ID M0J6R2_9EURY Unreviewed; 317 AA.
AC M0J6R2;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=tfb {ECO:0000256|HAMAP-Rule:MF_00383};
GN ORFNames=C438_13674 {ECO:0000313|EMBL:EMA03679.1};
OS Haloferax denitrificans ATCC 35960.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=662478 {ECO:0000313|EMBL:EMA03679.1, ECO:0000313|Proteomes:UP000011553};
RN [1] {ECO:0000313|EMBL:EMA03679.1, ECO:0000313|Proteomes:UP000011553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35960 {ECO:0000313|EMBL:EMA03679.1,
RC ECO:0000313|Proteomes:UP000011553};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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}.
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:EMA03679.1}.
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DR EMBL; AOLP01000014; EMA03679.1; -; Genomic_DNA.
DR RefSeq; WP_004043457.1; NZ_AOLP01000014.1.
DR AlphaFoldDB; M0J6R2; -.
DR GeneID; 8924833; -.
DR PATRIC; fig|662478.6.peg.2682; -.
DR Proteomes; UP000011553; Unassembled WGS sequence.
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:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
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 CDD; cd20550; CYCLIN_TFIIB_archaea_like_rpt2; 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; 2.
DR PROSITE; PS51134; ZF_TFIIB; 1.
PE 3: Inferred from homology;
KW Initiation factor {ECO:0000313|EMBL:EMA03679.1};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00383};
KW Protein biosynthesis {ECO:0000313|EMBL:EMA03679.1};
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 20..51
FT /note="TFIIB-type"
FT /evidence="ECO:0000259|PROSITE:PS51134"
FT REPEAT 137..220
FT /note="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT REPEAT 231..312
FT /note="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT REGION 1..23
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 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
SQ SEQUENCE 317 AA; 35732 MW; 01CB28E9E9D6280D CRC64;
MERPSRQRQR EEEATAQEDE QVNCPECGSD QIVTDADQGE LVCDDCGLVL DERQIDRGPE
WRAFNHSERQ SKSRVGAPIT ETMHDRGLTT TIDWKDKDAY GRSLSSEKRS QMHRLRKWQE
RIRTKDAGER NLQFALSEID RMASALGVPR SVREVASVIY RRALNEDLIR GRSIEGVATS
ALYAACRQEG IPRSLDEVAE VSRVPQKEIG RTYRYISQEL GLELKPVDPK QFVPRFASAL
DLSEEVQAKA TEIIDVSAEQ GLLSGKSPTG FAAAAIYAAS LLCNEKKTQR EVADVAQVTE
VTIRNRYQEQ IEAMGFR
//
