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
//