ID   UHRF1_CRYNH             Reviewed;         342 AA.
AC   J9VHE9;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2013, sequence version 2.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=UHRF1-like protein {ECO:0000303|PubMed:31955845};
GN   Name=UHF1 {ECO:0000303|PubMed:31955845};
GN   Synonyms=UHRF1 {ECO:0000303|PubMed:31955845};
GN   ORFNames=CNAG_00677 {ECO:0000312|EMBL:AFR92806.2};
OS   Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS   CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=235443 {ECO:0000312|Proteomes:UP000010091};
RN   [1] {ECO:0000312|Proteomes:UP000010091}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487
RC   {ECO:0000312|Proteomes:UP000010091};
RX   PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA   Janbon G., Ormerod K.L., Paulet D., Byrnes E.J. III, Yadav V.,
RA   Chatterjee G., Mullapudi N., Hon C.-C., Billmyre R.B., Brunel F.,
RA   Bahn Y.-S., Chen W., Chen Y., Chow E.W.L., Coppee J.-Y., Floyd-Averette A.,
RA   Gaillardin C., Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S.,
RA   Hamlin J.L., Hsueh Y.-P., Ianiri G., Jones S., Kodira C.D., Kozubowski L.,
RA   Lam W., Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K.,
RA   Proux C., Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A.,
RA   Zeng Q., Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA   Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA   Cuomo C.A., Dietrich F.S.;
RT   "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT   grubii reveals complex RNA expression and microevolution leading to
RT   virulence attenuation.";
RL   PLoS Genet. 10:E1004261-E1004261(2014).
RN   [2] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=31955845; DOI=10.1016/j.cell.2019.12.012;
RA   Catania S., Dumesic P.A., Pimentel H., Nasif A., Stoddard C.I., Burke J.E.,
RA   Diedrich J.K., Cook S., Shea T., Geinger E., Lintner R., Yates J.R. III,
RA   Hajkova P., Narlikar G.J., Cuomo C.A., Pritchard J.K., Madhani H.D.;
RT   "Evolutionary Persistence of DNA Methylation for Millions of Years after
RT   Ancient Loss of a De Novo Methyltransferase.";
RL   Cell 180:263.277.e20-263.277.e20(2020).
CC   -!- FUNCTION: Involved in the maintenance of DNA methylation
CC       (PubMed:31955845). Binds hemimethylated DNA (PubMed:31955845).
CC       {ECO:0000269|PubMed:31955845}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00358}.
CC   -!- DISRUPTION PHENOTYPE: Mildly decreases methylation of the fifth carbon
CC       of cytosine (5mC) in DNA; simultaneous disruption of CLR4 exacerbates
CC       the effect. {ECO:0000269|PubMed:31955845}.
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DR   EMBL; CP003820; AFR92806.2; -; Genomic_DNA.
DR   RefSeq; XP_012046390.1; XM_012191000.1.
DR   EnsemblFungi; AFR92806; AFR92806; CNAG_00677.
DR   GeneID; 23884459; -.
DR   VEuPathDB; FungiDB:CNAG_00677; -.
DR   HOGENOM; CLU_033265_0_0_1; -.
DR   Proteomes; UP000010091; Chromosome 1.
DR   GO; GO:0005634; C:nucleus; IC:UniProtKB.
DR   GO; GO:0044729; F:hemi-methylated DNA-binding; IDA:UniProtKB.
DR   Gene3D; 2.30.280.10; -; 1.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR036987; SRA-YDG_sf.
DR   InterPro; IPR003105; SRA_YDG.
DR   InterPro; IPR045134; UHRF1/2-like.
DR   PANTHER; PTHR14140; PTHR14140; 1.
DR   Pfam; PF02182; SAD_SRA; 1.
DR   SMART; SM00466; SRA; 1.
DR   SUPFAM; SSF88697; SSF88697; 1.
DR   PROSITE; PS51015; YDG; 1.
PE   3: Inferred from homology;
KW   Nucleus.
FT   CHAIN           1..342
FT                   /note="UHRF1-like protein"
FT                   /id="PRO_0000454229"
FT   DOMAIN          168..322
FT                   /note="YDG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00358"
FT   REGION          41..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          236..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..73
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..94
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..138
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        241..257
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         218
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /ligand_part="5-methylcytosine group"
FT                   /ligand_part_id="ChEBI:CHEBI:65274"
FT                   /evidence="ECO:0000250|UniProtKB:Q96T88"
SQ   SEQUENCE   342 AA;  38167 MW;  60B263906E11AB35 CRC64;
     MMRYEDVSQL SLMNLTYEEQ RLENIRKNED LLRSLGLGAP SEATTLATPS NLKTAGNQRR
     YNDTLVGKSN TGRNRSDSPR KRPTKDREDL NLVPQSAIKR RQSVRLGGKE KPNYTREQVT
     FNSDRDTPNT PSRQIKSTHS HPGSEEEDIR QVKTRTLGVR VHNPKTFGHI PGIGVGKWWA
     TRMEASADAV HAPTVAGISG NAHEGAWSVA LSGGYPDDID LGYAFTYTGC GGRDLKGTKQ
     NPKNLRTAPQ TSHQSFDNPL NAALKRSAET RNPVRVIRGF KLQSKYAPPT GYRYDGLYIV
     EKAWMAKGLT NGLMVCRYAF KRMDDQGPLP QKDLDHDDDN KA