ID A0A1X7U0F1_AMPQE Unreviewed; 1424 AA.
AC A0A1X7U0F1;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Amphimedon queenslandica (Sponge).
OC Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC Haplosclerida; Niphatidae; Amphimedon.
OX NCBI_TaxID=400682 {ECO:0000313|EnsemblMetazoa:Aqu2.1.20858_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:Aqu2.1.20858_001}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2017) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC {ECO:0000256|ARBA:ARBA00011031}.
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DR STRING; 400682.A0A1X7U0F1; -.
DR EnsemblMetazoa; Aqu2.1.20858_001; Aqu2.1.20858_001; Aqu2.1.20858.
DR eggNOG; KOG0891; Eukaryota.
DR InParanoid; A0A1X7U0F1; -.
DR Proteomes; UP000007879; Unassembled WGS sequence.
DR GO; GO:0031931; C:TORC1 complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051247; P:positive regulation of protein metabolic process; IEA:UniProt.
DR GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR CDD; cd05169; PIKKc_TOR; 1.
DR Gene3D; 1.20.120.150; FKBP12-rapamycin binding domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR009076; FRB_dom.
DR InterPro; IPR036738; FRB_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR026683; TOR_cat.
DR PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR PANTHER; PTHR11139:SF9; SERINE_THREONINE-PROTEIN KINASE MTOR; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF08771; FRB_dom; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM01345; Rapamycin_bind; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF47212; FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP); 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 3: Inferred from homology;
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:UP000007879};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 304..865
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 1039..1350
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1392..1424
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 1321..1350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1323..1350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1424 AA; 164228 MW; BF76B8F66EB11B2A CRC64;
MVQPVLRLFM QDQSEQKLVT QKMLCALQYC GSSLDDYLHL LVPAIVKVFQ NPTNPIEART
IALETIEKLS SSLDFSDYCS QIIHAVVDVL DTVPDLRGVA MDVLCSMMIQ LGPRYKIFIQ
MVKKVLTKYR YSHAAYELLL CRLLKDEPLT PDDDVERHIK SRKQQSTDDE AAEIEAVSFK
KFSLDVNSLT KAWSTAGRIS KDDWIEWLRR LGVELLKESP SPSLRSCWAL AQAYNPLARE
LFNAAFVSCW MELKSVHQED LVVNLKQFLT RDSIPEITQT VLNLAEFMEH CEEATGRFPL
SSELLGECAM NCRAYAKALH YKEEDFHRGV TPKLLESLIA INNKLQQPDA AVGVLMFAKE
RQQGDFKIQE EWYESLNDWE AALHLYQTKQ YSRPDDIKIA LGRMRCLHAM GEWNRLYDIA
SEMWPLGDDD TRQQMSVMAT AAAWGLNQWE SMEEYVRCIP KESFDGAFYQ SLLNIHNHCF
IDAQKSIDKA RSSLDAELTA LVGESYNRAY HLMVSVQLLS ELEEIIQCLV RPEKKKQLQK
TWWNRLLGCQ RNMEDWQRIL QVRSLVLTQQ EELKSWIKFA SICRKSGKLV LSERTLITLL
SNDQSFNIDA DPLSVKFPQV TLAYMKHKWH ADQKQEAFRL LDQFVVRLQS DNIDPSASNE
TNQLLARCYL KLGDWKAELN PDSSSLTTSF SSILHYYELA TKFDRQWYKA WHAWAFMNFQ
ALLHQRQEQQ KLQKTNVILS EDSTSSESTN KIGPVDMTAS IQYSSSAVHG FFRSISLSSG
NSLQDTLRLL TLWFDYGHIS EVHEALEEGI KTVDIENWLQ VIPQLIARID SPRRLVSKLI
HELLTDVGRH HPQALIYPLT VAAKSQSTVR RDAADMILSN MREHSSDLVQ QAVMVSEELI
RVAILWHEQW HETLEDASRM YFGEHNVQGM FKVLDPLHQK LDKGPETLKE ISFNHAYGRD
LAEASEWCKK FQTSSNVKDL TQAWELYYHV FRRISKQLPQ LTTLELQYVS PKLLACKDLE
LAIPGSYEPH CPIIHIKSVS SSLNVITSKQ RPRKLVMEGS DGRSYMFLLK GHEDLRQDER
VMQLFGLVNT LLDNDPETFK RHLRIQRYSV IPLSPNSGLI GWVPHCDTIH ALIRDYRDKK
KIMLNIEHRL MLQTSSDYDH LMLMQKVEVF EQAINSTTGD DLAKVLWLKS PSSEVWFDRR
TNYTRSLAVM SMVGYVLGLG DRHPSNLMLD RLTGRILHID FGDCFEVAMT REKFPEKIPF
RLTRMLTNAM EVTGIEGNFR RTCCSVMRVL RDNKDSVMAV LEAFVYDPLL NWRLMDDNGK
AKSKPIPQQS DTTTITTSNA TTNNSTGRLF PTPGVDVPES QQYHPEELNR KALAIIERVR
QKLTGNDFRH EKMINVDRQV QLLIEQATSH ENLCQCYIGW CPFW
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