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Protein

DNA-directed RNA polymerase II subunit RPB2

Gene

RPB2

Organism
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB2 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template (By similarity).By similarity

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi835Magnesium; shared with RPB1By similarity1
Metal bindingi1161ZincBy similarity1
Metal bindingi1164ZincBy similarity1
Metal bindingi1180ZincBy similarity1
Metal bindingi1183ZincBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1161 – 1183C4-typeAdd BLAST23

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Transcription

Keywords - Ligandi

Magnesium, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-directed RNA polymerase II subunit RPB2 (EC:2.7.7.6)
Short name:
RNA polymerase II subunit 2
Short name:
RNA polymerase II subunit B2
Gene namesi
Name:RPB2
Ordered Locus Names:AFR404C
OrganismiAshbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
Taxonomic identifieri284811 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium
Proteomesi
  • UP000000591 Componenti: Chromosome VI

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

DNA-directed RNA polymerase, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000480881 – 1222DNA-directed RNA polymerase II subunit RPB2Add BLAST1222

Interactioni

Subunit structurei

Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ753Q4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RNA polymerase beta chain family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1161 – 1183C4-typeAdd BLAST23

Keywords - Domaini

Zinc-finger

Phylogenomic databases

HOGENOMiHOG000222962.
InParanoidiQ753Q4.
KOiK03010.
OMAiRTQPHFE.
OrthoDBiEOG092C06IY.

Family and domain databases

CDDicd00653. RNA_pol_B_RPB2. 1 hit.
Gene3Di2.40.270.10. 2 hits.
2.40.50.150. 1 hit.
3.90.1110.10. 1 hit.
InterProiIPR015712. DNA-dir_RNA_pol_su2.
IPR007120. DNA-dir_RNA_pol_su2_6.
IPR007121. RNA_pol_bsu_CS.
IPR007644. RNA_pol_bsu_protrusion.
IPR007642. RNA_pol_Rpb2_2.
IPR007645. RNA_pol_Rpb2_3.
IPR007646. RNA_pol_Rpb2_4.
IPR007647. RNA_pol_Rpb2_5.
IPR007641. RNA_pol_Rpb2_7.
IPR014724. RNA_pol_RPB2_OB-fold.
[Graphical view]
PANTHERiPTHR20856. PTHR20856. 2 hits.
PfamiPF04563. RNA_pol_Rpb2_1. 1 hit.
PF04561. RNA_pol_Rpb2_2. 1 hit.
PF04565. RNA_pol_Rpb2_3. 1 hit.
PF04566. RNA_pol_Rpb2_4. 1 hit.
PF04567. RNA_pol_Rpb2_5. 1 hit.
PF00562. RNA_pol_Rpb2_6. 1 hit.
PF04560. RNA_pol_Rpb2_7. 1 hit.
[Graphical view]
PROSITEiPS01166. RNA_POL_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q753Q4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLEYYDDDAY VYDDDDEDAP ITAEDSWTVI SAFFREKGLV SQQLDSFNQF
60 70 80 90 100
INYTIQDLIL EDSTLILEQL AQHTTEADNI SRKYEISFGK IYLAKPSMTE
110 120 130 140 150
SDGVSHAMYP QEARLRNLTY ASGLFVEIKK RTYEAVDIPG RDLKYEIIQE
160 170 180 190 200
ESEDTEEGKI FIGRVPIMLR SKYCLLDDLS ESDLYRLKEC PFDMGGYFII
210 220 230 240 250
NGSEKVLIAQ ERSAGNIVQV FKKSAPSPIS HIAEIRSALE KGSRFISTLQ
260 270 280 290 300
VKLYGREGST SRTIKATLPY IKQDIPIVII FRALGIIPDG EILEHICYDQ
310 320 330 340 350
NDWQMLEMLK PCVEEGFVIQ DRETALDFIG RRGTALGIKK EKRIQYAKDI
360 370 380 390 400
LQKEFLPHIT QLEGFESRKA FFLGYMINRL LLCALDRKDQ DDRDHFGKKR
410 420 430 440 450
LDLAGPLLAQ LFKTLFRKLT RDILRFMQRS VEEAKDFNLK LAVKATTITA
460 470 480 490 500
GLKYALATGN WGEQKKAMSS RAGVSQVLNR YTYSSTLSHL RRTNTPIGRD
510 520 530 540 550
GKLAKPRQLH NTHWGLVCPA ETPEGQACGL VKNLSLMSCI SVGTDPVPII
560 570 580 590 600
TFLNEWGMEP LEDYVPHQSP DATRVFVNGV WHGIHRNPAR LVDTIRKLRR
610 620 630 640 650
KGDITAEVSI VRDIREKELK IFTDAGRVYR PLFVVADTQH ADGHKDLKVR
660 670 680 690 700
KGHIRKLMLT EYQDIEGGFE DEDINYTWTS LLNDGIVEYI DAEEEETILI
710 720 730 740 750
AMQQEDLDPS VPQTVDPSDE LDPARRIKAI HHSNTFTHCE IHPSMILGVA
760 770 780 790 800
ASVIPFPDHN QSPRNTYQSA MGKQAMGVFL TNYNVRMDTM ANILYYPQKP
810 820 830 840 850
LGTTRAMEYL KFRELPAGQN AIVAIACYSG YNQEDSMIMN QSSIDSGLFR
860 870 880 890 900
SLFFRSYMDQ EKRIGMSITE SFEKPHRTNT LRMKHGTYEK LDDDGLIAPG
910 920 930 940 950
VRVSGDDIII GKTTPIPPDA EELGQRTAFH SKRDASTPLR STENGIVDQV
960 970 980 990 1000
LITTNQEGLK FVKVRVRTTK VPQIGDKFAS RHGQKGTIGI TYRREDMPFT
1010 1020 1030 1040 1050
AEGVVPDLII NPHAIPSRMT VAHLIECLLS KVAALSGNEG DASPFTDITV
1060 1070 1080 1090 1100
DGISKLLREH GYQSRGFEVM YNGHTGKKLM AQIFFGPTYY QRLRHMVDDK
1110 1120 1130 1140 1150
IHARARGPMQ VLTRQPVEGR SRDGGLRFGE MERDCMIAHG AAAFLKERLM
1160 1170 1180 1190 1200
EASDAFRVHI CGICGLMTVV AKLKHNQFEC RGCKNKIDIY QVHIPYAAKL
1210 1220
LFQELMAMNI APRLYTDRSR DF
Length:1,222
Mass (Da):138,617
Last modified:July 5, 2004 - v1
Checksum:i7974639275076525
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016819 Genomic DNA. Translation: AAS53775.1.
AY497595 Genomic DNA. Translation: AAT12521.1.
RefSeqiNP_985951.1. NM_211306.1.

