ID S7KJF8_9CHLA Unreviewed; 941 AA.
AC S7KJF8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Valine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02004};
DE EC=6.1.1.9 {ECO:0000256|HAMAP-Rule:MF_02004};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02004};
DE Short=ValRS {ECO:0000256|HAMAP-Rule:MF_02004};
GN Name=valS {ECO:0000256|HAMAP-Rule:MF_02004,
GN ECO:0000313|EMBL:EPP34565.1};
GN ORFNames=CP10139811_0385 {ECO:0000313|EMBL:EPP34565.1};
OS Chlamydia ibidis.
OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=1405396 {ECO:0000313|EMBL:EPP34565.1, ECO:0000313|Proteomes:UP000016200};
RN [1] {ECO:0000313|EMBL:EPP34565.1, ECO:0000313|Proteomes:UP000016200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10_1398_11 {ECO:0000313|EMBL:EPP34565.1,
RC ECO:0000313|Proteomes:UP000016200};
RA Huot-Creasy H., McCracken C.L., Humphries M., Sachse K., Laroucau K.,
RA Bavoil P., Myers G.S.;
RT "Genome sequence of Chlamydia psittaci 10-1398/11.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|ARBA:ARBA00001624, ECO:0000256|HAMAP-
CC Rule:MF_02004};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02004}.
CC -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC activity. {ECO:0000256|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:0000256|HAMAP-Rule:MF_02004}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_02004}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPP34565.1}.
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DR EMBL; ATNB01000159; EPP34565.1; -; Genomic_DNA.
DR RefSeq; WP_020370382.1; NZ_KE360208.1.
DR AlphaFoldDB; S7KJF8; -.
DR PATRIC; fig|1238237.3.peg.506; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_0; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000016200; Unassembled WGS sequence.
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 CDD; cd00817; ValRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.287.380; Valyl-tRNA synthetase, C-terminal domain; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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 NCBIfam; TIGR00422; valS; 1.
DR PANTHER; PTHR11946:SF93; VALINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR PRINTS; PR00986; TRNASYNTHVAL.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF46589; tRNA-binding arm; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_02004};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02004}; Coiled coil {ECO:0000256|HAMAP-Rule:MF_02004};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02004};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02004};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02004};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02004}.
FT DOMAIN 19..526
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 564..603
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 652..820
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT COILED 873..903
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 47..57
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 565..569
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 568
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 941 AA; 107732 MW; A2C211FF8D53A5F4 CRC64;
MEEDVFPKVY DPKGVEEELY AFWEQSGMFL AQSSSNKLPY AIVMPPPNVT GILHMGHALV
NTLQDVLIRY KRMSGYEVCW IPGTDHAGIA TQTVVERHLY ASLGKRRMEF SREEFLEHIW
AWKEKSESVI LSQLRQLGCS CDWSRLRFTM EPLANRAVKK AFKCLFDKKY IYRGYYLVNW
DPTLQTALAD DEVEYEEQDG WLYYINYKVL GRDDEYLTVA TTRPETLLGD TAIAVSPNDE
RYAHLIGSTV MVPFVDREIP VIADISVDPS FGTGAVKITP AHDKDDYRMG INHDLPMINI
LTPSGDINEN GGIFAGLSKE QARVDIIAAL EAKGLFVKKQ PYKVRIGVSY RSGAVIEPYL
SKQWFVSVEH FRDQLREFVA SDSITIFPSE FKRNYLAWVN NLRDWCISRQ LWWGHRIPVW
YHRENEDRII CYDGDGEPEE VTKDPSSWYQ ESDVLDTWFS SGLWPLTCLG WPDVNSEDLK
KFYPTSVLVT GHDILFFWVT RMILLCSAMV DKKPFSDVFL HGLIFGKSYK RYNDIGEWHY
ISGLEKHEYD MGKPLPDNVV AKWEKLSKSK GNVIDPIEMI SKYGADAVRM TLCSCANRGE
QIDLDYRLFE EFKNFANKLW NGARFIFGHI SELTGTDLLD GIDESLLGLE DFYIIDGFNN
LLAQLEHAYA NYAFDKIASS GYEFFRKNLC STYLEIIKPT LFGKQGSDRE RLTKRKLLAV
LLINILGVLH PIVPFVTETL FLKVKKELGD IPSGMGDNIT GHALDMLRSS ACMLASYPKP
LSVAIPKDLH ESFTLAERLV YTIRNIRGEM QLDMRVPLQA FVCSIDMDIS QYLPMMQALG
GLSSVEILTE EPTDRLYSLG VVDSIRLGIY VPQEHLDKEM IRLEKEKTRL ENAIASAERL
LSSDDFRAKA NPDLVRNKEE SLKNNRVELQ SILDKLASFS K
//
