ID E1F607_GIAIA Unreviewed; 597 AA.
AC E1F607;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Kinase, NEK {ECO:0000313|EMBL:EFO62070.1};
GN ORFNames=GLP15_1906 {ECO:0000313|EMBL:EFO62070.1};
OS Giardia intestinalis (strain P15) (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=658858 {ECO:0000313|EMBL:EFO62070.1, ECO:0000313|Proteomes:UP000008974};
RN [1] {ECO:0000313|EMBL:EFO62070.1, ECO:0000313|Proteomes:UP000008974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P15 {ECO:0000313|EMBL:EFO62070.1,
RC ECO:0000313|Proteomes:UP000008974};
RX PubMed=20929575; DOI=10.1186/1471-2164-11-543;
RA Jerlstrom-Hultqvist J., Franzen O., Ankarklev J., Xu F., Nohynkova E.,
RA Andersson J.O., Svard S.G., Andersson B.;
RT "Genome analysis and comparative genomics of a Giardia intestinalis
RT assemblage E isolate.";
RL BMC Genomics 11:543-543(2010).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFO62070.1}.
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DR EMBL; ACVC01000194; EFO62070.1; -; Genomic_DNA.
DR AlphaFoldDB; E1F607; -.
DR STRING; 658858.E1F607; -.
DR EnsemblProtists; EFO62070; EFO62070; GLP15_1906.
DR VEuPathDB; GiardiaDB:GLP15_1906; -.
DR OMA; MNGHEEC; -.
DR OrthoDB; 5477929at2759; -.
DR Proteomes; UP000008974; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
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; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR43671:SF112; NIMA-LIKE KINASE; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00248; ANK; 7.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 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:0000313|EMBL:EFO62070.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Transferase {ECO:0000313|EMBL:EFO62070.1}.
FT DOMAIN 9..269
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 597 AA; 66400 MW; C37E40AF785BB1F0 CRC64;
MPGQFADRYQ ELELLGTGNF GKVYKVVERK EGKKFACKEI FLPKLPEDLV DAQMREVTLL
KTIRHPNIVE VIDAYHEGDY LYILMPIYSH GDLVAYRKKK NLSEADILII LIQILQALAF
LHGVREGTNG VPSKIVHRDI KPANILMGED DVVVLTDFGL SKILDSMTDT QTVAGSVAYI
APEMHARSAY TEAVDIWSLG VTIYELMTNG KPLINSFFGS HILQEIQQWK RPLVIPNASE
DLTRILNLML AFSPESRPTA LELLTMPALQ RVRRSLLEKD PITKTHTKLL TSYLKTTPTT
YLTDVDEDGN NIVMRCILHG AFHLVSDIVR CFRGEVNAAG KTALMIAAEL NATDVIAQLI
QPQKGYIDER RMRDAQGKTA LMCAAERGDM YEISVKLLKD AEAKLTTPEQ WTALMMAAAN
GSLLIVRQLQ GLEAGMTNNT GQTALMIAAA ANRVEVVRQL LRFEVRKRDS ARRTALMYAA
MNGHEECVDI LKRYEAKMRD KEKLTALAHA ITRRHAGAAC LLIAAEEGIL IKKQSCYRLA
IESNMRDIIG YFSKSMTNSN ISAHVDLETS NLSISSVLSV AISACDMSCS ALDSHIS
//
