PWD----GCKAKQIASAPR----TEDCVGCKRCESACPT 60
Cdd:PRK07569 148 CVLCTRCVRVC--DEIEGAhTWDvagrGAKSRVITDLNQpwgtSETCTSCGKCVQACPT 204
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
9-68 |
4.80e-04 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 42.92 E-value: 4.80e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 9 DTCIGCTQCVRACPTDVLEMipwdgcKAKQIASaPRTEDCVGCKRCESACPTDFLSVRVY 68
Cdd:COG1148 496 EKCTGCGRCVEVCPYGAISI------DEKGVAE-VNPALCKGCGTCAAACPSGAISLKGF 548
|
|
| PRK05113 |
PRK05113 |
electron transport complex protein RnfB; Provisional |
3-30 |
4.86e-04 |
|
electron transport complex protein RnfB; Provisional
Pssm-ID: 235347 [Multi-domain] Cd Length: 191 Bit Score: 41.47 E-value: 4.86e-04
10 20
....*....|....*....|....*...
gi 355505216 3 HSVkIYDTCIGCTQCVRACPTDVLEMIP 30
Cdd:PRK05113 139 HTV-ISDLCTGCDLCVAPCPTDCIEMIP 165
|
|
| NapH |
COG0348 |
Polyferredoxin NapH [Energy production and conversion]; |
8-64 |
5.54e-04 |
|
Polyferredoxin NapH [Energy production and conversion];
Pssm-ID: 440117 [Multi-domain] Cd Length: 263 Bit Score: 41.97 E-value: 5.54e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 355505216 8 YDTCIGCTQCVRACPTDVlemIPWDGckakqiasAPRTEDCVGCKRCESACPTDFLS 64
Cdd:COG0348 209 RGDCIDCGLCVKVCPMGI---DIRKG--------EINQSECINCGRCIDACPKDAIR 254
|
|
| DMSOR_beta_like |
cd16370 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
9-64 |
6.13e-04 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319892 [Multi-domain] Cd Length: 131 Bit Score: 39.95 E-value: 6.13e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 355505216 9 DTCIGCTQCVRACPTDVlemIPWDGCKAKQIAsaprtedCVGCKRCESACPTDFLS 64
Cdd:cd16370 83 EKCIGCGNCVKACIVGA---IFWDEETNKPII-------CIHCGYCARYCPHDVLA 128
|
|
| Fer4_13 |
pfam13370 |
4Fe-4S single cluster domain of Ferredoxin I; Fer4_13 is a ferredoxin I from sulfate-reducing ... |
9-61 |
6.21e-04 |
|
4Fe-4S single cluster domain of Ferredoxin I; Fer4_13 is a ferredoxin I from sulfate-reducing bacteria. Chemical sequence analysis suggests that this characteriztic [4Fe-4S] cluster sulfur environment is widely distributed among ferredoxins.
Pssm-ID: 433153 [Multi-domain] Cd Length: 58 Bit Score: 38.06 E-value: 6.21e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 355505216 9 DTCIGCTQCVRACPtDVLEMIPWDGckAKQIASAPRTEDCVgcKRCESA---CPTD 61
Cdd:pfam13370 4 DTCIDCGTCRELAP-EVFKYDDDGG--ASFVHDQPVNEEEE--DLAEEAldsCPVE 54
|
|
| ND5 |
MTH00209 |
NADH dehydrogenase subunit 5; Provisional |
294-470 |
7.47e-04 |
|
NADH dehydrogenase subunit 5; Provisional
Pssm-ID: 177252 [Multi-domain] Cd Length: 564 Bit Score: 42.33 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 294 LIAFAVKSPIIPLHTWLPDTHGEAHYSTCMLLAGILLKMGAYGLVRINMELFSHahSIFCPWLMILGSIQIIYAASTSFG 373
Cdd:MTH00209 182 VLAAMTKSAQIPFSAWLPAAMAAPTPVSALVHSSTLVTAGVYLLIRFFPSLFSS--PFFSMSLLLLGSLTTLMASMSANV 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 374 QRNLKKRIAYSSVSHMG--FIILGIGSIsdtglNGAILQIISHGFIGAALFFLAGTS-YDRLRLLYLDEMGGMAIPMPKI 450
Cdd:MTH00209 260 ESDLKKIIALSTLSQLGlmMCSLGLNQP-----ELAFFHLITHALFKALLFICAGNIiHSHGHSQDIRMVGNLWYQMPIT 334
|
170 180
....*....|....*....|
gi 355505216 451 FTIFTILSMASLALPGMSGF 470
Cdd:MTH00209 335 SICLNIANLSLCGIPFLAGF 354
|
|
| FDH-O_like |
cd10560 |
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ... |
9-84 |
7.76e-04 |
|
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes beta subunit of formate dehydrogenase family O (FDH-O), which is highly homologous to formate dehydrogenase N (FDH-N), a member of the DMSO reductase family. In E. coli three formate dehydrogenases are synthesized that are capable of oxidizing formate; Fdh-H, couples formate disproportionation to hydrogen and CO2, and is part of the cytoplasmically oriented formate hydrogenlyase complex, while FDH-N and FDH-O indicate their respective induction after growth with nitrate and oxygen. Little is known about FDH-O, although it shows formate oxidase activity during aerobic growth and is also synthesized during nitrate respiration, similar to FDH-N.
