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Database: UniProt
Entry: A0A1Y2F037_9BASI
LinkDB: A0A1Y2F037_9BASI
Original site: A0A1Y2F037_9BASI 
ID   A0A1Y2F037_9BASI        Unreviewed;      1137 AA.
AC   A0A1Y2F037;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   13-SEP-2023, entry version 21.
DE   RecName: Full=R3H domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BCR35DRAFT_305534 {ECO:0000313|EMBL:ORY77238.1};
OS   Leucosporidium creatinivorum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Leucosporidiales; Leucosporidium.
OX   NCBI_TaxID=106004 {ECO:0000313|EMBL:ORY77238.1, ECO:0000313|Proteomes:UP000193467};
RN   [1] {ECO:0000313|EMBL:ORY77238.1, ECO:0000313|Proteomes:UP000193467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=62-1032 {ECO:0000313|EMBL:ORY77238.1,
RC   ECO:0000313|Proteomes:UP000193467};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the NFX1 family.
CC       {ECO:0000256|ARBA:ARBA00007269}.
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:ORY77238.1}.
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DR   EMBL; MCGR01000032; ORY77238.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2F037; -.
DR   STRING; 106004.A0A1Y2F037; -.
DR   InParanoid; A0A1Y2F037; -.
DR   OrthoDB; 1412at2759; -.
DR   Proteomes; UP000193467; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd06008; NF-X1-zinc-finger; 5.
DR   Gene3D; 3.30.1370.50; R3H-like domain; 1.
DR   InterPro; IPR034078; NFX1_fam.
DR   InterPro; IPR001374; R3H_dom.
DR   InterPro; IPR036867; R3H_dom_sf.
DR   InterPro; IPR000967; Znf_NFX1.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR001841; Znf_RING.
DR   PANTHER; PTHR12360; NUCLEAR TRANSCRIPTION FACTOR, X-BOX BINDING 1 NFX1; 1.
DR   PANTHER; PTHR12360:SF12; TRANSCRIPTIONAL REPRESSOR NF-X1; 1.
DR   Pfam; PF01424; R3H; 1.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00393; R3H; 1.
DR   SMART; SM00438; ZnF_NFX; 7.
DR   SUPFAM; SSF82708; R3H domain; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51061; R3H; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193467};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          244..318
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          247..316
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          868..930
FT                   /note="R3H"
FT                   /evidence="ECO:0000259|PROSITE:PS51061"
FT   REGION          1..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..177
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..227
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1137 AA;  120868 MW;  EEB81541AFE6E754 CRC64;
     MSSSPAAAPS ATAPSSSTTA PPPSNPPSSS STSTRGNGRP RNRRGRGAKG IAQQQIPAIQ
     AGEAANAPPP STTSSRGGGT GRGSRGGRGG RGGSSRGGRG GGRAGAQNGV SQTGEGAEAA
     QGDATSTPID GPSAPTTSTT RQQRLRNQSR SRQPTAQAQD GLTPSSSTAA TNAEPNPNAE
     QPKPPARGGR RAKFNASLSS STSLHPTAAS FTPSTTPSHA HSHNPAPVSQ TLLSRLTTEL
     TSGTAECSIC VSDISRTARI HSCSTCSTPF HLNCIKEWAT RSVNDSAERA RLLATSANPP
     TDPRATEGSW RCPSCQSLSY SPSSIPTRYH CYCHRLLDPS HRPPTTPHSC GQPCAKPRPE
     GCGHETCGLM CHPGPCPPCS VVLEKSCWCG DEEKRVRCSA MFPPRGVVSV GEEKEALLSC
     GKICAKMLEC GMHVCERVCH EGACGGCEEV RRKRCFCGRG ERVEGCGVGS EARVEGCRRV
     GKDGEEEKSE SWLGEWSCEE VCGAPFDCTH HSCTSPCHAH TSPSPLPVPS HPLKSQHATT
     SRICSSSAEG GEGEGEEFMC GRVCKAMRTC GRHQCNRVCC PLSYQEALQL KSTNKRRGAT
     NEQWQVEDDP LGIHACDRVC GRKLNCGVHF CEMGDHRGAC GPCLRADFDE LVCNCGSTVV
     LPPIPCSYTI DCRHPCIRPS SCGHQTMPHA CHEDPIPCPP CPFLVEKECA CGKKRVGNVR
     CSLGKEKVSC GTVCGKLLRC GFHRCRRSCH PSGSCESCDQ TCLKPLRLCH HPCPSPCHSP
     TSCPTDSPCP KLITVTCACG HLQQSARCGS CDAKPEGNQG RLLKCGDACA AAKRSKQLAE
     ALGVEKREPR VREVEYEPLM LSFYGANVAW CNSIEAQLAE FVKGDIPSLH FPVMKRPQRA
     FTHELAELFD LRSESLDEEP RRSVVVHRQS NSAIPTPTLA NALIAQRKSA STTLTFGSLR
     KPTQPEKKAS NAIYLEGVLG FDEAMLKDIL RPLTRGLVFS CTWVGEEDVL VTFDTSVPEI
     LDPKLPLMVN SFRTLASDTG FCATVEPVHL SPEDGKITRG AWTPVASTSR SSGGNSWRNG
     ASQNVFTPNA FASLGGGGTQ SAPTPARTAW GAGGGVVGPA AYKVRSSSFL RNLSLRR
//
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