ID A0A0F4GWI5_9PEZI Unreviewed; 587 AA.
AC A0A0F4GWI5;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 03-MAY-2023, entry version 31.
DE SubName: Full=PHD and RING finger domain-containing protein {ECO:0000313|EMBL:KJY01413.1};
GN ORFNames=TI39_contig291g00023 {ECO:0000313|EMBL:KJY01413.1};
OS Zymoseptoria brevis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJY01413.1, ECO:0000313|Proteomes:UP000033647};
RN [1] {ECO:0000313|EMBL:KJY01413.1, ECO:0000313|Proteomes:UP000033647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zb18110 {ECO:0000313|EMBL:KJY01413.1,
RC ECO:0000313|Proteomes:UP000033647};
RA Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT "RNA-seq based gene annotation and comparative genomics of four
RT Zymoseptoria species reveal species-specific pathogenicity related genes
RT and transposable element activity.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:KJY01413.1}.
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DR EMBL; LAFY01000283; KJY01413.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4GWI5; -.
DR STRING; 1047168.A0A0F4GWI5; -.
DR OrthoDB; 5490909at2759; -.
DR Proteomes; UP000033647; 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); 2.
DR InterPro; IPR047157; PHRF1-like.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12618; PHD AND RING FINGER DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR12618:SF20; PHD AND RING FINGER DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS01359; ZF_PHD_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:UP000033647};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 39..83
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 19..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 587 AA; 64915 MW; 5A988F5B6EFA3A88 CRC64;
MADTCIVCLG DLRSAFVEDP PPSTAAADDA SKGSDAKDCT DSNAQSIQSD DEAIAHLLPC
KHDLHNSCLK PWVERANSCP ICRTTFNMVE ISRTVGGPVV DSYPVRDKAQ EAEIDPGMIA
DDELFAVEAW EPCVVCGVSD DGHSAMYCDG CDRTVHIFCA GFDDAPEVWY CEACLVDMEN
DADLPGMASA VNRRPRARNV AGVARSRAPP RRRRNNDAVW ARVWQEVAQR LDLDLDFPFD
EEIIEQRTEE QRREFQRWQR RFEVASNNQG ATQRLRGIAQ GRLNSSSEPQ PAPESQEEIR
AWNAFDKARE SHDAPPAAQR RKRRVTESPA SPQDGENTEQ PQLKKPRLRR PPTAPGQPES
SNAAAARRVE PTFLSSLLRE VENKPMTAAS PATSDQAYGH VSPHNSSPAR SPESSDCGTP
HATTPPPQRP LSPPLSSTVL PVTSPLAATF SPFSPTGNGE HARHPEGLHR RGRRRRGHSD
PQDQYDSAPE DRASSQSPSR NMSYSAKEEL QRMVKLALGT RYRDKEITKD QYTDINKSVS
RRLYDLVRDA SALADQEQRE KWQGVANEEV QKAIGALSPI SSGPDDN
//
