GenomeNet

Database: UniProt
Entry: M2RVA2_ENTHI
LinkDB: M2RVA2_ENTHI
Original site: M2RVA2_ENTHI 
ID   M2RVA2_ENTHI            Unreviewed;       731 AA.
AC   M2RVA2;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Protein kinase, putative {ECO:0000313|EMBL:EMD42407.1};
GN   ORFNames=EHI5A_122090 {ECO:0000313|EMBL:EMD42407.1};
OS   Entamoeba histolytica KU27.
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=885311 {ECO:0000313|EMBL:EMD42407.1, ECO:0000313|Proteomes:UP000011755};
RN   [1] {ECO:0000313|EMBL:EMD42407.1, ECO:0000313|Proteomes:UP000011755}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KU27 {ECO:0000313|EMBL:EMD42407.1,
RC   ECO:0000313|Proteomes:UP000011755};
RA   Hannick L., Zafar N., Lorenzi H., Ali I.A., Petri W.P., Caler E.;
RL   Submitted (FEB-2013) 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}.
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DR   EMBL; KB445524; EMD42407.1; -; Genomic_DNA.
DR   AlphaFoldDB; M2RVA2; -.
DR   EnsemblProtists; EMD42407; EMD42407; EHI5A_122090.
DR   VEuPathDB; AmoebaDB:EHI5A_122090; -.
DR   Proteomes; UP000011755; 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: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; IPR001660; SAM.
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; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
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; 2.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 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:EMD42407.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000313|EMBL:EMD42407.1}.
FT   REPEAT          252..286
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          287..319
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          341..405
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   DOMAIN          441..718
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         469
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   731 AA;  83855 MW;  DED167EE90E2D779 CRC64;
     MSKGGSETNL LRIEVLEGQH LFVRENTSGE ATLVISVEKE KKKIKINRKD NPIPGTPNNK
     IEIGKIPMGE HEIHFLFTDA EKKQPAKHYR CSVPMTELLP YNTNHVKELE FKNEANAEDE
     QKPIFKISMF LFQQRDTKAD KAILKKAGAL LIATNNSDLM LIMSALELPK IDVNMCDKEE
     KNTALHIATM KSTNEHILLT LLKDPRIDVN VKNKDDNTPL HYFCLNFSNP NCEEAFSLFQ
     QRSANMNAKN KIGETPLHKA VFNKCIRLIL VELLLKAGAE VDATTKNGST AMHYAMYMER
     TDLISILLEN NASMEIKNEK GETPLSIVSK SKNQSFQNTV KYFKEVIEYL KGINADTQEI
     KMFIHNRLFK WKLKEITAKQ LDKIGIKAIG RQRELMKEFK KIEDIDPAKL SDKSTQIESE
     EKEREKLLNN ILSSSKFLYK VEYTELIGTG TSGKVFKGIL EGKIDVAVKT LKAGSLKEVE
     EFQHEFGVLS KLDHTNIVKF FGVFQDEHQK MMMVMEYCDR GSLYDVLSKG DLKMKFETLF
     DFSEQIAKGL EYLHNKNILH RDLKSLNILV QTKVNEKGQE HLVLKICDFG LSRFNSTDNL
     NTLQKLRGTY AYCAPEIYFS QPFTYKSDIF SYGIILWEMT YRTIHQKYQR PYQEFPDIKL
     DVQIILKSAT LNLRPTIPAS TPLSLTNLIK QCIIKEQDGR PSSSDILMDI NKMKKEYESN
     PSAWDTCIIS N
//
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