ID W7A3V4_9APIC Unreviewed; 982 AA.
AC W7A3V4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Arginyl-tRNA synthetase catalytic core domain-containing protein {ECO:0000259|Pfam:PF00750};
GN ORFNames=C922_01574 {ECO:0000313|EMBL:EUD67962.1};
OS Plasmodium inui San Antonio 1.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=1237626 {ECO:0000313|EMBL:EUD67962.1, ECO:0000313|Proteomes:UP000030640};
RN [1] {ECO:0000313|EMBL:EUD67962.1, ECO:0000313|Proteomes:UP000030640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=San Antonio 1 {ECO:0000313|EMBL:EUD67962.1,
RC ECO:0000313|Proteomes:UP000030640};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium inui San Antonio 1.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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; KI965464; EUD67962.1; -; Genomic_DNA.
DR RefSeq; XP_008815399.1; XM_008817177.1.
DR AlphaFoldDB; W7A3V4; -.
DR EnsemblProtists; EUD67962; EUD67962; C922_01574.
DR GeneID; 20036848; -.
DR VEuPathDB; PlasmoDB:C922_01574; -.
DR OrthoDB; 241454at2759; -.
DR Proteomes; UP000030640; Unassembled WGS sequence.
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; 3.
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};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU363038};
KW Protein biosynthesis {ECO:0000256|RuleBase:RU363038};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..982
FT /note="Arginyl-tRNA synthetase catalytic core domain-
FT containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004890397"
FT DOMAIN 218..283
FT /note="Arginyl-tRNA synthetase catalytic core"
FT /evidence="ECO:0000259|Pfam:PF00750"
FT DOMAIN 388..494
FT /note="Arginyl-tRNA synthetase catalytic core"
FT /evidence="ECO:0000259|Pfam:PF00750"
FT DOMAIN 578..723
FT /note="Arginyl-tRNA synthetase catalytic core"
FT /evidence="ECO:0000259|Pfam:PF00750"
FT REGION 303..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 982 AA; 111795 MW; 9B8708429F339919 CRC64;
MVRAAFLILL FRSCLRCYQL SRAAINYEHL WNAVLPNVRG RTAYVRGPQP IRWILRKRAA
NRTHTKRCRG HAPGEEVHCP GEEVHTPRED LHTILNKQLQ NVAKQILQDE NVNLPKHCLV
EDNKIFDDYE YQSSVILFLE HSLGQGKDVR SEVLRIFRRT GGELIDSLHL SPNGILNIRV
GDPFVMREFL RFCKDAGAHM GTAPVGGYRS NYTPEKENRQ IGGKGTVLLD FCGVNMAKNM
HMGHLKSLLL GSALSNIFRS LNYDVKCRSH IGDWNMNLAI VLSFVVMFPH EVVSMGKSNE
RKVPRIGGSA KHDKAESYQG DTTPCVDSGQ VDKHTGVEPP LRADSTQGGV KEQSENLLEE
EMYIKMLSKL KEENFDKRYQ QLDPSKWEDI DLGNIEFAYK MGKKLFTSSD VFRRISRSTL
RMMYQKDEKI ISLWDNICRS SKRANKEILD KLKIRKLKDK GESFYLKFVP IILRRLEDAN
VVFHLGGKSC LLLRSNPVSR NPVSGDSVSG DSVSGDSVSG DSVSGDPVRG DPVSGNPLSG
GCTPSRRKET HILSSREDHY DVMQVTPELL EHVRRNDVDE LKKNFTLLTL QNDVSFTYAA
IDLAAIHYRV VYEKANKIIY VVDENQRKHF MQIFSIAKFA HILLDHVECV CLNYGFVLNS
ENRKMKTKDL CEKNISVKDM LQNVQLANPS GHEKNEHTYL KKIHMEKTHR ESFLLSSVIY
SYLAVKNYKR QVINNILNTP HVEYLFIHNC YNQVSSILGK EKKGHFSSLL GKRKNVLIEN
NLKKLMLHII RFNNVTEEVT RTYSVDRLCS FLFTLSQKMQ PLLQSSFVKK FIPHLGSSSV
HNFLSMLNGL RKGKAKIEEK TKVKRETEVE EQVEGAPAEA QNPTENIIDK VAGDKDEVTH
LMNKITQAEL FLLIKNSGLL DLREGRSLPE QSGKMETLIF NRILEVLIMQ TYLSLVGRTF
SMLNLQLVNF GSPGSRLGSS DL
//
