RPB2_SCHPO
ID RPB2_SCHPO Reviewed; 1210 AA.
AC Q02061; Q9P7B1; Q9P7T2;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=DNA-directed RNA polymerase II subunit RPB2;
DE Short=RNA polymerase II subunit 2;
DE Short=RNA polymerase II subunit B2;
DE EC=2.7.7.6;
DE AltName: Full=DNA-directed RNA polymerase II 138 kDa polypeptide;
GN Name=rpb2; ORFNames=SPAC23G3.01, SPAC521.06;
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].
RX PubMed=8441660; DOI=10.1093/nar/21.3.469;
RA Kawagishi M., Yamagishi M., Ishihama A.;
RT "Cloning and sequence determination of the Schizosaccharomyces pombe rpb2
RT gene encoding the subunit 2 of RNA polymerase II.";
RL Nucleic Acids Res. 21:469-473(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).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Second largest component of RNA polymerase II which synthesizes mRNA
CC precursors and many functional non-coding RNAs. Proposed to contribute
CC to the polymerase catalytic activity and forms the polymerase active
CC center together with the largest subunit. Pol II is the central
CC component of the basal RNA polymerase II transcription machinery. It is
CC composed of mobile elements that move relative to each other. RPB2 is
CC part of the core element with the central large cleft, the clamp
CC element that moves to open and close the cleft and the jaws that are
CC thought to grab the incoming DNA template (By similarity).
CC {ECO:0000250}.
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=2.7.7.6;
CC -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting
CC of 12 subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- MISCELLANEOUS: The binding of ribonucleoside triphosphate to the RNA
CC polymerase II transcribing complex probably involves a two-step
CC mechanism. The initial binding seems to occur at the entry (E) site and
CC involves a magnesium ion coordinated by three conserved aspartate
CC residues of the two largest RNA Pol II subunits (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000305}.
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DR EMBL; D13337; BAA02600.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB86470.1; -; Genomic_DNA.
DR PIR; S35548; S35548.
DR PIR; T50175; T50175.
DR RefSeq; NP_593101.2; NM_001018498.2.
DR PDB; 3H0G; X-ray; 3.65 A; B/N=1-1210.
DR PDB; 5U0S; EM; 7.80 A; b=1-1210.
DR PDBsum; 3H0G; -.
DR PDBsum; 5U0S; -.
DR AlphaFoldDB; Q02061; -.
DR SMR; Q02061; -.
DR BioGRID; 277951; 23.
DR IntAct; Q02061; 2.
DR MINT; Q02061; -.
DR STRING; 4896.SPAC23G3.01.1; -.
DR iPTMnet; Q02061; -.
DR MaxQB; Q02061; -.
DR PaxDb; Q02061; -.
DR PRIDE; Q02061; -.
DR EnsemblFungi; SPAC23G3.01.1; SPAC23G3.01.1:pep; SPAC23G3.01.
DR GeneID; 2541446; -.
DR KEGG; spo:SPAC23G3.01; -.
DR PomBase; SPAC23G3.01; rpb2.
DR VEuPathDB; FungiDB:SPAC23G3.01; -.
DR eggNOG; KOG0214; Eukaryota.
DR HOGENOM; CLU_000524_5_2_1; -.
DR InParanoid; Q02061; -.
DR OMA; RDLHGTH; -.
DR PhylomeDB; Q02061; -.
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; Q02061; -.
DR PRO; PR:Q02061; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA: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:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IDA:PomBase.
DR GO; GO:0031048; P:heterochromatin assembly by small RNA; IMP:PomBase.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IGI:PomBase.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 1.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007646; RNA_pol_Rpb2_4.
DR InterPro; IPR007647; RNA_pol_Rpb2_5.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR PANTHER; PTHR20856; PTHR20856; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 1.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF04566; RNA_pol_Rpb2_4; 1.
DR Pfam; PF04567; RNA_pol_Rpb2_5; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Transcription;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1210
FT /note="DNA-directed RNA polymerase II subunit RPB2"
FT /id="PRO_0000048090"
FT ZN_FING 1152..1173
FT /note="C4-type"
FT BINDING 826
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="ligand shared with RPB1"
FT /evidence="ECO:0000250"
FT BINDING 1152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CONFLICT 727
FT /note="W -> R (in Ref. 1; BAA02600)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1210 AA; 137849 MW; C5D3794A743494CC CRC64;
MSYEDYQYNE TLTQEDCWTV ISSFFEETSL ARQQLFSFDE FVQNTMQEIV DDDSTLTLDQ
YAQHTGAQGD VTRRYEINFG QIYLSRPTMT EADGSTTTMF PQEARLRNLT YSSPLYVDMR
KKVMVAADSN VPIGEEEWLV EEEDEEPSKV FIGKIPIMLR STFCILNGVS DSELYDLNEC
PYDQGGYFII NGSEKVIIAQ ERSAANIVQV FKKAAPSPIA YVAEIRSALE RGSRLISSMQ
IKLMARNTEN SGQTIRATLP YIRSDIPIVI VFRALGVVPD RDILEHICYD PNDFQMLEMM
KPCIEEAFVI QDKDIALDYI GKRGSTTGVT REKRLRYAHD ILQKELLPHI TTMEGFETRK
AFFLGYMIHR MLLCALERRE PDDRDHFGKK RLDLAGPLLA SLFRMLFRKM TRDVYKYMQK
CVETNREFNL TLAVKSNIIT NGLRYSLATG NWGDQKRSMV NRVGVSQVLN RYTFASTLSH
LRRTNTPIGR DGKLAKPRQL HNTHWGMVCP AETPEGQACG LVKNLSLMSY VSVGSPSAPI
IEFLEEWGLE TLEDYNPSAS PNATKVFVNG VWLGVHRDPA HLTETLRSLR RRLDISAEVS
IVRDIREKEL RLFTDAGRIC RPLFIVDNNP NSERRGELCI RKEHIQQLIE DKDRYDIDPE
QRFGWTALVS SGLIEYLDAE EEETVMIAMS PEDLEASRQM QAGYEVKEEL DPAQRVKPAP
NPHVHAWTHC EIHPAMILGI LASIIPFPDH NQSPRNTYQS AMGKQAMGVY LTNYQVRMDT
MANILYYPQK PLATTRSMEY LKFRELPAGQ NAIVAILCYS GYNQEDSIIM NQASIDRGLF
RSIFYRTYTD QEKKIGMTVM EEFERPVRST TLRMKHGTYD KLEDDGLIAP GTRVSGEDII
IGKTAPIPLD HEELGQRTQL HAKRDVSTPL RSTESGIVDQ VMVTTNQEGL KFVKVRMRST
RIPQIGDKFA SRHGQKGTIG MTYRHEDMPF SAQGIVPDII INPHAIPSRM TVAHLVECQL
SKVSALSGFE GDATPFTDVT VEAVSKLLRS HGFQSRGFEV MYHGHTGRKL VAQVFLGPTY
YQRLKHLVDD KIHARARGPV QILTRQPVEG RSRDGGLRFG EMERDCQISH GCSSVLRERL
FDCSDAYRVI VCDICGLIAI ASYKKDSYEC RSCQNRTRFS QVYLPYAAKL LFQELMSMNI
APRLFTKNHK
