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Database: UniProt
Entry: A0A139TV64_9BACT
LinkDB: A0A139TV64_9BACT
Original site: A0A139TV64_9BACT 
ID   A0A139TV64_9BACT        Unreviewed;       537 AA.
AC   A0A139TV64;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Methionine--tRNA ligase {ECO:0000256|ARBA:ARBA00018753};
DE            EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
DE   AltName: Full=Methionyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030904};
GN   ORFNames=HMPREF3039_00255 {ECO:0000313|EMBL:KXU55524.1};
OS   Akkermansia sp. KLE1798.
OC   Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC   Akkermansiaceae; Akkermansia.
OX   NCBI_TaxID=1574265 {ECO:0000313|EMBL:KXU55524.1, ECO:0000313|Proteomes:UP000070454};
RN   [1] {ECO:0000313|EMBL:KXU55524.1, ECO:0000313|Proteomes:UP000070454}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KLE1798 {ECO:0000313|EMBL:KXU55524.1,
RC   ECO:0000313|Proteomes:UP000070454};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Is required not only for elongation of protein synthesis but
CC       also for the initiation of all mRNA translation through initiator
CC       tRNA(fMet) aminoacylation. {ECO:0000256|ARBA:ARBA00003314}.
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:KXU55524.1}.
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DR   EMBL; LTZM01000007; KXU55524.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139TV64; -.
DR   PATRIC; fig|1574265.3.peg.235; -.
DR   OrthoDB; 9810191at2; -.
DR   Proteomes; UP000070454; 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; 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}.
FT   DOMAIN          2..135
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          153..366
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          379..528
FT                   /note="Methionyl-tRNA synthetase anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF19303"
SQ   SEQUENCE   537 AA;  60504 MW;  0F57B3226E98B789 CRC64;
     MYYITTAIDY TNGPPHIGHA YEKVLADVLA RWHRMKGEEV YFLTGVDQHG QKVQQTAEKL
     GITPQEHVDN ITARFLALWE RLGISYDGWA ATTDPRHKAC VQKILTSLKD KGQLYKKSYR
     GFYSVRQEQF LTDKERDENG NFGPEWGEVV ELEEENWYFR LADQAEWMKQ FVEKSGSFVL
     PAFRKAEVLN AIERSFDADL CISRPKERLS WGIELPFDPD FVTYVWFDAL INYVSFAGYL
     AEPGSGLPEF SKLWPADCEV IGKDILVPAH GVYWPAMLHA MGFSDEEMPT LLVHGWWNIN
     GEKMSKSIGN VVDPNLLVEE FGPEPVRYYL VRDITTGKDA NFDADRLVML YNTELANDLG
     NLCNRSINMT RRYCESVLPA PGEYDDDASK ALRATMDQAV VQFSRFMDEN MVSDALAALN
     AQVSACNAYI EQQQPWQLAK DEASAPRLGC VLRHLLECCA QTGYLIGCVL PGASSRILEQ
     LNADSLFQGL TPSVLSWGVL PAGHRINDPA PVFPRILSEE EKAKLAEKAA KAANKQG
//
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