(data stored in SCRATCH zone)

SWISSPROT: D1YV17_METPS

ID   D1YV17_METPS            Unreviewed;       295 AA.
AC   D1YV17;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   11-DEC-2019, entry version 48.
DE   RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN   OrderedLocusNames=MCP_0217 {ECO:0000313|EMBL:BAI60289.1};
OS   Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS   SANAE).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=304371 {ECO:0000313|EMBL:BAI60289.1, ECO:0000313|Proteomes:UP000001882};
RN   [1] {ECO:0000313|Proteomes:UP000001882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE
RC   {ECO:0000313|Proteomes:UP000001882};
RX   PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA   Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA   Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA   Mori K., Fujita N., Imachi H., Takai K.;
RT   "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT   paludicola, the first cultivated representative of the order
RT   Methanocellales.";
RL   PLoS ONE 6:E22898-E22898(2011).
CC   -!- FUNCTION: Binds and transfers iron-sulfur (Fe-S) clusters to target
CC       apoproteins. Can hydrolyze ATP. {ECO:0000256|HAMAP-Rule:MF_02040}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02040}.
CC   -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC       {ECO:0000256|HAMAP-Rule:MF_02040}.
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DR   EMBL; AP011532; BAI60289.1; -; Genomic_DNA.
DR   STRING; 304371.MCP_0217; -.
DR   EnsemblBacteria; BAI60289; BAI60289; MCP_0217.
DR   KEGG; mpd:MCP_0217; -.
DR   eggNOG; arCOG00585; Archaea.
DR   eggNOG; COG0489; LUCA.
DR   HOGENOM; HOG000079916; -.
DR   OMA; NMAYFTP; -.
DR   BioCyc; MPAL304371:GI7G-227-MONOMER; -.
DR   Proteomes; UP000001882; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   HAMAP; MF_02040; Mrp_NBP35; 1.
DR   InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR   InterPro; IPR000808; Mrp_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR033756; YlxH/NBP35.
DR   PANTHER; PTHR23264; PTHR23264; 1.
DR   Pfam; PF10609; ParA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS01215; MRP; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1YV17.
DR   SWISS-2DPAGE; D1YV17.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02040};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_02040};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_02040};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_02040};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_02040};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02040};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001882}.
FT   NP_BIND         58..65
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ   SEQUENCE   295 AA;  31577 MW;  A8D2766159E4CDAE CRC64;
     MSSTNATDEA CNTCKDGKGS SKCDMCPSKG KHGDKPAWDE RIMKRLATIK HRIAIVSGKG
     GVGKSTVTAG LALNLSMMGF KVGVLDADVS GPNMPHLLGL EGKKLMGSEL GIEPVQSRNG
     IKVVSSEMVL TGSDTPMIWR GPMRTTLVNQ FVADVNWGDL DYLLVDLPPG TGDEPLSVMQ
     MMPLDGIIIV STSSNLSTLD VSKIINMAKE LNVTILGVVE NMSYLQCPDC NKKIHLFGES
     KVEKLAKKYG VPLIGEIPLD PQNAGIDELP ADGRSLIVSA LRPIAEKVAH DVEHK
//

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