Q8SR75 (RPB2_ENCCU) 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

Gene names

Name:	RPB2
Ordered Locus Names:	ECU10_0250

Organism

Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite)

Taxonomic identifier

284813 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Microsporidia › Unikaryonidae › Encephalitozoon

Protein attributes

Sequence length	1141 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 Reference proteome
Gene Ontology (GO)
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 metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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 – 1141	1141	DNA-directed RNA polymerase II subunit RPB2		PRO_0000048087
Regions
	Zinc finger	1087 – 1106	20	C4-type
Sites
	Metal binding	763	1	Magnesium; shared with RPB1 By similarity
	Metal binding	1087	1	Zinc By similarity
	Metal binding	1090	1	Zinc By similarity
	Metal binding	1103	1	Zinc By similarity
	Metal binding	1106	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8SR75 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: B01FF9AA4B5A2217	FASTA	1,141	127,881
	10 20 30 40 50 60 MESAFTKEHS WSIISSFFEQ KGLVRQQLDS FDQFVKTKMQ EVINESPVII VQSAPTAGIE 70 80 90 100 110 120 TQKRIAVRFG QIYVSKPPVY TESDGRTITV FPNEARIRDL TYASPLFIDV TKETLSELGV 130 140 150 160 170 180 VDKHKYSRVP FGSLPVMLRS SYCVLYGLGD KDLIDLGECP YDQGGYFIVN GSEKVIVAQE 190 200 210 220 230 240 RMASNTVYVF KKAQPATYTH YAEIRSVPEK SSRNPSTLSM KLCRSPGVIR VSLPLVKQDV 250 260 270 280 290 300 PLFVLYRALG FLSDKEIIDH ILYEDDEEMF ELLKESIEEG TVVQDQNVAL DYIGKRSAPI 310 320 330 340 350 360 GTPQEKRIVM AKDLLAKEVL PHIGTQEFCE TKKAYFIGYI VQRLLLVALG RRNPDDRDHY 370 380 390 400 410 420 GKKRMDLSGP LLASLFRTLF KKLCVDTTRH MQKCIENGRE FNIALGLKAS IITQGFRYAL 430 440 450 460 470 480 ATGNWGDQAK AMQTRAGVAQ VLNRYNFVST LSHLRRVNTP IEKEGKLAAP RQLHNTHWGM 490 500 510 520 530 540 VCPAETPEGQ ACGLVKNLSL MAYISVGSSS GPLVEFLEEC GVESLEEIST SQLDAATKIF 550 560 570 580 590 600 VNGVWVGIHS DPVGLIKSLK LLRRSLEMDK EVSIVRDIRE KEIRVQSDAG RPCRPLLVVK 610 620 630 640 650 660 DNKLVITAED IRKLKRGEIK WDNLVTSGFI EFLDVEEEEM SMIAMNTKIL ADESRNSSDV 670 680 690 700 710 720 SVSYTHCEIH PALILGICAS TIPFPDHNQS PRNTYQSAMG KQAMGIYATN FLLRMDTLSN 730 740 750 760 770 780 ILFYPQKPLV TTKSMEYLRF KELPSGQNAL VAIACYSGYN QEDSIIMNQS AIDRGLFRSF 790 800 810 820 830 840 FYRTYTDQES MSRPGVNEEF CKPSRGAVLR MKNLNYNKLD DDGLISPGTR VTGDDVLIGK 850 860 870 880 890 900 ITPILDPERS TKEAPVYVYK DSSTAMRRTE TGIVDTVIVT NKDGYKFSKV KVRSGRIPQM 910 920 930 940 950 960 GDKFASRHAQ KGTIGITLRQ EDMPFTSEGI VPDIIINPHA IPSRMTIGHL IECLLGKVSA 970 980 990 1000 1010 1020 MSGEEGDATP FSGVTVDGIS SRLKSYGFQQ RGLEVMYNGM TGRKLRAQMF FGPTYYQRLK 1030 1040 1050 1060 1070 1080 HMVDDKIHAR ARGPLQILTR QPVEGRSRDG GLRFGEMERD CIISHGASAF LKERLMDVSD 1090 1100 1110 1120 1130 1140 AYSCYVCDFC GLLAMGGSKV NECKGCNNTT NVSMVEIPYA FKLLIQELMG MNIAPRIRFE E

References

[1]

"Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi." Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F., Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P., Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J., Vivares C.P. Nature 414:450-453(2001) [PubMed: 11719806] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: GB-M1.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL590449 Genomic DNA. Translation: CAD25744.1.
RefSeq	NP_586140.1. NM_001041973.1.
3D structure databases
ProteinModelPortal	Q8SR75.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8SR75.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	859788.
GenomeReviews	Gene locus ECU10_0250 in contig AL590449_GR.
KEGG	ecu:ECU10_0250.
NMPDR	fig|6035.1.peg.1254.
Organism-specific databases
EuPathDB	EupathDB:ECU10_0250.
Phylogenomic databases
eggNOG	fuNOG05309.
HOGENOM	HBG317648.
OMA	FGPTYYQ.
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_ENCCU

Accession

Primary (citable) accession number: Q8SR75

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	June 1, 2002
Last modified:	December 14, 2011
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program