ID Q8J116_CRYNV Unreviewed; 850 AA.
AC Q8J116;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 2.
DT 22-FEB-2023, entry version 88.
DE SubName: Full=ZNF1 {ECO:0000313|EMBL:AAN75157.2};
OS Cryptococcus neoformans var. grubii (Filobasidiella neoformans var.
OS grubii).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=178876 {ECO:0000313|EMBL:AAN75157.2};
RN [1] {ECO:0000313|EMBL:AAN75157.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=125.91 {ECO:0000313|EMBL:AAN75157.2};
RX PubMed=12455690; DOI=10.1128/EC.1.5.704-718.2002;
RA Lengeler K.B., Fox D.S., Fraser J.A., Allen A., Forrester K.,
RA Dietrich F.S., Heitman J.;
RT "Mating-type locus of Cryptococcus neoformans: a step in the evolution of
RT sex chromosomes.";
RL Eukaryot. Cell 1:704-718(2002).
RN [2] {ECO:0000313|EMBL:AAN75157.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=125.91 {ECO:0000313|EMBL:AAN75157.2};
RX PubMed=15538538; DOI=10.1371/journal.pbio.0020384;
RA Fraser J.A., Diezmann S., Subaran R.L., Allen A., Lengeler K.B.,
RA Dietrich F.S., Heitman J.;
RT "Convergent evolution of chromosomal sex-determining regions in the animal
RT and fungal kingdoms.";
RL PLoS Biol. 2:2243-2255(2004).
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DR EMBL; AF542528; AAN75157.2; -; Genomic_DNA.
DR AlphaFoldDB; Q8J116; -.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15571; ePHD; 1.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR029617; Snt2.
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; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR47672; E3 UBIQUITIN-PROTEIN LIGASE SNT2; 1.
DR PANTHER; PTHR47672:SF1; E3 UBIQUITIN-PROTEIN LIGASE SNT2; 1.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00439; BAH; 1.
DR SMART; SM00249; PHD; 3.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 1..124
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 161..213
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 571..715
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 393..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 850 AA; 96601 MW; 22E19CC25889BB6D CRC64;
MCMFHSRGRI EMASTPYNIA RIIEFLPPHT SPKKGSRVAP SSDIMVRLAL YYRPSDISAR
NFADARLLLA AIHTDIQPIS NVRGKCYVRH KDRIPDLLEW KRLPDHFYFS KFFDPYIKRE
FEVIRTVNVN NIPSTVKDVL MRRYEYLITE REMVADLTDD FRICCCCRQW SSFQDSVKCE
SCREYYHMTC LQPPLLAKPA KGYSWVCPSC FFQRNTQPEG QKLLLQNDWS GTGKLRAAKT
KMKSNTLDFT PDTMFRGWPW RYFGHVRSGR CNIPPGRYSL ADYMEHVRSL SLAVPPWDVE
RINLALSSYS SMGREAAYHF MCHTVLSDFH PVHFTEEESA VFEAELERNG GLDVISCSKI
LKRTTSDILR FSYIWKNDKL KVENEALRQH RRVSVSHARQ NRTLGPPSLG KMRIGDKSKV
EDDETSLYGS SIGESTMRCA TCSTKLGQVW WKSPRTVPGI AMCESCGSNY RKYGVISFVR
SDDSKRIDHR EHVAKKGKNE VNDQPIGSLW SSKHNQCACC RRVEPKSQLV RCRNCNFIAH
TGCYGTTLLD QKSDWECDLC VNEKTEECHV EPHCVLCPRT PHLAMKVKKK TAEYNLLTAL
KPSEGRRWAH LLCSAWTNGV EYGDAVSFKQ IEGIMSIRGD IWAAACSLCG QNDGAVIKCS
DCDIQFHVSC AWQCGFTLGF EFILAKPGKS QNQIVIKFKE SEGVMNAGAW CKSHDLSNRT
VYDMFDVESD GGETAFQVYV RAYKSATWHS AFPLLRKAIR LELITQSPSN TDSPENIQTD
VVRCDSCGVL NSPMWHKHDT GTVPSGAPSD PADDSKSVSK SAVGDERGSE ERQLCHLCWY
QINLNGAPSF
//
