ID   NRKA_TRYBB              Reviewed;         431 AA.
AC   Q08942;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Putative serine/threonine-protein kinase A;
DE            EC=2.7.11.1;
GN   Name=NRKA;
OS   Trypanosoma brucei brucei.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=5702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ISTar1;
RX   PubMed=8515773; DOI=10.1016/0166-6851(93)90012-m;
RA   Gale M.J. Jr., Parsons M.;
RT   "A Trypanosoma brucei gene family encoding protein kinases with catalytic
RT   domains structurally related to Nek1 and NIMA.";
RL   Mol. Biochem. Parasitol. 59:111-122(1993).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; L03778; AAB59252.1; -; mRNA.
DR   PIR; T11854; T11854.
DR   AlphaFoldDB; Q08942; -.
DR   SMR; Q08942; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   Gene3D; 2.30.29.30; -; 1.
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   Pfam; PF00169; PH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 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; Kinase; Nucleotide-binding; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..431
FT                   /note="Putative serine/threonine-protein kinase A"
FT                   /id="PRO_0000086447"
FT   DOMAIN          20..279
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          331..429
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   ACT_SITE        147
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         26..34
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         49
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   VARIANT         192
FT                   /note="A -> P (in strain: TREU66)"
FT   VARIANT         199
FT                   /note="K -> L (in strain: TREU66)"
SQ   SEQUENCE   431 AA;  47916 MW;  2E68B70275884224 CRC64;
     MAEPFSTILG TDGSGGRCKY LNKGIVGLGS YGEAYVAESV EDGSLCVAKV MDLSKMSQRD
     KRYAQSEIKC LANCNHPNII RYIEDHEEND RLLIVMEFAD SGNLDEQIKL RGSGDARYFQ
     EHEALFLFLQ LCLALDYIHS HKMLHRDIKS ANVLLTSTGL VKLGDFGFSH QYEDTVSGVV
     ASTFCGTPYY LAPELWNNKR YNKKADVWSL GVLLYEIMGM KKPFSASNLK GLMSKVLAGT
     YAPLPDSFSS EFKRVVDGIL VADPNDRPSV REIFQIPYIN KGLKLFVQAL KKNERISDSV
     KEVLVTQVSE ILSSEVSPDA HRFLVSQINY DVTHRGHVNK LGGGNGKSWK PRFLQIVRGQ
     LILTDDEEGN NPKGLNLEQV QGACPVPHST AKRDFVFALN TVGGKGMWFQ AVSHGDMEMW
     VHAIQRGIGV A