ID RPB2_PICGU Reviewed; 1236 AA. AC A5DHT2; B3DFH1; Q6H184; Q6H185; Q6H190; Q6JEG3; Q6RYI5; DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 3. DT 16-JUN-2009, entry version 15. DE RecName: Full=DNA-directed RNA polymerase II subunit RPB2; DE Short=RNA polymerase II subunit B2; DE Short=RNA polymerase II subunit 2; DE EC=2.7.7.6; GN Name=RPB2; ORFNames=PGUG_02833; OS Pichia guilliermondii (Yeast) (Candida guilliermondii). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Pichia. OX NCBI_TaxID=4929; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 6260 / CBS 566 / IFO 10279 / JCM 1539 / NRRL Y-324; RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., RA Cuomo C., Kellis M., Rasmussen M.D., Grochow J.A., Jaffe D.B., RA Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., RA Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K., RA LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., RA Engels R., Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., RA White J., Zeng Q., Kodira C.D., Yandava C., Alvarado L., O'Leary S., RA Reedy J., Heitman J.; RT "The genome sequence of Pichia guilliermondii ATCC 6260."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1219. RX PubMed=15070748; DOI=10.1073/pnas.0400938101; RA Liu Y.J., Hall B.D.; RT "Body plan evolution of ascomycetes, as inferred from an RNA RT polymerase II phylogeny."; RL Proc. Natl. Acad. Sci. U.S.A. 101:4507-4512(2004). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 398-766, AND VARIANTS ALA-401; RP VAL-519; THR-722 AND LYS-727. RC STRAIN=ATCC 46036 / CBS 2030 / IFO 10106 / NRRL Y-2075, MMRL 1635, RC MMRL 1636, and MMRL 1759; RX PubMed=15583292; DOI=10.1128/JCM.42.12.5624-5635.2004; RA Diezmann S., Cox C.J., Schoenian G., Vilgalys R.J., Mitchell T.G.; RT "Phylogeny and evolution of medical species of Candida and related RT taxa: a multigenic analysis."; RL J. Clin. Microbiol. 42:5624-5635(2004). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription CC of DNA into RNA using the four ribonucleoside triphosphates as CC substrates. Second largest component of RNA polymerase II which CC synthesizes mRNA precursors and many functional non-coding RNAs. CC Proposed to contribute to the polymerase catalytic activity and CC forms the polymerase active center together with the largest CC subunit. Pol II is the central component of the basal RNA CC polymerase II transcription machinery. It is composed of mobile CC elements that move relative to each other. RPB2 is part of the CC core element with the central large cleft, the clamp element that CC moves to open and close the cleft and the jaws that are thought to CC grab the incoming DNA template (By similarity). CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). CC -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex CC consisting of 12 subunits (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). CC -!- MISCELLANEOUS: The binding of ribonucleoside triphosphate to the CC RNA polymerase II transcribing complex probably involves a two- CC step mechanism. The initial binding seems to occur at the entry CC (E) site and involves a magnesium ion coordinated by three CC conserved aspartate residues of the two largest RNA Pol II CC subunits (By similarity). CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family. CC -!