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Database: UniProt
Entry: T1G965_HELRO
LinkDB: T1G965_HELRO
Original site: T1G965_HELRO 
ID   T1G965_HELRO            Unreviewed;       998 AA.
AC   T1G965;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ESN96607.1, ECO:0000313|EnsemblMetazoa:HelroP95514};
GN   Name=20217612 {ECO:0000313|EnsemblMetazoa:HelroP95514};
GN   ORFNames=HELRODRAFT_95514 {ECO:0000313|EMBL:ESN96607.1};
OS   Helobdella robusta (Californian leech).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Hirudinea; Rhynchobdellida; Glossiphoniidae; Helobdella.
OX   NCBI_TaxID=6412 {ECO:0000313|EnsemblMetazoa:HelroP95514, ECO:0000313|Proteomes:UP000015101};
RN   [1] {ECO:0000313|Proteomes:UP000015101}
RP   NUCLEOTIDE SEQUENCE.
RA   Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA   Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA   Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA   Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA   Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ESN96607.1, ECO:0000313|Proteomes:UP000015101}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23254933; DOI=10.1038/nature11696;
RA   Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA   Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA   Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA   Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA   Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT   "Insights into bilaterian evolution from three spiralian genomes.";
RL   Nature 493:526-531(2013).
RN   [3] {ECO:0000313|EnsemblMetazoa:HelroP95514}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the MAGUK family.
CC       {ECO:0000256|ARBA:ARBA00007014}.
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DR   EMBL; AMQM01001431; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KB097495; ESN96607.1; -; Genomic_DNA.
DR   RefSeq; XP_009025270.1; XM_009027022.1.
DR   AlphaFoldDB; T1G965; -.
DR   STRING; 6412.T1G965; -.
DR   EnsemblMetazoa; HelroT95514; HelroP95514; HelroG95514.
DR   GeneID; 20217612; -.
DR   KEGG; hro:HELRODRAFT_95514; -.
DR   CTD; 20217612; -.
DR   eggNOG; KOG0708; Eukaryota.
DR   HOGENOM; CLU_001715_4_2_1; -.
DR   InParanoid; T1G965; -.
DR   OMA; WIASSDF; -.
DR   OrthoDB; 2879721at2759; -.
DR   Proteomes; UP000015101; Unassembled WGS sequence.
DR   GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR   GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central.
DR   GO; GO:0019900; F:kinase binding; IEA:InterPro.
DR   GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR   GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IBA:GO_Central.
DR   GO; GO:0043113; P:receptor clustering; IBA:GO_Central.
DR   GO; GO:0097120; P:receptor localization to synapse; IBA:GO_Central.
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; 1.
DR   InterPro; IPR016313; DLG1-like.
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; PF00018; SH3_1; 1.
DR   PIRSF; PIRSF001741; MAGUK_DLGH; 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:UP000015101};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          49..109
FT                   /note="L27"
FT                   /evidence="ECO:0000259|PROSITE:PS51022"
FT   DOMAIN          255..342
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          360..447
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          539..620
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          651..730
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          807..982
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50052"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          219..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          450..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..242
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   998 AA;  111500 MW;  0EDD4A3C18C2005D CRC64;
     MSMPVKQSEG LGHTDHMIKN DIDNSNNNNN INDNDDDDSL KNLSSKTMSR SDAHRALELL
     EEYYGRLIRP QDQNLRLAIE RVIRIFKSRL FQALLDIQEF YEVTLLDDEK SVEQKTDETL
     LVASRWEENP PIASNRPLSN CHSDNSNVSF CREQLKANMT TAATSSSSNR QLQTWTLSLY
     YQFVFDVILF FCFCVNALSK SLHQLSQQQQ QFQQLHYQQN NNTHQQQQQI PQQQQYQRQH
     QPPHPITLDD WEYETINLDR GGTGLGFSIS GGTDNPHVGD DPGIYITKII ENRAASIDGR
     LKINDMIVSV NGISTIDVTH AEAVAALKKA GNSVSLVVRR KKLMSSSSSS AAAPDDNVIL
     LELVKRSKGL GFSIAGGVGN EHIPGDVGIY VTKVIDGGAA QVDGRLQVGD RLLAVNEVSL
     DNVTHEEAVA ALKATREYVR LLIRKRPSYD DGSQPLTPLM GNSPRVMSSM PHLPMNHVTS
     PHPHSLQQQP QQQQSLINNN STMSRFGNVN SSYSSINYNL GRTFSRGDDE HDVGREPRKV
     VMKKGPNGLG FNIVGGEDGE GIFVSFILPG GSADLSGGLY RGDQLLSVNG IDITGATHEQ
     AAVTLKSAGD VVEVIVIYKP EEYSRFEAKI HELREQMMSC GNTGSLRTTQ KKMLFVRALF
     DYDPSKDSGL PGRGLIFKFG DILHVTNASD DEWWQAKKLT GYPGDSEDSG GIGGVGLGII
     PSKKRVERKE RSRMKNVKFI GKSVSFLFLF LATLPADKNK KKIFGKKLSF TKVKDRSGSE
     DALSADDLSD EPIASYEPVV QHEMKFPRPV IILGPLKDRL NDDLILEFPD KFSSCIPHTT
     RPRREYEVDG RDYYFVESRD QMEKDIQNHM FIEAGQYNDN LYGTSIKSVR DVAESGKHCI
     LDVSGNAIKR LQVAGLFPIA LFIKPKSYET VMEWNKRITE DQARKTFEQT LKIEHEFGEL
     FTAIVTGDTG DEVYQNVKEV IAEQSGPIAW IPSQDIYL
//
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