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Database: UniProt
Entry: E3M7V7_CAERE
LinkDB: E3M7V7_CAERE
Original site: E3M7V7_CAERE 
ID   E3M7V7_CAERE            Unreviewed;      1058 AA.
AC   E3M7V7;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=CRE-MAGI-1 protein {ECO:0000313|EMBL:EFO93861.1};
GN   Name=Cre-magi-1 {ECO:0000313|EMBL:EFO93861.1};
GN   ORFNames=CRE_12791 {ECO:0000313|EMBL:EFO93861.1};
OS   Caenorhabditis remanei (Caenorhabditis vulgaris).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN   [1] {ECO:0000313|Proteomes:UP000008281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG   Caenorhabditis remanei Sequencing Consortium;
RA   Wilson R.K.;
RT   "PCAP assembly of the Caenorhabditis remanei genome.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
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DR   EMBL; DS268427; EFO93861.1; -; Genomic_DNA.
DR   RefSeq; XP_003107962.1; XM_003107914.1.
DR   AlphaFoldDB; E3M7V7; -.
DR   STRING; 31234.E3M7V7; -.
DR   EnsemblMetazoa; CRE12791.1; CRE12791.1; WBGene00062589.
DR   eggNOG; KOG0707; Eukaryota.
DR   eggNOG; KOG3209; Eukaryota.
DR   HOGENOM; CLU_004562_0_0_1; -.
DR   InParanoid; E3M7V7; -.
DR   OMA; VECYADD; -.
DR   OrthoDB; 2902917at2759; -.
DR   Proteomes; UP000008281; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   CDD; cd00992; PDZ_signaling; 5.
DR   CDD; cd00201; WW; 2.
DR   Gene3D; 2.20.70.10; -; 2.
DR   Gene3D; 2.30.42.10; -; 5.
DR   Gene3D; 3.30.63.10; Guanylate Kinase phosphate binding domain; 1.
DR   InterPro; IPR008145; GK/Ca_channel_bsu.
DR   InterPro; IPR008144; Guanylate_kin-like_dom.
DR   InterPro; IPR020590; Guanylate_kinase_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   PANTHER; PTHR10316:SF40; LD27118P; 1.
DR   PANTHER; PTHR10316; MEMBRANE ASSOCIATED GUANYLATE KINASE-RELATED; 1.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF00595; PDZ; 4.
DR   Pfam; PF00397; WW; 2.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00228; PDZ; 5.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 5.
DR   SUPFAM; SSF51045; WW domain; 2.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS50106; PDZ; 5.
DR   PROSITE; PS01159; WW_DOMAIN_1; 2.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008281};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          157..246
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50052"
FT   DOMAIN          265..298
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          297..330
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          427..493
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          540..603
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          722..804
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          826..908
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          974..1044
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          358..399
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          614..696
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..377
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        668..696
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1058 AA;  115361 MW;  95B72F70D2F86CE5 CRC64;
     MVDQTAELHL KIGGTEGCEE EKDDFTLEIE KLQATLQEML DCTSSPSTSL DSTDKSPAGL
     SARRLIRIAS EHHHISTTSS CHSDSGNSSS RDFVTPFTVH GGASIGRLIL IDIVRRDDLI
     GIVSPNDILL TIENIKVSGM VRSEVNRILE DMMREHDQIA IEILPAGSIS DDICELLADR
     KSSGELQTII RENLYQKTVP YTTRPPREGE IDGEHYRFVS VDDFNKLLDN GDLLENGTYQ
     GHLYGTPRPV ECYADDDMML MGSEGLLPPN WETAYTENGD KYFIDHNTGT TTWDDPRELP
     PGWEQVDDQN YGTFYVDHIN RKTQYERPYG FGGSTATIDQ PIKYGTLPSS ANHNNMYSHY
     NSGTLKSSSS PRDSGFDSSP TRYRKFGDPP ETAASSADYD HHSKMFSRSS NPLFTTDPSR
     LGGELISTKI VKGAKGLGFT LIGNDASSRG DEFIQVKSVL TGGPAAANGV LRSGDILVRV
     NGRLLLGATQ KEACDVFVAI PIGEAVDIQV CRGYELFIDP TNRIITENVY AAAKNRDLHE
     IDIYKGPEGF GFTIADNLNG QRIKKILFPS QCPNLMEGDT IVELDGRNVR PIPHTQLVDM
     LRERPIGYRG KLVVRRGSPK TRSRTPSAAF RYGEPPSNMP DSAAPVPGRS KTPAGRQSSR
     AEEEQTFRNT LQRQPAVTSE WDGMNGSAPA SRMRPSSTTL GFATPNYIPL SQYNQKPSDL
     ITVSLIRKPV GFGFRLLGGV ESKTPLSVGQ IVIGGAAEED GRLNEGDEIV EIDGHNVEGA
     SHSEAVVLLE AAAQNKHVKL VVRRSTRIDA ARRGSLNSAG PSGSYDVLLH RNDNDGFGFV
     LMSSHHKNGS TIGQIQPGSP ASRCGRLSVG DRVIAVNGID ILNLAHPDII ALIKDSGLSV
     RLTIAPPDTA GPVLPVVSAT LGRNFTMNGH YESNNYGLPP PPPSIYEKHP PPTYLPFEGL
     SINDRIPMDG NLIDVSLERG TKGFGFSIRG GQEFGSMPLF VLRIADDGPA KADGRLQVGD
     QLTTINGQST KGMSHDDAIR IIKQHAIVNL TVLRNRLP
//
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