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Database: UniProt
Entry: S2K7I3_MUCC1
LinkDB: S2K7I3_MUCC1
Original site: S2K7I3_MUCC1 
ID   S2K7I3_MUCC1            Unreviewed;       268 AA.
AC   S2K7I3;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Methionyl-tRNA synthetase {ECO:0000313|EMBL:EPB88225.1};
GN   ORFNames=HMPREF1544_04933 {ECO:0000313|EMBL:EPB88225.1};
OS   Mucor circinelloides f. circinelloides (strain 1006PhL) (Mucormycosis
OS   agent) (Calyptromyces circinelloides).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX   NCBI_TaxID=1220926 {ECO:0000313|EMBL:EPB88225.1, ECO:0000313|Proteomes:UP000014254};
RN   [1] {ECO:0000313|Proteomes:UP000014254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1006PhL {ECO:0000313|Proteomes:UP000014254};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., Earl A., Findley K., Lee S.C., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome sequence of Mucor circinelloides f. circinelloides 1006PhL.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein
CC       assembly (CIA) machinery. Required for maturation of extramitochondrial
CC       Fe-S proteins. The NBP35-CFD1 heterotetramer forms a Fe-S scaffold
CC       complex, mediating the de novo assembly of an Fe-S cluster and its
CC       transfer to target apoproteins. {ECO:0000256|HAMAP-Rule:MF_03039}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_03039}.
CC   -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC       NUBP2/CFD1 subfamily. {ECO:0000256|HAMAP-Rule:MF_03039}.
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DR   EMBL; KE123954; EPB88225.1; -; Genomic_DNA.
DR   AlphaFoldDB; S2K7I3; -.
DR   STRING; 1220926.S2K7I3; -.
DR   VEuPathDB; FungiDB:HMPREF1544_04933; -.
DR   eggNOG; KOG3022; Eukaryota.
DR   InParanoid; S2K7I3; -.
DR   OMA; KTMMIKQ; -.
DR   OrthoDB; 228512at2759; -.
DR   Proteomes; UP000014254; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140663; F:ATP-dependent FeS chaperone activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:UniProtKB-UniRule.
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   HAMAP; MF_03039; NUBP2; 1.
DR   InterPro; IPR000808; Mrp-like_CS.
DR   InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR   InterPro; IPR028600; NUBP2/Cfd1_eukaryotes.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR033756; YlxH/NBP35.
DR   PANTHER; PTHR23264:SF38; CYTOSOLIC FE-S CLUSTER ASSEMBLY FACTOR NUBP2; 1.
DR   PANTHER; PTHR23264; NUCLEOTIDE-BINDING PROTEIN NBP35 YEAST -RELATED; 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   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_03039};
KW   Aminoacyl-tRNA synthetase {ECO:0000313|EMBL:EPB88225.1};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_03039};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03039};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_03039};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_03039};
KW   Ligase {ECO:0000313|EMBL:EPB88225.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_03039};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_03039}; Reference proteome {ECO:0000313|Proteomes:UP000014254}.
FT   BINDING         18..25
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03039"
FT   BINDING         192
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03039"
FT   BINDING         195
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03039"
SQ   SEQUENCE   268 AA;  29122 MW;  0E7432329C38F985 CRC64;
     MSDINLSGIK NIVLVLSGKG GVGKSSVTTQ LALGLVHQGK KVGVLDIDLT GPSIPRMLGL
     DGKKVHQASQ GWVPVYADEH QRLSCMSIGF LLTNKNDSVV WRGPKKNAMI KQFLQDVYWG
     ELDYLLIDTP PGTSDEHIGI VEYLKEFNPD GAVIVTTPQG VAIADVRKEI SFCNKVKLPI
     LGVVENMSGF VCPHCAECTN IFSSGGGESM AKDYGIDFFG RVPIDPGFTS MVETEGSGSY
     VKMFEKSNLF PVFQQICDKV TEKVESNK
//
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