ID   Q26801_9TRYP            Unreviewed;       437 AA.
AC   Q26801;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2001, sequence version 2.
DT   24-JAN-2024, entry version 115.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS   Trypanosoma brucei.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=5691 {ECO:0000313|EMBL:AAA19808.2};
RN   [1] {ECO:0000313|EMBL:AAA19808.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TREU667 {ECO:0000313|EMBL:AAA19808.2};
RX   PubMed=8126084; DOI=10.1002/jcb.240540104;
RA   Hua S.B., Wang C.C.;
RT   "Differential accumulation of a protein kinase homolog in Trypanosoma
RT   brucei.";
RL   J. Cell. Biochem. 54:20-31(1994).
RN   [2] {ECO:0000313|EMBL:AAA19808.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TREU667 {ECO:0000313|EMBL:AAA19808.2};
RA   Li Z., Hu H., Wang C.C.;
RL   Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00001433};
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; Evidence={ECO:0000256|ARBA:ARBA00000775};
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DR   EMBL; AF359249; AAA19808.2; -; mRNA.
DR   AlphaFoldDB; Q26801; -.
DR   VEuPathDB; TriTrypDB:Tb1125.10.4940; -.
DR   VEuPathDB; TriTrypDB:Tb427_100137300; -.
DR   VEuPathDB; TriTrypDB:Tb927.10.4940; -.
DR   VEuPathDB; TriTrypDB:Tbg972.10.5990; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR   GO; GO:0005829; C:cytosol; IDA:GeneDB.
DR   GO; GO:0020023; C:kinetoplast; IDA:GeneDB.
DR   GO; GO:0005524; F:ATP binding; ISM:GeneDB.
DR   GO; GO:0004672; F:protein kinase activity; IDA:GeneDB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000281; P:mitotic cytokinesis; TAS:GeneDB.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:GeneDB.
DR   GO; GO:0051726; P:regulation of cell cycle; EXP:GeneDB.
DR   GO; GO:1902412; P:regulation of mitotic cytokinesis; IMP:GeneDB.
DR   CDD; cd05573; STKc_ROCK_NDR_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR24356:SF184; SERINE/THREONINE-PROTEIN KINASE TRICORNERED; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Kinase {ECO:0000313|EMBL:AAA19808.2};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:AAA19808.2};
KW   Transferase {ECO:0000313|EMBL:AAA19808.2}.
FT   DOMAIN          54..350
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         93
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   437 AA;  50054 MW;  3357405EE3F90413 CRC64;
     MSDVPKSQVG TDAKVAVAKK YTGEYYVKGM VGDKKSFAIE HSRGRQKKHT VNEFCVGDAI
     GRGAFAEVFQ CWRPEEPHIV YAMKKIRKDL IVKRKQSLNV HTERDLLSDA KLRQKRVSCP
     WITDLVVAFQ DQDFLYIVTE YCSGGDLISW LIRYDVFPEE TARFYFVELV LALNALHKMG
     YVRRDVKPDN VLIDREGHVK LADFGLSKRD PDQAESTSVA DDSYLTEDVT VDDDVKKRFR
     DKKERKVMFF STVGSPAYIA PEVLIGRGYD YSCDWWSAGV ILYEMIFGYP PFFNDNNTAT
     AKKIIQFKEH LEFPKDQTTV SKEAIDLISH LIADSKERYG FEEIIRHPFC KGVPLTDSIR
     NEEAPFSVVL NDPKDLQYFE PAPDNADIQK QPMTAVSRED QSVFVGFTSK LCDRNQSTTC
     SRALGRFHEL QNFSDDD
//