TF2B_METMA
ID TF2B_METMA Reviewed; 337 AA.
AC P0CW15; Q977U3;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Transcription initiation factor IIB {ECO:0000255|HAMAP-Rule:MF_00383};
DE Short=TFIIB {ECO:0000255|HAMAP-Rule:MF_00383};
GN Name=tfb {ECO:0000255|HAMAP-Rule:MF_00383}; OrderedLocusNames=MM_1772;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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:0000255|HAMAP-Rule:MF_00383}.
CC -!- SIMILARITY: Belongs to the TFIIB family. {ECO:0000255|HAMAP-
CC Rule:MF_00383}.
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DR EMBL; AE008384; AAM31468.1; -; Genomic_DNA.
DR RefSeq; WP_011033712.1; NC_003901.1.
DR AlphaFoldDB; P0CW15; -.
DR SMR; P0CW15; -.
DR STRING; 192952.MM_1772; -.
DR EnsemblBacteria; AAM31468; AAM31468; MM_1772.
DR GeneID; 44088592; -.
DR GeneID; 66136747; -.
DR KEGG; mma:MM_1772; -.
DR PATRIC; fig|192952.21.peg.2048; -.
DR eggNOG; arCOG01981; Archaea.
DR HOGENOM; CLU_043736_0_1_2; -.
DR OMA; DHDQRMK; -.
DR Proteomes; UP000000595; 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; cd00043; CYCLIN; 2.
DR HAMAP; MF_00383; TF2B_arch; 1.
DR InterPro; IPR013763; Cyclin-like.
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; PTHR11618; 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; SSF47954; 2.
DR PROSITE; PS00782; TFIIB; 2.
DR PROSITE; PS51134; ZF_TFIIB; 1.
PE 3: Inferred from homology;
KW Metal-binding; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..337
FT /note="Transcription initiation factor IIB"
FT /id="PRO_0000408040"
FT REPEAT 154..237
FT /note="1"
FT REPEAT 248..329
FT /note="2"
FT ZN_FING 37..68
FT /note="TFIIB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
SQ SEQUENCE 337 AA; 38290 MW; 39C58CA8D9ACD879 CRC64;
MVEVERVRYS DTLEREKIRA MIKARKEKQK EQTVENEKAV CPECGSRNLV HDYERAELVC
GDCGLVIDAD FVDEGPEWRA FDHDQRMKRS RVGAPMTYTI HDKGLSTMID WRNRDSYGKS
ISSKNRAQLY RLRKWQRRIR VSNATERNLA FALSELDRMA SALGLPRTVR ETAAVVYRKA
VDKNLIRGRS IEGVAAAALY AACRQCSVPR TLDEIEEVSR VSRKEIGRTY RFISRELALK
LMPTSPIDYV PRFCSGLNLK GEVQSKSVEI LRQASEKELT SGRGPTGVAA AAIYIASILC
GERRTQREVA DVAGVTEVTI RNRYKELAEE LDIEIIL