SYV_MYCGA
ID SYV_MYCGA Reviewed; 860 AA.
AC Q7NAR7;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02004};
DE EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02004};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02004};
DE Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02004};
GN Name=valS {ECO:0000255|HAMAP-Rule:MF_02004}; OrderedLocusNames=MYCGA5680;
GN ORFNames=MGA_0338;
OS Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
OS (Mycoplasmoides gallisepticum).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=710127;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R(low / passage 15 / clone 2);
RX PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT "The complete genome sequence of the avian pathogen Mycoplasma
RT gallisepticum strain R(low).";
RL Microbiology 149:2307-2316(2003).
CC -!- FUNCTION: Catalyzes the attachment of valine to tRNA(Val). As ValRS can
CC inadvertently accommodate and process structurally similar amino acids
CC such as threonine, to avoid such errors, it has a 'posttransfer'
CC editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-
CC dependent manner. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-
CC tRNA(Val); Xref=Rhea:RHEA:10704, Rhea:RHEA-COMP:9672, Rhea:RHEA-
CC COMP:9708, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57762,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78537, ChEBI:CHEBI:456215; EC=6.1.1.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02004};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02004}.
CC -!- DOMAIN: ValRS has two distinct active sites: one for aminoacylation and
CC one for editing. The misactivated threonine is translocated from the
CC active site to the editing site. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC activity. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02004}.
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DR EMBL; AE015450; AAP56918.2; -; Genomic_DNA.
DR RefSeq; WP_011113825.1; NC_004829.2.
DR AlphaFoldDB; Q7NAR7; -.
DR SMR; Q7NAR7; -.
DR KEGG; mga:MGA_0338; -.
DR PATRIC; fig|233150.7.peg.640; -.
DR HOGENOM; CLU_001493_0_2_14; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000001418; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd07962; Anticodon_Ia_Val; 1.
DR Gene3D; 1.10.287.380; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.90.740.10; -; 1.
DR HAMAP; MF_02004; Val_tRNA_synth_type1; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033705; Anticodon_Ia_Val.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR010978; tRNA-bd_arm.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
DR PANTHER; PTHR11946; PTHR11946; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR PRINTS; PR00986; TRNASYNTHVAL.
DR SUPFAM; SSF46589; SSF46589; 1.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00422; valS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Coiled coil; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..860
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224507"
FT COILED 794..860
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 53..63
FT /note="'HIGH' region"
FT MOTIF 527..531
FT /note="'KMSKS' region"
FT BINDING 530
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 860 AA; 100869 MW; F003BA7ACF44E62D CRC64;
MKRLKKIDLN QKYDHKTVSE GVVDFWLTTD YANQDSDFCD PNAKPFSIIM PPPNLTGILH
IGHAWNLSIQ DLIVRYQKLV MGKINWIPGT DHAGIATQTK FESIQRTKEI NYKKDDRTTH
FNNIYQWSQE SSQTIKNQAK SLGLALNWKK EKFTLSQESN KYVLDVFVKL YQQGYIVKKY
TLVNWDTKLN TAISNIEVIN KETTQKLHYI KYYLKDSNDY LVIATTRPET IYADVAVFVN
PNDQRYLKYH NQMVINPLNN KLIPILVDEY IDMEFGSAVM KCTPGHDHND YALSKKYQLE
ELSCINFDGT LNELALEFSG LDLYEARELI VKKLISEDKY VKFEEITSNV GYSDRSNVIV
QPLLSKQWFL ITTKFVDEIK KLVNNEDQIK IYPKRFLDTI NNWLDHNQDW CISRQLVWGH
QIPAWYHKDH PDEVIVSINS PGDDYYRDSD VLDTWFSSAL WPLICFDDGL DQKEFNANFP
NSLLVTAYDI VFFWVLRMIF MSWLLKKSIP FHDLLLHGLI LDEHNRKMSK SLNNGVDPIQ
IIDQYGADAL RLFLTSNTSP GEDVSYNVEK INAAASFLNK LWNLARYLKL IDQSKLTDQP
LDSLDHWIIH RFNEVNAGIQ DKLKEYRFAL SNKQLSDFIW DDFANVYIEL NKKAQWSKAK
FELANDIFRK FLIMLHPSVP FITEQIYNTF EFSDSKPSII LEKWPGLIKI ENALDHFDQI
FNLIIKIRNF KQSFDLKNKD TLDLLYKNEV SYIKDLTKYL KTENVNLIKI SDQKLNDLFL
IATEDNEFYV VYTQDKTKIV DKLVVEIAKL EKEVERSSNI VNNKNFKKKA PKEKYEAELK
KLSNYQEELK LKQDKLNSLK
