ID A0A368G005_ANCCA Unreviewed; 1331 AA.
AC A0A368G005;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=valine--tRNA ligase {ECO:0000256|ARBA:ARBA00013169};
DE EC=6.1.1.9 {ECO:0000256|ARBA:ARBA00013169};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029936};
GN ORFNames=ANCCAN_18231 {ECO:0000313|EMBL:RCN35897.1};
OS Ancylostoma caninum (Dog hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=29170 {ECO:0000313|EMBL:RCN35897.1, ECO:0000313|Proteomes:UP000252519};
RN [1] {ECO:0000313|EMBL:RCN35897.1, ECO:0000313|Proteomes:UP000252519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Baltimore {ECO:0000313|EMBL:RCN35897.1,
RC ECO:0000313|Proteomes:UP000252519};
RA Mitreva M.;
RT "Draft genome of the hookworm Ancylostoma caninum.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
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:RCN35897.1}.
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DR EMBL; JOJR01000613; RCN35897.1; -; Genomic_DNA.
DR STRING; 29170.A0A368G005; -.
DR Proteomes; UP000252519; Unassembled WGS sequence.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd07962; Anticodon_Ia_Val; 1.
DR CDD; cd00817; ValRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033705; Anticodon_Ia_Val.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000357; HEAT.
DR InterPro; IPR021133; HEAT_type_2.
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; IPR002303; Valyl-tRNA_ligase.
DR NCBIfam; TIGR00422; valS; 1.
DR PANTHER; PTHR11946:SF109; VALINE--TRNA LIGASE; 1.
DR PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF02985; HEAT; 2.
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; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 8.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363035};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363035};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363035};
KW Reference proteome {ECO:0000313|Proteomes:UP000252519};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 20..58
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT REPEAT 97..135
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT REPEAT 174..212
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT REPEAT 252..290
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT REPEAT 291..328
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT REPEAT 334..372
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT REPEAT 373..411
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT REPEAT 412..450
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT DOMAIN 509..590
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 753..1027
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 1049..1199
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT COILED 1263..1290
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1331 AA; 149448 MW; 171FC1A63F2886DE CRC64;
MTTVVAQSPG HEESDDSLYP IAVLIDELRN EDVHLRLNSI RKLSTIALAL GVERTRNELI
QFLTDTIYDE DEVLLILADQ LGNFTPLVGG PDYVHCLLPP LENLATVEET VVRDKAVESL
RKIADKHSTA ALEEYFIPML KRLATGDWFT SRTSACGLFS VAYPRVSPAI KAELRSLFRQ
MCRDDTPMVR RAAAAKLGDF AKVFERDYLV DELHAMFCDL AVDEQDSVRL LAVEGCIAMA
GLLSEDSRRD LVRPVLSGLI DDKSWRVRFM VAEKLTEIQD AIGEEMTMTE LVPAFTNLLK
DPEGEVRGAA AQKLNTFCAN LKKSARESAI LNNILPVVKE LVTDPNQHVK TELAGVIMGL
APLVGKENTI SQLLPIYMQL LKDSTAEVRL NIISSLDKVN DVIGASQLSQ SLLPAIVELA
EDGKWRVRLA IVQFMPLLAA QLGQQFFDEK MLPLCLNWLC DHVQKKVVKE QRTVVEKPKY
IPGQRPGEKK DISQGLPNVY DPSYVEADWY SWWEKQGFFK PEYGRENNEK PNPKGHFTIC
IPPPNVTGTL HVGHALATTV EDTLTRWNRM KGKTTLFNPG CDHAGIATQV DKKELPGRTL
LPVPGYEEKV EFGVLVSFAY RIKGEESEVV VSTTRVETML GDTAVAVHPE DPRYQHLIGK
LPIVPDSFVD REFGTGAVKI TPAHDHNDYE VGQRHNLPFI TCIDDDGNIS PGCGKFSGMR
RFDARKAVIE ALKERGLYRG SEDNAMVVPV CSRSKDIIEP LLKAQWYVKC DEMARRAVAA
VESGELKLIP DYHVATWNRW LQSNRDWCIS RQLWWGHRIP AYFVTVTDGK TPAGDPCDDR
YWVSAHSEEI AVQKAAKKFN VDPKFIKLKW DEDVLDTWFS SGMWPFAIMG WPENTSDMQL
YFPSNVLETG HDILFFWVAR MVFMSQELTG KLPFKEVYLH AMIRDAHGRK MSKSLGNVID
PLDVIRGVTL AELNRQLTSG NLDAKELAIA QAGQARDYPK GIPECGTDAL RFALLAYTSQ
GRDINLDVLR VQGYRFFCNK ISGKESIMDK WILSRMACAV GRCNGEMDTY NFTQFTTTLY
EFWLYDLCDI YLEAVKPVIA SGSDEARKVA KATLYHCVET GLRLISPVMP FLSEELWQHL
PRLAIHPPSI IVHAYPETSE YPFANEKIEA DVSFAMSVIR TIRSLRSDYE LTNKTKTDLY
ASVSSEEDHR CLTSLIPLIE TLASSNKVEI LLQSKINPES IPSGCAHVTI SSRCTAYIAL
QGIINVEREL VKLAGKKEKN EAQVAKLLEQ QNRPDYEEKV PLPVRIANAE KKEALLIEMK
SIEAAMAALS G
//
