RSP5_ASPFC
ID RSP5_ASPFC Reviewed; 813 AA.
AC B0XQ72;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 25-MAY-2022, entry version 65.
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=AFUB_008950;
OS Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDP56186.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS499594; EDP56186.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; B0XQ72; -.
DR SMR; B0XQ72; -.
DR PhylomeDB; B0XQ72; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001699; 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:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
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 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; Repeat; Transferase; Ubl conjugation pathway.
FT CHAIN 1..813
FT /note="Probable E3 ubiquitin-protein ligase hulA"
FT /id="PRO_0000395704"
FT DOMAIN 1..109
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 227..260
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 331..364
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 391..424
FT /note="WW 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 480..813
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT REGION 131..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 781
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 813 AA; 91969 MW; 1F55A021412E5298 CRC64;
MGSNLPAQPN LRLTTDGLYK RDVFRFPDPF AVATVGGEQT HTTSVIKKTL NPYWNEMFDL
RVNEDSILAI QIFDQKKFKK KDQGFLGVIN VRIGDVIDLQ MGGDEMLTRD LKKSNDNLVV
HGKLIINLST NLSTPNTNQA NGLHRSHVQS STSSGLVPQV APSSSHPAAS GTAPVDPSAS
NPSLNPQRVP STTRPSSTAA PASAAGAAVS NSHGSRTNLS SFEDSQGRLP AGWERREDNL
GRTYYVDHNT RTTTWTRPSS NYNEHAQRSQ REANMQLERR AHQSRMLPED RTGANSPNLP
ESSQQAHTPP AGGSANAVSM MATGATTAGT GELPPGWEQR TTPEGRPYFV DHNTRTTTWV
DPRRQQYIRM YGQNANGTNT TIQQQPVSQL GPLPSGWEMR LTNTARVYFV DHNTKTTTWD
DPRLPSSLDQ GVPQYKRDFR RKLIYFRSQP ALRIMSGQCH VKVRRNNIFE DSYAEIMRQS
ASDLKKRLMI KFDGEDGLDY GGLSREFFFL LSHEMFNPFY CLFEYSAHDN YTLQINPHSG
VNPEHLNYFK FIGRVVGLAI FHRRFLDSFF IGAFYKMMLR KKVSLQDMEG VDEDLHRNLT
WTLDNDIEGV LELTFSVDDE KFGERRTIDL KPGGRDIPVT NENKAEYVEL VTEWKIVKRV
EEQFNAFMSG FNELIPADLV NVFDERELEL LIGGIADIDV DDWKKHTDYR GYQESDEVIQ
NFWKIVRSWD AEQKSRLLQF TTGTSRIPVN GFKDLQGSDG PRRFTIEKSG DPAALPKSHT
CFNRLDLPPY KSYETLEHKM SIAVEETLGF GQE
