ID A0A016SU83_9BILA Unreviewed; 1007 AA.
AC A0A016SU83;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
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 Name=Acey_s0173.g402 {ECO:0000313|EMBL:EYB94288.1};
GN ORFNames=Y032_0173g402 {ECO:0000313|EMBL:EYB94288.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB94288.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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:EYB94288.1}.
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DR EMBL; JARK01001509; EYB94288.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016SU83; -.
DR STRING; 53326.A0A016SU83; -.
DR Proteomes; UP000024635; 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; 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; 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 PANTHER; PTHR11946:SF109; VALINE--TRNA LIGASE; 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|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:UP000024635}.
FT DOMAIN 93..681
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 725..876
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT COILED 12..45
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1007 AA; 114530 MW; EE4A1864599DAF82 CRC64;
MVSADQPRQK TEKELKKEAE KAAKLAKFEE KQRKLKEKAA AAEAKPKEKK VVKEQRTVVE
KPKYIPGQRP GEKKDISQGL PNVYDPSYVE SDWYSWWEKQ GFFKPEYGRG NNEKPNPKGH
FTICIPPPNV TGTLHVGHAL ATTVEDTLTR WNRMKGKTTL FNPGCDHAGI ATQVVVEKKL
QREKGLSRHD LGRDRFIQEV WKWKHEKGGV IYDQLRKMGA SVDWDRACFM MDPKMVRAVT
EAFVRMHESG TIYRSNRLVN WSCALRSAIS DIEVDKKELP GRTLLPVPGY DEKVEFGVLV
SFAYKIKGGE AEVVVSTTRV ETMLGDTAVA VHPEDPRYQH LIGKVGQRHN LPFITCIDDD
GNISPGCGEF SGMRRFDARK AVIEALKKRG LYRGSEDNAM VVPICSRSKD IIEPLLKAQW
YVKCDEMARR AVAAVESGEL KLIPDYHVAT WNRWLQSNRD WCISRQLWWG HRIPAYFITV
TDGKTPAGDP CDDHYWVSAH SEEIAIQKAA KKFNVDPKFI KLKWDEDVLD TWFSSGMWPF
AIMGWPENTS DMQLYFPSNV LETGHDILFF WVARMVFMSQ ELTGTLPFRE VYLHAMIRDA
HGRKMSKSLG NVIDPLDVIR GVTLAELNRQ LTSGNLDAKE LAIAQAGQAR DYPKGIPECG
TDALRFALLA YTSQGRDINL DVLRVQGYRF FCNKIWQAVR FTLMQLGSDY KAEPFRISGK
ESIMDKWILS RMAYAVDRCN HAMDVYNFTQ FTTTLYEFWL YDLCDIYLEA VKPVISSGTD
EARKVAKATL YHCVETGLRL ISPVMPFLSE ELWQHLPRLA THPPSIIVHA YPETSEYPFA
NEKIEADVSF AMSVVRTVRS LRSDYELTNK TKTDLYICVN VEEDHHCLTS LIPLIETLAS
SNKVEVFLDS GTNPKNIPDG CARTTISSRC TAYVALQGIV NVERELTKLA GKKEKNEALV
AKLLEQQHRP DYEEKVPLAV RITNTEKMEA LLAETRGIEA AMKALRS
//
