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Database: UniProt
Entry: A0A2A5QUN0_9EURY
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Original site: A0A2A5QUN0_9EURY 
ID   A0A2A5QUN0_9EURY        Unreviewed;       358 AA.
AC   A0A2A5QUN0;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN   ORFNames=CP557_08350 {ECO:0000313|EMBL:PCR90525.1};
OS   Natrinema ejinorense.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrinema.
OX   NCBI_TaxID=373386 {ECO:0000313|EMBL:PCR90525.1, ECO:0000313|Proteomes:UP000219689};
RN   [1] {ECO:0000313|EMBL:PCR90525.1, ECO:0000313|Proteomes:UP000219689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 13890 {ECO:0000313|EMBL:PCR90525.1,
RC   ECO:0000313|Proteomes:UP000219689};
RA   Roh S.W., Kim Y.B., Kim J.Y.;
RT   "Genome sequences of Natrinema ejinorence JCM 13890T.";
RL   Submitted (SEP-2017) 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}.
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:PCR90525.1}.
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DR   EMBL; NXNI01000001; PCR90525.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A5QUN0; -.
DR   OrthoDB; 8297at2157; -.
DR   Proteomes; UP000219689; Unassembled WGS sequence.
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; 3.30.300.130; Fe-S cluster assembly (FSCA); 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_02040; Mrp_NBP35; 1.
DR   InterPro; IPR034904; FSCA_dom_sf.
DR   InterPro; IPR002744; MIP18-like.
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; PF01883; FeS_assembly_P; 1.
DR   Pfam; PF10609; ParA; 1.
DR   SUPFAM; SSF117916; Fe-S cluster assembly (FSCA) domain-like; 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|HAMAP-Rule:MF_02040};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_02040}.
FT   DOMAIN          3..65
FT                   /note="MIP18 family-like"
FT                   /evidence="ECO:0000259|Pfam:PF01883"
FT   REGION          304..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          337..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..351
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         101..108
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ   SEQUENCE   358 AA;  37863 MW;  A865750E546D78BF CRC64;
     MDEAAVRDRL RTVEDPELGD DIVSLGLVND ISVDGDEVDI DLALGAPYSP SESDIAAEVR
     EVLTAEGLEP DLTASVPDRD DLTSEEQVLP NVKNVIAVAS GKGGVGKSTV AVNLAAGLSQ
     LGARVGLFDA DVYGPNVPRM VDADEPPMAT EDETLVPPEK YGVKLMSMAF LTGEDDPVIW
     RGPMVHKVIT QLTEDVEWGH LDYLVVDLPP GTGDTQLTML QTMPVTGAVI VTTPQDVALD
     DARKGLEMFA KHDTVVLGIA ENMSTFACPD CGGEHDIFGS GGGEDFAEEH ELPFLGSIPL
     DPAVREGGDG GKPTVLKDGD GTSDALRTIT ENVANNTGIV HRQAISQSRR NEAASPDR
//
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