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Conserved domains on  [gi|489524335|ref|WP_003429109|]
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NADH-dependent [FeFe] hydrogenase, group A6 [Clostridioides difficile]

Protein Classification

2Fe-2S iron-sulfur cluster binding domain-containing protein( domain architecture ID 13374584)

2Fe-2S iron-sulfur cluster binding domain-containing protein similar to Clostridium pasteurianum [FeFe]-hydrogenase CpI that uses 4Fe-4S and 2Fe-2S iron-sulfur clusters for the generation and oxidation of molecular hydrogen

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FeFe_hydrog_A6 NF040763
NADH-dependent [FeFe] hydrogenase, group A6;
4-576 0e+00

NADH-dependent [FeFe] hydrogenase, group A6;


:

Pssm-ID: 468723 [Multi-domain]  Cd Length: 571  Bit Score: 1087.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335   4 VNLTINGKHVSAPSGTSILDAAKLINIKIHNLCHLHMneidkLDTCASCRVCMVETE--RGLVPACGTVIKEGMKVQTNS 81
Cdd:NF040763   1 VNLTINGKEVEVPEGTTILEAAKKAGIKIPTLCYLKD-----INEIGACRVCVVEVEgaRNLVAACATPVAEGMVVKTNT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335  82 AKALNARRTIVELLLSDHPQDCFVCEKNGDCELQTIAADLGVRKIRYQG--SKSFAGKDTSTKSLVKDHSKCILCRRCET 159
Cdd:NF040763  76 PRVREARKTVLELILSNHPQDCLTCVRNGNCELQKLAAELGIREIRYEGgeEKSYYIDDTSSPSIVRDPNKCILCRRCVT 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335 160 VCNDIQTVGALSGVNRGFNTLVSTFFNSDMVETECTFCGQCISVCPTGALTEVDNVPKLWDVLNKKEKTIVVQVAPAVRV 239
Cdd:NF040763 156 VCNEVQGVGALGAVNRGFKTVVGPAFGKPLADTACTNCGQCIAVCPTGALTEKDNTDKVWDALADPDKHVVVQTAPAVRV 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335 240 AIGEEFGLEPGSISTGKMVAALKALGFEHVFDTNFGADFTIMEEATEFIERIQKGENLPILTSCCPAWVNFLEHNYPDKL 319
Cdd:NF040763 236 ALGEEFGLPPGTIVTGKMVAALRRLGFDKVFDTDFAADLTIMEEGTELLDRLKNGGVLPMITSCSPGWVKFCEHFYPDLL 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335 320 NLASSCKSPQGMFGSIAKNYYAPKIlGINPEELYVVSVMPCVAKKYEASREELSESGILDVDLSITTRELAKMIKEAAID 399
Cdd:NF040763 316 DNLSTCKSPQQMFGAIAKTYYAEKM-GIDPKDIVVVSIMPCTAKKYEAARPEMSVDGYPDVDIVLTTRELARMIKEAGID 394

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335 400 LPNLQDQDFDNPLGKSTGAASIFGASGGVLEAALRTSYEKITNKTLDNVNFTNVRGLKGIREASIDVDGTTVNVCIVNTL 479
Cdd:NF040763 395 FANLPDEEFDNPLGESTGAGVIFGATGGVMEAALRTAYEVLTGKELEKVDFTEVRGLEGIKEATVDINGTEVKVAVAHGL 474

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335 480 KNARKIMDKVRSGECKYHIIEVMACPGGCVGGAGQPYHHGNTEIVDRRANALYEIDRNKAIRKSHENPDLQAIYKDFFGE 559
Cdd:NF040763 475 GNARKLLEKIKAGESDYHFIEIMACPGGCIGGGGQPIHTGNVDVRKKRAKALYEEDKNKPLRKSHENPAIKKLYEEFLGE 554

                        570
                 ....*....|....*..
gi 489524335 560 PNSDVAHKYLHTHYFDK 576
Cdd:NF040763 555 PLSHKAHELLHTHYTKR 571
 
Name Accession Description Interval E-value
FeFe_hydrog_A6 NF040763
NADH-dependent [FeFe] hydrogenase, group A6;
4-576 0e+00

NADH-dependent [FeFe] hydrogenase, group A6;


Pssm-ID: 468723 [Multi-domain]  Cd Length: 571  Bit Score: 1087.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335   4 VNLTINGKHVSAPSGTSILDAAKLINIKIHNLCHLHMneidkLDTCASCRVCMVETE--RGLVPACGTVIKEGMKVQTNS 81
Cdd:NF040763   1 VNLTINGKEVEVPEGTTILEAAKKAGIKIPTLCYLKD-----INEIGACRVCVVEVEgaRNLVAACATPVAEGMVVKTNT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335  82 AKALNARRTIVELLLSDHPQDCFVCEKNGDCELQTIAADLGVRKIRYQG--SKSFAGKDTSTKSLVKDHSKCILCRRCET 159
Cdd:NF040763  76 PRVREARKTVLELILSNHPQDCLTCVRNGNCELQKLAAELGIREIRYEGgeEKSYYIDDTSSPSIVRDPNKCILCRRCVT 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335 160 VCNDIQTVGALSGVNRGFNTLVSTFFNSDMVETECTFCGQCISVCPTGALTEVDNVPKLWDVLNKKEKTIVVQVAPAVRV 239
Cdd:NF040763 156 VCNEVQGVGALGAVNRGFKTVVGPAFGKPLADTACTNCGQCIAVCPTGALTEKDNTDKVWDALADPDKHVVVQTAPAVRV 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335 240 AIGEEFGLEPGSISTGKMVAALKALGFEHVFDTNFGADFTIMEEATEFIERIQKGENLPILTSCCPAWVNFLEHNYPDKL 319
Cdd:NF040763 236 ALGEEFGLPPGTIVTGKMVAALRRLGFDKVFDTDFAADLTIMEEGTELLDRLKNGGVLPMITSCSPGWVKFCEHFYPDLL 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335 320 NLASSCKSPQGMFGSIAKNYYAPKIlGINPEELYVVSVMPCVAKKYEASREELSESGILDVDLSITTRELAKMIKEAAID 399
Cdd:NF040763 316 DNLSTCKSPQQMFGAIAKTYYAEKM-GIDPKDIVVVSIMPCTAKKYEAARPEMSVDGYPDVDIVLTTRELARMIKEAGID 394

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335 400 LPNLQDQDFDNPLGKSTGAASIFGASGGVLEAALRTSYEKITNKTLDNVNFTNVRGLKGIREASIDVDGTTVNVCIVNTL 479
Cdd:NF040763 395 FANLPDEEFDNPLGESTGAGVIFGATGGVMEAALRTAYEVLTGKELEKVDFTEVRGLEGIKEATVDINGTEVKVAVAHGL 474

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335 480 KNARKIMDKVRSGECKYHIIEVMACPGGCVGGAGQPYHHGNTEIVDRRANALYEIDRNKAIRKSHENPDLQAIYKDFFGE 559
Cdd:NF040763 475 GNARKLLEKIKAGESDYHFIEIMACPGGCIGGGGQPIHTGNVDVRKKRAKALYEEDKNKPLRKSHENPAIKKLYEEFLGE 554

