ID A0A2X0NZY1_9BASI Unreviewed; 429 AA.
AC A0A2X0NZY1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=BQ5605_C018g08635 protein {ECO:0000313|EMBL:SGY25531.1};
GN Name=BQ5605_C018g08635 {ECO:0000313|EMBL:SGY25531.1};
GN ORFNames=BQ5605_C018G08635 {ECO:0000313|EMBL:SGY25531.1};
OS Microbotryum silenes-dioicae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=796604 {ECO:0000313|EMBL:SGY25531.1, ECO:0000313|Proteomes:UP000249464};
RN [1] {ECO:0000313|EMBL:SGY25531.1, ECO:0000313|Proteomes:UP000249464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FQNC01000020; SGY25531.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2X0NZY1; -.
DR STRING; 796604.A0A2X0NZY1; -.
DR Proteomes; UP000249464; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140082; F:SUMO-ubiquitin ligase activity; IEA:InterPro.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR049627; SLX8.
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; PTHR47094; ELFLESS, ISOFORM B; 1.
DR PANTHER; PTHR47094:SF12; ELFLESS, ISOFORM B; 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.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000249464};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 218..375
FT /note="RING-type"
FT /evidence="ECO:0000259|SMART:SM00184"
FT REGION 1..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..202
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..369
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 429 AA; 45541 MW; 23720D7F1F30B1F2 CRC64;
MASTSSASAL ALASASTSTS ALHSSPVLPS AAARATPPLD STRFNSASSP AESAPAPTTH
PRPTADHAVQ SDSEPDTDDE RGLPPPVRMR PASRVAVAIA GAATTTTTTT RTQFRAHPQR
TLQSSRQNRD QATTSTFSRA ETPVLDLTDD QAERSSPAAQ DDESLLILHS SQPQTTAPVP
SKRKRLRSRS RSSSHSRSRS RSRSRSPSQP TSLSNLTCPI CFGPPVPIAA TSCGHVFCAP
CLHAALLAGP ELTPPPPRVA AEVERNYGAN GFGRRINPAG GGGGIFNPSR GRNRSRVGPT
TTNNRSRSSY GGGASTYAHH PTPPWDERIE NDDNEEEELD DYEIYHPPNR NRQQVPPPLP
PPPPPGELDK HCPVCRKPLR GGWGRALRGV VLRMEPKKSK ETVSVTGKET GTGKVMEGDS
DVEGEGTGA
//
