NRKB_TRYBB
ID NRKB_TRYBB Reviewed; 431 AA.
AC Q03428;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Putative serine/threonine-protein kinase B;
DE EC=2.7.11.1;
GN Name=NRKB;
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=Isolate TREU66;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L03777; AAB59253.1; -; mRNA.
DR AlphaFoldDB; Q03428; -.
DR SMR; Q03428; -.
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; 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; 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 B"
FT /id="PRO_0000086448"
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"
SQ SEQUENCE 431 AA; 48172 MW; F6B4B3EF9E99FF74 CRC64;
MSEPFSTILG TDGSGGRCKY LNKGIVGLGS YGEGYVAERV EDGSLCVAKV MDLSKMSRRD
KRYAQSEIKY PTNCNHPNII RYIEDHEEND RLLIVMEFAD SGNLDEQIKP WGTGDARYFQ
EHEALFLFLQ LCLALDYIHS HKMLHRDIKS ANVLLTSTGL VKLGDFGFSH QYEDTVSGVV
ASTFCGTPYY LAPELWNNLR YNKKADVWSL GVLLYEIMGM KKPFSASNLK GLMSKVLAGT
YAPLPDSFSS EFKRVVDGIL VADPNDRPSV RENFQIPYIN KGLKLFVQAL KKNERILDSV
KEVLVSQVSE ILSSEVSPDA HRFLESQINY DVTHRGHVNK LGGGNGKSWK PRFLQIVRGQ
LILTDDEEGN NPKGLNLEQV QGACPVPYST AKRDFVFALN TVGGEGMWFQ AVSHGDMEMW
VHAIQRGIGV A