ID A0A317XQ94_9BASI Unreviewed; 554 AA.
AC A0A317XQ94;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 28-JUN-2023, entry version 17.
DE SubName: Full=RCC1/BLIP-II {ECO:0000313|EMBL:PWZ00060.1};
GN ORFNames=BCV70DRAFT_200229 {ECO:0000313|EMBL:PWZ00060.1};
OS Testicularia cyperi.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Anthracoideaceae; Testicularia.
OX NCBI_TaxID=1882483 {ECO:0000313|EMBL:PWZ00060.1, ECO:0000313|Proteomes:UP000246740};
RN [1] {ECO:0000313|EMBL:PWZ00060.1, ECO:0000313|Proteomes:UP000246740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 3645 {ECO:0000313|EMBL:PWZ00060.1,
RC ECO:0000313|Proteomes:UP000246740};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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DR EMBL; KZ819193; PWZ00060.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317XQ94; -.
DR STRING; 1882483.A0A317XQ94; -.
DR InParanoid; A0A317XQ94; -.
DR Proteomes; UP000246740; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR028641; RCC2.
DR InterPro; IPR000408; Reg_chr_condens.
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; PTHR46207; PROTEIN RCC2; 1.
DR PANTHER; PTHR46207:SF1; PROTEIN RCC2; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF00415; RCC1; 2.
DR Pfam; PF13540; RCC1_2; 1.
DR PRINTS; PR00633; RCCNDNSATION.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR PROSITE; PS00626; RCC1_2; 2.
DR PROSITE; PS50012; RCC1_3; 5.
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 Reference proteome {ECO:0000313|Proteomes:UP000246740};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT REPEAT 85..156
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 157..212
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 213..276
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 277..332
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 394..448
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT DOMAIN 466..518
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 519..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 554 AA; 59113 MW; 35B4BB0F28B15793 CRC64;
MTATDKTSQA STSDLPDWGR VLVTGGIDWP TLGRKATKNG PPLVINPEHP DLPSPHILRS
VSNIRMRRIF SSHSSCHAVL LSVDGDAYIL GRNEQGQCGL PIRPESSSPK PSGTSIWNAY
KLDRATDFIP PLPPTEAGDI VAAACGRSHT LLITASGSVY GTGLNTSGQC GLPNMSILST
FQKIETAPFI KEKDPVVAAS CGNTFSMLLT KSGKVYTMGS SEKGQLGNGR TGEHFISGTK
LAFNTFSEPF LVKQLADKKI VQLACGQQHT IAMDDEGFVY VWGFGGYGRL GLGSQQDQLL
PTLVPQYARE NVLTRATAVF AGSTNSAVID GQRMFWLAGK WKTSGEGSAG QGFMTFKYLP
DLMGVKVKNA GLGGVTLLCT AQEDASIQGE HQATMNICWG QNANCGELGL GEGKPRSATK
PMRCETLDGI AILDIAAGQN TTFYLARNMG PAYSELPRFP EMVDSAETCL VCGSDNSTDE
NALLECEKCE NPWHLKCLDP PLTEIPEGEW HCPRCAPATT SASAASNKRT AVSATAADED
LHSASTPAAK KRRT
//