ID   M7W0H0_ENTHI            Unreviewed;       974 AA.
AC   M7W0H0;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=KM1_074770 {ECO:0000313|EMBL:EMS11190.1};
OS   Entamoeba histolytica HM-3:IMSS.
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=885315 {ECO:0000313|EMBL:EMS11190.1, ECO:0000313|Proteomes:UP000030780};
RN   [1] {ECO:0000313|EMBL:EMS11190.1, ECO:0000313|Proteomes:UP000030780}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HM-3:IMSS {ECO:0000313|EMBL:EMS11190.1,
RC   ECO:0000313|Proteomes:UP000030780};
RA   Inman J., Zafar N., Lorenzi H., Caler E.;
RL   Submitted (JAN-2013) 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; KB638801; EMS11190.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7W0H0; -.
DR   EnsemblProtists; EMS11190; EMS11190; KM1_074770.
DR   VEuPathDB; AmoebaDB:KM1_074770; -.
DR   Proteomes; UP000030780; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05579; STKc_MAST_like; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
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   PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR24356:SF1; SERINE_THREONINE-PROTEIN KINASE GREATWALL; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EMS11190.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000313|EMBL:EMS11190.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          181..275
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          600..860
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          861..927
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          939..974
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        953..967
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   974 AA;  112419 MW;  AF52470056DB25B3 CRC64;
     MKIEKKLNLK SKICITMSLL NETTTPTKLS KKKKSIFNSD CITFTPIGSG SSTPRRESIL
     SSLPNDELKE VSIENVISEL YFDQLTLTTS IVHIININLP KTHIVLHKFM HELNELDKYV
     TAVYGITAPY LPKKSFYPLH NEEITQYLQE VICLDKFFDS IYVKEFFREN HQISQCMSLH
     HPQMSGVLMK EGYLLKRWKE RFVVVKNSYL FYFVSEKSMV RLEQPRCIVS LSGAILSTNG
     LVIKITTKER QSFNFSCTDE TTLNQWLVAL NAVICFKPSP QKQQRMTKKY TLLGVDELST
     PIQSTKENKT VTPRRSTEFL ISRVNCLKDE ADKIIESYEH QPDKESLVMV LKQFKQIQSV
     DLSSTSLIDY YNSKIVQFGD DPLLFRFLQI FKEIRELSGM RPNVPKLCTS PLGRYSLQPK
     SSCSSSQTSP RTLTSQFTTQ CRLCNNTYYV DELTKHSYYC KLCNEICLKQ TTCKTRLLAI
     AEEINKQKRY HKGSIEYSGL AEKALKCSQI EVINQNNIDY MNDAEQLLEQ SINQKSDVCY
     KTFALIVIKL IKLRRQMFIN ILKGDYGENG NMWEFLSVVS NELVIEDPQS KWQQVGLDDF
     EVIKKFSEGA YSKLYLVKKK TTGDVYAMKV SKKSDMKRKN VIDGVLAEKK ILQLSNTRSV
     VKLYYAFQDS SNLFLVMEYC PGGDLRCILR NLNYLEESVV RIYTAEIILA LEYIHSLGCI
     HRDLKPDNVL IDKNGHLLLT DFGLSVVGLC NEQHGIKESR LLCTPDYVAP ESLRDYYYCQ
     ASDYFSLGCM VYEMLLGIPP FHCDSPNQIF ELIKEGIYDW PEDVNISEEC KDFVNGLLTV
     DYNQRLGAKS IDEIKNHKWM KPISFDSLLS ESREDIFVPE LENELDTGYF DIDVDRNNTL
     IKDEDWTGDN TFYSFDCVNT NQVIDQNIEI VERRSSAVNL CDDDDESSQE TTSEQDDNNN
     DMTRSMSMFN FHHK
//