Pssm-ID: 319882 [Multi-domain] Cd Length: 225 Bit Score: 41.22 E-value: 7.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 9 DTCIGCTQCVRACPTDVLEMIPWDGckakqiasapRTEDCVGC----KR-----CESACPTDflSVRvyLGP-ETTRSMA 78
Cdd:cd10560 108 DICNGCGYCVAACPFGVIDRNEETG----------RAHKCTLCydrlKDglepaCAKACPTG--SIQ--FGPlEELRERA 173
|
....*.
gi 355505216 79 RAFLAQ 84
Cdd:cd10560 174 RARVEQ 179
|
|
| FDH_b_like |
cd10562 |
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ... |
11-61 |
9.06e-04 |
|
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes the beta-subunit of formate dehydrogenases that are as yet uncharacterized. Members of the DMSO reductase family include formate dehydrogenase N and O (FDH-N, FDH-O) and tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N, a major component of nitrate respiration of Escherichia coli, is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. It forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. W-FDH contains a tungsten instead of molybdenum at the catalytic center. This enzyme seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It is a heterodimer of a large and a small subunit; the large subunit harbors the W site and one [4Fe-4S] center and the small subunit, containing three [4Fe-4S] clusters, functions to transfer electrons.
Pssm-ID: 319884 [Multi-domain] Cd Length: 161 Bit Score: 40.36 E-value: 9.06e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 355505216 11 CIGCTQ--CVRACPTDVLEmipwdgcKAKQIASAPRTEDCVGCKRCESACPTD 61
Cdd:cd10562 70 CMHCTDaaCVKVCPTGALY-------KTENGAVVVDEDKCIGCGYCVAACPFD 115
|
|
| PRK02504 |
PRK02504 |
NAD(P)H-quinone oxidoreductase subunit N; |
248-500 |
9.76e-04 |
|
NAD(P)H-quinone oxidoreductase subunit N;
Pssm-ID: 235044 [Multi-domain] Cd Length: 513 Bit Score: 41.96 E-value: 9.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 248 AGGSVFLLMGILGIGLYG--SNEPTLNFETLTNQSYPVALEIIlytaFLIA-FAVKSPIIPLHTWLPD------THGEAH 318
Cdd:PRK02504 172 ASSAIFLYGSSLLYGLSGgsTQLSAIALALITSPSLGLALALV----FVIAgIAFKISAVPFHQWTPDvyegspTPVVAF 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 319 YSTCMLLAG----ILLKMGAYGLVRINMELFSHAHSIFCpwlMILGSIQIIyaASTSfgqrnLKKRIAYSSVSHMGFIIL 394
Cdd:PRK02504 248 LSVGSKAAGfalaIRLLVTAFPSFDEQWKLLFTALAILS---MVLGNVVAL--AQTS-----MKRMLAYSSIGQAGFVMI 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 395 GIGSISDTGLNGAILQIISH------GFIGAALFFLAgTSYDRlrllyLDEMGGMAIPMPKIfTIFTILSMASLA-LPGM 467
Cdd:PRK02504 318 GLVAGTEAGYASMVFYLLAYlfmnlgAFACVILFSLR-TGTDQ-----ISDYAGLYQKDPLL-TLGLSLCLLSLGgIPPL 390
|
250 260 270
....*....|....*....|....*....|...
