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Conserved domains on  [gi|505341154|ref|WP_015528256|]
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[FeFe] hydrogenase, group A [[Ruminococcus] torques]

Protein Classification

Fe_hyd_lg_C and Fe_hyd_SSU domain-containing protein( domain architecture ID 13374611)

protein containing domains fer2, DMSOR_beta-like, Fe_hyd_lg_C, and Fe_hyd_SSU

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FeFe_hydrog_A6 super family cl48993
NADH-dependent [FeFe] hydrogenase, group A6;
5-558 0e+00

NADH-dependent [FeFe] hydrogenase, group A6;


The actual alignment was detected with superfamily member NF040763:

Pssm-ID: 468723 [Multi-domain]  Cd Length: 571  Bit Score: 780.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154   5 TIDGQVIEFTDEPNVLSVIRKAGIDIPTLCYHSELSIYGACRLCTVEDDRGKTF-ASCSEKPRDGMIIYTNTPRLMRYRK 83
Cdd:NF040763   4 TINGKEVEVPEGTTILEAAKKAGIKIPTLCYLKDINEIGACRVCVVEVEGARNLvAACATPVAEGMVVKTNTPRVREARK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  84 LILELLLAAHCRDCTTCIKSGECHLQELAHRMGVHEIRFENVREIQ--PIDTSSHAIIRDPNKCILCGDCVRMCDNVQNI 161
Cdd:NF040763  84 TVLELILSNHPQDCLTCVRNGNCELQKLAAELGIREIRYEGGEEKSyyIDDTSSPSIVRDPNKCILCRRCVTVCNEVQGV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 162 NAIDFAYRGTDAQVIPAFNKKIAETDCVGCGQCRVVCPTGAISIHTNIDEVWEALADKNTKVIAQIAPAVRVAIGDNFGY 241
Cdd:NF040763 164 GALGAVNRGFKTVVGPAFGKPLADTACTNCGQCIAVCPTGALTEKDNTDKVWDALADPDKHVVVQTAPAVRVALGEEFGL 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 242 AKGENVMGKLVGVLHRLGFDEVYDTSYGADLTVVEESKEFIERFTSGEKMPLFTSCCPAWVKYCENKYPEFVPNLSTCRS 321
Cdd:NF040763 244 PPGTIVTGKMVAALRRLGFDKVFDTDFAADLTIMEEGTELLDRLKNGGVLPMITSCSPGWVKFCEHFYPDLLDNLSTCKS 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 322 PQQMFGAVVREYY-----KDPeknegKKIVSVSIMPCTAKKEEILRPESYTNGKQDVDYVLTTTEIVRMIRKSGIVFDKV 396
Cdd:NF040763 324 PQQMFGAIAKTYYaekmgIDP-----KDIVVVSIMPCTAKKYEAARPEMSVDGYPDVDIVLTTRELARMIKEAGIDFANL 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 397 EIEAADVPFGIGSGSGVIFGVTGGVTEAVLRRLQQGHNRVDMESIKKSGVRGDDGIKVLTYNYNGREIKAAVVNGLANAD 476
Cdd:NF040763 399 PDEEFDNPLGESTGAGVIFGATGGVMEAALRTAYEVLTGKELEKVDFTEVRGLEGIKEATVDINGTEVKVAVAHGLGNAR 478

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 477 KVLQQIKNHEAEYDFVEVMACRRGCIMGGGQP-VNAGPRTRKARMKGLYDTDVNTQIKKSNENPMILSLYDTLLKG---- 551
Cdd:NF040763 479 KLLEKIKAGESDYHFIEIMACPGGCIGGGGQPiHTGNVDVRKKRAKALYEEDKNKPLRKSHENPAIKKLYEEFLGEplsh 558


                 ....*..
gi 505341154 552 KEHELLH 558
Cdd:NF040763 559 KAHELLH 565
 
Name Accession Description Interval E-value
FeFe_hydrog_A6 NF040763
NADH-dependent [FeFe] hydrogenase, group A6;
5-558 0e+00

NADH-dependent [FeFe] hydrogenase, group A6;


Pssm-ID: 468723 [Multi-domain]  Cd Length: 571  Bit Score: 780.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154   5 TIDGQVIEFTDEPNVLSVIRKAGIDIPTLCYHSELSIYGACRLCTVEDDRGKTF-ASCSEKPRDGMIIYTNTPRLMRYRK 83
Cdd:NF040763   4 TINGKEVEVPEGTTILEAAKKAGIKIPTLCYLKDINEIGACRVCVVEVEGARNLvAACATPVAEGMVVKTNTPRVREARK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  84 LILELLLAAHCRDCTTCIKSGECHLQELAHRMGVHEIRFENVREIQ--PIDTSSHAIIRDPNKCILCGDCVRMCDNVQNI 161
Cdd:NF040763  84 TVLELILSNHPQDCLTCVRNGNCELQKLAAELGIREIRYEGGEEKSyyIDDTSSPSIVRDPNKCILCRRCVTVCNEVQGV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 162 NAIDFAYRGTDAQVIPAFNKKIAETDCVGCGQCRVVCPTGAISIHTNIDEVWEALADKNTKVIAQIAPAVRVAIGDNFGY 241
Cdd:NF040763 164 GALGAVNRGFKTVVGPAFGKPLADTACTNCGQCIAVCPTGALTEKDNTDKVWDALADPDKHVVVQTAPAVRVALGEEFGL 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 242 AKGENVMGKLVGVLHRLGFDEVYDTSYGADLTVVEESKEFIERFTSGEKMPLFTSCCPAWVKYCENKYPEFVPNLSTCRS 321
Cdd:NF040763 244 PPGTIVTGKMVAALRRLGFDKVFDTDFAADLTIMEEGTELLDRLKNGGVLPMITSCSPGWVKFCEHFYPDLLDNLSTCKS 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 322 PQQMFGAVVREYY-----KDPeknegKKIVSVSIMPCTAKKEEILRPESYTNGKQDVDYVLTTTEIVRMIRKSGIVFDKV 396
Cdd:NF040763 324 PQQMFGAIAKTYYaekmgIDP-----KDIVVVSIMPCTAKKYEAARPEMSVDGYPDVDIVLTTRELARMIKEAGIDFANL 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 397 EIEAADVPFGIGSGSGVIFGVTGGVTEAVLRRLQQGHNRVDMESIKKSGVRGDDGIKVLTYNYNGREIKAAVVNGLANAD 476
Cdd:NF040763 399 PDEEFDNPLGESTGAGVIFGATGGVMEAALRTAYEVLTGKELEKVDFTEVRGLEGIKEATVDINGTEVKVAVAHGLGNAR 478

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 477 KVLQQIKNHEAEYDFVEVMACRRGCIMGGGQP-VNAGPRTRKARMKGLYDTDVNTQIKKSNENPMILSLYDTLLKG---- 551
Cdd:NF040763 479 KLLEKIKAGESDYHFIEIMACPGGCIGGGGQPiHTGNVDVRKKRAKALYEEDKNKPLRKSHENPAIKKLYEEFLGEplsh 558


                 ....*..
gi 505341154 552 KEHELLH 558
Cdd:NF040763 559 KAHELLH 565
FeFe_hydrog_A TIGR02512
[FeFe] hydrogenase, group A; This model describes iron-only hydrogenases of anaerobic and ...
 137-509 8.50e-173

[FeFe] hydrogenase, group A; This model describes iron-only hydrogenases of anaerobic and microaerophilic bacteria and protozoa. This model is narrower, and covers a longer stretch of sequence, than pfam02906. This family represents a division among families that belong to pfam02906, which also includes proteins such as nuclear prelamin A recognition factor in animals. Note that this family shows some heterogeneity in terms of periplasmic, cytosolic, or hydrogenosome location, NAD or NADP dependence, and overal protein protein length.


