Reviewed, UniProtKB/Swiss-Prot Q753Q4 (RPB2_ASHGO)

Names and origin

Protein names

Recommended name:
    DNA-directed RNA polymerase II subunit RPB2
      Short name=RNA polymerase II subunit B2
      Short name=RNA polymerase II subunit 2
    EC=2.7.7.6

Gene names

Name:	RPB2
Ordered Locus Names:	AFR404C

Organism

Ashbya gossypii (Yeast) (Eremothecium gossypii) [Complete proteome]

Taxonomic identifier

33169 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Eremothecium

Protein attributes

Sequence length	1222 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	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.
Catalytic activity	Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
Subunit structure	Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits By similarity.
Subcellular location	Nucleus By similarity.
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.
Sequence similarities	Belongs to the RNA polymerase beta chain family.

Ontologies

Keywords
Biological process	Transcription
Cellular component	DNA-directed RNA polymerase Nucleus
Domain	Zinc-finger
Ligand	Magnesium Metal-binding Zinc
Molecular function	Nucleotidyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro DNA-directed RNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW ribonucleoside binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1222	1222	DNA-directed RNA polymerase II subunit RPB2		PRO_0000048088
Regions
	Zinc finger	1161 – 1183	23	C4-type
Sites
	Metal binding	835	1	Magnesium; shared with RPB1 By similarity
	Metal binding	1161	1	Zinc By similarity
	Metal binding	1164	1	Zinc By similarity
	Metal binding	1180	1	Zinc By similarity
	Metal binding	1183	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q753Q4-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 7974639275076525	FASTA	1,222	138,617
	10 20 30 40 50 60 MLEYYDDDAY VYDDDDEDAP ITAEDSWTVI SAFFREKGLV SQQLDSFNQF INYTIQDLIL 70 80 90 100 110 120 EDSTLILEQL AQHTTEADNI SRKYEISFGK IYLAKPSMTE SDGVSHAMYP QEARLRNLTY 130 140 150 160 170 180 ASGLFVEIKK RTYEAVDIPG RDLKYEIIQE ESEDTEEGKI FIGRVPIMLR SKYCLLDDLS 190 200 210 220 230 240 ESDLYRLKEC PFDMGGYFII NGSEKVLIAQ ERSAGNIVQV FKKSAPSPIS HIAEIRSALE 250 260 270 280 290 300 KGSRFISTLQ VKLYGREGST SRTIKATLPY IKQDIPIVII FRALGIIPDG EILEHICYDQ 310 320 330 340 350 360 NDWQMLEMLK PCVEEGFVIQ DRETALDFIG RRGTALGIKK EKRIQYAKDI LQKEFLPHIT 370 380 390 400 410 420 QLEGFESRKA FFLGYMINRL LLCALDRKDQ DDRDHFGKKR LDLAGPLLAQ LFKTLFRKLT 430 440 450 460 470 480 RDILRFMQRS VEEAKDFNLK LAVKATTITA GLKYALATGN WGEQKKAMSS RAGVSQVLNR 490 500 510 520 530 540 YTYSSTLSHL RRTNTPIGRD GKLAKPRQLH NTHWGLVCPA ETPEGQACGL VKNLSLMSCI 550 560 570 580 590 600 SVGTDPVPII TFLNEWGMEP LEDYVPHQSP DATRVFVNGV WHGIHRNPAR LVDTIRKLRR 610 620 630 640 650 660 KGDITAEVSI VRDIREKELK IFTDAGRVYR PLFVVADTQH ADGHKDLKVR KGHIRKLMLT 670 680 690 700 710 720 EYQDIEGGFE DEDINYTWTS LLNDGIVEYI DAEEEETILI AMQQEDLDPS VPQTVDPSDE 730 740 750 760 770 780 LDPARRIKAI HHSNTFTHCE IHPSMILGVA ASVIPFPDHN QSPRNTYQSA MGKQAMGVFL 790 800 810 820 830 840 TNYNVRMDTM ANILYYPQKP LGTTRAMEYL KFRELPAGQN AIVAIACYSG YNQEDSMIMN 850 860 870 880 890 900 QSSIDSGLFR SLFFRSYMDQ EKRIGMSITE SFEKPHRTNT LRMKHGTYEK LDDDGLIAPG 910 920 930 940 950 960 VRVSGDDIII GKTTPIPPDA EELGQRTAFH SKRDASTPLR STENGIVDQV LITTNQEGLK 970 980 990 1000 1010 1020 FVKVRVRTTK VPQIGDKFAS RHGQKGTIGI TYRREDMPFT AEGVVPDLII NPHAIPSRMT 1030 1040 1050 1060 1070 1080 VAHLIECLLS KVAALSGNEG DASPFTDITV DGISKLLREH GYQSRGFEVM YNGHTGKKLM 1090 1100 1110 1120 1130 1140 AQIFFGPTYY QRLRHMVDDK IHARARGPMQ VLTRQPVEGR SRDGGLRFGE MERDCMIAHG 1150 1160 1170 1180 1190 1200 AAAFLKERLM EASDAFRVHI CGICGLMTVV AKLKHNQFEC RGCKNKIDIY QVHIPYAAKL 1210 1220 LFQELMAMNI APRLYTDRSR DF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome." Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P. Science 304:304-307(2004) [PubMed: 15001715] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.
[2]	"Molecular phylogeny and evolution of Candida and related species within the order saccharomycetales as inferred from multilocus sequence analysis." Diezmann S., Cox C.J., Schoenian G., Vilgalys R.J., Mitchell T.G. Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 399-755. Strain: ATCC 8717 / IMI 31268.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016819 Genomic DNA. Translation: AAS53775.1. AY497595 Genomic DNA. Translation: AAT12521.1.
RefSeq	NP_985951.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q753Q4.
Genome annotation databases
GeneID	4622223.
GenomeReviews	Gene locus AFR404C in contig AE016819_GR.
KEGG	ago:AGOS_AFR404C.
NMPDR	fig|33169.1.peg.3596.
Organism-specific databases
AGD	AFR404C.
Phylogenomic databases
eggNOG	fuNOG05309.
HOGENOM	HBG317648.
OMA	FGPTYYQ.
OrthoDB	EOG9F4TT7.
Enzyme and pathway databases
BRENDA	2.7.7.6. 279361.
Family and domain databases
InterPro	IPR015712. 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. [Graphical view]
PANTHER	PTHR20856. RNA_pol_I_sub2. 1 hit.
Pfam	PF04563. 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]
PROSITE	PS01166. RNA_POL_BETA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RPB2_ASHGO

Accession

Primary (citable) accession number: Q753Q4
Secondary accession number(s): Q6JEI5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	July 5, 2004
Last modified:	January 19, 2010
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)