ID C3ZQ17_BRAFL Unreviewed; 843 AA.
AC C3ZQ17;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BRAFLDRAFT_77827 {ECO:0000313|EMBL:EEN45396.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN45396.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN45396.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN45396.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
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DR EMBL; GG666659; EEN45396.1; -; Genomic_DNA.
DR RefSeq; XP_002589385.1; XM_002589339.1.
DR AlphaFoldDB; C3ZQ17; -.
DR STRING; 7739.C3ZQ17; -.
DR eggNOG; KOG0192; Eukaryota.
DR eggNOG; KOG0619; Eukaryota.
DR InParanoid; C3ZQ17; -.
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:0030154; P:cell differentiation; 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:0008152; P:metabolic process; IEA:UniProt.
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; 3.80.10.10; Ribonuclease Inhibitor; 4.
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; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_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; PTHR48051; -; 1.
DR PANTHER; PTHR48051:SF43; LEUCINE-RICH REPEAT-CONTAINING PROTEIN 47-LIKE PROTEIN; 1.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00005; DEATH; 1.
DR SMART; SM00364; LRR_BAC; 11.
DR SMART; SM00365; LRR_SD22; 5.
DR SMART; SM00369; LRR_TYP; 12.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47986; DEATH domain; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50017; DEATH_DOMAIN; 1.
DR PROSITE; PS51450; LRR; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Kinase {ECO:0000256|ARBA:ARBA00022527};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT DOMAIN 437..507
FT /note="Death"
FT /evidence="ECO:0000259|PROSITE:PS50017"
FT DOMAIN 553..821
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 582
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 843 AA; 94282 MW; 30AE9AD841ACDF58 CRC64;
MATGLNLQPQ TVNGRLELDL SNQGLTSIPE EVFDITDLEV LDVSRNKLTS IPEAIGRLQK
LYRLDAYSNM LTSLPQAIGS LQKLTHLYIY DNQLTEVPSG VCSLPNLEVL SVGKTKLSTF
PPGAEKLQKL RELDIGDNQL TEVPSGVCSL PNLEVLDVNN NKLSTFPPGV EKLQKLRVLD
IGDNQLTEVP SGVCSLPNLE ALNVYTNKLS TFPPGVEKLQ KLRLLGIADN KLTELPQGVC
LLSNLEILIA NRNPIAHLPD DVTRLKRLKT LDVPCCQFDE FPRQVLQLKT LEKLYAGGCK
FDIVPDEVGD LQHLWFLSLP NNLLRTLPST LNHLHNLRQV HLWNNKFDTF PEVLCELPAM
EKLDIRNNNI TRLPIALHRA DKLKDLDVSG NPLTYPPRDV CKQGTGAIMA FLKQEAEKDE
RILRAFNRLS VRMSQTQWKP LARSLGLSNR AMDAIKASAP DDVPDQVYQT LVQWRAKAGE
AATLSALEQH LRDLDFQQLA DQLSPTHRTP DASARGLGPA LGAVGGQEAD VLQNRYPSVT
IDRRFPIVES GRLEEQSILG RGGFAFVTKA RHLDWRQDVA VKCLLTRKLE GSEQELLYSE
ARKLNLGSRS DHVISLLGVC LDPNFAIVMP YMENGSLAGL LRDVDVPWAL RWRMAHEISL
GMTFLHCQNP QILHCDLKAE NVLLDGDFHV KISDFGLSKW KAESRVVTKT SPEGSTITHA
PPEYHSNINL APNTKFDVYS FGVLLWEIVT RRQPYALAAN SALISMAVTM GQRPDLTLIP
TDREDVTSVS QLMQTCWSQD PEDRPTFDDC ADRLRHVQDR FSREEIRQAI ITVEKMKAAA
SRK
//
