ID   RPAB1_SCHPO             Reviewed;         210 AA.
AC   Q09191;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=DNA-directed RNA polymerases I, II, and III subunit RPABC1;
DE            Short=RNA polymerases I, II, and III subunit ABC1;
DE   AltName: Full=RPC24B;
GN   Name=rpb5; ORFNames=SPAC23C4.15;
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 [MRNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=9499374;
RA   Shpakovski G.V., Lebedenko E.N.;
RT   "Molecular cloning of rpb5+, rpb7+ and rpb11+ genes of the fission yeast
RT   Schizosaccharomyces pombe: completing primary structure of all
RT   indispensable subunits of its RNA polymerase II.";
RL   Bioorg. Khim. 23:988-991(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND IDENTIFICATION IN THE RNA POLYMERASE
RP   II COMPLEX.
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=9077438; DOI=10.1046/j.1365-2443.1996.730274.x;
RA   Miyao T., Yasui K., Sakurai H., Yamagishi M., Ishihama A.;
RT   "Molecular assembly of RNA polymerase II from the fission yeast
RT   Schizosaccharomyces pombe: subunit-subunit contact network involving
RT   Rpb5.";
RL   Genes Cells 1:843-854(1996).
RN   [3]
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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
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, II and III which synthesize
CC       ribosomal RNA precursors, mRNA precursors and many functional non-
CC       coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively.
CC       Pol II is the central component of the basal RNA polymerase II
CC       transcription machinery. Pols are composed of mobile elements that move
CC       relative to each other. In Pol II, RPB5 is part of the lower jaw
CC       surrounding the central large cleft and thought to grab the incoming
CC       DNA template. Seems to be the major component in this process (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the RNA polymerase I (Pol I), RNA polymerase II
CC       (Pol II) and RNA polymerase III (Pol III) complexes consisting of at
CC       least 14, 12 and 17 subunits, respectively. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the archaeal Rpo5/eukaryotic RPB5 RNA polymerase
CC       subunit family. {ECO:0000305}.
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DR   EMBL; AF027820; AAB92515.1; -; mRNA.
DR   EMBL; D43785; BAA07843.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB16886.1; -; Genomic_DNA.
DR   PIR; T38270; T38270.
DR   RefSeq; NP_593187.1; NM_001018583.2.
DR   PDB; 3H0G; X-ray; 3.65 A; E/Q=1-210.
DR   PDB; 5U0S; EM; 7.80 A; e=1-210.
DR   PDB; 7AOC; EM; 3.84 A; E=1-210.
DR   PDB; 7AOD; EM; 4.50 A; E/Q=1-210.
DR   PDB; 7AOE; EM; 3.90 A; E=1-210.
DR   PDBsum; 3H0G; -.
DR   PDBsum; 5U0S; -.
DR   PDBsum; 7AOC; -.
DR   PDBsum; 7AOD; -.
DR   PDBsum; 7AOE; -.
DR   AlphaFoldDB; Q09191; -.
DR   SMR; Q09191; -.
DR   BioGRID; 278400; 25.
DR   IntAct; Q09191; 2.
DR   STRING; 4896.SPAC23C4.15.1; -.
DR   iPTMnet; Q09191; -.
DR   MaxQB; Q09191; -.
DR   PaxDb; Q09191; -.
DR   EnsemblFungi; SPAC23C4.15.1; SPAC23C4.15.1:pep; SPAC23C4.15.
DR   GeneID; 2541910; -.
DR   KEGG; spo:SPAC23C4.15; -.
DR   PomBase; SPAC23C4.15; rpb5.
DR   VEuPathDB; FungiDB:SPAC23C4.15; -.
DR   eggNOG; KOG3218; Eukaryota.
DR   HOGENOM; CLU_058320_0_0_1; -.
DR   InParanoid; Q09191; -.
DR   OMA; VRDRGYF; -.
DR   PhylomeDB; Q09191; -.
DR   Reactome; R-SPO-113418; Formation of the Early Elongation Complex.
DR   Reactome; R-SPO-5578749; Transcriptional regulation by small RNAs.
DR   Reactome; R-SPO-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-SPO-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-SPO-6782135; Dual incision in TC-NER.
DR   Reactome; R-SPO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-SPO-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR   Reactome; R-SPO-6807505; RNA polymerase II transcribes snRNA genes.
DR   Reactome; R-SPO-72086; mRNA Capping.
DR   Reactome; R-SPO-72165; mRNA Splicing - Minor Pathway.
DR   Reactome; R-SPO-73762; RNA Polymerase I Transcription Initiation.
DR   Reactome; R-SPO-73772; RNA Polymerase I Promoter Escape.
DR   Reactome; R-SPO-73776; RNA Polymerase II Promoter Escape.
DR   Reactome; R-SPO-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR   Reactome; R-SPO-75953; RNA Polymerase II Transcription Initiation.
DR   Reactome; R-SPO-75955; RNA Polymerase II Transcription Elongation.
DR   Reactome; R-SPO-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
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   Reactome; R-SPO-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR   Reactome; R-SPO-9018519; Estrogen-dependent gene expression.
DR   EvolutionaryTrace; Q09191; -.
DR   PRO; PR:Q09191; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005736; C:RNA polymerase I complex; IGI:PomBase.
DR   GO; GO:0005665; C:RNA polymerase II, core complex; IDA:PomBase.
DR   GO; GO:0005666; C:RNA polymerase III complex; IGI:PomBase.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR   GO; GO:0006360; P:transcription by RNA polymerase I; IGI:PomBase.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IDA:PomBase.
DR   GO; GO:0006383; P:transcription by RNA polymerase III; IGI:PomBase.
DR   Gene3D; 3.40.1340.10; -; 1.
DR   Gene3D; 3.90.940.20; -; 1.
DR   HAMAP; MF_00025; RNApol_Rpo5_RPB5; 1.
DR   InterPro; IPR014381; Arch_Rpo5/euc_Rpb5.
DR   InterPro; IPR005571; RNA_pol_Rpb5_N.
DR   InterPro; IPR036710; RNA_pol_Rpb5_N_sf.
DR   InterPro; IPR000783; RNA_pol_subH/Rpb5_C.
DR   InterPro; IPR020608; RNA_pol_subH/Rpb5_CS.
DR   InterPro; IPR035913; RPB5-like_sf.
DR   PANTHER; PTHR10535; PTHR10535; 1.
DR   Pfam; PF01191; RNA_pol_Rpb5_C; 1.
DR   Pfam; PF03871; RNA_pol_Rpb5_N; 1.
DR   PIRSF; PIRSF000747; RPB5; 1.
DR   SUPFAM; SSF53036; SSF53036; 1.
DR   SUPFAM; SSF55287; SSF55287; 1.
DR   PROSITE; PS01110; RNA_POL_H_23KD; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-directed RNA polymerase; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription.
FT   CHAIN           1..210
FT                   /note="DNA-directed RNA polymerases I, II, and III subunit
FT                   RPABC1"
FT                   /id="PRO_0000146084"
FT   MOD_RES         152
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   210 AA;  23915 MW;  EB74C07B9F048762 CRC64;
     MSAEEKNIVR VFRAWKTAHQ LVHDRGYGVS QAELDLTLDQ FKAMHCGMGR NLDRTTLSFY
     AKPSNDSNKG TIYIEFAKEP SVGIKEMRTF VHTLGDHNHK TGILIYANSM TPSAAKIIAT
     VTGQFTIETF QESDLIVNIT HHELVPKHIL LSPDEKKELL DRYKLRETQL PRIQLADPVA
     RYLGLKRGEV VKIVRRSETS GRYNSYRICA