                        570
                 ....*....|....*..
gi 489524335 560 PNSDVAHKYLHTHYFDK 576
Cdd:NF040763 555 PLSHKAHELLHTHYTKR 571
FeFe_hydrog_A TIGR02512
[FeFe] hydrogenase, group A; This model describes iron-only hydrogenases of anaerobic and ...
 143-517 0e+00

[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: 580.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335  143 SLVKDHSKCILCRRCETVCNDIQTVGALSGVNRGFNTLVSTFFNSDMVETECTFCGQCISVCPTGALTEVDNVPKLWDVL 222
Cdd:TIGR02512   1 SIVRDMSKCIGCGRCVRACTNVQIVGALGFLNRGGKTEVAPKFGRLLDESNCIGCGQCSLVCPVGAITEKDHVDRVLKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335  223 NKKEKTIVVQVAPAVRVAIGEEFGLEPGSISTGKMVAALKALGFEHVFDTNFGADFTIMEEATEFIERIQKGENLPILTS 302
Cdd:TIGR02512  81 ADPKKVVVVQIAPAVRVALGEEFGMPIGTDVTGKMVAALRKLGFDYVFDTNFAADLTIMEEGTELLERLKNGGKLPMFTS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335  303 CCPAWVNFLEHNYPDKLNLASSCKSPQGMFGSIAKNYYApKILGINPEELYVVSVMPCVAKKYEASREELSESGILDVDL 382
Cdd:TIGR02512 161 CCPGWVNYAEKYYPELLPNLSSCKSPQQMLGAVIKTYWA-KKMGIDPEDVYVVSIMPCTAKKDEAQRPELKSDGYRDVDA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335  383 SITTRELAKMIKEAAIDLPNLQDQDFDNPLGKSTGAASIFGASGGVLEAALRTSYEKITNKTLDNVNFTNVRGLKGIREA 462
Cdd:TIGR02512 240 VLTTRELARMIKEAGIDFAKLPDSQFDSPFGEYSGAGAIFGATGGVMEAALRTAYEIVTGKELELIEFKAVRGLDGVKEA 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 489524335  463 SIDVDGTTVNVCIVNTLKNARKIMDKVRSGECKYHIIEVMACPGGCVGGAGQPYH 517
Cdd:TIGR02512 320 TVDIGGTKVKVAVAHGLGNARKLLDDVKAGEADYHFIEVMACPGGCVNGGGQPKV 374
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
60-573 0e+00

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 534.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335  60 ERGLVPACGTVIKEGMKVQTNSAKALNARRTIVELLLSDHPQDCFVCEKNGDCELQTIAADLGVRKIRYQGSKSFAGKDT 139
Cdd:COG4624    2 LLLLRACCCCCIEEGDELLLLEEAERVLRIIILEALLPEHVDDDSACSCCPRCCLCCCCCCRCCVAISCIQVRGIIIIDK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335 140 STKSLVKDHSKCILCRRCETVCNdiqtVGALSGVNRGfntlvstffnSDMVETECTFCGQCISVCPTGALTEVDNVPKLW 219
Cdd:COG4624   82 RGPSIIRDKEKCKNCYPCVRACP----VKAIKVDDGK----------AEIDEEKCISCGQCVAVCPFGAITEKSDIEKVK 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335 220 DVLNKKEKtIVVQVAPAVRVAigeeFGlepGSISTGKMVAALKALGFEHVFDTNFGADFTIMEEATEFIERIQKGeNLPI 299
Cdd:COG4624  148 KALKDPEK-VVAQVAPAVRGQ----FG---GTVTPGKLVAALKKLGFDDVFETAFGADLTIMEEAKELLERLKKG-KLPM 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335 300 LTSCCPAWVNFLEHNYPDKLNLASSCKSPQGMFGSIAKNYYAPKIlginpeelYVVSVMPCVAKKYEASREELSEsgilD 379
Cdd:COG4624  219 ITSCCPAWVKLIEKYYPELLPNLSPCKSPMQAFGALIKTYYAPDI--------KVVFIGPCIAKKFEAKRPEMKG----D 286

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335 380 VDLSITTRELAKMIKEAAIDLPNLQDQDFDNPlgkSTGAASIFGASGGVLEAALRTSYEKITnktldnvnftnvrglkgi 459
Cdd:COG4624  287 VDYVLTFRELARMIKEAGIDLANLEEEEFDNE---SSGAGRIFGVTGGVMEAALRTAYELLP------------------ 345

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335 460 reasidvDGTTVNVCIVNTLKNARKIMDKVRSGECKYHIIEVMACPGGCVGGAGQPYHHGNTEIVDRRAnALYEidRNKA 539
Cdd:COG4624  346 -------DGLELKVAVVSGLKNCRKLLEEIKAGKIDYHFIEVMACPGGCIGGPGQPIPPGSLEKRRKRV-ALYA--KEAP 415

                        490       500       510
                 ....*....|....*....|....*....|....
gi 489524335 540 IRKSHENPDLQAIYKDFFGEPNSDVAHKYLHTHY 573
Cdd:COG4624  416 IRKSHENPEILDLYREFLGKPLSEKAHELLHTHY 449
Fe_hyd_lg_C pfam02906
Iron only hydrogenase large subunit, C-terminal domain;
227-512 2.74e-161

Iron only hydrogenase large subunit, C-terminal domain;


Pssm-ID: 397172  Cd Length: 277  Bit Score: 461.70  E-value: 2.74e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335  227 KTIVVQVAPAVRVAIGEEFGLEPgSISTGKMVAALKALGFEHVFDTNFGADFTIMEEATEFIERIQKGENLPILTSCCPA 306
Cdd:pfam02906   1 KKVVAQIAPAVRGAFGEEFGLPP-TVTTGKLVAALRKLGFDYVFDTAFGADLTIMEEATEFLERLEKGKKLPMFTSCCPG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335  307 WVNFLEHNYPDKLNLASSCKSPQGMFGSIAKNYYAPKilginpEELYVVSVMPCVAKKYEASREELSesGILDVDLSITT 386
Cdd:pfam02906  80 WVKYVEKYYPELLPNLSTCKSPMQMFGALIKTYYAED------LKIYVVSIMPCTAKKFEAARPEMK--GDRDVDAVLTT 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335  387 RELAKMIKEAAIDLPNLQDQDFDNPLGKSTGAASIFGASGGVLEAALRTSYEKITNKTLDNVNFTNVRGLKGIREASIDV 466
Cdd:pfam02906 152 RELAAMIKEAGIDFAKLEDEEFDNPLGESSGAGRIFGVTGGVMEAALRTAYELLTGKELPAIEFKEVRGLEGIKEATVEI 231

