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Database: UniProt
Entry: D2W1D2_NAEGR
LinkDB: D2W1D2_NAEGR
Original site: D2W1D2_NAEGR 
ID   D2W1D2_NAEGR            Unreviewed;       977 AA.
AC   D2W1D2;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 69.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EFC37165.1};
GN   ORFNames=NAEGRDRAFT_75175 {ECO:0000313|EMBL:EFC37165.1};
OS   Naegleria gruberi (Amoeba).
OC   Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC   Vahlkampfiidae; Naegleria.
OX   NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN   [1] {ECO:0000313|EMBL:EFC37165.1, ECO:0000313|Proteomes:UP000006671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEG-M {ECO:0000313|EMBL:EFC37165.1,
RC   ECO:0000313|Proteomes:UP000006671};
RX   PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA   Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA   Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA   Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA   Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT   "The genome of Naegleria gruberi illuminates early eukaryotic
RT   versatility.";
RL   Cell 140:631-642(2010).
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00104}.
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DR   EMBL; GG738921; EFC37165.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2W1D2; -.
DR   STRING; 5762.D2W1D2; -.
DR   EnsemblProtists; EFC37165; EFC37165; NAEGRDRAFT_75175.
DR   VEuPathDB; AmoebaDB:NAEGRDRAFT_75175; -.
DR   eggNOG; KOG0581; Eukaryota.
DR   InParanoid; D2W1D2; -.
DR   OrthoDB; 5476927at2759; -.
DR   Proteomes; UP000006671; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 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; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24361; MITOGEN-ACTIVATED KINASE KINASE KINASE; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00248; ANK; 3.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   REPEAT          127..159
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          293..556
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          636..706
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   COILED          197..238
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   977 AA;  112636 MW;  0A86D817209A77AD CRC64;
     MSTTFDQVFH AVSEGNIEFL RHIDLRPFIN HEQDDPDDEG IVTLLCTACG RGHLKIVELL
     LNVDGVDVNK CGPLFFACQN GYVEIVKLLL SVDGIDVNQI RVLREACEKG YFEIVKLLLD
     FDGINVDAYK ALHGACYGGN FNIVKLLLAK NARIGKEERK EYDKKIKPKK DLFKSLAEIK
     DKIEDIEYAK DTLIFEIKTQ KRNKIGKVEE IERLEKKLSD MIQELSNMHE RKSEIQNDLM
     ELIPKFPEII IEMEQPLAID GVVISSSMTP KEKFRVFALQ NSILLLNTQF SNYTNIQTLH
     TGLSVVYKAS KSNSQVVILK EISLSENNCE TVMNEIMNLV ILKGHPRIIK LNGVFIESQF
     NKVYIETPYY SNGNLLEYIN KIRNHHDLPT LKNMLRSLFR KMTETLQFIH SKDILHRDLK
     PQNILVNENG EPIIADFGSS KKLIAQLTNN TMGVGTLKYM APEVKRQEES PSEKSDIWSL
     GVSLYECWQL IQQISMMNNA TVEILNFDSK GKVVLPTSTL NDEIDITLMK MLSHMFNSNP
     EDRPSSLTLL TDSDYFTNEN PTTDILSKSN QKELEGSEKI SLWQARLKKM KQFLPESTEG
     EIKVDIYRHR LLEDIASIYK DLIPIGYSVI FYKTFVKYKG ETGIDAGGLS NEMYSKYIEA
     ILESKHFQNS ESSPNENFIL TDEPLTDESK NQLRTLGLLL KKLLIDCDDK TVYLPLNSFI
     FYYLLNGNAL NKETLQFNAI SLLLSKFLRE YDFELDNQIF SVKKCKNDEE LQSITMEETF
     IDVLSKSEKP LIMENVQLFI ISQLYSYFYS DLKIEKLKLI KQGFDWFNLT KFKQSSKLPP
     KLKEFLDLQG SNFDEKCLSV NELKILLSGQ SYIDADLLLN EIDMTRISPI MQDHFTKCIR
     KLTKSQLRQL LVWMTSLSSI PIRGFSRKIS IREYNRFESH TCSFVFDIPS QITNYEQFET
     QFMNCLRLSS VATMEDQ
//
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