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Database: UniProt
Entry: A0A0P1BLH8_9BASI
LinkDB: A0A0P1BLH8_9BASI
Original site: A0A0P1BLH8_9BASI 
ID   A0A0P1BLH8_9BASI        Unreviewed;       957 AA.
AC   A0A0P1BLH8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Cytoplasm protein {ECO:0000313|EMBL:CEH17592.1};
OS   Ceraceosorus bombacis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX   NCBI_TaxID=401625 {ECO:0000313|EMBL:CEH17592.1, ECO:0000313|Proteomes:UP000054845};
RN   [1] {ECO:0000313|EMBL:CEH17592.1, ECO:0000313|Proteomes:UP000054845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A.,
RA   Brescovit A.D., Santos A.J.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CCYA01000265; CEH17592.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P1BLH8; -.
DR   STRING; 401625.A0A0P1BLH8; -.
DR   OrthoDB; 463769at2759; -.
DR   Proteomes; UP000054845; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:UniProt.
DR   GO; GO:0051716; P:cellular response to stimulus; IEA:UniProt.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR15067; E3 UBIQUITIN-PROTEIN LIGASE RNF8; 1.
DR   PANTHER; PTHR15067:SF8; E3 UBIQUITIN-PROTEIN LIGASE RNF8; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF17123; zf-RING_11; 1.
DR   SMART; SM00240; FHA; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054845};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          305..352
FT                   /note="FHA"
FT                   /evidence="ECO:0000259|PROSITE:PS50006"
FT   DOMAIN          449..493
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          120..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          280..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          540..630
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          659..695
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          759..957
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..79
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..169
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..564
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        602..618
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        769..783
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        825..846
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        861..879
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        882..896
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        908..957
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   957 AA;  99076 MW;  B611B623F161D6A8 CRC64;
     MPRSPGHNSS TSFSGSPSAA SGEGAPRPSL SSSGSSFLRH FRPRTSDGRR NGSGFSGFGP
     FGNHSTAAVT STQPSSPGAE TEEMADLTRV SSTGLRANVA FLPRMVRRIS LGTGRSEAAD
     LAAARAPPAR TNQEAPNGSR NVTPLPSATP VSAVSSPARP SDERTGPTAS TTAALALNGA
     TSTAASSSPA DGQARQTHRI RLVPHLEATR SLHFEPIERD LVEGSNTVKI GRFTDRNASQ
     VANAGTQAAA AATSASAPAA ATTGNASNAL STGGVASNST QLAGAASGAP GARGGAIPSS
     AGGGGRVDSA RIAFKSKVVS RGHAEVWCES GGNFFIRDTK SSSGTFLNHI RLSAPNAESR
     PFPIKDGDVV QLGVDYQGGT EEIYRCVKMR VELNRGWQRA ANEFNMSALR QLRALQGTPM
     ESAKAKTPAI ATTGPQPPTN RQSMSVTDCC ICLFSVTVCQ SLFIAPCSHV FHYKCIRPLL
     LQHHPGFSCP LCRTFADLEA DVEQDDAWQE ALIKEAEKLA SAADPEVSAS TPMAEIEPSP
     LAMADSTGSP LAHHSHQPSD SLTVAGSHVR RPAPAEAPRT NGWARPGTAV ANGPAPTHSL
     DATAAGGSSQ SRSAATPPLE SPGNAGMEDE QEELMDEAAD YANLIDEGDL AGLTTVAGVS
     ESRRGSNPID MPAGQQRHSF APPIPSPSAD LENARTPQNN TFLSTLAEAP APARSAIRGA
     ASSEMSRPNM PSLSAALRAD EVPLASNEAE RFLHASGDLR RPSEVSVQSD FEVFATPQDG
     NSPSAAHAKA RGIPSNQEDT AQLFGASTPF AYASELDDGD LTGPSSLDGP SSQTHGRPSS
     TKGKRPLNLS VAEEEDELVE LGSDIRGSHD RRSPYKSVEM DKNLSRASSN TSRSALGHSK
     GHERNSLGGS AGGSSIATGN SALDRRGSGS QESAGSTPSN QGKISRLLKR AQNAVQS
//
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