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Database: UniProt
Entry: D5VQD8_METIM
LinkDB: D5VQD8_METIM
Original site: D5VQD8_METIM 
ID   D5VQD8_METIM            Unreviewed;       281 AA.
AC   D5VQD8;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN   OrderedLocusNames=Metin_0119 {ECO:0000313|EMBL:ADG12791.1};
OS   Methanocaldococcus infernus (strain DSM 11812 / JCM 15783 / ME).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=573063 {ECO:0000313|EMBL:ADG12791.1, ECO:0000313|Proteomes:UP000002061};
RN   [1] {ECO:0000313|EMBL:ADG12791.1, ECO:0000313|Proteomes:UP000002061}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11812 / JCM 15783 / ME {ECO:0000313|Proteomes:UP000002061};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Woyke T.;
RT   "Complete sequence of Methanocaldococcus infernus ME.";
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
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; CP002009; ADG12791.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5VQD8; -.
DR   STRING; 573063.Metin_0119; -.
DR   KEGG; mif:Metin_0119; -.
DR   eggNOG; arCOG00585; Archaea.
DR   HOGENOM; CLU_024839_0_1_2; -.
DR   OrthoDB; 8297at2157; -.
DR   Proteomes; UP000002061; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0140663; F:ATP-dependent FeS chaperone activity; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR   CDD; cd02037; Mrp_NBP35; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_02040; Mrp_NBP35; 1.
DR   InterPro; IPR000808; Mrp-like_CS.
DR   InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR   InterPro; IPR044304; NUBPL-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR033756; YlxH/NBP35.
DR   PANTHER; PTHR42961; IRON-SULFUR PROTEIN NUBPL; 1.
DR   PANTHER; PTHR42961:SF2; IRON-SULFUR PROTEIN NUBPL; 1.
DR   Pfam; PF10609; ParA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS01215; MRP; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_02040}; 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|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_02040};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_02040}.
FT   BINDING         46..53
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ   SEQUENCE   281 AA;  30774 MW;  0EF75ABEB210E38A CRC64;
     MECNGKCDSC KIKDQCPDTK KFFIQQENKI KERMSKIKYK IAILSGKGGV GKSTVSTNLA
     VALAKRGKKV GLLDADIHGP NVPKILGLEG YPEVREGEII PLEKYGVKVI SMANLLPDEK
     TPIIWRGPKV SGAIRQFLAD VNWGELDYLI IDTPPGTGDV QLTIMQSIPL DGAIIVTTPE
     ELSVLDVRKS ISMAKMLKVP ILGIIENMSG FVCPKCGELT YIFGVGGGEK AAKEFGVDFL
     GRIPIDIKAR EAQDKGVPMV LMDCRAKEEF EKIIDKIIEK L
//
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