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 489524335  467 DGTTVNVCIVNTLKNARKIMDKVRSGECKYHIIEVMACPGGCVGGA 512
Cdd:pfam02906 232 GGTTVKVAVVSGLKNARKLLEKIKAGELKYHFIEVMACPGGCIGGG 277
PRK07569 PRK07569
bidirectional hydrogenase complex protein HoxU; Validated
 1-209 1.22e-53

bidirectional hydrogenase complex protein HoxU; Validated


Pssm-ID: 181037 [Multi-domain]  Cd Length: 234  Bit Score: 182.54  E-value: 1.22e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335   1 MSLVNLTINGKHVSAPSGTSILDAAKLINIKIHNLCHLhmneiDKLDTCASCRVCMVETE--RGLVPACGTVIKEGMKVQ 78
Cdd:PRK07569   1 MSVKTLTIDDQLVSAREGETLLEAAREAGIPIPTLCHL-----DGLSDVGACRLCLVEIEgsNKLLPACVTPVAEGMVVQ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335  79 TNSAKALNARRTIVELLLSDHPQDCFVCEKNGDCELQTIAADLGVRKIRYQGSKSFAGKDTSTKSLVKDHSKCILCRRCE 158
Cdd:PRK07569  76 TNTPRLQEYRRMIVELLFAEGNHVCAVCVANGNCELQDLAIEVGMDHVRFPYLFPRRPVDISHPRFGIDHNRCVLCTRCV 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489524335 159 TVCNDIQTVGALSGVNRGFNTLVSTFFNSDMVETE-CTFCGQCISVCPTGAL 209
Cdd:PRK07569 156 RVCDEIEGAHTWDVAGRGAKSRVITDLNQPWGTSEtCTSCGKCVQACPTGAI 207
Fe_hyd_SSU smart00902
Iron hydrogenase small subunit; Many microorganisms, such as methanogenic, acetogenic, ...
 526-577 5.01e-23

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: 91.93  E-value: 5.01e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 489524335   526 RRANALYEIDRNKAIRKSHENPDLQAIYKDFFGEPNSDVAHKYLHTHYFDKS 577
Cdd:smart00902   1 QRAEALYNIDKSLPLRKSHENPAVKKLYEEFLGGPLSHKAHELLHTHYHDRE 52
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 144-210 6.91e-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: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 45.65  E-value: 6.91e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489524335 144 LVKDHSKCILCRRCETVCndiqtvgalSGVNRG-FN------TLVSTFFNSDMVETECTFCGQ--CISVCPTGALT 210
Cdd:cd10550    1 LVVDPEKCTGCRTCELAC---------SLKHEGvFNpslsriRVVRFEPEGLDVPVVCRQCEDapCVEACPVGAIS 67
 
Name Accession Description Interval E-value
FeFe_hydrog_A6 NF040763
NADH-dependent [FeFe] hydrogenase, group A6;
4-576 0e+00

NADH-dependent [FeFe] hydrogenase, group A6;


Pssm-ID: 468723 [Multi-domain]  Cd Length: 571  Bit Score: 1087.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335   4 VNLTINGKHVSAPSGTSILDAAKLINIKIHNLCHLHMneidkLDTCASCRVCMVETE--RGLVPACGTVIKEGMKVQTNS 81
Cdd:NF040763   1 VNLTINGKEVEVPEGTTILEAAKKAGIKIPTLCYLKD-----INEIGACRVCVVEVEgaRNLVAACATPVAEGMVVKTNT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335  82 AKALNARRTIVELLLSDHPQDCFVCEKNGDCELQTIAADLGVRKIRYQG--SKSFAGKDTSTKSLVKDHSKCILCRRCET 159
Cdd:NF040763  76 PRVREARKTVLELILSNHPQDCLTCVRNGNCELQKLAAELGIREIRYEGgeEKSYYIDDTSSPSIVRDPNKCILCRRCVT 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335 160 VCNDIQTVGALSGVNRGFNTLVSTFFNSDMVETECTFCGQCISVCPTGALTEVDNVPKLWDVLNKKEKTIVVQVAPAVRV 239
Cdd:NF040763 156 VCNEVQGVGALGAVNRGFKTVVGPAFGKPLADTACTNCGQCIAVCPTGALTEKDNTDKVWDALADPDKHVVVQTAPAVRV 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335 240 AIGEEFGLEPGSISTGKMVAALKALGFEHVFDTNFGADFTIMEEATEFIERIQKGENLPILTSCCPAWVNFLEHNYPDKL 319
Cdd:NF040763 236 ALGEEFGLPPGTIVTGKMVAALRRLGFDKVFDTDFAADLTIMEEGTELLDRLKNGGVLPMITSCSPGWVKFCEHFYPDLL 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335 320 NLASSCKSPQGMFGSIAKNYYAPKIlGINPEELYVVSVMPCVAKKYEASREELSESGILDVDLSITTRELAKMIKEAAID 399
Cdd:NF040763 316 DNLSTCKSPQQMFGAIAKTYYAEKM-GIDPKDIVVVSIMPCTAKKYEAARPEMSVDGYPDVDIVLTTRELARMIKEAGID 394

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335 400 LPNLQDQDFDNPLGKSTGAASIFGASGGVLEAALRTSYEKITNKTLDNVNFTNVRGLKGIREASIDVDGTTVNVCIVNTL 479
Cdd:NF040763 395 FANLPDEEFDNPLGESTGAGVIFGATGGVMEAALRTAYEVLTGKELEKVDFTEVRGLEGIKEATVDINGTEVKVAVAHGL 474

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335 480 KNARKIMDKVRSGECKYHIIEVMACPGGCVGGAGQPYHHGNTEIVDRRANALYEIDRNKAIRKSHENPDLQAIYKDFFGE 559
Cdd:NF040763 475 GNARKLLEKIKAGESDYHFIEIMACPGGCIGGGGQPIHTGNVDVRKKRAKALYEEDKNKPLRKSHENPAIKKLYEEFLGE 554

                        570
                 ....*....|....*..
gi 489524335 560 PNSDVAHKYLHTHYFDK 576
Cdd:NF040763 555 PLSHKAHELLHTHYTKR 571
FeFe_hydrog_A TIGR02512
[FeFe] hydrogenase, group A; This model describes iron-only hydrogenases of anaerobic and ...
 143-517 0e+00

[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: 580.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335  143 SLVKDHSKCILCRRCETVCNDIQTVGALSGVNRGFNTLVSTFFNSDMVETECTFCGQCISVCPTGALTEVDNVPKLWDVL 222
Cdd:TIGR02512   1 SIVRDMSKCIGCGRCVRACTNVQIVGALGFLNRGGKTEVAPKFGRLLDESNCIGCGQCSLVCPVGAITEKDHVDRVLKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335  223 NKKEKTIVVQVAPAVRVAIGEEFGLEPGSISTGKMVAALKALGFEHVFDTNFGADFTIMEEATEFIERIQKGENLPILTS 302
Cdd:TIGR02512  81 ADPKKVVVVQIAPAVRVALGEEFGMPIGTDVTGKMVAALRKLGFDYVFDTNFAADLTIMEEGTELLERLKNGGKLPMFTS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335  303 CCPAWVNFLEHNYPDKLNLASSCKSPQGMFGSIAKNYYApKILGINPEELYVVSVMPCVAKKYEASREELSESGILDVDL 382
Cdd:TIGR02512 161 CCPGWVNYAEKYYPELLPNLSSCKSPQQMLGAVIKTYWA-KKMGIDPEDVYVVSIMPCTAKKDEAQRPELKSDGYRDVDA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335  383 SITTRELAKMIKEAAIDLPNLQDQDFDNPLGKSTGAASIFGASGGVLEAALRTSYEKITNKTLDNVNFTNVRGLKGIREA 462
Cdd:TIGR02512 240 VLTTRELARMIKEAGIDFAKLPDSQFDSPFGEYSGAGAIFGATGGVMEAALRTAYEIVTGKELELIEFKAVRGLDGVKEA 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 489524335  463 SIDVDGTTVNVCIVNTLKNARKIMDKVRSGECKYHIIEVMACPGGCVGGAGQPYH 517
Cdd:TIGR02512 320 TVDIGGTKVKVAVAHGLGNARKLLDDVKAGEADYHFIEVMACPGGCVNGGGQPKV 374
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
60-573 0e+00

