SYV_FUSNN
ID SYV_FUSNN Reviewed; 887 AA.
AC Q8RHK3;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=FN2011;
OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX NCBI_TaxID=190304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355;
RX PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA Overbeek R.;
RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT strain ATCC 25586.";
RL J. Bacteriol. 184:2005-2018(2002).
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; AE009951; AAL94101.1; -; Genomic_DNA.
DR RefSeq; NP_602802.1; NC_003454.1.
DR AlphaFoldDB; Q8RHK3; -.
DR SMR; Q8RHK3; -.
DR STRING; 190304.FN2011; -.
DR PRIDE; Q8RHK3; -.
DR EnsemblBacteria; AAL94101; AAL94101; FN2011.
DR KEGG; fnu:FN2011; -.
DR PATRIC; fig|190304.8.peg.479; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_0; -.
DR InParanoid; Q8RHK3; -.
DR OMA; FATKLWN; -.
DR BioCyc; FNUC190304:G1FZS-498-MON; -.
DR Proteomes; UP000002521; 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 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..887
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224480"
FT COILED 817..887
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 45..55
FT /note="'HIGH' region"
FT MOTIF 528..532
FT /note="'KMSKS' region"
FT BINDING 531
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 887 AA; 103049 MW; AE9F5FAC9757B3FE CRC64;
MNELDKNYSP NEIEEKWYKI WEDSKYFAAS LSSEKENYSI VIPPPNVTGI LHMGHVLNNS
IQDTLIRYNR MTGKNTLWMP GCDHAGIATQ NKVERKLAED GLKKEDIGRE KFLEMTWDWK
EKYGGIITKQ LRKLGASLDW DRERFTMDEG LSYAVRKIFN DLYHDGLIYQ GEYMVNWCPS
CGTALADDEV DHEEKDGHLW QIKYPVKDSD EYIIIATSRP ETMLADVAVA VHPEDERYKH
LIGKTLILPL VNREIPVIAD EYVDKEFGTG ALKITPAHDP NDYNLGKKYN LPIINMLTPD
GKIVEDYPKY AGLDRFEARK KIVEDLKAQD LFIKTEHLHH AVGQCYRCQT VIEPRVSPQW
FVKMKPLAEK ALEVVRNGEV KILPKRMEKI YYNWLENIRD WCISRQIWWG HRIPAWYGPD
RHVFVAMDEA EAKEQAKKHY GHDVELSQEE DVLDTWFSSA LWPFSTMGWP EKTKELDLFY
PTNTLVTGAD IIFFWVARMI MFGMYELKKI PFKNVFFHGI VRDEIGRKMS KSLGNSPDPL
DLIKEYGVDA IRFSMIYNTS QGQDVHFSTD LLGMGRNFAN KIWNATRFVI MNLKGFDVKS
VDKTKLDYEL VDKWIISRLN ETAKDVKDCL EKFELDNAAK AVYEFLRGDF CDWYVEIAKI
RLYNDDEDKK ISKLTAQYML WTILEQGLRL LHPFMPFITE EIWQKIKVDG DTIMLQQYPV
ADDSLIDVKI EKSFEYIKEV VSSLRNIRAE KGISPAKPAK VVVSTSNSEE LETLEKNELF
IKKLANLEEL TCGTDLEAPS QSSLRVAGNS SVYMILTGLL NNEAEIKKIN EQLAKLEKEL
EPVNRKLSDE KFTSKAPQHI IDRELRIQKE YQDKIKKLKE SLKSFEE
