ID A0A0P7BQ71_9HYPO Unreviewed; 720 AA.
AC A0A0P7BQ71;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=PHD and RING finger domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AK830_g3078 {ECO:0000313|EMBL:KPM43513.1};
OS Neonectria ditissima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM43513.1, ECO:0000313|Proteomes:UP000050424};
RN [1] {ECO:0000313|EMBL:KPM43513.1, ECO:0000313|Proteomes:UP000050424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R09/05 {ECO:0000313|EMBL:KPM43513.1,
RC ECO:0000313|Proteomes:UP000050424};
RA Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT ditissima.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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:KPM43513.1}.
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DR EMBL; LKCW01000032; KPM43513.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7BQ71; -.
DR STRING; 78410.A0A0P7BQ71; -.
DR OrthoDB; 5490909at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000050424; Unassembled WGS sequence.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProt.
DR CDD; cd15545; PHD_BAZ2A_like; 1.
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 InterPro; IPR024766; Znf_RING_H2.
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; PF12678; zf-rbx1; 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; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000050424};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 93..116
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 164..212
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 220..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..634
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 720 AA; 79589 MW; 249A641801D08340 CRC64;
MSEPEQCIIC LDPLPLPRST SFDAGHGAGA GAGAGSGAAG GAGGAGDAVP VPAATAPEAV
QVKVEGDVEN DHSNGSGNDD SSYLNIVAAL DGCNHIIHDA CIRSWAQKTN TCPICRNPFH
SVRVYNGVDG SEICEYDVQD KKQVAEFDVQ QWLGDNPEEE EEQGNPCPVC NSAEREDVLL
LCDSCDAAYH THCVGLECIP DGDWYCMECS HLFQLVEDPA TAESGERSPR PQDVRRPNPR
SVRGYHVRTR ERLRRARRQA RNVEWQGAWG QFSGRFYEMS ELDLDNHDNE DEDLEQFRQF
QELGRRELDR WQQRMEIAQR LGAREAFVNN IPQAISDRLQ SIPEPVEETR DERRAWGALD
RAREVDEPAP NTNSRKRKVR SVTASPREPV VQEPERKLKR PRTRRLPTQV AEASSSMSSP
ANVATASAAS APAGPSATRT TNGTSSSNGV AGRNNIDPPL VSSLLKELEP HAMSDDETSV
VGWRYPPEAS SPVLSPAISP SPSARGSPRA LSLTPPPLPS VGGRPNSPPL SLSTHIQPVY
PPANYSPNRK NHDRSDSESR PSRSEGRPSS PPLSLSTNIQ PRYPPANYSP TRKSHNHSDS
ESLLSRPETR PEGRPLELRQ PRPRRAHQVP AHSDDQHSPT RWTMSQEEKR SINDIVKIAL
RPHWRAQKLT TEQYATINRD ISRKLYDEVK DAISLNGDAR QSWEKRATKE VAQAVEELQA
//
