ID D0N7K1_PHYIT Unreviewed; 2550 AA.
AC D0N7K1;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=PITG_07230 {ECO:0000313|EMBL:EEY53550.1};
OS Phytophthora infestans (strain T30-4) (Potato late blight agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=403677 {ECO:0000313|EMBL:EEY53550.1, ECO:0000313|Proteomes:UP000006643};
RN [1] {ECO:0000313|Proteomes:UP000006643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T30-4 {ECO:0000313|Proteomes:UP000006643};
RX PubMed=19741609; DOI=10.1038/nature08358;
RG The Broad Institute Genome Sequencing Platform;
RA Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E., Cano L.M.,
RA Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T., Bozkurt T.O.,
RA Ah-Fong A.M., Alvarado L., Anderson V.L., Armstrong M.R., Avrova A.,
RA Baxter L., Beynon J., Boevink P.C., Bollmann S.R., Bos J.I., Bulone V.,
RA Cai G., Cakir C., Carrington J.C., Chawner M., Conti L., Costanzo S.,
RA Ewan R., Fahlgren N., Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S.,
RA Green P.J., Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K.,
RA Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D.,
RA Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L.,
RA Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J.,
RA Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M.,
RA Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S.,
RA Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D.,
RA Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J., Studholme D.J.,
RA Sykes S., Thines M., van de Vondervoort P.J., Phuntumart V., Wawra S.,
RA Weide R., Win J., Young C., Zhou S., Fry W., Meyers B.C., van West P.,
RA Ristaino J., Govers F., Birch P.R., Whisson S.C., Judelson H.S.,
RA Nusbaum C.;
RT "Genome sequence and analysis of the Irish potato famine pathogen
RT Phytophthora infestans.";
RL Nature 461:393-398(2009).
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};
CC -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily.
CC {ECO:0000256|ARBA:ARBA00006331}.
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DR EMBL; DS028127; EEY53550.1; -; Genomic_DNA.
DR RefSeq; XP_002905168.1; XM_002905122.1.
DR STRING; 403677.D0N7K1; -.
DR EnsemblProtists; PITG_07230T0; PITG_07230T0; PITG_07230.
DR GeneID; 9471565; -.
DR KEGG; pif:PITG_07230; -.
DR VEuPathDB; FungiDB:PITG_07230; -.
DR eggNOG; KOG0170; Eukaryota.
DR HOGENOM; CLU_228449_0_0_1; -.
DR InParanoid; D0N7K1; -.
DR OMA; HVKAAKC; -.
DR OrthoDB; 1093891at2759; -.
DR Proteomes; UP000006643; Partially assembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
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 Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR045322; HECTD1/TRIP12-like.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR45670; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR PANTHER; PTHR45670:SF1; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00547; ZnF_RBZ; 2.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 2.
DR PROSITE; PS50199; ZF_RANBP2_2; 2.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006643};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT DOMAIN 60..89
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 99..128
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT REPEAT 673..705
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 705..737
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 2253..2545
