ID A0A1Y3G9X1_9EURY Unreviewed; 329 AA.
AC A0A1Y3G9X1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=AMET1_0997 {ECO:0000313|EMBL:OUJ18100.1}, AMET1_1543
GN {ECO:0000313|EMBL:OUJ18050.1};
OS Methanonatronarchaeum thermophilum.
OC Archaea; Euryarchaeota; Methanonatronarchaeia; Methanonatronarchaeales;
OC Methanonatronarchaeaceae; Methanonatronarchaeum.
OX NCBI_TaxID=1927129 {ECO:0000313|EMBL:OUJ18050.1, ECO:0000313|Proteomes:UP000195137};
RN [1] {ECO:0000313|EMBL:OUJ18050.1, ECO:0000313|Proteomes:UP000195137}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMET1 {ECO:0000313|EMBL:OUJ18050.1};
RA Sorokin D.Y., Makarova K.S., Abbas B., Ferrer M., Golyshin P.N.;
RT "Discovery of methanogenic haloarchaea.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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:OUJ18050.1}.
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DR EMBL; MRZU01000006; OUJ18050.1; -; Genomic_DNA.
DR EMBL; MRZU01000004; OUJ18100.1; -; Genomic_DNA.
DR OrthoDB; 7429at2157; -.
DR Proteomes; UP000195137; 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; 1.
DR PROSITE; PS51134; ZF_TFIIB; 1.
PE 3: Inferred from homology;
KW Initiation factor {ECO:0000313|EMBL:OUJ18050.1};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00383};
KW Protein biosynthesis {ECO:0000313|EMBL:OUJ18050.1};
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 28..59
FT /note="TFIIB-type"
FT /evidence="ECO:0000259|PROSITE:PS51134"
FT REPEAT 145..228
FT /note="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT REPEAT 239..320
FT /note="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
SQ SEQUENCE 329 AA; 37024 MW; 6358A3FFD9DB5762 CRC64;
MSTEIGKTQN EIEKKVKSER DHIGEYEESD KCPECGGIKL IRDYERAELV CEKCGLVIDG
DFIDTGPDWR AFDSEERNKK MRVGAPMDIM THDKGLSTNI GTGTRDSNGN SISSNKKTKF
YRLRKWHRQS KFSDSKERDL ALALGELNRM ASQLNIPKSV SEDASMIYRK IAEKGLVKGR
SIEAMVGSVL YISCRQNKIP RTLDEISDSA RVSRKEIGRA YRYIASELGI MLQPAKPEEY
VPRFCSQLGL TNKVQFKAEE ILKQASEKEL TSGRDPTSIA AAGIYIASVK CGEKRSQKKV
ANAASTTEVT VRNRYQELCE ELNIEMNVN
//
