RSP5_ASPNC
ID RSP5_ASPNC Reviewed; 821 AA.
AC A2QQ28;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Probable E3 ubiquitin-protein ligase hulA;
DE EC=2.3.2.26;
DE AltName: Full=HECT ubiquitin ligase A;
DE AltName: Full=HECT-type E3 ubiquitin transferase hulA;
GN Name=hulA; ORFNames=An08g01060;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an
CC E2 ubiquitin-conjugating enzyme in the form of a thioester and then
CC directly transfers the ubiquitin to targeted substrates. Probably
CC involved in the regulatory network controlling carbon source
CC utilization. {ECO:0000250|UniProtKB:Q5BDP1}.
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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with creD. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RSP5/NEDD4 family. {ECO:0000305}.
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DR EMBL; AM270158; CAK39787.1; -; Genomic_DNA.
DR RefSeq; XP_001392224.1; XM_001392187.2.
DR AlphaFoldDB; A2QQ28; -.
DR SMR; A2QQ28; -.
DR PaxDb; A2QQ28; -.
DR EnsemblFungi; CAK39787; CAK39787; An08g01060.
DR GeneID; 4982420; -.
DR KEGG; ang:ANI_1_154074; -.
DR VEuPathDB; FungiDB:An08g01060; -.
DR HOGENOM; CLU_002173_0_0_1; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000006706; Chromosome 8R.
DR GO; GO:0005934; C:cellular bud tip; IEA:EnsemblFungi.
DR GO; GO:0010008; C:endosome membrane; IEA:EnsemblFungi.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IEA:EnsemblFungi.
DR GO; GO:0005794; C:Golgi apparatus; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:1990306; C:RSP5-BUL ubiquitin ligase complex; IEA:EnsemblFungi.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:EnsemblFungi.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:EnsemblFungi.
DR GO; GO:0043130; F:ubiquitin binding; IEA:EnsemblFungi.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:EnsemblFungi.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0034644; P:cellular response to UV; IEA:EnsemblFungi.
DR GO; GO:0006325; P:chromatin organization; IEA:EnsemblFungi.
DR GO; GO:0072671; P:mitochondria-associated ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
DR GO; GO:0007005; P:mitochondrion organization; IEA:EnsemblFungi.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IEA:EnsemblFungi.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IEA:EnsemblFungi.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0051865; P:protein autoubiquitination; IEA:EnsemblFungi.
DR GO; GO:0006513; P:protein monoubiquitination; IEA:EnsemblFungi.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:EnsemblFungi.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:EnsemblFungi.
DR GO; GO:0010794; P:regulation of dolichol biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0032443; P:regulation of ergosterol biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0031384; P:regulation of initiation of mating projection growth; IEA:EnsemblFungi.
DR GO; GO:0010793; P:regulation of mRNA export from nucleus; IEA:EnsemblFungi.
DR GO; GO:0010796; P:regulation of multivesicular body size; IEA:EnsemblFungi.
DR GO; GO:0006808; P:regulation of nitrogen utilization; IEA:EnsemblFungi.
DR GO; GO:0019220; P:regulation of phosphate metabolic process; IEA:EnsemblFungi.
DR GO; GO:0032880; P:regulation of protein localization; IEA:EnsemblFungi.
DR GO; GO:2000203; P:regulation of ribosomal large subunit export from nucleus; IEA:EnsemblFungi.
DR GO; GO:2000232; P:regulation of rRNA processing; IEA:EnsemblFungi.
DR GO; GO:2000238; P:regulation of tRNA export from nucleus; IEA:EnsemblFungi.
DR GO; GO:2000235; P:regulation of tRNA processing; IEA:EnsemblFungi.
DR GO; GO:0010795; P:regulation of ubiquinone biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:EnsemblFungi.
DR GO; GO:0034517; P:ribophagy; IEA:EnsemblFungi.
DR GO; GO:0070086; P:ubiquitin-dependent endocytosis; IEA:EnsemblFungi.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 3.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR024928; E3_ub_ligase_SMURF1.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 3.
DR PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 3.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF51045; SSF51045; 3.
DR SUPFAM; SSF56204; SSF56204; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 3.
DR PROSITE; PS50020; WW_DOMAIN_2; 3.
PE 3: Inferred from homology;
KW Cytoplasm; Reference proteome; Repeat; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..821
FT /note="Probable E3 ubiquitin-protein ligase hulA"
FT /id="PRO_0000395707"
FT DOMAIN 1..112
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 231..264
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 339..372
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 399..432
FT /note="WW 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 488..821
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT REGION 140..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 789
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 821 AA; 92877 MW; 69517C8A14447BE6 CRC64;
MGSNLPAQPN LRVTIIAADG LYKRDVFRFP DPFAVATVGG EQTHTTSVIK KTLNPYWNEM
FDLRVNEDSI LAIQIFDQKK FKKKDQGFLG VINVRIGDVI DLQMGGDEML TRDLKKSNDN
LVVHGKLIIN LSTNLSTPIP NQANGLHRSH AQSSTSSGLV PQVSSASHPS VSPGQAEPSA
AASNVSLHPQ RVPSTTRPTS TVGPVNGGPA PPPNGPQGSR TNLSSFEDSQ GRLPAGWERR
EDNLGRTYYV DHNTRTTTWT RPSSNYNEQT QRTQREANMQ LERRAHQSRM LPEDRTGANS
PNLQESPQPQ PQQAHTPPAG GSASAVSMMA TGATTAGTGE LPPGWEQRTT PEGRPYFVDH
NTRTTTWVDP RRQQYIRMYG HNANGGNTTI QQQPVSQLGP LPSGWEMRLT NTARVYFVDH
NTKTTTWDDP RLPSSLDQGV PQYKRDFRRK LIYFRSQPAL RIMSGQCHVK VRRNNIFEDS
YAEIMRQSAS DLKKRLMIKF DGEDGLDYGG LSREFFFLLS HEMFNPFYCL FEYSAHDNYT
LQINPHSGVN PEHLNYFKFI GRVVGLAIFH RRFLDSFFIG AFYKMMLRKK VSLQDMEGVD
EDLHRNLAWT LENDIEGIIE LTFSVDDEKF GERTTIDLKP GGRDIPVTNE NKGEYVELVT
EWKIVKRVEE QFNAFMSGFN ELIPADLVNV FDERELELLI GGIADIDVDD WKKHTDYRGY
QEQDEVIQNF WKIVRTWDAE QKSRLLQFTT GTSRIPVNGF KDLQGSDGPR RFTIEKSGDP
IALPKSHTCF NRLDLPPYKT HDVLEHKLSI AVEETLGFGQ E
