SYV_NITOC
ID SYV_NITOC Reviewed; 929 AA.
AC Q3JC50;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=Noc_1091;
OS Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB
OS 11848 / C-107).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Nitrosococcus.
OX NCBI_TaxID=323261;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB 11848 / C-107;
RX PubMed=16957257; DOI=10.1128/aem.00463-06;
RA Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J.,
RA Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., Poret-Peterson A.T.,
RA Vergez L.M., Ward B.B.;
RT "Complete genome sequence of the marine, chemolithoautotrophic, ammonia-
RT oxidizing bacterium Nitrosococcus oceani ATCC 19707.";
RL Appl. Environ. Microbiol. 72:6299-6315(2006).
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; CP000127; ABA57596.1; -; Genomic_DNA.
DR RefSeq; WP_002809071.1; NC_007484.1.
DR AlphaFoldDB; Q3JC50; -.
DR SMR; Q3JC50; -.
DR STRING; 323261.Noc_1091; -.
DR PRIDE; Q3JC50; -.
DR EnsemblBacteria; ABA57596; ABA57596; Noc_1091.
DR KEGG; noc:Noc_1091; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_6; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000006838; 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 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; 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..929
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224518"
FT COILED 855..926
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 40..50
FT /note="'HIGH' region"
FT MOTIF 522..526
FT /note="'KMSKS' region"
FT BINDING 525
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 929 AA; 106475 MW; E4C8A3B0D87B7475 CRC64;
MDKNYNPQAI EQYWYQIWEQ KGYFTPQGKD SSYCIMIPPP NVTGHLHMGH AFQSTIMDAL
IRYHRMRGDD TLWQVGADHA GIATQMVVEN QLNAEGKTRH DLGREAFIQR VWEWKEHSGG
TITRQLRRMG TSVDWSRERF TMDEGLSQAV GEVFVRLYDE GLLYRGKRLV NWDSVLHTAI
SDLEVISEEE NSHLWHMRYP LSDGSGHLVV ATTRPETMLG DTAVAVHPED PRYQHLIGKT
VALPLTDRTI PVIADDYVEP EFGSGCVKIT PAHDFNDYEV GQRHGLPFIN IFTVDASLNE
NVPERYRNLD RFEARKLVVA DLEAAGLLEK IEDHKLMVPR GDRSRTVIEP YLTDQWFVKT
APLAEPAIQA VENGQIRFIP ENWNKIYFEW MRNIQDWCIS RQIWWGHRIP AWYDPEGKIY
VAPTETQARQ KYNLPPDLPL EQDPDVLDTW FSSALWPFST LGWPEDTSLL RAFYPTSVLV
TGFDIIFFWV ARMIMMGLKF TGEVPFHEVY IHGLVRDAEG QKMSKSKGNV LDPLDLIDGI
DLETLVTKRT GGLMQPAMAK RIEKATRKEF PQGIPSFGCD ALRFTFAILA TRGRDIRFDL
GRIEGYRNFC NKLWNAARYV LINVSSEISV ERQGKPEQAE ENLMLGAPER WIISRFHSTT
QEVIEGIENY RFDRVAQAIY NFTWNEYCDW YLELSKPVLN NPASPEAAKR RTRHTLVHVL
EALLRLAHPI IPFITEEIWQ QVGPLAGRQG KTIMLQPYPQ PEIDKIDEDA VAEIEWVIAF
VTGVRSIRSQ MNIAPGKPIP LLLQAGKAHD RTRLESNQKF LAALAKLDSI QWLKDETPPP
AATALVDELK LLIPLAGLID KEAELKRLDR EMQRMRKDLA RVQGKLANSN YVERAPAEIV
AKERQRAQEV TAALSTLEQQ HAEITDLNP
