ID W2ZPI9_PHYPR Unreviewed; 1163 AA.
AC W2ZPI9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=E3 ubiquitin-protein ligase HACE1 {ECO:0000256|ARBA:ARBA00040370};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
DE AltName: Full=HECT domain and ankyrin repeat-containing E3 ubiquitin-protein ligase 1 {ECO:0000256|ARBA:ARBA00042378};
DE AltName: Full=HECT-type E3 ubiquitin transferase HACE1 {ECO:0000256|ARBA:ARBA00041409};
GN ORFNames=F442_05164 {ECO:0000313|EMBL:ETP49292.1};
OS Phytophthora parasitica P10297.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317064 {ECO:0000313|EMBL:ETP49292.1, ECO:0000313|Proteomes:UP000018948};
RN [1] {ECO:0000313|EMBL:ETP49292.1, ECO:0000313|Proteomes:UP000018948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P10297 {ECO:0000313|EMBL:ETP49292.1,
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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}. Golgi apparatus, Golgi stack membrane
CC {ECO:0000256|ARBA:ARBA00037859}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00104}.
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:ETP49292.1}.
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DR EMBL; ANIY01001113; ETP49292.1; -; Genomic_DNA.
DR AlphaFoldDB; W2ZPI9; -.
DR EnsemblProtists; ETP49292; ETP49292; F442_05164.
DR Proteomes; UP000018948; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic 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 InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR PANTHER; PTHR11254:SF67; E3 UBIQUITIN-PROTEIN LIGASE HUWE1; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50237; HECT; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Reference proteome {ECO:0000313|Proteomes:UP000018948};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT REPEAT 63..96
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 904..1163
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1163 AA; 131438 MW; BB828B3D6EEF48C4 CRC64;
MASATPRRRP NRKPKAKTTS SSTPPSSPPV TSQLVTAIRR NDLDAFSSLL QTPKLDVNRR
TPHGDAPLVE ACRYARLEMA TRLLSVHGAN VNVSSSNRSA NRVGLTPLIA ACMALQPKLV
TLLLSQSQKR VNLLKTFGQV NAVTVLLLFC VANGRTEEQN DAALLILEQL LRYAKQQNQL
KELLTAKPDK VNSLLHVAAG LSNWKALKML RERADEFDVE FNARNAVEHS LLHVVEMNAF
QARSMQFCEP PRPEVETGGK KSKGRNRRRH KQKKQESKEE EKEGDDVKEE QEQEQSEADK
QTFTRSRPDR AVEAFHVTRT VMELTKNSGV GAIFSRKGDE GLRGLYIKAL VLAEVGLVSI
INEIAQMPDT QQEKLVYIDG LMYTAASVYP LSVKNAKEYQ SLWRQALDKR HNLEATTAAR
VDEEEKKRIP TNEQPIELSH DGFKLILNGM LSYNSLSKRV KVWTLILMHL LTPFASGTPL
AADKRPVMEE CSQLKFFERI TEMLCRSGTK LAFCIFDRTD IEDDESYDEE IEFHLLISLF
ELFLQFFAPY ARIIRDGESK EPLGITESFQ RAIKPVKQLW TLVNAALGSM DDAIATPQRF
SLLLHLLQVF EQLEAAFVSD EDMTLVKLFG VMNRFVKQDA RKKRIKMFVA EQSHLLHTIA
ATFPIPASFV DKVIPLKDSV DVLIRSDPKV LGMDLYSFAA IPGLIRLEHK VDYLAMLAEE
RNGSVSVSIS RASEANYVDF ILQQILSTSA SNLKGEMNIT LVNEPGVGVG VTREFFQIVQ
RCFFQPGLTG SSQSRGAPPA PHVLEIGAQW LQLARSQNTH DSSKKRNAKR SRPTQSSGFT
ELFPLFDFVD EQKRGVLGIA PRPVYISKQV MDAKRSAKSL SLSCKDMLVD PSEVDALKKV
YLCIGRLIGL SIRNHQPLGA DFPVVFWKFM MRDGSLTWES YCESSDVFKR SLQFVLDHDF
DGEPLDMRFE YTTEVVIVDE EAKQKEEATD AAVAAPSNVT MSMEMELQDG MGDVEVTNAN
KAQYVLLRAQ QFFFGNELVY YKKIRDGFND TIARSDLKLF RPEELRRLVR GERTIDFESL
KKNVVYSRGA LPSRGVVQRF WEVVESFDQE NRSKLLTFWS GSPLPPIFGF DSKYRSMNAD
TACWYIDVDT RMQTSFCPMA NTW
//
