ID W2P681_PHYPR Unreviewed; 1544 AA.
AC W2P681;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=L914_00701 {ECO:0000313|EMBL:ETM56291.1};
OS Phytophthora parasitica (Potato buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4792 {ECO:0000313|EMBL:ETM56291.1};
RN [1] {ECO:0000313|EMBL:ETM56291.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAC_01/95 {ECO:0000313|EMBL:ETM56291.1};
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 IAC_01/95.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885};
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DR EMBL; KI690546; ETM56291.1; -; Genomic_DNA.
DR EnsemblProtists; ETM56291; ETM56291; L914_00701.
DR VEuPathDB; FungiDB:PPTG_00647; -.
DR Proteomes; UP000054532; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR PANTHER; PTHR11254:SF446; HECT-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50237; HECT; 1.
PE 4: Predicted;
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1093..1395
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1466..1544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..34
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..77
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..664
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1490..1516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1530..1544
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1386
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1544 AA; 171210 MW; 49AC04A352958375 CRC64;
MATAKREFVA KNLLDQRHPR KAGRRKPNHS ARGHRHLVKL SEEELSRREQ GWNDRFAIDP
PPKSNKVPSP PHSPTFSTPA TPLSKESRIQ NERAQYGKRG GKRNRAPKKP SSGKLVPLST
LSKPPPEAAQ PTKEEKLRFK VLKAIDARET LLYQLNALIL CTPVQESLFI PSRPTEPPTV
NNAGRQQMRS RGGMALAPAP LSRHSGNPGA MTNAREATKL AQQLATDLQV TGIQCVEALV
EWMLEAGAQA ETPPPFLWRG RNYFLKMFND LDFAESELAA RGVNLDCFKQ QNPLLIRPNQ
KLGRVLAAHS IILEMIEFAK EMTPMELLAL SGRMRDSDRE ETEADNGKTD SRTNSTAGLN
AANDNNDPTV NIEKMQLNTI NKQALERHDH ESAADLVNLL DESLDFTRES ASRDGDTKQT
DATNACEDEH YNSNDASEEK SARPMTGRSL TDAVDNNLEP DDGDEPLGNG EADGPTDNQS
DYGDNSMDDI DNNDEPCVPE ASAPQLKSEI SESPTEDTGD IVGPEQKHND TPADEIVPDI
EPEALGTTAE PGLGTEQHSP RSNTSDNQQE NDNSFDAKAG GRNDDGMSEA SDDVQQAEDT
LAVSVSAAPE TIVSDQTAPP ENSTHDEAIN RSASPEKLLT SRTEDTNGSE YDNSFDEDVD
EEKTSTDVNA DTRVTSPYSA IAPATIDNIS RIQGMEPDKH LVASENDQPV PETDDPQAIS
KRLESELKRW TFLEDENRPT EVNAQSCLMW HSTRALKENL QRHSSISECM EGSIISMLDQ
YGLTVPETPM RSLLWSDVAQ ELDLASHLIE ECQVVLDDIC SVVAEAIQAS LRLKNSLVSE
IEIQEVLETA EAVRLEYHNS TWEFVKIASM LLVFLLGADN DALASFKDRS PISVGLSRLV
KVFYPYLVNQ PREELSDNWH PVSSVLAAMG LSTDHLYIML DPMCKTILLA VKLCSWSNQE
SKDEGDLAIF PKVTVICDRE DVLQSSVEYV RRTHFSSDKA ISNFSLFPFY KSSFGEKLVD
GVKVEEGEGK GPLKEWFTLV GSQLASKWKQ VPLSNILADA YSTQVTASGN TITIPGASDM
ICPGFQVEWE TSEGETIRRV INKRMEHDNF LLDRSVQYHS FVASQLRLSQ PITAIFEYVQ
GSESYWLNET TRDSRENRNV LVFVGWFLAS AVTHFSSIQL RIHPLFFHLL LNPQHCVTLE
EIQSFDPQLF TSLSGMKDMK PLDFSQFLKF EGAHEGLSVE AYISNVLEEK FGPASGFGWQ
LQVIRGGFTR VIGIDQLSSV GITEADLVES ICGSNGGPGD DFVINEVFRV AADTDFTGCR
ALMNAFWQTV NSFEPQLKRK FIKFVTGVDT LPLPGTEFLR IEMPFTAISS DDHKKCAQML
PQAHTCDNML ELPNYWKALC WREKHDEKEP NSKLEEELVL LLSKKLRDAV EYSSGYGLDG
TSDVGGVRAD KSKDYADQLA KEESYDSLGL PALAEGGNAA DLPFEDTPPS PPRSDHDEAE
QDEAAKPADE LEAKPADSSE TAMSPRPEDS YDDDYDDWEE ESMA
//
