RPB2_ASHGO
ID RPB2_ASHGO Reviewed; 1222 AA.
AC Q753Q4; Q6JEI5;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-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=AFR404C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 399-755.
RC STRAIN=ATCC 8717 / IMI 31268;
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; AE016819; AAS53775.1; -; Genomic_DNA.
DR EMBL; AY497595; AAT12521.1; -; Genomic_DNA.
DR RefSeq; NP_985951.1; NM_211306.1.
DR AlphaFoldDB; Q753Q4; -.
DR SMR; Q753Q4; -.
DR STRING; 33169.AAS53775; -.
DR EnsemblFungi; AAS53775; AAS53775; AGOS_AFR404C.
DR GeneID; 4622223; -.
DR KEGG; ago:AGOS_AFR404C; -.
DR eggNOG; KOG0214; Eukaryota.
DR HOGENOM; CLU_000524_5_2_1; -.
DR InParanoid; Q753Q4; -.
DR OMA; RDLHGTH; -.
DR Proteomes; UP000000591; Chromosome VI.
DR GO; GO:0005721; C:pericentric heterochromatin; IEA:EnsemblFungi.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IBA:GO_Central.
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..1222
FT /note="DNA-directed RNA polymerase II subunit RPB2"
FT /id="PRO_0000048088"
FT ZN_FING 1161..1183
FT /note="C4-type"
FT BINDING 835
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="ligand shared with RPB1"
FT /evidence="ECO:0000250"
FT BINDING 1161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1222 AA; 138617 MW; 7974639275076525 CRC64;
MLEYYDDDAY VYDDDDEDAP ITAEDSWTVI SAFFREKGLV SQQLDSFNQF INYTIQDLIL
EDSTLILEQL AQHTTEADNI SRKYEISFGK IYLAKPSMTE SDGVSHAMYP QEARLRNLTY
ASGLFVEIKK RTYEAVDIPG RDLKYEIIQE ESEDTEEGKI FIGRVPIMLR SKYCLLDDLS
ESDLYRLKEC PFDMGGYFII NGSEKVLIAQ ERSAGNIVQV FKKSAPSPIS HIAEIRSALE
KGSRFISTLQ VKLYGREGST SRTIKATLPY IKQDIPIVII FRALGIIPDG EILEHICYDQ
NDWQMLEMLK PCVEEGFVIQ DRETALDFIG RRGTALGIKK EKRIQYAKDI LQKEFLPHIT
QLEGFESRKA FFLGYMINRL LLCALDRKDQ DDRDHFGKKR LDLAGPLLAQ LFKTLFRKLT
RDILRFMQRS VEEAKDFNLK LAVKATTITA GLKYALATGN WGEQKKAMSS RAGVSQVLNR
YTYSSTLSHL RRTNTPIGRD GKLAKPRQLH NTHWGLVCPA ETPEGQACGL VKNLSLMSCI
SVGTDPVPII TFLNEWGMEP LEDYVPHQSP DATRVFVNGV WHGIHRNPAR LVDTIRKLRR
KGDITAEVSI VRDIREKELK IFTDAGRVYR PLFVVADTQH ADGHKDLKVR KGHIRKLMLT
EYQDIEGGFE DEDINYTWTS LLNDGIVEYI DAEEEETILI AMQQEDLDPS VPQTVDPSDE
LDPARRIKAI HHSNTFTHCE IHPSMILGVA ASVIPFPDHN QSPRNTYQSA MGKQAMGVFL
TNYNVRMDTM ANILYYPQKP LGTTRAMEYL KFRELPAGQN AIVAIACYSG YNQEDSMIMN
QSSIDSGLFR SLFFRSYMDQ EKRIGMSITE SFEKPHRTNT LRMKHGTYEK LDDDGLIAPG
VRVSGDDIII GKTTPIPPDA EELGQRTAFH SKRDASTPLR STENGIVDQV LITTNQEGLK
FVKVRVRTTK VPQIGDKFAS RHGQKGTIGI TYRREDMPFT AEGVVPDLII NPHAIPSRMT
VAHLIECLLS KVAALSGNEG DASPFTDITV DGISKLLREH GYQSRGFEVM YNGHTGKKLM
AQIFFGPTYY QRLRHMVDDK IHARARGPMQ VLTRQPVEGR SRDGGLRFGE MERDCMIAHG
AAAFLKERLM EASDAFRVHI CGICGLMTVV AKLKHNQFEC RGCKNKIDIY QVHIPYAAKL
LFQELMAMNI APRLYTDRSR DF
