RSP5_ASPOR
ID RSP5_ASPOR Reviewed; 816 AA.
AC Q2UBP1;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 25-MAY-2022, entry version 86.
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=AO090012000923;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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=BAE61024.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP007161; BAE61024.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001727863.2; XM_001727811.2.
DR AlphaFoldDB; Q2UBP1; -.
DR SMR; Q2UBP1; -.
DR STRING; 510516.Q2UBP1; -.
DR EnsemblFungi; BAE61024; BAE61024; AO090012000923.
DR GeneID; 5988337; -.
DR KEGG; aor:AO090012000923; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000006564; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
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_0000395708"
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..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 253..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..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..328
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; 92553 MW; FD67AE9C93D52F4B CRC64;
MGSNLPAQPN LRVTIIAADG LYKRDVFRFP DPFAVATVGG EQTHTTSVIK KTLNPYWNEM
FDLRVNEDSI LAIQIFDQKK FKKKDQGFLG VINVRIGDVI DLQMGGDEML TRDLKKSNDN
LVVHGKLIIN LSTNLSTPNT NQANGLHRSH MQPSTSSGLV PQVSASTPQP SPGPSQADPT
ASNPSLHPQR VPSTTRPSST IVPANGPPAP PNGQQGSRTN LSSFEDSQGR LPAGWERRED
NLGRTYYVDH NTRTTTWTRP SNNYNEQTSR TQREASMQLE RRAHQSRMLP EDRTGASSPN
LQENQQQAQT PPAGGSASAV SMMATGATTA GTGELPPGWE QRTTPEGRPY FVDHNTRTTT
WVDPRRQQYI RMYGQNANGT NTTIQQQPVS QLGPLPSGWE MRLTNTARVY FVDHNTKTTT
WDDPRLPSSL DQGVPQYKRD FRRKLIYFRS QPALRIMSGQ CHVKVRRNNI FEDSYAEIMR
QSASDLKKRL MIKFDGEDGL DYGGLSRREF FFLLSHEMFN PFYCLFEYSA HDNYTLQINP
HSGVNPEHLN YFKFIGRVVG LAIFHRRFLD SFFIGAFYKM MLRKKVSLQD MEGVDEDLHR
NLTWTLDNDI EGIIELTFAV DDEKFGERRT IDLKPGGRDI PVTNENKGEY VELVTEWKIV
KRVEEQFNAF MSGFNELIPA DLVNVFDERE LELLIGGIAD IDVDDWKKHT DYRGYQESDE
VIQNFWKIVR TWDAEQKSRL LQFTTGTSRI PVNGFKDLQG SDGPRRFTIE KSGDPGALPK
SHTCFNRLDL PPYKTNDVLE HKLSIAVEET LGFGQE
