ID C0D811_9FIRM Unreviewed; 683 AA.
AC C0D811;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE SubName: Full=Rubredoxin {ECO:0000313|EMBL:EEG52537.1};
GN ORFNames=CLOSTASPAR_05409 {ECO:0000313|EMBL:EEG52537.1};
OS [Clostridium] asparagiforme DSM 15981.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Enterocloster.
OX NCBI_TaxID=518636 {ECO:0000313|EMBL:EEG52537.1, ECO:0000313|Proteomes:UP000004756};
RN [1] {ECO:0000313|EMBL:EEG52537.1, ECO:0000313|Proteomes:UP000004756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG52537.1,
RC ECO:0000313|Proteomes:UP000004756};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEG52537.1, ECO:0000313|Proteomes:UP000004756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG52537.1,
RC ECO:0000313|Proteomes:UP000004756};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Clostridium asparagiforme (DSM 15981).";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000256|ARBA:ARBA00001965};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEG52537.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACCJ01000444; EEG52537.1; -; Genomic_DNA.
DR AlphaFoldDB; C0D811; -.
DR HOGENOM; CLU_018240_3_0_9; -.
DR Proteomes; UP000004756; Unassembled WGS sequence.
DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR CDD; cd00729; rubredoxin_SM; 1.
DR CDD; cd01046; Rubrerythrin_like; 1.
DR Gene3D; 1.20.1260.10; -; 1.
DR Gene3D; 2.20.28.10; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.1780; -; 1.
DR Gene3D; 4.10.260.20; Iron hydrogenase, small subunit; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR009016; Fe_hydrogenase.
DR InterPro; IPR004108; Fe_hydrogenase_lsu_C.
DR InterPro; IPR003149; Fe_hydrogenase_ssu.
DR InterPro; IPR036991; Fe_hydrogenase_ssu_sf.
DR InterPro; IPR013352; Fe_hydrogenase_subset.
DR InterPro; IPR012347; Ferritin-like.
DR InterPro; IPR009040; Ferritin-like_diiron.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR045236; RevRr_diiron-bd_dom.
DR InterPro; IPR003251; Rr_diiron-bd_dom.
DR InterPro; IPR024934; Rubredoxin-like_dom.
DR InterPro; IPR048574; RUBY_RBDX.
DR NCBIfam; TIGR02512; FeFe_hydrog_A; 1.
DR PANTHER; PTHR11615:SF345; CATALYTIC SUBUNIT OF IRON-ONLY HYDROGENASE-RELATED; 1.
DR PANTHER; PTHR11615; NITRATE, FORMATE, IRON DEHYDROGENASE; 1.
DR Pfam; PF02906; Fe_hyd_lg_C; 1.
DR Pfam; PF02256; Fe_hyd_SSU; 1.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF02915; Rubrerythrin; 1.
DR Pfam; PF21349; RUBY_RBDX; 1.
DR SMART; SM00902; Fe_hyd_SSU; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF53920; Fe-only hydrogenase; 1.
DR SUPFAM; SSF47240; Ferritin-like; 1.
DR SUPFAM; SSF57802; Rubredoxin-like; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS50905; FERRITIN_LIKE; 1.
DR PROSITE; PS50903; RUBREDOXIN_LIKE; 1.
PE 4: Predicted;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 26..54
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 57..86
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 503..537
FT /note="Rubredoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50903"
FT DOMAIN 553..683
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000259|PROSITE:PS50905"
FT REGION 456..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 683 AA; 74412 MW; BB22F02B8A2556BF CRC64;
MIKGEEKRMS KHLSPEVRVP IERDNVSIFR DEDKCIKCGQ CRDMCRDYIG VLGHYSLEAT
GDRAVCINCG QCANVCPVGS ISEVKEYRQV AEAISDPDKI VIMSTSPSVR AALGEEFGMG
SAFVQGKMVS LLRALGADYV LDTNFAADLT ILEEASELIE RVTKGNKPLP QFTSCCPAWV
KFAEIYYPDM LDHISSAKSP IGMQGPTIKT YFAKKMGIDP RTIVNVAVTP CTAKKYEIRR
EEMSAAGKYL GIEDMRDMDY VITTRELAQW AREAEVDFEA LEDGTYDRLM GEGSGAGVIF
GNTGGVMEAA LRTAYEYITG EKAPQVLYQL EPVRGLEAVK EASLQVGGLT VNVAVIFGTA
NVRSFIRRMK EGGKQYHFVE VMTCPGGCIG GGGQPKDKEF EGDALRARRI ESLYGRDRSM
TVRASHENEE IKELYHEFYG QPLSELAEQM LHTGYEDKSR ELGDPSPAAA GEEKAASSDQ
AGNQSGNAEN ADESNGSTAI PAARRFVCQI CGYVHEGESA PDQCPVCKAG PDKFTEQKAS
MSWAAEHIVG AASGAPEDIL ADLRANFSGE CSEAGMYLAM SRVAFREGYP EIGLYWEQAA
FEEAEHAAKF AELLGEVVTA STKENLTLRV AAENGATAGK ADLAARAKKL GLDAIHDTVH
EMAKDEARHG KAFEGLLQRY FGN
//