ID A0A452HC42_9SAUR Unreviewed; 644 AA.
AC A0A452HC42;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Methionine--tRNA ligase, mitochondrial {ECO:0000256|ARBA:ARBA00026124};
DE EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
DE AltName: Full=Methionyl-tRNA synthetase 2 {ECO:0000256|ARBA:ARBA00029831};
DE AltName: Full=Mitochondrial methionyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030331};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000012336.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000012336.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363039}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR STRING; 38772.ENSGAGP00000012336; -.
DR Ensembl; ENSGAGT00000014125.1; ENSGAGP00000012336.1; ENSGAGG00000009486.1.
DR Proteomes; UP000291020; 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; 2.
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; 2.
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:UP000291020}.
FT DOMAIN 33..65
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 137..457
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 487..591
FT /note="Methionyl-tRNA synthetase anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19303"
FT REGION 62..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 644 AA; 72096 MW; 8C4357E05FBA8681 CRC64;
MLSLPARCLL RPPRQPLPAP PRRGSSGPGR RWLLSTPIFY VNGPPHIGHL YSALLADALH
RHRGLLGPGP GRLATGERER GGGGAGPGAD PCGGXGLAAL HPRPAGGALL AGQCPREAGA
PALQPPWPST QLPRLTVPGT DEHGLKIQQA AAAAGTAPSE LCAHVSGLFR DLFSRAAVSF
TDFIRTTEPR HRRAVQCFWA ALQGRGLLYK DFYEGWYCTP DECFLTQAQI TERPDAQGRP
CKVSLDSGHQ VHWTKEENYM FKLSEFQEPL RKWLQGNRHV ISPEPFYQVV LRWLEEDLPD
LSVSRERNRL QWGIPVPGDS TQTIYVWVDA LVNYLTVAGY PDAHHTWWPA AHHVVGKDIL
KFHAIYWPAL LMAVGLDPPE QIYVHSHWTV RGQKMSKSLG NVVDPVACFK QYTVDGFRYF
LLRQGVPERD CDYYEEKVIK LVNSELADAL GGLLNRCTAP SINPSGIYPH FSESCFRKGS
DHMDVEASGR ALAEDYELIA SVDRLPLQVT DYFEHFQIYK ALESVVTCVR QTNGFFQRHA
PWKLCRDNPA EKCWLDTVLH VTLECLRIYG ILLQPVIPAT AEKLLSRLSI KPEERAFTGL
TFLPRYHGKP CPFEGRKLGP DMGALFPRLE TPRRHQMEIK GLRP
//