gi 355505216 468 SGFVAELIVFFGIITSQKYLFMMKILITFVTAI 500
Cdd:PRK02504 391 AGFFGKIYLFWAGWQAGLYLLVLVGLVTSVISI 423
|
|
| PRK09898 |
PRK09898 |
ferredoxin-like protein; |
11-65 |
9.80e-04 |
|
ferredoxin-like protein;
Pssm-ID: 182135 [Multi-domain] Cd Length: 208 Bit Score: 40.59 E-value: 9.80e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 355505216 11 CIGCTQCVRACPTDVLEMIPWDGCKAKqiasaprtedCVGCKRCESACPTDFLSV 65
Cdd:PRK09898 156 CIGCSACTTACPWMMATVNTESKKSSK----------CVLCGECANACPTGALKI 200
|
|
| ND5 |
MTH00165 |
NADH dehydrogenase subunit 5; Provisional |
250-546 |
1.10e-03 |
|
NADH dehydrogenase subunit 5; Provisional
Pssm-ID: 214444 [Multi-domain] Cd Length: 573 Bit Score: 41.67 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 250 GSVFLLMGILGIGLYGSneptLNFETLTNQSYPVALEIILYTAFLIAFAVKSPIIPLHTWLPdthgEA-----------H 318
Cdd:MTH00165 147 GDVAILLSIAWMMNFGS----WNFIFYLDFMKNSFEMLLIGLLIMLAAMTKSAQIPFSSWLP----AAmaaptpvsalvH 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 319 YSTcmllagiLLKMGAYGLVRINMELFShahSIFCPWLMILGSIQIIYAASTSFGQRNLKKRIAYSSVSHMG--FIILGI 396
Cdd:MTH00165 219 SST-------LVTAGVYLLIRFNNLLFS---SFFSKFLLLISLLTMFMAGLGANFEFDLKKIIALSTLSQLGlmMSILSL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 397 GSIsdtglNGAILQIISHGFIGAALFFLAGT------SYDRLRLlyldeMGGMAIPMPKIFTIFTILSMASLALPGMSGF 470
Cdd:MTH00165 289 GFP-----KLAFFHLLTHALFKALLFLCAGSiihnmsNSQDIRF-----MGGLSNFMPLTSSCFNISNLSLCGFPFLSGF 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 471 VA-ELIVffgiitsqKYLFMMKI--LITFVTAIGMILTPIYllsILRQMFYGY-KFFNTPNSYFFDSGPRELFISISILI 546
Cdd:MTH00165 359 YSkDLIL--------EMVSMSNLnfFIFFLFFFSTGLTVSY---SFRLIYYSMsGDFNLKSLNNLSDESKFMLKSMILLL 427
|
|
| PreA |
COG1146 |
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
5-30 |
1.51e-03 |
|
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];
Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 37.38 E-value: 1.51e-03
10 20
....*....|....*....|....*.
gi 355505216 5 VKIYDTCIGCTQCVRACPTDVLEMIP 30
Cdd:COG1146 36 VINPEECIGCGACELVCPVGAITVED 61
|
|
| Fer4 |
pfam00037 |
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ... |
45-64 |
1.63e-03 |
|
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 459642 [Multi-domain] Cd Length: 24 Bit Score: 36.07 E-value: 1.63e-03
|
| FDH_beta_like |
cd16366 |
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ... |
9-61 |
1.72e-03 |
|
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family contains beta FeS subunits of several dehydrogenases in the DMSO reductase superfamily, including formate dehydrogenase N (FDH-N), tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N is a major component of nitrate respiration of Escherichia coli; it catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate to a cytochrome. W-FDH contains a tungsten instead of molybdenum at the catalytic center and seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate.
