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Database: UniProt
Entry: W9YKK5_9EURO
LinkDB: W9YKK5_9EURO
Original site: W9YKK5_9EURO 
ID   W9YKK5_9EURO            Unreviewed;       332 AA.
AC   W9YKK5;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Methionyl-tRNA synthetase {ECO:0000313|EMBL:EXJ93412.1};
GN   ORFNames=A1O1_01804 {ECO:0000313|EMBL:EXJ93412.1};
OS   Capronia coronata CBS 617.96.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX   NCBI_TaxID=1182541 {ECO:0000313|EMBL:EXJ93412.1, ECO:0000313|Proteomes:UP000019484};
RN   [1] {ECO:0000313|EMBL:EXJ93412.1, ECO:0000313|Proteomes:UP000019484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 617.96 {ECO:0000313|EMBL:EXJ93412.1,
RC   ECO:0000313|Proteomes:UP000019484};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., 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 Capronia coronata CBS 617.96.";
RL   Submitted (MAR-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|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}.
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:EXJ93412.1}.
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DR   EMBL; AMWN01000002; EXJ93412.1; -; Genomic_DNA.
DR   RefSeq; XP_007720906.1; XM_007722716.1.
DR   AlphaFoldDB; W9YKK5; -.
DR   STRING; 1182541.W9YKK5; -.
DR   GeneID; 19156705; -.
DR   eggNOG; KOG3022; Eukaryota.
DR   HOGENOM; CLU_024839_0_1_1; -.
DR   OrthoDB; 228512at2759; -.
DR   Proteomes; UP000019484; 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; 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.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_03039};
KW   Aminoacyl-tRNA synthetase {ECO:0000313|EMBL:EXJ93412.1};
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:EXJ93412.1};
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:UP000019484}.
FT   BINDING         15..22
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03039"
FT   BINDING         235
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         238
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   332 AA;  35423 MW;  B6A84E6DE3BADA48 CRC64;
     MGLENVKHVV LVLSGKGGVG KSSVTLQLAL SLTQQGHNVG ILDIDLTGPS IPRLLNLEDK
     KVTQAPGGWL PVKVHDARDG EAETSNGHEA PLPVTPSRRG SLHALSLAFL LPSRSSAVIW
     RGPKKTAMIR QFVSDVLWPP NTDYLLIDTP PGTSDEHIAI VEELHKLAAD VQPQPTRNGN
     ALSLESDTGP KLSGAVVVTT PQAISTADVR KELNFCVKTQ IRVLGVIENM AGYMCPCCGE
     ISNVFSKGGG EVMARECNVP FLGSVPIDTG FGALVEGVKE EQNAVNGTQP TNGEASRKST
     ELVERYKECG LCPIFSDFAS RIDQKVRDAT TS
//
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