ID A0A0S7E301_9EURO Unreviewed; 789 AA.
AC A0A0S7E301;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=ALT_003238 {ECO:0000313|EMBL:GIM43610.1};
OS Aspergillus lentulus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=293939 {ECO:0000313|EMBL:GIM43610.1};
RN [1] {ECO:0000313|EMBL:GIM43610.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM43610.1};
RA Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT "Draft Genome sequence of the pathogenic filamentous fungus Aspergillus
RT lentulus IFM 54703T.";
RL Genome Announc. 4:e01568-15(2016).
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=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the ZNF598/HEL2 family.
CC {ECO:0000256|ARBA:ARBA00035113}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GIM43610.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BCLY01000016; GIM43610.1; -; Genomic_DNA.
DR STRING; 293939.A0A0S7E301; -.
DR VEuPathDB; FungiDB:TMP_alenIFM54703_9127; -.
DR OrthoDB; 3059402at2759; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0072344; P:rescue of stalled ribosome; IEA:InterPro.
DR CDD; cd16615; RING-HC_ZNF598; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR041888; RING-HC_ZNF598/Hel2.
DR InterPro; IPR044288; ZNF598/Hel2.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22938:SF0; E3 UBIQUITIN-PROTEIN LIGASE ZNF598; 1.
DR PANTHER; PTHR22938; ZINC FINGER PROTEIN 598; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..789
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 789 AA; 85784 MW; FE275F57C503F0EC CRC64;
MSETEQLRAT PSQGQNRGGN RRRGRGGFSH QTGQTEGAQH PPDGAGRGPR SRGQGFRRGG
GGRDKQNRSA RPGQAADENA TPEANGETPS QGAPVADESE GKQVAAAATD DADDGEICFI
CASNVAHSSV SPCNHRTCHI CALRLRALYK NKACAHCRTE SSYVIFTDDP AKRYEDFTDA
DFSQKDDNLG IKYENNDIFE DTVLLLRYNC PDRSCDVACL GWPDLHRHVK SKHGKVMCDL
CTRNKKVFTH EHELFTMAEL RKHEKYGDDV PGALDQSGFK GHPECGFCRK RFYGDDELYA
HCRDRHERCH ICDRRSASRQ QQYYIDYNAL EDHFQKDHFL CLDKECLEKK FVVFESQMDL
KAHQLECHPN GLSKDARRDA RTVDLSDFEL RAPYQPQRQR RGAGRGRDPN ADALPVSSAQ
PLRRDEIAYQ RQMAIQSAQS VSTRSFGGQL TRNDTQTVRA PARSGAATPV RTPPAGPPVA
EMEALNVGTP SGPATPQDQA RRLRHAAVVE RASNLLRNDA SKLADFRSKV SQYRTSALSP
TELIDAFFSL FDTSSTELGK LIKELAEIYE DESKRNALLK AWNDWRAINE DYPALPGPGG
QIPGMSPGTV NGSGVGGKRV LRLKSSTAQS SRSAVGRSGS IVSTSSSSST NPFPPLSAAT
ARSAPRATAT STPWAAAAPT PARTMASAIN PSSRPAPTTS RTVRNTNDSE AFPALPTAPK
PNVLMAGLTR GTVRWDNRQP PPVNAWASSA GGGSASAANG PDDDYGESSS AGGKKGKGKK
GKQTLFHFG
//
