ID   A0AA35RP73_GEOBA        Unreviewed;       559 AA.
AC   A0AA35RP73;
DT   24-JAN-2024, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2024, sequence version 1.
DT   29-MAY-2024, entry version 3.
DE   RecName: Full=Serine/threonine-protein kinase receptor {ECO:0000256|RuleBase:RU361271};
DE            EC=2.7.11.30 {ECO:0000256|RuleBase:RU361271};
GN   ORFNames=GBAR_LOCUS9176 {ECO:0000313|EMBL:CAI8014689.1};
OS   Geodia barretti (Barrett's horny sponge).
OC   Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC   Tetractinellida; Astrophorina; Geodiidae; Geodia.
OX   NCBI_TaxID=519541 {ECO:0000313|EMBL:CAI8014689.1, ECO:0000313|Proteomes:UP001174909};
RN   [1] {ECO:0000313|EMBL:CAI8014689.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Steffen K., Cardenas P.;
RL   Submitted (MAR-2023) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-
CC         L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA-
CC         COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
CC         ChEBI:CHEBI:456216; EC=2.7.11.30;
CC         Evidence={ECO:0000256|RuleBase:RU361271};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU361271};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|RuleBase:RU361271};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU361271}; Single-
CC       pass type I membrane protein {ECO:0000256|RuleBase:RU361271}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. TGFB receptor subfamily.
CC       {ECO:0000256|ARBA:ARBA00009605, ECO:0000256|RuleBase:RU361271}.
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:CAI8014689.1}.
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DR   EMBL; CASHTH010001387; CAI8014689.1; -; Genomic_DNA.
DR   Proteomes; UP001174909; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR003605; GS_dom.
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; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR000333; TGFB_receptor.
DR   InterPro; IPR017194; Transform_growth_fac-b_typ-2.
DR   PANTHER; PTHR23255:SF71; RECEPTOR PROTEIN SERINE_THREONINE KINASE; 1.
DR   PANTHER; PTHR23255; TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I AND II; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF08515; TGF_beta_GS; 1.
DR   PIRSF; PIRSF037393; TGFRII; 2.
DR   PRINTS; PR00653; ACTIVIN2R.
DR   SMART; SM00467; GS; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51256; GS; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR037393-
KW   2}; Disulfide bond {ECO:0000256|PIRSR:PIRSR037393-3};
KW   Kinase {ECO:0000256|RuleBase:RU361271};
KW   Magnesium {ECO:0000256|RuleBase:RU361271};
KW   Manganese {ECO:0000256|RuleBase:RU361271};
KW   Membrane {ECO:0000256|RuleBase:RU361271};
KW   Metal-binding {ECO:0000256|RuleBase:RU361271};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR037393-2};
KW   Receptor {ECO:0000256|RuleBase:RU361271, ECO:0000313|EMBL:CAI8014689.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP001174909};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|RuleBase:RU361271}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transferase {ECO:0000256|RuleBase:RU361271};
KW   Transmembrane {ECO:0000256|RuleBase:RU361271};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361271}.
FT   TRANSMEM        170..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361271"
FT   DOMAIN          225..255
FT                   /note="GS"
FT                   /evidence="ECO:0000259|PROSITE:PS51256"
FT   DOMAIN          256..550
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          116..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        384
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037393-1"
FT   BINDING         283
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037393-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   DISULFID        11..17
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037393-3"
FT   DISULFID        91..96
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037393-3"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAI8014689.1"
SQ   SEQUENCE   559 AA;  61381 MW;  038988DCB36E1C19 CRC64;
     HSHPDTLSCN CEGPYNCNQA NNSCVARRGG DTPEIACLIY KEFRDTGVTA EVSLCLAVDK
     TYYLINCAPE SQVRPETRGG IPWKTVVTYC CTSDYCNTKE ALQEVIDGLD PSVLPPNFVT
     SETTPDGVTT AVSAPPSSSS SSSSSSPSEQ PATSATSSSS SSSSSSDTPV YAIVVFAVLS
     LTVVVIVAVI VIILTLHFLP QRFSHSVKGS GSSIVSVSFP VDSSSYSDPS LNELLEDSGS
     GSGLPLLIQR SISGQIRLHN LIGKGRFGEV WRGMYKGDQV AVKIFHTREE LSWFHEVEVY
     QTCLLRHPNV LRFIAADNRD VGLQMQLWLI SDYCELGSLF DLLSRETFSQ ATAFKLCHTA
     AGGIDHLHTE IVGAQCKPAI AHRDLKSRNI LVKSDYSCCI ADLGLSLTYE QATGVVKTPP
     RTTVGTRRYL APEVLTESIT IKNFESFKRS DIYSFGLVMW EIGRRAECNG HAEEAQLPYF
     DLIPSDPTLE EVQRVVVEEG RRPSLPNPWN QHEVMVGLSR IIQQCWLHEA QARLTSLRIK
     KSLANLRELL RDTKEPGQP
//