ID A0A371DED0_9APHY Unreviewed; 622 AA.
AC A0A371DED0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=RCC1/BLIP-II {ECO:0000313|EMBL:RDX50919.1};
GN ORFNames=OH76DRAFT_1402151 {ECO:0000313|EMBL:RDX50919.1};
OS Polyporus brumalis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Polyporus.
OX NCBI_TaxID=139420 {ECO:0000313|EMBL:RDX50919.1, ECO:0000313|Proteomes:UP000256964};
RN [1] {ECO:0000313|EMBL:RDX50919.1, ECO:0000313|Proteomes:UP000256964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM 1820 {ECO:0000313|EMBL:RDX50919.1,
RC ECO:0000313|Proteomes:UP000256964};
RX PubMed=30061923; DOI=10.1186/s13068-018-1198-5;
RA Miyauchi S., Rancon A., Drula E., Hage H., Chaduli D., Favel A., Grisel S.,
RA Henrissat B., Herpoel-Gimbert I., Ruiz-Duenas F.J., Chevret D., Hainaut M.,
RA Lin J., Wang M., Pangilinan J., Lipzen A., Lesage-Meessen L., Navarro D.,
RA Riley R., Grigoriev I.V., Zhou S., Raouche S., Rosso M.N.;
RT "Integrative visual omics of the white-rot fungus Polyporus brumalis
RT exposes the biotechnological potential of its oxidative enzymes for
RT delignifying raw plant biomass.";
RL Biotechnol. Biofuels 11:201-201(2018).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KZ857397; RDX50919.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371DED0; -.
DR STRING; 139420.A0A371DED0; -.
DR Proteomes; UP000256964; Unassembled WGS sequence.
DR Gene3D; 1.20.1280.50; -; 1.
DR Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 1.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR PANTHER; PTHR45982; REGULATOR OF CHROMOSOME CONDENSATION; 1.
DR PANTHER; PTHR45982:SF1; REGULATOR OF CHROMOSOME CONDENSATION 1; 1.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF13540; RCC1_2; 1.
DR PRINTS; PR00633; RCCNDNSATION.
DR SMART; SM00256; FBOX; 1.
DR SUPFAM; SSF81383; F-box domain; 1.
DR SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR PROSITE; PS50012; RCC1_3; 2.
PE 4: Predicted;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000256964}.
FT DOMAIN 7..48
FT /note="F-box"
FT /evidence="ECO:0000259|SMART:SM00256"
FT REPEAT 76..132
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 133..188
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REGION 557..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 622 AA; 69392 MW; 260B5ED6D1FD7786 CRC64;
MPGIVDLPVE LFFDQIFDYL PVRDILNLGC TNRFFSSVVS DEIFWHRRIQ EDFNFSGSDT
ARKTGWKIIY KRLSNSHVYV WGEKSQGRLG TLDFPKTNVR DGVPYPIRLD IPGVRVVSLV
AGGMSFHAID SKGDIYVWGV LDGTSMALRS DGFSEPSKKA ERPVRLNLPE KFRLLSCGRL
HTTALDAKGQ VWTFTSWGRP YRLSSSLIDR SSPETTPKQI ESGWSFSSIL TESGDILVYW
PFGGRLKAIA DQKKEELDSS DNEAVKAAAK ARPTEAEPNV VPCYWWVMHG ADPVRLPPIP
VENLPVLPCT GLSQKQRDEE TKVVKIASLD NNILALTNKG HVLRHGELYG EETYRAGRWE
YLPLFSDISK IKQQPAYSPS PENPTPLLAP DTMQITHISA SFQTFFAYSS TVVLTGHEIP
PQRTVNPNPN QDNFNNYFAP TILPELQNRN VISVVVGDYH YGALTADGKL LTWGAFSRGA
LGLGDPVDIP VGEPGGFTTQ ELKNHAFHER WGLMHAPPDV RTPTEVRFDW QEKRKRPKFC
FGAAALGWHM GALVIDLDPD QDGDDEHVAE PPTDTESRRD EESQETSGSD LPFLGRGRGM
FPFRIGHAGR GMYRGGLPPG GQ
//
