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RRN7_SCHPO
ID   RRN7_SCHPO              Reviewed;         537 AA.
AC   Q9UST5;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=RNA polymerase I-specific transcription initiation factor rrn7;
GN   Name=rrn7; ORFNames=SPBC336.09c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   IDENTIFICATION, AND FUNCTION.
RX   PubMed=12095692; DOI=10.1016/s0378-1119(02)00597-8;
RA   Boukhgalter B., Liu M., Guo A., Tripp M., Tran K., Huynh C., Pape L.;
RT   "Characterization of a fission yeast subunit of an RNA polymerase I
RT   essential transcription initiation factor, SpRrn7h/TAF(I)68, that bridges
RT   yeast and mammals: association with SpRrn11h and the core ribosomal RNA
RT   gene promoter.";
RL   Gene 291:187-201(2002).
RN   [3]
RP   INTERACTION WITH ACR1.
RX   PubMed=18362178; DOI=10.1083/jcb.200708170;
RA   Nakazawa N., Nakamura T., Kokubu A., Ebe M., Nagao K., Yanagida M.;
RT   "Dissection of the essential steps for condensin accumulation at
RT   kinetochores and rDNAs during fission yeast mitosis.";
RL   J. Cell Biol. 180:1115-1131(2008).
RN   [4]
RP   DNA-BINDING.
RX   PubMed=21673110; DOI=10.1074/jbc.m111.224337;
RA   Rojas D.A., Moreira-Ramos S., Zock-Emmenthal S., Urbina F.,
RA   Contreras-Levicoy J., Kaufer N.F., Maldonado E.;
RT   "Rrn7 protein, an RNA polymerase I transcription factor, is required for
RT   RNA polymerase II-dependent transcription directed by core promoters with a
RT   HomolD box sequence.";
RL   J. Biol. Chem. 286:26480-26486(2011).
CC   -!- FUNCTION: Component of RNA polymerase I core factor complex (CF) that
CC       acts as a sua7/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 HomolD box in rDNA promoters and plays a role in
CC       Pol I recruitment. {ECO:0000269|PubMed:12095692}.
CC   -!- SUBUNIT: Component of the core factor (CF) complex. Interacts with
CC       acr1. {ECO:0000269|PubMed:18362178}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC   -!- DOMAIN: Although it shares weak sequence similarity with sua7/TFIIB,
CC       displays a similar subdomain organization as sua7/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; CU329671; CAB58161.1; -; Genomic_DNA.
DR   PIR; T40247; T40247.
DR   RefSeq; NP_596129.1; NM_001022047.2.
DR   AlphaFoldDB; Q9UST5; -.
DR   BioGRID; 276768; 8.
DR   STRING; 4896.SPBC336.09c.1; -.
DR   iPTMnet; Q9UST5; -.
DR   MaxQB; Q9UST5; -.
DR   PaxDb; Q9UST5; -.
DR   PRIDE; Q9UST5; -.
DR   EnsemblFungi; SPBC336.09c.1; SPBC336.09c.1:pep; SPBC336.09c.
DR   GeneID; 2540236; -.
DR   KEGG; spo:SPBC336.09c; -.
DR   PomBase; SPBC336.09c; rrn7.
DR   VEuPathDB; FungiDB:SPBC336.09c; -.
DR   eggNOG; ENOG502RYCI; Eukaryota.
DR   HOGENOM; CLU_016553_2_1_1; -.
DR   InParanoid; Q9UST5; -.
DR   OMA; IACSEGH; -.
DR   PhylomeDB; Q9UST5; -.
DR   Reactome; R-SPO-73772; RNA Polymerase I Promoter Escape.
DR   PRO; PR:Q9UST5; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0070860; C:RNA polymerase I core factor complex; ISO:PomBase.
DR   GO; GO:0000120; C:RNA polymerase I transcription regulator complex; IDA:PomBase.
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; IDA:PomBase.
DR   GO; GO:0001181; F:RNA polymerase I general transcription initiation factor activity; IC:PomBase.
DR   GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IBA:GO_Central.
DR   GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; IDA:PomBase.
DR   InterPro; IPR033599; TAF1B/Rrn7.
DR   InterPro; IPR021752; TF_Rrn7_Zf.
DR   PANTHER; PTHR31576; PTHR31576; 1.
DR   Pfam; PF11781; zf-RRN7; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Metal-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..537
FT                   /note="RNA polymerase I-specific transcription initiation
FT                   factor rrn7"
FT                   /id="PRO_0000097449"
FT   ZN_FING         4..37
FT                   /note="RRN7-type"
FT   REGION          38..64
FT                   /note="B-reader"
FT                   /evidence="ECO:0000250"
FT   REGION          65..80
FT                   /note="B-linker"
FT                   /evidence="ECO:0000250"
FT   REGION          81..232
FT                   /note="N-terminal cyclin fold"
FT                   /evidence="ECO:0000250"
FT   REGION          142..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          233..349
FT                   /note="C-terminal cyclin fold"
FT                   /evidence="ECO:0000250"
FT   BINDING         11
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         30
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"
SQ   SEQUENCE   537 AA;  61911 MW;  5EF44F491BAA5090 CRC64;
     MEGNWFEGPP CSVRNCKSTW YFKNAGQTFC RRGHAQHGIE IAQDDEPGAG TFYQTRKRKV
     VRNHLDTGDE DEIVYGTAGR SLYLQAFQII LQLQCQALTT KLGFDQRIEG MIRDLWALYL
     SLSYESFTSS FLSLNQNSTQ SESSDSDFDL IDPESQPGAD PSSRKTKETS QSHSISYPRL
     LYSSAFIYVA CLLLRLPLTI HKLEVLIRKN IIPYYRAYKQ IPLKIFKRLQ KNYVRMLIPF
     HYPTYQRIQS AVLTLVDVLV SKYELKVPPP NEPLILFELI NSFFFPLEIF IPASRLLNLV
     HSQISLQGTS SDNYQSKIRS AQSIHEKLSD AEVMLLATIL VAANVCYGFD DAQTRNSKYK
     DSMFTVKTNW NMWLSQVQKI NEKEKDKFYE IDEQSILTLN NSEMDKYFQW YEKEFVEENN
     PNNIPEGILN VFPILSKDSH LQENQPTDIL TDESVIAEDV KLEQVFKPVG IKESDKMDFS
     RRKDAYISML PFSPNTENTA HRVTIMVAKL YNIKLDSLIA AIRYVESCLK TGIHNQD
 
 
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