SYSC_PLAF7
ID SYSC_PLAF7 Reviewed; 618 AA.
AC Q8I5P7; A0A143ZZQ0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Serine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.11 {ECO:0000250|UniProtKB:P34945};
DE AltName: Full=Seryl-tRNA synthetase;
DE Short=SerRS {ECO:0000250|UniProtKB:P34945};
DE AltName: Full=Seryl-tRNA(Ser/Sec) synthetase {ECO:0000250|UniProtKB:P34945};
GN ORFNames=PF3D7_1216000, PFL0770w;
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [2] {ECO:0000305}
RP SYNTHESIS OF 239-272, AND POSSIBLE CANDIDATE MALARIA EPITOPE.
RX PubMed=17653272; DOI=10.1371/journal.pone.0000645;
RA Villard V., Agak G.W., Frank G., Jafarshad A., Servis C., Nebie I.,
RA Sirima S.B., Felger I., Arevalo-Herrera M., Herrera S., Heitz F.,
RA Baecker V., Druilhe P., Kajava A.V., Corradin G.;
RT "Rapid identification of malaria vaccine candidates based on alpha-helical
RT coiled coil protein motif.";
RL PLoS ONE 2:E645-E645(2007).
CC -!- FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also able
CC to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-
CC seryl-tRNA(Sec), which will be further converted into selenocysteinyl-
CC tRNA(Sec) (By similarity). {ECO:0000250|UniProtKB:P34945}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-
CC seryl-tRNA(Ser); Xref=Rhea:RHEA:12292, Rhea:RHEA-COMP:9669,
CC Rhea:RHEA-COMP:9703, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
CC Evidence={ECO:0000250|UniProtKB:P34945};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-serine + tRNA(Sec) = AMP + diphosphate + H(+) + L-
CC seryl-tRNA(Sec); Xref=Rhea:RHEA:42580, Rhea:RHEA-COMP:9742,
CC Rhea:RHEA-COMP:10128, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
CC Evidence={ECO:0000250|UniProtKB:P34945};
CC -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
CC {ECO:0000250|UniProtKB:P34945}.
CC -!- SUBUNIT: Homodimer. The tRNA molecule binds across the dimer (By
CC similarity). {ECO:0000250|UniProtKB:P34945}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P49591}.
CC -!- DOMAIN: Consists of two distinct domains, a catalytic core and a N-
CC terminal extension that is involved in tRNA binding.
CC {ECO:0000250|UniProtKB:P34945}.
CC -!- BIOTECHNOLOGY: Possible candidate for an effective malaria vaccine as
CC determined by epitope response in sera. {ECO:0000269|PubMed:17653272}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type-1 seryl-tRNA synthetase subfamily. {ECO:0000255}.
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DR EMBL; LN999947; CZT99321.1; -; Genomic_DNA.
DR RefSeq; XP_001350563.1; XM_001350527.1.
DR AlphaFoldDB; Q8I5P7; -.
DR SMR; Q8I5P7; -.
DR STRING; 5833.PFL0770w; -.
DR EnsemblProtists; CZT99321; CZT99321; PF3D7_1216000.
DR GeneID; 811207; -.
DR KEGG; pfa:PF3D7_1216000; -.
DR VEuPathDB; PlasmoDB:PF3D7_1216000; -.
DR HOGENOM; CLU_023797_1_1_1; -.
DR InParanoid; Q8I5P7; -.
DR OMA; FSASICY; -.
DR PhylomeDB; Q8I5P7; -.
DR UniPathway; UPA00906; UER00895.
DR Proteomes; UP000001450; Chromosome 12.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; NAS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004828; F:serine-tRNA ligase activity; ISS:UniProtKB.
DR GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006434; P:seryl-tRNA aminoacylation; ISS:UniProtKB.
DR Gene3D; 3.30.930.10; -; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR002317; Ser-tRNA-ligase_type_1.
DR PANTHER; PTHR43697; PTHR43697; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR00981; TRNASYNTHSER.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00414; serS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Merozoite;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..618
FT /note="Serine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000370214"
FT BINDING 417..419
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000250|UniProtKB:P34945"
FT BINDING 448..450
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P34945"
FT BINDING 472
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000250|UniProtKB:P34945"
FT BINDING 536..539
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P34945"
FT BINDING 570
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000250|UniProtKB:P34945"
SQ SEQUENCE 618 AA; 73272 MW; E0B85181B060DC76 CRC64;
MHLSKIIFLL IILFPYHVNS RKPIKYKNVN NVFIEIYPCK AIKWERKKKK RDLIKNNKLI
HNVDVNYINM ITNDNHISSE KCRDIKKKRK ITSSEYGMSL EFFKKNPKKV VQNLKKRGME
KYLNVIVMLK KLINEKNENE VLRNKLRNRR KLLSDHIKNL IFNSKKYEDI INRDITNDSD
HKTNLIHVDE EKKKTEKKND TQDILKDNQK IRYINKENQA TNNNINNQDN SNDVLKKNKI
QIEEIKKETN QINKDIDHIE MNIINLKKKI EFNLYKLPNI LLNKVPKGKT TEDNKIIKFY
KKENIIQLNN EEYDFIEPHE EIIKKYENNF IFSNISNKIG FGYNILVNDI AKLERALIDF
MINTHVNKFL YTYVKAPEIV TKSALFNTGQ LPKFEEDLFK ITDNYKLLNE DAYLIPTSEV
SLLNLFKNSQ IDYIHLPIKL VSHSSCFRTE KNNTYGKTSK GLLREHIFQK VELINITDKK
TSPFYYKKLI KQSTYILKQL NIPYRLVLLN SIETPYSASI CYDIEAWLPS QQRYVEVSSC
SNCLDFQARR LNLKYKIKDS NNFCHTINGS GLAVGRVLAI ILEQYQIKKK HKNEITKIQV
PKVLRKYMNK DIIQVEYN