Pssm-ID: 274171 [Multi-domain]  Cd Length: 374  Bit Score: 493.76  E-value: 8.50e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  137 AIIRDPNKCILCGDCVRMCDNVQNINAIDFAYRGTDAQVIPAFNKKIAETDCVGCGQCRVVCPTGAISIHTNIDEVWEAL 216
Cdd:TIGR02512   1 SIVRDMSKCIGCGRCVRACTNVQIVGALGFLNRGGKTEVAPKFGRLLDESNCIGCGQCSLVCPVGAITEKDHVDRVLKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  217 ADKNTKVIAQIAPAVRVAIGDNFGYAKGENVMGKLVGVLHRLGFDEVYDTSYGADLTVVEESKEFIERFTSGEKMPLFTS 296
Cdd:TIGR02512  81 ADPKKVVVVQIAPAVRVALGEEFGMPIGTDVTGKMVAALRKLGFDYVFDTNFAADLTIMEEGTELLERLKNGGKLPMFTS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  297 CCPAWVKYCENKYPEFVPNLSTCRSPQQMFGAVVREYYkdPEKN--EGKKIVSVSIMPCTAKKEEILRPESYTNGKQDVD 374
Cdd:TIGR02512 161 CCPGWVNYAEKYYPELLPNLSSCKSPQQMLGAVIKTYW--AKKMgiDPEDVYVVSIMPCTAKKDEAQRPELKSDGYRDVD 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  375 YVLTTTEIVRMIRKSGIVFDKVEIEAADVPFGIGSGSGVIFGVTGGVTEAVLRRLQQGHNRVDMESIKKSGVRGDDGIKV 454
Cdd:TIGR02512 239 AVLTTRELARMIKEAGIDFAKLPDSQFDSPFGEYSGAGAIFGATGGVMEAALRTAYEIVTGKELELIEFKAVRGLDGVKE 318

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 505341154  455 LTYNYNGREIKAAVVNGLANADKVLQQIKNHEAEYDFVEVMACRRGCIMGGGQPV 509
Cdd:TIGR02512 319 ATVDIGGTKVKVAVAHGLGNARKLLDDVKAGEADYHFIEVMACPGGCVNGGGQPK 373
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
59-561 1.07e-171

Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 493.77  E-value: 1.07e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  59 ASCSEKPRDGMIIYTNTPRLMRYRKLILELLLAAHCRDCTTCIKSGECHLQELAHRMGVHEIRFENVREIQPIDTSSHAI 138
Cdd:COG4624    7 ACCCCCIEEGDELLLLEEAERVLRIIILEALLPEHVDDDSACSCCPRCCLCCCCCCRCCVAISCIQVRGIIIIDKRGPSI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 139 IRDPNKCILCGDCVRMCdnvqNINAIDFAYRGtdaqvipafnKKIAETDCVGCGQCRVVCPTGAISIHTNIDEVWEALAD 218
Cdd:COG4624   87 IRDKEKCKNCYPCVRAC----PVKAIKVDDGK----------AEIDEEKCISCGQCVAVCPFGAITEKSDIEKVKKALKD 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 219 KNtKVIAQIAPAVRVAigdnFGyakGENVMGKLVGVLHRLGFDEVYDTSYGADLTVVEESKEFIERFTSGeKMPLFTSCC 298
Cdd:COG4624  153 PE-KVVAQVAPAVRGQ----FG---GTVTPGKLVAALKKLGFDDVFETAFGADLTIMEEAKELLERLKKG-KLPMITSCC 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 299 PAWVKYCENKYPEFVPNLSTCRSPQQMFGAVVREYYkdpekneGKKIVSVSIMPCTAKKEEILRPESytngKQDVDYVLT 378
Cdd:COG4624  224 PAWVKLIEKYYPELLPNLSPCKSPMQAFGALIKTYY-------APDIKVVFIGPCIAKKFEAKRPEM----KGDVDYVLT 292

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 379 TTEIVRMIRKSGIVFDKVEIEAADvpfGIGSGSGVIFGVTGGVTEAVLRRLQQGHNrvdmesikksgvrgddgikvltyn 458
Cdd:COG4624  293 FRELARMIKEAGIDLANLEEEEFD---NESSGAGRIFGVTGGVMEAALRTAYELLP------------------------ 345

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 459 yNGREIKAAVVNGLANADKVLQQIKNHEAEYDFVEVMACRRGCIMGGGQPVNAGPRTRKARMKGLYDTdvNTQIKKSNEN 538
Cdd:COG4624  346 -DGLELKVAVVSGLKNCRKLLEEIKAGKIDYHFIEVMACPGGCIGGPGQPIPPGSLEKRRKRVALYAK--EAPIRKSHEN 422

                        490       500
                 ....*....|....*....|....*..
gi 505341154 539 PMILSLYDTLLKG----KEHELLHRNF 561
Cdd:COG4624  423 PEILDLYREFLGKplseKAHELLHTHY 449
Fe_hyd_lg_C pfam02906
Iron only hydrogenase large subunit, C-terminal domain;
222-505 5.48e-142

Iron only hydrogenase large subunit, C-terminal domain;


Pssm-ID: 397172  Cd Length: 277  Bit Score: 411.24  E-value: 5.48e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  222 KVIAQIAPAVRVAIGDNFGYAKgENVMGKLVGVLHRLGFDEVYDTSYGADLTVVEESKEFIERFTSGEKMPLFTSCCPAW 301
Cdd:pfam02906   2 KVVAQIAPAVRGAFGEEFGLPP-TVTTGKLVAALRKLGFDYVFDTAFGADLTIMEEATEFLERLEKGKKLPMFTSCCPGW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  302 VKYCENKYPEFVPNLSTCRSPQQMFGAVVREYYkdpekNEGKKIVSVSIMPCTAKKEEILRPESYTNgkQDVDYVLTTTE 381
Cdd:pfam02906  81 VKYVEKYYPELLPNLSTCKSPMQMFGALIKTYY-----AEDLKIYVVSIMPCTAKKFEAARPEMKGD--RDVDAVLTTRE 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  382 IVRMIRKSGIVFDKVEIEAADVPFGIGSGSGVIFGVTGGVTEAVLRRLQQGHNRVDMESIKKSGVRGDDGIKVLTYNYNG 461
Cdd:pfam02906 154 LAAMIKEAGIDFAKLEDEEFDNPLGESSGAGRIFGVTGGVMEAALRTAYELLTGKELPAIEFKEVRGLEGIKEATVEIGG 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 505341154  462 REIKAAVVNGLANADKVLQQIKNHEAEYDFVEVMACRRGCIMGG 505
Cdd:pfam02906 234 TTVKVAVVSGLKNARKLLEKIKAGELKYHFIEVMACPGGCIGGG 277
PRK07569 PRK07569
bidirectional hydrogenase complex protein HoxU; Validated
 4-204 4.02e-59

bidirectional hydrogenase complex protein HoxU; Validated


Pssm-ID: 181037 [Multi-domain]  Cd Length: 234  Bit Score: 196.41  E-value: 4.02e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154   4 MTIDGQVIEFTDEPNVLSVIRKAGIDIPTLCYHSELSIYGACRLCTVE-DDRGKTFASCSEKPRDGMIIYTNTPRLMRYR 82
Cdd:PRK07569   6 LTIDDQLVSAREGETLLEAAREAGIPIPTLCHLDGLSDVGACRLCLVEiEGSNKLLPACVTPVAEGMVVQTNTPRLQEYR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  83 KLILELLLAAHCRDCTTCIKSGECHLQELAHRMGVHEIRFENVREIQPIDTSSHAIIRDPNKCILCGDCVRMCDNVQNIN 162
Cdd:PRK07569  86 RMIVELLFAEGNHVCAVCVANGNCELQDLAIEVGMDHVRFPYLFPRRPVDISHPRFGIDHNRCVLCTRCVRVCDEIEGAH 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 505341154 163 AIDFAYRGTDAQVIPAFNKKIAETD-CVGCGQCRVVCPTGAIS 204
Cdd:PRK07569 166 TWDVAGRGAKSRVITDLNQPWGTSEtCTSCGKCVQACPTGAIF 208
NADH-G_4Fe-4S_3 smart00929
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
82-122 2.09e-15

NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;


Pssm-ID: 214918 [Multi-domain]  Cd Length: 41  Bit Score: 69.92  E-value: 2.09e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 505341154    82 RKLILELLLAAHCRDCTTCIKSGECHLQELAHRMGVHEIRF 122
Cdd:smart00929   1 RKTILELLLANHPLDCPVCDKNGECELQDLAYELGVDEQRY 41
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 138-212 6.10e-10

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: 57.41  E-value: 6.10e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505341154 138 IIRDPNKCILCGDCVRMCDNvqniNAIDFAYRGtdaqvIPAFNKKIAETDCVGCGQCRVVCPTGAISIHTNIDEV 212
Cdd:cd10549    1 LKYDPEKCIGCGICVKACPT----DAIELGPNG-----AIARGPEIDEDKCVFCGACVEVCPTGAIELTPEGKEY 66
 
Name Accession Description Interval E-value
FeFe_hydrog_A6 NF040763
NADH-dependent [FeFe] hydrogenase, group A6;
5-558 0e+00

NADH-dependent [FeFe] hydrogenase, group A6;


