[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 6260 / CBS 566 / IFO 10279 / JCM 1539 / NRRL Y-324; Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C., Kellis M., Rasmussen M.D., Grochow J.A., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K., LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J., Zeng Q., Kodira C.D., Yandava C., Alvarado L., O'Leary S., Reedy J., Heitman J.; "The genome sequence of Pichia guilliermondii ATCC 6260."; Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1219. DOI=10.1073/pnas.0400938101; PubMed=15070748 [NCBI, ExPASy, EBI, Israel, Japan] Liu Y.J., Hall B.D.; "Body plan evolution of ascomycetes, as inferred from an RNA polymerase II phylogeny."; Proc. Natl. Acad. Sci. U.S.A. 101:4507-4512(2004).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 398-766, AND 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; DOI=10.1128/JCM.42.12.5624-5635.2004; PubMed=15583292 [NCBI, ExPASy, EBI, Israel, Japan] Diezmann S., Cox C.J., Schoenian G., Vilgalys R.J., Mitchell T.G.; "Phylogeny and evolution of medical species of Candida and related taxa: a multigenic analysis."; J. Clin. Microbiol. 42:5624-5635(2004).

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: 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).
SIMILARITY: Belongs to the RNA polymerase beta chain family.
SEQUENCE CAUTION:
- Sequence=AAT47730.1; Type=Frameshift; Positions=594, 601;

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

CH408157; EDK38735.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY485613; AAS67502.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY497607; AAT47725.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY497627; AAT12543.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY497628; AAT47730.1; ALT_FRAME; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY497629; AAT47731.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

A5DHT2.

Ontologies

GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0003677;	Molecular function: DNA binding (inferred from electronic annotation from InterPro).
GO:0003899;	Molecular function: DNA-directed RNA polymerase activity (inferred from electronic annotation from InterPro).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006350;	Biological process: transcription (inferred from electronic annotation from InterPro).
QuickGo view.

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 of domain structure.

PANTHER

PTHR20856; RNA_pol_I_sub2; 1.

Pfam

PF04563; RNA_pol_Rpb2_1; 1.
PF04561; RNA_pol_Rpb2_2; 1.
PF04565; RNA_pol_Rpb2_3; 1.
PF04566; RNA_pol_Rpb2_4; 1.
PF04567; RNA_pol_Rpb2_5; 1.
PF00562; RNA_pol_Rpb2_6; 1.
PF04560; RNA_pol_Rpb2_7; 1.
Pfam graphical view of domain structure.

PROSITE

PS01166; RNA_POL_BETA; 1.

Other

ProtoNet

A5DHT2.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; DNA-directed RNA polymerase; Magnesium; Metal-binding; Nucleotidyltransferase; Nucleus; Transcription; Transferase; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 1236`	`1236`	`DNA-directed RNA polymerase II subunit RPB2.`	`PRO_0000295037`
`ZN_FING`	`1172 1194`	`23`	`C4-type.`
`METAL`	`846 846`		`Magnesium; shared with RPB1 (By similarity).`
`METAL`	`1172 1172`		`Zinc (By similarity).`
`METAL`	`1175 1175`		`Zinc (By similarity).`
`METAL`	`1191 1191`		`Zinc (By similarity).`
`METAL`	`1194 1194`		`Zinc (By similarity).`
`VARIANT`	`401 401`	`1`	`D -> A (in strain: MmRL 1635).`
`VARIANT`	`519 519`	`1`	`A -> V (in strain: MmRL 1759).`
`VARIANT`	`722 722`	`1`	`S -> T (in strain: MmRL 1635 and MmRL 1759).`
`VARIANT`	`727 727`	`1`	`E -> K (in strain: MmRL 1636).`
`CONFLICT`	`13 13`		`D -> G (in Ref. 2; AAS67502).`
`CONFLICT`	`1056 1056`		`F -> L (in Ref. 2; AAS67502).`
`CONFLICT`	`1203 1203`		`I -> V (in Ref. 2; AAS67502).`

Sequence information

Length: 1236 AA [This is the length of the unprocessed precursor]

Molecular weight: 140194 Da [This is the MW of the unprocessed precursor]

CRC64: 31F6C07ECFA7C2CD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSDQASDPYM YDDDSLSITP 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 DEEPLTKVYL 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 ETFEKPLRSD 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

A5DHT2 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools