ID A0A0V1CRF6_TRIBR Unreviewed; 605 AA.
AC A0A0V1CRF6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=B-related factor 1 {ECO:0000256|ARBA:ARBA00031009};
GN Name=Brf1 {ECO:0000313|EMBL:KRY51893.1};
GN ORFNames=T03_13507 {ECO:0000313|EMBL:KRY51893.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY51893.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY51893.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY51893.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the TFIIB family.
CC {ECO:0000256|ARBA:ARBA00010857}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRY51893.1}.
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DR EMBL; JYDI01000115; KRY51893.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1CRF6; -.
DR STRING; 45882.A0A0V1CRF6; -.
DR Proteomes; UP000054653; 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; 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 Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00469};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
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 1..31
FT /note="TFIIB-type"
FT /evidence="ECO:0000259|PROSITE:PS51134"
FT REGION 333..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 605 AA; 68210 MW; 5A321FEF6C6447CD CRC64;
MSTCPECGGR ELVEDSTMGN NVCGNCGHVI SENTIVSEVE FYETAAGRSV LLGQFIHKDG
SSISLTGMKN MNNLSSTELT YIKVRKHMEN VASQLQLSQA VTEAGFRFYK IAHGRSLTRG
RKSSHVIPSL LYISCRLNAV PQMLIDFSDV AEVNVFTLGR TFSFLAREMH LKLPPTDPCI
YVLRFAQKLR FGDKENQVIH LALRLIQRMK NDWMTYGRRP AGLCGAALII AARYYGFNRT
IENVVRVVHI GAGVLRKRLD EFCLTPSASF TLDEFCKFEI LEQCDPPSFT RNMEKEEMKK
LLEEKLKPFD EELRETEKKV QLALKQKVRS RYGASSWSSD DEQQTAVKDS VTNEVASIDY
PEESPTVGRL SEEEAAEASL MSLPSWSDTI PSSSSEMTSM EDEAPVDSTL EPQQTDASEL
NTLDDLDDDE LDGYLLTPEE AALKTKLWIR VNGEFMEEYE KRKLLKEQEK EEGSKSRRNC
RKRGEEGIAA TPGEAIKRMV FEKRLSKKIN YEVLMEEDNF EDVSSPVQSA AETAPCAFAG
DQLEEKLQKV EETTTPVSDI VEKVKQAEEA EEVVDSSDSE NVQKRPSRIK LKPKFATVDV
KRRIG
//
