RDP1_SCHPO
ID RDP1_SCHPO Reviewed; 1215 AA.
AC O14227;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=RNA-dependent RNA polymerase 1;
DE Short=Protein rdp1;
DE EC=2.7.7.48;
GN Name=rdp1; Synonyms=csp7, rdr1; ORFNames=SPAC6F12.09;
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12193640; DOI=10.1126/science.1074973;
RA Volpe T.A., Kidner C., Hall I.M., Teng G., Grewal S.I.S., Martienssen R.A.;
RT "Regulation of heterochromatic silencing and histone H3 lysine-9
RT methylation by RNAi.";
RL Science 297:1833-1837(2002).
RN [3]
RP FUNCTION.
RX PubMed=12215653; DOI=10.1126/science.1076466;
RA Hall I.M., Shankaranarayana G.D., Noma K., Ayoub N., Cohen A.,
RA Grewal S.I.S.;
RT "Establishment and maintenance of a heterochromatin domain.";
RL Science 297:2232-2237(2002).
RN [4]
RP FUNCTION.
RX PubMed=12733640; DOI=10.1023/a:1022815931524;
RA Volpe T., Schramke V., Hamilton G.L., White S.A., Teng G.,
RA Martienssen R.A., Allshire R.C.;
RT "RNA interference is required for normal centromere function in fission
RT yeast.";
RL Chromosome Res. 11:137-146(2003).
RN [5]
RP FUNCTION.
RX PubMed=12509501; DOI=10.1073/pnas.232688099;
RA Hall I.M., Noma K., Grewal S.I.S.;
RT "RNA interference machinery regulates chromosome dynamics during mitosis
RT and meiosis in fission yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:193-198(2003).
RN [6]
RP FUNCTION, IDENTIFICATION OF THE COMPONENTS OF THE RDRC AND RITS COMPLEXES
RP BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=15607976; DOI=10.1016/j.cell.2004.11.034;
RA Motamedi M.R., Verdel A., Colmenares S.U., Gerber S.A., Gygi S.P.,
RA Moazed D.;
RT "Two RNAi complexes, RITS and RDRC, physically interact and localize to
RT noncoding centromeric RNAs.";
RL Cell 119:789-802(2004).
RN [7]
RP FUNCTION.
RX PubMed=15371329; DOI=10.1101/gad.1218004;
RA Sigova A., Rhind N., Zamore P.D.;
RT "A single Argonaute protein mediates both transcriptional and
RT posttranscriptional silencing in Schizosaccharomyces pombe.";
RL Genes Dev. 18:2359-2367(2004).
RN [8]
RP FUNCTION.
RX PubMed=14699070; DOI=10.1091/mbc.e03-06-0433;
RA Carmichael J.B., Provost P., Ekwall K., Hobman T.C.;
RT "ago1 and dcr1, two core components of the RNA interference pathway,
RT functionally diverge from rdp1 in regulating cell cycle events in
RT Schizosaccharomyces pombe.";
RL Mol. Biol. Cell 15:1425-1435(2004).
RN [9]
RP FUNCTION, POLYMERASE ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ASP-903.
RX PubMed=15615848; DOI=10.1073/pnas.0407641102;
RA Sugiyama T., Cam H., Verdel A., Moazed D., Grewal S.I.S.;
RT "RNA-dependent RNA polymerase is an essential component of a self-enforcing
RT loop coupling heterochromatin assembly to siRNA production.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:152-157(2005).
CC -!- FUNCTION: Has a role in the RNA interference (RNAi) pathway which is
CC important for heterochromatin formation, accurate chromosome
CC segregation, centromere cohesion and telomere function during mitosis
CC and meiosis. Required for both post-transcriptional and transcriptional
CC gene silencing. Required for silencing at the centromeres and for
CC initiation of transcriptionally silent heterochromatin at the mating
CC type locus. Promotes histone H3 'Lys-10' methylation necessary for
CC centromere function. Required for recruitment of swi6 and cohesin to an
CC ectopic dg repeat. A member of the RNA-directed RNA polymerase complex
CC (RDRC) which is involved in the generation of small interfering RNAs
CC (siRNAs) and mediates their association with the RNA-induced
CC transcriptional silencing (RITS) complex. RITS acts as a priming
CC complex for dsRNA synthesis at the site of non-coding centromeric RNA.
CC Its RNA-dependent RNA polymerase activity is critical in siRNA
CC production necessary for heterochromatin formation.
CC {ECO:0000269|PubMed:12193640, ECO:0000269|PubMed:12215653,
CC ECO:0000269|PubMed:12509501, ECO:0000269|PubMed:12733640,
CC ECO:0000269|PubMed:14699070, ECO:0000269|PubMed:15371329,
CC ECO:0000269|PubMed:15607976, ECO:0000269|PubMed:15615848}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48;
CC -!- SUBUNIT: Cid12, hrr1 and rdp1 interact forming the RNA-directed RNA
CC polymerase complex (RDRC). The RDRC complex interacts with the RITS
CC complex via interaction between ago1 and hrr1. Clr4 has a role in
CC mediating this interaction.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15607976}. Nucleus
CC {ECO:0000269|PubMed:12193640, ECO:0000269|PubMed:15607976}. Chromosome,
CC telomere {ECO:0000269|PubMed:15615848}. Chromosome, centromere
CC {ECO:0000269|PubMed:15615848}. Note=Associates with telomeric and
CC mating-type region heterochromatin. {ECO:0000269|PubMed:15615848}.
CC -!- SIMILARITY: Belongs to the RdRP family. {ECO:0000305}.
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DR EMBL; CU329670; CAB11093.1; -; Genomic_DNA.
DR PIR; T11660; T11660.
DR RefSeq; NP_593295.1; NM_001018725.2.
