ID A0A081CFH9_PSEA2 Unreviewed; 630 AA.
AC A0A081CFH9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 13-SEP-2023, entry version 35.
DE RecName: Full=methionine--tRNA ligase {ECO:0000256|ARBA:ARBA00012838};
DE EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
GN ORFNames=PAN0_008c3642 {ECO:0000313|EMBL:GAK65425.1};
OS Pseudozyma antarctica (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=84753 {ECO:0000313|EMBL:GAK65425.1};
RN [1] {ECO:0000313|EMBL:GAK65425.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 10317 {ECO:0000313|EMBL:GAK65425.1};
RA Morita T., Saika A., Koike H.;
RT "Draft genome sequence of the yeast Pseudozyma antarctica JCM 10317 known
RT as a producer of lipase B which used in a wide range of industrial
RT applications.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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; DF830075; GAK65425.1; -; Genomic_DNA.
DR RefSeq; XP_014656629.1; XM_014801143.1.
DR AlphaFoldDB; A0A081CFH9; -.
DR GeneID; 26304332; -.
DR HOGENOM; CLU_009710_9_0_1; -.
DR OrthoDB; 166496at2759; -.
DR Proteomes; UP000053758; 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; cd00814; MetRS_core; 1.
DR Gene3D; 2.170.220.10; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
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; 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; 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:UP000053758}.
FT DOMAIN 48..81
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 97..449
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
SQ SEQUENCE 630 AA; 70142 MW; 5F3ECBFEFA0120B4 CRC64;
MSCQSRPLVQ PPRCAASCER LARRHFTSTI NARSAPGPAS SGSSLKPYYV TTPIFYVNAD
PHIGHLYSDV IADVLARYHG YMNSGYSAYD RNGRPVSADS YGLQARVAQQ SPVSPIFSTG
TDEHGLKVQK VAEAAGEDPR ALCDRISQRF RHLADAANVD FSTFIRTTDA DHAVAVEHLW
RTLRERGHIY QGSHEGWYAV SDEAFYPETQ VRKVVVDGQE QMQSIETGAK VEWSQEVNYK
FRLSAFQQPL IDWLRANPTA IQPAQRHAQV LQEIESGLAD LSISRPRSRL SWGIPVPDDA
DHTIYVWVDA LTNYLTVTGY PAWANDASKE SSAVERSAWP ADVHVVGKDI LRFHAIYWPA
MLLAAGLPLP KTIVAHSHWT MNRAKMSKSR GNVANPFEAI DMFGVDTLRF FLMRVGGNLG
ADSDYNPAVL VEYHRKYLQG QLGNLVSRIS APKIHAGLAD SPRDEKGVLL RPSAEDVRAV
LDQETYALCE RLEEELKQLP GKVDELMQAF ELAKVLELVL ETAVGTANEM VQRIEPWNAA
TPVAAVREAV VLTTETLRIA ALLLHPFMPT KMTQLLDALL IPQNLRTSSK HLVRQDVNGR
LVSHARWRDP AQPKVEPLFP KIQPDPTTKA
//