ID A0A0C9N9Q4_9FUNG Unreviewed; 542 AA.
AC A0A0C9N9Q4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=methionine--tRNA ligase {ECO:0000256|ARBA:ARBA00012838};
DE EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
GN ORFNames=MAM1_0627d11046 {ECO:0000313|EMBL:GAN11483.1};
OS Mucor ambiguus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN11483.1};
RN [1] {ECO:0000313|EMBL:GAN11483.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN11483.1};
RA Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT ambiguus NBRC6742.";
RL Submitted (SEP-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; DF836916; GAN11483.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9N9Q4; -.
DR STRING; 91626.A0A0C9N9Q4; -.
DR OrthoDB; 166496at2759; -.
DR Proteomes; UP000053815; 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; 2.170.220.10; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
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; 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:UP000053815}.
FT DOMAIN 32..398
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 415..528
FT /note="Methionyl-tRNA synthetase anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19303"
SQ SEQUENCE 542 AA; 61834 MW; C00BFB807C0FF2AB CRC64;
MRIKSLVHIS RQALCKPNFS LVSRHAKHTK AFVSTPIYYV NAVPHIGHLY STVLADTIRR
NYALHEKEVL MSTGTDEHGL KIQQAAEKNN MKPIDFCDKV SQSFKELCQA ANIGYDSFER
TTNPHHKTAV HELWSQLLEN GYLYKGKHEG WYAVSDEAFY ANNQVQEAVD EKTGEKIMVA
IESGQRVEWT SEENYKFKLS AFGDRLLQWI NENPNAIVPN NRKNEVISWI NQGLADLSVS
RLRSRLDWGI QVPNDPEHTI YVWLDALTNY LTATGYPWSK DAPLKEFFPP DVQVVGKDIV
RFHAIYWPAF LMAAGLPLPK QILAHAHWTM GKQKMSKSRG NVADPFQVMK DYGVDPVRYY
LVRDGGLADD GADYSEEMIH TRYKKDLAGQ LGNLLNRATA ASLLPSGNVP GRNQAVDPRD
QMLHHQISQT AENYNKAFEE RDFSRAYTCI FDMANKHFAE NEPWKMAKQS QDNERLSTVL
YYSLEACRVA GILLQPVMPT KMDLLLTRLG VSPQDRYFKN AAQLELKERP LGQIEGVLFP
RL
//
