Reviewed, UniProtKB/Swiss-Prot A5DHT2 (RPB2_PICGU)

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
ORF Names:	PGUG_02833

Organism

Pichia guilliermondii (Yeast) (Candida guilliermondii) [Complete proteome]

Taxonomic identifier

4929 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1236 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.
Sequence caution	The sequence ACE73644.1 differs from that shown. Reason: Frameshift at positions 594 and 601.

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 – 1236	1236	DNA-directed RNA polymerase II subunit RPB2		PRO_0000295037
Regions
	Zinc finger	1172 – 1194	23	C4-type
Sites
	Metal binding	846	1	Magnesium; shared with RPB1 By similarity
	Metal binding	1172	1	Zinc By similarity
	Metal binding	1175	1	Zinc By similarity
	Metal binding	1191	1	Zinc By similarity
	Metal binding	1194	1	Zinc By similarity
Natural variations
	Natural variant	401	1	D → A in strain: MmRL 1635. Ref.3
	Natural variant	519	1	A → V in strain: MmRL 1759. Ref.3
	Natural variant	722	1	S → T in strain: MmRL 1635 and MmRL 1759. Ref.3
	Natural variant	727	1	E → K in strain: MmRL 1636. Ref.3
Experimental info
	Sequence conflict	13	1	D → G in AAS67502. Ref.2
	Sequence conflict	1056	1	F → L in AAS67502. Ref.2
	Sequence conflict	1203	1	I → V in AAS67502. Ref.2
	Sequence conflict	1216	1	L → S in AAS67502. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	A5DHT2-1 [UniParc]. Last modified February 10, 2009. Version 3. Checksum: 111D7C5FC0DA5C52	FASTA	1,236	140,115
	10 20 30 40 50 60 MSDQASDPYM YDDDSSSITP EDCWTVISSF FQEKGLVSQQ LDSFDEFIES TIQELVWEDS 70 80 90 100 110 120 RLILDQPAQH TSEEDHENRR YEITFGKIYI SKPTQTEGDG TTHPMFPQEA RLRNLTYSSP 130 140 150 160 170 180 LYVDMTKRVL KSDDNAGNEH ELEWIEEEIK DEEPSTKVYL GKVPIMLRSK FCMLRDLGEH 190 200 210 220 230 240 EFYELKECPY DMGGYFVING SEKVLIAQER SAANIVQVFK KAAPSPISHV AEIRSALERG 250 260 270 280 290 300 SRLISSMQIK LYGREEKSTS NRTIKATLPY IKEDIPIVIV FRALGIVPDG DILEHICYDA 310 320 330 340 350 360 NDWQMLEMLK PCVEEGFVIQ EREVALDFIG RRGALGIKRE KRIQYAKDIL QKELLPNITQ 370 380 390 400 410 420 DEGFETRKAF FLGYMVNRLL LCALERKEPD DRDHFGKKRL DLAGPLLASL FRILFKKLTK 430 440 450 460 470 480 DIYNYMQRCV ENDKVFNLTL AVKSQTITDG LRYSLATGNW GEQKKAMSSR AGVSQVLNRY 490 500 510 520 530 540 TYSSTLSHLR RTNTPIGRDG KIAKPRQLHN THWGLVCPAE TPEGQACGLV KNLSLMSCIS 550 560 570 580 590 600 VGTPSEPILY FLEEWGMEPL EDYVPSNSPD STRVFVNGVW VGTHREPAHL VDTMRSLRRR 610 620 630 640 650 660 GDISPEVSII RDIREKEFKI FTDAGRVYRP LFIVDDDPES ETKGELKLQK EHIHKLLNAE 670 680 690 700 710 720 YSEEYATNEF GEEEGPYGWS SLVNDGVVEY VDAEEEETIM IAMTPEDLEA SKSSLTATQQ 730 740 750 760 770 780 KSLQLEEQEL DPAKRIKPTN SSTTSTFTHC EIHPSMILGV AASIIPFPDH NQSPRNTYQS 790 800 810 820 830 840 AMGKQAMGVF LTNYSVRMDT MANILYYPQK PLATTRAMEH LKFRELPAGQ NAIVAIACYS 850 860 870 880 890 900 GYNQEDSMIM NQSSIDRGLF RSLFFRTYMD LEKRQGMKAL ETFEKPSRSD TLRLKHGTYE 910 920 930 940 950 960 KLDDDGLIAP GIRVSGEDII IGKTTPIPPD TEELGQRTQY HTKRDASTPL RSTESGIVDQ 970 980 990 1000 1010 1020 VLLTTNGDGA KFVKVRMRTT KVPQIGDKFA SRHGQKGTVG VTYRHEDMPF TSQGIVPDLI 1030 1040 1050 1060 1070 1080 INPHAIPSRM TVAHLIECLL SKVSSLSGLE GDASPFTDVT AEAVSKLLRE HGYQSRGFEV 1090 1100 1110 1120 1130 1140 MYHGHTGKKL MAQVFFGPTY YQRLRHMVDD KIHARARGPV QVLTRQPVEG RSRDGGLRFG 1150 1160 1170 1180 1190 1200 EMERDCMIAH GAAGFLKERL MEASDAFRVH VCGVCGLMSV IANLKKNQFE CRSCKNKTNI 1210 1220 1230 YQIHIPYAAK LLFQELMAMN ISPRLYTERS GVSVRT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Evolution of pathogenicity and sexual reproduction in eight Candida genomes." Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S., Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I., Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C., Fitzpatrick D.A., de Groot P.W.J. , Harris D., Hoyer L.L., Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D., Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T., Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., Birren B.W., Kellis M., Cuomo C.A. Nature 459:657-662(2009) [PubMed: 19465905] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 6260 / CBS 566 / IFO 10279 / JCM 1539 / NRRL Y-324.
[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 1-1219.
[3]	"Phylogeny and evolution of medical species of Candida and related taxa: a multigenic analysis." Diezmann S., Cox C.J., Schoenian G., Vilgalys R.J., Mitchell T.G. J. Clin. Microbiol. 42:5624-5635(2004) [PubMed: 15583292] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 398-766, VARIANTS ALA-401; VAL-519; THR-722 AND LYS-727. Strain: ATCC 46036 / CBS 2030 / IFO 10106 / NRRL Y-2075, MMRL 1635, MMRL 1636 and MMRL 1759.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CH408157 Genomic DNA. Translation: EDK38735.2. Different initiation. AY485613 Genomic DNA. Translation: AAS67502.2. AY497607 Genomic DNA. Translation: AAT47725.1. AY497627 Genomic DNA. Translation: AAT12543.1. AY497628 Genomic DNA. Translation: AAT47730.2. AY497628 Genomic DNA. Translation: ACE73644.1. Frameshift. AY497629 Genomic DNA. Translation: AAT47731.1.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.7.7.6. 3704.
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_PICGU

Accession

Primary (citable) accession number: A5DHT2
Secondary accession number(s): B3DFH1 , Q6H184, Q6H185, Q6H190, Q6JEG3, Q6RYI5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 10, 2007
Last sequence update:	February 10, 2009
Last modified:	October 13, 2009
This is version 17 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)