ID A0A509AJC5_PLABA Unreviewed; 888 AA.
AC A0A509AJC5;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Arginine--tRNA ligase, putative {ECO:0000313|EMBL:VUC55308.1};
GN ORFNames=PBANKA_0814900 {ECO:0000313|EMBL:VUC55308.1};
OS Plasmodium berghei (strain Anka).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=5823 {ECO:0000313|EMBL:VUC55308.1, ECO:0000313|Proteomes:UP000074855};
RN [1] {ECO:0000313|EMBL:VUC55308.1, ECO:0000313|Proteomes:UP000074855}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ANKA {ECO:0000313|EMBL:VUC55308.1,
RC ECO:0000313|Proteomes:UP000074855};
RX PubMed=25359557; DOI=10.1186/preaccept-1233682211145405;
RA Otto T.D., Bohme U., Jackson A.P., Hunt M., Franke-Fayard B.,
RA Hoeijmakers W.A., Religa A.A., Robertson L., Sanders M., Ogun S.A.,
RA Cunningham D., Erhart A., Billker O., Khan S.M., Stunnenberg H.G.,
RA Langhorne J., Holder A.A., Waters A.P., Newbold C.I., Pain A., Berriman M.,
RA Janse C.J.;
RT "A comprehensive evaluation of rodent malaria parasite genomes and gene
RT expression.";
RL BMC Biol. 12:86-86(2014).
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363038}.
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DR EMBL; LK023123; VUC55308.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A509AJC5; -.
DR STRING; 5823.A0A509AJC5; -.
DR VEuPathDB; PlasmoDB:PBANKA_0814900; -.
DR InParanoid; A0A509AJC5; -.
DR OrthoDB; 241454at2759; -.
DR Proteomes; UP000074855; Chromosome 8.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR001278; Arg-tRNA-ligase.
DR InterPro; IPR035684; ArgRS_core.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR11956:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00750; tRNA-synt_1d; 2.
DR PRINTS; PR01038; TRNASYNTHARG.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|RuleBase:RU363038};
KW ATP-binding {ECO:0000256|RuleBase:RU363038};
KW Ligase {ECO:0000256|RuleBase:RU363038, ECO:0000313|EMBL:VUC55308.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU363038};
KW Protein biosynthesis {ECO:0000256|RuleBase:RU363038};
KW Reference proteome {ECO:0000313|Proteomes:UP000074855};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..888
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5021199146"
FT DOMAIN 209..356
FT /note="Arginyl-tRNA synthetase catalytic core"
FT /evidence="ECO:0000259|Pfam:PF00750"
FT DOMAIN 511..620
FT /note="Arginyl-tRNA synthetase catalytic core"
FT /evidence="ECO:0000259|Pfam:PF00750"
SQ SEQUENCE 888 AA; 107144 MW; 47E9A14E92B5333A CRC64;
MNRWVFMVWV FFFFLEEFKF KQMSHILNDC SYLYNQIKKK TRYINAYLER NKIISLKKGK
SKQKKINSLN THLHSSLYSN PHNDIKKEVQ IYEILNNAIK NVVKKVIKNE NLLIPKQYLL
EYNKLYDDYE YQSGIIMFID KDIRDGVSIN GSENEHKHFR QKIIESLKNE CSDIIDDIRL
SQNGILNIRV KDEYIKRRFY EFHTQLNENK QNDQIKTDEK KNVVVLDYCG VNMAKHMHVG
HLKSLFLGYA LNNIFDYFNF NVKSRNHIGN WNSNIAMVIT FFIFFLSENW CNQFVINSSS
LLQNSENIKT NNNCFSDIFV EKNENFQIVK KYLDILNNLK ENNFYDNYEK FNINKIENIN
LDNIDNAYKI SKELYSINTL FQKCTKHILS LMYKYDDKTI QLWNVLCDKT RKENDEILRI
FKIHKLIEKG EDFYVKYVPK VLEEMEKKKI LFKFGNKLCV LFKKKKNLEI EKTKINCNDK
DYYEVVQVQD KIYDDLKNGD INILKKNYHI LTLKNDIAYT YAGIDLASIY YRVYFEKADK
IIYVVDENQK NHFMQIFSIY KNMNMFSKDV EYKCICYGFV LNNEKKKIKT KNFTNNTFVK
DVIQNLQQIE EKKIKKNDEN EYNENCYDDN NEGKFIYNKR YYTKKNYKNL LLSSIVYSYI
SVKNCKRQTI NNLINSYNFE YIYIINNYND IYFILGNLKK SDYSFIYEEK YYINMDYRLK
KLLLDIMNFK NILKNVIYNY NVDKLCSYLF SLSQKTHHFA RDSFNKNFLH NFEEKNIHKF
LNFIKNISKE KIANTIINLE KKKYDIFDDE KITYLNLFIN FIKSDKDHNP TINKINSFSK
DELNKIMSFF LNKTFEIIVM QSYLFIVSEI FDILNLYLVK FDTPEIIK
//