SYV_HAEIN
ID SYV_HAEIN Reviewed; 954 AA.
AC P43834;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 140.
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=HI_1391;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7959067; DOI=10.1016/0378-1119(94)90861-3;
RA Nwankwo D.O., Moran L.S., Slatko B.E., Waite-Rees P.A., Dorner L.F.,
RA Benner J.S., Wilson G.G.;
RT "Cloning, analysis and expression of the HindIII R-M-encoding genes.";
RL Gene 150:75-80(1994).
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; L42023; AAC23038.1; -; Genomic_DNA.
DR EMBL; L15391; AAA61960.1; -; Genomic_DNA.
DR PIR; G64121; G64121.
DR RefSeq; NP_439545.1; NC_000907.1.
DR RefSeq; WP_005693970.1; NC_000907.1.
DR AlphaFoldDB; P43834; -.
DR SMR; P43834; -.
DR STRING; 71421.HI_1391; -.
DR EnsemblBacteria; AAC23038; AAC23038; HI_1391.
DR KEGG; hin:HI_1391; -.
DR PATRIC; fig|71421.8.peg.1450; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_6; -.
DR OMA; FATKLWN; -.
DR PhylomeDB; P43834; -.
DR BioCyc; HINF71421:G1GJ1-1419-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd07962; Anticodon_Ia_Val; 1.
DR Gene3D; 1.10.287.380; -; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 3.90.740.10; -; 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..954
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000106225"
FT COILED 883..953
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 48..58
FT /note="'HIGH' region"
FT MOTIF 560..564
FT /note="'KMSKS' region"
FT BINDING 563
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 954 AA; 108826 MW; FE26264932F2F78A CRC64;
MTQKFEMADR FNPSAVEQAL YQRWEESGYF KPSENENAPS YCIAIPPPNV TGSLHMGHAF
QQTLMDTLIR FNRMEGHNTL WQTGTDHAGI ATQMVVERKI AAEEGKTRHD YGREAFINKI
WDWKAYSGGT ISQQMRRLGN SIDWERERFT MDDGLSNAVK EVFVRLHEEG LIYRGKRLVN
WDPKLHTAIS DLEVENKESK GSLWHFRYPL ANDAKTADGK DYLVVATTRP ETMLGDTAVA
VHPEDERYQS LIGKTVVLPL ANREIPIIAD EYVDREFGTG VVKITPAHDF NDYEVGKRHN
LPMVNVLTLN ANIRDEAEII GTDGKPLAGY EATIPADYRG LERFAARKKI VADFEALGLL
DEIKPHDLKV PYGDRGGVPI EPMLTDQWYV SVKPLADVAI KAVEDGEIQF VPKQYENLYF
SWMRDIQDWC ISRQLWWGHR IPAWYDAEGN VYVARNEEEV RSKYNLDSAV ELKQDEDVLD
TWFSSGLWTF STLGWPEQTK ELKMFHPTDV LITGFDIIFF WVARMIMFTM HFVKDENGKP
QVPFKTVYVT GLIRDEQGQK MSKSKGNVLD PIDMIDGISL EDLLEKRTGN MMQPQLAEKI
AKATRKEFAE GIAAHGTDAL RFTLAALASN GRDINWDMKR LEGYRNFCNK LWNASRFVLT
NEKLDLSQGE IEFSLADRWI QSEFNRTVET FRSSLSQYRF DLCANAIYEF TWNQFCDWYL
ELTKPVFANG NAAQIRAASQ TLVHVLEKLL RLAHPLIPFI TEEIWQKVKG FVGITADSIM
LQPFPQVEES GFDPEAEAEI EWLKEVIVAV RNIRAESNIA PSKGLDLLFR NLSAENAKIL
EKQTALLKAM AKLDNVQVLA TNETAPLAVA KLVGNAELLV PMAGFINKEA ELARLTKEIE
KYQNEVKRIE NKLSNEAFVA KAPEAVIAKE REKQAEYQSG LEKIQEQYKA IEAL
