SYV_BIFLO
ID SYV_BIFLO Reviewed; 911 AA.
AC Q8G777;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02005};
DE EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02005};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02005};
DE Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02005};
GN Name=valS {ECO:0000255|HAMAP-Rule:MF_02005}; OrderedLocusNames=BL0395;
OS Bifidobacterium longum (strain NCC 2705).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=206672;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCC 2705;
RX PubMed=12381787; DOI=10.1073/pnas.212527599;
RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT the human gastrointestinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(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_02005}.
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_02005};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02005}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02005}.
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_02005}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02005}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN24231.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014295; AAN24231.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_695595.1; NC_004307.2.
DR RefSeq; WP_007054756.1; NC_004307.2.
DR AlphaFoldDB; Q8G777; -.
DR SMR; Q8G777; -.
DR STRING; 206672.BL0395; -.
DR EnsemblBacteria; AAN24231; AAN24231; BL0395.
DR GeneID; 66504464; -.
DR KEGG; blo:BL0395; -.
DR PATRIC; fig|206672.9.peg.1137; -.
DR HOGENOM; CLU_001493_0_2_11; -.
DR OMA; RQWYIRN; -.
DR Proteomes; UP000000439; 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; 3.40.50.620; -; 2.
DR Gene3D; 3.90.740.10; -; 1.
DR HAMAP; MF_02005; Val_tRNA_synth_type2; 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; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR022874; Valine-tRNA_ligase_type_2.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
DR PANTHER; PTHR11946; PTHR11946; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR PRINTS; PR00986; TRNASYNTHVAL.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..911
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224607"
FT REGION 882..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 57..67
FT /note="'HIGH' region"
FT MOTIF 599..603
FT /note="'KMSKS' region"
FT BINDING 602
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ SEQUENCE 911 AA; 102115 MW; C23AE6C70F2C9887 CRC64;
MTEGKSIINA NLTPLPDKVG VDGLEDKWRT VWDEDGTYKF RNTRDRKAVY SIDTPPPTVS
GSLHVGHVFS YTHTDVIARY KRMRGYDVFY PMGWDDNGLP TERRVQNYYG VRVDVSLPYD
PDFKPPFEGT DGKKIDAKDQ VPISRKNFIE LCERLTAQDE KLFEALWRKL GLSIDWSQTY
HTIGQHPQRV AQKAFLRNLA RGEAYQQDAP GLWDVTFQTA VAQAELESRE YPGFYHKVAF
RFEDGTPIYI ETTRPELLAA CTSLIANPND ERYKQYFGQY VYSPLFKVKV PILAHPAAEM
DKGAGIAMCC TFGDVTDVEW WRDLKLPTRP IIQRNGRIVM DTPDWIEDPA GREVFAETAG
KTTFSARKII VDKLRESGDL DGEPTPTKRM TNFYEKGDKP LEIVTSRQWY LKNGGTDAKL
NAELIERGKE LEFHPDFMRV RYENWVHGLN GDWLISRQRF FGVPFPLWYP VNASGEPDYD
HPITPSEDRL PIDPTIDVPE GYDESQRDVP GGFTAEKDIM DTWATSSLTP QIVTHWAEPD
EASKALFAST FPMDLRPQGQ DIIRTWLFST VDRAHLENKC LPWAHATLSG WILDPDHKKM
SKSKGNVVVP NEPIEKFGAD AVRYWAAAAR LGLDATYDIG QMKIGRRLAI KLLNATKFAL
AIGREDENHH VGAAAEAAWN PADVTEPLDR AAMAKLALVV RQATEALESY EHSKALEVIE
SYFWQFCDDY IELVKNRAYG TPDEHGNVPS EKAVKSARTA LGLGLDAFAR LLAPYLPYAT
EEVWSWMHAG SGSVHRAAWP VVDPYVEAAT GASPELLTWA GKAVEQLRKI KSEAKVSMKT
PILSVALSAA SEGVEAIHAA LGDIAQAGRV VGKFDLVAKH AEESAAEGTP ETEVAVEASE
LGEPPAKKPK H