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Database: UniProt
Entry: M5FXQ6_DACPD
LinkDB: M5FXQ6_DACPD
Original site: M5FXQ6_DACPD 
ID   M5FXQ6_DACPD            Unreviewed;       738 AA.
AC   M5FXQ6;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=B-related factor 1 {ECO:0000256|ARBA:ARBA00031009};
GN   ORFNames=DACRYDRAFT_107836 {ECO:0000313|EMBL:EJU01279.1};
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:EJU01279.1, ECO:0000313|Proteomes:UP000030653};
RN   [1] {ECO:0000313|EMBL:EJU01279.1, ECO:0000313|Proteomes:UP000030653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJM-731 SS1 {ECO:0000313|EMBL:EJU01279.1,
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).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the TFIIB family.
CC       {ECO:0000256|ARBA:ARBA00010857}.
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DR   EMBL; JH795864; EJU01279.1; -; Genomic_DNA.
DR   AlphaFoldDB; M5FXQ6; -.
DR   STRING; 1858805.M5FXQ6; -.
DR   HOGENOM; CLU_010293_2_1_1; -.
DR   OMA; FRESRYI; -.
DR   OrthoDB; 5483352at2759; -.
DR   Proteomes; UP000030653; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0017025; F:TBP-class protein binding; IEA:InterPro.
DR   GO; GO:0070897; P:transcription preinitiation complex assembly; IEA:InterPro.
DR   CDD; cd20554; CYCLIN_TFIIIB90_rpt2; 1.
DR   Gene3D; 2.20.25.10; -; 1.
DR   Gene3D; 1.10.472.10; Cyclin-like; 2.
DR   Gene3D; 1.20.5.650; Single helix bin; 1.
DR   InterPro; IPR011665; BRF1_TBP-bd_dom.
DR   InterPro; IPR013763; Cyclin-like_dom.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR000812; TFIIB.
DR   InterPro; IPR013150; TFIIB_cyclin.
DR   InterPro; IPR013137; Znf_TFIIB.
DR   PANTHER; PTHR11618:SF4; TRANSCRIPTION FACTOR IIIB 90 KDA SUBUNIT; 1.
DR   PANTHER; PTHR11618; TRANSCRIPTION INITIATION FACTOR IIB-RELATED; 1.
DR   Pfam; PF07741; BRF1; 1.
DR   Pfam; PF08271; TF_Zn_Ribbon; 1.
DR   Pfam; PF00382; TFIIB; 2.
DR   PRINTS; PR00685; TIFACTORIIB.
DR   SMART; SM00385; CYCLIN; 2.
DR   SUPFAM; SSF47954; Cyclin-like; 2.
DR   SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR   PROSITE; PS51134; ZF_TFIIB; 1.
PE   3: Inferred from homology;
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00469};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030653};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00469};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00469}.
FT   DOMAIN          16..47
FT                   /note="TFIIB-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51134"
FT   REGION          302..442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          455..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          584..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          660..711
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..328
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        585..599
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        686..702
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   738 AA;  81557 MW;  5E323E18BF9FFF8F CRC64;
     MQTGGHTGYC KFAPQPPQRC PECGGVRFDF DASAGASFCL TCGCVTEENT IVAEVTFGET
     SGGAAIVQGS HVAAGATRAK INAPWGRQGN FESMEQAKHK ARQILQGLKR HLGITETVIG
     YAERWWILAY EMGFTKGRRS LLVIGACCYI AVRQHQRPIM LIDLSDLLQA NVFDLGNVYL
     QLVQLLPVKN LDLVDPEFYI ERFSKLLEFG EDREKIRDDA VRIVHRFKRD WLYTGRRPSG
     ICGAALLLAA RMNNYRRSVL EIVQVVKIAD TTLKKRLVEF GKTPSASFSL DEFRHKWLDV
     EQNPPSFTKG QEKEERAQAK LLKQSSGKEN KRKGKKRKRG EEEEDESVAD SSVAGTPGPS
     TPEPSPKRPR LENGQSSVIA PSGVISKRKR GDKTDGADGD GSVVGLSAPP SPATKRPRLE
     DDLSVVPSVP TLPPPSGMPD MSFKRLIDEM ASMGVPPTET AADEPLFLPD EPTQVASSGP
     LVPTANDAEE TDRLIEQLIS SEVTLPLTAE RSVIEESLAI ADQLDEKRLQ IMRASAPAWE
     DGEEEIDLDE AELDDYILTD AEVEAKERVW VELNRQYLEK CAAREAVAQG EEEPAPKKRK
     HSNKRTGPRD SSNPRGATPA ESAMALITGT YRKKGEPQVR SKRINYDALE QLFNRPLKLG
     VTSPTQSKAG LRSAAEEKRA AAGGEEGAEE EEEEEEMEVV EEDGPIPGYR TLQRFQGGEQ
     YDDGYEEVYD ESGWQEEV
//
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