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Database: UniProt
Entry: A0A1I8FXU1_9PLAT
LinkDB: A0A1I8FXU1_9PLAT
Original site: A0A1I8FXU1_9PLAT 
ID   A0A1I8FXU1_9PLAT        Unreviewed;       542 AA.
AC   A0A1I8FXU1;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=MAGUK p55 subfamily member 4 {ECO:0000313|WBParaSite:maker-uti_cns_0000306-snap-gene-0.4-mRNA-1};
OS   Macrostomum lignano.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC   Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX   NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0000306-snap-gene-0.4-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:maker-uti_cns_0000306-snap-gene-0.4-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the MAGUK family.
CC       {ECO:0000256|ARBA:ARBA00007014}.
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DR   AlphaFoldDB; A0A1I8FXU1; -.
DR   WBParaSite; maker-uti_cns_0000306-snap-gene-0.4-mRNA-1; maker-uti_cns_0000306-snap-gene-0.4-mRNA-1; maker-uti_cns_0000306-snap-gene-0.4.
DR   Proteomes; UP000095280; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 1.10.287.650; L27 domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR008145; GK/Ca_channel_bsu.
DR   InterPro; IPR008144; Guanylate_kin-like_dom.
DR   InterPro; IPR014775; L27_C.
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   PANTHER; PTHR23122; MEMBRANE-ASSOCIATED GUANYLATE KINASE MAGUK; 1.
DR   PANTHER; PTHR23122:SF42; MENAGE A TROIS, ISOFORM A; 1.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF02828; L27; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00569; L27; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF101288; L27 domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS51022; L27; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        273..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          59..116
FT                   /note="L27"
FT                   /evidence="ECO:0000259|PROSITE:PS51022"
FT   DOMAIN          133..214
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          335..528
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50052"
FT   REGION          212..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          300..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   542 AA;  59347 MW;  32E2470984992DCC CRC64;
     MLQLQQGICD SPLSMESLIK SGSLSSDDKE FLQQFSNDAN MNAVVKLCDI LEGYLARRVA
     PVTPSALEDV VEAYDYLRCH PHAEGCHELV HLLRKPHMKA LIQCHDDLAN RTYGPRLSPV
     PHEVDEDDVS VKIVELVKQD EPLGATIKIN ERTGAILIAR VMHGGLADRS DLLQAGDEVQ
     AVNQVLVAGQ DPMTAIRMLT TARGNVRLSV LPSERRSSST AGGVGSVSSG GQQQVGVSPA
     TVRVLFNYNP ADDGLIPCQE AGLCLRLGDI LQLLILLVTS LLSSMLSYFL LFVLSKKADS
     SGSDQQQPPP QFYEELGRFY PGQPDGPTGS PVPPYRPLVL IGPSGVGRRE LARQLVGTDR
     EHFALPVLVS TRSQQRPEPF VSLTAAQIRA LAEAGRLAEQ WTEDGGNETW ALPVDSLTKL
     LRDGRVPVCV PHGPPPHCLL GLRTPSLRAF VVYVKPPPLD VLRETRAPHL LQQQDSLYDT
     GRQLTLSELE AMVIEGQRME SACAHLIDFT LVNDDLPVAL ETLSELAYRL ETDFSYVPKH
     WL
//
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