Pssm-ID: 468723 [Multi-domain]  Cd Length: 571  Bit Score: 780.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154   5 TIDGQVIEFTDEPNVLSVIRKAGIDIPTLCYHSELSIYGACRLCTVEDDRGKTF-ASCSEKPRDGMIIYTNTPRLMRYRK 83
Cdd:NF040763   4 TINGKEVEVPEGTTILEAAKKAGIKIPTLCYLKDINEIGACRVCVVEVEGARNLvAACATPVAEGMVVKTNTPRVREARK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  84 LILELLLAAHCRDCTTCIKSGECHLQELAHRMGVHEIRFENVREIQ--PIDTSSHAIIRDPNKCILCGDCVRMCDNVQNI 161
Cdd:NF040763  84 TVLELILSNHPQDCLTCVRNGNCELQKLAAELGIREIRYEGGEEKSyyIDDTSSPSIVRDPNKCILCRRCVTVCNEVQGV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 162 NAIDFAYRGTDAQVIPAFNKKIAETDCVGCGQCRVVCPTGAISIHTNIDEVWEALADKNTKVIAQIAPAVRVAIGDNFGY 241
Cdd:NF040763 164 GALGAVNRGFKTVVGPAFGKPLADTACTNCGQCIAVCPTGALTEKDNTDKVWDALADPDKHVVVQTAPAVRVALGEEFGL 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 242 AKGENVMGKLVGVLHRLGFDEVYDTSYGADLTVVEESKEFIERFTSGEKMPLFTSCCPAWVKYCENKYPEFVPNLSTCRS 321
Cdd:NF040763 244 PPGTIVTGKMVAALRRLGFDKVFDTDFAADLTIMEEGTELLDRLKNGGVLPMITSCSPGWVKFCEHFYPDLLDNLSTCKS 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 322 PQQMFGAVVREYY-----KDPeknegKKIVSVSIMPCTAKKEEILRPESYTNGKQDVDYVLTTTEIVRMIRKSGIVFDKV 396
Cdd:NF040763 324 PQQMFGAIAKTYYaekmgIDP-----KDIVVVSIMPCTAKKYEAARPEMSVDGYPDVDIVLTTRELARMIKEAGIDFANL 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 397 EIEAADVPFGIGSGSGVIFGVTGGVTEAVLRRLQQGHNRVDMESIKKSGVRGDDGIKVLTYNYNGREIKAAVVNGLANAD 476
Cdd:NF040763 399 PDEEFDNPLGESTGAGVIFGATGGVMEAALRTAYEVLTGKELEKVDFTEVRGLEGIKEATVDINGTEVKVAVAHGLGNAR 478

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 477 KVLQQIKNHEAEYDFVEVMACRRGCIMGGGQP-VNAGPRTRKARMKGLYDTDVNTQIKKSNENPMILSLYDTLLKG---- 551
Cdd:NF040763 479 KLLEKIKAGESDYHFIEIMACPGGCIGGGGQPiHTGNVDVRKKRAKALYEEDKNKPLRKSHENPAIKKLYEEFLGEplsh 558


                 ....*..
gi 505341154 552 KEHELLH 558
Cdd:NF040763 559 KAHELLH 565
FeFe_hydrog_A TIGR02512
[FeFe] hydrogenase, group A; This model describes iron-only hydrogenases of anaerobic and ...
 137-509 8.50e-173

[FeFe] hydrogenase, group A; This model describes iron-only hydrogenases of anaerobic and microaerophilic bacteria and protozoa. This model is narrower, and covers a longer stretch of sequence, than pfam02906. This family represents a division among families that belong to pfam02906, which also includes proteins such as nuclear prelamin A recognition factor in animals. Note that this family shows some heterogeneity in terms of periplasmic, cytosolic, or hydrogenosome location, NAD or NADP dependence, and overal protein protein length.


Pssm-ID: 274171 [Multi-domain]  Cd Length: 374  Bit Score: 493.76  E-value: 8.50e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  137 AIIRDPNKCILCGDCVRMCDNVQNINAIDFAYRGTDAQVIPAFNKKIAETDCVGCGQCRVVCPTGAISIHTNIDEVWEAL 216
Cdd:TIGR02512   1 SIVRDMSKCIGCGRCVRACTNVQIVGALGFLNRGGKTEVAPKFGRLLDESNCIGCGQCSLVCPVGAITEKDHVDRVLKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  217 ADKNTKVIAQIAPAVRVAIGDNFGYAKGENVMGKLVGVLHRLGFDEVYDTSYGADLTVVEESKEFIERFTSGEKMPLFTS 296
Cdd:TIGR02512  81 ADPKKVVVVQIAPAVRVALGEEFGMPIGTDVTGKMVAALRKLGFDYVFDTNFAADLTIMEEGTELLERLKNGGKLPMFTS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  297 CCPAWVKYCENKYPEFVPNLSTCRSPQQMFGAVVREYYkdPEKN--EGKKIVSVSIMPCTAKKEEILRPESYTNGKQDVD 374
Cdd:TIGR02512 161 CCPGWVNYAEKYYPELLPNLSSCKSPQQMLGAVIKTYW--AKKMgiDPEDVYVVSIMPCTAKKDEAQRPELKSDGYRDVD 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  375 YVLTTTEIVRMIRKSGIVFDKVEIEAADVPFGIGSGSGVIFGVTGGVTEAVLRRLQQGHNRVDMESIKKSGVRGDDGIKV 454
Cdd:TIGR02512 239 AVLTTRELARMIKEAGIDFAKLPDSQFDSPFGEYSGAGAIFGATGGVMEAALRTAYEIVTGKELELIEFKAVRGLDGVKE 318

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 505341154  455 LTYNYNGREIKAAVVNGLANADKVLQQIKNHEAEYDFVEVMACRRGCIMGGGQPV 509
Cdd:TIGR02512 319 ATVDIGGTKVKVAVAHGLGNARKLLDDVKAGEADYHFIEVMACPGGCVNGGGQPK 373
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
59-561 1.07e-171

Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 493.77  E-value: 1.07e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  59 ASCSEKPRDGMIIYTNTPRLMRYRKLILELLLAAHCRDCTTCIKSGECHLQELAHRMGVHEIRFENVREIQPIDTSSHAI 138
Cdd:COG4624    7 ACCCCCIEEGDELLLLEEAERVLRIIILEALLPEHVDDDSACSCCPRCCLCCCCCCRCCVAISCIQVRGIIIIDKRGPSI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 139 IRDPNKCILCGDCVRMCdnvqNINAIDFAYRGtdaqvipafnKKIAETDCVGCGQCRVVCPTGAISIHTNIDEVWEALAD 218
Cdd:COG4624   87 IRDKEKCKNCYPCVRAC----PVKAIKVDDGK----------AEIDEEKCISCGQCVAVCPFGAITEKSDIEKVKKALKD 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 219 KNtKVIAQIAPAVRVAigdnFGyakGENVMGKLVGVLHRLGFDEVYDTSYGADLTVVEESKEFIERFTSGeKMPLFTSCC 298
Cdd:COG4624  153 PE-KVVAQVAPAVRGQ----FG---GTVTPGKLVAALKKLGFDDVFETAFGADLTIMEEAKELLERLKKG-KLPMITSCC 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 299 PAWVKYCENKYPEFVPNLSTCRSPQQMFGAVVREYYkdpekneGKKIVSVSIMPCTAKKEEILRPESytngKQDVDYVLT 378
Cdd:COG4624  224 PAWVKLIEKYYPELLPNLSPCKSPMQAFGALIKTYY-------APDIKVVFIGPCIAKKFEAKRPEM----KGDVDYVLT 292

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 379 TTEIVRMIRKSGIVFDKVEIEAADvpfGIGSGSGVIFGVTGGVTEAVLRRLQQGHNrvdmesikksgvrgddgikvltyn 458
Cdd:COG4624  293 FRELARMIKEAGIDLANLEEEEFD---NESSGAGRIFGVTGGVMEAALRTAYELLP------------------------ 345

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 459 yNGREIKAAVVNGLANADKVLQQIKNHEAEYDFVEVMACRRGCIMGGGQPVNAGPRTRKARMKGLYDTdvNTQIKKSNEN 538
Cdd:COG4624  346 -DGLELKVAVVSGLKNCRKLLEEIKAGKIDYHFIEVMACPGGCIGGPGQPIPPGSLEKRRKRVALYAK--EAPIRKSHEN 422

                        490       500
                 ....*....|....*....|....*..
gi 505341154 539 PMILSLYDTLLKG----KEHELLHRNF 561
Cdd:COG4624  423 PEILDLYREFLGKplseKAHELLHTHY 449
Fe_hyd_lg_C pfam02906
Iron only hydrogenase large subunit, C-terminal domain;
222-505 5.48e-142

