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TAF1B_XENLA
ID   TAF1B_XENLA             Reviewed;         582 AA.
AC   Q32N22; Q7ZYP3;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=TATA box-binding protein-associated factor RNA polymerase I subunit B;
DE   AltName: Full=RNA polymerase I-specific TBP-associated factor 63 kDa;
DE            Short=TAFI63;
DE   AltName: Full=TATA box-binding protein-associated factor 1B;
DE            Short=TBP-associated factor 1B;
GN   Name=taf1b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo, and Lung;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-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 (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; BC042352; AAH42352.1; -; mRNA.
DR   EMBL; BC108876; AAI08877.1; -; mRNA.
DR   RefSeq; NP_001079454.1; NM_001085985.1.
DR   AlphaFoldDB; Q32N22; -.
DR   DNASU; 379141; -.
DR   GeneID; 379141; -.
DR   KEGG; xla:379141; -.
DR   CTD; 379141; -.
DR   Xenbase; XB-GENE-992279; taf1b.L.
DR   OMA; PRSFVWL; -.
DR   OrthoDB; 329399at2759; -.
DR   Proteomes; UP000186698; Chromosome 5L.
DR   Bgee; 379141; Expressed in blastula and 19 other tissues.
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   DNA-binding; Metal-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..582
FT                   /note="TATA box-binding protein-associated factor RNA
FT                   polymerase I subunit B"
FT                   /id="PRO_0000416872"
FT   ZN_FING         4..39
FT                   /note="RRN7-type"
FT   REGION          40..69
FT                   /note="B-reader"
FT                   /evidence="ECO:0000250"
FT   REGION          70..74
FT                   /note="B-linker"
FT                   /evidence="ECO:0000250"
FT   REGION          75..256
FT                   /note="N-terminal cyclin fold"
FT                   /evidence="ECO:0000250"
FT   REGION          257..367
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   CONFLICT        377
FT                   /note="T -> M (in Ref. 1; AAH42352)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   582 AA;  68123 MW;  72D410EE9B6F1291 CRC64;
     MEAEDGRGYN VPCPQCSEIN WAISDEGRYY CMSCHTIIEK TREVEDSEVF VNLGKIQYIS
     RGLRKKRKQE KGWEWYVCEG FQFILIKQAE SLQALGVAPQ IKDEIICTFW RRYLQKTNQA
     YVKRPVYRNT LNLRESDSSA TELDSETDEF SDGITTDASD RLSVATEDIA SGSESAVSIQ
     SGSVDGVSHT KMSKNWKPWN YVKMSMPMTL AFCYLALLWL RASITLSDLL RFVFEKRIPY
     FNAHQYLPEE IKLYGQDVRI FRMQSFPVYN DILNKAYELG HYLDLPRFPE IIKNCYLHPN
     VLCMKYLMEA NLPDELHHWT CQVAEKTGTD DLHLLTFDPA CKKARHIRYD VQAVALIIVV
     LKLLFALDDN TEWQLSTFAE RMNQRDKEKP IFEFQSWYQT VRSCYEKAQQ ALEEEYGRFT
     WKSDCLLYYS HTSKAVLQKR KQMSENLHRQ FSKLAGAAPD TGKQGPSSFL FKWDEQNTDR
     ICFHGHSLEA ILQQGDKPAT AINTHYWLNS LKKCKSRICQ HSELYEQSNF PRSYHFIVSL
     FAFLLRVEHC VVHHEVCLIE ETFFQEFQGK KNKQKQKPRK QN
 
 
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