Genome annotation databases

EnsemblFungiiAAS53775; AAS53775; AGOS_AFR404C.
GeneIDi4622223.
KEGGiago:AGOS_AFR404C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016819 Genomic DNA. Translation: AAS53775.1.
AY497595 Genomic DNA. Translation: AAT12521.1.
RefSeqiNP_985951.1. NM_211306.1.

3D structure databases

ProteinModelPortaliQ753Q4.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiAAS53775; AAS53775; AGOS_AFR404C.
GeneIDi4622223.
KEGGiago:AGOS_AFR404C.

Phylogenomic databases

HOGENOMiHOG000222962.
InParanoidiQ753Q4.
KOiK03010.
OMAiRTQPHFE.
OrthoDBiEOG092C06IY.

Family and domain databases

CDDicd00653. RNA_pol_B_RPB2. 1 hit.
Gene3Di2.40.270.10. 2 hits.
2.40.50.150. 1 hit.
3.90.1110.10. 1 hit.
InterProiIPR015712. DNA-dir_RNA_pol_su2.
IPR007120. DNA-dir_RNA_pol_su2_6.
IPR007121. RNA_pol_bsu_CS.
IPR007644. RNA_pol_bsu_protrusion.
IPR007642. RNA_pol_Rpb2_2.
IPR007645. RNA_pol_Rpb2_3.
IPR007646. RNA_pol_Rpb2_4.
IPR007647. RNA_pol_Rpb2_5.
IPR007641. RNA_pol_Rpb2_7.
IPR014724. RNA_pol_RPB2_OB-fold.
[Graphical view]
PANTHERiPTHR20856. PTHR20856. 2 hits.
PfamiPF04563. RNA_pol_Rpb2_1. 1 hit.
PF04561. RNA_pol_Rpb2_2. 1 hit.
PF04565. RNA_pol_Rpb2_3. 1 hit.
PF04566. RNA_pol_Rpb2_4. 1 hit.
PF04567. RNA_pol_Rpb2_5. 1 hit.
PF00562. RNA_pol_Rpb2_6. 1 hit.
PF04560. RNA_pol_Rpb2_7. 1 hit.
[Graphical view]
PROSITEiPS01166. RNA_POL_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRPB2_ASHGO
AccessioniPrimary (citable) accession number: Q753Q4
Secondary accession number(s): Q6JEI5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: July 5, 2004
Last modified: September 7, 2016
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

The binding of ribonucleoside triphosphate to the RNA polymerase II transcribing complex probably involves a two-step mechanism. The initial binding seems to occur at the entry (E) site and involves a magnesium ion coordinated by three conserved aspartate residues of the two largest RNA Pol II subunits (By similarity).By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.