ID B0EGJ7_ENTDS Unreviewed; 1737 AA.
AC B0EGJ7;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Protein serine/threonine kinase, putative {ECO:0000313|EMBL:EDR26344.1};
DE EC=2.7.11.25 {ECO:0000313|EMBL:EDR26344.1};
DE EC=3.4.21.75 {ECO:0000313|EMBL:EDR26344.1};
GN ORFNames=EDI_058780 {ECO:0000313|EMBL:EDR26344.1};
OS Entamoeba dispar (strain ATCC PRA-260 / SAW760).
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=370354 {ECO:0000313|Proteomes:UP000008076};
RN [1] {ECO:0000313|Proteomes:UP000008076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC PRA-260 / SAW760 {ECO:0000313|Proteomes:UP000008076};
RA Lorenzi H., Inman J., Schobel S., Amedeo P., Caler E.;
RT "Annotation of Entamoeba dispar SAW760.";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; DS549210; EDR26344.1; -; Genomic_DNA.
DR RefSeq; XP_001737369.1; XM_001737317.1.
DR EnsemblProtists; EDR26344; EDR26344; EDI_058780.
DR GeneID; 5882410; -.
DR KEGG; edi:EDI_058780; -.
DR VEuPathDB; AmoebaDB:EDI_058780; -.
DR eggNOG; KOG0192; Eukaryota.
DR OMA; CITEDIA; -.
DR OrthoDB; 21861at2759; -.
DR Proteomes; UP000008076; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR006212; Furin_repeat.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
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; PTHR45756; PALMITOYLTRANSFERASE; 1.
DR PANTHER; PTHR45756:SF1; SERINE_THREONINE-PROTEIN KINASE DDB_G0278665-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00261; FU; 6.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 3.
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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Hydrolase {ECO:0000313|EMBL:EDR26344.1};
KW Kinase {ECO:0000313|EMBL:EDR26344.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:EDR26344.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1737
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002747729"
FT TRANSMEM 1299..1322
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1471..1735
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 1498
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1737 AA; 199236 MW; 1C70A79022B2906C CRC64;
MLETFVQIIL FITFINDVIA SSIVEEQKKE GYPWCDIDKN MSWCDINDEG IIYLIEDTEK
TCYYDEDKWR GWMSRCNESN GLWKYDEFVI QKDCCGKDYQ EEPYNNELVI MDTVRNTNKV
IKFSAETTAY SREYLNITIY ETFKNVQLKF LLEYVLENSI ISISRSIENS ERNPKTSQPE
YVLLKYNKII TPFVKLTGKA NVIVEDNIIQ ENDPCEYRFT SSKDIELFNT INSNNKIERM
CSFNEYKRMA VCGKNVEVIS NCNCEYENHE YLNNMVDCSY FNEELVFFIH ENQIETPFQT
RWKSFTTNGK PTTFFIEKGR NITFIGDVYL PKTPVYFEYG KVIFEGTIYF SDEDGLCDLG
EYNINNVNID KVTNNRHILF VGKCGMGYEN CQNFIKDNKF KEVKCGGSQS RILKESSKLK
CECEQENEIN YIQSDCELFS IHKEYSYDLF INYNYNGGNN IRYWNSIIVN NNSIVFNGSK
TIVKEICDFT KVERLDLFGY LSCKELHLKS TTRIIGHENS ELNTYSIFID GKVNNLNKDA
LIQMGKGKFL SDGSTLFTFT EEVTECFELV SSLQELSNSI NSDKINKEGE KYINVQVIDK
IVRICPYEKI DKQVKCNVIE NTLKIFNYEQ CPCNGEYCFF YLDNLKYKEL YLDETNKITG
NIVLSNNFTI NSIGGEAFIY NILFDDPYSN YFISINGNCM LSYTSPILQT FILNGKLTLY
KTTYAHIISN TNRSSIVFQN EPSYLKLDAS VSTSVEMING IIQMGNGRLN DMNGIVISNS
YKGCLIGYFE EHKFSCITCS DGPLTNNCSS STNVLYCQSY NSFSQCIECV NGYFLNEGCL
SCSANCKKCR DDNHCLQCED GYTLSDDQCS KEIAQDCLLY YNNKCVKCAE GKYSIDGVSC
TGDCQKNCVQ CYKSDNDKSK CTICKDGFIL FNNECLSTTD VSNSKKFNSI VGNTGVECES
GYVLVDGSCQ SCSSYHHDED CNLCDLNQCL SCKTKLLLNG ICTLSSDNCN SITNSKCFLC
KEQYYKKENC QKCGQGCKVC DETGTCLECI NESALLKGEV CEDKETTKTQ SLTENEFDIT
FEECDIIRYG SCLRCKDGYY ASNGICKKCD ENCGSCVINS KYCMSCKGNA ILSNHTCLND
YKSLSTSCEL QIKNGLGCII CNDGYYKKDS ICFSCEDPME TCITEDIATN CKKGYFLDNG
KCINQNELKN CKIKTPLGCS QCEKGYYVDN LYCTKCEEHC KLCTNKYCDV CEENYISIDG
TCYYFRAVNK CESSDGLKCT KCSSGYTPEG KYCAKKNLWY VWVIIVVGII FIISLIILGI
VYKRIHHKIK KTNFNVKSID SICQTTDLVF CSPHILTDKP VIEFYGDDEL KVKQTKEVTF
YIANAGKSKI KIQPTIMENE KYEFIIEPEV VVLRSKEVVV FKAEITPLCS TQIDDKILFH
SYDMKKDIMT EFSIGLEFIT EQTNIIDYDE LIFDKKLGEG GFGIVYKGIF RENEVAIKVL
KDNEMTEGSM EEFKIEVDML DKFRCEYIVQ FYGACFIPTK TCMVTEYAKY GSLHKWIKNK
KKVSHHLKIK FCLDAAKAIE YLHSNGILHR DIKPDNMLVF SFAEQVGVNL KLTDFGSARS
INRLMTNMTF TKGIGTPVYM APEVLQQKRY KTTADIYSFG ISIYEILTWQ EAYPTSDPRF
VYPWKIAEFV ISGKRLEKPT KLPENEYRII SDCWKDKSDD RIRACDAISR LERLITY
//
