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Database: UniProt
Entry: A0A497XQ44_9AQUI
LinkDB: A0A497XQ44_9AQUI
Original site: A0A497XQ44_9AQUI 
ID   A0A497XQ44_9AQUI        Unreviewed;      1171 AA.
AC   A0A497XQ44;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
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   ORFNames=BCF55_0645 {ECO:0000313|EMBL:RLJ70374.1};
OS   Hydrogenivirga caldilitoris.
OC   Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Hydrogenivirga.
OX   NCBI_TaxID=246264 {ECO:0000313|EMBL:RLJ70374.1, ECO:0000313|Proteomes:UP000267841};
RN   [1] {ECO:0000313|EMBL:RLJ70374.1, ECO:0000313|Proteomes:UP000267841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16510 {ECO:0000313|EMBL:RLJ70374.1,
RC   ECO:0000313|Proteomes:UP000267841};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (OCT-2018) 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:RLJ70374.1}.
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DR   EMBL; RCCJ01000001; RLJ70374.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A497XQ44; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000267841; 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; 3.
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; IPR019499; Val-tRNA_synth_tRNA-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   InterPro; IPR002303; Valyl-tRNA_ligase.
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; 3.
DR   Pfam; PF10458; Val_tRNA-synt_C; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000267841}.
FT   DOMAIN          16..389
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          546..605
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          709..842
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          885..1047
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   DOMAIN          1105..1167
FT                   /note="Valyl-tRNA synthetase tRNA-binding arm"
FT                   /evidence="ECO:0000259|Pfam:PF10458"
FT   COILED          1106..1171
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT   MOTIF           44..54
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT   MOTIF           802..806
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT   BINDING         805
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   1171 AA;  137146 MW;  40120FDC225CFF1A CRC64;
     MKELKEYNPK EIEEKWSRFW IEKAIYHVEK PDKRKKFSVV IPPPNVTGSL HMGHALNSTL
     QDIIARWQRM KGRQVVWVPG FDHAGIATQY VVDKQLQEEG KSRLELGRQE FLKKVWEWVP
     KSRNAIRTQL EKLGVSVDWK RERFTLDEGF SRAVRKAFRE LYERGLIYRS EYIINWCPKD
     LTALSDLEVE HEEEKGKLWY IKYPLEDGSG YVTVATTRPE TMLGDTAVAV NPEDERYKNL
     IGKRLRLPLV RWKRKTLTGE EIDELIPIIA DERVKPEFGT GAVKVTPAHD PNDFEIGKAH
     ALPFVRVMDE RAHMNENAGD FAGLDRYEAR KRILERLKEE GFLEKEEDHV HAVGKCYRCK
     TVVEPMVSEQ WFVKVSDPAI KDISIKVVEE GIEEEEEKEV FLQLAEVEGL SITIPVNDEI
     SGGTRSVVIL SEGIEFLAGV REGELAYVYY PSGREEVISK AKELAYEFMK KPYGLEFLIG
     VDGEISVIKQ GIESRVERGR YLIASEGNRL NLYRWGTEGY EYLQMLESGQ ARLEPVQKSI
     RVKVEREKRR EVHKRQVKFI PEQWRKFYLD WMHNLRDWCI SRQIWWGHRI PVWYCQECGE
     ANVFTDDDFD RVYDKLIFNL IADGKVGTEF TPEEIEGILH SPDFVHPEMT VLDFYKKFVF
     HRYHSTNVDA NSLRLFFTQE ANPMAMLTPG VSTRGLYRYD SKSKKWRMVL KCKKCRSENL
     KQEEDVLDTW FSSALWPFGV FGWPESSEDL KNLYPTDLLV TGFDIIFFWV ARMIMMGTYF
     MEDIPFHDVY VHALVRDEKG QKMSKTKGNV IDPLEIIDKY GADALRFTLA ILTVQGRDIK
     LSEKRFEGYK HFANKIWNAS RFVLMNTPED FISTLPYMAP LKPEDKWIMT LLNETADKVS
     KALENYDFSQ AAQSIYDFFW SDFCDWYIEF TKERIYRETP EGEDEDTKKE KAKVISERTT
     ALYTLHYVLE KALRILHPFM PYITEELWHK LPASDGESIS LKDFPEKKQE ELFPEETERI
     ERLKEIISAI RSLRSDLQIE PSKRLRAFYK AGKDLSREVV GEFKNHILNL ARLEEFTEVS
     ERPENTVATF SKDVEIYISI EGHVDIDKLT ESYERKKEKL LAELERVKGK LSNENFVRKA
     PPDVVEKEKR IKEELEEDLK KVERILGVLK S
//
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