SYV_MYCMO
ID SYV_MYCMO Reviewed; 839 AA.
AC Q6KID2;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=MMOB1580;
OS Mycoplasma mobile (strain ATCC 43663 / 163K / NCTC 11711) (Mesomycoplasma
OS mobile).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX NCBI_TaxID=267748;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43663 / 163K / NCTC 11711;
RX PubMed=15289470; DOI=10.1101/gr.2674004;
RA Jaffe J.D., Stange-Thomann N., Smith C., DeCaprio D., Fisher S., Butler J.,
RA Calvo S., Elkins T., FitzGerald M.G., Hafez N., Kodira C.D., Major J.,
RA Wang S., Wilkinson J., Nicol R., Nusbaum C., Birren B., Berg H.C.,
RA Church G.M.;
RT "The complete genome and proteome of Mycoplasma mobile.";
RL Genome Res. 14:1447-1461(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}.
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DR EMBL; AE017308; AAT27644.1; -; Genomic_DNA.
DR RefSeq; WP_011264678.1; NC_006908.1.
DR AlphaFoldDB; Q6KID2; -.
DR SMR; Q6KID2; -.
DR STRING; 267748.MMOB1580; -.
DR EnsemblBacteria; AAT27644; AAT27644; MMOB1580.
DR KEGG; mmo:MMOB1580; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_14; -.
DR OMA; RQWYIRN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000009072; 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; -; 3.
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; 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; 1.
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..839
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224511"
FT COILED 315..343
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT COILED 813..839
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 41..51
FT /note="'HIGH' region"
FT MOTIF 517..521
FT /note="'KMSKS' region"
FT BINDING 520
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 839 AA; 99399 MW; 95C1AA9615212B7E CRC64;
MEKIYNHKIV EKDKNEKWIK KEYFSTHDLT KKPFSILLPP PNVTGKLHIG HAWNTTLQDF
LIRLKRLQGY DVLWLPGTDH AGIATQAKVE KRLLDQKIFK SDLTKEELFE KAMDWKNEYA
NEIKKQWSKL GLALDYKKER FTLDELSNKA VNDIFVMLYK DGYIYRGNRA IYYDTFLQTS
LSNIEVINVE KESKMYYLKY FLENSNSEYV LVATTRPETL ASDVALIINP NDKKNSHYLG
KNFVNPLTKK IIKMHSDDYA IMNFGSGIVK ISAHDMNDFD VIKRLNLEVI ETIDKFGKMT
NAIPEFENMS SLEARENIVL KLKKENLIDK IENIKSNIIM SERSNTVAEV LVMPQWFIKM
EPFSKMILKK IQNENEDDKK VLFFPKKFEN ILKIWMQEAH DWNISRQLWW GHKIPAWYDE
KGNIKVQTTS PGSNWTQDQD VLDTWFSSGI APFSFLNWPQ KSEFLKRYYP TSVIVTAYDI
IFFWVARMYF MGIYSMKNIP FKKALIHGLI RDEQGRKMSK SLGNGIDPMD LIEKYGADSL
RWFLMTNSTP GQDIRFNYDK IESAWSLINK IWNISRYIKM LDSDKKEIIP EEIEQNANSW
ILEKFENLKI LIYEKSETFE FSVIGKEIFK FINEDFSSVY IEIIKGTDSK EFISKIWSNF
LILLHPFLPF LTDHLYFELN KKELLESDFF ELKSRKNNLF IDETIEIIST LREYRTRFNL
SHKIDLNYNL VSINNSNQCD FNLDLKKYLI KKMANANFSE NGQIFFKLNN YELRLQIPEE
VKKEEETIRI KRILFLESEI KRSQSILSNE KFINNASEIK VKEEKEKLEK YIKEFEEIK
