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Database: UniProt
Entry: C0D811_9FIRM
LinkDB: C0D811_9FIRM
Original site: C0D811_9FIRM 
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}.
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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
//
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