DR AlphaFoldDB; O14227; -.
DR SMR; O14227; -.
DR BioGRID; 278673; 82.
DR DIP; DIP-57038N; -.
DR IntAct; O14227; 2.
DR STRING; 4896.SPAC6F12.09.1; -.
DR PaxDb; O14227; -.
DR PRIDE; O14227; -.
DR EnsemblFungi; SPAC6F12.09.1; SPAC6F12.09.1:pep; SPAC6F12.09.
DR PomBase; SPAC6F12.09; rdp1.
DR VEuPathDB; FungiDB:SPAC6F12.09; -.
DR eggNOG; KOG0988; Eukaryota.
DR HOGENOM; CLU_001366_0_0_1; -.
DR InParanoid; O14227; -.
DR OMA; VTYMKND; -.
DR PhylomeDB; O14227; -.
DR BRENDA; 2.7.7.48; 5613.
DR PRO; PR:O14227; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0099115; C:chromosome, subtelomeric region; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0031934; C:mating-type region heterochromatin; IDA:PomBase.
DR GO; GO:0031380; C:nuclear RNA-directed RNA polymerase complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:PomBase.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IDA:PomBase.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0033562; P:co-transcriptional gene silencing by RNA interference machinery; IMP:PomBase.
DR GO; GO:0070314; P:G1 to G0 transition; IMP:PomBase.
DR GO; GO:0031048; P:heterochromatin assembly by small RNA; IDA:PomBase.
DR GO; GO:0070317; P:negative regulation of G0 to G1 transition; IMP:PomBase.
DR GO; GO:0031508; P:pericentric heterochromatin assembly; IMP:PomBase.
DR GO; GO:0030422; P:siRNA processing; IBA:GO_Central.
DR InterPro; IPR007855; RNA-dep_RNA_pol_euk-typ.
DR PANTHER; PTHR23079; PTHR23079; 1.
DR Pfam; PF05183; RdRP; 1.
PE 1: Evidence at protein level;
KW Centromere; Chromosome; Chromosome partition; Cytoplasm;
KW Nucleotidyltransferase; Nucleus; Reference proteome; RNA-binding;
KW RNA-directed RNA polymerase; RNA-mediated gene silencing; Telomere;
KW Transferase.
FT CHAIN 1..1215
FT /note="RNA-dependent RNA polymerase 1"
FT /id="PRO_0000097211"
FT MUTAGEN 903
FT /note="D->A: Abolishes RNA-dependent RNA polymerase
FT activity and results in loss of transcriptional silencing
FT and heterochromatin formation at centromeres together with
FT defects in mitotic chromosome segregation and telomere
FT clustering."
FT /evidence="ECO:0000269|PubMed:15615848"
SQ SEQUENCE 1215 AA; 139478 MW; 389B95C8217CB05C CRC64;
MAVSLNDFIS VKLKRYSRES PWERLRVPYR NKKQKKWASV HNNEAQLHSA NKRNDNCLIQ
RSSTWRLGDM ITLVIKDIPV TWLSNEGGKL YNLWEPLHDY GTIEFMKINE PLNGQTSTTA
IVQFAPPPKV PFWEPNGKIN VKGVDLAVQI DITAHRSHIS RQVFSKNSFR SDQLVKIPLS
SFKLGQVYDE RIVPLFGVDC GITVTESNLL VYFNFKKLCV LFDASFDKQI ETFRLDFDFH
SIIGDVGTDY YDDHISLVFR FRFSPLIFRK SKNATESRVQ TFWTASHLWR RHYDILPFNV
SPTTASPIEL LNCHNAPIGR CNVLVLSFSI RDESDKDDIA FLLHNLEKFN LKSQLDKVVF
HLVPDYKHRC SLINDKEIEE EIAYLLQACL SKNLLSEIDL PIILANLKKL SKERAKKFLR
LILTSKTALI NPSELDFTKS FVFYDLSSAS SIHIKKLYVT PTTLRIVEDS LEAGNRVIRN
FKDFANRFMR VQITDEYYKQ KIRGGSDGFR NEKLYSRIQQ LLTYGIKVGN QIYEFLAFGN
SQLREHGAYF FASGSDLNAK QIREWMGDFS EINSVSKYAA RMGQCFSTTK EINRFCVDIS
LQDDIVRNNH CFTDGVGMAS LSVIRRLSLE VKNHDMFPSA FQFRMGGYKG VLSLAPPTKL
EYHQGNLVFP RRSQDKFKSF HSTLEVIKIS RFSNAHLNMQ LITLLEGLGV EKTVFLELTR
SQLSKMNESI NSKQKSILML RDNVDEYHST LIIADFIQAG FLERDDAFTE NLLNLYYEWV
LRLIKEKQKV SVPKGAYLLG VADETGTLKG HYDDAVLSVP EIFIQITDTS TSFGSYSTGK
LKTRVIVGLC IVARNPSLHP GDVRVCKAVR CDELMHLKNV IVFPTTGDRS IPAMCSGGDL
DGDEYTVIWD QRLLPKIVNY PPLLESSPKK SIDFLEGKPL IDSVKEFFVN YIKYDSLGLI
SNAWKAWAHD HDNNPEGIFG NVCLELAEMH SKAVDFAKSG VACKMQAKYH PKRYPDFMQK
TKTRSFRSET AVGKIFRYAA RFQRESGRPA TYNPIMNTVY DPCMKLPRFK TEYLNVAEEV
KKHYDNDLRS IMARFDISTE YEVYTAFILF KDDLAKTVNE YGLREEVSFQ FDLLKKKYTQ
EYLEKCALSN QSAFDSSEYE ERINSAVAAT YDVTYDQRVK SVGNGTTEVL ISFPYLFSSR
LCQLSRKAML TANNF
