RSP5_ASPCL
ID RSP5_ASPCL Reviewed; 815 AA.
AC A1CQG2;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 03-AUG-2022, entry version 87.
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=ACLA_026000;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAW07883.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS027059; EAW07883.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001269309.1; XM_001269308.1.
DR AlphaFoldDB; A1CQG2; -.
DR SMR; A1CQG2; -.
DR STRING; 5057.CADACLAP00001699; -.
DR EnsemblFungi; EAW07883; EAW07883; ACLA_026000.
DR GeneID; 4701851; -.
DR KEGG; act:ACLA_026000; -.
DR eggNOG; KOG0940; Eukaryota.
DR OrthoDB; 167687at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
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..815
FT /note="Probable E3 ubiquitin-protein ligase hulA"
FT /id="PRO_0000395703"
FT DOMAIN 1..112
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 229..262
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 333..366
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 393..426
FT /note="WW 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 482..815
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT REGION 134..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 783
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 815 AA; 92245 MW; 00F696BAD1320B00 CRC64;
MGSNLPSQPN LRLTIIAADG LYKRDVFRFP DPFAVATVGG EQTQTTSVIK KTLNPYWNEM
FDLRVNEESI LAIQIFDQKK FKKKDQGFLG VINVRIGDVI DLEMGGDEML TRDLKKSNDN
LVVHGKLIIN LSTNLSTPNT NQANGLHRSH IQPSTSSGLV PQVGASAAHP AASPAPIDPA
ASNPSLHPQR VPSTNRPPST VAPGAAAGAT PTNTQGSRTN LSSFEDSQGR LPAGWERRED
NLGRTYYVDH NTRTTTWTRP SSNYNEQTQR TQREANMQLE RRAHQSRMLP EDRTGANSPN
LPETSQQAPT PPAGGSANAV SMMATGATTA GTGELPPGWE QRTTPEGRPY FVDHNTRTTT
WVDPRRQQYI RMYGQNANGT NTTIQQQPVS QLGPLPSGWE MRLTNTARVY FVDHNTKTTT
WDDPRLPSSL DQGVPQYKRD FRRKLIYFRS QPALRIMSGQ CHVKVRRNNI FEDSYAEIMR
QSASDLKKRL MIKFDGEDGL DYGGLSREFF FLLSHEMFNP FYCLFEYSAH DNYTLQINPH
SGVNPEHLNY FKFIGRVVGL AIFHRRFLDS FFIGAFYKMM LRKKVSLQDM EGVDEDLHRN
LTWTLDNDIE GVLELTFAVD DEKFGERRTI DLKPGGRDIP VTNENKGEYV ELVTEWKIVK
RVEEQFNAFM SGFNELIPAD LVNVFDEREL ELLIGGIADI DVDDWKKHTD YRGYQESDDV
IQNFWKVVRT WDAEQKSRLL QFTTGTSRIP VNGFKDLQGS DGPRRFTIEK SGDPVALPKS
HTCFNRLDLP PYKTYETLEH KMSIAVEETL GFGQE
