ID W6UY62_ECHGR Unreviewed; 1251 AA.
AC W6UY62;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Disks large protein {ECO:0000313|EMBL:EUB58499.1};
GN ORFNames=EGR_06680 {ECO:0000313|EMBL:EUB58499.1};
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:EUB58499.1, ECO:0000313|Proteomes:UP000019149};
RN [1] {ECO:0000313|EMBL:EUB58499.1, 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:EUB58499.1}.
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DR EMBL; APAU02000061; EUB58499.1; -; Genomic_DNA.
DR AlphaFoldDB; W6UY62; -.
DR STRING; 6210.W6UY62; -.
DR EnsemblMetazoa; XM_024495929.1; XP_024349695.1; GeneID_36342395.
DR OMA; WIASSDF; -.
DR OrthoDB; 2879721at2759; -.
DR Proteomes; UP000019149; Unassembled WGS sequence.
DR CDD; cd00992; PDZ_signaling; 3.
DR Gene3D; 2.30.42.10; -; 3.
DR Gene3D; 3.30.63.10; Guanylate Kinase phosphate binding domain; 1.
DR Gene3D; 1.10.287.470; Helix hairpin bin; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR015143; L27_1.
DR InterPro; IPR036892; L27_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR PANTHER; PTHR23119; DISCS LARGE; 1.
DR PANTHER; PTHR23119:SF51; DISKS LARGE 1 TUMOR SUPPRESSOR PROTEIN; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF09058; L27_1; 1.
DR Pfam; PF00595; PDZ; 3.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00228; PDZ; 3.
DR SUPFAM; SSF101288; L27 domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 3.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS50106; PDZ; 3.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000019149};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 216..306
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 536..624
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 745..832
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1051..1235
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT REGION 104..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 980..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..1009
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1031
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1251 AA; 137439 MW; 524F608BF26DD837 CRC64;
MHSKRSAERA LREIIDFRDG LDKRTDKELI AALDCVVEVM QNHLYHAYLE VRDFYETTLL
SMAIPMKVKA DMALDIAGRW EQIDKSSSAL STFYTHSDRS SNELASGVRS RSLSHLTRPV
TLEPGACKRS SARDRTSVMT SSFGRLDLRR HHHRYEHRLH QHNNNQEQHH SRRVRDNGEP
LFDDNTEASS QSPSFGSVSV SNSSSERRRG FSSIFRVQLT RGPQGFGFSI AGGTDQEPPL
PTIDARFVYV ARITPGGVAD LDGRLRVNDV ILSVNGFGLV GLPHLKAVTI FEKSGAHLDL
KVQRPQSAFA QEISRPVHLP TSPKISSTVS KRVHADRGSG GETHAASVRS RVTALSRSHC
IILPAASNSP SPTESSGPPP TTVSPLSSLI TSCQHPPLSA SSNAEIPRKK VMGAGMGTAV
TTAVKVVEEE RQHNEGDVEN EDEDDTVWFF DPEQTGSGRS VLQTTSNTNS RDLDADAASS
NIKVAVEDNA LSKPAVESER KRIYQMKKPS SPIPIDQWEL STRPQPDPSP GPIIVEVPLV
RGTSNGFGFS IAGGIGTEFL EGDSGIFITK ITSGGVADTS GRIAVGDRLI RVNSVSLVDV
THAEAVEALN TAGDFVFLLL VKVPLQSSPQ WINRRQCQET VRNLRISPNP STNKEGQITD
RHPPIAAAEG LAERGQSHRR RPERRRLMPQ QLQSTVLGPF NRTVEALPLS SSSHGSEDYA
AAHAVPESIL QRWPRARLVT LYKEEVPMAS NGVGGRSGGS LGFSIVSGDA TDGIFVSHIH
PKGPAASSTA ISVGDRLLMV NSTEVVGSTY EEAAILLKTA PSRVDLVLSY APTEYKKLED
QIRTQTEVRS DDTEGEGDEY DNEGAPSRLC RSIEADGLFV RVLVNFDPHE VTELDQVIPC
SAISVRSGDI LQLINITDRE WWQPLGPAGL VPSRCRLEHQ ERVKWRVLFG RRSCLLRASS
SETSSPLVSD PQSTDKAIES IPLSQSDGPI ISSKQSSFPE ASAAETRSQR RSTDSSRVSK
KSAPRRAHSE FTREILPPTY IPVTSMQTVN TRPVVILGDL KHNISEDLLS EFPDDFSTCV
PHTTRHRRRG EVDGRDYHFI KSRSRMESEI QLNRYIEAGE YNGNLYGTHL HSVFKVASAG
FHCLLDVSTM ALQRLTAAGL PPIAIFVLSN SPGQSLGAVN RTGAIPKQEK TVHNRLTKRR
EKNFTFLREY SPLLTAILID DDYDKITERI HKIVQDNKGP NVWIASSDFL P
//
