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Database: UniProt
Entry: D9Q0X1_ACIS3
LinkDB: D9Q0X1_ACIS3
Original site: D9Q0X1_ACIS3 
ID   D9Q0X1_ACIS3            Unreviewed;       303 AA.
AC   D9Q0X1;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Transcription initiation factor IIB {ECO:0000256|ARBA:ARBA00013932};
GN   OrderedLocusNames=ASAC_0552 {ECO:0000313|EMBL:ADL18959.1};
OS   Acidilobus saccharovorans (strain DSM 16705 / JCM 18335 / VKM B-2471 /
OS   345-15).
OC   Archaea; Thermoproteota; Thermoprotei; Acidilobales; Acidilobaceae;
OC   Acidilobus.
OX   NCBI_TaxID=666510 {ECO:0000313|EMBL:ADL18959.1, ECO:0000313|Proteomes:UP000000346};
RN   [1] {ECO:0000313|EMBL:ADL18959.1, ECO:0000313|Proteomes:UP000000346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16705 / JCM 18335 / VKM B-2471 / 345-15
RC   {ECO:0000313|Proteomes:UP000000346};
RX   PubMed=20581186; DOI=10.1128/AEM.00599-10;
RA   Mardanov A.V., Svetlitchnyi V.A., Beletsky A.V., Prokofeva M.I.,
RA   Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT   "The genome sequence of the crenarchaeon Acidilobus saccharovorans supports
RT   a new order, Acidilobales, and suggests an important ecological role in
RT   terrestrial acidic hot springs.";
RL   Appl. Environ. Microbiol. 76:5652-5657(2010).
CC   -!- SIMILARITY: Belongs to the TFIIB family.
CC       {ECO:0000256|ARBA:ARBA00010857}.
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DR   EMBL; CP001742; ADL18959.1; -; Genomic_DNA.
DR   AlphaFoldDB; D9Q0X1; -.
DR   STRING; 666510.ASAC_0552; -.
DR   KEGG; asc:ASAC_0552; -.
DR   eggNOG; arCOG01981; Archaea.
DR   HOGENOM; CLU_917028_0_0_2; -.
DR   InParanoid; D9Q0X1; -.
DR   Proteomes; UP000000346; Chromosome.
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:0070897; P:transcription preinitiation complex assembly; IEA:InterPro.
DR   CDD; cd00350; rubredoxin_like; 1.
DR   Gene3D; 1.10.472.170; -; 1.
DR   Gene3D; 1.10.472.10; Cyclin-like; 1.
DR   InterPro; IPR013763; Cyclin-like_dom.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR000812; TFIIB.
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; 1.
DR   PRINTS; PR00685; TIFACTORIIB.
DR   SMART; SM00385; CYCLIN; 1.
DR   SUPFAM; SSF47954; Cyclin-like; 1.
DR   SUPFAM; SSF57783; Zinc beta-ribbon; 1.
PE   3: Inferred from homology;
KW   Initiation factor {ECO:0000313|EMBL:ADL18959.1};
KW   Protein biosynthesis {ECO:0000313|EMBL:ADL18959.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000346};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          212..295
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
SQ   SEQUENCE   303 AA;  33108 MW;  5ABCCB1FF39BECFC CRC64;
     MCPRCGSKLV DDNGVLVCPN CGYIYDGNEL SDGPEWRSLS NGNVKGVERA SYSNDPLMHD
     LGIGNLRMSP ARSRSPLMRV RNLRMRIGSS HPLLKGEAPL VNMFSIAKKA ASAFELSDSA
     KDALGQVLHA YAERAKKPIG RDVNKVVAAA LEKVVEVYNL SISKGEIESF FEIDDNDLWD
     GLKKLNDVGA LDMLKVVVAS EGQGRVLERS FTYINRIASS LSLPQQVVQD SLNFIRKSLG
     VAGKTPYGKK PEALAAAAVY LVARLNGYEI SQSDVAKVVG IKESTVRKLY RFLMDNMVVV
     VDV
//
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