ID   A0A1B0AG58_GLOPL        Unreviewed;      1338 AA.
AC   A0A1B0AG58;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Non-specific serine/threonine protein kinase {ECO:0000313|EnsemblMetazoa:GPAI044733-PA};
OS   Glossina pallidipes (Tsetse fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC   Glossinidae; Glossina.
OX   NCBI_TaxID=7398 {ECO:0000313|EnsemblMetazoa:GPAI044733-PA, ECO:0000313|Proteomes:UP000092445};
RN   [1] {ECO:0000313|Proteomes:UP000092445}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAEA {ECO:0000313|Proteomes:UP000092445};
RA   Aksoy S., Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:GPAI044733-PA}
RP   IDENTIFICATION.
RC   STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GPAI044733-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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DR   STRING; 7398.A0A1B0AG58; -.
DR   EnsemblMetazoa; GPAI044733-RA; GPAI044733-PA; GPAI044733.
DR   VEuPathDB; VectorBase:GPAI044733; -.
DR   Proteomes; UP000092445; 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; cd05583; STKc_MSK_N; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24351:SF175; CHROMOSOMAL SERINE_THREONINE-PROTEIN KINASE JIL-1; 1.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF00069; Pkinase; 2.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
PE   4: Predicted;
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}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          290..559
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          560..628
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   DOMAIN          655..916
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          170..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          949..979
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1038..1062
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..260
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        949..964
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         322
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1338 AA;  152151 MW;  BA30DF376F901BA1 CRC64;
     MSRYQNKNKP AHAVSLENTK RMSMRRQLDH EIGYYEDISD GRYCHGNNNK RQTLSSNEAR
     IKRQKIMQSS GRATVTTTTA TATHADSSTN KMVYYASNLN NLNNNYTSNA LNSQSAYTRS
     ASFLHNNNNN VNKFSSKDKG NALFNNGTNR KPAINIDAIP LPGEIVEVKD SDSEEDVPHT
     SKARNSKYAN GHSTPISNLP SYMVDEGSNR SYSNQHYRKL EPSNNYSSND LSWGNVQRGS
     KQTNTADSEE KSSTNANGDF ERLQREIEEV TQVNTKCTAM DDEKVNLSHF TLIRVLGTGA
     YGKVFLVRKN GGDDDEKLYA MKVLKKDTVV QKKKTAEHTT TERQVLEAIQ QSPFLVGLHY
     AFQTESKLYL VLDYVSGGEL FTHLYKAEHF SEATVKIYIA EVVLALEHLH KLGIIYRDIK
     LENILLDGQG HIVLADFGLS KIFSSESDHR AHSFCGTLEY MAPEIIRAGP GGHDLAVDWW
     SVGVLTYELL TGASPFTVVE QQNSQSDISR RIQKVDPVLP PTLGETVKDF ILKMLHKDPK
     KRLGGNKKSA GDIKNHPFFR GINWNELKSK RRKAPFKPTL NGDEDTQNFS EEFTKQPVID
     SPAPVPVNTH RLFRGYSYVA PQHLRRRLST KSVAAFPVEY LNEPITDPPS APETLLLKRL
     ISAGSFGKCY TTIYSNQTYV VKVVPEAKYR PSEVDALISC GRDGHKSIAQ YVATYRKGSD
     IWIVQEYVPG YEVAERIANH EYSFDELKCC DIFKQLIDAV KHIHEKRYIH GDLKMENIIF
     VDDGMDQIKL VDFGAASYNS KRNKWNDVPR YTIDYAPPEA LQHPEYATYS ASFDIWCLGA
     TLYSIFMGHT PFRHGRADRH VNMTTLKQRI LDDEIFTHAH RWEQASLELR NLILRCLQKD
     IAKRPTLEQI LQHPWLQIKT KLATSNVSRA VSPPHCSVYV TNTNKCRDRA VEGQKPDRTS
     RKGQKRGGLS RNNLVGRNNT CHETMAVEHE NIERSQSVAG NAGRREERQS YQQRYHGRQM
     AKSLFVSTEA STENVITSSE TRIRNDTSGP LLRSKHKSSG QLAVNTKPLS VNQSRCVGTS
     QCSYNDPEYT ALEDFCGFDE NIAPLIVPPL DSTKEMKLKN YKPTAAKKVV ESNSNVPALK
     KPNSRNTQIV VDKPINQAKI MHKESSIDKK DEQNKTNSCA IYDGIFKMPT MIRGRNLSLR
     LTSGKPFKND VKRSFSHVIE KRISVDNSDD FLGFEESKNR RIRIRIKGRC RVYDLLLYFT
     QNSLRYFKIE RRVYKKPTGE SVLKKDLKRL NTCISEKDLP QLRKFKQELK TPTPRSALLP
     TRTQPDRLAR RHTPYYCQ
//