RSP5_NEOFI
ID RSP5_NEOFI Reviewed; 816 AA.
AC A1D3C5;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
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 RSP5;
GN Name=hulA; ORFNames=NFIA_016110;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
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}.
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DR EMBL; DS027688; EAW22918.1; -; Genomic_DNA.
DR RefSeq; XP_001264815.1; XM_001264814.1.
DR AlphaFoldDB; A1D3C5; -.
DR SMR; A1D3C5; -.
DR STRING; 36630.CADNFIAP00001250; -.
DR EnsemblFungi; EAW22918; EAW22918; NFIA_016110.
DR GeneID; 4591930; -.
DR KEGG; nfi:NFIA_016110; -.
DR VEuPathDB; FungiDB:NFIA_016110; -.
DR eggNOG; KOG0940; Eukaryota.
DR HOGENOM; CLU_002173_0_0_1; -.
DR OMA; FNAFITG; -.
DR OrthoDB; 167687at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000006702; 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..816
FT /note="Probable E3 ubiquitin-protein ligase hulA"
FT /id="PRO_0000395711"
FT DOMAIN 1..112
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 230..263
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 334..367
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 394..427
FT /note="WW 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 483..816
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT REGION 134..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 784
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 816 AA; 92178 MW; 8DD596C59165B2E7 CRC64;
MGSNLPAQPN LRLTIIAADG LYKRDVFRFP DPFAVATVGG EQTHTTSVIK KTLNPYWNEM
FDLRVNEDSI LAIQIFDQKK FKKKDQGFLG VINVRIGDVI DLQMGGDEML TRDLKKSNDN
LVVHGKLIIN LSTNLSTPNT NQANGLHRSH VQSSTSSGLV PQVAPSSSHP AASGAAPVDP
SASNPSLNPQ RVPSTTRPSS TAAPASAAGA AASNTHGSRT NLSSFEDSQG RLPAGWERRE
DNLGRTYYVD HNTRTTTWTR PSSNYNEHAQ RSQREANMQL ERRAHQSRML PEDRTGANSP
NLPESSQQAH TPPAGGSANA VSMMATGATT AGTGELPPGW EQRTTPEGRP YFVDHNTRTT
TWVDPRRQQY IRMYGQNANG TNTTIQQQPV SQLGPLPSGW EMRLTNTARV YFVDHNTKTT
TWDDPRLPSS LDQGVPQYKR DFRRKLIYFR SQPALRIMSG QCHVKVRRNN IFEDSYAEIM
RQSASDLKKR LMIKFDGEDG LDYGGLSREF FFLLSHEMFN PFYCLFEYSA HDNYTLQINP
HSGVNPEHLN YFKFIGRVVG LAIFHRRFLD SFFIGAFYKM MLRKKVSLQD MEGVDEDLHR
NLTWTLDNDI EGVLELTFSV DDEKFGERRT IDLKPGGRDI PVTNENKAEY VELVTEWKIV
KRVEEQFNAF MSGFNELIPA DLVNVFDERE LELLIGGIAD IDVDDWKKHT DYRGYQESDE
VIQNFWKVVR SWDAEQKSRL LQFTTGTSRI PVNGFKDLQG SDGPRRFTIE KSGDPAALPK
SHTCFNRLDL PPYKSYETLE HKMSIAVEET LGFGQE
