ID A0A165GDA3_9APHY Unreviewed; 563 AA.
AC A0A165GDA3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 28-JUN-2023, entry version 28.
DE SubName: Full=RCC1/BLIP-II {ECO:0000313|EMBL:KZT10189.1};
GN ORFNames=LAESUDRAFT_797258 {ECO:0000313|EMBL:KZT10189.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT10189.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT10189.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT10189.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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DR EMBL; KV427610; KZT10189.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165GDA3; -.
DR STRING; 1314785.A0A165GDA3; -.
DR InParanoid; A0A165GDA3; -.
DR OrthoDB; 5940at2759; -.
DR Proteomes; UP000076871; 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; 4.
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:UP000076871};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT REPEAT 92..150
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 151..206
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 207..270
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 271..326
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 383..437
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT DOMAIN 454..505
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..563
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 563 AA; 60239 MW; 1D91547F2E5A1377 CRC64;
MSTSETKSLS DKQSAEPQST EQWGRVLLCG GTDWPKLGRR ERGGGSKNAP EGDESGPDLL
EPHILRSLSN VKITSIHTSC VGCHVVAIDI DGAAWLFGRN ERAALGCTGM EYISENAPKR
LTARELGAPK GTRFVHAACG RNHTLLVGSG GQLWTAGANN HGQCGHPVCS EITSFKLVHG
PKVAGEKEEV IKAAAGVTFS IVLTTSGKVF SFGSAEHGQL GQGKTGEYIV TAGKTAFDIE
WDPILIKGLE DKRIVKIACG QQHSVALDSE GLVYVWGYNG YCRLGLGNQQ DALVPKVVPQ
FAVPDELTMG DDIVAGPSNT VVIDKQRMYW MAGKWKNTGD GSSGQPYSSF RYIQDIAACK
VTHAACGGVT HWALAPDEDD GGVMTIAFGQ GAANGELGLG PDETKSATKP IRNQPLIGVD
VFQIAAGQHT TFFLAKPNEK MSELPRHPVD VGAPDLCVVC KTNKGEDDVL LECDKCDRPY
HLKCLDPPLD AVPEGEWFCP ECVEYPGAPI GPEGVDTSQA RHGNPETTDE EEAADEEKKP
AHKASRKRKS SGKAKTGTTK RRK
//