Iron only hydrogenase large subunit, C-terminal domain;


Pssm-ID: 397172  Cd Length: 277  Bit Score: 411.24  E-value: 5.48e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  222 KVIAQIAPAVRVAIGDNFGYAKgENVMGKLVGVLHRLGFDEVYDTSYGADLTVVEESKEFIERFTSGEKMPLFTSCCPAW 301
Cdd:pfam02906   2 KVVAQIAPAVRGAFGEEFGLPP-TVTTGKLVAALRKLGFDYVFDTAFGADLTIMEEATEFLERLEKGKKLPMFTSCCPGW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  302 VKYCENKYPEFVPNLSTCRSPQQMFGAVVREYYkdpekNEGKKIVSVSIMPCTAKKEEILRPESYTNgkQDVDYVLTTTE 381
Cdd:pfam02906  81 VKYVEKYYPELLPNLSTCKSPMQMFGALIKTYY-----AEDLKIYVVSIMPCTAKKFEAARPEMKGD--RDVDAVLTTRE 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  382 IVRMIRKSGIVFDKVEIEAADVPFGIGSGSGVIFGVTGGVTEAVLRRLQQGHNRVDMESIKKSGVRGDDGIKVLTYNYNG 461
Cdd:pfam02906 154 LAAMIKEAGIDFAKLEDEEFDNPLGESSGAGRIFGVTGGVMEAALRTAYELLTGKELPAIEFKEVRGLEGIKEATVEIGG 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 505341154  462 REIKAAVVNGLANADKVLQQIKNHEAEYDFVEVMACRRGCIMGG 505
Cdd:pfam02906 234 TTVKVAVVSGLKNARKLLEKIKAGELKYHFIEVMACPGGCIGGG 277
FeFe_hydrog_B1 TIGR04105
[FeFe] hydrogenase, group B1/B3; See for descriptions of different groups.
 137-506 2.60e-72

[FeFe] hydrogenase, group B1/B3; See for descriptions of different groups.


Pssm-ID: 274983 [Multi-domain]  Cd Length: 462  Bit Score: 238.65  E-value: 2.60e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  137 AIIrDPNKCILCGDCVRMCDnvqnINAIDFAYR------GTDAQVIPAFNK-KIAETDCVGCGQCRVVCPTGAISIHTNI 209
Cdd:TIGR04105 137 AYI-DQEKCIECGKCKKACP----YNAIVEIERpcekacPVGAISSDEDGRaVIDYDKCISCGACMVACPFGAISDKSQI 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  210 DEVWEALAdKNTKVIAQIAPAVrvaIGdNFG-YAKgenvMGKLVGVLHRLGFDEVYDTSYGADLTVVEESKEFIERFTSG 288
Cdd:TIGR04105 212 VQVIKALK-SGKKVYAMVAPAI---VG-QFGpKAT----PGQVKTALKKLGFADVVEVALGADMVAVHEAEEFAERVEEG 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  289 EKmPLFTSCCPAWVKYCENKYPEFVPNLSTCRSPQQMFGAVVREYYKDpeknegkkIVSVSIMPCTAKKEEILRPEsytn 368
Cdd:TIGR04105 283 KK-FMTTSCCPAFVNMIKKHFPELAENISTTVSPMVATARYIKKKDPD--------AKVVFIGPCIAKKLEAQRDE---- 349

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  369 GKQDVDYVLTTTEIVRMIRKSGIVFDKVEIEAADVPfgigSGSGVIFGVTGGVTEAVlrrlqqghnrvdMESIKKSGVrg 448
Cdd:TIGR04105 350 VKGDVDYVLTFEELAAMFDAKGIDLEECEEEDLDDA----SAFGRGFAVSGGVAAAV------------KAAIKEKGP-- 411

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 505341154  449 ddgikvltynynGREIKAAVVNGLANADKVLQQIKNHEAEYDFVEVMACRRGCIMGGG 506
Cdd:TIGR04105 412 ------------DVEVKPVKCNGLDECKKALTLAKAGKLPGNFIEGMACEGGCVGGPG 457
NuoG COG1034
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ...
 1-203 1.36e-61

NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 440657 [Multi-domain]  Cd Length: 453  Bit Score: 209.70  E-value: 1.36e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154   1 MGIMTIDGQVIEFTDEPNVLSVIRKAGIDIPTLCYHSELSIYGACRLCTVEDD-RGKTFASCSEKPRDGMIIYTNTPRLM 79
Cdd:COG1034    1 MVTITIDGKEVEVPKGTTVLQAAEKAGIEIPRFCYHPKLSIAGACRMCLVEVEgAPKPVASCATPVTDGMVVKTDSPKVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  80 RYRKLILELLLAAHCRDCTTCIKSGECHLQELAHRMGVHEIRFENVREIQPIDTSSHAIIRDPNKCILCGDCVRMCDNVQ 159
Cdd:COG1034   81 KARKGVMEFLLINHPLDCPICDQGGECDLQDQAMEYGVDESRYEEEKRTVPKKDLGPLILLDMNRCILCTRCVRFCDEIA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 505341154 160 NINAIDFAYRGTDAQVIPAFNKKIaetDCVGCGQCRVVCPTGAI 203
Cdd:COG1034  161 GDPELGVIGRGEHSEIGTYLGKPL---DSEFSGNCIDVCPVGAL 201
PRK07569 PRK07569
bidirectional hydrogenase complex protein HoxU; Validated
 4-204 4.02e-59

bidirectional hydrogenase complex protein HoxU; Validated


Pssm-ID: 181037 [Multi-domain]  Cd Length: 234  Bit Score: 196.41  E-value: 4.02e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154   4 MTIDGQVIEFTDEPNVLSVIRKAGIDIPTLCYHSELSIYGACRLCTVE-DDRGKTFASCSEKPRDGMIIYTNTPRLMRYR 82
Cdd:PRK07569   6 LTIDDQLVSAREGETLLEAAREAGIPIPTLCHLDGLSDVGACRLCLVEiEGSNKLLPACVTPVAEGMVVQTNTPRLQEYR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  83 KLILELLLAAHCRDCTTCIKSGECHLQELAHRMGVHEIRFENVREIQPIDTSSHAIIRDPNKCILCGDCVRMCDNVQNIN 162
Cdd:PRK07569  86 RMIVELLFAEGNHVCAVCVANGNCELQDLAIEVGMDHVRFPYLFPRRPVDISHPRFGIDHNRCVLCTRCVRVCDEIEGAH 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 505341154 163 AIDFAYRGTDAQVIPAFNKKIAETD-CVGCGQCRVVCPTGAIS 204
Cdd:PRK07569 166 TWDVAGRGAKSRVITDLNQPWGTSEtCTSCGKCVQACPTGAIF 208
PRK08493 PRK08493
NADH-quinone oxidoreductase subunit G;
4-204 4.86e-42

NADH-quinone oxidoreductase subunit G;


Pssm-ID: 236277 [Multi-domain]  Cd Length: 819  Bit Score: 161.41  E-value: 4.86e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154   4 MTIDGQVIEFTDEPNVLSVIRKAGIDIPTLCYHSELSIYGACRLCTVEDDrGKTFASCSEKPRDGMIIYTNTPRLMRYRK 83
Cdd:PRK08493   4 ITINGKECEAQEGEYILNVARRNGIFIPAICYLSGCSPTLACRLCMVEAD-GKRVYSCNTKAKEGMNILTNTPNLMDERN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  84 LILELLLAAHCRDCTTCIKSGECHLQELAHRMGVHEIRFEnVREI-QPIDTSSHaIIRDPNKCILCGDCVRMCDNVQNIN 162
Cdd:PRK08493  83 AIMQTYDVNHPLECGVCDKSGECELQNFTHEMGVNHQPYA-IKDThKPHKHWGK-INYDPSLCIVCERCVTVCKDKIGES 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505341154 163 AIDFAYRGTDA--------------QVIPAFNKKI------AETDCVGCGQCRVVCPTGAIS 204
Cdd:PRK08493 161 ALKTVPRGLDApdksfkesmpkdayAVWSKKQKSLigpvggETLDCSFCGECIAVCPVGALS 222
PRK07860 PRK07860
NADH dehydrogenase subunit G; Validated
 5-175 1.50e-21

