ID C3XR77_BRAFL Unreviewed; 772 AA.
AC C3XR77;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EEN69195.1};
DE Flags: Fragment;
GN ORFNames=BRAFLDRAFT_210451 {ECO:0000313|EMBL:EEN69195.1};
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:EEN69195.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN69195.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN69195.1};
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).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. PKD subfamily. {ECO:0000256|ARBA:ARBA00008582}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG666456; EEN69195.1; -; Genomic_DNA.
DR RefSeq; XP_002613186.1; XM_002613140.1.
DR AlphaFoldDB; C3XR77; -.
DR eggNOG; KOG4236; Eukaryota.
DR InParanoid; C3XR77; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd20795; C1_PKD_rpt1; 1.
DR CDD; cd01239; PH_PKD; 1.
DR CDD; cd14082; STKc_PKD; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22968; PROTEIN KINASE C, MU; 1.
DR PANTHER; PTHR22968:SF24; SERINE_THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 75..125
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 188..238
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 330..446
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 479..735
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 249..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..275
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 508
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 772
FT /evidence="ECO:0000313|EMBL:EEN69195.1"
SQ SEQUENCE 772 AA; 88337 MW; 82750CE533019C52 CRC64;
MPLNHKVFLP SVPFFLQFPE WSFYGFSDKI LLFRHDDSSD NILQLVSSPE HIMEGALIEV
VLSSSATEEE TQIRPHALFV HSYRSPAFCD FCGQMLFGLV RQGLKCDGCG GNYHKRCAYK
IPNNCNYTRR RRSSVAMRLP SDDSDSIMVS LVFFVSSQCS CHQYKRSTSW SGRPIWIERA
VAGRIRVPHT LQVHTYTKPT ICQYCKKLLK GLFRQGLQCK DCKFNVHKKC APKLPKDCTG
EVAFHRGRRD DELELGAENS TVSEEGEENE SEIDFDEIST EKSENDESSQ EQEEGVDQDR
AALLSPVMSN NIPLQRIVQS VKHTKRRSSK VLKEGWMVHF TNKDNMRKRH YWRLDTKSLT
FFQSDVGSKY YKDIPLAEIL RVQAAQQERS FEGGRGAHCF EIVSANVVYY VGEKRVDGEV
PTVDPESGVG AAVSKMWEMA IRQALMPVTP QASTASTTSI TSHSKFHFLV TDISQQYQIF
ADDILGSGQF GVVYGGVHRK SGRQVAIKVI DKLRFPTKQE TQLKNEVSIL RSINHPGIVR
LERMFETPER VFVVMEKLKG DMLEMILSSQ KGRLNERVTK FLVTQILVAL KYLHSKNIVH
CDLKPENVLL SSDNAFPQVK LCDFGFARII GEKSFRRSVV GTPAYLAPEV LRNKGYNRSL
DMWSVGVIIY VSLSGTFPFN EDEDINDQIQ NAAFMFPPNP WKEISDEAVD LITNLLQVKM
RRRFTADKCL AHIWLQDFYT WCDLRELEGQ VGSRYLTHES DDARWEAYRR EH
//
