GenomeNet

Database: UniProt
Entry: A0A1I0PI45_9EURY
LinkDB: A0A1I0PI45_9EURY
Original site: A0A1I0PI45_9EURY 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system