(data stored in SCRATCH zone)

SWISSPROT: D1YVX1_METPS

ID   D1YVX1_METPS            Unreviewed;       287 AA.
AC   D1YVX1;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   11-DEC-2019, entry version 51.
DE   RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN   OrderedLocusNames=MCP_0521 {ECO:0000313|EMBL:BAI60593.1};
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:BAI60593.1, 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; BAI60593.1; -; Genomic_DNA.
DR   STRING; 304371.MCP_0521; -.
DR   EnsemblBacteria; BAI60593; BAI60593; MCP_0521.
DR   KEGG; mpd:MCP_0521; -.
DR   eggNOG; arCOG00585; Archaea.
DR   eggNOG; COG0489; LUCA.
DR   HOGENOM; HOG000079916; -.
DR   KO; K03593; -.
DR   OMA; SDEHMAV; -.
DR   BioCyc; MPAL304371:GI7G-535-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; D1YVX1.
DR   SWISS-2DPAGE; D1YVX1.
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         53..60
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..28
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   287 AA;  30523 MW;  C759FA12D080E648 CRC64;
     MSSSTKSSAC ESCSSKTSTC SPDSCGNAEK NEQELRIKNN MARIKYRIAI VSGKGGVGKS
     TVTAGLAIAL AKSGYTVGVL DADVSGPNMP HLLGIEDEKM TGDENGFLPV EAPHGIEVAS
     VESIISASDA PVVWRGPMRS SLVNQFLADV QWGQLDFLLV DLPPGTGDEP LSIMQTMPLT
     GLVVVSTPSN LSLLDVSKIV NMAKMLNTRI LGVVENMAYF ECPGCHEKVF PFGEDTVKRL
     CEKYGLDMLG SIPMDASNRG SDVITEGSGI EKYTGDIARK ITGILER
//

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