SYV_PORG3
ID SYV_PORG3 Reviewed; 876 AA.
AC B2RK53;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=PGN_1229;
OS Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM
OS 12257 / NCTC 11834 / 2561).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=431947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561;
RX PubMed=18524787; DOI=10.1093/dnares/dsn013;
RA Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
RA Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
RA Nakayama K.;
RT "Determination of the genome sequence of Porphyromonas gingivalis strain
RT ATCC 33277 and genomic comparison with strain W83 revealed extensive genome
RT rearrangements in P. gingivalis.";
RL DNA Res. 15:215-225(2008).
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; AP009380; BAG33748.1; -; Genomic_DNA.
DR RefSeq; WP_012458123.1; NZ_CP025930.1.
DR AlphaFoldDB; B2RK53; -.
DR SMR; B2RK53; -.
DR STRING; 431947.PGN_1229; -.
DR EnsemblBacteria; BAG33748; BAG33748; PGN_1229.
DR GeneID; 29256433; -.
DR KEGG; pgn:PGN_1229; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_10; -.
DR OMA; FATKLWN; -.
DR BioCyc; PGIN431947:G1G2V-1404-MON; -.
DR Proteomes; UP000008842; 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; 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..876
FT /note="Valine--tRNA ligase"
FT /id="PRO_1000189242"
FT COILED 804..876
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 43..53
FT /note="'HIGH' region"
FT MOTIF 533..537
FT /note="'KMSKS' region"
FT BINDING 536
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 876 AA; 100258 MW; 434B5CDB77401299 CRC64;
MEIASKYNPE EVESKWYNYW MEYGCFISVP DGRKPYTVVI PPPNVTGVLH MGHMLNNTIQ
DILVRRARMK GYNACWVPGT DHASIATEAK VVGRLAAQGI SKQDLGREEF LRHAWDWTHE
HGGIILEQLK RLGASCDWTR TAFTMDESRS ESVIKVFVDL YNKGLIYRGI RVVNWDPKAL
TALSDEEVIY KETNGKLYYL RYFVENEPDK YIIVATTRPE TIMGDTAVCV NPNDERYRWL
RGKRVIVPTV GRAVPIIEDE YVDMEFGTGC LKVTPAHDVN DYMLGQKHRL ESIDIFHDNG
ILNEHGGPYA GMDRFDVRKK IEQDLIDAGL MERVENYVNK VGYSERTDVP IEPKLSMQWF
LQMESLAKSA LDAVMNDEIK LHPAKFKNTY RHWMENVKDW CISRQLWWGH RIPAYYLPDG
SIVVAETAEK AVELARKQTG SDSLTAEDLR QDSDSLDTWF SSWLWPISVF GDVMDPENEE
LDYYYPTSDL VTAPDILFFW VARMIMAGYE YRGKKPFDNV YLTGIVRDGQ GRKMSKSLGN
SPDPIMLMEK YGADGVRMGL MMAAPAGNDV LFDESLSEQG RNFCNKIWNA FRLVKGWQQA
ETATQPEASA LAVKWFGYRL DEVKTELDDL FSKYRLSEAL TLVYKLFWDD FSSWYLEMVK
PAYGQPMDAK TYGSTIGFFD QLLRLLHPFM PFITEELWHA LASRHDGETI MLCLLPDAHE
TDRDFLQAFD RTREIIAAIR NIRTGKNVPF KEKLTLEAGN EHDASFDAVI IKMGNLEAIN
RVEEKTSGST SFLIGTLEYA IPMGALIDVE EEIKKLSDEL AYQEKFLASV MKKLGNESFV
AKAPQAVIEL EQKKKSDAEA RIATLRDSLN QLQSTK
