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Database: UniProt
Entry: D2W386_NAEGR
LinkDB: D2W386_NAEGR
Original site: D2W386_NAEGR 
ID   D2W386_NAEGR            Unreviewed;       452 AA.
AC   D2W386;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EFC36447.1};
GN   ORFNames=NAEGRDRAFT_54368 {ECO:0000313|EMBL:EFC36447.1};
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:EFC36447.1, ECO:0000313|Proteomes:UP000006671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEG-M {ECO:0000313|EMBL:EFC36447.1,
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).
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DR   EMBL; GG738930; EFC36447.1; -; Genomic_DNA.
DR   RefSeq; XP_002669191.1; XM_002669145.1.
DR   AlphaFoldDB; D2W386; -.
DR   EnsemblProtists; EFC36447; EFC36447; NAEGRDRAFT_54368.
DR   GeneID; 8862688; -.
DR   VEuPathDB; AmoebaDB:NAEGRDRAFT_54368; -.
DR   InParanoid; D2W386; -.
DR   OrthoDB; 1614410at2759; -.
DR   Proteomes; UP000006671; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR   Gene3D; 1.10.287.4070; -; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR002687; Nop_dom.
DR   InterPro; IPR036070; Nop_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   PANTHER; PTHR47989; OS01G0750732 PROTEIN; 1.
DR   PANTHER; PTHR47989:SF62; OS05G0423500 PROTEIN; 1.
DR   Pfam; PF01798; Nop; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SUPFAM; SSF89124; Nop domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        88..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          191..452
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   452 AA;  51136 MW;  6E9CC07814D3F780 CRC64;
     MYDIDQDIVL SLNFSTDSTI QITPYPVQKE IGALERSLTL YSEDSQYFFN VSFTFVKCPQ
     MFTMDDVVIS GQPAVECIPE QVVLSRDFVI LVAVPTSIAV LILGISIGLF SLYVLNFISV
     RMWRLKKKEK AELELEMRII DKKVIFQNSV VSSQSTLSET AKSKQSNNSD LSVPLIEKNE
     KPSFIIPIEN IEIVRKLAEG GLGIVYLGKL VGKIDVAIKL LKSTDQGDEF EQEASLLSSL
     RHDNILTLFG ICVTSENKYM VTEFAEMGSL DKSLYRARIG EITLPLKNKL SILIATAKGI
     EYLHNLTPTV VHRDLHYFLT QLKKMQDSDE TFIIRNIQQY EEVDMPLSAL LLQIVQSYGF
     QLKDHSQFDD LERKIRESAI STSGSELSDK ELQEISKLAQ QAEPLLTEKS KIRGALRERM
     ILVAPRVYEK LGEVVGARMI QKFGLENMIN QE
//
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