- SEQUENCE CAUTION: CC Sequence=ACE73644.1; Type=Frameshift; Positions=594, 601; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH408157; EDK38735.2; ALT_INIT; Genomic_DNA. DR EMBL; AY485613; AAS67502.2; -; Genomic_DNA. DR EMBL; AY497607; AAT47725.1; -; Genomic_DNA. DR EMBL; AY497627; AAT12543.1; -; Genomic_DNA. DR EMBL; AY497628; AAT47730.2; -; Genomic_DNA. DR EMBL; AY497628; ACE73644.1; ALT_FRAME; Genomic_DNA. DR EMBL; AY497629; AAT47731.1; -; Genomic_DNA. DR BRENDA; 2.7.7.6; 3704. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW. DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0006350; P:transcription; IEA:UniProtKB-KW. DR InterPro; IPR015712; DNA-dir_RNA_pol_su2. DR InterPro; IPR007120; DNA-dir_RNA_pol_su2_6. DR InterPro; IPR007121; RNA_pol_bsu_CS. DR InterPro; IPR007644; RNA_pol_bsu_protrusion. DR InterPro; IPR007642; RNA_pol_Rpb2_2. DR InterPro; IPR007645; RNA_pol_Rpb2_3. DR InterPro; IPR007646; RNA_pol_Rpb2_4. DR InterPro; IPR007647; RNA_pol_Rpb2_5. DR InterPro; IPR007641; RNA_pol_Rpb2_7. DR PANTHER; PTHR20856; RNA_pol_I_sub2; 1. DR Pfam; PF04563; RNA_pol_Rpb2_1; 1. DR Pfam; PF04561; RNA_pol_Rpb2_2; 1. DR Pfam; PF04565; RNA_pol_Rpb2_3; 1. DR Pfam; PF04566; RNA_pol_Rpb2_4; 1. DR Pfam; PF04567; RNA_pol_Rpb2_5; 1. DR Pfam; PF00562; RNA_pol_Rpb2_6; 1. DR Pfam; PF04560; RNA_pol_Rpb2_7; 1. DR PROSITE; PS01166; RNA_POL_BETA; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-directed RNA polymerase; Magnesium; KW Metal-binding; Nucleotidyltransferase; Nucleus; Transcription; KW Transferase; Zinc; Zinc-finger. FT CHAIN 1 1236 DNA-directed RNA polymerase II subunit FT RPB2. FT /FTId=PRO_0000295037. FT ZN_FING 1172 1194 C4-type. FT METAL 846 846 Magnesium; shared with RPB1 (By FT similarity). FT METAL 1172 1172 Zinc (By similarity). FT METAL 1175 1175 Zinc (By similarity). FT METAL 1191 1191 Zinc (By similarity). FT METAL 1194 1194 Zinc (By similarity). FT VARIANT 401 401 D -> A (in strain: MmRL 1635). FT VARIANT 519 519 A -> V (in strain: MmRL 1759). FT VARIANT 722 722 S -> T (in strain: MmRL 1635 and MmRL FT 1759). FT VARIANT 727 727 E -> K (in strain: MmRL 1636). FT CONFLICT 13 13 D -> G (in Ref. 2; AAS67502). FT CONFLICT 1056 1056 F -> L (in Ref. 2; AAS67502). FT CONFLICT 1203 1203 I -> V (in Ref. 2; AAS67502). FT CONFLICT 1216 1216 L -> S (in Ref. 2; AAS67502). SQ SEQUENCE 1236 AA; 140115 MW; 111D7C5FC0DA5C52 CRC64; MSDQASDPYM YDDDSSSITP EDCWTVISSF FQEKGLVSQQ LDSFDEFIES TIQELVWEDS RLILDQPAQH TSEEDHENRR YEITFGKIYI SKPTQTEGDG TTHPMFPQEA RLRNLTYSSP LYVDMTKRVL KSDDNAGNEH ELEWIEEEIK DEEPSTKVYL GKVPIMLRSK FCMLRDLGEH EFYELKECPY DMGGYFVING SEKVLIAQER SAANIVQVFK KAAPSPISHV AEIRSALERG SRLISSMQIK LYGREEKSTS NRTIKATLPY IKEDIPIVIV FRALGIVPDG DILEHICYDA NDWQMLEMLK PCVEEGFVIQ EREVALDFIG RRGALGIKRE KRIQYAKDIL QKELLPNITQ DEGFETRKAF FLGYMVNRLL LCALERKEPD DRDHFGKKRL DLAGPLLASL FRILFKKLTK DIYNYMQRCV ENDKVFNLTL AVKSQTITDG LRYSLATGNW GEQKKAMSSR AGVSQVLNRY TYSSTLSHLR RTNTPIGRDG KIAKPRQLHN THWGLVCPAE TPEGQACGLV KNLSLMSCIS VGTPSEPILY FLEEWGMEPL EDYVPSNSPD STRVFVNGVW VGTHREPAHL VDTMRSLRRR GDISPEVSII RDIREKEFKI FTDAGRVYRP LFIVDDDPES ETKGELKLQK EHIHKLLNAE YSEEYATNEF GEEEGPYGWS SLVNDGVVEY VDAEEEETIM IAMTPEDLEA SKSSLTATQQ KSLQLEEQEL DPAKRIKPTN SSTTSTFTHC EIHPSMILGV AASIIPFPDH NQSPRNTYQS AMGKQAMGVF LTNYSVRMDT MANILYYPQK PLATTRAMEH LKFRELPAGQ NAIVAIACYS GYNQEDSMIM NQSSIDRGLF RSLFFRTYMD LEKRQGMKAL ETFEKPSRSD TLRLKHGTYE KLDDDGLIAP GIRVSGEDII IGKTTPIPPD TEELGQRTQY HTKRDASTPL RSTESGIVDQ VLLTTNGDGA KFVKVRMRTT KVPQIGDKFA SRHGQKGTVG VTYRHEDMPF TSQGIVPDLI INPHAIPSRM TVAHLIECLL SKVSSLSGLE GDASPFTDVT AEAVSKLLRE HGYQSRGFEV MYHGHTGKKL MAQVFFGPTY YQRLRHMVDD KIHARARGPV QVLTRQPVEG RSRDGGLRFG EMERDCMIAH GAAGFLKERL MEASDAFRVH VCGVCGLMSV IANLKKNQFE CRSCKNKTNI YQIHIPYAAK LLFQELMAMN ISPRLYTERS GVSVRT //