TAF1B_MACFA
ID TAF1B_MACFA Reviewed; 588 AA.
AC Q4R657;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=TATA box-binding protein-associated factor RNA polymerase I subunit B;
DE AltName: Full=TATA box-binding protein-associated factor 1B;
DE Short=TBP-associated factor 1B;
DE AltName: Full=Transcription initiation factor SL1/TIF-IB subunit B;
GN Name=TAF1B; ORFNames=QtsA-19105;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of RNA polymerase I core factor complex that acts
CC as a GTF2B/TFIIB-like factor and plays a key role in multiple steps
CC during transcription initiation such as pre-initiation complex (PIC)
CC assembly and postpolymerase recruitment events in polymerase I (Pol I)
CC transcription. Binds rDNA promoters and plays a role in Pol I
CC recruitment as a component of the SL1/TIF-IB complex and, possibly,
CC directly through its interaction with RRN3 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with FLNA (via N-terminus) (By similarity).
CC Component of the transcription factor SL1/TIF-IB complex, notably
CC composed of TBP and at least TAF1A, TAF1B, TAF1C and TAF1D. In the
CC complex interacts directly with TBP, TAF1A and TAF1C. Interaction of
CC the SL1/TIF-IB subunits with TBP excludes interaction of TBP with the
CC transcription factor IID (TFIID) subunits. Interacts with TBP and RRN3
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- DOMAIN: Although it shares weak sequence similarity with GTF2B/TFIIB,
CC displays a similar subdomain organization as GTF2B/TFIIB, with a N-
CC terminal zinc finger, a connecting region (composed of B-reader and B-
CC linker regions), followed by 2 cyclin folds. The RRN7-type zinc finger
CC plays an essential postrecruitment role in Pol I transcription at a
CC step preceding synthesis of the first 40 nucleotides (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RRN7/TAF1B family. {ECO:0000305}.
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DR EMBL; AB169333; BAE01418.1; -; mRNA.
DR RefSeq; NP_001272301.1; NM_001285372.1.
DR AlphaFoldDB; Q4R657; -.
DR STRING; 9541.XP_005576638.1; -.
DR GeneID; 101865468; -.
DR CTD; 9014; -.
DR eggNOG; ENOG502QVGU; Eukaryota.
DR OrthoDB; 329399at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0070860; C:RNA polymerase I core factor complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001164; F:RNA polymerase I core promoter sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0001188; P:RNA polymerase I preinitiation complex assembly; ISS:UniProtKB.
DR InterPro; IPR033599; TAF1B/Rrn7.
DR InterPro; IPR021752; TF_Rrn7_Zf.
DR PANTHER; PTHR31576; PTHR31576; 1.
DR Pfam; PF11781; zf-RRN7; 1.
PE 2: Evidence at transcript level;
KW Acetylation; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..588
FT /note="TATA box-binding protein-associated factor RNA
FT polymerase I subunit B"
FT /id="PRO_0000261393"
FT ZN_FING 4..39
FT /note="RRN7-type"
FT REGION 40..68
FT /note="B-reader"
FT /evidence="ECO:0000250"
FT REGION 69..73
FT /note="B-linker"
FT /evidence="ECO:0000250"
FT REGION 74..261
FT /note="N-terminal cyclin fold"
FT /evidence="ECO:0000250"
FT REGION 262..372
FT /note="C-terminal cyclin fold"
FT /evidence="ECO:0000250"
FT BINDING 13
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q53T94"
FT MOD_RES 440
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q53T94"
SQ SEQUENCE 588 AA; 68548 MW; 1EAE031FB0CFCDDF CRC64;
MDLEEAEEFK ERCSQCAAVS WGLTDEGKYY CTSCHNVTER SQEVINTDLI PNTQIKALNR
GLKKKNNSEK GWDWYVCEGF QNILCQQAEA LKNLGIGPEL KNDVLHNFWK RYLQKSKQAY
CKNPVYTTGR KPTVLEDNRS HSDWASEPEL LSDVSCPPFL ESGAESQSDI HTRKPFPISK
ASQSETSVCS GSLGGVEYSQ RKEKGIVKMT VPQTLAFCYL SLLWQREAIT LSDLLRFVEE
DHIPYINAFQ HFPEQMKLYG RDRGIFGIES WPDYEDIYKK TIEVGTFLDL PRFPDITEDC
YLHPNILCMK YLMEVNLPDE MHNLTCHVVK MTGMGEVDFL TFDPIAKMAK TVKYDVQAVA
IIVVVLKLLF LLDDNLEWSL SNLAEKHNEK NKKDKPWFDF RKWYQIMKKA FDEKKQKWEE
ARAKYLWKSE KPLYYSFVDK PVAYKKREMV VNLQKQFSTL VDSTATAGKK SPSSFQFNWT
EEDTDRTCFH GHSLQGVLKE KGQSLLTKNS LYWLSTQKFC RCYCTHVTTY EESNYSLSYQ
FILNLFSFLL RIKTSLLHEE VSLVEKKLFE KKYSVTKKKS RSKKARRH
