GenomeNet

Database: UniProt
Entry: A1CH95_ASPCL
LinkDB: A1CH95_ASPCL
Original site: A1CH95_ASPCL 
ID   A1CH95_ASPCL            Unreviewed;       574 AA.
AC   A1CH95;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 91.
DE   RecName: Full=methionine--tRNA ligase {ECO:0000256|ARBA:ARBA00012838};
DE            EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
GN   ORFNames=ACLA_047190 {ECO:0000313|EMBL:EAW10250.1};
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW10250.1, ECO:0000313|Proteomes:UP000006701};
RN   [1] {ECO:0000313|EMBL:EAW10250.1, ECO:0000313|Proteomes:UP000006701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC   {ECO:0000313|Proteomes:UP000006701};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363039}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS027054; EAW10250.1; -; Genomic_DNA.
DR   RefSeq; XP_001271676.1; XM_001271675.1.
DR   AlphaFoldDB; A1CH95; -.
DR   STRING; 344612.A1CH95; -.
DR   EnsemblFungi; EAW10250; EAW10250; ACLA_047190.
DR   GeneID; 4704357; -.
DR   KEGG; act:ACLA_047190; -.
DR   VEuPathDB; FungiDB:ACLA_047190; -.
DR   eggNOG; KOG0436; Eukaryota.
DR   HOGENOM; CLU_009710_9_0_1; -.
DR   OMA; MDTQAFC; -.
DR   OrthoDB; 166496at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd07957; Anticodon_Ia_Met; 1.
DR   CDD; cd00814; MetRS_core; 1.
DR   Gene3D; 2.170.220.10; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR041872; Anticodon_Met.
DR   InterPro; IPR014758; Met-tRNA_synth.
DR   InterPro; IPR023457; Met-tRNA_synth_2.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR   InterPro; IPR033911; MetRS_core.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   NCBIfam; TIGR00398; metG; 1.
DR   PANTHER; PTHR43326:SF1; METHIONINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43326; METHIONYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|RuleBase:RU363039};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363039};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363039};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363039};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363039};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006701}.
FT   DOMAIN          55..421
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
SQ   SEQUENCE   574 AA;  64917 MW;  148512C41A5CAC24 CRC64;
     MAPYRGGFRA LSWAGQFLGH KRPAWRCASC RTATGTIPPR RYVTTTSEKV SKKPYYVTTP
     IFYVNAAPHV GHFYTMVIAD ILKRWQVLLG NKNAQLLTGT DEHGMKIQQA ALAAGMDTQA
     FCDMNCKTFE ALAKAANIDN DHFIRTTDPA HKEAVQYFWE ILNHRGYIYT SKHEGWYSVS
     DETFYPPTQV QNSLDPSTGR KRMVSTETGK EVEWSSETNY HFRLSAFQDR LLEFYSSTDF
     IAPGNYKTDI VKSVSSGLSD LSISRPVERL TWGIPVPGDE TQTIYVWLDA LVNYLTRAGY
     PFVPGQESRL GWPADVHVVG KDIVRFHCVY WPAFLMALDL PLPRRVLVHG HWTMNREKMS
     KSTGNVVNPF FAIDRFGVDT MRFFLAYQGG LVGDADYDNS FIIRDYKKML QWGIGNLAHR
     TIGCAKGKLR SYIQDAAADK LPPATPADQE HQSLLEHTPG KVAEQMEKLN PRAALQDIMT
     IIERTNKYFH AAEPWSNPAE SQRVLYNVAE SLRISGILLQ PFMPSKSNEL LDILRVDSAD
     PSKRSFPAAT FGRDPDYGED VKKSVLFPPL IIEE
//
DBGET integrated database retrieval system