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Database: UniProt
Entry: K2SG95_MACPH
LinkDB: K2SG95_MACPH
Original site: K2SG95_MACPH 
ID   K2SG95_MACPH            Unreviewed;       674 AA.
AC   K2SG95;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 48.
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=MPH_01180 {ECO:0000313|EMBL:EKG21459.1};
OS   Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Macrophomina.
OX   NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG21459.1, ECO:0000313|Proteomes:UP000007129};
RN   [1] {ECO:0000313|EMBL:EKG21459.1, ECO:0000313|Proteomes:UP000007129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS6 {ECO:0000313|EMBL:EKG21459.1,
RC   ECO:0000313|Proteomes:UP000007129};
RX   PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA   Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA   Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA   Saito J.A., Alam M.;
RT   "Tools to kill: Genome of one of the most destructive plant pathogenic
RT   fungi Macrophomina phaseolina.";
RL   BMC Genomics 13:493-493(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:EKG21459.1}.
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DR   EMBL; AHHD01000049; EKG21459.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2SG95; -.
DR   STRING; 1126212.K2SG95; -.
DR   VEuPathDB; FungiDB:MPH_01180; -.
DR   eggNOG; KOG1247; Eukaryota.
DR   HOGENOM; CLU_009710_1_0_1; -.
DR   InParanoid; K2SG95; -.
DR   OrthoDB; 1341752at2759; -.
DR   Proteomes; UP000007129; 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; 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; IPR023458; Met-tRNA_ligase_1.
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   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; 2.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007129}.
FT   DOMAIN          16..179
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          191..432
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          444..608
FT                   /note="Methionyl-tRNA synthetase anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF19303"
FT   REGION          613..674
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        613..637
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        649..674
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   674 AA;  75481 MW;  90046FD5DB518ADA CRC64;
     MASSQPILPQ EGKRNILITS ALPYVNNIPH LGNIIGSVLS ADVYSRYCKA RGYPTLFVCG
     SDEYGTATET KAIDEGLTPQ ELCDKYHKIH ADVYSWFNIG FDKFGRTPTK EQTEIAQDIF
     LKLHKNGYLE EKTTVQPYCE KHGSFLADRF VEGECSICGD PGARGDQCDK CGNLLDPLEP
     ESEAKTPPTS DEPEPVGEAK ATGFLINPRC KLDGAAPVKR ETKHVYIRLD ALKDQIVEWF
     KKASTEGKWS SNCIQITQSW IDKGLKPRGI TRDLKWGTAV PLPGYEDKVM YVWFDACIGY
     VSITATYTDE WEKWWKNPEN VKLYQFMGKD NVQFHTIIFP GSQLGTGDKW TQVHHLSTTE
     YLNYEDTKFS KSKGVGVFGN NAKDTGIPSD VWRYYLLSRR PETSDSEFKW KDFIDSNNND
     LLKNLGNFVN RVIKFVAAKY DSVVPDYTKY KDEDEYLKKH EEAVNELLKT YETHLEAVKL
     KAGLSTVLHV SALGNKLLQD NKLDNRLFSE EPERCAAVVG MALNHIHLLA SLVEPYMPAT
     ARGGVTDKGE PIAGIFQQLN VEAVPHIPEK WTTGAIKPGH KIGKAGYLFT QIKAEKEQEW
     REAYGGEEAK KAKQLEAEKR AAKKAQKEKD KAKKAAKKAA AAAGGIEAAE KKQEADPAIE
     KVTEAMEKAD VHTS
//
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