SYV_ONYPE
ID SYV_ONYPE Reviewed; 882 AA.
AC Q6YRJ6;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 108.
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=PAM_018;
OS Onion yellows phytoplasma (strain OY-M).
OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC Candidatus Phytoplasma; Candidatus Phytoplasma asteris.
OX NCBI_TaxID=262768;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OY-M;
RX PubMed=14661021; DOI=10.1038/ng1277;
RA Oshima K., Kakizawa S., Nishigawa H., Jung H.-Y., Wei W., Suzuki S.,
RA Arashida R., Nakata D., Miyata S., Ugaki M., Namba S.;
RT "Reductive evolution suggested from the complete genome sequence of a
RT plant-pathogenic phytoplasma.";
RL Nat. Genet. 36:27-29(2004).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD04103.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AP006628; BAD04103.1; ALT_FRAME; Genomic_DNA.
DR AlphaFoldDB; Q6YRJ6; -.
DR SMR; Q6YRJ6; -.
DR STRING; 262768.PAM_018; -.
DR EnsemblBacteria; BAD04103; BAD04103; PAM_018.
DR KEGG; poy:PAM_018; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_14; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000002523; 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; 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; 2.
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..882
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224522"
FT COILED 849..873
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 42..52
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 882 AA; 103099 MW; B17DE16AE8C0900A CRC64;
MQTKYDFKKV EHQRYQQWLE KKYFCANPNA NKKTFTVVIP PPNVTGKLHL GHAWNNTIQD
IIIRFKKMQG FDVLFLPGMD HAGIATQNKV KEQLKQEGLL TKTLSKEIFL KYAWQWKEEH
AQNIRQQWQV LGLHLDYNFE KFTLDPDLSQ QVQEVFGKLF QKKLIYRDYK IINWDPETKT
ALSNVEVNYH ETEGKLYYIK YFLVDFPTNS NLSDASLVPS FLEIATTRPE TMFADQALMV
NPNDPRYQSF IGKKVFIPDT NIQIPVISDN YVDINFGTGV VKVTPGHDIN DFEVAKRHQL
KALLCMNEDG TMNDLALQYQ GLDRFVCRQK LVQTLKQKGF FTKTENHLHK VGYSSISDAI
IEPRLSLQWV LKTKAIAQIA LKTNKINFFP LRFENIFNNW LQNIEDWCIS RQLWWGHQIP
AWHKGQEIKV QIESPGPEWS LDCDVLDTWF SSALWPFSTL GWPNCNAPLF QNRFPTDVLV
TGYDILTFWV SKMVFQSILL THKDPFKDVL LHGLVRDNKG QKMSKSKGNG VDPLEVVAKY
GTDALRWFLT TNAAPGFDLF YDETKVASSW NFINKLWNIS RFVKLNTSTL DTDFDINLLT
LTQKALLTQL HLTTQKVTTL YQKYELKEIG KILYHFVWED FANWHLEFAK HDLDQNNSNL
TNLHNSQKFL VYMMKHILQL LHPFIPFVTD ALYENFDNKT NITQTTLQKT SYCNLDALAD
FENLKNLIIK TRHLRQESNI NCKLNLELEV ASQFSTILQD FVNLQQALEK FFKTLQIKIT
NKVTNSKKTI WLIEKNLSLY IDRKTLNELN ETKFESNFLQ QKNTLLKEIK RSETILNNPS
FLQKAASAKI EIEKKKYESY CKQYKKLLES KNNSNPLNPN KK
