SYV_MANSM
ID SYV_MANSM Reviewed; 954 AA.
AC Q65S97;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-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=MS1556;
OS Mannheimia succiniciproducens (strain MBEL55E).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Basfia.
OX NCBI_TaxID=221988;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBEL55E;
RX PubMed=15378067; DOI=10.1038/nbt1010;
RA Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA Jeong H., Hur C.G., Kim J.J.;
RT "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT succiniciproducens.";
RL Nat. Biotechnol. 22:1275-1281(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; AE016827; AAU38163.1; -; Genomic_DNA.
DR RefSeq; WP_011200728.1; NC_006300.1.
DR AlphaFoldDB; Q65S97; -.
DR SMR; Q65S97; -.
DR STRING; 221988.MS1556; -.
DR EnsemblBacteria; AAU38163; AAU38163; MS1556.
DR KEGG; msu:MS1556; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_6; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000000607; 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; -; 2.
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; IPR019499; Val-tRNA_synth_tRNA-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 Pfam; PF10458; Val_tRNA-synt_C; 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.
FT CHAIN 1..954
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224502"
FT COILED 886..954
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 48..58
FT /note="'HIGH' region"
FT MOTIF 560..564
FT /note="'KMSKS' region"
FT BINDING 563
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 954 AA; 108962 MW; A64D3A5F4921EAB4 CRC64;
MTQKLQMADR FDASAVEQAL YNHWEQKGYF KPSYDAGRPS YSIAIPPPNV TGSLHMGHAF
QQTLMDTLIR YHRMQGDNTL WQAGTDHAGI ATQMVVERKI AAEENKTRHD YGREAFIEKI
WDWKAYSGGT ISQQMRRLGN SIDWERERFT MDEGLSEAVK EVFVRLHEEG LIYRGKRLVN
WDPKLHTAIS DLEVENKESK GSLWHFRYPL AKGAKTAEGL DYLVVATTRP ETVLGDTAVA
VHPEDERYQS LIGKTVVLPL ANREIPIVAD EYVDREFGTG VVKITPAHDF NDYEVGKRHN
LPMVNVMTFN ADIREEAEII GTDGQPLTTY EAEIPQDYRG LERFAARKKV VADFDSLGLL
EKIQPHDLKV PYGDRGGVPI EPMLTDQWYV SVKPLAETAI KAVEEGEIQF VPKQYENLYY
SWMRDIQDWC ISRQLWWGHR IPAWYDEQGN VYVGRSEEEV RSKNGLNSSV ALRQDEDVLD
TWFSSALWTF STLGWPQQTK ELAMFHPTNV LITGFDIIFF WVARMIMMTM HFIKDENGKP
QVPFKTVYVT GLIRDEQGQK MSKSKGNVID PLDMIDGIDL ESLLAKRTGN MMQPQLAEKI
AKATKKEFPE GIQPHGTDAL RFTLSALAST GRDINWDMKR LEGYRNFCNK LWNASRFVLT
NDKLDLSTGE RELSLADKWI QAEFNKTVQN FRNALDQYRF DLAATELYEF TWNQFCDWYL
ELTKPVFANG TDAQIRAASF TLVNVLEKLL RLAHPLIPFI TEEIWQKVKD FAGVEGETIM
TQPFPAFDEA LVNDEAVAQI SWIKEVITAV RNIRAESNIA PSKGLDLLLR NLPDTEQKTL
ENNRTLMQIM AKLDSVKVLA QDEEAPLSVA KLVGSAELLV PMAGFINKDT ELARLNKEIE
KLIGEVKRIE GKLGNEAFVA KAPEAVIAKE REKMQDYQEG LEKLRAQYLS IENL
