ID W2YH08_PHYPR Unreviewed; 2720 AA.
AC W2YH08;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=F442_17675 {ECO:0000313|EMBL:ETP33923.1};
OS Phytophthora parasitica P10297.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317064 {ECO:0000313|EMBL:ETP33923.1, ECO:0000313|Proteomes:UP000018948};
RN [1] {ECO:0000313|EMBL:ETP33923.1, ECO:0000313|Proteomes:UP000018948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P10297 {ECO:0000313|EMBL:ETP33923.1,
RC ECO:0000313|Proteomes:UP000018948};
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 P10297.";
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};
CC -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily.
CC {ECO:0000256|ARBA:ARBA00006331}.
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:ETP33923.1}.
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DR EMBL; ANIY01003692; ETP33923.1; -; Genomic_DNA.
DR EnsemblProtists; ETP33923; ETP33923; F442_17675.
DR Proteomes; UP000018948; Unassembled 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:UP000018948};
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 55..84
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 94..123
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT REPEAT 674..706
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 706..738
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 2409..2715
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1253..1275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1381..1418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1733..1824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2017..2048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..165
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..807
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..841
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..908
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..923
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1733..1817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2687
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 2720 AA; 298883 MW; 03707931AA3854CE CRC64;
MEEPSAPGRG GRKRRGGKRK RSTSHQSASE ERKTEEPPPK QEEEEKQEEK HEDKTPQKWS
CPACTFLNEA SRCFCEMCET PNPSPSAPRE LGTASSDWSC AACTMVNPAA MRVCGVCGTL
NPRPPMPPGL SIRLSDALGG GDDSFSSSSE DSEDSDSGDE EEDTWTCTTC DSLSSGRTCA
NCFAQRPIAA RKAADEENSS EKKQAKKRKR RKHEKLQERA KLAYGVSIYE LKKLVLEPTG
SRLVDTLQTL THTLAMMDAS ADNEWADGPS FLIRGFGGGR SSETAKDPEL LTVLADIFRG
QERTYSVEVR LLAVQSINYL MKMDRHMFAR AKMVEIVGLY IAELLAWKDK SSTGTGDSKT