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 534.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335  60 ERGLVPACGTVIKEGMKVQTNSAKALNARRTIVELLLSDHPQDCFVCEKNGDCELQTIAADLGVRKIRYQGSKSFAGKDT 139
Cdd:COG4624    2 LLLLRACCCCCIEEGDELLLLEEAERVLRIIILEALLPEHVDDDSACSCCPRCCLCCCCCCRCCVAISCIQVRGIIIIDK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335 140 STKSLVKDHSKCILCRRCETVCNdiqtVGALSGVNRGfntlvstffnSDMVETECTFCGQCISVCPTGALTEVDNVPKLW 219
Cdd:COG4624   82 RGPSIIRDKEKCKNCYPCVRACP----VKAIKVDDGK----------AEIDEEKCISCGQCVAVCPFGAITEKSDIEKVK 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335 220 DVLNKKEKtIVVQVAPAVRVAigeeFGlepGSISTGKMVAALKALGFEHVFDTNFGADFTIMEEATEFIERIQKGeNLPI 299
Cdd:COG4624  148 KALKDPEK-VVAQVAPAVRGQ----FG---GTVTPGKLVAALKKLGFDDVFETAFGADLTIMEEAKELLERLKKG-KLPM 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335 300 LTSCCPAWVNFLEHNYPDKLNLASSCKSPQGMFGSIAKNYYAPKIlginpeelYVVSVMPCVAKKYEASREELSEsgilD 379
Cdd:COG4624  219 ITSCCPAWVKLIEKYYPELLPNLSPCKSPMQAFGALIKTYYAPDI--------KVVFIGPCIAKKFEAKRPEMKG----D 286

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335 380 VDLSITTRELAKMIKEAAIDLPNLQDQDFDNPlgkSTGAASIFGASGGVLEAALRTSYEKITnktldnvnftnvrglkgi 459
Cdd:COG4624  287 VDYVLTFRELARMIKEAGIDLANLEEEEFDNE---SSGAGRIFGVTGGVMEAALRTAYELLP------------------ 345

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335 460 reasidvDGTTVNVCIVNTLKNARKIMDKVRSGECKYHIIEVMACPGGCVGGAGQPYHHGNTEIVDRRAnALYEidRNKA 539
Cdd:COG4624  346 -------DGLELKVAVVSGLKNCRKLLEEIKAGKIDYHFIEVMACPGGCIGGPGQPIPPGSLEKRRKRV-ALYA--KEAP 415

                        490       500       510
                 ....*....|....*....|....*....|....
gi 489524335 540 IRKSHENPDLQAIYKDFFGEPNSDVAHKYLHTHY 573
Cdd:COG4624  416 IRKSHENPEILDLYREFLGKPLSEKAHELLHTHY 449
Fe_hyd_lg_C pfam02906
Iron only hydrogenase large subunit, C-terminal domain;
227-512 2.74e-161

Iron only hydrogenase large subunit, C-terminal domain;


Pssm-ID: 397172  Cd Length: 277  Bit Score: 461.70  E-value: 2.74e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335  227 KTIVVQVAPAVRVAIGEEFGLEPgSISTGKMVAALKALGFEHVFDTNFGADFTIMEEATEFIERIQKGENLPILTSCCPA 306
Cdd:pfam02906   1 KKVVAQIAPAVRGAFGEEFGLPP-TVTTGKLVAALRKLGFDYVFDTAFGADLTIMEEATEFLERLEKGKKLPMFTSCCPG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335  307 WVNFLEHNYPDKLNLASSCKSPQGMFGSIAKNYYAPKilginpEELYVVSVMPCVAKKYEASREELSesGILDVDLSITT 386
Cdd:pfam02906  80 WVKYVEKYYPELLPNLSTCKSPMQMFGALIKTYYAED------LKIYVVSIMPCTAKKFEAARPEMK--GDRDVDAVLTT 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335  387 RELAKMIKEAAIDLPNLQDQDFDNPLGKSTGAASIFGASGGVLEAALRTSYEKITNKTLDNVNFTNVRGLKGIREASIDV 466
Cdd:pfam02906 152 RELAAMIKEAGIDFAKLEDEEFDNPLGESSGAGRIFGVTGGVMEAALRTAYELLTGKELPAIEFKEVRGLEGIKEATVEI 231

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 489524335  467 DGTTVNVCIVNTLKNARKIMDKVRSGECKYHIIEVMACPGGCVGGA 512
Cdd:pfam02906 232 GGTTVKVAVVSGLKNARKLLEKIKAGELKYHFIEVMACPGGCIGGG 277
NuoG COG1034
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ...
 3-210 1.63e-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: 210.47  E-value: 1.63e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335   3 LVNLTINGKHVSAPSGTSILDAAKLINIKIHNLCHLhmneiDKLDTCASCRVCMVETE--RGLVPACGTVIKEGMKVQTN 80
Cdd:COG1034    1 MVTITIDGKEVEVPKGTTVLQAAEKAGIEIPRFCYH-----PKLSIAGACRMCLVEVEgaPKPVASCATPVTDGMVVKTD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335  81 SAKALNARRTIVELLLSDHPQDCFVCEKNGDCELQTIAADLGVRKIRYQGSK-SFAGKDTStkSLVK-DHSKCILCRRCE 158
Cdd:COG1034   76 SPKVKKARKGVMEFLLINHPLDCPICDQGGECDLQDQAMEYGVDESRYEEEKrTVPKKDLG--PLILlDMNRCILCTRCV 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489524335 159 TVCNDIQTVGALSGVNRGFNTLVSTFFNSDMvetECTFCGQCISVCPTGALT 210
Cdd:COG1034  154 RFCDEIAGDPELGVIGRGEHSEIGTYLGKPL---DSEFSGNCIDVCPVGALT 202
FeFe_hydrog_B1 TIGR04105
[FeFe] hydrogenase, group B1/B3; See for descriptions of different groups.
 147-513 1.54e-59

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


Pssm-ID: 274983 [Multi-domain]  Cd Length: 462  Bit Score: 205.52  E-value: 1.54e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335  147 DHSKCILCRRCETVCndiqTVGALSGVNR------GFNTLVSTFFNSDMV-ETECTFCGQCISVCPTGALTEVDNVPKLW 219
Cdd:TIGR04105 140 DQEKCIECGKCKKAC----PYNAIVEIERpcekacPVGAISSDEDGRAVIdYDKCISCGACMVACPFGAISDKSQIVQVI 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335  220 DVLNKKEKTIVVqVAPAVrvaIGEeFGLEpgsISTGKMVAALKALGFEHVFDTNFGADFTIMEEATEFIERIQKGENLpI 299
Cdd:TIGR04105 216 KALKSGKKVYAM-VAPAI---VGQ-FGPK---ATPGQVKTALKKLGFADVVEVALGADMVAVHEAEEFAERVEEGKKF-M 286

