ID W5MWF3_LEPOC Unreviewed; 694 AA.
AC W5MWF3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=B-related factor 1 {ECO:0000256|ARBA:ARBA00031009};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000012712.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000012712.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; AHAT01003765; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01003766; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01003767; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MWF3; -.
DR STRING; 7918.ENSLOCP00000012712; -.
DR Ensembl; ENSLOCT00000012736.1; ENSLOCP00000012712.1; ENSLOCG00000010360.1.
DR eggNOG; KOG1598; Eukaryota.
DR GeneTree; ENSGT00390000010349; -.
DR HOGENOM; CLU_010293_2_3_1; -.
DR InParanoid; W5MWF3; -.
DR OMA; AEPPCKV; -.
DR Proteomes; UP000018468; Linkage group LG7.
DR Bgee; ENSLOCG00000010360; Expressed in ovary and 13 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000126; C:transcription factor TFIIIB complex; IBA:GO_Central.
DR GO; GO:0097550; C:transcription preinitiation complex; IBA:GO_Central.
DR GO; GO:0000995; F:RNA polymerase III general transcription initiation factor activity; IBA:GO_Central.
DR GO; GO:0001006; F:RNA polymerase III type 3 promoter sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0017025; F:TBP-class protein binding; IEA:InterPro.
DR GO; GO:0006352; P:DNA-templated transcription initiation; IBA:GO_Central.
DR GO; GO:0006383; P:transcription by RNA polymerase III; IBA:GO_Central.
DR GO; GO:0070897; P:transcription preinitiation complex assembly; IEA:InterPro.
DR CDD; cd20553; CYCLIN_TFIIIB90_rpt1; 1.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cyclin {ECO:0000256|ARBA:ARBA00023127};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00469};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
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 2..33
FT /note="TFIIB-type"
FT /evidence="ECO:0000259|PROSITE:PS51134"
FT REGION 388..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 300..334
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 551..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 694 AA; 76273 MW; 05BC64D21C1C464E CRC64;
MSSRVCKNCG CTDIDIDQAR GDAVCTGCGS VLEDNIIVSE VQFVENSGGG SSAVGQFVSS
DGSGKAPVLG TGFHTSLGKE SRAQTLQNGK RQIHNLGHQL QLNQHCMDTA FNFFKMAVSK
HLTRGRKMMH VIAACLYLVC RTEGTPHMLL DLSDLLQVNV YVLGKTFLLL ARELCINAPA
IDPCLYIPRF AHMLEFGDKN HEVSMTALRL LQRMKRDWMH TGRRPSGLCG AALLVAARMH
DFRRTVKEVI GVVKVCEATL RKRLTEFEDT PTSQLTISEF MKVDLEQECD PPSFTAGQRK
VKLQQLEHEL AKKLDEVEGE ISGYQDEIET ELENSRPRLK GLYASYAKED IQDDSLSLAS
SSLAGDDERD DEELEAAAQH LSKDFCHEVL PQSGGPGAGG EPGQASPAKQ PLPLATLLGP
LPTAASLGLT ESLRECIATA NENDGNPENG ELDLNGIDDD EIDRYILNET EVKIKTELWT
RENSDYLKEQ KEKEERIAKE KELGIYKEQK PKRSLKKREP IRASTAGEAI EKMLEQKKIS
SKINYDVLRD LNSKGSGSSP SKRQEDSGDN GTGAKKTSSH RKTTSTSRAL ATPVSSVGKR
LQPLISAQPC KKRATEQLFS SLPSAFSLLQ TACSSNPPAP SDPSQPVVVE SGPVQYTEED
VEEEEEEEEE PCVSALELMG ANDYGYEVDD EDGY
//
