RPB2_CANGA
ID RPB2_CANGA Reviewed; 1223 AA.
AC Q6FLD5; Q6JEI1; Q6RYI6;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
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;
GN Name=RPB2; OrderedLocusNames=CAGL0L04246g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 208-1092.
RX PubMed=15070748; DOI=10.1073/pnas.0400938101;
RA Liu Y.J., Hall B.D.;
RT "Body plan evolution of ascomycetes, as inferred from an RNA polymerase II
RT phylogeny.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:4507-4512(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 402-756.
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RA Diezmann S., Cox C.J., Schoenian G., Vilgalys R.J., Mitchell T.G.;
RT "Molecular phylogeny and evolution of Candida and related species within
RT the order saccharomycetales as inferred from multilocus sequence
RT analysis.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
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; CR380958; CAG61929.1; -; Genomic_DNA.
DR EMBL; AY485612; AAS67501.1; -; Genomic_DNA.
DR EMBL; AY497601; AAT12525.1; -; Genomic_DNA.
DR RefSeq; XP_448959.1; XM_448959.1.
DR AlphaFoldDB; Q6FLD5; -.
DR SMR; Q6FLD5; -.
DR STRING; 5478.XP_448959.1; -.
DR EnsemblFungi; CAG61929; CAG61929; CAGL0L04246g.
DR GeneID; 2890773; -.
DR KEGG; cgr:CAGL0L04246g; -.
DR CGD; CAL0135754; RPB2.
DR VEuPathDB; FungiDB:CAGL0L04246g; -.
DR eggNOG; KOG0214; Eukaryota.
DR HOGENOM; CLU_000524_5_2_1; -.
DR InParanoid; Q6FLD5; -.
DR OMA; RDLHGTH; -.
DR Proteomes; UP000002428; Chromosome L.
DR GO; GO:0005721; C:pericentric heterochromatin; IEA:EnsemblFungi.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IEA:EnsemblFungi.
DR GO; GO:0003677; F:DNA binding; IEA:EnsemblFungi.
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; IEA:EnsemblFungi.
DR GO; GO:0001055; F:RNA polymerase II activity; IEA:EnsemblFungi.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:EnsemblFungi.
DR GO; GO:0031048; P:heterochromatin assembly by small RNA; IEA:EnsemblFungi.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IEA:EnsemblFungi.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IEA:EnsemblFungi.
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 3: Inferred from homology;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Transcription;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1223
FT /note="DNA-directed RNA polymerase II subunit RPB2"
FT /id="PRO_0000048089"
FT ZN_FING 1162..1184
FT /note="C4-type"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 836
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="ligand shared with RPB1"
FT /evidence="ECO:0000250"
FT BINDING 1162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CONFLICT 208
FT /note="K -> C (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="I -> H (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 739
FT /note="H -> L (in Ref. 3; AAT12525)"
FT /evidence="ECO:0000305"
FT CONFLICT 1092
FT /note="Q -> G (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1223 AA; 138714 MW; 50DF19BAC27C1E63 CRC64;
MSADNEDYYD EDPYGFEEEN APITAEDTWA VISAFFREKG LVSQQLDSFN QFVDYTLQDI
ISEDSTLILE QLAQHTTEQD NISRKYEISF GKIYVTKPMV NESDGVTHAL YPQEARLRNL
TYSSGLFVDV TKRTYEAVDV PGRDLNYQLI AEESEEDSES GKVFIGRLPI MLRSKNCYLS
DATESDLYKL KECPFDMGGY FIINGSEKVL IAQERSAGNI VQVFKKAAPS PISHVAEIRS
ALEKGSRFIS TLQVKLYGRE SSSARTIKAT LPYIKQDIPI VIIFRALGII PDGEILEHIC
YDVNDWQMLE MLKPCVEDGF VIQDRETALD FIGRRGTALG IKKEKRIQYA KDILQKEFLP
HITQLEGFES RKAFFLGYMI NRLLLCALDR KDQDDRDHFG KKRLDLAGPL LAQLFKTLFR
KLTKDIFRYM QRTVEEANDF NMKLAINAKT ITSGLKYALA TGNWGEQKKA MSSRAGVSQV
LNRYTYSSTL SHLRRTNTPI GRDGKLAKPR QLHNTHWGLV CPAETPEGQA CGLVKNLSLM
SCISVGADPM PIITFLSEWG MEPLEDYVPH QSPDATRVFV NGVWHGVHRN PARLMETLRT
LRRKGDINPE VSMIRDIREQ ELKIFTDAGR VYRPLFIVED DEELGRKELK VRKGHVAKLM
ATEYQDIEGG FEDAEDYTWS SLLNEGLVEY IDAEEEESIL IAMQPEDLEP TAVEQDIPKE
NVDLAKRIKV THHATTFTHC EIHPSMILGV AASIIPFPDH NQSPRNTYQS AMGKQAMGVF
LTNYNFRMDT MANILYYPQK PLGTTRAMEY LKFRELPAGQ NAIVAIACYS GYNQEDSMIM
NQSSIDRGLF RSLFFRSYMD QEKKYGMSIT ETFEKPQRTN TLRMKHGTYD KLDEDGLIAP
GVRVSGEDII IGKTTPIAPD EEELGQRTAY HSKRDASTPL RSTENGIVDQ VLITTNQDGL
KFVKVRVRTT KVPQIGDKFA SRHGQKGTIG ITYRREDMPF TAEGIVPDLI INPHAIPSRM
TVAHLIECLL SKVAALSGNE GDASPFTDIT VEGISKLLRE HGYQSRGFEV MYNGHTGKKL
MAQIFFGPTY YQRLRHMVDD KIHARARGPM QVLTRQPVEG RSRDGGLRFG EMERDCMIAH
GAAAFLKERL MEASDAFRVH ICGICGLMSV IAKLNHNQFE CKGCDNKIDI YQIHIPYAAK
LLFQELMAMN ITPRLYTDRS RDF