SQMIVEECLS GLSSVCSTEV FALRELLAQE KFLGYLDFLL SLVDGDEKDS GFHPSIVMTA
LGILQKCCMK LRWSGKSSSK SRLNDSKKSR LASPKKMTLS GELTLELAIK VIGLLRRALE
HKHVPLHVKA AKCLLLIFHR TPHDQVRELV TPEILRKFVA VVVNTDGEES DESRLAMVNL
LLHLFDNRPQ LVNMFVQEKI YTDLFNGVLQ ILQSSSTALR TNTLKLTAML TRVICRNHSS
GSVASGKSSP KRSGSRSPRN RRNRQRLNSL PDPDVLSTLL LDFIRTDSIP AVNVLLKDGA
DLNFPKMYDV HGNEIDKPLN IAVESASLGM VRLLLKRGAD VHQVGIGGTA LHVAARIGRC
DVAAFLLQCG ARVQARDREK KTVMDVVIAA DKETSESCRV VSIPSPMKKL LELHQRTAGM
RDYDSDLSEG DDMADGRSRA WFYPSDHDDE YGDDDDMDDE LEGEGGYFMD YDDDDEDDGE
DFEGTRQRGD EMSDEEIPSD DDMVFYDGGM SRKSRSSNKR RLGSVSSESN ETPQSTVSGT
SSSSPRRRRA SSVSDKGCPD EDAAMEQKTC SATADEIYDF SLAITQCLLA VLHDMDIQNV
ERSVISTVAC VLEMAPSQLI HSLKEADVVL ILDTVHFLLQ GEKHHHISSD TATPMAGAVP
SVASSATSTQ TANVAAHNSN LPSFILAVRM LQAIVRKSSK ESSIFHQIER RGISEQIEQL
NDASACWVST SQEGTSRSSS RDTIFGRGLD LLKSLRADML ESGMLHLHKL RNLSRRLKEF
SDASPSCEKE LILVDLVELF EEPNSITTYE FKQSELLPAI LQYLSPQGEL DEVRAMALMQ
TFERCPAALK HVIFRLQSII TQEEAFPLVS FNIGKGRELY PLARQLKIAV MRPGDRGAGD
RPPGGSSSRL KGKSIHSSPL THFQSFERTV SRSMPVIDSD LSLLYLNLVG HSIQKVVEGK
WRKFLVVGYD DTRCYHLLKP IGGTNDDLAE MVLHDSQCKL IDSVNVYEGV TLDLELFGSP
DGADSGGNSD GKKKRKNNKR KRKSSTQKQQ QLENEGTLQV EVKNSGMLKM RSLPGAWYAA
ILLDDSGEVR KSSEGKNPTC EEVLAAQATH SVKLLPENRI VRKVPADCIR PRALQPQIGS
VVEMDGCLGE VTRIYNNDRS SSSAANTFLD VKVNSYTEKK RVKKDRVRFP AQELPVPKDD
DESDQIEAMS IRRLFPARDS SLLAGSVGDR VWVLPPSGSS VTDICVAGTI KNFPSGLDSI
RDSSTVVVEI AFGSAQPSLA VKVNQDRILN FAVDGGVLSG RGPSRLLAAL QMASGRGGSS
RLFGGGRSGQ DSSTSAIHRA FERVAGSLQQ NRLGGGLGSS GSAMDHIRSL MSRNSNVTGP
NAPSDIETAE QAPTTAQGAA RANSPPNEPS GSDVQADEEA SASVTASSSN SNATSQRTSS
VGEKSSKKGT STVETYLKKP QGAKPKMTCT QLPKVNLVVG FRKCDASVPS QDRIVISSEF
GLERVDRNKV SKDTPATPLL TRLDPSTQRY EPNAGVRKAL LDVFHSFSKE SVSGASQKKK
RRKLSPDAQR KASAEAAPWD VEKFIAFMLA VRGPSQYDHP GSNAKYCVTF SKFADPETNR
RLLAADGFLA LIVHECKDAV KSKQLLKFLR SRGYSEKSLT SSGSRSSSGD DEEKDSPNSA
SKSAHTKIPG NKLLRQPVVL RGFPADQNVL KCLEDLRQEH RTRACTSTLT NDASSSGADA
VLPPWKLTYK LYCDFQVEWE TQSSSNTSTS ESLGSGAMSL ESLAVLESKP PTRVLLHGIV
ELDEMNASSA AEASRWLSRI TAPQTGSGKV NVSDSVASAV RLLRYLFQFR GDVASLDEAL
WTSPRLYNKL ETQMQDVLSM CSGIYPPWCD ALVTHCKFFF PRELREKLFR STSFGCTRSL
HWFRNQLNIE EGSADSMPSM VGGGIYNQEI SISPIPKERV KVHRENILQS AEAVMKMHAK
RKAILDVVFV GEKGYGSGVT AAFYSTTAHA LQAVTENQKN RYWIPGEDDE AEAVKAEARR
KDDVGVAGGI AEDVPVVRHS NGLFPYPHRK PSSKLVERFR MMGRLAGKAL MDERLLPLPL
SPQFVKLVVG ESFGLEELGD IFLSHGRILY SMYKASKKLR AGEQSVQIDQ MDVQDWLEAV
GFTFIDPFSQ APLVTGGDDI AVTASNLTLY VRAVLELWLD SGIRAQVQAF REGISEVLPV
GKLRLLFVPE LISLLCGEED IEWNVESLVK DTKLAHGYTK DSQPVQFFFE ALEEMSAAER
RAFLLYATGC PNLPPGGFQA LKPPFEVVRR VVDNLDVDRA LPFARTCTNT LHLPAYSSKD
VLVKQMTFAI ANSRGVIDRD
//
