ID W6UVY5_ECHGR Unreviewed; 961 AA.
AC W6UVY5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Protein kinase C-binding protein {ECO:0000313|EMBL:EUB57624.1};
GN ORFNames=EGR_07500 {ECO:0000313|EMBL:EUB57624.1};
OS Echinococcus granulosus (Hydatid tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus;
OC Echinococcus granulosus group.
OX NCBI_TaxID=6210 {ECO:0000313|EMBL:EUB57624.1, ECO:0000313|Proteomes:UP000019149};
RN [1] {ECO:0000313|EMBL:EUB57624.1, ECO:0000313|Proteomes:UP000019149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24013640; DOI=10.1038/ng.2757;
RA Zheng H., Zhang W., Zhang L., Zhang Z., Li J., Lu G., Zhu Y., Wang Y.,
RA Huang Y., Liu J., Kang H., Chen J., Wang L., Chen A., Yu S., Gao Z.,
RA Jin L., Gu W., Wang Z., Zhao L., Shi B., Wen H., Lin R., Jones M.K.,
RA Brejova B., Vinar T., Zhao G., McManus D.P., Chen Z., Zhou Y., Wang S.;
RT "The genome of the hydatid tapeworm Echinococcus granulosus.";
RL Nat. Genet. 45:1168-1175(2013).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EUB57624.1}.
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; APAU02000079; EUB57624.1; -; Genomic_DNA.
DR AlphaFoldDB; W6UVY5; -.
DR STRING; 6210.W6UVY5; -.
DR EnsemblMetazoa; XM_024496749.1; XP_024348820.1; GeneID_36343215.
DR OMA; ICEQEAS; -.
DR OrthoDB; 764287at2759; -.
DR Proteomes; UP000019149; Unassembled WGS sequence.
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; cd05841; PWWP_BS69-like; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46453; PROTEIN KINASE C-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR46453:SF5; PROTEIN KINASE C-BINDING PROTEIN 1 ISOFORM X1; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Kinase {ECO:0000313|EMBL:EUB57624.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000019149};
KW Transferase {ECO:0000313|EMBL:EUB57624.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 171..222
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 257..327
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..654
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 961 AA; 106165 MW; 36B3D358EF6036FD CRC64;
MPTRRKSAAK SRTPSRSSNT RFTDKGDSST RKKRRRISRD RLEDGSTPDM LDSLLTDPDW
NSLRESTGGR SSRNSSRTNR QSETRTPTPV RGRCVSLIEG TTVVQPVSSP VKKRSRNSRK
QGLENIQMSL LSQTEQTDWL LPRRSTGPMS PGLVPNIKAR HPSDSSQEAV DDFCWICHRP
GQLKSCSSCP RVYHSNCSNI PESKSGEGLS HENWQCALCR ELALGTSDGV KWGPVVSTVT
YENQLNKALA FMIDFLSIQS WAEPFRESVD SSENFGTSGA IRYPMDLRTL LQRVNAGQYK
STNAFLADFL WIIHNCFISE EKPNPQLLVK ARSLEQACLC EIELLRACPT CYLNRIIALP
VLPSTTFIFP AISKCEPHIY RRPEMRKPTE HLTTDLAEGL WFTKPCVSLL ILLASSKHDP
PSTHWEFSSK CNEVQTTVIH PVVWVRFEEG RRWPGKMMAE LPNKLLLVSF FGTYATRKTP
PNYVTLHTCL SVSVNANTPS GAAATTTAYS EKETEGGLRR LPDSGELKDA ETHARACEEL
RRHLSLLVQA FPKFRFPAAP ASRVLPFSQH IIKQHYGSFN QWILAGNNLP SPASSESGAA
ASPGPTGDEV DFVHTSESCL PSSPSLATSV PSATPPAPSP PLPPPPPPPS FQTRLASAPP
QSSSSSSSTF PLSGTSRSLT SEDFSEPLLA RLSTNLLSSF RNSHGDREGP PHEPLCSFPH
TDAGDKVQDS ERNTNVQVGN PVYENVEAPD METTPATDST SSTLPLRHLD NTPSGDPKAD
LIARFQEARD LFSGRFQSLM ESVFRNLEES INETCSISTA ATALGASAAS TAASEVEAPI
QEATLITTHD RETQTASNVV VSAQFLEENK MKMALLRAEV LRQSQELERL RLLLDYTRYE
VASSHRDRLT ELRAVWEAEL LAAVEGVVKI CEQEASRLID VVKRKQWVSA HFLHFLAVDA
C
//
