ID   A0A3Q0KRY8_SCHMA        Unreviewed;       948 AA.
AC   A0A3Q0KRY8;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Serine/threonine kinase {ECO:0000313|WBParaSite:Smp_163380.1};
OS   Schistosoma mansoni (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6183 {ECO:0000313|Proteomes:UP000008854, ECO:0000313|WBParaSite:Smp_163380.1};
RN   [1] {ECO:0000313|Proteomes:UP000008854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Puerto Rican {ECO:0000313|Proteomes:UP000008854};
RX   PubMed=22253936; DOI=10.1371/journal.pntd.0001455;
RA   Protasio A.V., Tsai I.J., Babbage A., Nichol S., Hunt M., Aslett M.A.,
RA   De Silva N., Velarde G.S., Anderson T.J., Clark R.C., Davidson C.,
RA   Dillon G.P., Holroyd N.E., LoVerde P.T., Lloyd C., McQuillan J.,
RA   Oliveira G., Otto T.D., Parker-Manuel S.J., Quail M.A., Wilson R.A.,
RA   Zerlotini A., Dunne D.W., Berriman M.;
RT   "A systematically improved high quality genome and transcriptome of the
RT   human blood fluke Schistosoma mansoni.";
RL   PLoS Negl. Trop. Dis. 6:E1455-E1455(2012).
RN   [2] {ECO:0000313|WBParaSite:Smp_163380.1}
RP   IDENTIFICATION.
RC   STRAIN=Puerto Rican {ECO:0000313|WBParaSite:Smp_163380.1};
RG   WormBaseParasite;
RL   Submitted (DEC-2018) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. CDC2/CDKX subfamily.
CC       {ECO:0000256|ARBA:ARBA00006485}.
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DR   AlphaFoldDB; A0A3Q0KRY8; -.
DR   EnsemblMetazoa; Smp_163380.1; Smp_163380.1; Smp_163380.
DR   WBParaSite; Smp_163380.1; Smp_163380.1; Smp_163380.
DR   InParanoid; A0A3Q0KRY8; -.
DR   Proteomes; UP000008854; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   CDD; cd07846; STKc_CDKL2_3; 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   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1.
DR   PANTHER; PTHR24056:SF400; CMGC FAMILY PROTEIN KINASE; 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.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
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}; Reference proteome {ECO:0000313|Proteomes:UP000008854};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          4..287
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          431..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          753..784
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        753..773
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         34
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   948 AA;  106638 MW;  EA2C9580C53CC6BF CRC64;
     MEKYENLGLV GEGSYGMVIK CKNKESGRIV AIKKFIDSED DKHVKKIALR EIRMLKQLRH
     DNLVNLLEVF RRKKRLYLVF EFVDNTILDD LEKNPNGIDE LRTKRTLFQV IRGVEFCHLH
     NIVHRDIKPE NILISRNGVV KLCDFGFART LAAPGEVYTD YVATRWYRAP ELLVGDTKYG
     RPIDIWAIGC LASEMLTGDP LFPGDSDIDQ LHRIVRCLGN LSEKYQNIFH RNPLFVGMRV
     PFAKEIDPLD KRLAKVSKLT LGFIKTCLRI DANDRPTSSA LLRSEYFTRE NFASIFLEEL
     KTLIKNETNI NIPSSSTNIT SDNSIVNNLN SNSNQIQVKN NQPCNASNNN NSNTVQSKVS
     TTSTTTITPT ISFTTTTTTT TTTGNTYPNA STTTTTAVKL FLSDIMNVKN QNKDKTTTPN
     RVDLSVTSQT GLHNSEIDEQ NKSSNISTGF SSNTKPTQLE GNKIKSTMAE QVNLTYVASK
     SRVATKSQLY NEYLVHDENI DPHHLLDTMK VSRKPHYGSD NVLNRNDDSD SKESFAVTEK
     MNDRLNEMPS IPQKSFGLLT TVKCKSPKPT NPISKPSILE DLREPLNDTD LSSASISISP
     LQVTNLTINE QSIINTTNQS PFNSSFVAKV TEVPNEQIDC TSTVIESSAS KYLDTKCGDS
     QPKEMTSNKR LPYLTLSQTS SYHFFPQQYR GVYQNSLKSD QTNTYNTGIV SSGTGLSSLS
     PLLTNSQTVS KHENHPTFQS INISASPSIP LQTWTTQKNS SNTNNSSKDS KSRRYYQPPN
     HHRKSTFSLQ FPMNISHSVC QPISTSLSNH YHNHNHHFSI LQPIGIMPSP NIFDTNHDYL
     HPEQNESRSY IGHVNFSTRS PLQSLSQQNI FKKSFTSNST TGTSKQDNTY PLTGNQHSFS
     PQVLPAFTCS SYSTNQYGTN TKSNHNNQFP INRLRNSDKF WLGSLPRR
//