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
//