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Database: UniProt
Entry: T1G7U0_HELRO
LinkDB: T1G7U0_HELRO
Original site: T1G7U0_HELRO 
ID   T1G7U0_HELRO            Unreviewed;       285 AA.
AC   T1G7U0;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   Name=20217137 {ECO:0000313|EnsemblMetazoa:HelroP90657};
GN   ORFNames=HELRODRAFT_90657 {ECO:0000313|EMBL:ESN90991.1};
OS   Helobdella robusta (Californian leech).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Hirudinea; Rhynchobdellida; Glossiphoniidae; Helobdella.
OX   NCBI_TaxID=6412 {ECO:0000313|EnsemblMetazoa:HelroP90657, ECO:0000313|Proteomes:UP000015101};
RN   [1] {ECO:0000313|Proteomes:UP000015101}
RP   NUCLEOTIDE SEQUENCE.
RA   Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA   Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA   Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA   Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA   Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ESN90991.1, ECO:0000313|Proteomes:UP000015101}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23254933; DOI=10.1038/nature11696;
RA   Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA   Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA   Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA   Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA   Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT   "Insights into bilaterian evolution from three spiralian genomes.";
RL   Nature 493:526-531(2013).
RN   [3] {ECO:0000313|EnsemblMetazoa:HelroP90657}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) 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   EMBL; AMQM01008211; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KB097736; ESN90991.1; -; Genomic_DNA.
DR   RefSeq; XP_009030917.1; XM_009032669.1.
DR   AlphaFoldDB; T1G7U0; -.
DR   STRING; 6412.T1G7U0; -.
DR   EnsemblMetazoa; HelroT90657; HelroP90657; HelroG90657.
DR   GeneID; 20217137; -.
DR   KEGG; hro:HELRODRAFT_90657; -.
DR   CTD; 20217137; -.
DR   eggNOG; KOG1025; Eukaryota.
DR   HOGENOM; CLU_000288_7_40_1; -.
DR   InParanoid; T1G7U0; -.
DR   OMA; VEMKFRI; -.
DR   OrthoDB; 1614410at2759; -.
DR   Proteomes; UP000015101; Unassembled WGS sequence.
DR   GO; GO:0009925; C:basal plasma membrane; IBA:GO_Central.
DR   GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR   GO; GO:0022008; P:neurogenesis; IBA:GO_Central.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
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:SF566; EPIDERMAL GROWTH FACTOR RECEPTOR; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PIRSF; PIRSF000615; TyrPK_CSF1-R; 2.
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   Magnesium {ECO:0000256|PIRSR:PIRSR000615-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000615-3};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015101}.
FT   DOMAIN          14..268
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   ACT_SITE        137
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT   BINDING         47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         142
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         155
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
SQ   SEQUENCE   285 AA;  32138 MW;  D9D1B699B228B4D3 CRC64;
     PDLSVLKLIE ESELKRGPEI GSGAFGTVYK GIWSPVGKRI KVAVAIKVLN EGSSTSLQNE
     LLDEARVMSS VTHPCCIKIL AVCMARTMML ITPLVNNGSL LEYIRKNKAD SSTLLKWATQ
     IARGMNYLEQ KGIVHRDLAA RNILVHNKSQ VKITDFGLAK LLNCEEYYLA TGGKMPIKWI
     ALESIEHRVF THKSDVWSYG VTLWELFTSG DRPYDNIKAI DMAQYLENGN RLSQPPICTI
     DVYMLMVKCW LVHAESRPSF AELETEFSIM SRDPGRYLVI EVRKN
//
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