NADH dehydrogenase subunit G; Validated


Pssm-ID: 236118 [Multi-domain]  Cd Length: 797  Bit Score: 98.86  E-value: 1.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154   5 TIDGQVIeftDEPNVLSVIRKA---GIDIPTLCYHSELSIYGACRLCTVEDdRG--KTFASCSEKPRDGMIIYT--NTPR 77
Cdd:PRK07860   8 TIDGVEV---SVPKGTLVIRAAellGIQIPRFCDHPLLDPVGACRQCLVEV-EGqrKPQASCTTTVTDGMVVKTqlTSPV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  78 LMRYRKLILELLLAAHCRDCTTCIKSGECHLQELAHRMGVHEIRFENVREI--QPIDTSSHaIIRDPNKCILCGDCVRMC 155
Cdd:PRK07860  84 ADKAQHGVMELLLINHPLDCPVCDKGGECPLQNQAMSNGRAESRFTDVKRTfpKPINISTQ-VLLDRERCVLCARCTRFS 162

                        170       180
                 ....*....|....*....|
gi 505341154 156 DNVQNINAIDFAYRGTDAQV 175
Cdd:PRK07860 163 DQIAGDPFIDLQERGALQQV 182
PTZ00305 PTZ00305
NADH:ubiquinone oxidoreductase; Provisional
 2-237 8.45e-21

NADH:ubiquinone oxidoreductase; Provisional


Pssm-ID: 140326 [Multi-domain]  Cd Length: 297  Bit Score: 93.18  E-value: 8.45e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154   2 GIMTIDGQVIEFT-DEPNVLSVIRKAGIDIPTLCYHSELSIYGACRLCTVEDDRGKTF-ASCSEKPRDGMIIYTNTpRLM 79
Cdd:PTZ00305  69 AIMFVNKRPVEIIpQEENLLEVLEREGIRVPKFCYHPILSVAGNCRMCLVQVDGTQNLvVSCATVALPGMSIITDS-RLV 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  80 R-YRKLILELLLAAHCRDCTTCIKSGECHLQELAHRMGVHEIRF-ENVREIQP--IDTSSHAIIrdpNKCILCGDCVR-M 154
Cdd:PTZ00305 148 RdAREGNVELILINHPNDCPICEQATNCDLQNVSMNYGTDIPRYkEDKRAVQDfyFDPQTRVVL---NRCIHCTRCVRfL 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 155 CDNVQNINaIDFAYRGTDAQVIPAFNKKIAETD-CVGCGQcrvVCPTGAISIHTnidevwealADKNTKVIAQIAPAVRV 233
Cdd:PTZ00305 225 NEHAQDFN-LGMIGRGGLSEISTFLDELEVKTDnNMPVSQ---LCPVGKLYLGD---------ADENNAIARELDAAEQT 291


                 ....
gi 505341154 234 AIGD 237
Cdd:PTZ00305 292 AAVA 295
NADH-G_4Fe-4S_3 pfam10588
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
82-121 2.93e-17

NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;


Pssm-ID: 463159 [Multi-domain]  Cd Length: 40  Bit Score: 75.18  E-value: 2.93e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 505341154   82 RKLILELLLAAHCRDCTTCIKSGECHLQELAHRMGVHEIR 121
Cdd:pfam10588   1 RKTILELLLSNHPLDCPTCDKNGNCELQDLAYELGVDEVR 40
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
 4-108 4.51e-17

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 84.78  E-value: 4.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154   4 MTIDGQVIEFTDEPNVLSVIRKAGIDIPTLCYHSELSIYGACRLCTVE-DDRGKTFASCSEKPRDGMIIYTNTPRLMRYR 82
Cdd:PRK12814   6 LTINGRSVTAAPGTSILEAAASAGITIPTLCFHQELEATGSCWMCIVEiKGKNRFVPACSTAVSEGMVIETENAELHAMR 85

                         90       100
                 ....*....|....*....|....*.
gi 505341154  83 KLILELLLAAHCRDCTtciksGECHL 108
Cdd:PRK12814  86 RQSLERLIEQHCGDCL-----GPCEL 106
NADH-G_4Fe-4S_3 smart00929
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
82-122 2.09e-15

NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;


Pssm-ID: 214918 [Multi-domain]  Cd Length: 41  Bit Score: 69.92  E-value: 2.09e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 505341154    82 RKLILELLLAAHCRDCTTCIKSGECHLQELAHRMGVHEIRF 122
Cdd:smart00929   1 RKTILELLLANHPLDCPVCDKNGECELQDLAYELGVDEQRY 41
Fe_hyd_SSU pfam02256
Iron hydrogenase small subunit; This family represents the small subunit of the Fe-only ...
 516-558 2.52e-11

Iron hydrogenase small subunit; This family represents the small subunit of the Fe-only hydrogenases EC:1.18.99.1. The subunit is comprised of alternating random coil and alpha helical structures that encompasses the large subunit in a novel protein fold.


Pssm-ID: 460511 [Multi-domain]  Cd Length: 56  Bit Score: 59.05  E-value: 2.52e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 505341154  516 RKARMKGLYDTDVNTQIKKSNENPMILSLYDTLLKG----KEHELLH 558
Cdd:pfam02256   4 RKKRAEALYKIDKNKPLRKSHENPAVKKLYEEFLGEplshKAHELLH 50
Fer2_4 pfam13510
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 5-76 9.76e-11

2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which a beta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated. This cluster appears within sarcosine oxidase proteins.


Pssm-ID: 433268 [Multi-domain]  Cd Length: 82  Bit Score: 57.93  E-value: 9.76e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505341154    5 TIDGQVIE-FTDEPnVLSVIRKAGIDIPTLCYHSE----LSIYGACRLCTVEDDRGKTFASCSEKPRDGMIIYTNTP 76
Cdd:pfam13510   7 TFDGRPVTaPEGDT-IAAALLANGVRVPRSCKYGRprgiFCAMGECRNCLVEVDGVPNVRACTTPVREGMVVRTQNG 82
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 138-212 6.10e-10

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: 57.41  E-value: 6.10e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505341154 138 IIRDPNKCILCGDCVRMCDNvqniNAIDFAYRGtdaqvIPAFNKKIAETDCVGCGQCRVVCPTGAISIHTNIDEV 212
Cdd:cd10549    1 LKYDPEKCIGCGICVKACPT----DAIELGPNG-----AIARGPEIDEDKCVFCGACVEVCPTGAIELTPEGKEY 66
Fe_hyd_SSU smart00902
Iron hydrogenase small subunit; Many microorganisms, such as methanogenic, acetogenic, ...
 518-558 7.73e-10

Iron hydrogenase small subunit; Many microorganisms, such as methanogenic, acetogenic, nitrogen-fixing, photosynthetic, or sulphate-reducing bacteria, metabolise hydrogen. Hydrogen activation is mediated by a family of enzymes, termed hydrogenases, which either provide these organisms with reducing power from hydrogen oxidation, or act as electron sinks. There are two hydrogenases families that differ functionally from each other: NiFe hydrogenases tend to be more involved in hydrogen oxidation, while Iron-only FeFe (Fe only) hydrogenases in hydrogen production. Fe only hydrogenases show a common core structure, which contains a moiety, deeply buried inside the protein, with an Fe-Fe dinuclear centre, nonproteic bridging, terminal CO and CN- ligands attached to each of the iron atoms, and a dithio moiety, which also bridges the two iron atoms and has been tentatively assigned as a di(thiomethyl)amine. This common core also harbours three [4Fe-4S] iron-sulphur clusters. In FeFe hydrogenases, as in NiFe hydrogenases, the set of iron-sulphur clusters is dispersed regularly between the dinuclear Fe-Fe centre and the molecular surface. These clusters are distant by about 1.2 nm from each other but the [4Fe-4S] cluster closest to the dinuclear centre is covalently bound to one of the iron atoms though a thiolate bridging ligand. The moiety including the dinuclear centre, the thiolate bridging ligand, and the proximal [4Fe-4S] cluster is known as the H-cluster. A channel, lined with hydrophobic amino acid side chains, nearly connects the dinuclear centre and the molecular surface. Furthermore hydrogen-bonded water molecule sites have been identified at the interior and at the surface of the protein. The small subunit is comprised of alternating random coil and alpha helical structures that encompass the large subunit in a novel protein fold.


