ID A0A0J0XBD1_9TREE Unreviewed; 962 AA.
AC A0A0J0XBD1;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 22-FEB-2023, entry version 30.
DE SubName: Full=Beta-trefoil-domain-containing protein {ECO:0000313|EMBL:KLT38378.1};
GN ORFNames=CC85DRAFT_306028 {ECO:0000313|EMBL:KLT38378.1};
OS Cutaneotrichosporon oleaginosum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT38378.1, ECO:0000313|Proteomes:UP000053611};
RN [1] {ECO:0000313|EMBL:KLT38378.1, ECO:0000313|Proteomes:UP000053611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBC0246 {ECO:0000313|EMBL:KLT38378.1,
RC ECO:0000313|Proteomes:UP000053611};
RG DOE Joint Genome Institute;
RA Kourist R., Kracht O., Bracharz F., Lipzen A., Nolan M., Ohm R.,
RA Grigoriev I., Sun S., Heitman J., Bruck T., Nowrousian M.;
RT "Genomics and transcriptomics of the oil-accumulating basidiomycete yeast
RT T. oleaginosus allow insights into substrate utilization and the diverse
RT evolutionary trajectories of mating systems in fungi.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the Su(H) family.
CC {ECO:0000256|ARBA:ARBA00009704}.
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DR EMBL; KQ087314; KLT38378.1; -; Genomic_DNA.
DR RefSeq; XP_018274869.1; XM_018425666.1.
DR AlphaFoldDB; A0A0J0XBD1; -.
DR STRING; 879819.A0A0J0XBD1; -.
DR GeneID; 28986269; -.
DR OrthoDB; 1384914at2759; -.
DR Proteomes; UP000053611; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:InterPro.
DR Gene3D; 2.80.10.50; -; 1.
DR Gene3D; 2.60.40.1450; LAG1, DNA binding domain; 1.
DR InterPro; IPR015350; Beta-trefoil_DNA-bd_dom.
DR InterPro; IPR036358; BTD_sf.
DR InterPro; IPR040159; CLS_fam.
DR InterPro; IPR008967; p53-like_TF_DNA-bd_sf.
DR InterPro; IPR015351; RBP-J/Cbf11/Cbf12_DNA-bd.
DR InterPro; IPR037095; RBP-J/Cbf11_DNA-bd_sf.
DR PANTHER; PTHR10665; RECOMBINING BINDING PROTEIN SUPPRESSOR OF HAIRLESS; 1.
DR PANTHER; PTHR10665:SF0; SUPPRESSOR OF HAIRLESS PROTEIN; 1.
DR Pfam; PF09270; BTD; 1.
DR Pfam; PF09271; LAG1-DNAbind; 1.
DR SMART; SM01268; BTD; 1.
DR SMART; SM01267; LAG1_DNAbind; 1.
DR SUPFAM; SSF110217; DNA-binding protein LAG-1 (CSL); 1.
DR SUPFAM; SSF49417; p53-like transcription factors; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053611};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 128..431
FT /note="RBP-J/Cbf11/Cbf12 DNA binding"
FT /evidence="ECO:0000259|SMART:SM01267"
FT DOMAIN 432..624
FT /note="Beta-trefoil DNA-binding"
FT /evidence="ECO:0000259|SMART:SM01268"
FT REGION 50..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 962 AA; 103001 MW; 53E95A14546B5210 CRC64;
MADDDENNNT PLDLLLNAIS GTGGYAFAEG DAQHFPEALE SHFDDECVAD NADVLAKPGA
PEEEGALGAP AGPEEGGGAE GTGEGAGGGQ AQRRDGDGGA AQPSPSSVAR IQRTLRDHFA
GGRDTFSTVE VWHPKTGQKS YGKERRIIQP PPTLRVSGPL ASLVTFVTLS AHPNVDAEPG
RPVYSSQSHR FGLSDPDPEP QFSGSKKVER DRRARQIRAQ ASKAGWGSTL PWERKRTGIR
GRDEVMDGVT FPGLWVGEES GKSKEFRLEL GLGAPGVEVD ESGHPLGLMV DGVDQPLDEA
ALRQVLGSNT VFPDMVIPPV LESDVDAAVA AAQEHQQETQ TQTQTQTQTQ TQTQPETLET
HLNTPDESLR ETHSSLAHGG STLDSVTIPD AELPAQSQQA LPPLPWATFV SNPLSVVSKP
SQKTARARSM ASCLSSHDPF ALIVRVNGQT VRTKLLNLEG ADSDSPTLTA RAAKWTPFRF
ETVQHAASPE DQRRGRFNPE EVVNYGSVVR LVDVTSGMRS DLLRLVRVDR NKAVVGNDVG
HPVSELQRVG LVRVKENLED DMPGGRRWYL SSPGALAGAG EVKTTRSRLR KGKLAEQTDT
EPESEQQRKK RKTKRHALAR AVIEEEEQGS SASGLMFKAA DREDVVDDQG NTSIVETVQD
SMCWVLSGVG CFSYTFFNGM GETGSIPSSS LEPVPRILVN PALDTSTTPA TLQLTLSEFF
VANELGEAQP FQVYIGPLGP LRATTWRSVA PKAKPFEPQA PLDALPYDGF GQYSQVAPRT
PAGVVRSNFP HSVPHVIVCV ELPATEELIR AMQPAELQNE EAEDAWLGLG EGTLTIQEAL
HNANKASASA SASASDDVVM TMPEQGEFGV NSLNQLASLN EVGNAASLNG SPRAVAVTQT
HGWAESTITM HRPSQTGGKE HALPVLVVRP DGVGYGMGWS VERVPPEDNG GGIRIVQAAT
RA
//
