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 27-MAR-2024, entry version 68.
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)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
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 -!- SUBUNIT: Interacts with creD. {ECO:0000250|UniProtKB:Q5BDP1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {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 GeneID; 18258649; -.
DR KEGG; cthr:CTHT_0046110; -.
DR eggNOG; KOG0940; Eukaryota.
DR HOGENOM; CLU_002173_0_0_1; -.
DR OrthoDB; 5480520at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd08382; C2_Smurf-like; 1.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 3.
DR Gene3D; 2.20.70.10; -; 2.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 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 PANTHER; PTHR11254:SF429; E3 UBIQUITIN-PROTEIN LIGASE SU(DX); 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
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; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF51045; WW domain; 3.
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..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
//
