ID A0A0V1DCD7_TRIBR Unreviewed; 311 AA.
AC A0A0V1DCD7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 03-MAY-2023, entry version 23.
DE RecName: Full=Transcription initiation factor IIB {ECO:0000256|ARBA:ARBA00013932};
DE AltName: Full=General transcription factor TFIIB {ECO:0000256|ARBA:ARBA00031706};
GN Name=Ptchd3 {ECO:0000313|EMBL:KRY59246.1};
GN ORFNames=T03_15177 {ECO:0000313|EMBL:KRY59246.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY59246.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY59246.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY59246.1};
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 -!- 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:KRY59246.1}.
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DR EMBL; JYDI01000014; KRY59246.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1DCD7; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0017025; F:TBP-class protein binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0070897; P:transcription preinitiation complex assembly; IEA:InterPro.
DR CDD; cd20551; CYCLIN_TFIIB_rpt1; 1.
DR CDD; cd20552; CYCLIN_TFIIB_rpt2; 1.
DR Gene3D; 2.20.25.10; -; 1.
DR Gene3D; 1.10.472.10; Cyclin-like; 2.
DR InterPro; IPR013763; Cyclin-like_dom.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR000812; TFIIB.
DR InterPro; IPR023486; TFIIB_CS.
DR InterPro; IPR013150; TFIIB_cyclin.
DR InterPro; IPR013137; Znf_TFIIB.
DR PANTHER; PTHR11618:SF13; TRANSCRIPTION INITIATION FACTOR IIB; 1.
DR PANTHER; PTHR11618; TRANSCRIPTION INITIATION FACTOR IIB-RELATED; 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; PS00782; TFIIB; 2.
DR PROSITE; PS51134; ZF_TFIIB; 1.
PE 3: Inferred from homology;
KW Initiation factor {ECO:0000313|EMBL:KRY59246.1};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00469};
KW Protein biosynthesis {ECO:0000313|EMBL:KRY59246.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 44..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 311 AA; 33538 MW; B4B2D7002A7BD0EE CRC64;
MSNVSCPAHP DAELIEDHRA GDMICMECGL VVGDRIVDVS SEWRSFSSDT NSKDPSRVGS
PENNLMSGGG LATSIAGGGS DESRSLSNLQ KRQASNNQDR ALIHAFGVIR EMADRIHLTK
SIQDQANLLF KQVQETKALK GKNNDAVASA CLYIACRKDG VPRTFKEIIL SILEICAVSK
LSKKEVGRCF KLILRALETN LNLITTSDFM SRFCGNLNLP QYVQTAATHI ARAAVENDLV
SGRSPVSIAA AAIYMASQAS LEKRCAKDIG DVAGVAEVTI RQSYKLMLGS AAKLFPADFK
FTTPISELPP A
//