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Database: UniProt
Entry: A0A0K9NYG4_ZOSMR
LinkDB: A0A0K9NYG4_ZOSMR
Original site: A0A0K9NYG4_ZOSMR 
ID   A0A0K9NYG4_ZOSMR        Unreviewed;       604 AA.
AC   A0A0K9NYG4;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=methionine--tRNA ligase {ECO:0000256|ARBA:ARBA00012838};
DE            EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
GN   ORFNames=ZOSMA_55G00370 {ECO:0000313|EMBL:KMZ60985.1};
OS   Zostera marina (Eelgrass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX   NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ60985.1, ECO:0000313|Proteomes:UP000036987};
RN   [1] {ECO:0000313|Proteomes:UP000036987}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX   PubMed=26814964; DOI=10.1038/nature16548;
RA   Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA   Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA   Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA   Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA   Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA   Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA   Van de Peer Y.;
RT   "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT   the sea.";
RL   Nature 530:331-335(2016).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {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:KMZ60985.1}.
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DR   EMBL; LFYR01001545; KMZ60985.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K9NYG4; -.
DR   STRING; 29655.A0A0K9NYG4; -.
DR   OMA; NMFLPDR; -.
DR   OrthoDB; 166496at2759; -.
DR   Proteomes; UP000036987; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IBA:GO_Central.
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   HAMAP; MF_01228; Met_tRNA_synth_type2; 1.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
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; PF00133; tRNA-synt_1; 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:UP000036987}.
FT   DOMAIN          55..127
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          195..422
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          445..575
FT                   /note="Methionyl-tRNA synthetase anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF19303"
FT   REGION          573..604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        573..588
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   604 AA;  67298 MW;  07EF6D35D0AB1738 CRC64;
     MAGMAFLYSS LPFVPTVTAR VKRNKNRSTD IGNRHLRCRS RRILVLASSG LGKREVKKKE
     TFMITTPLYY ANGPPHMGSA YTTIAADAIA RFHRLLGEKV IFVTGTDEHG EKIATSAAAA
     DAIGPKEHCD SISLSYQILW KDLEISHNKF IRTTDAKHEA IVKDFYSRVL QNGDIYRADY
     EGLYCVNCEE YKDEKELLEN NCCPTHLKPC AKRKEDNYFF SLSKYQKLLE DILSNNPDFV
     QPSFRANEVQ GWIDSGLKDF SISRSSVEWG IPVPNDEKQT IYVWFDALLG YISALLNDGD
     EPTLDNALAS GWPATLHLIG KDILRFHAVY WPAMLTSAGL SLPKMVFGHG FLTKDGMKMG
     KSLGNTIEPK DLVYKFGSDA VRYFFLKEVD FGNDGDYSEE RFVNIINAHL ANTIGNLLNR
     TLGLLKKNCQ SCLAVDSSIA SEGIEFKDTV TSLVKKAHFH YENLSLSLAC ETVLEIGNAG
     NLFMNERAPW SLFKKGGSSS EAAKKDLVII LEAVRIISVA LSPITPTISL KIYSQLGFTK
     DVFEKLTWDD TKWGGLKAGQ VMAEPKPIFA RIEVDKGGDE DTNPSKVIKS KKKKSQTQGL
     VEAS
//
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