RSP5_ASPTN
ID RSP5_ASPTN Reviewed; 808 AA.
AC Q0CCL1;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=ATEG_08573;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476606; EAU30705.1; -; Genomic_DNA.
DR RefSeq; XP_001217159.1; XM_001217158.1.
DR AlphaFoldDB; Q0CCL1; -.
DR SMR; Q0CCL1; -.
DR STRING; 341663.Q0CCL1; -.
DR EnsemblFungi; EAU30705; EAU30705; ATEG_08573.
DR GeneID; 4323535; -.
DR VEuPathDB; FungiDB:ATEG_08573; -.
DR eggNOG; KOG0940; Eukaryota.
DR HOGENOM; CLU_002173_0_0_1; -.
DR OMA; FNAFITG; -.
DR OrthoDB; 167687at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000007963; 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..808
FT /note="Probable E3 ubiquitin-protein ligase hulA"
FT /id="PRO_0000395709"
FT DOMAIN 1..112
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 223..256
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 326..359
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 386..419
FT /note="WW 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 475..808
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT REGION 134..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 776
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 808 AA; 91724 MW; DC5C588FFF81C17D CRC64;
MGSNLPAQPN LRVTIIAADG LYKRDVFRFP DPFAVATVGG EQTHTTSVIK KTLNPYWNEM
FDLRVNEDSI LAIQIFDQKK FKKKDQGFLG VINVRIGDVI DLQMGGDEML TRDLKKSNDN
LVVHGKLIIN LSTNLSTPNT NQANGLHRSN LQSSTSSGLV PQVTAPHASP GPSQLDPTAS
NPSLNPQRVP STTRPSSTVA PVNGAAAPGA SRTNLSSFED SQGRLPAGWE RREDNLGRTY
YVDHNTRTTT WTRPSSNYNE ATQRTQREAN MQLERRAHQS RMLPEDRTGA SSPNLQENQQ
AQTPPAGGSA NAVSMMATGA TTAGTGELPP GWEQRTTPEG RPYFVDHNTR TTTWVDPRRQ
QYIRMYGQNA NGNNTTIQQQ PVSQLGPLPS GWEMRLTNTA RVYFVDHNTK TTTWDDPRLP
SSLDQGVPQY KRDFRRKLIY FRSQPALRIM SGQCHVKVRR NNIFEDSYAE IMRQSASDLK
KRLMIKFDGE DGLDYGGLSR EFFFLLSHEM FNPFYCLFEY SAHDNYTLQI NPHSGVNPEH
LNYFKFIGRV VGLAIFHRRF LDSFFIGAFY KMMLRKKVSL QDMEGVDEDL HRNLTWTLDN
DIEGIIELTF AVDDEKFGER RTIDLKPGGR DIPVTNENKH EYVELVTEWK IVKRVEEQFN
AFMSGFNELI PADLVNVFDE RELELLIGGI ADIDVDDWKK HTDYRGYQEQ DEVIQNFWKI
VRTWDAEQKS RLLQFTTGTS RIPVNGFKDL QGSDGPRRFT IEKSGDPAAL PKSHTCFNRL
DLPPYKTHET LEHKLSIAVE ETLGFGQE
