ID   RPB2_ENCCU              Reviewed;        1141 AA.
AC   Q8SR75;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=ECU10_0250;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
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; AL590449; CAD25744.1; -; Genomic_DNA.
DR   RefSeq; NP_586140.1; NM_001041973.1.
DR   AlphaFoldDB; Q8SR75; -.
DR   SMR; Q8SR75; -.
DR   STRING; 284813.Q8SR75; -.
DR   GeneID; 859788; -.
DR   KEGG; ecu:ECU10_0250; -.
DR   VEuPathDB; MicrosporidiaDB:ECU10_0250; -.
DR   HOGENOM; CLU_000524_5_2_1; -.
DR   InParanoid; Q8SR75; -.
DR   OMA; HEKTFIG; -.
DR   OrthoDB; 42570at2759; -.
DR   Proteomes; UP000000819; Chromosome X.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0006351; P:transcription, DNA-templated; IEA:InterPro.
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..1141
FT                   /note="DNA-directed RNA polymerase II subunit RPB2"
FT                   /id="PRO_0000048087"
FT   ZN_FING         1087..1106
FT                   /note="C4-type"
FT   BINDING         763
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="ligand shared with RPB1"
FT                   /evidence="ECO:0000250"
FT   BINDING         1087
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         1090
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         1103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         1106
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1141 AA;  127881 MW;  B01FF9AA4B5A2217 CRC64;
     MESAFTKEHS WSIISSFFEQ KGLVRQQLDS FDQFVKTKMQ EVINESPVII VQSAPTAGIE
     TQKRIAVRFG QIYVSKPPVY TESDGRTITV FPNEARIRDL TYASPLFIDV TKETLSELGV
     VDKHKYSRVP FGSLPVMLRS SYCVLYGLGD KDLIDLGECP YDQGGYFIVN GSEKVIVAQE
     RMASNTVYVF KKAQPATYTH YAEIRSVPEK SSRNPSTLSM KLCRSPGVIR VSLPLVKQDV
     PLFVLYRALG FLSDKEIIDH ILYEDDEEMF ELLKESIEEG TVVQDQNVAL DYIGKRSAPI
     GTPQEKRIVM AKDLLAKEVL PHIGTQEFCE TKKAYFIGYI VQRLLLVALG RRNPDDRDHY
     GKKRMDLSGP LLASLFRTLF KKLCVDTTRH MQKCIENGRE FNIALGLKAS IITQGFRYAL
     ATGNWGDQAK AMQTRAGVAQ VLNRYNFVST LSHLRRVNTP IEKEGKLAAP RQLHNTHWGM
     VCPAETPEGQ ACGLVKNLSL MAYISVGSSS GPLVEFLEEC GVESLEEIST SQLDAATKIF
     VNGVWVGIHS DPVGLIKSLK LLRRSLEMDK EVSIVRDIRE KEIRVQSDAG RPCRPLLVVK
     DNKLVITAED IRKLKRGEIK WDNLVTSGFI EFLDVEEEEM SMIAMNTKIL ADESRNSSDV
     SVSYTHCEIH PALILGICAS TIPFPDHNQS PRNTYQSAMG KQAMGIYATN FLLRMDTLSN
     ILFYPQKPLV TTKSMEYLRF KELPSGQNAL VAIACYSGYN QEDSIIMNQS AIDRGLFRSF
     FYRTYTDQES MSRPGVNEEF CKPSRGAVLR MKNLNYNKLD DDGLISPGTR VTGDDVLIGK
     ITPILDPERS TKEAPVYVYK DSSTAMRRTE TGIVDTVIVT NKDGYKFSKV KVRSGRIPQM
     GDKFASRHAQ KGTIGITLRQ EDMPFTSEGI VPDIIINPHA IPSRMTIGHL IECLLGKVSA
     MSGEEGDATP FSGVTVDGIS SRLKSYGFQQ RGLEVMYNGM TGRKLRAQMF FGPTYYQRLK
     HMVDDKIHAR ARGPLQILTR QPVEGRSRDG GLRFGEMERD CIISHGASAF LKERLMDVSD
     AYSCYVCDFC GLLAMGGSKV NECKGCNNTT NVSMVEIPYA FKLLIQELMG MNIAPRIRFE
     E