ID   Q26178_PLAVI            Unreviewed;      1287 AA.
AC   Q26178;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 110.
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=GAM1 {ECO:0000313|EMBL:CAA59220.1};
OS   Plasmodium vivax (malaria parasite P. vivax).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX   NCBI_TaxID=5855 {ECO:0000313|EMBL:CAA59220.1};
RN   [1] {ECO:0000313|EMBL:CAA59220.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=7630377; DOI=10.1016/0166-6851(94)00040-T;
RA   Snewin V.A., Khouri E., Wattavidanage J., Perera L., Premawansa S.,
RA   Mendis K.N., David P.H.;
RT   "A new polymorphic marker for PCR typing of Plasmodium vivax parasites.";
RL   Mol. Biochem. Parasitol. 71:135-138(1995).
RN   [2] {ECO:0000313|EMBL:CAA59220.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=8964490; DOI=10.1016/0378-1119(96)00235-1;
RA   Snewin V.A., Khouri E., Mattei D., Tekaia F., Delarue M., Mendis K.N.,
RA   David P.H.;
RT   "Cloning and characterisation of a gene from Plasmodium vivax and P.
RT   knowlesi: homology with valine-tRNA synthetase.";
RL   Gene 173:137-145(1996).
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}.
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DR   EMBL; X84734; CAA59220.1; -; Genomic_DNA.
DR   VEuPathDB; PlasmoDB:PVP01_0829000; -.
DR   VEuPathDB; PlasmoDB:PVW1_080034600; -.
DR   VEuPathDB; PlasmoDB:PVX_119665; -.
DR   HOGENOM; CLU_005529_0_0_1; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004832; F:valine-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR002303; Valyl-tRNA_ligase.
DR   PANTHER; PTHR11946:SF109; VALINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 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   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   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}.
FT   DOMAIN          244..963
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          427..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          872..908
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        438..461
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        880..905
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1287 AA;  145130 MW;  DA56E44DDB333D40 CRC64;
     MAHLCLSPSP VEGRSRGGLP TGANLSPPGG EIRPPAPVVV PNRVLRIRYV ANQLNCCRRP
     SECPPAVTCD YYTSGRKSGR GRPPHRGALH FVEGTLSTAA GRRRKKKASR ICPTTEEKPL
     SLRLSPYGVL DPPTIRQNES RYSTVTLSGG AERRGDPLEE LYQRGEARRS ASPKYAFFKN
     AGSLLGLEKI YRIATRRWST TLSWGSLLQE ELLLKHISQV DDLKGLYSEE ITTSLYALKQ
     REEKRYLDRF SPSQYANAFI FLFPPPNLSG ELHAGHYFNF VQLHVLLLFS RHIWSRYSLA
     LYGADHGGLS AHAAFSRAAD PKWTREKHIS EMKRWQEKLK EKILTCMQKM NIAVDRSRFY
     STMSGNMKQL VTDTFYALYR NDLIVKRLYP VYYCPPLGTI ISKLDVEFRE TLQPRWRVTL
     RLVDGGEESH VDTESDSPHG DNTPPGVNSK RTVGEQSNCR YPPQLQQTNE VKFFPQSSHH
     FFYLKNTHEV PPEVTPSESI HVEVTNLEDL KRVVAILYFS PKKEKRYRGK YALLPLLNKG
     VPLICSNERN VLPLLGGRKT QEEGALHELG HGQSAGDVFI PVFSKEESYN HYANGGSGTN
     EAESSHWVNR EKRTVRKEQP NCQTERRELP PLVEHLLESG LAKVVTPRET QLKCAFYKNN
     ECMLTLAEQW CLRYEKLSKI FFDGPHGGGN RSYRIIPSKY GDYFTGAFPP PSEWTLSRQV
     PHGHPVPLFR YEPPGGGLSK KSHLGGVEGI HLGEAGDAHL EEAADAHLGT PSCYIYGNDV
     EEAYQNLCKS GLLHRSQVKR EFLKREEDVL DSWFSSCLYI LHCIKEMGVD LPHFLRVRRS
     LVDFLLTGRD ILQPWVVRTF VLLSYVMERV GEGGGKGEGS PRSGQNSSQD SGQNNRRTNR
     PSSAPPPLAG TVKFHGLLKD QAGRKISKSE TNATHYEGLV REANVDQVRL SFCFIQRDTE
     DVHLSENVTR KSSKLLAKLW SIAKYIREKC PPRAYERMDR WSSSPAANPN VVVLTHLEKS
     PRARISNVGT FRRYLQMVNA VLCEMKDYNV GRAINLIFSF VVNVFSKFYL TLHSGGDVGG
     GGDLLDGNFD GGGDRLIGHF DEGGDLLVEH FLPAYILRGV LKIVFPFAPH IAEVLFIRLF
     RRVQKDNGGT FQPLHGSTTP LSSNYQLMKN ETPPQLEEQS PLDRSFDAFM QIYTLLAKYK
     KGKSSPPPGR TFHVYLKQNY EGEVPLEYFK NEEAFLAKSL GVNVRFSLGC DHRLAGSSPG
     QPLPTWEVLH DGSSFTIAVG GRRPNRQ
//