ID A0A093H3F6_STRCA Unreviewed; 454 AA.
AC A0A093H3F6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 08-NOV-2023, entry version 40.
DE RecName: Full=receptor protein serine/threonine kinase {ECO:0000256|ARBA:ARBA00012401};
DE EC=2.7.11.30 {ECO:0000256|ARBA:ARBA00012401};
DE Flags: Fragment;
GN ORFNames=N308_06213 {ECO:0000313|EMBL:KFV73910.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV73910.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV73910.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV73910.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. TGFB receptor subfamily.
CC {ECO:0000256|ARBA:ARBA00009605}.
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DR EMBL; KL205752; KFV73910.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093H3F6; -.
DR STRING; 441894.ENSSCUP00000002308; -.
DR Proteomes; UP000053584; 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:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0002063; P:chondrocyte development; ISS:AgBase.
DR GO; GO:0060350; P:endochondral bone morphogenesis; ISS:AgBase.
DR GO; GO:1902731; P:negative regulation of chondrocyte proliferation; ISS:AgBase.
DR GO; GO:0061036; P:positive regulation of cartilage development; ISS:AgBase.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; ISS:AgBase.
DR CDD; cd14219; STKc_BMPR1b; 1.
DR Gene3D; 2.10.60.10; CD59; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000472; Activin_recp.
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; IPR045860; Snake_toxin-like_sf.
DR InterPro; IPR000333; TGFB_receptor.
DR PANTHER; PTHR23255:SF62; BONE MORPHOGENETIC PROTEIN RECEPTOR TYPE-1B; 1.
DR PANTHER; PTHR23255; TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I AND II; 1.
DR Pfam; PF01064; Activin_recp; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF08515; TGF_beta_GS; 1.
DR SMART; SM00467; GS; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF57302; Snake toxin-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|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022527, ECO:0000256|RuleBase:RU000304};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:KFV73910.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053584};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU000304}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022527, ECO:0000256|RuleBase:RU000304};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 79..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 126..155
FT /note="GS"
FT /evidence="ECO:0000259|PROSITE:PS51256"
FT DOMAIN 156..446
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 183
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV73910.1"
FT NON_TER 454
FT /evidence="ECO:0000313|EMBL:KFV73910.1"
SQ SEQUENCE 454 AA; 51714 MW; 51853CF4F68F2E40 CRC64;
TDGYCFTIIE EDESGGHLVT KGCLGLEGSD FQCRDTPIPH QRRSIECCTG QDYCNKHLHP
TLPPLKNRDF AEGNIHHKAL LISVTVCSIL LVLIIIFCYF RYKRQETRPR YSIGLEQDET
YIPPGESLKD LIEQSQSSGS GSGLPLLVQR TIAKQIQMVK QIGKGRYGEV WMGKWRGEKV
AVKVFFTTEE ASWFRETEIY QTVLMRHENI LGFIAADIKG TGSWTQLYLI TDYHENGSLY
DYLKSTTLDT KAMLKLAYSS VSGLCHLHTE IFSTQGKPAI AHRDLKSKNI LVKKNGTCCI
ADLGLAVKFI SDTNEVDIPP NTRVGTKRYM PPEVLDESLN RNHFQSYIMA DMYSFGLILW
EIARRCVSGG IVEEYQLPYH DLVPSDPSYE DMREIVCIKR LRPSFPNRWS SDECLRQMGK
LMMECWAHNP ASRLTALRVK KTLAKMSESQ DIKL
//
