GenomeNet

Database: UniProt
Entry: V9FIC3_PHYPR
LinkDB: V9FIC3_PHYPR
Original site: V9FIC3_PHYPR 
ID   V9FIC3_PHYPR            Unreviewed;      2283 AA.
AC   V9FIC3;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=F443_05434 {ECO:0000313|EMBL:ETI51235.1};
OS   Phytophthora parasitica P1569.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI51235.1, ECO:0000313|Proteomes:UP000018721};
RN   [1] {ECO:0000313|EMBL:ETI51235.1, ECO:0000313|Proteomes:UP000018721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1569 {ECO:0000313|EMBL:ETI51235.1,
RC   ECO:0000313|Proteomes:UP000018721};
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., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica P1569.";
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:ETI51235.1}.
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DR   EMBL; ANIZ01000941; ETI51235.1; -; Genomic_DNA.
DR   EnsemblProtists; ETI51235; ETI51235; F443_05434.
DR   eggNOG; KOG0940; Eukaryota.
DR   eggNOG; KOG1729; Eukaryota.
DR   HOGENOM; CLU_228648_0_0_1; -.
DR   OrthoDB; 55984at2759; -.
DR   Proteomes; UP000018721; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00065; FYVE_like_SF; 1.
DR   CDD; cd00201; WW; 2.
DR   Gene3D; 2.20.70.10; -; 2.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR005735; Znf_LSD1.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR23164; EARLY ENDOSOME ANTIGEN 1; 1.
DR   PANTHER; PTHR23164:SF30; LD23155P; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF00397; WW; 2.
DR   Pfam; PF06943; zf-LSD1; 1.
DR   SMART; SM00185; ARM; 4.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF48371; ARM repeat; 3.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF51045; WW domain; 2.
DR   PROSITE; PS01159; WW_DOMAIN_1; 2.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018721};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00091}.
FT   DOMAIN          72..105
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          106..139
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          360..422
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   REGION          135..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          270..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2175..2207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..167
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..227
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..300
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        323..338
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2175..2194
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2283 AA;  251964 MW;  F932BE68B2E6B594 CRC64;
     MYAAVVYSSW EVHHCTNSCT LHTCIYLIAT FILIKLFAIV RSCRQHEMGT EKVPFGIVRF