Pssm-ID: 214899 [Multi-domain]  Cd Length: 52  Bit Score: 54.57  E-value: 7.73e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 505341154   518 ARMKGLYDTDVNTQIKKSNENPMILSLYDTLLKG----KEHELLH 558
Cdd:smart00902   1 QRAEALYNIDKSLPLRKSHENPAVKKLYEEFLGGplshKAHELLH 45
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 141-206 1.75e-09

MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 53.96  E-value: 1.75e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505341154 141 DPNKCILCGDCVRMCdnvqNINAIdfayrgtdaQVIPAFNKKIAETDCVGCGQCRVVCPTGAISIH 206
Cdd:COG1149    9 DEEKCIGCGLCVEVC----PEGAI---------KLDDGGAPVVDPDLCTGCGACVGVCPTGAITLE 61
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
138-212 2.28e-09

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 53.97  E-value: 2.28e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505341154 138 IIRDPNKCILCGDCVRMCDNvqniNAIDFayrgtdaqvipafNKKIAETD---CVGCGQCRVVCPTGAISIHTNIDEV 212
Cdd:COG2768    6 PYVDEEKCIGCGACVKVCPV----GAISI-------------EDGKAVIDpekCIGCGACIEVCPVGAIKIEWEEDEE 66
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 141-213 7.08e-09

NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 52.40  E-value: 7.08e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505341154 141 DPNKCILCGDCVRMCDNvqniNAIDFAYRGTDAQVIpafnkkiAETDCVGCGQCRVVCPTGAISIHTNIDEVW 213
Cdd:COG1146    6 DTDKCIGCGACVEVCPV----DVLELDEEGKKALVI-------NPEECIGCGACELVCPVGAITVEDDEPEEQ 67
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 127-205 2.34e-08

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: 52.78  E-value: 2.34e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505341154 127 EIQPIDTSSHAIIRDPNKCILCGDCVRMCDnvqnINAIDFAYRGTDAQVIPAfNKKIAETDCVGCGQCRVVCPTGAISI 205
Cdd:cd10549   24 ELGPNGAIARGPEIDEDKCVFCGACVEVCP----TGAIELTPEGKEYVPKEK-EAEIDEEKCIGCGLCVKVCPVDAITL 97
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 142-214 3.59e-08

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: 50.13  E-value: 3.59e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505341154 142 PNKCILCGDCVRMCdnvqNINAIDFAYRGTDAQVIpafnkkIAETDCVGCGQCRVVCPTGAISIHTNIDEVWE 214
Cdd:COG1143    1 EDKCIGCGLCVRVC----PVDAITIEDGEPGKVYV------IDPDKCIGCGLCVEVCPTGAISMTPFELAVED 63
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 145-202 5.81e-08

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: 49.45  E-value: 5.81e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 505341154  145 CILCGDCVRMCDNvqniNAIDFAYRGTDAQVipaFNKKIAETDCVGCGQCRVVCPTGA 202
Cdd:pfam12838   1 CIGCGACVAACPV----GAITLDEVGEKKGT---KTVVIDPERCVGCGACVAVCPTGA 51
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 136-205 7.44e-08

Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 49.66  E-value: 7.44e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505341154 136 HAIIRDPNKCILCGDCVRMCDnvqnINAIDFAyrgtdaqvipafNKKIA--ETDCVGCGQCRVVCPTGAISI 205
Cdd:COG2221    8 WPPKIDEEKCIGCGLCVAVCP----TGAISLD------------DGKLVidEEKCIGCGACIRVCPTGAIKG 63
NapF COG1145
Ferredoxin [Energy production and conversion];
94-205 9.60e-08

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 53.19  E-value: 9.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  94 CRDCTTCIKSGECHLQELAHRMGVHEIRFENVREIQPIDTSSHAIIRDPNKCILCGDCVRMCDNvqniNAIDFAYRGTDA 173
Cdd:COG1145  133 LVIAAALAEAGLAILGAAAPVDALAISGGKKIEEELKIAIKKAKAVIDAEKCIGCGLCVKVCPT----GAIRLKDGKPQI 208

                         90       100       110
                 ....*....|....*....|....*....|..
gi 505341154 174 QVIPAfnkkiaetDCVGCGQCRVVCPTGAISI 205
Cdd:COG1145  209 VVDPD--------KCIGCGACVKVCPVGAISL 232
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
141-206 1.41e-07

Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 54.10  E-value: 1.41e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505341154 141 DPNKCILCGDCVRMCdnvqNINAIDFAYRGTdAQVIPAFnkkiaetdCVGCGQCRVVCPTGAISIH 206
Cdd:COG1148  494 DPEKCTGCGRCVEVC----PYGAISIDEKGV-AEVNPAL--------CKGCGTCAAACPSGAISLK 546
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 141-205 9.39e-07

TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 46.57  E-value: 9.39e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505341154 141 DPNKCILCGDCVRMCDnvqninaidfayrgtdAQVIPAFNKK--IAETDCVGCGQCRVVCPTGAISI 205
Cdd:COG4231   20 DEDKCTGCGACVKVCP----------------ADAIEEGDGKavIDPDLCIGCGSCVQVCPVDAIKL 70
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 141-205 1.62e-06

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: 46.20  E-value: 1.62e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505341154 141 DPNKCILCGDCVRMC-DNvqninAIDFAyRGTDAQVIPAfnkkiaetDCVGCGQCRVVCPTGAISI 205
Cdd:COG1144   28 DEDKCIGCGLCWIVCpDG-----AIRVD-DGKYYGIDYD--------YCKGCGICAEVCPVKAIEM 79
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
138-207 2.02e-06

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 49.29  E-value: 2.02e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 138 IIRDPNKCILCGDCVRMCDNVQNINaidfayrgtdaqvipafNKKIAETDCVGCGQCRVVCPTGAISIHT 207
Cdd:COG0348  205 VRYDRGDCIDCGLCVKVCPMGIDIR-----------------KGEINQSECINCGRCIDACPKDAIRFSS 257
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 117-205 4.75e-06

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: 46.24  E-value: 4.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 117 VHEIRFENVREIQPIDTSSHAIirDPNKCILCGDCVRMCDnvqnINAIDFAYRGtdaqvipafNKKIAETDCVGCGQCRV 196
Cdd:cd10549   54 TGAIELTPEGKEYVPKEKEAEI--DEEKCIGCGLCVKVCP----VDAITLEDEL---------EIVIDKEKCIGCGICAE 118


                 ....*....
gi 505341154 197 VCPTGAISI 205
Cdd:cd10549  119 VCPVNAIKL 127
PRK08348 PRK08348
NADH-plastoquinone oxidoreductase subunit; Provisional
 138-205 6.63e-06

NADH-plastoquinone oxidoreductase subunit; Provisional


Pssm-ID: 181399 [Multi-domain]  Cd Length: 120  Bit Score: 45.60  E-value: 6.63e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505341154 138 IIRDPNKCILCGDCVRMCDnvqnINAIDFayrgtdaqvIPAFNK-KIAETDCVGCGQCRVVCPTGAISI 205
Cdd:PRK08348  37 ILYDVDKCVGCRMCVTVCP----AGVFVY---------LPEIRKvALWTGRCVFCGQCVDVCPTGALQM 92
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 7-71 7.00e-06

2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.


Pssm-ID: 238126 [Multi-domain]  Cd Length: 84  Bit Score: 44.31  E-value: 7.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154   7 DGQVIEFTDEPNVLSVIRKAGIDIPTLCYHselsiyGACRLCTV-----------------EDDRGKTFASCSEKPRDGM 69
Cdd:cd00207    8 SGVEVEVPEGETLLDAAREAGIDIPYSCRA------GACGTCKVevvegevdqsdpslldeEEAEGGYVLACQTRVTDGL 81


                 ..
gi 505341154  70 II 71
Cdd:cd00207   82 VI 83
Fer4_9 pfam13187
4Fe-4S dicluster domain;
144-203 7.15e-06

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 43.31  E-value: 7.15e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  144 KCILCGDCVRMCdNVQNINAIDFAYRgtdaqvipaFNKKIAETDCVGCGQCRVVCPTGAI 203
Cdd:pfam13187   1 KCTGCGACVAAC-PAGAIVPDLVGQT---------IRGDIAGLACIGCGACVDACPRGAI 50
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
141-212 8.05e-06

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 47.62  E-value: 8.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 141 DPNKCILCGDCVRMCDNvqniNAIDFAYRgtDAQVIPAFN--------KKIAETDCVGCGQCRVVCPTGAISIHTNIDEV 212
Cdd:PRK07118 166 DEDKCTGCGACVKACPR----NVIELIPK--SARVFVACNskdkgkavKKVCEVGCIGCGKCVKACPAGAITMENNLAVI 239
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 145-208 1.07e-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: 45.31  E-value: 1.07e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505341154 145 CILCGDcvrMCDNvqniNAIDFAYRgtdaqVIPAFNKKIAETDCVGCGQCRVVCPTGAISIHTN 208
Cdd:cd10564   88 CRSCQD---ACPT----QAIRFRPR-----LGGIALPELDADACTGCGACVSVCPVGAITLTPL 139
PRK14028 PRK14028
pyruvate ferredoxin oxidoreductase subunit gamma/delta; Provisional
 139-205 1.80e-05

pyruvate ferredoxin oxidoreductase subunit gamma/delta; Provisional


Pssm-ID: 172522 [Multi-domain]  Cd Length: 312  Bit Score: 46.91  E-value: 1.80e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 139 IRDPNKCILCGDCVRMCDNvqniNAIDFAYRGTDAQVIPAFNKKIAETD---CVGCGQCRVVCPTGAISI 205
Cdd:PRK14028 243 VIDHSKCIMCRKCWLYCPD----DAIIEAWREAEGPRGRKFRMKMIDFDyqyCKGCGVCAEVCPTGAIQM 308
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 141-205 5.13e-05

bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.