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335  300 LTSCCPAWVNFLEHNYPDKLNLASSCKSPQGMFGSIAKNYYapkilginpEELYVVSVMPCVAKKYEASREELSEsgilD 379
Cdd:TIGR04105 287 TTSCCPAFVNMIKKHFPELAENISTTVSPMVATARYIKKKD---------PDAKVVFIGPCIAKKLEAQRDEVKG----D 353

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335  380 VDLSITTRELAKMIKEAAIDLPNLQDQDFDNplgkSTGAASIFGASGGVLEAALRTsyekitnktldnvnftnvrglkgI 459
Cdd:TIGR04105 354 VDYVLTFEELAAMFDAKGIDLEECEEEDLDD----ASAFGRGFAVSGGVAAAVKAA-----------------------I 406

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 489524335  460 REASIDVDgttVNVCIVNTLKNARKIMDKVRSGECKYHIIEVMACPGGCVGGAG 513
Cdd:TIGR04105 407 KEKGPDVE---VKPVKCNGLDECKKALTLAKAGKLPGNFIEGMACEGGCVGGPG 457
PRK07569 PRK07569
bidirectional hydrogenase complex protein HoxU; Validated
 1-209 1.22e-53

bidirectional hydrogenase complex protein HoxU; Validated


Pssm-ID: 181037 [Multi-domain]  Cd Length: 234  Bit Score: 182.54  E-value: 1.22e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335   1 MSLVNLTINGKHVSAPSGTSILDAAKLINIKIHNLCHLhmneiDKLDTCASCRVCMVETE--RGLVPACGTVIKEGMKVQ 78
Cdd:PRK07569   1 MSVKTLTIDDQLVSAREGETLLEAAREAGIPIPTLCHL-----DGLSDVGACRLCLVEIEgsNKLLPACVTPVAEGMVVQ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335  79 TNSAKALNARRTIVELLLSDHPQDCFVCEKNGDCELQTIAADLGVRKIRYQGSKSFAGKDTSTKSLVKDHSKCILCRRCE 158
Cdd:PRK07569  76 TNTPRLQEYRRMIVELLFAEGNHVCAVCVANGNCELQDLAIEVGMDHVRFPYLFPRRPVDISHPRFGIDHNRCVLCTRCV 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489524335 159 TVCNDIQTVGALSGVNRGFNTLVSTFFNSDMVETE-CTFCGQCISVCPTGAL 209
Cdd:PRK07569 156 RVCDEIEGAHTWDVAGRGAKSRVITDLNQPWGTSEtCTSCGKCVQACPTGAI 207
PRK08493 PRK08493
NADH-quinone oxidoreductase subunit G;
3-213 6.21e-41

NADH-quinone oxidoreductase subunit G;


Pssm-ID: 236277 [Multi-domain]  Cd Length: 819  Bit Score: 158.71  E-value: 6.21e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335   3 LVNLTINGKHVSAPSGTSILDAAKLINIKIHNLCHLhmneiDKLDTCASCRVCMVETERGLVPACGTVIKEGMKVQTNSA 82
Cdd:PRK08493   1 MITITINGKECEAQEGEYILNVARRNGIFIPAICYL-----SGCSPTLACRLCMVEADGKRVYSCNTKAKEGMNILTNTP 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335  83 KALNARRTIVELLLSDHPQDCFVCEKNGDCELQTIAADLGVrkiryqGSKSFAGKDT--STKS---LVKDHSKCILCRRC 157
Cdd:PRK08493  76 NLMDERNAIMQTYDVNHPLECGVCDKSGECELQNFTHEMGV------NHQPYAIKDThkPHKHwgkINYDPSLCIVCERC 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489524335 158 ETVCNDIQTVGALSGVNRGFNTLVSTF--------------FNSDMVE------TECTFCGQCISVCPTGALTEVD 213
Cdd:PRK08493 150 VTVCKDKIGESALKTVPRGLDAPDKSFkesmpkdayavwskKQKSLIGpvggetLDCSFCGECIAVCPVGALSSSD 225
PRK07860 PRK07860
NADH dehydrogenase subunit G; Validated
 3-210 4.40e-29

NADH dehydrogenase subunit G; Validated


Pssm-ID: 236118 [Multi-domain]  Cd Length: 797  Bit Score: 122.75  E-value: 4.40e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335   3 LVNLTINGKHVSAPSGTSILDAAKLINIKIHNLC-H-LhmneidkLDTCASCRVCMVETE--RGLVPACGTVIKEGMKVQ 78
Cdd:PRK07860   4 LVTLTIDGVEVSVPKGTLVIRAAELLGIQIPRFCdHpL-------LDPVGACRQCLVEVEgqRKPQASCTTTVTDGMVVK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335  79 T--NSAKALNARRTIVELLLSDHPQDCFVCEKNGDCELQTIAADLGVRKIRYQGSKSFAGKDT--STKSLVkDHSKCILC 154
Cdd:PRK07860  77 TqlTSPVADKAQHGVMELLLINHPLDCPVCDKGGECPLQNQAMSNGRAESRFTDVKRTFPKPIniSTQVLL-DRERCVLC 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489524335 155 RRCETVCNDI--------QTVGALSGVNRGFNTLvstfFNSdmvetecTFCGQCISVCPTGALT 210
Cdd:PRK07860 156 ARCTRFSDQIagdpfidlQERGALQQVGIYEGEP----FQS-------YFSGNTVQICPVGALT 208
Fe_hyd_SSU pfam02256
Iron hydrogenase small subunit; This family represents the small subunit of the Fe-only ...
 522-576 1.90e-26

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: 101.81  E-value: 1.90e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 489524335  522 EIVDRRANALYEIDRNKAIRKSHENPDLQAIYKDFFGEPNSDVAHKYLHTHYFDK 576
Cdd:pfam02256   2 DIRKKRAEALYKIDKNKPLRKSHENPAVKKLYEEFLGEPLSHKAHELLHTHYTPR 56
Fe_hyd_SSU smart00902
Iron hydrogenase small subunit; Many microorganisms, such as methanogenic, acetogenic, ...
 526-577 5.01e-23

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: 91.93  E-value: 5.01e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 489524335   526 RRANALYEIDRNKAIRKSHENPDLQAIYKDFFGEPNSDVAHKYLHTHYFDKS 577
Cdd:smart00902   1 QRAEALYNIDKSLPLRKSHENPAVKKLYEEFLGGPLSHKAHELLHTHYHDRE 52
PTZ00305 PTZ00305
NADH:ubiquinone oxidoreductase; Provisional
 16-209 1.23e-20

