Q02061 (RPB2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
DNA-directed RNA polymerase II 138 kDa polypeptide

Gene names

Name:	rpb2
ORF Names:	SPAC23G3.01, SPAC521.06

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	1210 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	chromatin silencing by small RNA Inferred from mutant phenotype. Source: GeneDB_Spombe transcription from RNA polymerase II promoter Inferred from genetic interaction. Source: GeneDB_Spombe
Cellular component	DNA-directed RNA polymerase II, core complex Inferred from direct assay. Source: GeneDB_Spombe chromosome, centromeric region Inferred from direct assay. Source: GeneDB_Spombe cytosol Inferred from direct assay. Source: GeneDB_Spombe nuclear chromatin Inferred by curator. Source: GeneDB_Spombe
Molecular function	DNA binding Inferred from direct assay. Source: GeneDB_Spombe DNA-directed RNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from direct assay. Source: GeneDB_Spombe metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: GeneDB_Spombe ribonucleoside binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1210	1210	DNA-directed RNA polymerase II subunit RPB2		PRO_0000048090
Regions
	Zinc finger	1152 – 1173	22	C4-type
Sites
	Metal binding	826	1	Magnesium; shared with RPB1 By similarity
	Metal binding	1152	1	Zinc By similarity
	Metal binding	1155	1	Zinc By similarity
	Metal binding	1170	1	Zinc By similarity
	Metal binding	1173	1	Zinc By similarity
Experimental info
	Sequence conflict	727	1	W → R in BAA02600. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q02061 [UniParc]. Last modified August 14, 2001. Version 2. Checksum: C5D3794A743494CC	FASTA	1,210	137,849
	10 20 30 40 50 60 MSYEDYQYNE TLTQEDCWTV ISSFFEETSL ARQQLFSFDE FVQNTMQEIV DDDSTLTLDQ 70 80 90 100 110 120 YAQHTGAQGD VTRRYEINFG QIYLSRPTMT EADGSTTTMF PQEARLRNLT YSSPLYVDMR 130 140 150 160 170 180 KKVMVAADSN VPIGEEEWLV EEEDEEPSKV FIGKIPIMLR STFCILNGVS DSELYDLNEC 190 200 210 220 230 240 PYDQGGYFII NGSEKVIIAQ ERSAANIVQV FKKAAPSPIA YVAEIRSALE RGSRLISSMQ 250 260 270 280 290 300 IKLMARNTEN SGQTIRATLP YIRSDIPIVI VFRALGVVPD RDILEHICYD PNDFQMLEMM 310 320 330 340 350 360 KPCIEEAFVI QDKDIALDYI GKRGSTTGVT REKRLRYAHD ILQKELLPHI TTMEGFETRK 370 380 390 400 410 420 AFFLGYMIHR MLLCALERRE PDDRDHFGKK RLDLAGPLLA SLFRMLFRKM TRDVYKYMQK 430 440 450 460 470 480 CVETNREFNL TLAVKSNIIT NGLRYSLATG NWGDQKRSMV NRVGVSQVLN RYTFASTLSH 490 500 510 520 530 540 LRRTNTPIGR DGKLAKPRQL HNTHWGMVCP AETPEGQACG LVKNLSLMSY VSVGSPSAPI 550 560 570 580 590 600 IEFLEEWGLE TLEDYNPSAS PNATKVFVNG VWLGVHRDPA HLTETLRSLR RRLDISAEVS 610 620 630 640 650 660 IVRDIREKEL RLFTDAGRIC RPLFIVDNNP NSERRGELCI RKEHIQQLIE DKDRYDIDPE 670 680 690 700 710 720 QRFGWTALVS SGLIEYLDAE EEETVMIAMS PEDLEASRQM QAGYEVKEEL DPAQRVKPAP 730 740 750 760 770 780 NPHVHAWTHC EIHPAMILGI LASIIPFPDH NQSPRNTYQS AMGKQAMGVY LTNYQVRMDT 790 800 810 820 830 840 MANILYYPQK PLATTRSMEY LKFRELPAGQ NAIVAILCYS GYNQEDSIIM NQASIDRGLF 850 860 870 880 890 900 RSIFYRTYTD QEKKIGMTVM EEFERPVRST TLRMKHGTYD KLEDDGLIAP GTRVSGEDII 910 920 930 940 950 960 IGKTAPIPLD HEELGQRTQL HAKRDVSTPL RSTESGIVDQ VMVTTNQEGL KFVKVRMRST 970 980 990 1000 1010 1020 RIPQIGDKFA SRHGQKGTIG MTYRHEDMPF SAQGIVPDII INPHAIPSRM TVAHLVECQL 1030 1040 1050 1060 1070 1080 SKVSALSGFE GDATPFTDVT VEAVSKLLRS HGFQSRGFEV MYHGHTGRKL VAQVFLGPTY 1090 1100 1110 1120 1130 1140 YQRLKHLVDD KIHARARGPV QILTRQPVEG RSRDGGLRFG EMERDCQISH GCSSVLRERL 1150 1160 1170 1180 1190 1200 FDCSDAYRVI VCDICGLIAI ASYKKDSYEC RSCQNRTRFS QVYLPYAAKL LFQELMSMNI 1210 APRLFTKNHK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequence determination of the Schizosaccharomyces pombe rpb2 gene encoding the subunit 2 of RNA polymerase II." Kawagishi M., Yamagishi M., Ishihama A. Nucleic Acids Res. 21:469-473(1993) [PubMed: 8441660] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D13337 Genomic DNA. Translation: BAA02600.1.
CU329670 Genomic DNA. Translation: CAB86470.1.

PIR

S35548.
T50175.

RefSeq

NP_593101.2. NM_001018498.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3H0G	X-ray	3.65	B/N	1-1210	[»]

ProteinModelPortal

Q02061.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q02061. 3 interactions.

MINT

MINT-1214536.

STRING

Q02061.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

SPAC23G3.01.1; SPAC23G3.01.1:pep; SPAC23G3.01.

GeneID

2541446.

GenomeReviews

Gene locus rpb2 in contig CU329670_GR.

KEGG

spo:SPAC23G3.01.

Organism-specific databases

GeneDB_Spombe

SPAC23G3.01.

Phylogenomic databases

eggNOG

fuNOG05309.

GeneTree

EFGT00050000004610.

HOGENOM

HBG317648.

OMA

FGPTYYQ.

OrthoDB

EOG45HW5D.

Enzyme and pathway databases

BioCyc

SPOM-XXX-01:SPOM-XXX-01-001963-MONOMER.

Gene expression databases

ArrayExpress

Q02061.

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.
IPR014724. RNA_pol_RPB2_OB-fold.
[Graphical view]

Gene3D

G3DSA:2.40.270.10. G3DSA:2.40.270.10. 2 hits.
G3DSA:2.40.50.150. Ribosomal_L2. 1 hit.

KO

K03010.

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_SCHPO

Accession

Primary (citable) accession number: Q02061
Secondary accession number(s): Q9P7B1, Q9P7T2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	August 14, 2001
Last modified:	December 14, 2011
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program