ID W8BFX6_CERCA Unreviewed; 604 AA.
AC W8BFX6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Serine/threonine-protein kinase dkf-1 {ECO:0000313|EMBL:JAB95853.1};
DE Flags: Fragment;
GN Name=DKF1 {ECO:0000313|EMBL:JAB95853.1};
OS Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC Tephritidae; Ceratitis; Ceratitis.
OX NCBI_TaxID=7213 {ECO:0000313|EMBL:JAB95853.1};
RN [1] {ECO:0000313|EMBL:JAB95853.1}
RP NUCLEOTIDE SEQUENCE.
RA Geib S.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAB95853.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24495485; DOI=10.1186/1471-2164-15-98;
RA Calla B., Hall B., Hou S., Geib S.M.;
RT "A genomic perspective to assessing quality of mass-reared SIT flies used
RT in Mediterranean fruit fly (Ceratitis capitata) eradication in
RT California.";
RL BMC Genomics 15:98-98(2014).
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DR EMBL; GAMC01010702; JAB95853.1; -; mRNA.
DR AlphaFoldDB; W8BFX6; -.
DR EnsemblMetazoa; XM_012306539.1; XP_012161929.1; LOC101453779.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd20817; C1_Stac; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR039688; STAC1/2/3.
DR PANTHER; PTHR15135; STAC; 1.
DR PANTHER; PTHR15135:SF7; STAC-LIKE, ISOFORM J; 1.
DR Pfam; PF00130; C1_1; 1.
DR SMART; SM00109; C1; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 2: Evidence at transcript level;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000313|EMBL:JAB95853.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transferase {ECO:0000313|EMBL:JAB95853.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 438..487
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT REGION 490..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 285..312
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 495..511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:JAB95853.1"
SQ SEQUENCE 604 AA; 67460 MW; 461B60721AA2F68C CRC64;
NFKLIKTVSD FTETLSHLYE EHATALQTLV SNFRKKNAEL RKERPACHLA IFQAWEAFLQ
EVETDSQASN DVANVLSRQV SRPMLDKSFH RKVQSRKIFT HRESFETIIA KTEEKLAKCR
LDYKQCYLSH RQNPTQLSLT EYIDAHNAYV QQLHATNAML ELYHCETVPQ LMQELEEIHN
DLCNIIAESI LQGADVIANK ASDQAKRYGA LTIQCNTVSP IQDLTNFVRI LPLPSLAQKV
PKRNFTPPQP PGEIDDNGDF NEMAPILRNE LVFDRHSTLA LRPALESLKR EANDLEMQIR
LLQDTVDGLI RTQQRGIEGQ LYNKVNELQE DLSLKKFDLR AKQLHFAAIK AQKDLYVSKV
DPGSPRAERK LSAATAPSMK TKWLKAFRSL KPASGSAPAD SQPRPNQMYH AVSTVLTLRR
NGAAGSSSQP LRPNEDGSHH LQEYTYKKIT ACDVCSQILR GHTRQGLRCR ICKLNAHGDC
ASQLPRCQPK QKLLRRQKST SELENRVDVE EENTNSSPAV RSPGEPLMLN KKILKNSQSG
GSEQSPNDVS SLSEIACASR ATPSQSSRVA TPAPSEGGGS VSGCVGRNSN AAAAKTSKKR
VQLK
//
