ID H0GVF6_SACCK Unreviewed; 751 AA.
AC H0GVF6;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 13-SEP-2023, entry version 41.
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=VIN7_7397 {ECO:0000313|EMBL:EHN02210.1};
OS Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7)
OS (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=1095631 {ECO:0000313|EMBL:EHN02210.1, ECO:0000313|Proteomes:UP000009009};
RN [1] {ECO:0000313|EMBL:EHN02210.1, ECO:0000313|Proteomes:UP000009009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VIN7 {ECO:0000313|EMBL:EHN02210.1,
RC ECO:0000313|Proteomes:UP000009009};
RX PubMed=22136070; DOI=10.1111/j.1567-1364.2011.00773.x;
RA Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA Pretorius I.S., Egholm M., Chambers P.J.;
RT "The genome sequence of the wine yeast VIN7 reveals an allotriploid hybrid
RT genome with Saccharomyces cerevisiae and Saccharomyces kudriavzevii
RT origins.";
RL FEMS Yeast Res. 12:88-96(2012).
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|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363039}.
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:EHN02210.1}.
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DR EMBL; AGVY01000232; EHN02210.1; -; Genomic_DNA.
DR AlphaFoldDB; H0GVF6; -.
DR HOGENOM; CLU_009710_4_1_1; -.
DR PhylomeDB; H0GVF6; -.
DR Proteomes; UP000009009; 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; cd10290; GST_C_MetRS_N_fungi; 1.
DR CDD; cd00814; MetRS_core; 1.
DR Gene3D; 1.20.1050.110; -; 1.
DR Gene3D; 3.40.30.170; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 2.20.28.20; Methionyl-tRNA synthetase, Zn-domain; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR041872; Anticodon_Met.
DR InterPro; IPR018285; Met-tRNA-synth_N.
DR InterPro; IPR023458; Met-tRNA_ligase_1.
DR InterPro; IPR014758; Met-tRNA_synth.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR033911; MetRS_core.
DR InterPro; IPR029038; MetRS_Zn.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR NCBIfam; TIGR00398; metG; 1.
DR PANTHER; PTHR45765; METHIONINE--TRNA LIGASE; 1.
DR PANTHER; PTHR45765:SF1; METHIONINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR Pfam; PF19303; Anticodon_3; 1.
DR Pfam; PF09635; MetRS-N; 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; SSF57770; Methionyl-tRNA synthetase (MetRS), Zn-domain; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 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 11..131
FT /note="Methionyl-tRNA synthetase N-terminal
FT heteromerisation"
FT /evidence="ECO:0000259|Pfam:PF09635"
FT DOMAIN 198..589
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 611..750
FT /note="Methionyl-tRNA synthetase anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19303"
SQ SEQUENCE 751 AA; 85307 MW; A7533E3494C70203 CRC64;
MSFQISFDKS KKHPAHLQLA NNLKIALALG LANKNLKLEV NDDNAAMELC STKEAFTLFD
ANAILRYIMD DFEDQSSDKY QFALASLQNL LYHKELPGQH VEVLTNKAFE NYLAELKEPL
TATDLILFAN VCALDSSFVQ SKFPDLPSKV RSAISLAQEH IPRDSSSFKN TGAVKIQPNL
TVKPKDAEIL PKPNERNVLI TSALPYVNNV PHLGNIIGSV LSADIFARYC RGRNYNALFI
CGTDEYGTAT ETKALEEKVT PRELCNKYHK IHGDVYKWFQ IGFDYFGRTT TDKQTEIAQD
IFTKLNSNGY LEEQSMKQLY CPVHNSYLAD RYVEGECPKC HYDDARGDQC DKCGTLLDPF
ELINPRCKLD DASPEPKYSD HIFLSLDKLE AQISGWVGKA SEDGNWSKNS KTITQSWLKD
GLKPRCITRD LVWGTPVPLE KYKDKVLYVW FDATIGYVSI TANYTKEWKQ WWKNPEHVSL
YQFMGKDNVP FHTVVFPGSQ LGTEENWTML HHLNTTEYLQ YENGKFSKSR GVGVFGNNAQ
DSGISPSVWR YYLASIRPES SDSHFSWDDF VARNNSELLA NLGNFVNRLI KFVNAKYSGV
VPKADPKKIS NYDSLVKDIN EILSSYIKEM ELGHERRGLE IAMSLSARGN QFLQENKLDN
TLFSQFPEKS DAVVTVGLNI IYAVSSIITP YMPEIGEKIN KMLNAPALKI DDIFHLAILE
GHNINKAEYL FQRIDENKID EWRAKYGGQQ V
//
