ID A0A2B4RDY5_STYPI Unreviewed; 645 AA.
AC A0A2B4RDY5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN Name=Cad96Ca {ECO:0000313|EMBL:PFX15356.1};
GN ORFNames=AWC38_SpisGene20427 {ECO:0000313|EMBL:PFX15356.1};
OS Stylophora pistillata (Smooth cauliflower coral).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Pocilloporidae; Stylophora.
OX NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX15356.1, ECO:0000313|Proteomes:UP000225706};
RN [1] {ECO:0000313|Proteomes:UP000225706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA Tambutte S., Allemand D., Aranda M.;
RT "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT digitifera provides evidence for extensive differences between species of
RT corals.";
RL bioRxiv 0:0-0(2017).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PFX15356.1}.
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DR EMBL; LSMT01000658; PFX15356.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B4RDY5; -.
DR Proteomes; UP000225706; 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:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00096; Ig; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin.
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; IPR006612; THAP_Znf.
DR PANTHER; PTHR24416:SF617; RECEPTOR PROTEIN-TYROSINE KINASE; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR Pfam; PF05485; THAP; 1.
DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 4.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00980; THAP; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50950; ZF_THAP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00309};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Kinase {ECO:0000313|EMBL:PFX15356.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000615-3};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000615-3};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Receptor {ECO:0000313|EMBL:PFX15356.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000225706};
KW Transferase {ECO:0000313|EMBL:PFX15356.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00309};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00309}.
FT TRANSMEM 230..252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 49..128
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 146..220
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 277..645
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 440..541
FT /note="THAP-type"
FT /evidence="ECO:0000259|PROSITE:PS50950"
FT ACT_SITE 419
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 424
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 437
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
SQ SEQUENCE 645 AA; 73265 MW; BF3067002BD484A0 CRC64;
MPDVKDTLKT SLSEEARVPA HFFKIMSSML SGAGDLRGLN SSLASQFHPR VKLEFKNVNI
EVNSTFTEKC YWSGDREIPL NWTKYGVLLS TNNILVIKGA TFKDKGYYKC TAQNDYGKAN
ASFGIDVTGK YSAQAAPDRY PTLITGDVLT LTCQVTEDII NVTWKKDGES PSERAKTYTQ
WDKKESELTI TKVLEEDGGK YSCEGRNKLG FVARSFVKIT VKGSQGSSSL WYYIGGSVAA
VIVISLIACF FCRTEQEIQL EPLNVEVDEW EIEVSHVLLQ EVIGRGAFGA VWRALLSSPN
GRPGNQTVAA KCFTPTAGEE GRNCLMREIE LRKLIDENNQ PSIVRFMGCV STQIHSILIM
EYMPCNDLLR YLRKCRGVRD RYYFGDGRAQ DLTNYDLVMF ANFAAGMVFL GSRRIIHRDL
VARNILLDNN YVCKVTDFCM AYQSFKYGHG NAKKCSNTPN KEKRIALHSI PFYGADDLEK
KKFRKKWVDF VQFKRAHWKP TKYSAVCSNH FREEDYSVMF SALTSETMQR RLRKDGVGIS
VFPTVELRSS PSRFNSPTPT RRRRTGLKTN SSTSLLDFIR RRVGVGGIPN DGWSEGRVVA
EVTKGCQMPK TDHVDKELHD MMKRCWNLNP DFRPPFENLR QRLDK
//