NADH:ubiquinone oxidoreductase; Provisional


Pssm-ID: 140326 [Multi-domain]  Cd Length: 297  Bit Score: 92.79  E-value: 1.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335  16 PSGTSILDAAKLINIKIHNLCHLHMneidkLDTCASCRVCMVETE--RGLVPACGTVIKEGMKVQTNSAKALNARRTIVE 93
Cdd:PTZ00305  82 PQEENLLEVLEREGIRVPKFCYHPI-----LSVAGNCRMCLVQVDgtQNLVVSCATVALPGMSIITDSRLVRDAREGNVE 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335  94 LLLSDHPQDCFVCEKNGDCELQTIAADLGVRKIRYQGSKSFAGK---DTSTKSLVkdhSKCILCRRCETVCNDIQTVGAL 170
Cdd:PTZ00305 157 LILINHPNDCPICEQATNCDLQNVSMNYGTDIPRYKEDKRAVQDfyfDPQTRVVL---NRCIHCTRCVRFLNEHAQDFNL 233

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 489524335 171 SGVNRGFNTLVSTFFNSDMVETECTFcgQCISVCPTGAL 209
Cdd:PTZ00305 234 GMIGRGGLSEISTFLDELEVKTDNNM--PVSQLCPVGKL 270
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
 1-114 1.46e-19

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 92.48  E-value: 1.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335   1 MSLVNLTINGKHVSAPSGTSILDAAKLINIKIHNLCHLhmneiDKLDTCASCRVCMVETeRG---LVPACGTVIKEGMKV 77
Cdd:PRK12814   1 MNTISLTINGRSVTAAPGTSILEAAASAGITIPTLCFH-----QELEATGSCWMCIVEI-KGknrFVPACSTAVSEGMVI 74

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489524335  78 QTNSAKALNARRTIVELLLSDHPQDCfvcekNGDCEL 114
Cdd:PRK12814  75 ETENAELHAMRRQSLERLIEQHCGDC-----LGPCEL 106
NADH-G_4Fe-4S_3 pfam10588
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
88-127 1.30e-18

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


Pssm-ID: 463159 [Multi-domain]  Cd Length: 40  Bit Score: 79.03  E-value: 1.30e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 489524335   88 RRTIVELLLSDHPQDCFVCEKNGDCELQTIAADLGVRKIR 127
Cdd:pfam10588   1 RKTILELLLSNHPLDCPTCDKNGNCELQDLAYELGVDEVR 40
NADH-G_4Fe-4S_3 smart00929
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
88-128 3.80e-18

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


Pssm-ID: 214918 [Multi-domain]  Cd Length: 41  Bit Score: 78.01  E-value: 3.80e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 489524335    88 RRTIVELLLSDHPQDCFVCEKNGDCELQTIAADLGVRKIRY 128
Cdd:smart00929   1 RKTILELLLANHPLDCPVCDKNGECELQDLAYELGVDEQRY 41
Fer2_4 pfam13510
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 4-81 9.55e-15

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: 69.49  E-value: 9.55e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489524335    4 VNLTINGKHVSAPSGTSILDAAKLINIKIHNLCHLHMNEiDKLDTCASCRVCMVETE-RGLVPACGTVIKEGMKVQTNS 81
Cdd:pfam13510   4 VTFTFDGRPVTAPEGDTIAAALLANGVRVPRSCKYGRPR-GIFCAMGECRNCLVEVDgVPNVRACTTPVREGMVVRTQN 81
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 147-219 1.23e-07

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 48.96  E-value: 1.23e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489524335 147 DHSKCILCRRCETVCNdiqtVGALSgVNRGFNTLVStffnsdmvETECTFCGQCISVCPTGALTEVDNVPKLW 219
Cdd:COG1149    9 DEEKCIGCGLCVEVCP----EGAIK-LDDGGAPVVD--------PDLCTGCGACVGVCPTGAITLEEREAGKI 68
NapF COG1145
Ferredoxin [Energy production and conversion];
145-210 4.12e-07

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 51.65  E-value: 4.12e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489524335 145 VKDHSKCILCRRCETVCndiqTVGALSGVNRGFNTLVStffnsdmvETECTFCGQCISVCPTGALT 210
Cdd:COG1145  178 VIDAEKCIGCGLCVKVC----PTGAIRLKDGKPQIVVD--------PDKCIGCGACVKVCPVGAIS 231
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 150-210 4.64e-07

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: 47.05  E-value: 4.64e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489524335 150 KCILCRRCETVCndiqTVGALSGVNRGFNTLVstffnsDMVETECTFCGQCISVCPTGALT 210
Cdd:COG1143    3 KCIGCGLCVRVC----PVDAITIEDGEPGKVY------VIDPDKCIGCGLCVEVCPTGAIS 53
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
140-214 6.66e-07

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 47.03  E-value: 6.66e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489524335 140 STKSLVKDHSKCILCRRCETVCNdiqtVGALSGVNRGFntlvstFFNSDmvetECTFCGQCISVCPTGALTEVDN 214
Cdd:COG2768    2 SLGKPYVDEEKCIGCGACVKVCP----VGAISIEDGKA------VIDPE----KCIGCGACIEVCPVGAIKIEWE 62
PRK14028 PRK14028
pyruvate ferredoxin oxidoreductase subunit gamma/delta; Provisional
 145-215 1.28e-06

pyruvate ferredoxin oxidoreductase subunit gamma/delta; Provisional


Pssm-ID: 172522 [Multi-domain]  Cd Length: 312  Bit Score: 50.77  E-value: 1.28e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489524335 145 VKDHSKCILCRRCETVCNDIQTVGALSGVN--RGfntlvsTFFNSDMVETE---CTFCGQCISVCPTGALTEVDNV 215
Cdd:PRK14028 243 VIDHSKCIMCRKCWLYCPDDAIIEAWREAEgpRG------RKFRMKMIDFDyqyCKGCGVCAEVCPTGAIQMVREI 312
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 151-208 2.11e-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: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 44.82  E-value: 2.11e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 489524335  151 CILCRRCETVCNDIQTVGALSGVNRGFNTLVstffnsdMVETECTFCGQCISVCPTGA 208
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEKKGTKTVV-------IDPERCVGCGACVAVCPTGA 51
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 147-219 3.94e-06

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 44.70  E-value: 3.94e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489524335 147 DHSKCILCRRCETVCndiqTVGALSGVNRGFNTLVStffnsdmVETECTFCGQCISVCPTGALTEVDNVPKLW 219
Cdd:COG1146    6 DTDKCIGCGACVEVC----PVDVLELDEEGKKALVI-------NPEECIGCGACELVCPVGAITVEDDEPEEQ 67
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 147-210 5.20e-06

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 44.27  E-value: 5.20e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489524335 147 DHSKCILCRRCETVCNdiqtVGALSGVNrgfNTLVstffnsdMVETECTFCGQCISVCPTGALT 210
Cdd:COG2221   13 DEEKCIGCGLCVAVCP----TGAISLDD---GKLV-------IDEEKCIGCGACIRVCPTGAIK 62
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 144-210 6.91e-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: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 45.65  E-value: 6.91e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489524335 144 LVKDHSKCILCRRCETVCndiqtvgalSGVNRG-FN------TLVSTFFNSDMVETECTFCGQ--CISVCPTGALT 210
Cdd:cd10550    1 LVVDPEKCTGCRTCELAC---------SLKHEGvFNpslsriRVVRFEPEGLDVPVVCRQCEDapCVEACPVGAIS 67
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 147-213 7.00e-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: 44.27  E-value: 7.00e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489524335 147 DHSKCILCRRCETVCNDiqtvGALSGVNRGFntlvsTFFNSDMveteCTFCGQCISVCPTGALTEVD 213
Cdd:COG1144   28 DEDKCIGCGLCWIVCPD----GAIRVDDGKY-----YGIDYDY----CKGCGICAEVCPVKAIEMVP 81
PRK08348 PRK08348
NADH-plastoquinone oxidoreductase subunit; Provisional
 144-209 1.29e-05

