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RRN5_SCHPO
ID   RRN5_SCHPO              Reviewed;         556 AA.
AC   O14013; Q9USB1;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 126.
DE   RecName: Full=RNA polymerase I-specific transcription initiation factor rrn5;
GN   Name=rrn5; ORFNames=SPAC29A4.10;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 340-537, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=ATCC 38364 / 968;
RX   PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA   Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA   Hiraoka Y.;
RT   "Large-scale screening of intracellular protein localization in living
RT   fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL   Genes Cells 5:169-190(2000).
RN   [3]
RP   FUNCTION, IDENTIFICATION IN THE UAF COMPLEX, AND INTERACTION WITH RRN10.
RX   PubMed=12490702; DOI=10.1093/nar/gkf683;
RA   Liu M., Guo A., Boukhgalter B., Van Den Heuvel K., Tripp M., Pape L.;
RT   "Characterization of the fission yeast ribosomal DNA binding factor:
RT   components share homology with upstream activating factor and with SWI/SNF
RT   subunits.";
RL   Nucleic Acids Res. 30:5347-5359(2002).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=17538026; DOI=10.1091/mbc.e06-09-0853;
RA   Jin Q.W., Ray S., Choi S.H., McCollum D.;
RT   "The nucleolar net1/cfi1-related protein dnt1 antagonizes the septation
RT   initiation network in fission yeast.";
RL   Mol. Biol. Cell 18:2924-2934(2007).
CC   -!- FUNCTION: Component of the UAF (upstream activation factor) complex
CC       which interacts with the upstream element of the RNA polymerase I
CC       promoter and forms a stable preinitiation complex. UAF seems to
CC       stimulate basal transcription to a fully activated level.
CC       {ECO:0000269|PubMed:12490702}.
CC   -!- SUBUNIT: Component of the UAF (upstream activation factor) complex
CC       which consists of spp27/uaf30, rrn5, rrn10, and histones H3 and H4.
CC       Interacts with rrn10. {ECO:0000269|PubMed:12490702}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10759889,
CC       ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:17538026}.
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DR   EMBL; CU329670; CAB10137.1; -; Genomic_DNA.
DR   EMBL; AB027899; BAA87203.1; -; Genomic_DNA.
DR   PIR; T38479; T38479.
DR   RefSeq; NP_594872.1; NM_001020301.2.
DR   AlphaFoldDB; O14013; -.
DR   SMR; O14013; -.
DR   BioGRID; 279184; 5.
DR   STRING; 4896.SPAC29A4.10.1; -.
DR   iPTMnet; O14013; -.
DR   MaxQB; O14013; -.
DR   PaxDb; O14013; -.
DR   EnsemblFungi; SPAC29A4.10.1; SPAC29A4.10.1:pep; SPAC29A4.10.
DR   GeneID; 2542734; -.
DR   KEGG; spo:SPAC29A4.10; -.
DR   PomBase; SPAC29A4.10; rrn5.
DR   VEuPathDB; FungiDB:SPAC29A4.10; -.
DR   eggNOG; ENOG502RY38; Eukaryota.
DR   HOGENOM; CLU_492710_0_0_1; -.
DR   InParanoid; O14013; -.
DR   OMA; QPICYYY; -.
DR   PRO; PR:O14013; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005730; C:nucleolus; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0000500; C:RNA polymerase I upstream activating factor complex; IDA:PomBase.
DR   GO; GO:0000182; F:rDNA binding; IDA: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; IMP:PomBase.
DR   CDD; cd00167; SANT; 1.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR039601; Rrn5.
DR   InterPro; IPR001005; SANT/Myb.
DR   PANTHER; PTHR28079; PTHR28079; 1.
DR   SMART; SM00717; SANT; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..556
FT                   /note="RNA polymerase I-specific transcription initiation
FT                   factor rrn5"
FT                   /id="PRO_0000116649"
SQ   SEQUENCE   556 AA;  64026 MW;  A1F97509E1802B72 CRC64;
     MSSSINGLNE SEGSTPLSTA SIIGSSEQLY MTHDERYLDV LQQYEVETEN KRDFDLEEEQ
     WGVLSGSCVD GTYWSAEEKE LFFQAVARNG KRDLDLIAYS IPSKSAVQIE RYINALENEL
     RWLRNHVDAS VRSQCLLKYE DIPIAMEMSQ NWIDWEEKIA ERLLEGSNIS GVETSHYNAQ
     SVKNKTSNED LFDTNEMRKI SERFYHFDRQ APFPSNPLSA GATEFLLQII KSKLKELIGT
     SIFLAESRFR KLEANNAFHR KPIIKNRDVV LSGKFLRFHR FNIPGFWKYL PTRQKMNVYK
     RNKRLKFQNY IHIMESDERQ SKLKLGRVRA RKTKNNENTM FFDSKEHSTD ESDGNLGEHD
     VKRKVDSVPA DETSINGFKK SVNQAEYPDN AQMFMDESVA EESLVEIDDS VEAYDMIQSK
     NYESFVWKYV LHLTDEMSTE DALFETIPLS NLLAQKRMKD KLKGSDVFTT LKITSKSLHN
     IDEHSDSDDE VQPICYYYKD PVVSHAPGAA EVVSELESGY VGLISYDLSN LPNSTEDPER
     KLAKPVSSWE LSLPLK
 
 
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