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Database: UniProt
Entry: G3FHD2_BRABE
LinkDB: G3FHD2_BRABE
Original site: G3FHD2_BRABE 
ID   G3FHD2_BRABE            Unreviewed;       566 AA.
AC   G3FHD2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Receptor interacting protein kinase 1a {ECO:0000313|EMBL:AEO79022.1};
OS   Branchiostoma belcheri tsingtauense.
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomatidae; Branchiostoma.
OX   NCBI_TaxID=155462 {ECO:0000313|EMBL:AEO79022.1};
RN   [1] {ECO:0000313|EMBL:AEO79022.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21911601; DOI=10.4049/jimmunol.1100816;
RA   Li J., Yuan S., Qi L., Huang S., Huang G., Yang M., Xu L., Li Y., Zhang R.,
RA   Yu Y., Chen S., Xu A.;
RT   "Functional Conservation and Innovation of Amphioxus RIP1-Mediated
RT   Signaling in Cell Fate Determination.";
RL   J. Immunol. 187:3962-3971(2011).
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DR   EMBL; JF719909; AEO79022.1; -; mRNA.
DR   AlphaFoldDB; G3FHD2; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0070887; P:cellular response to chemical stimulus; IEA:UniProt.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProt.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEA:UniProt.
DR   GO; GO:0031349; P:positive regulation of defense response; IEA:UniProt.
DR   GO; GO:0032103; P:positive regulation of response to external stimulus; IEA:UniProt.
DR   GO; GO:0010033; P:response to organic substance; IEA:UniProt.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd01670; Death; 1.
DR   Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011029; DEATH-like_dom_sf.
DR   InterPro; IPR000488; Death_domain.
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   PANTHER; PTHR23257:SF975; DUAL SPECIFICITY PROTEIN KINASE SPLA-RELATED; 1.
DR   PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF00531; Death; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00005; DEATH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF47986; DEATH domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50017; DEATH_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AEO79022.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          18..285
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          482..566
FT                   /note="Death"
FT                   /evidence="ECO:0000259|PROSITE:PS50017"
FT   REGION          350..415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          454..479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..402
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   566 AA;  62889 MW;  4C38FAF16005C608 CRC64;
     MDAARNRFSV ISKDKLKIYD SCLLGSGGFG FVIKAKHVDW SLDVAVKCIC SKQTMTEKQQ
     KDLYLEAEKL EAARFKHVVH FYGMCIEPTF YCLIMDLAES GSLKSLLGVD IPWALRWRIA
     FETAVGMNYL HNLAPRILHC DLKSENILLD EEYHVKITDF GLSKWKSITG ATSICNQGEV
     GGTATHIPPE SWEDVNCKPD TPWDVYSYGI VLWEILTRRQ PFEHAHNSAH IEIAVKREQR
     PDVKLIPTEP QECADFSRLM RQCWSQKPDD RPSFKDCVDR IDPIYRNYKK EVSAAIAALQ
     SGSSSNNTAG SRSSVSSVQG KLADLKLEDV VRHYTGGAAP QLDEAVPIQV QSAQGAQHQP
     TQDTQGGQHQ PTQDTKGGQY QPTQDTQGGQ YQPTQDTQGG QYQAPPAGGA WAGGLPQGAH
     NIPGLGAGAN FNLQSCQNVI IGNNNVINVT NVPAQPSSAK RKNTPMPKNS APQVSEPQRQ
     VTNKMLQVVS SHMGRDWKKL ARELDMTEPQ IDQIQYDYHH EGLVEITYQM LIKWKQQNGK
     QATVGKLAQA FGNIDKGYLA KHLSHL
//
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