     QCQYQKSIAS MSSRHGEWQR VQDAQGRYFY VNHATRETSW HLPSAEPLPP GWEELIDGQG
     RLYFVDHNTR TTTWMDPRVA AARRRTRGQS VLSSRPPSRS NIPPMDNARG RSPTYEDPRH
     ASVGSAGSRS DAGSNGFVRS RKSSGANLSA GSPSSSGARR DSADQTIRMN TSTLLERYRD
     ETNLGDTAVM QTTESTALPA DAEEWFTAHS EDLSRRSSVE KKEPELEQVT DSKEETPSAG
     VQEEETAASS SLVEEEKDLA KSGQQQQQEQ RVSGVRGSSF NTGDVQMVLR RYFAPNFVRD
     DDSPACRQCG MRFGTFRRRH HCRLCGNVYC ADCTTNKVKL PIEAPSYDKE QPVCTRCFRN
     VQAGDFFSIV GLRHKLEDPS STVDDRVEQI MQLSMTLSAG RPETDGNMGL HRVAQLNDVE
     AAGGVASFCQ LLTTDVEPLQ QAALEMLANL IELENSAGNE LSAGEAFANS GACAQLVKVM
     GNRVMEQQLG RSVRPEVERM ALRLVYHICQ STTCQNALRK AGGGTRLLEL LSVDSPSSLE
     MRVEAARCLK RFVQKNGENI TEMTQNKGVA LLCTLLGDFI ELRAGSNLGN SGVEATRDES
     HEVAMEAILS TICECIHFAD NGASQVQRGV QQIPADSIHS FVTVLQKGDR VNRMLASQVL
     IQVSKEPSLI TILAKEQEFI KEIMWMLDSD EDYTVASEIL CGLCSTMPKQ SLSDTVPGEN
     VDDAHEQVLK VIYDLEVFDL VLKKLNACVV GEKQLVGEIT FQRNLLGITM SYSAESAAYV
     DYICSRNCVP TLSAFLLSRK ERLIPLCAQT LMNLCEFNPS IFDELYDRNV SDFFHRLLQT
     PPDENRLSAL RYFRALVDNK RPFSVGVLDT LFLMASGRDE VLKAGSLDVL AHLSGVKSIG
     AVLEPLEEPP TPEIGEMVQK LQERVVGVAY FPVLMTIACS SGDTDMRSNA IKCLSCAVGG
     GEELVARMLD QEMLRAFWMG LRRWMDVPAD ELTPVEMQLN KALLQLLYLV LKMASSRIAS
     MGEDQVTNLV TVVTEFIVSQ PSRLVMGIRI IRLLIAHAAW KDSFVALYAV ESTSTGLKFL
     QALMNGIEQS SVTAKEDSEN TVFDDSVAVL KELIKDPQQF EEDDEQGGVA MANDAIVNLI
     ISAGVHISLL ELLRDNAVRE SIRKTQASVD SEADEKSEES HEYVVTRALE LLDLLARSRR
     IRLLILEAGT ALDALVTAYE GTTDDYAESS PARQLIAQDL GRILIHLSSD PLEFRKTLYD
     HRGVLPSAIL GNILSPVAEV AETAEEIVLN LVESDFATCP LWVDLIESAN VRLVFRVVVV
     AKRPSVKVTA ARKLIDIVFS HPNILDDEED GLSPEEKSTL VSMLIDFFVD FDPRTSVVGV
     LALTLLLKNG QTLNEEQMEK IAVDGAVSLV YWMQKGTERH QENAVKILHD GVKDPAILQK
     FYEQLQAPSV QRETAFLLEL GQQLLDVEIK SNPEGLFKRC KLLQGLLEVT DYDSLPSDCM
     EIVEEVSAYL LELTEEKGNE TEHKDEDADE KKTREKFLLV ITNFLAVLVS SSTFHSTLVH
     QDAIEKLAFV LNEQKKATES SALVVDQTRR LLKQLCVHEV PRLVACNGVE ILLETVMKHD
     EDSEEGSERV AEMLETFNSV VECGSAGKSA LMDTEGFLSS LSRGFKTVCG DLSEDQEVLT
     AKLLGTDFDG RSTNMEVACG LCLLVFLLAR GGAYRERVFK DTELMQHIVT MMAWFPSIFS
     TSDKVVTPEL KAKFGLIFAS GLPFLEAALV SAEGSMLDSD DKELFFRKTM SVYTKTLTTF
     ANGHESSDLF LASCEGLKSL FHSDSAVSVL ADDGQKELEI LLKEQVFRSL KATIYSMGCV
     VALLDIAVAV IPARPVTPDE EKEPARSSWL VAGVLHALFN FEAFGDDLDV SVLFTLLRRF
     CSSAMIRNSL YEHVDYDRLV EILVAFAQDS KWRRWRKYAL SVLLLLGEDG ALEQVSHDRG
     TMPMLQASTT SSFRDRDSEQ STCATRCFHC RQVVHAPVQV NLCVMPCPYC QKSIAVASDN
     ASTAVDTLPS VVEHNGSITL DNGAQSKISS DGSDFVCVNC SNVLELPDGL GPSEIVCPHC
     LQLASVKKTS QSVMPAFSSE KKRSSASSVR SVESGASLPK DPSMSGIDVR DTKVVSCGHC
     GKHLIVKNGA SAVKCPSCHG VSKLSTTTTQ EMMRCKNCNT LLSLPAGARA YKCMKCLQTT
     RLS
//
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