ID   RPB2_DROME              Reviewed;        1176 AA.
AC   P08266; Q04155; Q95027; Q9VFM7;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   16-JUN-2009, entry version 93.
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;
DE   AltName: Full=DNA-directed RNA polymerase II 140 kDa polypeptide;
GN   Name=RpII140; ORFNames=CG3180;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Embryo;
RX   MEDLINE=88011299; PubMed=3116266; DOI=10.1016/0022-2836(87)90496-7;
RA   Falkenburg D., Dworniczak B., Faust D.M., Bautz E.K.F.;
RT   "RNA polymerase II of Drosophila. Relation of its 140,000 Mr subunit
RT   to the beta subunit of Escherichia coli RNA polymerase.";
RL   J. Mol. Biol. 195:929-937(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RX   MEDLINE=22426069; PubMed=12537572;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   MEDLINE=22426066; PubMed=12537569;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69.
RC   TISSUE=Embryo;
RX   MEDLINE=91276237; PubMed=1905256; DOI=10.1016/0378-1119(91)90361-E;
RA   Sitzler S., Oldenburg I., Petersen G., Bautz E.K.F.;
RT   "Analysis of the promoter region of the housekeeping gene DmRP140 by
RT   sequence comparison of Drosophila melanogaster and Drosophila
RT   virilis.";
RL   Gene 100:155-162(1991).
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=CAA29180.2; Type=Frameshift; Positions=43; Note=The frameshift leads to an erroneous gene model prediction;
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DR   EMBL; X05709; CAA29180.2; ALT_FRAME; Genomic_DNA.
DR   EMBL; AE014297; AAF55024.1; -; Genomic_DNA.
DR   EMBL; BT003265; AAO25022.1; -; mRNA.
DR   EMBL; M62972; AAA28476.1; -; Genomic_DNA.
DR   PIR; A27826; A27826.
DR   RefSeq; NP_476706.1; -.
DR   UniGene; Dm.6926; -.
DR   HSSP; P08518; 1I50.
DR   DIP; DIP:17498N; -.
DR   IntAct; P08266; 3.
DR   Ensembl; FBgn0003276; Drosophila melanogaster.
DR   GeneID; 41721; -.
DR   KEGG; dme:Dmel_CG3180; -.
DR   NMPDR; fig|7227.3.peg.12716; -.
DR   FlyBase; FBgn0003276; RpII140.
DR   HOGENOM; P08266; -.
DR   OMA; P08266; FGPTYYQ.
DR   BioCyc; DMEL-XXX-02:DMEL-XXX-02-011546-MON; -.
DR   BRENDA; 2.7.7.6; 48.
DR   NextBio; 825231; -.
DR   ArrayExpress; P08266; -.
DR   GermOnline; CG3180; Drosophila melanogaster.
DR   GO; GO:0005665; C:DNA-directed RNA polymerase II, core complex; NAS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003899; F:DNA-directed RNA polymerase activity; NAS:UniProtKB.
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:0006366; P:transcription from RNA polymerase II promoter; NAS:UniProtKB.
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   2: Evidence at transcript level;
KW   Complete proteome; DNA-directed RNA polymerase; Magnesium;
KW   Metal-binding; Nucleotidyltransferase; Nucleus; Transcription;
KW   Transferase; Zinc; Zinc-finger.
FT   CHAIN         1   1176       DNA-directed RNA polymerase II subunit
FT                                RPB2.
FT                                /FTId=PRO_0000048084.
FT   ZN_FING    1121   1142       C4-type.
FT   METAL       794    794       Magnesium; shared with RPB1 (By
FT                                similarity).
FT   METAL      1121   1121       Zinc (By similarity).
FT   METAL      1124   1124       Zinc (By similarity).
FT   METAL      1139   1139       Zinc (By similarity).
FT   METAL      1142   1142       Zinc (By similarity).
FT   CONFLICT     72     72       A -> R (in Ref. 1; CAA29180).
FT   CONFLICT    666    667       ID -> MY (in Ref. 1; CAA29180).
SQ   SEQUENCE   1176 AA;  134043 MW;  224821B335BED7F0 CRC64;
     MMYDNEEELY EEENAEEISH ELWQEACWIV INAYFDEKGL VRQQLDSFDE FIQMSVQRIV
     EDSPAIELQA EAQHTSGEVE TPPRFSLKFE QIYLSKPTHW EKDGSPSPMM PNEARLRNLT
     YSAPLYVDIT KTKNVEGLDP VETQHQKTFI GKIPIMLRST YCLLSQLTDR DLTELNECPL
     DPGGYFIING SEKVLIAQEK MATNTVYVFS MKDGKYAFKT EIRSCLEHSS RPTSTLWVNM
     MARGSQNIKK SAIGQRIIAI LPYIKQEIPI MIVFRALGFV ADRDILEHII YDFDDPEMME
     MVKPSLDEAF VVQEQNVALN FIGARGARPG VTKDKRIKYA KEILQKEMLP HVGVSDFCET
     KKAYFLGYMV HRLLLASLGR RELDDRDHYG NKRLDLAGPL LAFLFRGLFK NLMKEVRMYT
     QKFIDRGKDF NLELAIKTNI ITDGLRYSLA TGNWGDQKKA HQARAGVSQV LNRLTFASTL
     SHLRRVNSPI GRDGKLAKPR QLHNTLWGML CPAETPEGAA VGLVKNLALM AYISVGSQPS
     PILEFLEEWS MENLEEIAPS AIADATKIFV NGCWVGIHRD PEQLMATLRK LRRQMDIIVS
     EVSMIRDIRD REIRIYTDAG RICRPLLIVE NGSLLLKKTH VEMLKERDYN NYSWQVLVAS
     GVVEYIDTLE EETVMIAMSP YDLKQDKDYA YCTTYTHCEI HPAMILGVCA SIIPFPDHNQ
     SPRNTYQSAM GKQAMGVYIT NFHVRMDTLA HVLYYPMKPL VTTRSMEYLR FRELPAGINS
     IVAILCYTGY NQEDSVILNA SAVERGFFRS VFYRSYKDSE NKRVGDQEEN FEKPHRGTCQ
     GMRNAHYDKL DDDGIIAPGI RVSGDDVVIG KTITLPENDD ELDSNTKRFS KRDASTFLRN
     SETGIVDQVM LTLNSEGYKF CKIRVRSVRI PQIGDKFASR HGQKGTCGIQ YRQEDMAFTC
     EGLAPDIIIN PHAIPSRMTI GHLIECLQGK LGSNKGEIGD ATPFNDAVNV QKISTFLQEY
     GYHLRGNEVM YNGHTGRKIN AQVFLGPTYY QRLKHMVDDK IHSRARGPVQ ILVRQPMEGR
     ARDGGLRFGE MERDCQISHG AAQFLRERLF EVSDPYRVHI CNFCGLIAIA NLRNNTFECK
     GCKNKTQISQ VRLPYAAKLL FQELMSMNIA PRLMVT
//