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Database: UniProt
Entry: A0A061J7L2_TRYRA
LinkDB: A0A061J7L2_TRYRA
Original site: A0A061J7L2_TRYRA 
ID   A0A061J7L2_TRYRA        Unreviewed;       458 AA.
AC   A0A061J7L2;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Rac serine-threonine kinase {ECO:0000313|EMBL:ESL09287.1};
GN   ORFNames=TRSC58_02995 {ECO:0000313|EMBL:ESL09287.1};
OS   Trypanosoma rangeli SC58.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Herpetosoma.
OX   NCBI_TaxID=429131 {ECO:0000313|EMBL:ESL09287.1, ECO:0000313|Proteomes:UP000031737};
RN   [1] {ECO:0000313|EMBL:ESL09287.1, ECO:0000313|Proteomes:UP000031737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC58 {ECO:0000313|EMBL:ESL09287.1,
RC   ECO:0000313|Proteomes:UP000031737};
RA   Stoco P.H., Wagner G., Gerber A., Zaha A., Thompson C., Bartholomeu D.C.,
RA   Luckemeyer D.D., Bahia D., Loreto E., Prestes E.B., Lima F.M.,
RA   Rodrigues-Luiz G., Vallejo G.A., Filho J.F., Monteiro K.M., Tyler K.M.,
RA   de Almeida L.G., Ortiz M.F., Siervo M.A., de Moraes M.H., Cunha O.L.,
RA   Mendonca-Neto R., Silva R., Teixeira S.M., Murta S.M., Sincero T.C.,
RA   Mendes T.A., Urmenyi T.P., Silva V.G., da Rocha W.D., Andersson B.,
RA   Romanha A.J., Steindel M., de Vasconcelos A.T., Grisard E.C.;
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. RAC subfamily. {ECO:0000256|ARBA:ARBA00006935}.
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:ESL09287.1}.
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DR   EMBL; AUPL01002995; ESL09287.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061J7L2; -.
DR   EnsemblProtists; ESL09287; ESL09287; TRSC58_02995.
DR   VEuPathDB; TriTrypDB:TRSC58_02995; -.
DR   OrthoDB; 5474699at2759; -.
DR   Proteomes; UP000031737; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05123; STKc_AGC; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR045270; STKc_AGC.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   PANTHER; PTHR24351:SF243; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ESL09287.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000031737};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          2..100
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          134..395
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          396..458
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   BINDING         163
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   458 AA;  52508 MW;  E0F1C4BFEC04A898 CRC64;
     MPAEHSGYLQ KVGGRFYKKK QTRYFELRGS ILYYWKRCPS TDESPPMGSI NLTDTQLIEN
     AKDPRSWAIE GVNLPKTYTL IADSEDQKKE WMEKMSNVRA ENQEPLKLAI HSSDEDETVT
     LYGERNREVS LDDFELDATI GAGSFSNVFV ASEKSTGKVY AIKEMRKELI QQQKMVGNIA
     AERHILQTIS HPFIVSLHYA FQTKKCLYLV LDFLPGGELF FHLAKEKVFD EYRAKFYCGE
     IALAIGYLHS LDIVFRDLKP ENIVLDKDGH ACLTDFGLAK MNVSSTNNLT FCGTSEYIAP
     EFLLGQPHGR AVDWWALGIL LYEMIEGIPP FFNENSNDMY EEILKGDLKF GTDDDKESGL
     PVISERAKDL LRRLLDRNPQ TRLQDLEEFK KHPFFDDIDW EKLSRREIEP PFRPSSNIFC
     NFDEDFTSKK PRALCQEEDG GEQANIAGFT FDRKVGTA
//
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