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Database: UniProt
Entry: M5G597_DACPD
LinkDB: M5G597_DACPD
Original site: M5G597_DACPD 
ID   M5G597_DACPD            Unreviewed;       551 AA.
AC   M5G597;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=RCC1/BLIP-II {ECO:0000313|EMBL:EJU03844.1};
GN   ORFNames=DACRYDRAFT_21271 {ECO:0000313|EMBL:EJU03844.1};
OS   Dacryopinax primogenitus (strain DJM 731) (Brown rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC   Dacrymycetales; Dacrymycetaceae; Dacryopinax.
OX   NCBI_TaxID=1858805 {ECO:0000313|EMBL:EJU03844.1, ECO:0000313|Proteomes:UP000030653};
RN   [1] {ECO:0000313|EMBL:EJU03844.1, ECO:0000313|Proteomes:UP000030653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJM-731 SS1 {ECO:0000313|EMBL:EJU03844.1,
RC   ECO:0000313|Proteomes:UP000030653};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
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DR   EMBL; JH795859; EJU03844.1; -; Genomic_DNA.
DR   AlphaFoldDB; M5G597; -.
DR   STRING; 1858805.M5G597; -.
DR   HOGENOM; CLU_005210_7_1_1; -.
DR   OMA; GKWKNTG; -.
DR   OrthoDB; 5940at2759; -.
DR   Proteomes; UP000030653; 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; 3.
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; 1.
DR   PROSITE; PS50012; RCC1_3; 4.
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:UP000030653};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   REPEAT          77..137
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   REPEAT          195..259
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   REPEAT          260..315
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   REPEAT          374..428
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   DOMAIN          445..497
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   REGION          504..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        512..551
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   551 AA;  58116 MW;  EA57BD9888D0A11F CRC64;
     MTDSAAAPDQ TEKEKWGRVL LCGGTNWLAL GKKGLPADPE YPDLPLPHTL RSLSNVKATG
     VYTSHSGCHV IVLDVAGAAY LFGRNTSSCL GVPHTSRPFI SQYTPLRLLP TDVGAAPGTK
     FVYAACGRAH SVLVGDEGSV WTAGLNAHGQ CGHPAGGEMG TWKLITGGWA RAKVGEKAVQ
     ASAGVNFTLV LTENGKVYAF GSGEHGQLAN GRTGERIAQA NKTTYDIEDE PIPVRGPLED
     KVTTQVACGQ QHAIALTSDG LVYVWGFNGY CRLGLGHPKD MLIPTLVPQY AGPNVLMRAA
     FVAAGPTSTI VIDRQKMLQM AGKFKTSGAG SVGQPFSTFR YFPEIQGCKV LLAAAGGVTH
     FATAVDEDAG PGGVMTIAWG QNAINSELGL GEGQPKSTPK PVRMETLNGI DVFALAAGQN
     TSFFLARPNE ALLDLPRFPD AVPAPNLCVV CNEDREASGE EALECEKCDT PYHLGCLDPP
     LKSIPEGQWF CPKCANEFED VLPLPGAKKS AGLPKADEEP KKKGRLAKRK AEDEEGDGGG
     GEAKKAKVAK K
//
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