ID R7S3C0_PUNST Unreviewed; 698 AA.
AC R7S3C0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 53.
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=PUNSTDRAFT_55248 {ECO:0000313|EMBL:EIN04905.1};
OS Punctularia strigosozonata (strain HHB-11173) (White-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Corticiales; Punctulariaceae; Punctularia.
OX NCBI_TaxID=741275 {ECO:0000313|EMBL:EIN04905.1, ECO:0000313|Proteomes:UP000054196};
RN [1] {ECO:0000313|Proteomes:UP000054196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-11173 SS5 {ECO:0000313|Proteomes:UP000054196};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(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}.
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DR EMBL; JH687552; EIN04905.1; -; Genomic_DNA.
DR RefSeq; XP_007387828.1; XM_007387766.1.
DR AlphaFoldDB; R7S3C0; -.
DR GeneID; 18883949; -.
DR KEGG; psq:PUNSTDRAFT_55248; -.
DR eggNOG; KOG1247; Eukaryota.
DR HOGENOM; CLU_009710_3_2_1; -.
DR OMA; HLNTTEY; -.
DR OrthoDB; 1341752at2759; -.
DR Proteomes; UP000054196; 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 CDD; cd01200; WHEPGMRS_RNA; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 2.20.28.20; Methionyl-tRNA synthetase, Zn-domain; 1.
DR Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR041872; Anticodon_Met.
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 InterPro; IPR009068; uS15_NS1_RNA-bd_sf.
DR InterPro; IPR000738; WHEP-TRS_dom.
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; 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 SUPFAM; SSF47060; S15/NS1 RNA-binding domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS51185; WHEP_TRS_2; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000054196}.
FT DOMAIN 644..698
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT COILED 668..695
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 698 AA; 77957 MW; D0121E0EA2D857EE CRC64;
MSAKIRTAPD VLRYVPNPGE TILPKEGEEN VLITSALPYC NNVPHLGNVI GSTLSADVFA
RYNRTRNRRT LYVCGTDEYG TATETQALKE GVTPRQLCDH YTEIHRETYK WFNLGFDYFG
RTSTPQHTEI CQEIYLNLRK NNYLEKQTKE QTYCEGCEKF LADRFVEGIC PHCGANDARG
DQCDSCTRTL DAIDLIKPRC LVNPSHNVVH RSTAHMYVRL NALQPTLEEW IKKSWKTGKW
SLNSVINAEG ELVDSRLKGG LRPSPLTRDL QWGVPVPEQG AEDDGMKGKV FYVWFDAPIG
YPSITANYTP EWRQWWFNQD NVRLYQFMGK DNVYFHTIFW PAIQLGDGRP WTMLHHISTT
EYLNYEGGKF SKSKNRGVFG PAAKETGVPP DVWRYYLLSI RPETADAMFS WEDFIAANNN
ILLNNFGNFV NRTVKFITSQ YNGVLPESPD TEGPVSPNDA VDADFIADVN RLIKEYIDAM
ESVKLRLGLQ TVMHLSARGN LYLQASGLGK ALMTEDPARC AQVLSRAVNL IYTLSALIHP
FMPVTSDSIL AQLNAPPRAV PEAFSIDILA GHQLGKPAYL FTKIDEKMAD AWRAKFGGSQ
PSAEPNADAT HVAPAMSKRK AAAAAKAAKK ATDATANDGL KSAEVLAWEQ KVAEQGQVVR
ELKAKPKSEE TDKEITAAVE ELKKLKGELA DALAASKA
//
