ID   RPB2_CAEEL              Reviewed;        1193 AA.
AC   Q10578;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   16-JUN-2009, entry version 59.
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=rbp-2; ORFNames=C26E6.4;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 200-1058.
RX   MEDLINE=95041334; PubMed=7953533; DOI=10.1016/S0960-9822(00)00131-7;
RA   Sidow A., Thomas W.K.;
RT   "A molecular evolutionary framework for eukaryotic model organisms.";
RL   Curr. Biol. 4:596-603(1994).
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.
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DR   EMBL; U13875; AAA21158.1; -; Genomic_DNA.
DR   EMBL; U10333; AAA50224.1; -; mRNA.
DR   PIR; E88445; E88445.
DR   PIR; T43701; T43701.
DR   RefSeq; NP_498047.1; -.
DR   UniGene; Cel.7716; -.
DR   HSSP; P08518; 1I50.
DR   Ensembl; C26E6.4; Caenorhabditis elegans.
DR   GeneID; 175668; -.
DR   KEGG; cel:C26E6.4; -.
DR   NMPDR; fig|6239.3.peg.9616; -.
DR   WormBase; WBGene00016140; rbp-2.
DR   WormPep; C26E6.4; CE01162.
DR   OMA; Q10578; FGPTYYQ.
DR   BRENDA; 2.7.7.6; 672.
DR   NextBio; 889138; -.
DR   ArrayExpress; Q10578; -.
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:0008340; P:determination of adult life span; IMP:WormBase.
DR   GO; GO:0009792; P:embryonic development ending in birth or eg...; IMP:WormBase.
DR   GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR   GO; GO:0040010; P:positive regulation of growth rate; IMP:WormBase.
DR   GO; GO:0000003; P:reproduction; IMP:WormBase.
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   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   1193       DNA-directed RNA polymerase II subunit
FT                                RPB2.
FT                                /FTId=PRO_0000048083.
FT   ZN_FING    1125   1146       C4-type.
FT   METAL       798    798       Magnesium; shared with RPB1 (By
FT                                similarity).
FT   METAL      1125   1125       Zinc (By similarity).
FT   METAL      1128   1128       Zinc (By similarity).
FT   METAL      1143   1143       Zinc (By similarity).
FT   METAL      1146   1146       Zinc (By similarity).
SQ   SEQUENCE   1193 AA;  134905 MW;  B8A85E74E9CC7EBE CRC64;
     MYDDEDEMVN DPMDGDYIDD SDEISAEAWQ EACWVVISAY FDEKGLVRQQ LDSFDEFVQM
     NVQRIVEDSP PVELQSENQH LGTDMENPAK FSLKFNQIYL SKPTHWEKDG APMPMMPNEA
     RLRNLTYASP LYVDITKVVT RDDSATEKVY DKVFVGKVPV MLRSSYCMLS NMTDRDLTEL
     NECPLDPGGY FVINGSEKVL IAQEKMATNT VYVFSMKDGK YAFKTECRSC LENSSRPTST
     MWVNMLARGG GGGKKTAMGQ RIIGILPYIK QEIPIMIVFR ALGFVSDRDI LGHIIYDFND
     PEMMEMVKPS LDEAFVIQEQ NVALNFIGAR GAKPGVTREQ RIKYAREILQ KELLPHVGVS
     EHCETKKAFF IGYMVHRLLL AALGRRELDD RDHIGNKRLD LAGPLLAFLF RSLFRNLLKE
     MRMTAQKYIN KNDDFALDVC VKTSTITRGL TYSLATGNWG DQKKAHQSRA GVSQVLNRLT
     YTATLSHLRR ANSPIGREGK LAKPRQLHNT QWGMVCPAET PEGQAVGLVK NLALMAYISV
     GSLPEPILEF LEEWSMENLE EVSPSAIADA TKIFVNGAWV GIHREPDQLM TTLKKLRRQM
     DIIVSEVSMV RDIRDREIRI YTDAGRVCRP LLIVENQKLA LKKRHIDQLK EAADEANKYT
     WSDLVGGGVV ELIDSMEEET SMIAMMPEDL RSGGYCDTHT HCEIHPAMIL GVCASIIPFP
     DHNQSPRNTY QSAMGKQAMG VYTTNFHVRM DTLAHVLYYP QKPLVTTRSM EYLRFNELPA
     GINAIVAILS YSGYNQEDSV IMNNSAIDRG LFRSVFYRSY RDNEANLDNA NEELIEKPTR
     EKCSGMRHSL YDKLDEDGII SPGMRVSGDD VIIGKTVALP DIDDDLDASG KKYPKRDAST
     FLRSSETGIV DQVMLSLNSD GNKFVKIRMR SVRLPQIGDK FASRHGQKGT MGIMYRQEDM
     PFTAEGLTPD IIINPHAVPS RMTIGHLIEC LQGKLSANKG EIGDATPFND TVNVQKISGL
     LCEYGYHLRG NEVMYNGHTG KKLTTQIFFG PTYYQRLKHM VDDKIHSRAR GPIQMMNRQP
     MEGRARDGGL RFGEMERDCQ ISHGATQFLR ERLFEVSDPY HVYVCNNCGL IVVANLRTNS
     FECKACRNKT QVSAVRIPYA CKLLFQELMS MSIAPRLMVK PRQSKRSKHQ SEA
//