ID A0A1I0PI45_9EURY Unreviewed; 887 AA.
AC A0A1I0PI45;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Valine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02005};
DE EC=6.1.1.9 {ECO:0000256|HAMAP-Rule:MF_02005};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02005};
DE Short=ValRS {ECO:0000256|HAMAP-Rule:MF_02005};
GN Name=valS {ECO:0000256|HAMAP-Rule:MF_02005};
GN ORFNames=SAMN05216285_2585 {ECO:0000313|EMBL:SEW13932.1};
OS Natrinema salifodinae.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=1202768 {ECO:0000313|EMBL:SEW13932.1, ECO:0000313|Proteomes:UP000183275};
RN [1] {ECO:0000313|Proteomes:UP000183275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12284 {ECO:0000313|Proteomes:UP000183275};
RA Varghese N.;
RL Submitted (OCT-2016) 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_02005}.
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_02005};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02005}.
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_02005}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_02005}.
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DR EMBL; FOIS01000003; SEW13932.1; -; Genomic_DNA.
DR RefSeq; WP_049992124.1; NZ_JROF01000050.1.
DR AlphaFoldDB; A0A1I0PI45; -.
DR STRING; 1202768.SAMN05216285_2585; -.
DR eggNOG; arCOG00808; Archaea.
DR OrthoDB; 23906at2157; -.
DR Proteomes; UP000183275; 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 Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR HAMAP; MF_02005; Val_tRNA_synth_type2; 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; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR022874; Valine-tRNA_ligase_type_2.
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; 1.
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; 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_02005};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02005}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02005};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02005};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02005};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02005}; Reference proteome {ECO:0000313|Proteomes:UP000183275}.
FT DOMAIN 27..589
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 632..774
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 58..68
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
FT MOTIF 554..558
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
FT BINDING 557
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
SQ SEQUENCE 887 AA; 101874 MW; C37A2443FCDFD667 CRC64;
MSMDAPEQTD EPSLDGDYDP EAVETRWQRR WVDEDVYAYD GNAKRDPNTV YSIDTPPPTV
SGSLHMGHLY GHTLQDFAAR FQRMADGDVL FPFGYDDNGI ASERLTEKEL DIRHQDYERR
EFQELCREVC QQYEDEFTEK MQGLGCSIDW NNTYKTIEPR VQRISQLSFL DLYEKDREYR
KKAPAIWCPE CETAISQVEM EDDERGSHFN DIAFEVVGED APREEFVIST TRPELIPACV
SVFVHPDDDE NQDLVGETAR VPIFEQEVPI IADERVDMEK GSGVVMCCTF GDQNDIEWYQ
AHDLPLRVAI DESATMTDLA GDYEGMSTEE AREAIVEDLD DEGYLRDRWE ISHAVQVHER
CDTPVEFRVS KQWYVEILDH KEEYLEAGRE MDWYPEKMFT RYKHWIEGLE WDWLISRQRD
SGIPFPVWYC ADCDHEIMAD RENLPVDPLS DEPPVDSCPE CGHDEFVAEE DVFDTWATSS
LTPLINAGWD WDAEAEEFAM DNPELYPFDL RPQGHDIISF WLFHTIVKCY EHTGEVPFDA
TMINGHVLDE NREKMSKSRG NVVAPDEVLA EYPVDAVRFW AASAAVGDDF PYQEKDLTAG
EKLLRKLWNA SKLVDTLAPR EPDEPADLDA IDRWLLAELD DAIEDLTAHL EAYEFAKARD
RLRTFFWNTF CDDYLEIAKQ REDEPSTQYA LRTAHRTFLE LWAPFLPHAT EEIWQAVYAD
GDEELDATSI HTRDWPAPQG HEADLEAGET AMEVISALRR YKSENQLPLN ADLESVSVFG
PIAGFEDAIQ NVMHVQELTV LEEPPEISTE VASIDLDYST LGPKFGSKVG EIDSGIESGD
YEIDDEADVL RVADEELEDD LFEVEYERTY SGEGEMLETE SAVVILG
//