GenomeNet

Database: UniProt
Entry: W2XPE8_PHYPR
LinkDB: W2XPE8_PHYPR
Original site: W2XPE8_PHYPR 
ID   W2XPE8_PHYPR            Unreviewed;       774 AA.
AC   W2XPE8;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=FYVE-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=F441_03125 {ECO:0000313|EMBL:ETP23809.1};
OS   Phytophthora parasitica CJ01A1.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1317063 {ECO:0000313|EMBL:ETP23809.1, ECO:0000313|Proteomes:UP000018958};
RN   [1] {ECO:0000313|EMBL:ETP23809.1, ECO:0000313|Proteomes:UP000018958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ01A1 {ECO:0000313|EMBL:ETP23809.1,
RC   ECO:0000313|Proteomes:UP000018958};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica CJ01A1.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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:ETP23809.1}.
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DR   EMBL; ANIX01000704; ETP23809.1; -; Genomic_DNA.
DR   AlphaFoldDB; W2XPE8; -.
DR   EnsemblProtists; ETP23809; ETP23809; F441_03125.
DR   Proteomes; UP000018958; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00065; FYVE_like_SF; 1.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR46680; NF-KAPPA-B INHIBITOR ALPHA; 1.
DR   PANTHER; PTHR46680:SF3; NF-KAPPA-B INHIBITOR CACTUS; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 4.
DR   SMART; SM00064; FYVE; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 2.
DR   PROSITE; PS50088; ANK_REPEAT; 3.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00091}.
FT   DOMAIN          39..123
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REPEAT          493..515
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          530..561
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          597..629
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          659..731
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   REGION          141..357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          395..442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..166
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..231
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..356
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..442
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   774 AA;  84831 MW;  08D269CAB8051A55 CRC64;
     MSNEHAGDAP DWMQEQAAEY QDLVGSFVES VVDSDTDEIL EYQLIWEGGD LGVALTTLEG
     EDGGVAVSRV TGKGFPFGIK NVGPGDLLLS INMKDTTKMT LDDVVAYLQV CDLPATLRFK
     KLSPVTDQPP VSVPRKSTYV ITSGAQGPTS PMGSQAPPSY PRGSQRGSTK YAPPPAAPSH
     PDRASMPVHK TPSDFPEPPA PPQRQSAKVP ATQQMMESPP KPAPTPVPAP VAFTDKPTYV
     KPTTEEDYQL VAPSSPHKAK SDKQKPAAPP VAPEESLREL DGLVLTSGVN DLGFEDSEDE
     SVRASRESRD SWRDESFDVD ANHGDWKIEE EEKEDVPHVD KKNSKDRAKE RFQRDKSGST
     VAMLGHFSVE TKGDGVPILP DAEEATGIAL IDNVSDFSPE THPSPAHASG QVRPSDVSSG
     SMVSSLNSSM NNTMNTDAPR PSVRVTMDST APIMKSHPIG TLHEMCAKGN LRGVVQHLRV
     DGPEALLNRE PNHGQTGLHL AVKSGKVPLV KVILEQYKPL EDIINVEDDK GNTALHFAAT
     KTPAMVHLLL ENGASANVKN SRKFTPLIIS VITSKDDSVI IPRMLLKFGA NPNDMHDSQT
     VIHTAISTGR LQIAGALVRA GAKMDVEDAE GKSVFEKLPR KDLRYLISHI YFPPTYITRK
     ERSECMLCRQ KFKFGHREHN CTHCGRLCCA ECSALHVEMV KFPMGFPGRT RRGAANREQK
     RVCKTCYNVF KERNDEPEKS DMTKFINRVI NIEWDEVNPE KLQKAQEAGR RGEK
//
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