(data stored in ACNUC7421 zone)

SWISSPROT: HUL4_ASHGO

ID   HUL4_ASHGO              Reviewed;         839 AA.
AC   Q757T0;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 87.
DE   RecName: Full=Probable E3 ubiquitin-protein ligase HUL4;
DE            EC=2.3.2.26;
DE   AltName: Full=HECT ubiquitin ligase 4;
DE   AltName: Full=HECT-type E3 ubiquitin transferase HUL4;
GN   Name=HUL4; OrderedLocusNames=AEL068W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Probable E3 ubiquitin-protein ligase, component of the TRAMP
CC       complex which has a poly(A) RNA polymerase activity and is involved in
CC       a post-transcriptional quality control mechanism limiting inappropriate
CC       expression of genetic information. Polyadenylation is required for the
CC       degradative activity of the exosome on several of its nuclear RNA
CC       substrates. {ECO:0000250|UniProtKB:P40985}.
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;
CC   -!- SUBUNIT: Component of the TRAMP complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the HUL4 family. {ECO:0000305}.
DR   EMBL; AE016818; AAS52617.1; -; Genomic_DNA.
DR   RefSeq; NP_984793.1; NM_210147.1.
DR   SMR; Q757T0; -.
DR   STRING; 33169.AAS52617; -.
DR   PRIDE; Q757T0; -.
DR   EnsemblFungi; AAS52617; AAS52617; AGOS_AEL068W.
DR   GeneID; 4620985; -.
DR   KEGG; ago:AGOS_AEL068W; -.
DR   HOGENOM; HOG000246763; -.
DR   InParanoid; Q757T0; -.
DR   KO; K12232; -.
DR   OMA; KEWFMLL; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0031499; C:TRAMP complex; IEA:EnsemblFungi.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   CDD; cd00078; HECTc; 1.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   Pfam; PF00632; HECT; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SUPFAM; SSF56204; SSF56204; 1.
DR   PROSITE; PS50237; HECT; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q757T0.
DR   SWISS-2DPAGE; Q757T0.
KW   Nucleus; Reference proteome; Transferase; Ubl conjugation pathway.
FT   CHAIN           1..839
FT                   /note="Probable E3 ubiquitin-protein ligase HUL4"
FT                   /id="PRO_0000227674"
FT   DOMAIN          497..839
FT                   /note="HECT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT   ACT_SITE        807
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   839 AA;  97485 MW;  E31B398FC3A24D2C CRC64;
     MSFFSRNINS KDRHKIQIIS NSTAPSFEPN NEFVTSSCCC CGTILQHPKN ISKFRCSVCY
     VTVVLQGTAF TQDKTELFDL DDMRELLSSC NNTYRELDKD EKRLRKHEVF HLLEDYIATR
     MVTIFPLNAS FESSNPREML DYDQVKEFYR ILMELPTKKP FYSFLVACNE LLKRPHVALN
     TPTPTNPKYK RIGLFRWILI ILEVPIFKQT LANAEARCNT PHFRAISYEV LKKAVGYMSC
     LDEASAKELV HFLKYMQKDI FASKVELVNM YITFHFARIL HTIGKETNNG KYSPQLEDFE
     HSEKLNPSLN QGSAKKLVHT NMNIFFGGIV RPMTSSANSK DILALNYRFS PEDYGNEWHI
     KTGARLLLCL YVANQSAYKC PVSNFYNTMI DFVDYKRDFE LWQDLSKLSA SHEKENSGSS
     GPRYSPVQFT ICQCPFLFSL GMKISILEYE TRRLMEYSAE QAFLKALDRK QVVDVYLKIR
     VRREFVTTDS LRSIQNQQKD LKKSLRIEFV NEPGIDAGGL RKEWFLLLTR DLFNPNNGLF
     VYVPESRLCW FSIMESIEHE LLQGEGSSSE LYYLFGVVLG LAIYNSTILD LKFPRAFYKK
     ICGEVLSVND FLELYPETGT NMLKMLEYDG EDFEDIFALT FETCFPDRFD ESKIHYRQLC
     PDGSTQAVTR ENKHEYFRLW MDFYLNRSIA PGFESFRNGF FHVIEGNSFR LFGSEELEQL
     VCGSNEQSLD VSMLRSVTRY QGGFDDNSPV VQWFWEILSE MEYPQQRKLL HFVTGSDRVP
     ATGVTTIPFR ISRIRSGADR LPLSHTCFNE ICLHEYKDKE TLRNKLIIAL EESQGYGFR
//

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