RSP5_CHATD
ID RSP5_CHATD Reviewed; 820 AA.
AC G0S9J5;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 2.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=E3 ubiquitin-protein ligase RSP5;
DE EC=2.3.2.26;
DE AltName: Full=HECT-type E3 ubiquitin transferase RSP5;
GN Name=RSP5; ORFNames=CTHT_0046110;
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=759272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719;
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
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.
CC {ECO:0000250|UniProtKB:P39940}.
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 {ECO:0000250|UniProtKB:P39940}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P39940}. Nucleus
CC {ECO:0000250|UniProtKB:P39940}. Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000250|UniProtKB:P39940}.
CC -!- SIMILARITY: Belongs to the RSP5/NEDD4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EGS20106.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; GL988043; EGS20106.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_006694991.1; XM_006694928.1.
DR AlphaFoldDB; G0S9J5; -.
DR SMR; G0S9J5; -.
DR STRING; 759272.G0S9J5; -.
DR PRIDE; G0S9J5; -.
DR EnsemblFungi; EGS20106; EGS20106; CTHT_0046110.
DR GeneID; 18258649; -.
DR KEGG; cthr:CTHT_0046110; -.
DR eggNOG; KOG0940; Eukaryota.
DR HOGENOM; CLU_002173_0_0_1; -.
DR OrthoDB; 167687at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
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:UniProtKB-SubCell.
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:0034644; P:cellular response to UV; IEA:EnsemblFungi.
DR GO; GO:0006325; P:chromatin organization; IEA:EnsemblFungi.
DR GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; 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: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 GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; 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; Cytoskeleton; Nucleus; Reference proteome; Repeat; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..820
FT /note="E3 ubiquitin-protein ligase RSP5"
FT /id="PRO_0000435819"
FT DOMAIN 1..118
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 247..280
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 397..430
FT /note="WW 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 486..820
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT REGION 140..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 788
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 820 AA; 93153 MW; 214AB2A9CFCF2C2B CRC64;
MSNNTRMDGL PAQPNLRVTI IAADGLYKRD VFRFPDPFAV ATINGEQTKT TQVSKRTLNP
YWNESFDFRV NEDSILAIQV FDQKKFKKKD QGFLGVINIR IGDVIDLVPD ADDQMLTRDL
KKSNDNLVVH GKLIINLSTN LSTPNRTQQT PSASRPSLLA PQTSTPNGTT DRPSSAMSSA
VSTNGTPAAS QPMPLAHRPA SLASTTSTSQ ATAAATTSTT TATANGTPVQ PRQVDVRQLS
PFEDALGRLP PGWERREDHL GRTYYVDHNT RTTSWNRPTG TGQSDAEATQ QAQRQQHQNR
SLPEDRTGAN SPTLQQQQAV AQAQATALVH TGATTAGTGE LPPGWEMRWT PEGRPYFVDH
NTRTTTWVDP RRQQYIRMYG GNNPNGIIQQ QPVSQLGPLP SGWEMRLTNT ARVYFVDHNT
KTTTWDDPRL PSSLDQNVPQ YKRDFRRKLI YFRSQPAMRI LSGQCHIKVR RSHIFEDAFA
EISRQSATDL KKRLMIKFDG EDGLDYGGLS REFFFLLSHE MFNPFYCLFE YSAHDNYTLQ
INPHSGINPE HLNYFKFIGR VVGLAIFHRR FLDAFFITAF YKMILGKPVT LADMEGVDAD
FHRSLQWMLD NDISGGIIEA TFSTEDERFG VITVEDLKPN GRNIEVTNEN KREYVELMVK
WRIQKRVEEQ FKAFKEGFNE LIPQDLINVF DERELELLIG GIAEIDVDDW KKHTDYRGYT
ESDEVIQFFW QTVRSWDSEQ KSRLLQFTTG TSRIPVNGFK DLQGSDGPRR FTIERAGDIN
NLPKAHTCFN RLDLPPYKTL EQLQQKLTMA VEETMGFGQE
