ID A0A074XZS0_AURPU Unreviewed; 356 AA.
AC A0A074XZS0;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 03-MAY-2023, entry version 33.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=M438DRAFT_330141 {ECO:0000313|EMBL:KEQ89109.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ89109.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ89109.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ89109.1,
RC ECO:0000313|Proteomes:UP000030706};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR023577}.
CC -!- SIMILARITY: Belongs to the NOSIP family.
CC {ECO:0000256|ARBA:ARBA00008126, ECO:0000256|PIRNR:PIRNR023577}.
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; KL584974; KEQ89109.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074XZS0; -.
DR STRING; 1043002.A0A074XZS0; -.
DR HOGENOM; CLU_053742_1_1_1; -.
DR OrthoDB; 5483933at2759; -.
DR Proteomes; UP000030706; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR016818; NOSIP.
DR InterPro; IPR031790; Znf-NOSIP.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR13063; ENOS INTERACTING PROTEIN; 1.
DR PANTHER; PTHR13063:SF10; NITRIC OXIDE SYNTHASE-INTERACTING PROTEIN; 1.
DR Pfam; PF15906; zf-NOSIP; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR PIRSF; PIRSF023577; ENOS_interacting; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR023577};
KW Reference proteome {ECO:0000313|Proteomes:UP000030706};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 250..305
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 198..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 65..109
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 198..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 356 AA; 39417 MW; B10B152A617E953B CRC64;
MSHSKHNTSL AFFTAHERAE LRDRWGSQST RLTRDSFLPF GSCRLCLLPA RDPVSCASHG
HLFCRECALS NLLAQKKDIK RLEKEYVQKK QEEAEAEDIK QEQERERAVQ DFELVQQGLN
SKLGPATTRH IVGREAGKVI VEGNNLDKQG TKRKLQIDED ELMRLGGQNT RLKKDSKDSQ
NPIDQKAATS FWIPSLTPSS TTTATKPTKL NPQCPAATPD KPHDFSLKSL VTVQFTEEKS
ETSNESVRSC PSCKKALTNS TKAMLAKPCG HVLCKPCAAK FMKPSEKDAH DATAEVGIVR
CYVCQANVTE KKREKKEGKE EKDKVRPGVV EISSEGTGFA GGGNNMVKKT GVAFQV
//