NADH-plastoquinone oxidoreductase subunit; Provisional


Pssm-ID: 181399 [Multi-domain]  Cd Length: 120  Bit Score: 44.83  E-value: 1.29e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489524335 144 LVKDHSKCILCRRCETVC--NDIQTVGALSGVNrgfntlvstffnsdMVETECTFCGQCISVCPTGAL 209
Cdd:PRK08348  37 ILYDVDKCVGCRMCVTVCpaGVFVYLPEIRKVA--------------LWTGRCVFCGQCVDVCPTGAL 90
Fer4_9 pfam13187
4Fe-4S dicluster domain;
150-209 1.38e-05

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 42.54  E-value: 1.38e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335  150 KCILCRRCETVCNdiqtvgalSGVNRGFNtlVSTFFNSDMVETECTFCGQCISVCPTGAL 209
Cdd:pfam13187   1 KCTGCGACVAACP--------AGAIVPDL--VGQTIRGDIAGLACIGCGACVDACPRGAI 50
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
150-214 2.15e-05

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 44.87  E-value: 2.15e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489524335 150 KCILCRRCETVC--NDIQtvgaLSGVNRGFNTLVSTFFNSDMveTECTFCGQCISVCPTGALTEVDN 214
Cdd:PRK05888  59 RCIACKLCAAICpaDAIT----IEAAEREDGRRRTTRYDINF--GRCIFCGFCEEACPTDAIVETPD 119
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 151-221 2.33e-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: 44.54  E-value: 2.33e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489524335 151 CILCRRCETVC-NDIQTVGAlsgvnRGFNTLvstffnsDMVETECTFCGQCISVCPTGALTevDNVPKLWDV 221
Cdd:cd10564   15 CTRCGDCVEACpEGIIVRGD-----GGFPEL-------DFSRGECTFCGACAEACPEGALD--PAREAPWPL 72
NuoI TIGR01971
NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of ...
 150-211 3.79e-05

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: 43.56  E-value: 3.79e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489524335  150 KCILCRRCETVC--NDIQTVGALSGVNRGFntlvSTFFNSDMveTECTFCGQCISVCPTGALTE 211
Cdd:TIGR01971  44 KCIGCTLCAAVCpaDAIRVVPAEGEDGKRR----LKFYEINF--GRCIFCGLCEEACPTDAIVL 101
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 144-210 4.20e-05

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: 43.54  E-value: 4.20e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489524335 144 LVKDHSKCILCRRCETVCndiqTVGALSgvnrgFNTLVSTFFNSDMVETECTFCGQCISVCPTGALT 210
Cdd:cd10549    1 LKYDPEKCIGCGICVKAC----PTDAIE-----LGPNGAIARGPEIDEDKCVFCGACVEVCPTGAIE 58
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 147-267 5.73e-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: 5.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335 147 DHSKCILCRRCETVCNdiqtvgalsgvnrgFNTLVSTFFNSDMVETECTFCGQCISVCPTGALTEVDNVPKLWDVLNKKE 226
Cdd:cd03110   62 DQEKCIRCGNCERVCK--------------FGAILEFFQKLIVDESLCEGCGACVIICPRGAIYLKDRDTGKIFISSSDG 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489524335 227 KTIVVQvapavRVAIGEEfglepgsiSTGKMVAALKALGFE 267
Cdd:cd03110  128 GPLVHG-----RLNIGEE--------NSGKLVTELRKKALE 155
napH PRK09477
quinol dehydrogenase membrane component; Provisional
 142-210 6.44e-05

quinol dehydrogenase membrane component; Provisional


Pssm-ID: 236535 [Multi-domain]  Cd Length: 271  Bit Score: 44.89  E-value: 6.44e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489524335 142 KSLVK----DHSKCILCRRCETVCNDIQTV-GALSGVNRGFNTLvstffnsdmvETECTFCGQCISVCPTGALT 210
Cdd:PRK09477 197 KSLIRvkahDRQKCTRCMDCFHVCPEPQVLrPPLKGKQSPSQVT----------SGDCITCGRCIDVCSEDVFN 260
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 141-209 1.35e-04

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: 42.00  E-value: 1.35e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489524335 141 TKSLVKDHSKCILCRRCETVCndiqTVGALSgVNRGFNTLVSTFFnsdmveteCTFCGQCISVCPTGAL 209
Cdd:cd10549   70 EKEAEIDEEKCIGCGLCVKVC----PVDAIT-LEDELEIVIDKEK--------CIGCGICAEVCPVNAI 125
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 144-213 1.68e-04

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: 41.99  E-value: 1.68e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489524335 144 LVKDHSKCILCRRCETVC---NDIQTVGALSGVNRgfntLVSTFFNSDMVETECTFCGQ--CISVCPTGALTEVD 213
Cdd:cd04410    1 LVVDLDRCIGCGTCEVACkqeHGLRPGPDWSRIKV----IEGGGLERAFLPVSCMHCEDppCVKACPTGAIYKDE 71
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 149-213 2.39e-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: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 41.86  E-value: 2.39e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489524335 149 SKCILCRRCETVC--NDIQtvgaLSGVNRGFNTLVSTFFNSDmvETECTFCG-QCISVCPTGALTEVD 213
Cdd:cd16373   14 ALCIRCGLCVEACptGVIQ----PAGLEDGLEGGRTPYLDPR--EGPCDLCCdACVEVCPTGALRPLD 75
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 142-211 2.41e-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: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 41.17  E-value: 2.41e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335 142 KSLVKDHSKCILCRRCETVCNDIQtvgaLSGVNRGFNTLVSTFFNSDMVETECTFCGQCISVCPTGALTE 211
Cdd:cd16372    1 KLLVTDPEKCIGCLQCEEACSKTF----FKEEDREKSCIRITETEGGYAINVCNQCGECIDVCPTGAITR 66
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 142-214 3.11e-04

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: 40.84  E-value: 3.11e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489524335 142 KSLVKDHSKCILCRRCETVCndiqTVGALSGVNRGFNTLVSTffNSDMV-ETECTFCGQCISVCPTGALTEVDN 214
Cdd:cd10549   33 RGPEIDEDKCVFCGACVEVC----PTGAIELTPEGKEYVPKE--KEAEIdEEKCIGCGLCVKVCPVDAITLEDE 100
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 144-205 3.39e-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: 38.77  E-value: 3.39e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489524335  144 LVKDHSKCILCRRCETVC-NDIQTVGALSGVNRGFNTLVSTFfnsdmvetECTFCGQCISVCP 205
Cdd:pfam13237   2 VVIDPDKCIGCGRCTAACpAGLTRVGAIVERLEGEAVRIGVW--------KCIGCGACVEACP 56
PRK09898 PRK09898
ferredoxin-like protein;
147-209 5.18e-04

