RPAC1_SCHPO
ID RPAC1_SCHPO Reviewed; 348 AA.
AC O94616;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=DNA-directed RNA polymerases I and III subunit RPAC1;
DE Short=RNA polymerases I and III subunit AC1;
DE AltName: Full=DNA-directed RNA polymerases I and III 40 kDa polypeptide;
DE Short=AC40;
DE AltName: Full=RPC39;
GN Name=rpc40; Synonyms=rpa42; ORFNames=SPBC1289.07c;
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 [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=10079952;
RA Shpakovskii G.V., Shematorova E.K.;
RT "Molecular cloning and characteristics of rpc19+ and rpc40+
RT Schizosaccharomyces pombe genes, coding for common subunits of nuclear RNA
RT polymerase I and III.";
RL Bioorg. Khim. 24:933-937(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=10541858; DOI=10.1007/s002940050492;
RA Shpakovski G.V., Shematorova E.K.;
RT "Rpc19 and Rpc40, two alpha-like subunits shared by nuclear RNA polymerases
RT I and III, are interchangeable between the fission and budding yeasts.";
RL Curr. Genet. 36:208-214(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Nogi Y., Imazawa Y.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
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).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Common component of RNA polymerases I and III which synthesize
CC ribosomal RNA precursors and small RNAs, such as 5S rRNA and tRNAs,
CC respectively. RPAC1 is part of the Pol core element with the central
CC large cleft and probably a clamp element that moves to open and close
CC the cleft (By similarity). {ECO:0000250|UniProtKB:O15160,
CC ECO:0000250|UniProtKB:P07703}.
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) and RNA polymerase
CC III (Pol III) complexes consisting of at least 13 and 17 subunits,
CC respectively. Interacts with RPAC19/RPAC2.
CC {ECO:0000250|UniProtKB:O15160}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O15160}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo3/eukaryotic RPB3 RNA polymerase
CC subunit family. {ECO:0000305}.
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DR EMBL; AF082512; AAD44503.1; -; Genomic_DNA.
DR EMBL; AB021859; BAA77385.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB38687.1; -; Genomic_DNA.
DR PIR; T39358; T39358.
DR RefSeq; NP_596831.1; NM_001023852.2.
DR PDB; 7AOC; EM; 3.84 A; C=1-348.
DR PDB; 7AOD; EM; 4.50 A; C/O=1-348.
DR PDB; 7AOE; EM; 3.90 A; C=1-348.
DR PDBsum; 7AOC; -.
DR PDBsum; 7AOD; -.
DR PDBsum; 7AOE; -.
DR AlphaFoldDB; O94616; -.
DR SMR; O94616; -.
DR BioGRID; 276218; 9.
DR DIP; DIP-29538N; -.
DR IntAct; O94616; 1.
DR STRING; 4896.SPBC1289.07c.1; -.
DR iPTMnet; O94616; -.
DR MaxQB; O94616; -.
DR PaxDb; O94616; -.
DR PRIDE; O94616; -.
DR EnsemblFungi; SPBC1289.07c.1; SPBC1289.07c.1:pep; SPBC1289.07c.
DR GeneID; 2539663; -.
DR KEGG; spo:SPBC1289.07c; -.
DR PomBase; SPBC1289.07c; rpc40.
DR VEuPathDB; FungiDB:SPBC1289.07c; -.
DR eggNOG; KOG1521; Eukaryota.
DR HOGENOM; CLU_038421_0_1_1; -.
DR InParanoid; O94616; -.
DR OMA; ECLRHPE; -.
DR PhylomeDB; O94616; -.
DR Reactome; R-SPO-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-SPO-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-SPO-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR Reactome; R-SPO-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR PRO; PR:O94616; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005736; C:RNA polymerase I complex; IGI:PomBase.
DR GO; GO:0005666; C:RNA polymerase III complex; IGI:PomBase.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0001054; F:RNA polymerase I activity; IEA:InterPro.
DR GO; GO:0001056; F:RNA polymerase III activity; IEA:InterPro.
DR GO; GO:0006360; P:transcription by RNA polymerase I; IGI:PomBase.
DR GO; GO:0006383; P:transcription by RNA polymerase III; IGI:PomBase.
DR CDD; cd07032; RNAP_I_II_AC40; 1.
DR Gene3D; 2.170.120.12; -; 1.
DR Gene3D; 3.30.1360.10; -; 1.
DR HAMAP; MF_00320; RNApol_arch_Rpo3; 1.
DR InterPro; IPR001514; DNA-dir_RNA_pol_30-40kDasu_CS.
DR InterPro; IPR011262; DNA-dir_RNA_pol_insert.
DR InterPro; IPR011263; DNA-dir_RNA_pol_RpoA/D/Rpb3.
DR InterPro; IPR036603; RBP11-like.
DR InterPro; IPR022842; RNAP_Rpo3/Rpb3/RPAC1.
DR InterPro; IPR033901; RNAPI/III_AC40.
DR InterPro; IPR036643; RNApol_insert_sf.
DR PANTHER; PTHR11800:SF13; PTHR11800:SF13; 1.
DR Pfam; PF01000; RNA_pol_A_bac; 1.
DR Pfam; PF01193; RNA_pol_L; 1.
DR SMART; SM00662; RPOLD; 1.
DR SUPFAM; SSF55257; SSF55257; 1.
DR SUPFAM; SSF56553; SSF56553; 1.
DR PROSITE; PS00446; RNA_POL_D_30KD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-directed RNA polymerase; Nucleotidyltransferase; Nucleus;
KW Reference proteome; Transcription; Transferase.
FT CHAIN 1..348
FT /note="DNA-directed RNA polymerases I and III subunit
FT RPAC1"
FT /id="PRO_0000132741"
SQ SEQUENCE 348 AA; 39155 MW; A9C209362521E4AE CRC64;
MAAVDRSRTE ISVLSDRVTD VGSVDFPGYY FDEDNIWDLD KFKKNLKVSI TSLDQETMVF
EISGIDASIA NAFRRILIAE IPTLAFEFVY IINNTSIIQD EVLSHRIGLV PISADPDMFK
WFQHPLPGQE ATHTDYDTVV FSLNKKCEFN KNAATDEKDP KRLYVNSEVY SGDLIWKPQG
RQEERFADNP IRVVNPDIVV AKLRPGQEID LEAHAILGIG QDHAKFSPVA TASYRLLPTI
HILSPIEGED AVKFQKCFPK GVIELEEGPD GKKQARVADV RKDTVSRECL RHPEFADKVQ
LGRVRDHYLF SVESTGIMKP DVLFIKSIAV LKSKCLAVKS SLQNISSD
