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Database: UniProt
Entry: D2VZP4_NAEGR
LinkDB: D2VZP4_NAEGR
Original site: D2VZP4_NAEGR 
ID   D2VZP4_NAEGR            Unreviewed;       820 AA.
AC   D2VZP4;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EFC37695.1};
GN   ORFNames=NAEGRDRAFT_53552 {ECO:0000313|EMBL:EFC37695.1};
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:EFC37695.1, ECO:0000313|Proteomes:UP000006671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEG-M {ECO:0000313|EMBL:EFC37695.1,
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; GG738915; EFC37695.1; -; Genomic_DNA.
DR   RefSeq; XP_002670439.1; XM_002670393.1.
DR   AlphaFoldDB; D2VZP4; -.
DR   STRING; 5762.D2VZP4; -.
DR   EnsemblProtists; EFC37695; EFC37695; NAEGRDRAFT_53552.
DR   GeneID; 8853606; -.
DR   VEuPathDB; AmoebaDB:NAEGRDRAFT_53552; -.
DR   eggNOG; KOG0575; Eukaryota.
DR   InParanoid; D2VZP4; -.
DR   OMA; KKSKNHA; -.
DR   OrthoDB; 5471704at2759; -.
DR   Proteomes; UP000006671; Unassembled WGS sequence.
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   CDD; cd13118; POLO_box_1; 1.
DR   CDD; cd13117; POLO_box_2; 1.
DR   CDD; cd14099; STKc_PLK; 1.
DR   Gene3D; 3.30.1120.30; POLO box domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR033701; POLO_box_1.
DR   InterPro; IPR033695; POLO_box_2.
DR   InterPro; IPR000959; POLO_box_dom.
DR   InterPro; IPR036947; POLO_box_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 1.
DR   PANTHER; PTHR24345:SF0; SERINE_THREONINE-PROTEIN KINASE PLK1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00659; POLO_box; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF82615; Polo-box domain; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50078; POLO_BOX; 2.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          90..344
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          613..683
FT                   /note="POLO box"
FT                   /evidence="ECO:0000259|PROSITE:PS50078"
FT   DOMAIN          734..801
FT                   /note="POLO box"
FT                   /evidence="ECO:0000259|PROSITE:PS50078"
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          418..584
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..533
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..548
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   820 AA;  92918 MW;  29EC99662052F0F4 CRC64;
     MYSTRSATPQ TSYRLPGSSS TTTSSGTSNA AAQKLTRPAT ASGVTATRRT PTPTVSQNKL
     QPTSSTPRII IEEKYHKKVD KDRQVLYRKY YQERFLGKGG FAQCYLFRQV GTNIFHAAKI
     IDKKTLEKEN VKQKLFSEIK IHSSLSHRHI VNFVRYFEDI NNVYILLEVC NCGSMMDLLK
     SRTRLTEQEA RFFLHQILLA CLYMNEKKVI HRDLKLGNLF LTDKMEIKIG DFGLATEVEF
     DGERKKTICG TPNYIAPEIL YNKGHSFEVD IWSIGVILYT MLVGTPPFET KDVKETYKKI
     KHNDYNFPPD IEISSKAKSL IRSILRRNPD DRPDIKTILS DPFFAGHSVD VCPVTLLEYA
     RTHALKIPDV EETMPGYSLK HPELQQQMLK LRQDRGALRQ IDNNTMHQRA QPTVETGLKK
     PLMSGFPTST MRPPLATVNT NINNENYNPN SQQVVTKQPL FTPSHPPQQQ TEQPQKPVHP
     TLQTHYTSTT TTQSVSTTNS PSHVTASSVT SSPSLGSQRS VQTTQTTSRL PTPKRRSPSE
     DERKSKPQTP TSESSLETSR SKGPPVKKVR NTVSSPYSPY DVLDPMTVDE DDTTNDNVTH
     DLPPIWITHW ADFSAKYGLT YLMSNGCVGA VYNDSSKMTY MPATEQINYY ERKATGDNIY
     EERSTFTVSD FPPQMNKKVT LIKYFADVLS KLKRNDHNLV SSPNSDTGRC SYRPKDDVFI
     QKTGLDDVFV KRWLRTSHAV IFRLSNKIVQ VCFHDQTEII LTGDSNLVSY TDPQGVRTTY
     ALNKVVKSPS QEIAKRLKYT KDVLCQLISG SATTDKHRNQ
//
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