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Database: UniProt
Entry: F2JJA1_CELLD
LinkDB: F2JJA1_CELLD
Original site: F2JJA1_CELLD 
ID   F2JJA1_CELLD            Unreviewed;       329 AA.
AC   F2JJA1;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=4Fe-4S ferredoxin-type domain-containing protein {ECO:0000259|PROSITE:PS51379};
GN   OrderedLocusNames=Clole_2693 {ECO:0000313|EMBL:ADZ84394.1};
OS   Cellulosilyticum lentocellum (strain ATCC 49066 / DSM 5427 / NCIMB 11756 /
OS   RHM5) (Clostridium lentocellum).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Cellulosilyticaceae;
OC   Cellulosilyticum.
OX   NCBI_TaxID=642492 {ECO:0000313|EMBL:ADZ84394.1, ECO:0000313|Proteomes:UP000008467};
RN   [1] {ECO:0000313|EMBL:ADZ84394.1, ECO:0000313|Proteomes:UP000008467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49066 / DSM 5427 / NCIMB 11756 / RHM5
RC   {ECO:0000313|Proteomes:UP000008467};
RX   PubMed=21398547; DOI=10.1128/JB.00239-11;
RG   US DOE Joint Genome Institute;
RA   Miller D.A., Suen G., Bruce D., Copeland A., Cheng J.F., Detter C.,
RA   Goodwin L.A., Han C.S., Hauser L.J., Land M.L., Lapidus A., Lucas S.,
RA   Meincke L., Pitluck S., Tapia R., Teshima H., Woyke T., Fox B.G.,
RA   Angert E.R., Currie C.R.;
RT   "Complete genome sequence of the cellulose-degrading bacterium
RT   Cellulosilyticum lentocellum.";
RL   J. Bacteriol. 193:2357-2358(2011).
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DR   EMBL; CP002582; ADZ84394.1; -; Genomic_DNA.
DR   RefSeq; WP_013657687.1; NC_015275.1.
DR   AlphaFoldDB; F2JJA1; -.
DR   STRING; 642492.Clole_2693; -.
DR   KEGG; cle:Clole_2693; -.
DR   eggNOG; COG1600; Bacteria.
DR   HOGENOM; CLU_030790_2_1_9; -.
DR   Proteomes; UP000008467; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR004453; QueG.
DR   InterPro; IPR013542; QueG_DUF1730.
DR   NCBIfam; TIGR00276; tRNA epoxyqueuosine(34) reductase QueG; 1.
DR   PANTHER; PTHR30002; EPOXYQUEUOSINE REDUCTASE; 1.
DR   PANTHER; PTHR30002:SF4; EPOXYQUEUOSINE REDUCTASE; 1.
DR   Pfam; PF13484; Fer4_16; 1.
DR   Pfam; PF08331; QueG_DUF1730; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   4: Predicted;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Queuosine biosynthesis {ECO:0000256|ARBA:ARBA00022785};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008467};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          175..204
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   329 AA;  38192 MW;  8FCE8A9461509007 CRC64;
     MMLKKRIEDF CKSIGLDTIG FIPCRRFDEL EVFYRERQKL GLQNEFEEQN IEKRLNPNLY
     MKEGKTIISI AFPYYHREIK DEVANGFSIY TKRLDYHRVV KKYLNEISEY IETLGGKALG
     FVDSNALPER YIAYLAGLGF IGRNNMLITK KYGSYVFLGE LMTDLKIECE DQRSQDELIK
     YAECGACKAC LKECPTKSIN MSRSNPNICL SYITQKKELS DQEIKLLKGN IFGCDFCQLK
     CPYNEEVATN VLEEFQTLVH MNEPANVYAG MDNSYFKEKM SPTSCGWRGK NVIRRNAIIH
     MDHAGLPIEQ YKGDSPYINN YIERLTQNK
//
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