ID A0A0Q3RH73_AMAAE Unreviewed; 964 AA.
AC A0A0Q3RH73;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Methionine--tRNA ligase, cytoplasmic {ECO:0000256|ARBA:ARBA00018335};
DE EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
DE AltName: Full=Methionyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030904};
GN ORFNames=AAES_44085 {ECO:0000313|EMBL:KQK84961.1};
OS Amazona aestiva (Blue-fronted Amazon parrot).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK84961.1, ECO:0000313|Proteomes:UP000051836};
RN [1] {ECO:0000313|EMBL:KQK84961.1, ECO:0000313|Proteomes:UP000051836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FVVF132 {ECO:0000313|EMBL:KQK84961.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KQK84961.1}.
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DR EMBL; LMAW01000929; KQK84961.1; -; Genomic_DNA.
DR STRING; 12930.A0A0Q3RH73; -.
DR Proteomes; UP000051836; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005869; C:dynactin complex; IEA:InterPro.
DR GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
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 GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR CDD; cd07957; Anticodon_Ia_Met; 1.
DR CDD; cd00814; MetRS_core; 1.
DR CDD; cd00939; MetRS_RNA; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 2.20.28.20; Methionyl-tRNA synthetase, Zn-domain; 1.
DR Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 1.
DR HAMAP; MF_00098; Met_tRNA_synth_type1; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR041872; Anticodon_Met.
DR InterPro; IPR028133; Dynamitin.
DR InterPro; IPR023458; Met-tRNA_ligase_1.
DR InterPro; IPR014758; Met-tRNA_synth.
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 InterPro; IPR009068; uS15_NS1_RNA-bd_sf.
DR InterPro; IPR000738; WHEP-TRS_dom.
DR NCBIfam; TIGR00398; metG; 1.
DR PANTHER; PTHR45765; METHIONINE--TRNA LIGASE; 1.
DR PANTHER; PTHR45765:SF1; METHIONINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR Pfam; PF19303; Anticodon_3; 1.
DR Pfam; PF04912; Dynamitin; 3.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR Pfam; PF00458; WHEP-TRS; 1.
DR PRINTS; PR01041; TRNASYNTHMET.
DR SMART; SM00991; WHEP-TRS; 1.
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 SUPFAM; SSF47060; S15/NS1 RNA-binding domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS00762; WHEP_TRS_1; 1.
DR PROSITE; PS51185; WHEP_TRS_2; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000051836}.
FT DOMAIN 904..960
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT REGION 261..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 165..192
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 964 AA; 108028 MW; 6374B1755D1CF0EF CRC64;
MRCCLCLLPP PTEELTSTSV EHLIINPNAA YEKFRDKRLG TEGVDFSDRI TKSRTTGYES
GEYEMMAELE KRLAQLEATV RCEPDSQNPL LVGLKGSSLM ETVQVLQAKV NILDVAVLDQ
VEARLQSVLG KVNEIAKHKS TVQDADTQSK VGEDLGAKET PQQRYQRLQY EVQELAREVE
QIQSTVKEVA AEEELTPMAL ARQVEGLKQQ LVSSHLEKLL GPTAAIDFAD PDGALAKAAA
DTVLVPEALL EFTSCLQKQP PPCPAVQRAT SNEPEEEEGS ERALTEDEIA AAADAWARGA
AALPRPWQPQ EPVLPVEGMR NVLITSALPY VNNVPHLGNI IGCVLSADTF ARYCRLRNWN
TLYVCGTDEY GTATETKAVE EGLTPQEICD KYNAIHADIY RWFGISFDCF GRTTTPSQTT
IAQDIFQRLL ARGFLLQDTV EQLRCEGCQR FLADRFVEGT CPFCGYEEAR GDQCDKCGKL
INAVELKSPH CKLCRGVPIV KPTQHLFLDL PKLEQRLEAW LEQSWATGDW TANARYITRS
WIRDGLKPRC ITRDLKWGTP VPLDGFRDKV FYVWFDAPIG YLSITANYTP EWERWWKNPQ
QVELYNFMAK DNVPFHSVIF PCSLLGADDN YTLVNHLIAT EYLNYEDGKF SKSRGVGVFG
DMAKDTGIPA DVWRFYLLYL RPEGQDSAFS WSDLMLKNNS ELLNNLGNFI NRAGMFVCKF
FGGAVPSMVL TPDDKRLLAR VTLELRRYHQ LLEKVRIRDA LRCILSISRH GNQYIQVNEP
WKRIKGDEQD RQRAGTVTGV AVNMASLLAV MLQPYMPSIS VAIQGQLRIP AECFVLSXDF
TCTLPPGHRV GTVSPLFQKL ENDRVEALRR RFGGAQPEDL AVEPQAKQTP PAPETPVAPT
DPQRLQELTQ EVARQGNHVR QLKAHKAEKA QIAVEVAKLL ELKQQLALAE GKSPQVPAPK
GKQK
//