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Database: UniProt
Entry: A0A401UWU0_9CELL
LinkDB: A0A401UWU0_9CELL
Original site: A0A401UWU0_9CELL 
ID   A0A401UWU0_9CELL        Unreviewed;       889 AA.
AC   A0A401UWU0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Valine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02005};
DE            EC=6.1.1.9 {ECO:0000256|HAMAP-Rule:MF_02005};
DE   AltName: Full=Valyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02005};
DE            Short=ValRS {ECO:0000256|HAMAP-Rule:MF_02005};
GN   Name=valS {ECO:0000256|HAMAP-Rule:MF_02005,
GN   ECO:0000313|EMBL:GCD19060.1};
GN   ORFNames=CTKZ_06220 {ECO:0000313|EMBL:GCD19060.1};
OS   Cellulomonas algicola.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=2071633 {ECO:0000313|EMBL:GCD19060.1, ECO:0000313|Proteomes:UP000288246};
RN   [1] {ECO:0000313|EMBL:GCD19060.1, ECO:0000313|Proteomes:UP000288246}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TKZ-21 {ECO:0000313|EMBL:GCD19060.1,
RC   ECO:0000313|Proteomes:UP000288246};
RA   Yamamura H., Hayashi T., Hamada M., Serisawa Y., Matsuyama K., Nakagawa Y.,
RA   Otoguro M., Yanagida F., Hayakawa M.;
RT   "Draft genome sequence of Cellulomonas takizawaensis strain TKZ-21.";
RL   Submitted (NOV-2018) 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:0000256|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:0000256|ARBA:ARBA00001624, ECO:0000256|HAMAP-
CC         Rule:MF_02005};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02005}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_02005}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       ValS type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_02005}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GCD19060.1}.
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DR   EMBL; BHYL01000048; GCD19060.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401UWU0; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000288246; Unassembled WGS sequence.
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; HUPs; 2.
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   InterPro; IPR048044; Valyl-tRNA_ligase_actino.
DR   NCBIfam; NF000540; alt_ValS; 1.
DR   PANTHER; PTHR11946:SF93; VALINE--TRNA LIGASE, CHLOROPLASTIC/MITOCHONDRIAL 2; 1.
DR   PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 2.
DR   PRINTS; PR00986; TRNASYNTHVAL.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_02005};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_02005};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02005};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02005};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_02005};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_02005}.
FT   DOMAIN          36..117
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          147..643
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          683..832
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           63..73
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
FT   MOTIF           605..609
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         608
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
SQ   SEQUENCE   889 AA;  97439 MW;  01ECB701B6DEDEF2 CRC64;
     MSDLNPTAPT TTPGTTGTRA VPDKVSLDGL EDRWDSAWTA QGLYAFDRSR TREEIYSIDT
     PPPTVSGSLH VGHVFSYTHT DVVARFRRMR GSEVFYPMGW DDNGLPTERR VQNYYGVRCD
     PSLPYVEGFV PPHEGTDGKP VKPADQVPVS RRNFVELCER LTADDERQFE ALWRHLGLSV
     DWSMTYQTVS AEARAVAQQA FLRNLARGEA YQAEAPGLWD VTFQTAVAQA ELEARDYPGA
     FHRVAFHRAG AADAAEPVYI ETTRPELLPA CVALIAHPDD ERYQHLFGTT VTSPLFGVEL
     PVLAHPAAEP DKGAGIAMCC TFGDLTDVQW WRELQLPTRS VVGRDGRIVR ETPEWLTTDA
     GRAAFEELAG KTTFSAREAV VNGLRASGDL DGEPQATQRK ANFYEKGDKP LEIVTSRQWY
     IRNGGRDADL REGLLARGAE LDFHPDFMRV RYENWVGGLN GDWLISRQRF FGVPFPVWYR
     LDENGDPDHD APLLPTEDQL PIDPSSDVPA GYTADQRGVP GGFVGDPDVM DTWATSSLTP
     QIVGGWRTDP DLFARVFPMD LRPQGQDIIR TWLFSTVVRS HLEHGTLPWT DAAISGWILD
     PDRKKMSKSK GNVVTPMGLL EEHGSDAVRY WAASARLGTD AAFEVGQMKI GRRLAIKILN
     ASKFALSFGT AELDPALVTV TLDRAMLAGL ADVVAKATEA LESYDHTRAL ELSETFFWTF
     CDDYLELVKD RAYGAGAQEV SAETASARAA LGIALDTMLR LFAPVLPFAT EEVWSWWREG
     SVHRAPWPDA APLRAAAGDA DPGVVAAAGA ALAALRKVKS EAKVSMRTEI TAVTLAVPAA
     LRAGVDVALD DVRAAGRAVG SLDLVEQDGE QVVARDAVLA EPQPKAAQA
//
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