SYV_NEIG1
ID SYV_NEIG1 Reviewed; 945 AA.
AC Q5F5W0;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=NGO1809;
OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=242231;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700825 / FA 1090;
RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT "The complete genome sequence of Neisseria gonorrhoeae.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
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; AE004969; AAW90427.1; -; Genomic_DNA.
DR RefSeq; WP_003690041.1; NC_002946.2.
DR RefSeq; YP_208839.1; NC_002946.2.
DR AlphaFoldDB; Q5F5W0; -.
DR SMR; Q5F5W0; -.
DR STRING; 242231.NGO_1809; -.
DR EnsemblBacteria; AAW90427; AAW90427; NGO_1809.
DR KEGG; ngo:NGO_1809; -.
DR PATRIC; fig|242231.10.peg.2170; -.
DR HOGENOM; CLU_001493_0_2_4; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000000535; 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..945
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224516"
FT COILED 879..945
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 552..556
FT /note="'KMSKS' region"
FT BINDING 555
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 945 AA; 106333 MW; 4C6FC95AD43CF380 CRC64;
MLDKYSPAEI ESKHYQNWES QGYFRPDMDL TKPSFSIQLP PPNVTGTLHM GHAFNQTIMD
GLTRYYRMKG CNTAWIPGTD HAGIATQIVV ERQLAAQNVS RHDLGREKFL EKVWEWKEVS
GGTITQQMRR VGCSADWTRE YFTMDGVRAE TVTEVFVRLY EQGLIYRGKR LVNWDPVLGT
AVSDLEVESM EEQGSMWHIR YPLADNPTEA VIVATTRPET LLGDAAVAVN PEDERYTHLI
GKELILPLTG RTIPVIADEY VEKDFGTGCV KITPAHDFND YEVGKRHDTR LINVFDLEAK
VLANAEVFNF KGEAQPGFSL PEKYAGLDRF AARKQMVADL QEQGFLVEIK PHTLMTPKGD
RTGSVIEPML TSQWFVAMSA TPNGGEPDNE FKGLSLADKA KKAVDSGAVR FIPENWVNTY
NQWMNNIQDW CISRQLWWGH QIPAWYDEAG NVYVARNQAE AEKQAGKTGL TREEDVLDTW
FSSALVPFST LGWPSETDEL KAFLPSNVLV TGYEIIFFWV ARMIMMTTHF TGKVPFKAVY
IHGIVRDHEG KKMSKSEGNV IDPVDLIDGI GLDKLLMKRT TGLRKPETAP KVEEATKKLF
PEGIPSMGAD ALRFTMASYA SLGRSVNFDF KRAEGYRNFC NKIWNATNFV LMNTENQDCG
YGATAAEPRG HSFPDMWIIG RLNQTIEQVT QAYETYRFDL AAETLYSFVW NDYCDWYLEL
AKVQLQTGCA SRQRATRHTL LRVLEAALRL LHPIIPFITE ELWQTVAPMC DAKTADSIML
ARFPETDGGE IVQTAFGQMT VLQDLIGAVR NLRGETGIQP NVKAPLFVES ADDLADYLKY
LPMMTRLTEA RQVAALPESG DAPVAVCNGA RLMLKVEIDK AAETARLSKE AEKLQKALDK
LNAKLSKPGY TEKAPAHLVE KDKADLAELE DKMAKVQNQL AKLKD
