SYV_MYCPA
ID SYV_MYCPA Reviewed; 882 AA.
AC Q73XN8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=MAP_2271c;
OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS (Mycobacterium paratuberculosis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=262316;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-968 / K-10;
RX PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA Kanjilal S., Kapur V.;
RT "The complete genome sequence of Mycobacterium avium subspecies
RT paratuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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; AE016958; AAS04588.1; -; Genomic_DNA.
DR RefSeq; WP_003878405.1; NC_002944.2.
DR AlphaFoldDB; Q73XN8; -.
DR SMR; Q73XN8; -.
DR STRING; 262316.MAP_2271c; -.
DR EnsemblBacteria; AAS04588; AAS04588; MAP_2271c.
DR KEGG; mpa:MAP_2271c; -.
DR PATRIC; fig|262316.17.peg.2415; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_11; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000000580; 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; -; 2.
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; IPR019499; Val-tRNA_synth_tRNA-bd.
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; 1.
DR Pfam; PF10458; Val_tRNA-synt_C; 1.
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..882
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224506"
FT COILED 816..882
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 52..62
FT /note="'HIGH' region"
FT MOTIF 539..543
FT /note="'KMSKS' region"
FT BINDING 542
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 882 AA; 98944 MW; 32C754D3A053C9BE CRC64;
MTASRSPATD LPKSWDPPAA EYAIYRQWVD AGYFTANPAS DKPGYSIVLP PPNVTGSLHM
GHALEHTMMD ALTRRKRMQG YEVLWQPGMD HAGIATQSVV EKQLAVDGKT KEDFGRELFI
EKVWDWKRES GGAIGGQMRR LGDGVDWSRD RFTMDEGLSR AVRTIFKRLY DAGLIYRAER
LVNWSPVLQT ALSDIEVNYE EVEGELVSFR YGSLDDSGPH IVVATTRVET MLGDTAIAVH
PDDERYRHLV GSSLPHPFVD RQLLIVADEH VDPEFGTGAV KVTPAHDPND FEIGLRHQLP
MISIMDTRGR IADTGTQFDG MDRFAARVAV REALAAQGRI VEEKRPYLHS VGHSERSGEP
IEPRLSLQWW VRVESLAKAA GDAVRNGDTV IHPTSMEPRW FAWVDDMHDW CVSRQLWWGH
RIPIWYGPNG EQRCVGPDET PPEGWEQDPD VLDTWFSSAL WPFSTLGWPE KTPELEKFYP
TSVLVTGYDI LFFWVARMMM FGTFVGDDDA ITLDGRRGPQ VPFTDVFLHG LIRDESGRKM
SKSKGNVIDP LDWVDMFGAD ALRFTLARGA SPGGDLAIGE DHVRASRNFC TKLFNATRYA
LLNGAQLAEL PPLDELTDAD RWILGRLEEV RAEVDSAFDN YEFSRACESL YHFAWDEFCD
WYVELAKTQL AEGITHTTAV LATTLDTLLR LLHPVIPFIT EALWQALTGN ESLVIADWPR
SSGIDLDQVA TQRITDMQKL VTEVRRFRSD QGLADRQKVP ARLAGVTESD LDTQVSAVTS
LAWLTDAGPD FRPSASVEVR LRGGTVVVEL DTSGSIDVAA ERRRLEKDLA AAHKELASTT
AKLANEDFLA KAPPHVVDKI RDRQRLAQEE SERINARLAV LQ
