SYV_UREPA
ID SYV_UREPA Reviewed; 874 AA.
AC Q9PQM4;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=UU267;
OS Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=273119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700970;
RX PubMed=11048724; DOI=10.1038/35037619;
RA Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA Cassell G.H.;
RT "The complete sequence of the mucosal pathogen Ureaplasma urealyticum.";
RL Nature 407:757-762(2000).
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; AF222894; AAF30676.1; -; Genomic_DNA.
DR RefSeq; WP_006688900.1; NC_002162.1.
DR AlphaFoldDB; Q9PQM4; -.
DR SMR; Q9PQM4; -.
DR STRING; 273119.UU267; -.
DR EnsemblBacteria; AAF30676; AAF30676; UU267.
DR GeneID; 29672606; -.
DR KEGG; uur:UU267; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_14; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000000423; 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..874
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000106242"
FT COILED 805..874
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 46..56
FT /note="'HIGH' region"
FT MOTIF 523..527
FT /note="'KMSKS' region"
FT BINDING 526
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 874 AA; 103390 MW; 3124ECE18B6F7E93 CRC64;
MKKKLSKKYS FKEVEANKLL FWQENNLFKA QINSTKKPFT IVLPPPNVTG HLHIGHAYDF
TLSDILMRYK KLKGYDSFII PGTDHAGIAT QTKFEKNLKV NAQTNRFNLG RELFLEKLKI
WKDEQINYIH KQWNALGLGL DYSNYLFTLD PIVVQTVREV FVKMFNEHII YRDKKLVNWD
IQLKTAISNI EVIHKEVEQK LYYIKYLSQD QKDFVVVATS RPETMFGDKY LVINPKDKRY
FHLHNKIFIN PINNIEMTVI LDDYIDIEFG TGVMKCTPAH DFNDYELAKK HNLEIINIMN
ADGTLNEKCG EFKGLDRLEA RSLIIDKLQK NNHLLKVESY RTSVGFSERT NEIVEPYLSH
QWFIKMDSLI KDTIKMQDDC NNKVDFYPNR FNKTLLTWLK NTEDWCISRQ LWWGHQIPVW
YHKKTNQIYC DTIPPKDLEN WIQDEDVLDT WFSSGMWPLL TTKWNYNSHF FDRYFPTSLI
VTGMDILFFW VSRMMNFSQY LVEKKPFKDV LIHGLIRDSQ GRKMSKSLGN GIDPFDIIDK
YGLDAMRLFF ASCTTIGEDL NFSTERLGAN WNYLNKIWNI AKYIENLDEI NDNLNFEDVD
KFCDVNKWIL TELSKLTLEI NKNMDKYNLV VATKYLYDFI WNTFASYYLE YTKVLLQDLT
LKNETIKTIR YVFNKILIML QPFAPNISEE IWLCLNQTNN SILLQEYPII NFEFETIIID
KIAKIILEIR KLRLEENINN RINLCFELIS PNDAFYKSKI KLVNLLLILV NAEINEIKKT
SSNNYTYELV IDDFILKTSY EKPIDYVFQM KKASEQLNYL ENEIQRATNL LNNSGFINKA
PAQLIIKEKN KLINLKKEHA NLLKTLTDLK QKVK