Pssm-ID: 319888 [Multi-domain] Cd Length: 156 Bit Score: 39.31 E-value: 1.72e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 355505216 9 DTCIGCTQ--CVRACPTDVLEMIPwDGCKAKQiasaprTEDCVGCKRCESACPTD 61
Cdd:cd16366 68 DQCMHCTDagCLAACPTGAIIRTE-TGTVVVD------PETCIGCGYCVNACPFD 115
|
|
| Fer4_6 |
pfam12837 |
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ... |
8-26 |
1.82e-03 |
|
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 432822 [Multi-domain] Cd Length: 24 Bit Score: 36.05 E-value: 1.82e-03
|
| NapF |
COG1145 |
Ferredoxin [Energy production and conversion]; |
9-30 |
1.86e-03 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440760 [Multi-domain] Cd Length: 238 Bit Score: 40.48 E-value: 1.86e-03
|
| DMSOR_beta_like |
cd16371 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
9-65 |
1.98e-03 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319893 [Multi-domain] Cd Length: 140 Bit Score: 38.70 E-value: 1.98e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 355505216 9 DTCIGCTQCVRACPTDvlemipwdgckAKQI-ASAPRTEDCVGCKR---------CESACPTDFLSV 65
Cdd:cd16371 84 DKCIGCGYCVWACPYG-----------APQYnPETGKMDKCDMCVDrldegekpaCVAACPTRALDF 139
|
|
| Fer4_7 |
pfam12838 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
48-77 |
2.07e-03 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 463724 [Multi-domain] Cd Length: 51 Bit Score: 36.35 E-value: 2.07e-03
10 20 30
....*....|....*....|....*....|
gi 355505216 48 CVGCKRCESACPTDFLSVRVYLGPETTRSM 77
Cdd:pfam12838 1 CIGCGACVAACPVGAITLDEVGEKKGTKTV 30
|
|
| COG1149 |
COG1149 |
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
9-30 |
2.30e-03 |
|
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];
Pssm-ID: 440763 [Multi-domain] Cd Length: 68 Bit Score: 36.63 E-value: 2.30e-03
|
| Fer4_7 |
pfam12838 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
9-25 |
2.37e-03 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 463724 [Multi-domain] Cd Length: 51 Bit Score: 36.35 E-value: 2.37e-03
|
| pyruv_ox_red |
TIGR02176 |
pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single ... |
9-59 |
3.78e-03 |
|
pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single chain form of pyruvate:ferredoxin (or flavodoxin) oxidoreductase. This enzyme may transfer electrons to nitrogenase in nitrogen-fixing species. Portions of this protein are homologous to gamma subunit of the four subunit pyruvate:ferredoxin (flavodoxin) oxidoreductase.
Pssm-ID: 131231 [Multi-domain] Cd Length: 1165 Bit Score: 40.14 E-value: 3.78e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 355505216 9 DTCIGCTQCVRACPTDVLEMIPWD------------GCKAK-----------QIAsaprTEDCVGCKRCESACP 59
Cdd:TIGR02176 683 DNCIQCNQCAFVCPHAAIRPKLADeeelenapagfkSLDAKgkelegmkfriQIS----PLDCTGCGNCVDICP 752
|
|
| PRK00783 |
PRK00783 |
DNA-directed RNA polymerase subunit D; Provisional |
5-65 |
4.18e-03 |
|
DNA-directed RNA polymerase subunit D; Provisional
Pssm-ID: 234837 [Multi-domain] Cd Length: 263 Bit Score: 39.10 E-value: 4.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 355505216 5 VKIYDTCIGCTQCVRACPTDVLEMipwDGCKAKQIasapRTEDCVGCKRCESACPTDFLSV 65
Cdd:PRK00783 165 IEVSEDCDECEKCVEACPRGVLEL---KEGKLVVT----DLLNCSLCKLCERACPGKAIRV 218
|
|
| HybA |
COG0437 |
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ... |
11-59 |
4.64e-03 |
|
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion];
Pssm-ID: 440206 [Multi-domain] Cd Length: 184 Bit Score: 38.39 E-value: 4.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 11 CIGCTQ--CVRACPTDVLEmipwdgckakqiasapRTED---------CVGCKRCESACP 59
Cdd:COG0437 60 CNHCDDppCVKVCPTGATY----------------KREDgivlvdydkCIGCRYCVAACP 103
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
45-61 |
4.90e-03 |
|
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440758 [Multi-domain] Cd Length: 66 Bit Score: 35.88 E-value: 4.90e-03
|
| Fer4_4 |
pfam12800 |
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ... |
8-24 |
5.57e-03 |
|
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 463714 Cd Length: 17 Bit Score: 34.64 E-value: 5.57e-03
|
| DsrA |
COG2221 |
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ... |
3-27 |
5.80e-03 |
|
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];
Pssm-ID: 441823 [Multi-domain] Cd Length: 69 Bit Score: 35.80 E-value: 5.80e-03
10 20
....*....|....*....|....*.
