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Database: UniProt
Entry: A0A024UGJ0_9STRA
LinkDB: A0A024UGJ0_9STRA
Original site: A0A024UGJ0_9STRA 
ID   A0A024UGJ0_9STRA        Unreviewed;       718 AA.
AC   A0A024UGJ0;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=methionine--tRNA ligase {ECO:0000256|ARBA:ARBA00012838};
DE            EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
DE   AltName: Full=Methionyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030904};
GN   ORFNames=H310_04272 {ECO:0000313|EMBL:ETW05320.1};
OS   Aphanomyces invadans.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Aphanomyces.
OX   NCBI_TaxID=157072 {ECO:0000313|EMBL:ETW05320.1};
RN   [1] {ECO:0000313|EMBL:ETW05320.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJM9701 {ECO:0000313|EMBL:ETW05320.1};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA   Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-
CC         methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667,
CC         Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530,
CC         ChEBI:CHEBI:456215; EC=6.1.1.10;
CC         Evidence={ECO:0000256|ARBA:ARBA00001234};
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|RuleBase:RU363039}.
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DR   EMBL; KI913957; ETW05320.1; -; Genomic_DNA.
DR   RefSeq; XP_008866758.1; XM_008868536.1.
DR   AlphaFoldDB; A0A024UGJ0; -.
DR   STRING; 157072.A0A024UGJ0; -.
DR   EnsemblFungi; H310_04272-t26_1; H310_04272-t26_1-p1; H310_04272.
DR   EnsemblProtists; ETW05320; ETW05320; H310_04272.
DR   GeneID; 20081322; -.
DR   VEuPathDB; FungiDB:H310_04272; -.
DR   eggNOG; KOG0436; Eukaryota.
DR   eggNOG; KOG2241; Eukaryota.
DR   OrthoDB; 166496at2759; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd07957; Anticodon_Ia_Met; 1.
DR   CDD; cd00814; MetRS_core; 1.
DR   CDD; cd02799; tRNA_bind_EMAP-II_like; 1.
DR   Gene3D; 2.170.220.10; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR002547; tRNA-bd_dom.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   NCBIfam; TIGR00398; metG; 1.
DR   PANTHER; PTHR43326; METHIONYL-TRNA SYNTHETASE; 1.
DR   PANTHER; PTHR43326:SF2; METHIONYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF19303; Anticodon_3; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 2.
DR   Pfam; PF01588; tRNA_bind; 1.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   PROSITE; PS50886; TRBD; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00209};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|PROSITE-
KW   ProRule:PRU00209}.
FT   DOMAIN          554..658
FT                   /note="TRNA-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50886"
SQ   SEQUENCE   718 AA;  80053 MW;  B553DB6A129B4F0F CRC64;
     MDALKDKVAA LDVSDVKLNG VTPASNEKFY ITTAIHYTNG QPHMGHAYEN VTSDVIARYH
     RTYGRDVFFL TGTDEHGQKI AQTAETQGIS PIELCDKYSG IFQQLAKDLN MSNDHFIRTT
     SKQHKEFAQL IFAKAEANGD IYKGTYEGWY NVREETFVTE NEAALINYKD PTTGTPLKKM
     QESSYFFRMS KYQERLIAHY HAHPEFLQPE NHRQIILKRL EEPLLDLSAS RTTFSHGVPL
     PNDPAHVMYV WFDALSNYLS GIDYPNGALA KYWPASVHII GKDITWFHCV IWPCILMSAG
     FPLPTRVFAH GFVNARDGTK MSKSIGNVVD PYDMIQKYGV DSFRYFLVRG AKYGSDMPFS
     EDEFFNIHNA ELNDTLGNLV HRGLTLSVKY TNGHVPDVAA TPCFDVAALK AATEEAFQAY
     ALQEAAFRFM EVVRATNGYL TTAAPWHMTD DHEKKVVVRT ILEAIYVFAH YMVPFMPATA
     ARVFEFLHTA PTTLPLLSND FNNLTPGTPI KEVTKDDILF EKLKSEAELA ALASKQAAAA
     APPVVKKAKE DLPLFASCDI RVGTIVKAWH HPDSDKLFCE EIDVGFETGP VQIASGLRPF
     YSLDDMTGRR CLVLLNIKAA KLAGFKSNGM VLCASNEAHD VVEFIEPPAG AANGERVFIA
     TESGDPVSEG QMKKQKIWEK LSVDLQTNDK REGTYKGHVI QTSAGPVVSK TLTNARIG
//
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