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Database: UniProt
Entry: G0LGD6_HALWC
LinkDB: G0LGD6_HALWC
Original site: G0LGD6_HALWC 
ID   G0LGD6_HALWC            Unreviewed;       366 AA.
AC   G0LGD6;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 75.
DE   RecName: Full=Transcription initiation factor IIB {ECO:0000256|ARBA:ARBA00013932, ECO:0000256|HAMAP-Rule:MF_00383};
DE            Short=TFIIB {ECO:0000256|HAMAP-Rule:MF_00383};
GN   Name=tfbA1 {ECO:0000313|EMBL:CCC39156.1};
GN   Synonyms=tfb {ECO:0000256|HAMAP-Rule:MF_00383};
GN   OrderedLocusNames=Hqrw_1188 {ECO:0000313|EMBL:CCC39156.1};
OS   Haloquadratum walsbyi (strain DSM 16854 / JCM 12705 / C23).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloquadratum.
OX   NCBI_TaxID=768065 {ECO:0000313|EMBL:CCC39156.1, ECO:0000313|Proteomes:UP000007954};
RN   [1] {ECO:0000313|EMBL:CCC39156.1, ECO:0000313|Proteomes:UP000007954}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16854 / JCM 12705 / C23
RC   {ECO:0000313|Proteomes:UP000007954};
RX   PubMed=21701686; DOI=10.1371/journal.pone.0020968;
RA   Dyall-Smith M., Pfeiffer F., Klee K., Palm P., Gross K., Schuster S.C.,
RA   Rampp M., Oesterhelt D.;
RT   "Haloquadratum walsbyi: limited diversity in a global pond.";
RL   PLoS ONE 6:E20968-E20968(2011).
CC   -!- FUNCTION: Stabilizes TBP binding to an archaeal box-A promoter. Also
CC       responsible for recruiting RNA polymerase II to the pre-initiation
CC       complex (DNA-TBP-TFIIB). {ECO:0000256|HAMAP-Rule:MF_00383}.
CC   -!- SIMILARITY: Belongs to the TFIIB family.
CC       {ECO:0000256|ARBA:ARBA00010857, ECO:0000256|HAMAP-Rule:MF_00383}.
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DR   EMBL; FR746099; CCC39156.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0LGD6; -.
DR   KEGG; hwc:Hqrw_1188; -.
DR   HOGENOM; CLU_043736_0_0_2; -.
DR   OMA; RMWQRRM; -.
DR   Proteomes; UP000007954; Chromosome.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0017025; F:TBP-class protein binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070897; P:transcription preinitiation complex assembly; IEA:InterPro.
DR   CDD; cd20549; CYCLIN_TFIIB_archaea_like_rpt1; 1.
DR   Gene3D; 1.10.472.170; -; 1.
DR   Gene3D; 1.10.472.10; Cyclin-like; 1.
DR   HAMAP; MF_00383; TF2B_arch; 1.
DR   InterPro; IPR013763; Cyclin-like_dom.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR000812; TFIIB.
DR   InterPro; IPR023484; TFIIB_arc.
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; 1.
DR   PROSITE; PS51134; ZF_TFIIB; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00383};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_00383};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_00383};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW   Rule:MF_00383}; Zinc {ECO:0000256|HAMAP-Rule:MF_00383};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00469}.
FT   DOMAIN          67..97
FT                   /note="TFIIB-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51134"
FT   REPEAT          183..266
FT                   /note="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   REPEAT          277..358
FT                   /note="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   REGION          1..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          112..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         71
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   BINDING         74
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   BINDING         89
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   BINDING         92
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
SQ   SEQUENCE   366 AA;  40507 MW;  7F9206018DAB267B CRC64;
     MSEKTTHTCE NARTRVESNN ESEVTTNSAH DRIRTDGGTV GQRWVRPGEK ESEEESVSES
     EEETTSESLV CPECSGNVVA DDEHGETICD DCGLVITEDS VDRGPEWRAF DAKEKDQKSR
     VGAPTTNTMH DKGLSTNIDW RDRDAYGNSL SSNQRQKMQR LRKWNERFRT RDSKERNLKQ
     ALGEVDRMAS ALGLPENVRE TASVIYRRAL DEDLLPGRSI EGVSTSCVYA AARMAGVPRS
     LDEIAEVSRV PKSEVARTYR YIARELSLEV KPADPEQYVP RFASELGLSD ESTLRARQLL
     QNAKEKGVHS GKSPVGLAAA AVYAAALLTN EKTTQAAVSE VADISEVTIR NRYHELLEAK
     DAVGAT
//
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