ID   A0A0A1TVX7_ENTIV        Unreviewed;       821 AA.
AC   A0A0A1TVX7;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Serine/threonine protein kinase TNNI3K, putative {ECO:0000313|EMBL:ELP84601.1};
DE            EC=2.7.10.2 {ECO:0000313|EMBL:ELP84601.1};
GN   ORFNames=EIN_172060 {ECO:0000313|EMBL:ELP84601.1};
OS   Entamoeba invadens IP1.
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=370355 {ECO:0000313|EMBL:ELP84601.1, ECO:0000313|Proteomes:UP000014680};
RN   [1] {ECO:0000313|EMBL:ELP84601.1, ECO:0000313|Proteomes:UP000014680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP1 {ECO:0000313|EMBL:ELP84601.1,
RC   ECO:0000313|Proteomes:UP000014680};
RA   Zafar N., Inman J., Hall N., Lorenzi H., Caler E.;
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. {ECO:0000256|ARBA:ARBA00005843}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KB207112; ELP84601.1; -; Genomic_DNA.
DR   RefSeq; XP_004183947.1; XM_004183899.1.
DR   AlphaFoldDB; A0A0A1TVX7; -.
DR   EnsemblProtists; ELP84601; ELP84601; EIN_172060.
DR   GeneID; 14883417; -.
DR   KEGG; eiv:EIN_172060; -.
DR   VEuPathDB; AmoebaDB:EIN_172060; -.
DR   OrthoDB; 9459at2759; -.
DR   Proteomes; UP000014680; Unassembled WGS sequence.
DR   GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd13999; STKc_MAP3K-like; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR23257:SF703; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE; 1.
DR   PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF13637; Ank_4; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00248; ANK; 5.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 3.
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   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ELP84601.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000014680};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000313|EMBL:ELP84601.1}; Transferase {ECO:0000313|EMBL:ELP84601.1}.
FT   REPEAT          276..309
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          349..383
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          384..416
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          533..813
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         560
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   821 AA;  93516 MW;  D7292EBD148AE5D3 CRC64;
     MSEKVGETRK EARLSFSEKK QLNRIIRAEF NYAEDLFPVP MTTGESYFSI SVGDKTNKVH
     VSRKTTSIYF RQPINTVEFR NVSTSIKEIV IEFHDHEKKK TPDIWTTRMQ INQLLPFNTV
     HTKTFQLEKM CDLIQPIIRA QTAPATPNIS GNVLSGSSEI PLNESFDVEA RIKSTLMNKV
     PSKSSSTHLS EMMEITPRDT LVGEKVEPPI MHADKIIQSK PRPTVTVTLY LFPEVNPKQE
     KMTKFPLHAA VLDTDLRKVL TLLESGKVDV NAQDEQGNTA LHVATLVSYN EHILVSLLKN
     APTIDVNKKN YDGNTPFHFF CLNFSNPNYS AAMDLFFRLG ADIEATNKNM ETVLYSAVRN
     KSIRMLLVTR LLEKGANVNA TTLRQSTALH YAVYNERTDL LSVLLEHKAN LHIKDSKGLT
     PYAIAMEKSE RYAQTVRDFN DLVEYLHSIS ASDEAVALLV KNKMFKHKLR GMSARSLEKI
     GITSAEGKVL AAKFKTLPNV EAKEDKSENE ETERGKLLAL IENGKTIIDQ SEIEFLQNIG
     SGASGVVYTA AYKGYIVAVK TLKATNMKEV KEFQQESEVL NRLQHKNVVK FYGIIVDKQF
     AMVMEYCSQG SLYDLLVKPE TAMTWEKVLD FSEQLALGME YLHSQNPPVL HRDLKTLNVL
     VSIEKDKETG KECEVLKICD FGLSRFDSEF ITSTKDRGTY AYCAPEVYYN QRYTTQSDVY
     SYGIILWELV YRLIYQKYQR PFQEFPELTM DVQIIIQSAT SDLRPTIPPS TPQKMATLIR
     QCVLREQDNR PKALDIVNTL AQMRKDFKSR PQLWNESIMQ N
//