ID A0A319DZU2_9EURO Unreviewed; 481 AA.
AC A0A319DZU2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=BO71DRAFT_354657 {ECO:0000313|EMBL:PYH93738.1};
OS Aspergillus ellipticus CBS 707.79.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448320 {ECO:0000313|EMBL:PYH93738.1, ECO:0000313|Proteomes:UP000247810};
RN [1] {ECO:0000313|EMBL:PYH93738.1, ECO:0000313|Proteomes:UP000247810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 707.79 {ECO:0000313|EMBL:PYH93738.1,
RC ECO:0000313|Proteomes:UP000247810};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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; KZ825886; PYH93738.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319DZU2; -.
DR STRING; 1448320.A0A319DZU2; -.
DR Proteomes; UP000247810; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR15898:SF13; RING FINGER PROTEIN PSH1; 1.
DR PANTHER; PTHR15898; UNCHARACTERIZED; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000247810};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 49..90
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..383
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 481 AA; 53733 MW; 479B58EE72A8EA01 CRC64;
MSKPTPARAA ASNGSANTNA PKVNAGDNAS GLFQTLQGHV DDIRSLIQCG VCIRPLYEPY
TLACGHTFCY SCLTSWFVGG RHNKTCPDCR APVKAQPAPA YLVRAVVQMF TSRPELLDKG
ETTDEHLRHQ CDEAERLEKD KRSTHPKEGG LFRGTFNKSR LPAAQPIVDL EDNVVRCPRC
SWELEEDAGC AQCGYRQDDD SAATDSSDWS DSEENSEMTD YLDDEEIEDG FGDADNYGWD
DYRDGPPLAP LDMRTAELDQ FYRQWYGLAP GDPHPPRTNG PFHRQDYYHW PSGVSSAIEE
DSDMDDEEDA DMDSFIDDEL ERDDYSESDS STVIGPHEFS VTHTTIIGGD SFDDMTDESD
DDESHDDESH DDEDDEDEDD EPVQPPVNAI RRHRQPAYRV PSSSSDPENE PSIRPFRQPG
SMSRTASRAE YRERGEPRGP QQPSAGSSAV NAISVEDESD EDPVRPTRRP RGRGVCRHSG
Y
//