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1086..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1213..1240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1605..1648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1847..1887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..168
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..845
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..915
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..930
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1614..1631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1632..1647
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2517
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 2550 AA; 279842 MW; 108C7D2F5BA3E80B CRC64;
MDQSSAPSRG GRKRRGGKRK RSTSRQSEDE ERKTEEPPPK QEEEEDKQEE KQEEKQEDKT
PQKWSCPACT FLNEASRCFC EMCETANPSP SVSRELGAAS SDWSCAACTM VNPAAMRVCG
VCGTLNPRPP LSGLSIRLSD ALGGGEDESF SSSSEDSDDS DSDDEEEDTW ACTSCDTVLI
GRMCTNCFTQ RPKAARMAAA DKSKKQAKNR KRRKHEKLQE RAKLAYGVSI YELKKLLLEP
TGSRLVDTLQ TLTHTLAMMD ASADNEWADG PSFLTRGFGG GRSSETAKDP ELLTVLADLF
RGQERTYPVE VRLLAVQSIN YLMKMDRHTF ARAKMVEVVG LYISELLAWK NKNSTDTQNL
KSSQMIVEEC LSGLSSVCST ESFALRELLA REKFFGYLDF LLSLVDGDEK DGGFHPSIVM
TALGILQKCC MKLRWSGESS QKHRLNDMKK PSPKKIIQGG ELTVELASKL IGFLRHALEH
KHVPLHVKAA KCLLLVFHRI PHGQGGELVT PEALRKFVAV VVNTDGAESD ESRLAMVNLL
LHLFDNRAQL VNVFVREKIY TDLFSGVLQL LQSASTALRT NTLKLTAMLT RVVCRKHSLG
SFSSAQTSPK GSASRSPRNS RNRQRVNSLP DPDVLSTLLL DFIRTDSIPA VNVLLKDGAD
LNFPKLYDVH GHEIDKPLNV AVESASLGMV RLLLKRGADV HQVGIGGTAL HVAARTGRCD
AAAFLLQCGA RIQAKDREKK SVMDVVIAAD KAASETCGVA SIPSPMTKLL ELHQRTTGMR
EYDSDLSEGD EMIAGRSRAW FCPSDHDDEY GDDDEMDDDL EGEGGYFMDY DDDDDDDDDD
DDGEGLGGGA GLRDDMEDEE IPSDDDMVYL GGGMSSKSRS TNKRRLGSVS SESMSTDEAP
QSTTSGSSTN STRRRRASSA SDKGCSDEDT AMEQKTFSAT ADEIYDFSLA ITECLLAVLH
DMDVQNVERS VISTVACVLE MAPSRLILDL VELFEEANSI TTYEFKQSEL LPAVLQYLSP
QGVLDEARAT ALMQTFERCP AALKHLILRL QSIITQEEAF PLVSYNTGKG RELYPLTRQL
RIAFMRPGDR GTGDRSASSR PKGKSIQSSP MTHFQSFEKT VFRSMPVIDS DLSLLYLNLV
GRSVQKVAEG KWKKFLVVGY DDTRSYHLLK PIDGTNDDLV EMVLHDSQCK LIKSIEVYEG
ITLDLELFGS RDAADSGGNS DSKKKRKINK RKRKASTLKQ QLESDGALQV EVKNSGVLKM
RSLPGAWYAA VLLDDSGEVR KSSDGKSPTR EEVLAAQAVH SVKLLTGNRV VHKVPADCIR
PRALQPQVGS VVEVDGSLGE VTRVYTNDRS SSTPANTLLD VKVNSYTEKK RVKKDRVRFP
PRDLSTLKEG DESDRIEAMS IRRLFPARDS SLLAGSVGDR VWVLPPTGSS VKDLCVAGTI
KSFPSGLDSI RDSSTVVVEI AFGSDQPSLA VKVNQDRVLN FAVDGGVLSG RGPSRLLAAL
QMASDRGGSS RLFGGGRSGQ DSAIHRAFER VAGSLQQSRL GGGLGSSGSA MDQIRSLISR
ASTAGGANAP SDIETADQAS TRLNSPPNEL VGSELVGSEL VGSELVGSEG QTEEEASALI
SASSTNANTS RQRKSSDREK PSEESVEAYV KKPQGTKPKM TCSLLPKVTV VVGFRKCDVS
APSQDRIVVS SEFGLERVDR NKVSKDAAAS LLTQFDPSTQ QYEPKIGARK ALLDVFHTNS
QESVSAGSQK KKRRKLTAET QRKASEAATW DVEKFIAFMQ AVRDPSKYGN PGSSAKYCVT
FSKFADPNTG RRVLKADGFI SLIGHECKDA VKSKQLLKFL RSRGYSEKSL TSGGSRSSSG
DDDEVKDPLN DASKTSQAKN PGKKALRQPV VLRAFPADRN ILKCVEELRQ EHQARSRTNT
SDTSSFAADS ALPPWKLTYK LYCDFQVEWE AQSPPETVAS DAHNSGAVSV EPLAVLESKP
PARLLLRGIV EFEEMNASSA AEASRWLSRL TAPQTGSDKV VVSDSVASAV RLLRYLFQSR
GDSASLDEAL WTSPRLYNKL ETQMQDVLSM CSGIYPPWCD ALVTHCKFFF PRELREKLLR
ATSFGCARSL HWLRNQLNIE ESSADSMSSM VGGGIYNQTI SITPMPKERV KVHRKNILQS
ADAVMKMHVK RKAILDVIFA GEKGYGSGVT AAFYSTTAHA LQAITENQKS KYWIPGEDDE
AEAGKAAARR KDEMDVTDEI AEDAAVIRHS NGLFPYPHRI PSSKLVERFR MMGRLAGKAL
MDGRLLPLPL STHFMKLVVG ESFGLEKLGD IFLSHGRVLY SMYKASKKLA AGEQNVQIDQ
MDVQDWLEAV GFTLIDPFSQ EPLVVGGDDI AVTADNLPLY VRAVLELWLD SGIRAQVLAF
REGISEVLSV GKLRLLFVPE LISLLCGEED IKWDVESLVK DTKLAHGYTK DSQPVQFFFE
ALEEMSAAER RAFLLYATGC PNLPPGGFQA LKPPFEVVRR VVDNLDVDRA LPFARTCTNT
LHLPAYSTKD VLVKQLTFAV ANSRGVIDRD
//
