Reviewed, UniProtKB/Swiss-Prot Q6FLD5 (RPB2_CANGA)

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:	CAGL0L04246g

Organism

Candida glabrata (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

5478 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces

Protein attributes

Sequence length	1223 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 – 1223	1223	DNA-directed RNA polymerase II subunit RPB2		PRO_0000048089
Regions
	Zinc finger	1162 – 1184	23	C4-type
Sites
	Metal binding	836	1	Magnesium; shared with RPB1 By similarity
	Metal binding	1162	1	Zinc By similarity
	Metal binding	1165	1	Zinc By similarity
	Metal binding	1181	1	Zinc By similarity
	Metal binding	1184	1	Zinc By similarity
Experimental info
	Sequence conflict	208	1	K → C Ref.2
	Sequence conflict	211	1	I → H Ref.2
	Sequence conflict	739	1	H → L in AAT12525. Ref.3
	Sequence conflict	1092	1	Q → G Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q6FLD5-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 50DF19BAC27C1E63	FASTA	1,223	138,714
	10 20 30 40 50 60 MSADNEDYYD EDPYGFEEEN APITAEDTWA VISAFFREKG LVSQQLDSFN QFVDYTLQDI 70 80 90 100 110 120 ISEDSTLILE QLAQHTTEQD NISRKYEISF GKIYVTKPMV NESDGVTHAL YPQEARLRNL 130 140 150 160 170 180 TYSSGLFVDV TKRTYEAVDV PGRDLNYQLI AEESEEDSES GKVFIGRLPI MLRSKNCYLS 190 200 210 220 230 240 DATESDLYKL KECPFDMGGY FIINGSEKVL IAQERSAGNI VQVFKKAAPS PISHVAEIRS 250 260 270 280 290 300 ALEKGSRFIS TLQVKLYGRE SSSARTIKAT LPYIKQDIPI VIIFRALGII PDGEILEHIC 310 320 330 340 350 360 YDVNDWQMLE MLKPCVEDGF VIQDRETALD FIGRRGTALG IKKEKRIQYA KDILQKEFLP 370 380 390 400 410 420 HITQLEGFES RKAFFLGYMI NRLLLCALDR KDQDDRDHFG KKRLDLAGPL LAQLFKTLFR 430 440 450 460 470 480 KLTKDIFRYM QRTVEEANDF NMKLAINAKT ITSGLKYALA TGNWGEQKKA MSSRAGVSQV 490 500 510 520 530 540 LNRYTYSSTL SHLRRTNTPI GRDGKLAKPR QLHNTHWGLV CPAETPEGQA CGLVKNLSLM 550 560 570 580 590 600 SCISVGADPM PIITFLSEWG MEPLEDYVPH QSPDATRVFV NGVWHGVHRN PARLMETLRT 610 620 630 640 650 660 LRRKGDINPE VSMIRDIREQ ELKIFTDAGR VYRPLFIVED DEELGRKELK VRKGHVAKLM 670 680 690 700 710 720 ATEYQDIEGG FEDAEDYTWS SLLNEGLVEY IDAEEEESIL IAMQPEDLEP TAVEQDIPKE 730 740 750 760 770 780 NVDLAKRIKV THHATTFTHC EIHPSMILGV AASIIPFPDH NQSPRNTYQS AMGKQAMGVF 790 800 810 820 830 840 LTNYNFRMDT MANILYYPQK PLGTTRAMEY LKFRELPAGQ NAIVAIACYS GYNQEDSMIM 850 860 870 880 890 900 NQSSIDRGLF RSLFFRSYMD QEKKYGMSIT ETFEKPQRTN TLRMKHGTYD KLDEDGLIAP 910 920 930 940 950 960 GVRVSGEDII IGKTTPIAPD EEELGQRTAY HSKRDASTPL RSTENGIVDQ VLITTNQDGL 970 980 990 1000 1010 1020 KFVKVRVRTT KVPQIGDKFA SRHGQKGTIG ITYRREDMPF TAEGIVPDLI INPHAIPSRM 1030 1040 1050 1060 1070 1080 TVAHLIECLL SKVAALSGNE GDASPFTDIT VEGISKLLRE HGYQSRGFEV MYNGHTGKKL 1090 1100 1110 1120 1130 1140 MAQIFFGPTY YQRLRHMVDD KIHARARGPM QVLTRQPVEG RSRDGGLRFG EMERDCMIAH 1150 1160 1170 1180 1190 1200 GAAAFLKERL MEASDAFRVH ICGICGLMSV IAKLNHNQFE CKGCDNKIDI YQIHIPYAAK 1210 1220 LLFQELMAMN ITPRLYTDRS RDF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65.
[2]	"Body plan evolution of ascomycetes, as inferred from an RNA polymerase II phylogeny." Liu Y.J., Hall B.D. Proc. Natl. Acad. Sci. U.S.A. 101:4507-4512(2004) [PubMed: 15070748] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 208-1092.
[3]	"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 402-756. Strain: ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR380958 Genomic DNA. Translation: CAG61929.1. AY485612 Genomic DNA. Translation: AAS67501.1. AY497601 Genomic DNA. Translation: AAT12525.1.
RefSeq	XP_448959.1.
3D structure databases
SMR	Q6FLD5. Positions 16-1223.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6FLD5.
Genome annotation databases
GeneID	2890773.
GenomeReviews	Gene locus CAGL0L04246g in contig CR380958_GR.
KEGG	cgr:CAGL0L04246g.
Phylogenomic databases
HOGENOM	Q6FLD5.
OMA	FGPTYYQ.
Enzyme and pathway databases
BRENDA	2.7.7.6. 189220.
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_CANGA

Accession

Primary (citable) accession number: Q6FLD5
Secondary accession number(s): Q6JEI1, Q6RYI6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	July 19, 2004
Last modified:	November 3, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)