RPB2_PICGU
ID RPB2_PICGU Reviewed; 1236 AA.
AC A5DHT2; B3DFH1; Q6H184; Q6H185; Q6H190; Q6JEG3; Q6RYI5;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 3.
DT 03-AUG-2022, entry version 79.
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; ORFNames=PGUG_02833;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1219.
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 398-766, AND VARIANTS ALA-401;
RP VAL-519; THR-722 AND LYS-727.
RC STRAIN=ATCC 46036 / CBS 2030 / IFO 10106 / NRRL Y-2075, MMRL 1635,
RC MMRL 1636, and MMRL 1759;
RX PubMed=15583292; DOI=10.1128/jcm.42.12.5624-5635.2004;
RA Diezmann S., Cox C.J., Schoenian G., Vilgalys R.J., Mitchell T.G.;
RT "Phylogeny and evolution of medical species of Candida and related taxa: a
RT multigenic analysis.";
RL J. Clin. Microbiol. 42:5624-5635(2004).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACE73644.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=EDK38735.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CH408157; EDK38735.2; ALT_INIT; Genomic_DNA.
DR EMBL; AY485613; AAS67502.2; -; Genomic_DNA.
DR EMBL; AY497607; AAT47725.1; -; Genomic_DNA.
DR EMBL; AY497627; AAT12543.1; -; Genomic_DNA.
DR EMBL; AY497628; AAT47730.2; -; Genomic_DNA.
DR EMBL; AY497628; ACE73644.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AY497629; AAT47731.1; -; Genomic_DNA.
DR RefSeq; XP_001485104.1; XM_001485054.1.
DR AlphaFoldDB; A5DHT2; -.
DR SMR; A5DHT2; -.
DR STRING; 4929.XP_001485104.1; -.
DR EnsemblFungi; EDK38735; EDK38735; PGUG_02833.
DR GeneID; 5126869; -.
DR KEGG; pgu:PGUG_02833; -.
DR eggNOG; KOG0214; Eukaryota.
DR HOGENOM; CLU_000524_5_2_1; -.
DR InParanoid; A5DHT2; -.
DR OrthoDB; 42570at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
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..1236
FT /note="DNA-directed RNA polymerase II subunit RPB2"
FT /id="PRO_0000295037"
FT ZN_FING 1172..1194
FT /note="C4-type"
FT BINDING 846
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="ligand shared with RPB1"
FT /evidence="ECO:0000250"
FT BINDING 1172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT VARIANT 401
FT /note="D -> A (in strain: MmRL 1635)"
FT /evidence="ECO:0000269|PubMed:15583292"
FT VARIANT 519
FT /note="A -> V (in strain: MmRL 1759)"
FT /evidence="ECO:0000269|PubMed:15583292"
FT VARIANT 722
FT /note="S -> T (in strain: MmRL 1635 and MmRL 1759)"
FT /evidence="ECO:0000269|PubMed:15583292"
FT VARIANT 727
FT /note="E -> K (in strain: MmRL 1636)"
FT /evidence="ECO:0000269|PubMed:15583292"
FT CONFLICT 13
FT /note="D -> G (in Ref. 2; AAS67502)"
FT /evidence="ECO:0000305"
FT CONFLICT 1056
FT /note="F -> L (in Ref. 2; AAS67502)"
FT /evidence="ECO:0000305"
FT CONFLICT 1203
FT /note="I -> V (in Ref. 2; AAS67502)"
FT /evidence="ECO:0000305"
FT CONFLICT 1216
FT /note="L -> S (in Ref. 2; AAS67502)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1236 AA; 140115 MW; 111D7C5FC0DA5C52 CRC64;
MSDQASDPYM YDDDSSSITP EDCWTVISSF FQEKGLVSQQ LDSFDEFIES TIQELVWEDS
RLILDQPAQH TSEEDHENRR YEITFGKIYI SKPTQTEGDG TTHPMFPQEA RLRNLTYSSP
LYVDMTKRVL KSDDNAGNEH ELEWIEEEIK DEEPSTKVYL GKVPIMLRSK FCMLRDLGEH
EFYELKECPY DMGGYFVING SEKVLIAQER SAANIVQVFK KAAPSPISHV AEIRSALERG
SRLISSMQIK LYGREEKSTS NRTIKATLPY IKEDIPIVIV FRALGIVPDG DILEHICYDA
NDWQMLEMLK PCVEEGFVIQ EREVALDFIG RRGALGIKRE KRIQYAKDIL QKELLPNITQ
DEGFETRKAF FLGYMVNRLL LCALERKEPD DRDHFGKKRL DLAGPLLASL FRILFKKLTK
DIYNYMQRCV ENDKVFNLTL AVKSQTITDG LRYSLATGNW GEQKKAMSSR AGVSQVLNRY
TYSSTLSHLR RTNTPIGRDG KIAKPRQLHN THWGLVCPAE TPEGQACGLV KNLSLMSCIS
VGTPSEPILY FLEEWGMEPL EDYVPSNSPD STRVFVNGVW VGTHREPAHL VDTMRSLRRR
GDISPEVSII RDIREKEFKI FTDAGRVYRP LFIVDDDPES ETKGELKLQK EHIHKLLNAE
YSEEYATNEF GEEEGPYGWS SLVNDGVVEY VDAEEEETIM IAMTPEDLEA SKSSLTATQQ
KSLQLEEQEL DPAKRIKPTN SSTTSTFTHC EIHPSMILGV AASIIPFPDH NQSPRNTYQS
AMGKQAMGVF LTNYSVRMDT MANILYYPQK PLATTRAMEH LKFRELPAGQ NAIVAIACYS
GYNQEDSMIM NQSSIDRGLF RSLFFRTYMD LEKRQGMKAL ETFEKPSRSD TLRLKHGTYE
KLDDDGLIAP GIRVSGEDII IGKTTPIPPD TEELGQRTQY HTKRDASTPL RSTESGIVDQ
VLLTTNGDGA KFVKVRMRTT KVPQIGDKFA SRHGQKGTVG VTYRHEDMPF TSQGIVPDLI
INPHAIPSRM TVAHLIECLL SKVSSLSGLE GDASPFTDVT AEAVSKLLRE HGYQSRGFEV
MYHGHTGKKL MAQVFFGPTY YQRLRHMVDD KIHARARGPV QVLTRQPVEG RSRDGGLRFG
EMERDCMIAH GAAGFLKERL MEASDAFRVH VCGVCGLMSV IANLKKNQFE CRSCKNKTNI
YQIHIPYAAK LLFQELMAMN ISPRLYTERS GVSVRT