Pssm-ID: 349764 [Multi-domain]  Cd Length: 246  Bit Score: 45.07  E-value: 5.13e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505341154 141 DPNKCILCGDCVRMCdnvqNINAIdfayrGTDAQVIPAFnkkiaETDCVGCGQCRVVCPTGAISI 205
Cdd:cd03110   62 DQEKCIRCGNCERVC----KFGAI-----LEFFQKLIVD-----ESLCEGCGACVIICPRGAIYL 112
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
91-207 1.04e-04

Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 42.34  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  91 AAHCRDCTTCIKSgeCHLqelAHRMGVHEIRFENvreiqpIDTSSHAIIRDPNKCILCGD--CVRMCDNvqniNAIdfaY 168
Cdd:COG1142    9 PEKCIGCRTCEAA--CAV---AHEGEEGEPFLPR------IRVVRKAGVSAPVQCRHCEDapCAEVCPV----GAI---T 70

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 505341154 169 RGTDAQVIpafnkkiAETDCVGCGQCRVVCPTGAISIHT 207
Cdd:COG1142   71 RDDGAVVV-------DEEKCIGCGLCVLACPFGAITMVG 102
ACS_1 cd01916
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ...
 143-284 1.06e-04

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: 45.09  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 143 NKCILCGDCVRMCDNVQNI-NAIDFAYRGTdaqvipaFNKKIAETD-CVGCGQCRVVCPTGaISIHTNIDEVWEA-LADK 219
Cdd:cd01916  365 AKCTDCGWCTRACPNSLRIkEAMEAAKEGD-------FSGLADLFDqCVGCGRCEQECPKE-IPIINMIEKAARErIKEE 436

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505341154 220 NTKVIAQIAPAVRVAIgdnfgYAKGEN-VMGKLVGVL-------HRLGFDEVYDTsygadltvveeSKEFIER 284
Cdd:cd01916  437 KGKMRAGRGPIKDTEI-----RKVGAPiVLGDIPGVIalvgcsnYPNGTKDVYKI-----------AEEFLER 493
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 137-199 1.20e-04

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: 39.93  E-value: 1.20e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505341154  137 AIIRDPNKCILCGDCVRMC-DNVQNINAIDFAYRGTDAQVIPafnkkiaeTDCVGCGQCRVVCP 199
Cdd:pfam13237   1 KVVIDPDKCIGCGRCTAACpAGLTRVGAIVERLEGEAVRIGV--------WKCIGCGACVEACP 56
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 141-206 1.59e-04

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: 43.44  E-value: 1.59e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505341154 141 DPNKCILCGDCVRMCDnvqnINAIDFAYRGTdAQVIPAFnkkiaetdCVGCGQCRVVCPTGAISIH 206
Cdd:COG2878  135 CEYGCIGCGDCIKACP----FDAIVGAAKGM-HTVDEDK--------CTGCGLCVEACPVDCIEMV 187
Fer4_17 pfam13534
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 144-201 2.11e-04

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: 39.37  E-value: 2.11e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  144 KCILCGDCVRMCD--NVQNINAIDFAYRGTDAQVIPAFNKKIAEtDCVGCGQCRVVCPTG 201
Cdd:pfam13534   1 RCIQCGCCVDECPryLLNGDEPKKLMRAAYLGDLEELQANKVAN-LCSECGLCEYACPMG 59
PRK08318 PRK08318
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
141-204 2.20e-04

NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;


Pssm-ID: 236237 [Multi-domain]  Cd Length: 420  Bit Score: 43.78  E-value: 2.20e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505341154 141 DPNKCILCGDCVRMCDNVQNiNAIDFAYRGTDaqvipafNKKIAETDCVGCGQCRVVCPT-GAIS 204
Cdd:PRK08318 340 DQDKCIGCGRCYIACEDTSH-QAIEWDEDGTR-------TPEVIEEECVGCNLCAHVCPVeGCIT 396
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 175-205 3.39e-04

Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 39.26  E-value: 3.39e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 505341154 175 VIPAFNKKIAETDCVGCGQCRVVCPTGAISI 205
Cdd:COG2221    4 IIGTWPPKIDEEKCIGCGLCVAVCPTGAISL 34
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 100-206 3.56e-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: 41.32  E-value: 3.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  100 CIKSGECHLQELAHRMGVHEIRFENVREIQPIDTSSHAIIrDPNKCILCGDCVRMCDnvqninaidfayrgTDAQV-IPA 178
Cdd:TIGR01944  71 CPPGGEAVILALAELLGVEPIPQPLDADAGTIQPPMVALI-DEDNCIGCTKCIQACP--------------VDAIVgAAK 135

                          90       100
                  ....*....|....*....|....*...
gi 505341154  179 FNKKIAETDCVGCGQCRVVCPTGAISIH 206
Cdd:TIGR01944 136 AMHTVIADECTGCDLCVEPCPTDCIEMI 163
PRK12387 PRK12387
formate hydrogenlyase complex iron-sulfur subunit; Provisional
 141-203 4.04e-04

formate hydrogenlyase complex iron-sulfur subunit; Provisional


Pssm-ID: 183492 [Multi-domain]  Cd Length: 180  Bit Score: 41.56  E-value: 4.04e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505341154 141 DPNKCILCGDCVRMCDNvqniNAIDFAYRGTDAQVIPAFNKkiaeTDCVGCGQCRVVCPTGAI 203
Cdd:PRK12387  36 NPQQCIGCAACVNACPS----NALTVETDLATGELAWEFNL----GRCIFCGRCEEVCPTAAI 90
Fer4_21 pfam14697
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 137-200 5.67e-04

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: 38.03  E-value: 5.67e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505341154  137 AIIrDPNKCILCGDCVRMCdNVQNINAIdfayRGTDAQVIPafnkkIAETDCVGCGQCRVVCPT 200
Cdd:pfam14697   1 ARI-DEDTCIGCGKCYIAC-PDTSHQAI----VGDGKRHHT-----VIEDECTGCNLCVSVCPV 53
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 144-201 5.92e-04

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: 38.45  E-value: 5.92e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505341154  144 KCILCGDCVRMCDNVQNIN---AIDFAYRGTDAQVIPAFNKKIAET--DCVGCGQCRVVCPTG 201
Cdd:pfam13183   1 RCIRCGACLAACPVYLVTGgrfPGDPRGGAAALLGRLEALEGLAEGlwLCTLCGACTEVCPVG 63
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
5-67 6.63e-04

2Fe-2S iron-sulfur cluster binding domain;


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 38.66  E-value: 6.63e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505341154    5 TIDGQVIEFT---DEPNVLSVIRKAGIDIPTLCYHselsiyGACRLCTVEDDRGKTFASCSEKPRD 67
Cdd:pfam00111   2 TINGKGVTIEvpdGETTLLDAAEEAGIDIPYSCRG------GGCGTCAVKVLEGEDQSDQSFLEDD 61
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 137-205 7.22e-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: 39.87  E-value: 7.22e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505341154 137 AIIRDPNKCILCGDCVRMCDnvqnINAIdfayrgtdaQVIPAFNKKIAETDCVGCGQCRVVCPTGAISI 205
Cdd:cd10550   74 AVVVDEDKCIGCGMCVEACP----FGAI---------RVDPETGKAIKCDLCGGDPACVKVCPTGALEF 129
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 138-208 1.17e-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: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 39.24  E-value: 1.17e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505341154 138 IIRDPNKCILCGDCVRMCDNVQninaidfaYRGTDAQ----VIPAFNKKIAETDCVGCGQCRVVCPTGAISIHTN 208
Cdd:cd16372    3 LVTDPEKCIGCLQCEEACSKTF--------FKEEDREksciRITETEGGYAINVCNQCGECIDVCPTGAITRDAN 69
PRK06273 PRK06273
ferredoxin; Provisional
 181-203 1.19e-03

ferredoxin; Provisional


Pssm-ID: 235764 [Multi-domain]  Cd Length: 165  Bit Score: 40.08  E-value: 1.19e-03
                         10        20
                 ....*....|....*....|...
gi 505341154 181 KKIAETDCVGCGQCRVVCPTGAI 203
Cdd:PRK06273  44 KKVFEELCIGCGGCANVCPTKAI 66
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 182-204 1.32e-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: 36.46  E-value: 1.32e-03
                          10        20
                  ....*....|....*....|...
gi 505341154  182 KIAETDCVGCGQCRVVCPTGAIS 204
Cdd:pfam00037   2 VIDEEKCIGCGACVEVCPVGAIT 24
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
137-205 1.54e-03

