(data stored in ACNUC11299 zone)

HOGENOM: ENCUN1_2_PE28

ID   ENCUN1_2_PE28                        STANDARD;      PRT;   1599 AA.
AC   ENCUN1_2_PE28; Q8SSC4;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=DNA-directed RNA polymerase II subunit RPB1; Short=RNA
DE   polymerase II subunit 1; Short=RNA polymerase II subunit B1; EC=2.7.7
DE   6;AltName: Full=DNA-directed RNA polymerase III largest subunit;
DE   (ENCUN1_2.PE28).
GN   Name=RPB1; OrderedLocusNames=ECU03_0290;
OS   ENCEPHALITOZOON CUNICULI GB-M1.
OC   Eukaryota; Fungi; Microsporidia; Unikaryonidae; Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ENCUN1_2.PE28.
CC       Encephalitozoon cuniculi (strain GB-M1) chromosome III, complete sequen
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:RPB1_ENCCU
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription
CC       of DNA into RNA using the four ribonucleoside triphosphates as
CC       substrates. Largest and catalytic component of RNA polymerase II
CC       which synthesizes mRNA precursors and many functional non-coding
CC       RNAs. Forms the polymerase active center together with the second
CC       largest 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. RPB1 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. At the start of transcription, a
CC       single stranded DNA template strand of the promoter is positioned
CC       within the central active site cleft of Pol II. A bridging helix
CC       emanates from RPB1 and crosses the cleft near the catalytic site
CC       and is thought to promote translocation of Pol II by acting as a
CC       ratchet that moves the RNA-DNA hybrid through the active site by
CC       switching from straight to bent conformations at each step of
CC       nucleotide addition. During transcription elongation, Pol II moves
CC       on the template as the transcript elongates. Elongation is
CC       influenced by the phosphorylation status of the C-terminal domain
CC       (CTD) of Pol II largest subunit (RPB1), which serves as a platform
CC       for assembly of factors that regulate transcription initiation,
CC       elongation, termination and mRNA processing (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   -!- PTM: The tandem 7 residues repeats in the C-terminal domain (CTD)
CC       can be highly phosphorylated. The phosphorylation activates Pol
CC       II. Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5'
CC       of the heptapepdtide repeat. The phosphorylation state is believed
CC       to result from the balanced action of site-specific CTD kinases
CC       and phosphataes, and a "CTD code" that specifies the position of
CC       Pol II within the transcription cycle has been proposed (By
CC       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 temporarily coordinated by
CC       three conserved aspartate residues of the two largest RNA Pol II
CC       subunits. The ribonucleoside triphosphate is transferred by a
CC       rotation to the nucelotide addition (A) site for pairing with the
CC       template DNA. The catalytic A site involves three conserved
CC       aspartate residues of the RNA Pol II largest subunit which
CC       permanently coordinate a second magnesium ion.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC   -!- GENE_FAMILY: HOG000222975 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q8SSC4; -.
DR   EMBL; AL590443; CAD26175.1; -; Genomic_DNA.
DR   RefSeq; NP_597540.1; NM_001040904.1.
DR   ProteinModelPortal; Q8SSC4; -.
DR   STRING; Q8SSC4; -.
DR   GeneID; 858702; -.
