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Database: UniProt
Entry: A0A1X7UYE6_AMPQE
LinkDB: A0A1X7UYE6_AMPQE
Original site: A0A1X7UYE6_AMPQE 
ID   A0A1X7UYE6_AMPQE        Unreviewed;       505 AA.
AC   A0A1X7UYE6;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Non-specific serine/threonine protein kinase {ECO:0008006|Google:ProtNLM};
GN   Name=100640366 {ECO:0000313|EnsemblMetazoa:Aqu2.1.32726_001};
OS   Amphimedon queenslandica (Sponge).
OC   Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC   Haplosclerida; Niphatidae; Amphimedon.
OX   NCBI_TaxID=400682 {ECO:0000313|EnsemblMetazoa:Aqu2.1.32726_001, ECO:0000313|Proteomes:UP000007879};
RN   [1] {ECO:0000313|Proteomes:UP000007879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20686567; DOI=10.1038/nature09201;
RA   Srivastava M., Simakov O., Chapman J., Fahey B., Gauthier M.E., Mitros T.,
RA   Richards G.S., Conaco C., Dacre M., Hellsten U., Larroux C., Putnam N.H.,
RA   Stanke M., Adamska M., Darling A., Degnan S.M., Oakley T.H.,
RA   Plachetzki D.C., Zhai Y., Adamski M., Calcino A., Cummins S.F.,
RA   Goodstein D.M., Harris C., Jackson D.J., Leys S.P., Shu S., Woodcroft B.J.,
RA   Vervoort M., Kosik K.S., Manning G., Degnan B.M., Rokhsar D.S.;
RT   "The Amphimedon queenslandica genome and the evolution of animal
RT   complexity.";
RL   Nature 466:720-726(2010).
RN   [2] {ECO:0000313|Proteomes:UP000007879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lucas S., Shapiro H., Lindquist E., Tice H., Dalin E., Glavina del Rio T.,
RA   Bruce D., Barry K., Pitluck S., Srivastava M., Simakov O., Chapman J.,
RA   Mitros T., Hellsten U., Putnam N.H., Fahey B., Gauthier M., Larroux C.,
RA   Richards G.S., Stanke M., Adamska M., Darling A., Dacre M., Degnan S.M.,
RA   Zhai Y., Adamski M., Calcino A., Cummins S.F., Goodstein D.M., Harris C.,
RA   Shu S., Woodcroft B., Leys S.P., Manning G., Degnan B.M., Rokhsar D.S.;
RT   "The genome of the haplosclerid demosponge Amphimedon queenslandica and the
RT   evolution of animal complexity.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblMetazoa:Aqu2.1.32726_001}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (MAY-2017) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
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DR   RefSeq; XP_011403713.2; XM_011405411.2.
DR   AlphaFoldDB; A0A1X7UYE6; -.
DR   STRING; 400682.A0A1X7UYE6; -.
DR   EnsemblMetazoa; Aqu2.1.32726_001; Aqu2.1.32726_001; Aqu2.1.32726.
DR   GeneID; 100640366; -.
DR   KEGG; aqu:100640366; -.
DR   eggNOG; KOG0598; Eukaryota.
DR   InParanoid; A0A1X7UYE6; -.
DR   OMA; SEPNTWA; -.
DR   OrthoDB; 3028764at2759; -.
DR   Proteomes; UP000007879; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05575; STKc_SGK; 1.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 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; IPR017892; Pkinase_C.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24351:SF249; -; 1.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   Pfam; PF00787; PX; 1.
DR   SMART; SM00312; PX; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50195; PX; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007879};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          19..131
FT                   /note="PX"
FT                   /evidence="ECO:0000259|PROSITE:PS50195"
FT   DOMAIN          170..428
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          429..505
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         208
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   505 AA;  58159 MW;  EADE38F005C19218 CRC64;
     MATLDPSAAN GGGDPARPRG QTTAAVEDHE TWVEEKRFTM YKVVVRLEDR SYFIFRRYNE
     FNTLLDKIKK RYPDSNLKLP GKRIFLNNFD PAFIKQRRQG LNDFIVNLIK IPSIFDDEAV
     RDFLSLDDQR STIPIYDRES LDEEAGSEDK TANRFDLGTS EKESAAITDF KLLKVIGKGS
     FGKVYLGRHI DTNKHYAIKV LQKKAIVKRN EVKHIMAERN VLLRNVTHPF LVGLHYSFQT
     GTKLYFVLDY VNGGELFFHL QRERVFEEPR ARFYAAEITS ALGYLHEQDI VYRDLKPENI
     LLDKQGHIIL TDFGLCKEDV KQGETTSTFC GTPEYLAPEV LRKQDYGRPV DWWCLGVVTY
     EMMYGLPPFY SRDVAEMYDG ILHKPLRLRP NITPAGRSLL EGLLQKDKNH RLGSGVRDYK
     DIMDHLFFRS INWDDLFLKK LEPPFNPNVS GDLDLRHFDQ EFTNEAISDN PSPPKSTSAG
     MSISVQDETF AGFSYIPNEG KYMPS
//
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