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Database: UniProt
Entry: W6U8K2_ECHGR
LinkDB: W6U8K2_ECHGR
Original site: W6U8K2_ECHGR 
ID   W6U8K2_ECHGR            Unreviewed;      1029 AA.
AC   W6U8K2;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Protein phosphatase 1 regulatory subunit {ECO:0000313|EMBL:EUB57588.1};
GN   ORFNames=EGR_07530 {ECO:0000313|EMBL:EUB57588.1};
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:EUB57588.1, ECO:0000313|Proteomes:UP000019149};
RN   [1] {ECO:0000313|EMBL:EUB57588.1, 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   -!- SIMILARITY: Belongs to the NRARP family.
CC       {ECO:0000256|ARBA:ARBA00038386}.
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:EUB57588.1}.
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DR   EMBL; APAU02000080; EUB57588.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6U8K2; -.
DR   STRING; 6210.W6U8K2; -.
DR   EnsemblMetazoa; XM_024496779.1; XP_024348784.1; GeneID_36343245.
DR   OrthoDB; 5482573at2759; -.
DR   Proteomes; UP000019149; Unassembled WGS sequence.
DR   GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR   CDD; cd21930; IPD_PPP1R12; 1.
DR   Gene3D; 6.10.140.390; -; 1.
DR   Gene3D; 6.10.250.1820; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR031775; PRKG1_interact.
DR   PANTHER; PTHR24179:SF21; MYOSIN BINDING SUBUNIT, ISOFORM O; 1.
DR   PANTHER; PTHR24179; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 12; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF15898; PRKG1_interact; 1.
DR   SMART; SM00248; ANK; 5.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 4.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
PE   3: Inferred from homology;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019149}.
FT   REPEAT          50..82
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          83..115
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          176..198
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          210..242
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          919..1024
FT                   /note="cGMP-dependent protein kinase interacting"
FT                   /evidence="ECO:0000259|Pfam:PF15898"
FT   REGION          270..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          752..817
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          860..907
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          963..982
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          924..958
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          992..1019
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        287..333
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..383
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..422
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..462
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        757..799
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1029 AA;  112241 MW;  00776FEFC1CD66CB CRC64;
     MNKEIVTPRP ADRVNFPIEV QFHAACKNSE LDEVKELLSK GVDIDVANVD GLTVLHQACI
     DNNYEVVQFL LSNNANVNAQ DNEGWTPLHA CASCSYTELA KLLLEHGADA GIVSFEQELP
     LDVAQGGDMV ALLKDWMQRQ SIDEKAARGA EEQQMLNDAR EWLRSGQYPS VVDPRTGATA
     LHIAAAKGYS EVLELLLKLP NVEIDATDVD GWTPLHAAAH WAKEKPLRLL AAAGASFDTI
     TLTNQSIYDV ADRSVTMLLR QLRIEQQRTA AAAAEEKPVV APPTVATRRK AEDDEKEISK
     SRKMMEVEEE RIKVEDDVKP AASKVPKTTQ DNEEKEAEEE EEEQEATLPK VQKDEIAMKI
     EKEEEKKARE RLLEKEEVKE AEKPSSSSPS QPTVAPPIKE EEESKVEEQP TTPMKEVEKV
     GEKSAVPSPP PPPPQPQTAN VAGVSSVKTP HSTNQNSQVS ETVVTLDTTS ISTGSGPSRR
     ISAVLAPARS EETEAQRSSK ARLVRSTRRS TQGIANDVLE EAKRLSVAGA STPTSSTTTP
     AVAAIVSPTP VQPIDKAIAS SFTSSFISPV SAVASPLFLH MHDRLCLVRG IPSKVARAPE
     MKQANCFHVC VRLRISFRVE FSFSSYDFSL VEFINTTTTT ATTTKITTAI LCLKGHTGSP
     CSTGEMFLIL TPLYLSHFFA EKITPQPDSQ SLISRLHRNA FIGRVNRAES FEVSISCEDT
     ESRVSPPRGP RLSISLRSVR CLSARKLPAG LDLDETEQKP TSFTSTTHVS KATITPTQSS
     SATTTAPAAD TSPSSIITHT RARRAARDRV PTGRLNTNDV LAAAKQVEQN ASIDNTAAAT
     TTTTVADPIP RPTTRALRST ILNTTPSTTT NDAVSNGAGG DRHNSPATSQ FSPTSSSASP
     VSSVGKLSDQ RYNWRENLDY RLLYEEERSE KERLKRTLDQ VNREVAALRS ELARLHVSNS
     ASTTLNANRH GSSASNTDAS PAALQRRSVD FFEDQAKEID RLRQENARMA DENKSLIRVI
     SKLSARTTS
//
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