gi 355505216 3 HSVKI-YDTCIGCTQCVRACPTDVLE 27
Cdd:COG2221 37 GKLVIdEEKCIGCGACIRVCPTGAIK 62
|
|
| PsrB |
cd10551 |
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ... |
17-59 |
6.48e-03 |
|
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial polysulfide reductase (PsrABC), an integral membrane-bound enzyme responsible for quinone-coupled reduction of polysulfides, a process important in extreme environments such as deep-sea vents and hot springs. Polysulfide reductase contains three subunits: a catalytic subunit PsrA, an electron transfer PsrB subunit and the hydrophobic transmembrane PsrC subunit. PsrB belongs to the DMSO reductase superfamily that contains [4Fe-4S] clusters which transfer the electrons from the A subunit to the hydrophobic integral membrane C subunit via the B subunit. In Shewanella oneidensis, which has highly diverse anaerobic respiratory pathways, PsrABC is responsible for H2S generation as well as its regulation via respiration of sulfur species. PsrB transfers electrons from PsrC (serving as quinol oxidase) to the catalytic subunit PsrA for reduction of corresponding electron acceptors. It has been shown that T. thermophilus polysulfide reductase could be a key energy-conserving enzyme of the respiratory chain, using polysulfide as the terminal electron acceptor and pumping protons across the membrane.
Pssm-ID: 319873 [Multi-domain] Cd Length: 185 Bit Score: 37.90 E-value: 6.48e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 355505216 17 CVRACPTdvlemipwdgcKAKQiasapRTED---------CVGCKRCESACP 59
Cdd:cd10551 61 CVKVCPT-----------GATY-----KREDgivlvdydkCIGCRYCMAACP 96
|
|
| Fer4_2 |
pfam12797 |
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ... |
8-23 |
8.00e-03 |
|
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 463711 [Multi-domain] Cd Length: 22 Bit Score: 33.91 E-value: 8.00e-03
|
| ND2 |
MTH00198 |
NADH dehydrogenase subunit 2; Provisional |
290-404 |
8.17e-03 |
|
NADH dehydrogenase subunit 2; Provisional
Pssm-ID: 214454 [Multi-domain] Cd Length: 607 Bit Score: 39.07 E-value: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355505216 290 YTAFLIAFAVKSPIIPLHTWLPDTHGEAHYSTCMLLAgILLKMGAYGLVRinmelfshAHSIFCPWLMILGSIQIIYAAS 369
Cdd:MTH00198 302 YLFITVAILFKLAAAPFHMWTPDVYEGAPTPTTALIA-IIPKFTVYILLT--------SLVITSKLLLSVAIISLVVGAF 372
|
90 100 110
....*....|....*....|....*....|....*
gi 355505216 370 TSFGQRNLKKRIAYSSVSHMGFIILGIGSISDTGL 404
Cdd:MTH00198 373 GALNQTRIKRLLAYSGIGHIGFILIGVSAGTYESL 407
|
|
| DMSOR_beta_like |
cd16369 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
11-59 |
8.30e-03 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319891 [Multi-domain] Cd Length: 172 Bit Score: 37.37 E-value: 8.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 355505216 11 CIGCTQ--CVRACPTDVLEMIPwDGckAKQIASAPRtedCVGCKRCESACP 59
Cdd:cd16369 51 CMHCEDptCAEVCPADAIKVTE-DG--VVQSALKPR---CIGCSNCVNACP 95
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
1-22 |
8.97e-03 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 404174 [Multi-domain] Cd Length: 56 Bit Score: 34.92 E-value: 8.97e-03
|
| Fer4_2 |
pfam12797 |
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ... |
45-60 |
9.64e-03 |
|
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 463711 [Multi-domain] Cd Length: 22 Bit Score: 33.91 E-value: 9.64e-03
|
| |
