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Database: UniProt
Entry: D0NB97_PHYIT
LinkDB: D0NB97_PHYIT
Original site: D0NB97_PHYIT 
ID   D0NB97_PHYIT            Unreviewed;      1645 AA.
AC   D0NB97;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=PITG_09260 {ECO:0000313|EMBL:EEY55326.1};
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:EEY55326.1, 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=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the ubiquitin conjugation factor E4 family.
CC       {ECO:0000256|ARBA:ARBA00007434}.
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DR   EMBL; DS028131; EEY55326.1; -; Genomic_DNA.
DR   RefSeq; XP_002903550.1; XM_002903504.1.
DR   STRING; 403677.D0NB97; -.
DR   EnsemblProtists; PITG_09260T0; PITG_09260T0; PITG_09260.
DR   GeneID; 9461744; -.
DR   KEGG; pif:PITG_09260; -.
DR   VEuPathDB; FungiDB:PITG_09260; -.
DR   eggNOG; KOG2042; Eukaryota.
DR   HOGENOM; CLU_244966_0_0_1; -.
DR   InParanoid; D0NB97; -.
DR   OMA; CFTRIPN; -.
DR   OrthoDB; 145583at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000006643; Partially assembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro.
DR   GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:InterPro.
DR   CDD; cd19757; Bbox1; 1.
DR   Gene3D; 3.30.60.90; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR019474; Ub_conjug_fac_E4_core.
DR   InterPro; IPR045132; UBE4.
DR   InterPro; IPR003613; Ubox_domain.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR000433; Znf_ZZ.
DR   InterPro; IPR043145; Znf_ZZ_sf.
DR   PANTHER; PTHR13931:SF2; UBIQUITIN CONJUGATION FACTOR E4 B; 1.
DR   PANTHER; PTHR13931; UBIQUITINATION FACTOR E4; 1.
DR   Pfam; PF04564; U-box; 1.
DR   Pfam; PF10408; Ufd2P_core; 2.
DR   Pfam; PF00569; ZZ; 1.
DR   SMART; SM00504; Ubox; 1.
DR   SMART; SM00291; ZnF_ZZ; 2.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   SUPFAM; SSF57850; RING/U-box; 2.
DR   PROSITE; PS51698; U_BOX; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006643};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00228}.
FT   DOMAIN          632..700
FT                   /note="ZZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50135"
FT   DOMAIN          1520..1600
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
FT   REGION          882..901
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1626..1645
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1645 AA;  184180 MW;  69F72CC0E43586A2 CRC64;
     MFVCARAQGG SEDVHALPDS LNASLSTSQR ASRDSSLSVA IDDASSYLQL LGALTRFVAQ
     LLDVHTLSPS LRFSAGESVA VDAAEWWKEV QRQSIALSQR QKIAQEAHRD TEEPTARRLW
     LLSPRTREKS PVRESRVINN NLWAGEAFKD LPEHVPKANF FMQALYLIMR ALERATRRQQ
     GRIEEDSVLG ETLVDALASV DAALAFAAAE LLQLWAPVSH KRVVDSAEKL SKLMNVAVVN
     ALLQPRNVGT KHTFHGHILL PSMPLRAFLG AKQWACSVCE RISQTTGSDA PCVYRCAACN
     FNLCRECFTR IPNVTNPPAS SPLEELTKLT SDRFFSLVVP QLKHETGKVV VRQITQELRR
     RVLELYPHNF QGAAEFAQLF LRLAASDKSA AIALVTSPPA SVPSSGRATC SWFPLFMRTW
     TMSLSTLLGP FLRASTMLDE THDLDAAVRA ANHGSVVADC LRAQWTSGYA ELRETLQNIM
     QTLLAEGQDP IVVDATLCWL ALALMTADPR RRLNYDAHER LDGFLVNVTT MLLAHALPLL
     DKAQHDPSRI DASYHQSVEP VRVYASKDFP EVPLHYSRSQ DTHNENAAGV ETCEIKARDE
     DAIAAYNKRR QQEHEEGERA VPSTYYPRLS CHEGVVCDQC EFPNLHGVRY KCAFCGDMDL
     CSDCFEIFRS HQAAPDSESE SESILHSPDH VFLRIESPIP VFALKHFQSL PVECLTSKHK
     GESCSVLDEG FEGSRIHCAD CGDALGASGQ PDEVFYKCAN CLSSRVVCAA CLAREERLSE
     GNPNDMHAPG HVYFVITDPW RRHLSVPWDY VLGKLHFRRL LHPPALIPRR RFPRDTEMFY
     ITLKYLHFGP LATLSRWLGM TKELRELQAF CACDEERFEL ERHQRSSRNG SQRQTLKPSV
     HYKASKSRLE DIRVKCVKVE LHLLASANVA GWLIFYARTC RWLLYSASAA PETGKAPQDP
     FSEPISHFSS MFSGFPEHFF FDLCDVVHLL GLERLEYRDL VSELKRTRPP CEAVDEVTEV
     VEPLLVMLTQ IVVAPKFTKN PHLRIEALRS LTTLVTFVSK GQQVHHRPGY QRIESLFKSH
     RLLSQCLTPG LLQFHADMDR YNASNNGLAF TSAVSSGDHM LWGFLPTRLS VTMLLRYLWQ
     VPSARQSLLH MLSTSETRHT SVSAEPSTDS TQQLTELVSG LWSDIAKLFD EANNKITTLR
     QIHDLLEDSL DGSVVVLPFR RDMLDGYVAI NAKHLRLTMR LLLEALESTS WFASIVSGER
     SFRSRSLSAP AAALRHVLLQ PLVVEQAART LSFLVASLAS AHEENEWKFS LPLVDDGRLL
     LAHLIVLVVR YAGHSAVKSG ASSGACSPSS FWKMIRSGGD IMAKRVGDLD THVRWGFNAL
     CTRMESESYL GTSLDDDVED IRVETQAGHE LDEDEALALL EKQAVSSTVS VVDTAAKKRL
     SKRFIATLAK DGRFDFRLFV GGCRFLRPQR GSSDNSDERE DVDEGYLYLD DAWVQQFVRA
     MQEADEMIHV QEAMEACLGD IPDQYLDPLL STLMTDPVRL PSGNIVDRAV IARHLLASSQ
     QGGSTGRDPF TREPLTMAMV EPCDALRSEI QMYLRTKMRH FRQTAREDVL ATWGLGWDVL
     FDSSSETEAD AEDGVDGNNA TLRSQ
//
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