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Database: UniProt
Entry: F2PW38_TRIEC
LinkDB: F2PW38_TRIEC
Original site: F2PW38_TRIEC 
ID   F2PW38_TRIEC            Unreviewed;       592 AA.
AC   F2PW38;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=methionine--tRNA ligase {ECO:0000256|ARBA:ARBA00012838};
DE            EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
GN   ORFNames=TEQG_05219 {ECO:0000313|EMBL:EGE06106.1};
OS   Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN   [1] {ECO:0000313|Proteomes:UP000009169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363039}.
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DR   EMBL; DS995744; EGE06106.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2PW38; -.
DR   VEuPathDB; FungiDB:TEQG_05219; -.
DR   eggNOG; KOG0436; Eukaryota.
DR   HOGENOM; CLU_009710_9_0_1; -.
DR   Proteomes; UP000009169; 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; PF19303; Anticodon_3; 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}.
FT   DOMAIN          55..423
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          465..552
FT                   /note="Methionyl-tRNA synthetase anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF19303"
FT   REGION          569..592
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   592 AA;  66801 MW;  97B01AA46BC8344D CRC64;
     MLKAELRTFS QSLRFRKTKP TSWICGSCRQ ARAPWQPLNR GYTTEATPGA KPKPYYVTTP
     IFYVNAAPHI GHLYTILIAD ILKRWQVLLG NGDAKLLTGT DEHGMKIQQA ALQNGLEPQA
     LCDRNCETFK LLAREANASY DHFIRTTDSA HKAAVQFFWE NLNHRGYIYE GKHEGWYSVS
     DETFYPASAV HSTLDPATGR KMMASIETGK EVKFSQETNY HFKLSAFQDR LLEHYRKNPK
     FIQPKVYMDS IVQNVASGLQ DLSISRPVDR LSWGIPVPGD TTQTIYVWLD ALVNYITYAG
     YPFTPGREQE SIWPADIHVV GKDITRFHCI YWPAFLMALD LPLPRTILTH AHWTMNHSKM
     SKSTGNVVNP MFAMARYGVD PMRFYLAMNG GLASDTDYDN SYIVRDYKNI LQGGLGNLCS
     RVMRGKGWNV RESVVKMANG QGSRRAKDPS EIEHMEFLEK VPGLVSNQMD ELNPRRALEE
     IVKIIDQTNR YVQSTGPWNL AKEASTDPTA HDQLVGVIYN ATESLRIAGI LLQPFMPEKA
     KKLLDMLGVE EDLSKRSYAA AKYGADPDYG TPRVPLGKGQ AGTLFPPLLS EE
//
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