ID C3ZV30_BRAFL Unreviewed; 865 AA.
AC C3ZV30;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EEN43606.1};
GN ORFNames=BRAFLDRAFT_230463 {ECO:0000313|EMBL:EEN43606.1};
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:EEN43606.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN43606.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN43606.1};
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; GG666687; EEN43606.1; -; Genomic_DNA.
DR RefSeq; XP_002587595.1; XM_002587549.1.
DR AlphaFoldDB; C3ZV30; -.
DR STRING; 7739.C3ZV30; -.
DR eggNOG; KOG0193; Eukaryota.
DR InParanoid; C3ZV30; -.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR CDD; cd20812; C1_KSR; 1.
DR CDD; cd14063; PK_KSR; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 6.10.140.1120; -; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR025561; KSR_SAM-like_dom.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR046861; SAM_KSR1_N.
DR InterPro; IPR046933; SAM_KSR1_N_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR23257:SF780; AT08303P; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF13543; SAM_KSR1; 1.
DR Pfam; PF20406; SAM_KSR1_N; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022527};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 331..377
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 575..842
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 163..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 601
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 865 AA; 97297 MW; 2F36723B3DA95067 CRC64;
MGTEEREEAV KKALESCKTL QSMIDISASN LNGLRTMCET SHDLTQTEIR TLEGKLVKLF
SKQLQAKNKV PEDQRTSELQ RYPSVKQWLE VVDIQPVAIR GIENKKISLE DLLKMTKVEI
VSLMSYYGAE EGETIRLLSA VNHLRTFTGD STTDLYWESW AGGFSGSPNT PPKRPSTSSM
PADFGDRDPP QTPTLRTPDR RASDTHDRTL YPSTGDSETY ISEDEEFPLS PSYLTNAGMT
PPSTPTILTR RPTPPATPPL RVIQKKMKTP GTPPPSKSNL QLPEYQLNPL TRSRSHEAQL
THRTTNKIED YNVLVGGTLP KVGRSMGHSI NHRYNNQFWM TQTCFYCNKA IMFKGFKCKD
CKVKCHHKCA QRAPPSCGLP PDLEKVFRDT LQGTAQWGQN WGSPIITSGR YAKVAANTAL
TVYSTDRIVC LTQDQMQVPP FPHGDSSSNP SSTTSSTPSS PFQPSSSDSQ PSPMTRQAFR
FPVLVKSICF PQCSRCNIKS VRFRGGQSRQ RRHHFKLTDT VDTVKSEDTV KSEESQGSDK
TEVADVSALF SRSWPTRQNS RSSVLSEWDI PYEELEIQDL IGAGRFGRVF KGKWHGDVAI
KVFNIETDND LQLASFKTEV SMFRKTRHEN LVLFMGACMK LPHLAIVTSL CKGKTLYDTV
RDRRETLNMS RIVNIATQIA QGMGYLHARE ILHKDLKSKN IFLENGKVVI TDFGLFSVTK
LIQYGERKDD TLAIPPGWLP YLAPEVITSL RATSQYTDSD LPFSQASDVY AFGTVWYELL
VGDLPFKTQP AESIIWQVGK GLRQSPSNVQ SRDAKDILMQ CWKTQPDKRP QFSDLTQTLD
RLPRKRLTRS PSTPLHLSRS AESII
//
