ID A0A0V0ZZG6_9BILA Unreviewed; 934 AA.
AC A0A0V0ZZG6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Disks large-like protein 1 {ECO:0000313|EMBL:KRY17893.1};
GN Name=Dlg1 {ECO:0000313|EMBL:KRY17893.1};
GN ORFNames=T12_873 {ECO:0000313|EMBL:KRY17893.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY17893.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY17893.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY17893.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the MAGUK family.
CC {ECO:0000256|ARBA:ARBA00007014}.
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:KRY17893.1}.
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DR EMBL; JYDQ01000054; KRY17893.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0ZZG6; -.
DR STRING; 990121.A0A0V0ZZG6; -.
DR Proteomes; UP000054783; Unassembled WGS sequence.
DR GO; GO:0030054; C:cell junction; IEA:UniProt.
DR CDD; cd00071; GMPK; 1.
DR CDD; cd00992; PDZ_signaling; 3.
DR CDD; cd11861; SH3_DLG-like; 1.
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; IPR004172; L27_dom.
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 InterPro; IPR001452; SH3_domain.
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 Pfam; PF07653; SH3_2; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00569; L27; 1.
DR SMART; SM00228; PDZ; 3.
DR SMART; SM00326; SH3; 1.
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; PS51022; L27; 1.
DR PROSITE; PS50106; PDZ; 3.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 4..64
FT /note="L27"
FT /evidence="ECO:0000259|PROSITE:PS51022"
FT DOMAIN 188..276
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 298..385
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 496..579
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 605..675
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 745..919
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT REGION 121..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 934 AA; 102840 MW; B4BCA6B7ABEC2592 CRC64;
MPVKKQEAHR ALELLEEYHK SLIRADDRQL REAIERVITI FKCRLFQALL EIQEFYEETL
LNEHKSLLQK TVETNLVADR WEGNPPIVGP NASNKTTDSY ASFVDAYKKS TSPTVATSTI
SSFPASLRGG PQRDLDSPGP FYTSAPSGQP KLFNNISQPV RDSWQDDSLA ADSRYTNGSH
DDNWEYEEII LEKGTIAGLG FSISGGRDNP HVADDPSIYV TKIIPGGAAA YDGRLRKDDI
ILRVNQIDTT DVYHHVAVDA LKQAGNIVKL FVRRRVRDDD ATATTAADCA VGAGVERRIE
LLKGNKGLGF SIAGGVGNEH VPNDAGIYVT KIIDGGAAQV DGRLAVGDKL LAVGNCSLDN
VTHETAVAAL KATADRVVLT VLKPISSGSA IPFADGNEPG LGSNPGLFDH SATTPTTIGG
TATALRLSRQ QEMRRAMGAG AEDALSASAS SSSYTPYALP EPAATVAERR HSVGAVFGEP
NADAGGVGLP GRSPRRVTLN KGGAGGGLGF NIVGGEDGEG IYISYILPGG VADVSGLLHK
GDQLLEVNGV DLRNATHEEA AAALKSGGQK IYILAAYRPE EYYRFEAKIE QLRNVMIDQN
SPQPRRELYV RALFDYDPSK DSGLPSRGLA FNYGDILHVT NACDDDWWQA RKRLKDGTED
GYGIIPSKRR VEKRERSRRK QVNFGSSRQS SMSEKHSGAR KQLSLSRKFP FMKSKERLHE
ELENERLEDY ILSYQPVEQH YLNYVRPVII LGALKDRIND DLTAEYPDNF ACCVPHTSRP
RREHEVDGRD YYFVSREVME HDIHNHLFIE AGQYNGNLYG TSIGSVRDVS EQNKHCILDV
SGNAIKRLQL AGLYPIVIFI KPYGPGQLME WNRRITEDDA VRVYQRCLQI EQEFGESFTA
VVQGDVPEEI YERVKEVIRD QSGPVVWVPS QEGL
//
