(data stored in ACNUC11299 zone)

HOGENOM: ASHGO_4_PE494

ID   ASHGO_4_PE494                        STANDARD;      PRT;   1745 AA.
AC   ASHGO_4_PE494; Q75A34; Q6JED0;
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   (ASHGO_4.PE494).
GN   Name=RPB1; OrderedLocusNames=ADR086C;
OS   ASHBYA GOSSYPII ATCC 10895.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ASHGO_4.PE494.
CC       Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-
CC       1056) chromosome IV, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:RPB1_ASHGO
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   EMBL; AAT12576.1; - ;
DR   UniProtKB/Swiss-Prot; Q75A34; Q6JED0; -.
DR   EMBL; AE016817; AAS52006.1; -; Genomic_DNA.
DR   EMBL; AY497699; AAT12576.1; -; Genomic_DNA.
DR   RefSeq; NP_984182.2; NM_209535.2.
DR   ProteinModelPortal; Q75A34; -.
DR   STRING; Q75A34; -.
DR   GeneID; 4620331; -.
DR   GenomeReviews; AE016817_GR; ADR086C.
DR   KEGG; ago:AGOS_ADR086C; -.
DR   NMPDR; fig|33169.1.peg.1827; -.
DR   AGD; ADR086C; -.
DR   eggNOG; fuNOG04507; -.
DR   OMA; SPTSPHY; -.
DR   OrthoDB; EOG4J14H5; -.
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; 14.
DR   SMART; SM00663; RPOLA_N; 1.
DR   PROSITE; PS00115; RNA_POL_II_REPEAT; 23.
DR   HOGENOMDNA; ASHGO_4.PE494; -.
KW   AAS52006.2003186affold_1320000031; AAT12576.1;
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; Repeat; Transcription; Transferase; Zinc.
SQ   SEQUENCE   1745 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MVDFPYSSAP LRTIKEVQFG LFSPEEVRAI SVAKIEFPET MDETQMRAKV GGLNDPRLGS
     IDRNFKCQTC GEGMNDCPGH FGHIELAKPV FHIGFISKIK KVCECVCMHC GKLLLDEYNE
     LMRQAIKIKD PKRRFNAVWS LCKAKMVCDT EVPSEDDPSK YISRGGCGNA QPSIRKDGLS
     LVGTWKKDKN AEDADQPEKR IISAEEILNV FKHISPEDSW RLGFNEDFSR PEWMLLTVLP
     VPPPPVRPSI SFNESQRGED DLTYKLGDIL KANINVQRLE INGSPQHVIQ ESESLLQFHV
     ATYMDNDIAG QPQAVQKSGR PIKSIRARLK GKEGRIRGNL MGKRVDFSAR TVISGDPNLD
     LDQVGVPKSI AKTLTYPEVV TPYNIDRLTQ LVRNGPNEHP GAKYVIRDNG DRIDLRYSKR
     AGDIQLQYGW KVERHIMDDD PVLFNRQPSL HKMSMMAHRV KVMPYSTFRL NLSVTSPYNA
     DFDGDEMNLH VPQSEETRAE LSQLCAVPLQ IVSPQSNKPC MGIVQDTLCG IRKMTLRDTF
     IELDQVLNML YWIPDWDGVI PTPTILKPKP LWSGKQLLSM AIPSGIHLQR FDEGTTYLSP
     KDNGMLIIDG QIIFGVVDKK TVGSSSGGLI HVVTREKGPE VCAKLFGNIQ KVVNYWLLHN
     GFSIGIGDTI ADEKTMREIT DAIALAKKKV EEVTKEAQAN LLTAKHGMTL RESFEDNVVR
     YLNEARDKAG RSAEVNLKDL NNVKQMVSAG SKGSFINIAQ MSACVGQQSV EGKRIAFGFA
     DRTLPHFSKD DYSPESKGFV ENSYLRGLTP QEFFFHAMGG REGLIDTAVK TAETGYIQRR
     LVKALEDIMV HYDGTTRNSL GNIIQFVYGE DGMDAAHIEK QSIDTIPGSD LAFEKRYRID
     LLNPNYALDP NLLESGTEIV GDLKLQNLLD EEYKQLVQDR HFLRKIFMDG EHNWPLPVNI
     RRIIQNAQQT FRIDSTKPTD LSIQDVVQGV RGLQERLLVL RGKSQILQEA QENAITLFCC
     LLRSRLATRR VITEYRLTKQ TFEWVLNNIE AQFLRSIVHP GEMVGVLAAQ SIGEPATQMT
     LNTFHFAGVA SKKVTSGVPR LKEILNVAKN MKTPSLTVYL EESYATDQEK AKLIRSAIEH
     TTLKSVTVAS EIYYDPDPSS TVIEEDEEII QLHFSLMDEE TEASLKHQSP WLLRLELDRV
     AMTDKDLTMG QVGEKIKETF KNDLFVIWSE DNAEKLIIRC RVVRDPKTLD AEAEAEEDHM
     LKKIENTMLE SITLRGVQDI TRVVMMKYDR KVPSETGEYH KIPEWVLETD GVNLSEVMSV
     PGVDPTRIYT NSFIDIMNVL GIEAGRAALY KEVYNVIASD GSYVNYRHMA LLVDVMTSQG
     FLMSVTRHGF NRADTGALMR CSFEETVEIL FEAGAAAELD DCSGVSENVI LGQMAPIGTG
     SFDVMIDDES LIKYMPEQKL STAVEVNDGG ATPYNSDAGL VNTKVDIKDE LMFSPLVEAG
     TSDAIASGGF TAYGGADYGG ATSPFSGYGN GPTSPGFGDV SSPGFSPTSP AYSPTSPSYS
     PTSPSYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP TSPSYSPTSP
     SYSPTSPSYS PTSPSYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP
     TSPSYSPTSP SYSPTSPSYS PTSPSYSPTS PSYSPTSPQY SPRSPSYSPS FNNNDKEQKD
     ENGTH
//

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