GenomeNet

Database: UniProt
Entry: A0RX88_CENSY
LinkDB: A0RX88_CENSY
Original site: A0RX88_CENSY 
ID   A0RX88_CENSY            Unreviewed;       328 AA.
AC   A0RX88;
DT   09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2007, sequence version 1.
DT   25-OCT-2017, entry version 62.
DE   RecName: Full=Transcription initiation factor IIB {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   OrderedLocusNames=CENSYa_1332 {ECO:0000313|EMBL:ABK77955.1};
OS   Cenarchaeum symbiosum (strain A).
OC   Archaea; Thaumarchaeota; Cenarchaeales; Cenarchaeaceae; Cenarchaeum.
OX   NCBI_TaxID=414004 {ECO:0000313|EMBL:ABK77955.1, ECO:0000313|Proteomes:UP000000758};
RN   [1] {ECO:0000313|EMBL:ABK77955.1, ECO:0000313|Proteomes:UP000000758}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A {ECO:0000313|Proteomes:UP000000758};
RX   PubMed=17114289; DOI=10.1073/pnas.0608549103;
RA   Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y.,
RA   Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.;
RT   "Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum
RT   symbiosum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006).
CC   -!- FUNCTION: Stabilizes TBP binding to an archaeal box-A promoter.
CC       Also responsible for recruiting RNA polymerase II to the pre-
CC       initiation complex (DNA-TBP-TFIIB). {ECO:0000256|HAMAP-
CC       Rule:MF_00383}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00383};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00383};
CC   -!- SIMILARITY: Belongs to the TFIIB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00383}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; DP000238; ABK77955.1; -; Genomic_DNA.
DR   ProteinModelPortal; A0RX88; -.
DR   EnsemblBacteria; ABK77955; ABK77955; CENSYa_1332.
DR   KEGG; csy:CENSYa_1332; -.
DR   PATRIC; fig|414004.10.peg.1217; -.
DR   HOGENOM; HOG000108633; -.
DR   KO; K03124; -.
DR   OMA; REVACVI; -.
DR   Proteomes; UP000000758; Chromosome.
DR   GO; GO:0017025; F:TBP-class protein binding; IEA:InterPro.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:UniProtKB-UniRule.
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:DNA-templated transcriptional preinitiation complex assembly; IEA:InterPro.
DR   CDD; cd00043; CYCLIN; 2.
DR   Gene3D; 1.10.472.10; -; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000758};
KW   Initiation factor {ECO:0000313|EMBL:ABK77955.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00383, ECO:0000256|PROSITE-
KW   ProRule:PRU00469};
KW   Protein biosynthesis {ECO:0000313|EMBL:ABK77955.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000758};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_00383};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_00383};
KW   Transcription regulation {ECO:0000256|HAMAP-Rule:MF_00383};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00383, ECO:0000256|PROSITE-
KW   ProRule:PRU00469};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00469}.
FT   DOMAIN       34     65       TFIIB-type. {ECO:0000259|PROSITE:
FT                                PS51134}.
FT   REPEAT      150    233       1. {ECO:0000256|HAMAP-Rule:MF_00383}.
FT   REPEAT      244    325       2. {ECO:0000256|HAMAP-Rule:MF_00383}.
FT   ZN_FING      34     65       TFIIB-type. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00469}.
FT   COILED      138    165       {ECO:0000256|SAM:Coils}.
FT   METAL        38     38       Zinc. {ECO:0000256|HAMAP-Rule:MF_00383}.
FT   METAL        41     41       Zinc. {ECO:0000256|HAMAP-Rule:MF_00383}.
FT   METAL        57     57       Zinc. {ECO:0000256|HAMAP-Rule:MF_00383}.
FT   METAL        60     60       Zinc. {ECO:0000256|HAMAP-Rule:MF_00383}.
SQ   SEQUENCE   328 AA;  35922 MW;  9693D240AF35E7B0 CRC64;
     MVSSTYPQIT LRCLVKRINA QGAHTKHMER HAPPAHKCPS CGKQKIVTDE NQGELFCATC
     GFVITDKLED MGAEWRSFSG DETSRSRSGA GTSLAMHDMG LSTVIGSANK DTTGKPLSAS
     MRTSIERLRT WDSRTQAHSS ADRNLRQALN EMDKMKDKLA LADAVIEKAA YIYRKAMEKK
     LVRGRSIHGL VAACLYAACR NTETPRTLDD IAKGINIRRK DVARCYRLIF RELELKMPVV
     DPVKGVSRIA SIAELNERTK RRAITILDQA KKLGMVAGKD PMGIAAAALY LACIGSGEAK
     SQKDISLASG VTEVTIRNRC AGLRKIVG
//
DBGET integrated database retrieval system