SYV_MYCPN
ID SYV_MYCPN Reviewed; 838 AA.
AC P75304;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 132.
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=MPN_480;
GN ORFNames=MP361;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
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; U00089; AAB96009.1; -; Genomic_DNA.
DR PIR; S73687; S73687.
DR RefSeq; NP_110168.1; NC_000912.1.
DR RefSeq; WP_010874836.1; NC_000912.1.
DR AlphaFoldDB; P75304; -.
DR SMR; P75304; -.
DR IntAct; P75304; 1.
DR STRING; 272634.MPN_480; -.
DR EnsemblBacteria; AAB96009; AAB96009; MPN_480.
DR KEGG; mpn:MPN_480; -.
DR PATRIC; fig|272634.6.peg.519; -.
DR HOGENOM; CLU_001493_0_2_14; -.
DR OMA; FATKLWN; -.
DR BioCyc; MPNE272634:G1GJ3-786-MON; -.
DR Proteomes; UP000000808; 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..838
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000106231"
FT COILED 768..838
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 46..56
FT /note="'HIGH' region"
FT MOTIF 514..518
FT /note="'KMSKS' region"
FT BINDING 517
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 838 AA; 95720 MW; B44C80058F7F223C CRC64;
MDKQFSFQGQ YDFKTVSTGL YDSWSSASFF KPQKNKVPFT AILPPPNLTG TLHIGHAFEV
SITDQIMRFK RLRGYGVNWI PGFDHAGIAT QTKYEKLARE TNPEYFQAPR KQKVKMIMDW
ALTQGDTIQS QIKSLGASLN WNQVNFTLSK KASQIVNDSF IQLFEQGFIY QAETLVNWDT
KLNTAISNIE VINKPVDQQL YYIAYKLANN PKKRLVVATT RPETIFVDVC LFVHPKDKHY
HSFVKQKVVN PLTGALMPVF TDSYVDKKFG TGVLKCTPAH DFNDFALNEK YRLPFVSCID
HNGLLNEHAK QFTGLTVSAA RQQVVEFLQT QKLLVKTMPL TSNVGFSERS DTVVEPLLSK
QWFVDLPKLK KALAIKKYPE LIPKRFNKQV TRWLSQLKPW CISRQLIWGH PIPVWTHKQS
GALHVGSTAP TDKQNYTQST DVLDTWFSSS LWPLICLDWH KNKHFVPTDL LVTGYDILFF
WVLRMTFNSY FQTKQLPFKQ VLIHGLVRDA QNRKMSKSLN NGINPMDLIR DYGADATRLF
LTSNHTPGDD LIFNEQKLKS AANFLNKLWN VTKYVLQLGE QAKTVPSTHL PSTLSERWIW
AKLKQLIVQT TKLLDKYQLA LANQALVNFI WNDFCNTFIE TIKQEDTALL PQLYTTAKTV
LSTAVVMLST VTPFLAERIY QQFHSGSVMQ ASWPTAKAVK PPKLFADVVE AVSSLRHYKA
NNQLVANQNL AVVLSGKAAP VVQNYFHFNW VDLRIEVNKT PGFQIKIVDN AANNLAHLEK
QRSFYLAEVQ RSQAITTNPA FLKKAPPHKV KAELLKLEEY QKKLAEVNHL IAKLTKAE