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 41.33  E-value: 1.54e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505341154 137 AII-RD---PNKCILcgDCVRMCDNVQNinaidfayrGTDAQVIPAFNKK--IAETDCVGCGQCRVVCPTGAISI 205
Cdd:PRK13409   5 AVVdYDrcqPKKCNY--ECIKYCPVVRT---------GEETIEIDEDDGKpvISEELCIGCGICVKKCPFDAISI 68
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 137-206 1.74e-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: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 39.16  E-value: 1.74e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505341154 137 AIIrDPNKCIL------CGDCVRMCdNVQNInAIDFAYRGTDAQVIPAFnkkiaetdCVGCGQCRVVCPT---GAISIH 206
Cdd:cd16373   86 AVI-DKDRCLAwqggtdCGVCVEAC-PTEAI-AIVLEDDVLRPVVDEDK--------CVGCGLCEYVCPVeppKAIVVE 153
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 126-261 1.91e-03

Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];


Pssm-ID: 440017 [Multi-domain]  Cd Length: 420  Bit Score: 40.83  E-value: 1.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 126 REIQPIDTSSHAIIRDP-NKCILCGDCVRMC----------DN-VQNINAIDFAYRGTDAQVIPAFNKKIAETdCVGCGQ 193
Cdd:COG0247   60 LHDKNLKTLPWKELLDAlDACVGCGFCRAMCpsykatgdekDSpRGRINLLREVLEGELPLDLSEEVYEVLDL-CLTCKA 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 194 CRVVCPTGaISIHTNIDEVWEALADKN-------------TKVIAQIAPAVRVAI----GDNFGYAKgenVMGKLVGVLH 256
Cdd:COG0247  139 CETACPSG-VDIADLIAEARAQLVERGgrplrdrllrtfpDRVPAADKEGAEVLLfpgcFTNYFDPE---IGKAAVRLLE 214


                 ....*
gi 505341154 257 RLGFD 261
Cdd:COG0247  215 AAGVE 219
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 137-205 2.32e-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: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 38.09  E-value: 2.32e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505341154 137 AIIRDPN--------KCILCGDCVRMCDnvqnINAIDFAyrgtdaqvipafNKKIAETDCVGCGQCRVVCPTGAISI 205
Cdd:cd16372   63 AITRDANgvvminkkLCVGCLMCVGFCP----EGAMFKH------------EDYPEPFKCIACGICVKACPTGALEL 123
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 182-205 2.50e-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: 2.50e-03
                         10        20
                 ....*....|....*....|....
gi 505341154 182 KIAETDCVGCGQCRVVCPTGAISI 205
Cdd:COG1149    7 VIDEEKCIGCGLCVEVCPEGAIKL 30
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
145-223 3.27e-03

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 39.53  E-value: 3.27e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505341154 145 CILCGDCVRMCDnvqninaidfayrgTDAQVIPAFNKKIAETDCVGCGQCRVVCPTGAIsIHTNIDEVWEALADKNTKV 223
Cdd:PRK07118 215 CIGCGKCVKACP--------------AGAITMENNLAVIDQEKCTSCGKCVEKCPTKAI-RILNKPPKVKEPKKAAAEA 278
sulfite_red_C TIGR02912
sulfite reductase, subunit C; Members of this protein family include the C subunit, one of ...
 141-202 3.39e-03

sulfite reductase, subunit C; Members of this protein family include the C subunit, one of three subunits, of the anaerobic sulfite reductase of Salmonella, and close homologs from various Clostridum species, where the three-gene neighborhood is preserved. Two such gene clusters are found in Clostridium perfringens, but it may be that these sets of genes correspond to the distinct assimilatory and dissimilatory forms as seen in Clostridium pasteurianum. Note that any one of these enzymes may have secondary substates such as NH2OH, SeO3(2-), and SO3(2-). Heterologous expression of the anaerobic sulfite reductase of Salmonella confers on Escherichia coli the ability to produce hydrogen sulfide gas from sulfite. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 131958 [Multi-domain]  Cd Length: 314  Bit Score: 39.85  E-value: 3.39e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505341154  141 DPNKCILCGDCVRMCdnvqninaidfAYRGTDAQVIPAFNKKIAETDCVGCGQCRVVCPTGA 202
Cdd:TIGR02912 167 DADRCIGCGACVKVC-----------KKKAVGALSFENYKVVRDHSKCIGCGECVLKCPTGA 217
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 137-205 4.09e-03

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 40.15  E-value: 4.09e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505341154 137 AII-RD---PNKCILcgDCVRMCDNVQNinaidfayrGTDAQVIPAFNKK--IAETDCVGCGQCRVVCPTGAISI 205
Cdd:COG1245    5 AVVdRDrcqPKKCNY--ECIKYCPVNRT---------GKEAIEIDEDDGKpvISEELCIGCGICVKKCPFDAISI 68
PRK09898 PRK09898
ferredoxin-like protein;
137-205 6.17e-03

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 38.28  E-value: 6.17e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505341154 137 AIIRDPNKCILCGDCVRMCDNVQninaidfayrgtdAQVIPAFNKkiaETDCVGCGQCRVVCPTGAISI 205
Cdd:PRK09898 148 CITVDHKRCIGCSACTTACPWMM-------------ATVNTESKK---SSKCVLCGECANACPTGALKI 200
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 128-211 6.42e-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: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 36.93  E-value: 6.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 128 IQPIDTSSHAIIrdpNKCILCGDCVRMCdNVQNInaidfaYRgtDAQVIPAFNKKIaetdCVGCGQCRVVCPTGAISIHT 207
Cdd:cd16372   35 IRITETEGGYAI---NVCNQCGECIDVC-PTGAI------TR--DANGVVMINKKL----CVGCLMCVGFCPEGAMFKHE 98


                 ....
gi 505341154 208 NIDE 211
Cdd:cd16372   99 DYPE 102
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 106-226 7.96e-03

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 38.96  E-value: 7.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 106 CHLQELAHRMGVHEIRF-ENVREIQP-IDTSSHAIIRDPNKCILCGD--CVRMCDNvqniNAIdfAYRGTDAQVIpafnk 181
Cdd:PRK12769  15 CHACEIACVMAHNDEQHvLSQHHFHPrITVIKHQQQRSAVTCHHCEDapCARSCPN----GAI--SHVDDSIQVN----- 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 505341154 182 kiaETDCVGCGQCRVVCPTGAISIhtnideVWEALADKNTKVIAQ 226
Cdd:PRK12769  84 ---QQKCIGCKSCVVACPFGTMQI------VLTPVAAGKVKATAH 119
NapF COG1145
Ferredoxin [Energy production and conversion];
22-205 9.37e-03

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 38.17  E-value: 9.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154  22 VIRKAGIDIPTLCYHSELSIYGACRLCTVEDDRGKTFASCSEKPRDGMIIytNTPRLMRYRKLILELLLAAHCRDCTTCI 101
Cdd:COG1145   21 VVTGILGKIILNVIAGALLKAVALGGLLPIIGILAKEAFDALKDVLGILG--AIVIGIGAGEIVRVGIAAADLNLKAVAL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341154 102 KSGECHLQELAHRMGVHEIRFENVREIQPIDTSSHAIIRDPNKCILCGDCVRMCDNVQNINAIDFAYRGTDAQVIPAFNK 181
Cdd:COG1145   99 VLLLALAVAGAAKRLIISAVKLVAGLVVAAGEVLLVIAAALAEAGLAILGAAAPVDALAISGGKKIEEELKIAIKKAKAV 178

                        170       180
                 ....*....|....*....|....
gi 505341154 182 KIAETdCVGCGQCRVVCPTGAISI 205
Cdd:COG1145  179 IDAEK-CIGCGLCVKVCPTGAIRL 201
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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