ID S6CXR4_LEIDO Unreviewed; 510 AA.
AC S6CXR4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=RAC/AKT-like {ECO:0000313|EMBL:CCO56209.1};
GN Name=AKT-like {ECO:0000313|EMBL:CCO56209.1};
GN Synonyms=RAC {ECO:0000313|EMBL:CCO56209.1};
OS Leishmania donovani.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5661 {ECO:0000313|EMBL:CCO56209.1};
RN [1] {ECO:0000313|EMBL:CCO56209.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MHOM/IN/80Dd8 {ECO:0000313|EMBL:CCO56209.1};
RA Varela-M R.E., Mollinedo F.;
RT "Ld-RAC/AKT-like from Leishmania donovani (MHOM/IN/80Dd8).";
RL Submitted (NOV-2012) 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}.
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DR EMBL; HF548848; CCO56209.1; -; mRNA.
DR AlphaFoldDB; S6CXR4; -.
DR SMR; S6CXR4; -.
DR VEuPathDB; TriTrypDB:LdBPK_300850.1; -.
DR VEuPathDB; TriTrypDB:LdCL_300013600; -.
DR VEuPathDB; TriTrypDB:LDHU3_30.1060; -.
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; IPR008271; Ser/Thr_kinase_AS.
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.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..93
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 106..359
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 360..423
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 417..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 510 AA; 57613 MW; CC067A0FBFDE77C0 CRC64;
MSGYLKVLSP DGRWETRYIE IDDAKLRIWR TKGDKESSAA VVKELDLKCA TLREVSEPNT
WAVQPEKAEA TYFQADGEER KTEWMDTLRH YNSSSSGSEK VTLRDFEKKF VLGKGSYGKV
FMVVKKDTDK WYAMKEMSAE KMRQAEIKAP FAERIILEEI DHPFIVHLHY SFQEQGNLYM
ILDLLAGGEL FTYIEQHAPL DEEVVKFYAA EVALALGYLH SRNIIYRDLK PENVVFDRDG
HACLTDFGLA KANVHEPNAV TYCGTNEYLA PELLKGVPHG KAVDWWSLGL MMCEMLFNDL
PFYDENPMQM QMKILTEDVA FPPHIQITEE TKDLIRCLLN KNPERRLQTL EAFKAHKCFS
NLDFGLLEAR KLKAPITPDP NPAHNFAKEF TSEVIVQNES PSQAVVTLAG YTYDRDLSEQ
EKSPSHSPTI AEELRQRRAS KKRSTNGSDA ASPPVTGENR PSNSSPAGAP TKQAAGGPVK
KVEHHIPAKV APQAARKKLT GNKSFDKPTK
//