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 41.75  E-value: 5.18e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489524335 147 DHSKCILCRRCETVCNdiqtvgalsgvnrgfnTLVSTFFNSDMVETECTFCGQCISVCPTGAL 209
Cdd:PRK09898 152 DHKRCIGCSACTTACP----------------WMMATVNTESKKSSKCVLCGECANACPTGAL 198
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 142-210 8.75e-04

Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion];


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 40.70  E-value: 8.75e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489524335 142 KSLVKDHSKCILCRRCETVCNDIQTVGAlsGVNRgfnTLVSTFFNSDMVETECTF----CGQ-----CISVCPTGALT 210
Cdd:COG0437    6 YGMVIDLTKCIGCRACVVACKEENNLPV--GVTW---RRVRRYEEGEFPNVEWLFvpvlCNHcddppCVKVCPTGATY 78
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 147-217 1.22e-03

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 37.71  E-value: 1.22e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489524335 147 DHSKCILCRRCETVCndiqTVGALSGVNRgfntlvSTFFNsdmvETECTFCGQCISVCPTGALTEVDNVPK 217
Cdd:COG4231   20 DEDKCTGCGACVKVC----PADAIEEGDG------KAVID----PDLCIGCGSCVQVCPVDAIKLEKRVPE 76
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 152-210 1.60e-03

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: 39.15  E-value: 1.60e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489524335 152 ILCRRCETVCNdiqtVGALSgvnrgFNTLVSTFFNSDMVETECTFCGQCISVCPTGALT 210
Cdd:cd10564   86 VECRSCQDACP----TQAIR-----FRPRLGGIALPELDADACTGCGACVSVCPVGAIT 135
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 4-78 1.96e-03

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: 37.37  E-value: 1.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335   4 VNLTINGKHVSAPSGTSILDAAKLINIKIHNLCHlhmneidkldtCASCRVCMVE------------------TERGLVP 65
Cdd:cd00207    3 INVPGSGVEVEVPEGETLLDAAREAGIDIPYSCR-----------AGACGTCKVEvvegevdqsdpslldeeeAEGGYVL 71

                         90
                 ....*....|...
gi 489524335  66 ACGTVIKEGMKVQ 78
Cdd:cd00207   72 ACQTRVTDGLVIE 84
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
141-218 1.99e-03

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 38.87  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335 141 TKSLVKDHSKCILCRRCETVCNDIQTvGALSGVNRGFNTLVSTffNSDMVETECTFCGQ--CISVCPTGALTEVDNVPKL 218
Cdd:COG1142    2 NKFIIADPEKCIGCRTCEAACAVAHE-GEEGEPFLPRIRVVRK--AGVSAPVQCRHCEDapCAEVCPVGAITRDDGAVVV 78
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
147-210 2.08e-03

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 41.00  E-value: 2.08e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489524335 147 DHSKCILCRRCETVCndiqTVGALSGVNRGfntlvstffNSDMVETECTFCGQCISVCPTGALT 210
Cdd:COG1148  494 DPEKCTGCGRCVEVC----PYGAISIDEKG---------VAEVNPALCKGCGTCAAACPSGAIS 544
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 151-234 2.13e-03

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: 40.36  E-value: 2.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335 151 CILCRRCETVCndiqTVGALSGVNRGFNTLVstffnsdmvETECTFCGQCISVCPTGALTEVDNVPKLWdVLNKKEKTIV 230
Cdd:COG2878  139 CIGCGDCIKAC----PFDAIVGAAKGMHTVD---------EDKCTGCGLCVEACPVDCIEMVPVSPTVV-VSSWDKGKAV 204


                 ....
gi 489524335 231 VQVA 234
Cdd:COG2878  205 RKVV 208
PRK08318 PRK08318
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
147-212 2.55e-03

NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;


Pssm-ID: 236237 [Multi-domain]  Cd Length: 420  Bit Score: 40.70  E-value: 2.55e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489524335 147 DHSKCILCRRCETVCNDI--QTVGALSGVNRGFNTlvstffnsdmVETECTFCGQCISVCPT-GALTEV 212
Cdd:PRK08318 340 DQDKCIGCGRCYIACEDTshQAIEWDEDGTRTPEV----------IEEECVGCNLCAHVCPVeGCITMG 398
Fer4_21 pfam14697
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 147-206 2.67e-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: 434137 [Multi-domain]  Cd Length: 59  Bit Score: 36.49  E-value: 2.67e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335  147 DHSKCILCRRCETVCNDiQTVGALSGVNRGFNTLVstffnsdmvETECTFCGQCISVCPT 206
Cdd:pfam14697   4 DEDTCIGCGKCYIACPD-TSHQAIVGDGKRHHTVI---------EDECTGCNLCVSVCPV 53
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 194-220 3.05e-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: 3.05e-03
                         10        20
                 ....*....|....*....|....*..
gi 489524335 194 CTFCGQCISVCPTGALTEVDNVPKLWD 220
Cdd:COG1149   13 CIGCGLCVEVCPEGAIKLDDGGAPVVD 39
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 191-220 3.08e-03

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 36.57  E-value: 3.08e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 489524335 191 ETECTFCGQCISVCPTGALTEVDNVPKLWD 220
Cdd:COG2221   14 EEKCIGCGLCVAVCPTGAISLDDGKLVIDE 43
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
190-219 4.37e-03

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 36.25  E-value: 4.37e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 489524335 190 VETECTFCGQCISVCPTGALTEVDNVPKLW 219
Cdd:COG2768    9 DEEKCIGCGACVKVCPVGAISIEDGKAVID 38
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 191-210 5.46e-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: 34.53  E-value: 5.46e-03
                          10        20
                  ....*....|....*....|
gi 489524335  191 ETECTFCGQCISVCPTGALT 210
Cdd:pfam00037   5 EEKCIGCGACVEVCPVGAIT 24
NapF COG1145
Ferredoxin [Energy production and conversion];
194-219 5.82e-03

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 38.94  E-value: 5.82e-03
                         10        20
                 ....*....|....*....|....*.
gi 489524335 194 CTFCGQCISVCPTGALTEVDNVPKLW 219
Cdd:COG1145  184 CIGCGLCVKVCPTGAIRLKDGKPQIV 209
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 106-210 7.65e-03

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: 37.47  E-value: 7.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524335  106 CEKNGDCELQTIAADLGVrKIRYQGSKSFAGKDTSTKSLVKDHSKCILCRRCETVCndiqTVGALSGVNRGFNTLVstff 185
Cdd:TIGR01944  71 CPPGGEAVILALAELLGV-EPIPQPLDADAGTIQPPMVALIDEDNCIGCTKCIQAC----PVDAIVGAAKAMHTVI---- 141

                          90       100
                  ....*....|....*....|....*
gi 489524335  186 nsdmvETECTFCGQCISVCPTGALT 210
Cdd:TIGR01944 142 -----ADECTGCDLCVEPCPTDCIE 161
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
147-213 9.14e-03

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 36.94  E-value: 9.14e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489524335 147 DHSKCILCRRCETVCndiqTVGALSGVNRGFNTLVStffnsdmvetECTFCG------QCISVCPTGALTEVD 213
Cdd:COG1142   79 DEEKCIGCGLCVLAC----PFGAITMVGEKSRAVAV----------KCDLCGgreggpACVEACPTGALRLVD 137
 
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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