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Database: UniProt
Entry: A0A1X7VEX0_AMPQE
LinkDB: A0A1X7VEX0_AMPQE
Original site: A0A1X7VEX0_AMPQE 
ID   A0A1X7VEX0_AMPQE        Unreviewed;       930 AA.
AC   A0A1X7VEX0;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
OS   Amphimedon queenslandica (Sponge).
OC   Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC   Haplosclerida; Niphatidae; Amphimedon.
OX   NCBI_TaxID=400682 {ECO:0000313|EnsemblMetazoa:Aqu2.1.38576_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:Aqu2.1.38576_001}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (MAY-2017) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001171};
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DR   AlphaFoldDB; A0A1X7VEX0; -.
DR   STRING; 400682.A0A1X7VEX0; -.
DR   EnsemblMetazoa; Aqu2.1.38576_001; Aqu2.1.38576_001; Aqu2.1.38576.
DR   eggNOG; KOG0196; Eukaryota.
DR   InParanoid; A0A1X7VEX0; -.
DR   Proteomes; UP000007879; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IEA:InterPro.
DR   CDD; cd00192; PTKc; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   PANTHER; PTHR24416:SF539; RECEPTOR PROTEIN-TYROSINE KINASE; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007879};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        44..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          623..894
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          103..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          181..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          255..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          359..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          427..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..297
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        323..341
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..381
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        451..473
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..500
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         654
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   930 AA;  103114 MW;  F6AE10F9CC58D0F7 CRC64;
     MCESETSSIN MMPTSLALIS TSSTPTPSVT PEGGTSQKGL PLSILVGVPV GGTILLLVLI
     VLLVIACLGL KYGKNMLKRK TEKVYHYNAD NGSEYAFPMK TRDNRTNEDE TDKMERIENE
     EAEGAEEKGK GRRLEAVIIN DEEHETSDLL TPLPSNFKYF TIGSPSPSTI QPYAALVNTS
     PEEATRGRSA TVSGPIGHHM NRKPKLETLV SMPALDVAGV SDAFPYLEAT SSVNNISRNP
     PPLPPPRLEE MRKISQPSRF PRVSSATTRK TASQQQLNTP RVSSAKVRKS SQPAKPQKLM
     QLKGEAKRKI SHPAKFPGSN GLPPSPKMQN KENSMSLTLG PLPLTPNERL LQIKRDKSFS
     TTALSSQSQA TRTSPRTAQE GKKSFGKTGG EPSPYMEPSP TTKLKRITQR NLEKSLSHDV
     LTVTGEFSPT FDKKNQVDGM PSPYLEPSTT SPKKPRKKFA TIDTKDRKLS APLDRRGLNL
     TPPEVASKNK EPNTGQVLSG QPVPLEAPPP VSTGPVPSRK MLISTTSTLV ELISPTETIS
     DGSPSKDQLF HTDEPLCVPD SSARQLWEDS PEFEIYSKLE RFEGAGRMSA ANKEFNTPPS
     STSELYNTLS NQKYREIIRG QIGITGDCLG TGHFANVYKG TWNMKGGKLY VAVKTLKPNA
     PYEEEVKFLQ EACITGQFMH PNIVQLHGVV TLGKPLMIVL ELMNNGDLKS YLKYQKKNII
     DENINQEKLI RQFVMFARSI ASGMDYLSQK SFVHRDLAAR NIFLTNNFTC KIGDFGMARD
     LAKDDCYEAR GTTIPLKWTA PEAVDYRRYT SASDVWSYGM LLYEIWSVGH KPFYNYKNHE
     VLELIRNGFC QPPPPGCTRG IYRLMVRCWN PVGPDRPSFS DIVEYLAQPD EAFLPNEGED
     VGRLGNDMEE WRHLHSDLQN SYTTSSSSII
//
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