TAF1B_CAEEL
ID TAF1B_CAEEL Reviewed; 865 AA.
AC O01914;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 3.
DT 03-AUG-2022, entry version 118.
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;
GN ORFNames=F23H11.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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 (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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RRN7/TAF1B family. {ECO:0000305}.
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DR EMBL; FO081212; CCD69943.1; -; Genomic_DNA.
DR PIR; T34064; T34064.
DR RefSeq; NP_497287.2; NM_064886.4.
DR AlphaFoldDB; O01914; -.
DR BioGRID; 40520; 1.
DR IntAct; O01914; 3.
DR MINT; O01914; -.
DR STRING; 6239.F23H11.2; -.
DR EPD; O01914; -.
DR PaxDb; O01914; -.
DR EnsemblMetazoa; F23H11.2.1; F23H11.2.1; WBGene00017758.
DR GeneID; 175251; -.
DR KEGG; cel:CELE_F23H11.2; -.
DR UCSC; F23H11.2; c. elegans.
DR CTD; 175251; -.
DR WormBase; F23H11.2; CE34542; WBGene00017758; -.
DR eggNOG; ENOG502SDRV; Eukaryota.
DR HOGENOM; CLU_015505_0_0_1; -.
DR InParanoid; O01914; -.
DR OMA; VAFCHSE; -.
DR OrthoDB; 562034at2759; -.
DR Reactome; R-CEL-73772; RNA Polymerase I Promoter Escape.
DR PRO; PR:O01914; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00017758; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0070860; C:RNA polymerase I core factor complex; IBA:GO_Central.
DR GO; GO:0005668; C:RNA polymerase transcription factor SL1 complex; IBA:GO_Central.
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:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IBA:GO_Central.
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 3: Inferred from homology;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..865
FT /note="TATA box-binding protein-associated factor RNA
FT polymerase I subunit B"
FT /id="PRO_0000416875"
FT ZN_FING 1..33
FT /note="RRN7-type"
FT REGION 35..99
FT /note="B-reader"
FT /evidence="ECO:0000250"
FT REGION 100..111
FT /note="B-linker"
FT /evidence="ECO:0000250"
FT REGION 112..348
FT /note="N-terminal cyclin fold"
FT /evidence="ECO:0000250"
FT REGION 233..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..496
FT /note="C-terminal cyclin fold"
FT /evidence="ECO:0000250"
FT COMPBIAS 243..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 865 AA; 99740 MW; E76410E76E6C3AD8 CRC64;
MHSAKNEKCN ACGGYRFSVN DGFKYCDRCG ALFENFEELE EEEGGLQQTV GQGKVKVRKN
DDQKRVRNNA APVNLPKAQV MREALEKRSD FLQQQAIKGE ELELPHDATP DYLYRLALRL
FSFTQILAKS GHILVHELNF ESRVQENILA TFQKYLAHCQ VAFCHSEQCG NDEHLRFVAV
MENLRYEQEE REEKQRKRMA KRGKGVNALS KSAAAWTLLT QGNITEHLDI ASDEDGDQDA
QGGQQLDDLT LETTQNPDES IRVNDTTMGF VRKVTTALSK EALRRASQLI LNLEMLVAIL
HSALMSSGYQ TILTSDVVRW IREDRFRISR RSIRLIRQSQ PERMKQGEVV KPTIVDYAEP
FLRFPLYEIM RTCTIFHQSL KLASSMAPQS FESMSARLVD NLNLPSDILS RMLILESIIP
CDVSPQLLKQ VDVDMGYNCG QLAAMSPNVY YSGFLTSFGR KERGTQDADF CDEVLLSPDA
KLIAYLLLTL RLTFQLDNAQ CALQDDQYFD VDSWIHQLEM RIKCWQGHNM SLVMRSSSHV
PEMVVDPPFG TNYLFHQEKG APQVSCRRRQ AGFQKCIPTE MSFNSTSTLP TVFDVRHMGL
LTERCQMEAL ISPVKFQRTV LGNEIERDPL TFENVDRQSK NTFFKHFSAF KTTESCDTFE
EYFPCAKNYL LFKRPDWIQN CTARQTHFNP VTGPIRFYLS NQSCDDLLGT AATSFSRRFQ
FLLDALSLII GEDKKAVYAA FVMLEMHLTS SERIQSIRDD LLTSSPITLK CQKFRNSTHH
IPRKYGVISE VPIDRIENLR YFRLSRQFFE HEEMPTTINM ELIDYRNQEI RDSVTETEVQ
RAQNRIMKLC YEFEQFFGIL AVKFW
