SYV_PARUW
ID SYV_PARUW Reviewed; 949 AA.
AC Q6MAM1;
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=pc1654;
OS Protochlamydia amoebophila (strain UWE25).
OC Bacteria; Chlamydiae; Parachlamydiales; Parachlamydiaceae;
OC Candidatus Protochlamydia.
OX NCBI_TaxID=264201;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UWE25;
RX PubMed=15073324; DOI=10.1126/science.1096330;
RA Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U.,
RA Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T.,
RA Mewes H.-W., Wagner M.;
RT "Illuminating the evolutionary history of chlamydiae.";
RL Science 304:728-730(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; BX908798; CAF24378.1; -; Genomic_DNA.
DR RefSeq; WP_011176200.1; NC_005861.1.
DR AlphaFoldDB; Q6MAM1; -.
DR SMR; Q6MAM1; -.
DR STRING; 264201.pc1654; -.
DR PRIDE; Q6MAM1; -.
DR EnsemblBacteria; CAF24378; CAF24378; PC_RS07910.
DR KEGG; pcu:PC_RS07910; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_0; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000000529; 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; 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; 2.
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; Reference proteome.
FT CHAIN 1..949
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224523"
FT COILED 882..949
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 45..55
FT /note="'HIGH' region"
FT MOTIF 561..565
FT /note="'KMSKS' region"
FT BINDING 564
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 949 AA; 110265 MW; 2BD68DE583E4FA25 CRC64;
MTELPKAYEA KKIDEKWYQF WDAKRYFTAN PLSNKPTYCI VIPPPNVTGV LHMGHALVNT
VQDILIRWKR MLGFETLWVP GTDHAGIATQ MVVERHLIKT EGKKRTDYTR EEFLKHVWTW
KEKSENRIIE QLKRLGNSCD WTRLRFTMDE NNSLAVRTMF KKLFDDGLIY RGDYLVNWDP
HTQTALADDE VEYEDKQSFL WYFKYPLRDE SEFISIATTR PETMLGDTAV AVSPNDERFK
HLIGKEIRLP LMNRLIPIIA DHHVDPSFGT GVVKITPAHD PNDYQIGLSH RLPFINIMTP
DGKINENGGH FQGLSMTEAR HAVVSEMKEK GLLEKVEPHL NRVGISYRSK AIIEPYLSKQ
WFVKMDGFSK KLREVVQNGQ VKLIPSHWES TYFHWIDNLR DWCISRQLWW GHRIPIWYHK
EDSNRLICYA GSDLPDEVKN APEEWIQDSD VLDTWFSSAL WPFSTLGWPE QTSELAKFYP
TSVLVTGHDI LFFWVARMIL MGDYALDQPP FPETYLLGLI YGKSYWRQES NGGILYVNEQ
ERSDFDMGKP IPKEVFSKWE KMSKSKGNII DPLEMIDQFG TDAVRMALCA SATQARQIDL
DRRRFEEFKN FTNKIWNGAR FVLMNLDGNE QNRTMSLTSQ GFSQGLDEAL FTLEDRWILS
VLNRTVESVN VHLNHYQFDQ AAIEAYDFFW KEFCAYYVEI AKPILFGKIG TAQERTNKQK
LLVIVLCQAI RLIHPMAPFI TEELFHILKE RLEGVEALTN ADPYTKECIQ ALQSSACLVA
PYPVRIGEKN QKVEAVFALM EQIVYTIRNI RGEMKLSPGT ATDVYIIGQA DDPEWQSARE
HITMISALVK TRRILVETEE PKIGFACTGV YHALKIQLPL PEELLKQEKT RLNKEQEKLE
ISLEKLKNQL SNTDFVRRAP AHLTEKQNQQ LSQTEQELRE IKEKLMTLP