DR   GenomeReviews; AL590443_GR; ECU03_0290.
DR   KEGG; ecu:ECU03_0290; -.
DR   NMPDR; fig|6035.1.peg.185; -.
DR   EuPathDB; EupathDB:ECU03_0290; -.
DR   eggNOG; fuNOG04507; -.
DR   OMA; SPTSPHY; -.
DR   PhylomeDB; Q8SSC4; -.
DR   GO; GO:0005665; C:DNA-directed RNA polymerase II, core complex; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; IEA:InterPro.
DR   InterPro; IPR000722; RNA_pol_asu.
DR   InterPro; IPR000684; RNA_pol_II_repeat_euk.
DR   InterPro; IPR006592; RNA_pol_N.
DR   InterPro; IPR007080; RNA_pol_Rpb1_1.
DR   InterPro; IPR007066; RNA_pol_Rpb1_3.
DR   InterPro; IPR007083; RNA_pol_Rpb1_4.
DR   InterPro; IPR007081; RNA_pol_Rpb1_5.
DR   InterPro; IPR007075; RNA_pol_Rpb1_6.
DR   InterPro; IPR007073; RNA_pol_Rpb1_7.
DR   Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR   Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR   Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR   Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR   Pfam; PF04992; RNA_pol_Rpb1_6; 1.
DR   Pfam; PF04990; RNA_pol_Rpb1_7; 1.
DR   Pfam; PF05001; RNA_pol_Rpb1_R; 12.
DR   SMART; SM00663; RPOLA_N; 1.
DR   PROSITE; PS00115; RNA_POL_II_REPEAT; 14.
DR   HOGENOMDNA; ENCUN1_2.PE28; -.
KW   CAD26175.1002754575old_1320000031;
KW   DNA-directed RNA polymerase II subunit RPB1 ;
KW   Complete proteome; DNA-binding; DNA-directed RNA polymerase;
KW   Magnesium; Metal-binding; Nucleotidyltransferase; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Transcription;
KW   Transferase; Zinc.
SQ   SEQUENCE   1599 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MFEAKVKKQI KSIQFGLFSP DEVRNGSVAL IVHPEVMEGG VPKTGGLIDL RMGTTDRMYL
     CQSCGGDNFS CPGHFGHIEL TKPMFHVGYI SKIKKVLECV CFYCSKIKIP RKGIKSTLSN
     VWGMSKGRSV CEGEVLDNGR SGCGNKQPVI KREGLTLVAF MKGEESNEGK VMLNGERVYS
     IFKKISDEDS VYMGFDLKYS RPEWMILTVL LVPPPAVRPS IVMEGSLRGE DDLTHKLADI
     IKSNGYLKKY EQEGAPGHIV RDYEQLLQFH VATFIDNDIG GLPQALQKSG RPLKSLSARL
     KGKEGRIRGN LMGKRVDFSA RTVITPDPNI SLEEVGVPLE IAKIHTFPEK VTSFNIDRLE
     KLVRAGPNEH PGANYVLRSD GQKIDLNFNR SDIRLEEGYV VERHMQSGDV VLFNRQPSLH
     KMSMMAHYAR VMGNKTFRLN LSVTSPYNAD FDGDEMNLHM PQSYTSKAEL EELALVSRQI
     ISPQSNKPVM GIVQDTLTGL RLFTLRDTFL NEREVMSLLY AVNLEFCDIP LGDAVQTGLR
     KGKDYDIMKI LRKPAIAKPM RLWTGKQVLS FVLPNLNYIG LSSEHDDDDK ENIGDTRVII
     QDGYIHSGVI DKKAAGATQG GLVHIIFNDF GPKRAAQFFD GVQRMINAFM TGIHTFSMGI
     GDTIADPKTV KVVESAIRKA KEEVSALIEN ARQNRLERLP GMTMKESFES HLNLVLNRAR
     DVSGTSAQRS LSENNNMKTM VLAGSKGSFI NISQVTACVG QQNVEGKRIP FGFSHRTLPH
     FVKDDYTGKS RGFVENSYLT GLDPEEFFFH AMGGREGLID TAIKTAETGY IQRRLVKALE
     DAIVRQDESV RSGNGLVYQI KYGEDGFDAT FLESQKVDVK NFTKRYYIDM FGTEELEIKH
     GQVSEEVYGM LSSDVDLQKL LDQEYEWLVG EIFEGPPILS VGEVDIERDY KVRDIYQSAV
     MSPCNFTRIL ATAKRTFHLS TGDVSPYYIL EAHKHLTTSN RILNVLIRTN LSVKRVLLEH
     RLNTEAFNWV VEVIDAKILK AKITPNEMVG TLAAQSVGEP ATQMTLNTFH LAGVASTVTM
     GVPRLKEIFN VTKNLKTPSM KIYLDREHGK SIEAAKTIQN EIECLTVKDL CLFSEIYYDP
     EITGTEISDD KDFVEAYFEF PDEDVDFSCL SPFLMRLVVD RAKLVGRGIN LEYVAMFIRK
     ELGGGAHVIC SDENAVNMVV RVRTTKSEDE SLNFYTTALN SLLRLQLGGY KNVKKVYISE
     DKDRKEWYLQ TDGICLSQIL GNPAVNSRLT ISNDLVEIAE TLGIEAARES ILRELTIVID
     GNGSYVNYRH MSLLADVMTM RGYLCGITRH GVNKVGAGAL KRSSFEETVE ILLDAALVSE
     KNICRGITEN IMMGQLAPMG TGNIEIMLDM KKLDKAIPLS NPVFKPNEPA TPVISTPSSD
     SFSISSGNWS PTHLEMAYSR DLGERLSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS
     YSPTSPSYSP TSPSYSPTSP SYSPTSPSYS PTSPSYSPTS PSYSPTSPSY SPTSPSYSPT
     SPSYSPTSPS YSVSMSSFSN KNKSKNQDGD KKRRNDGSF
//

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