ID A0A2C8ZWN6_9MICO Unreviewed; 878 AA.
AC A0A2C8ZWN6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 ORFNames=SAMN06296378_2206 {ECO:0000313|EMBL:SOE70354.1};
OS Salinibacterium xinjiangense.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Salinibacterium.
OX NCBI_TaxID=386302 {ECO:0000313|EMBL:SOE70354.1, ECO:0000313|Proteomes:UP000219440};
RN [1] {ECO:0000313|EMBL:SOE70354.1, ECO:0000313|Proteomes:UP000219440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.05381 {ECO:0000313|EMBL:SOE70354.1,
RC ECO:0000313|Proteomes:UP000219440};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) 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}.
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DR EMBL; OCST01000004; SOE70354.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C8ZWN6; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000219440; 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}; Reference proteome {ECO:0000313|Proteomes:UP000219440}.
FT DOMAIN 39..125
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 153..643
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 685..824
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 71..81
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 BINDING 608
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
SQ SEQUENCE 878 AA; 96455 MW; A9A3E5B25B0BEC23 CRC64;
MSCRDRDTDS VPHISNWSTA LSPAIPEKPA LEGLEDKWAP QWEARGVYQF DRDAALAAGS
AELFSVDTPP PTASGSLHIG HVFSYTHMDL VTRFQRMRGK HIFYPMGWDD NGLPTERRVQ
NYYGVRCDPT LAYDPAFTPP LQGGDNASSK AADQLPISRR NFIELCETLT AEDEKQFEDL
WRQLGLSVDW KLTYRTIGHE AQLAAQRAFV RNLGRGEAYQ AEAPTLWDIT FRTAVAQAEL
EDKEQPAAYH RLAFHRPGGD DVHIETTRPE LLAACVALVA HPDDERYQAL FGTTVTTPIF
GVEVPVVAHH LAQKDKGSGI AMICTFGDVT DVVWWRELDL PNRTIIGADG RIVADAPEAI
ETDAARAAYA ELAGKTVFSA KAAMVELLKA SGEMIGDARP ITHSVKFFEK GDKPLEIIST
RQWYIKNGAR DADLRARLVE AGKQIGFTPD HMRVRYENWV GGLTGDWLIS RQRFFGVPIP
VWYHLDADGA KGEPIVPPED RLPIDPSSDV PDGFIEADRG VTFVGELDIM DTWATSSLTP
QIAGGWVTDP ELFDLVFPYS LRSQGQDIIR TWLFSTVLRA ELEEGRIPWK NAGISGFIVD
PDRKKMSKSK GNVVTPKGML DDHGSDAVRY WAASSRLGTD AAFDPQNPKQ IKIGRRLAIK
VLNAAKFVYS FPEADGAVTV PLDIDMLGEL NSVIEAATKA LDEFDHAKAL EVTEKFFWTF
CDDYLELVKE RAYGAGTPEA HASATTALRT AIDVLLRLLA PYLPFATEEV WSWTHDDSVH
TSAWPTAADT GVVAAPTGLL GAVSAALIGI RRAKTDAKAS QKSDVTSATI AGPAMLELAL
DDLSAVGRIA SVEFVESESI EVRDIVLAEV AELPTEGV
//
