RPB3_SCHPO
ID RPB3_SCHPO Reviewed; 297 AA.
AC P37382; P78959; P78960; Q9UUM9;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=DNA-directed RNA polymerase II subunit RPB3;
DE Short=RNA polymerase II subunit 3;
DE Short=RNA polymerase II subunit B3;
DE AltName: Full=DNA-directed RNA polymerase II 33 kDa polypeptide;
GN Name=rpb3; ORFNames=SPCC1442.10c;
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], AND IDENTIFICATION IN THE RNA POLYMERASE
RP II COMPLEX.
RC STRAIN=972 / ATCC 24843;
RX PubMed=8367291; DOI=10.1093/nar/21.16.3749;
RA Azuma Y., Yamagishi M., Ishihama A.;
RT "Subunits of the Schizosaccharomyces pombe RNA polymerase II: enzyme
RT purification and structure of the subunit 3 gene.";
RL Nucleic Acids Res. 21:3749-3754(1993).
RN [2]
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 [3]
RP VARIANTS.
RC STRAIN=JY265;
RX PubMed=8537315; DOI=10.1093/oxfordjournals.jbchem.a124881;
RA Azuma Y., Yasui K., Yamagishi M., Ishihama A.;
RT "Isolation of thermolabile mutant RNA polymerase II from fission yeast
RT Schizosaccharomyces pombe with mutations in the subunit 3 gene.";
RL J. Biochem. 118:216-220(1995).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Component of RNA polymerase II which synthesizes mRNA precursors and
CC many functional non-coding RNAs. Pol II is the central component of the
CC basal RNA polymerase II transcription machinery. It is composed of
CC mobile elements that move relative to each other. RPB3 is part of the
CC core element with the central large cleft and the clamp element that
CC moves to open and close the cleft (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting
CC of 12 subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the archaeal Rpo3/eukaryotic RPB3 RNA polymerase
CC subunit family. {ECO:0000305}.
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DR EMBL; D15070; BAA22566.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA21444.1; -; Genomic_DNA.
DR EMBL; D50661; BAA09315.1; -; Genomic_DNA.
DR EMBL; D50662; BAA09316.1; -; Genomic_DNA.
DR PIR; S43201; S43201.
DR PIR; T40975; T40975.
DR RefSeq; NP_588324.1; NM_001023315.2.
DR PDB; 3H0G; X-ray; 3.65 A; C/O=1-297.
DR PDB; 5U0S; EM; 7.80 A; c=1-297.
DR PDBsum; 3H0G; -.
DR PDBsum; 5U0S; -.
DR AlphaFoldDB; P37382; -.
DR SMR; P37382; -.
DR BioGRID; 275397; 23.
DR IntAct; P37382; 4.
DR MINT; P37382; -.
DR STRING; 4896.SPCC1442.10c.1; -.
DR iPTMnet; P37382; -.
DR MaxQB; P37382; -.
DR PaxDb; P37382; -.
DR EnsemblFungi; SPCC1442.10c.1; SPCC1442.10c.1:pep; SPCC1442.10c.
DR GeneID; 2538816; -.
DR KEGG; spo:SPCC1442.10c; -.
DR PomBase; SPCC1442.10c; rpb3.
DR VEuPathDB; FungiDB:SPCC1442.10c; -.
DR eggNOG; KOG1522; Eukaryota.
DR HOGENOM; CLU_038421_1_1_1; -.
DR InParanoid; P37382; -.
DR OMA; PENIVMM; -.
DR PhylomeDB; P37382; -.
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-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-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR Reactome; R-SPO-9018519; Estrogen-dependent gene expression.
DR EvolutionaryTrace; P37382; -.
DR PRO; PR:P37382; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IDA: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:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0006366; P:transcription by RNA polymerase II; EXP:PomBase.
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; IPR036643; RNApol_insert_sf.
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; Nucleus; Reference proteome;
KW Transcription.
FT CHAIN 1..297
FT /note="DNA-directed RNA polymerase II subunit RPB3"
FT /id="PRO_0000132747"
FT REGION 270..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 7
FT /note="I -> L (in strain: Isolate TS99)"
FT VARIANT 14..15
FT /note="KN -> RD (in strain: Isolate TS54)"
FT VARIANT 24
FT /note="T -> S (in strain: Isolate TS54)"
FT VARIANT 29
FT /note="A -> P (in strain: Isolate TS99)"
FT VARIANT 67
FT /note="G -> D (in strain: Isolate TS54)"
SQ SEQUENCE 297 AA; 33716 MW; 94F639734B162DDF CRC64;
MDSETHITIR NISKNSVDFV LTNTSLAVAN SLRRVVLAEI PTVAIDLVEI NVNTSVMPDE
FLAHRLGMIP LDSSNIDEPP PVGLEYTRNC DCDQYCPKCS VELFLNAKCT GEGTMEIYAR
DLVVSSNSSL GHPILADPKS RGPLICKLRK EQEISLRCIA KKGIAKEHAK WSPTSAVAFE
YDPWNKLQHT DYWFENDADA EWPKSKNADW EEPPREGEPF NFQEEPRRFY MDVESVGSIP
PNEIMVQGLR ILQEKLAVLV RDLDEEQPTQ LSANELNMEE NAEMNWSPYQ NGEENTW
