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Database: UniProt
Entry: M0CKD8_9EURY
LinkDB: M0CKD8_9EURY
Original site: M0CKD8_9EURY 
ID   M0CKD8_9EURY            Unreviewed;       329 AA.
AC   M0CKD8;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 47.
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=C475_17593 {ECO:0000313|EMBL:ELZ22349.1};
OS   Halosimplex carlsbadense 2-9-1.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Halosimplex.
OX   NCBI_TaxID=797114 {ECO:0000313|EMBL:ELZ22349.1, ECO:0000313|Proteomes:UP000011626};
RN   [1] {ECO:0000313|EMBL:ELZ22349.1, ECO:0000313|Proteomes:UP000011626}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2-9-1 {ECO:0000313|EMBL:ELZ22349.1,
RC   ECO:0000313|Proteomes:UP000011626};
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:ELZ22349.1}.
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DR   EMBL; AOIU01000036; ELZ22349.1; -; Genomic_DNA.
DR   RefSeq; WP_006885185.1; NZ_AOIU01000036.1.
DR   AlphaFoldDB; M0CKD8; -.
DR   STRING; 797114.C475_17593; -.
DR   PATRIC; fig|797114.5.peg.3585; -.
DR   eggNOG; arCOG01981; Archaea.
DR   OrthoDB; 7429at2157; -.
DR   Proteomes; UP000011626; 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: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   Reference proteome {ECO:0000313|Proteomes:UP000011626};
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          32..62
FT                   /note="TFIIB-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51134"
FT   REPEAT          148..231
FT                   /note="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   REPEAT          242..323
FT                   /note="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         36
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   BINDING         39
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"
FT   BINDING         57
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
SQ   SEQUENCE   329 AA;  36531 MW;  371A770D34E459E8 CRC64;
     MTSTNQRVTG RHVQPIERTD EETESGSESE RERDECPECG AAGITDEKRG ETVCQECGVV
     LEEDVVDRGP EWRSFDARDK AQKSRVGSPT TEMLHDKGLS SVIDWQNKDA NGQTLSAKKR
     EQMSRLRTWD ERFRSQSAQD RNLKQALGEI DRMASALGIP KDARETASVI YRRALDEELI
     PGRSIEAMAT GSLYAGARQA GVPRTLDELE TVSRVDRKEF ARAYRYIARE LELAMEPTDP
     AQYVPRLVSD LDLPEETKQR AVELLEAGKR EAVHSGKNPV GLAAAAIYAA GRLTNVDVTQ
     HEVADAADVS AVTIRDRYTE LLDAADRVA
//
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