ID D2V466_NAEGR Unreviewed; 463 AA.
AC D2V466;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:EFC48465.1};
GN ORFNames=NAEGRDRAFT_82980 {ECO:0000313|EMBL:EFC48465.1};
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:EFC48465.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC48465.1,
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. RAC subfamily. {ECO:0000256|ARBA:ARBA00006935}.
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DR EMBL; GG738851; EFC48465.1; -; Genomic_DNA.
DR RefSeq; XP_002681209.1; XM_002681163.1.
DR AlphaFoldDB; D2V466; -.
DR STRING; 5762.D2V466; -.
DR EnsemblProtists; EFC48465; EFC48465; NAEGRDRAFT_82980.
DR GeneID; 8849786; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_82980; -.
DR eggNOG; KOG0690; Eukaryota.
DR InParanoid; D2V466; -.
DR OrthoDB; 5474699at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05123; STKc_AGC; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045270; STKc_AGC.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR PANTHER; PTHR24351:SF243; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50003; PH_DOMAIN; 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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EFC48465.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU000304};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..102
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 144..401
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 402..463
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT BINDING 182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 463 AA; 52901 MW; 3154FBD095467A8F CRC64;
MEVNPMEKPD FSGYLKKKGG KIKTYKRRWF ELRGKLLFYF KKQGELKPTG FINIQGAKVE
IDETKPMSFK LRGKNLARVY EISAENETEF QVWMKELNKA MNYNPSSDKE GLEEFKEEIL
KAKSLEQITI GNKSSDVKVS LNDFELLTVV GRGSFGKVMK VKQKGASRVY AMKVLRKDMI
IKENMVSHTL AEKKILQSID HPFIVSLHYA FQTEEKLYLV LDYLPGGELF FHLREETKFD
VERAKFYAAQ IVMAIEHLHK NDIIYRDLKP ENVVLDGDGY AVLTDFGLAK TSMGNNTPTY
TFCGTPEYLA PEILKGQGHG KAVDWWSLGI LLYEMIVGLP PFYSENINEM YELILKAPLK
FPSSVPADAQ SLLKGLLDRE EYKRLGGGPS DGAEIRAHPF FKNINWDNLY SKGISAPFKP
QLHDGNDTKY VDTEFTSERA HDSFAIGVSK DENKSFDDFD FSK
//
