(data stored in ACNUC11299 zone)

HOGENOM: SCHPO_2_PE627

ID   SCHPO_2_PE627                        STANDARD;      PRT;   1752 AA.
AC   SCHPO_2_PE627; P36594;
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   (SCHPO_2.PE627).
GN   Name=rpb1; ORFNames=SPBC28F2.12;
OS   SCHIZOSACCHAROMYCES POMBE.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SCHPO_2.PE627.
CC       Schizosaccharomyces pombe chromosome II EF1 full sequence 1..4539804
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:RPB1_SCHPO
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.
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   HOGENOM:Schizosaccharomyces_pombe;SPBC28F2.12;SPBC28F2.12-1;SPBC28F2.12-1.
DR   UniProtKB/Swiss-Prot; P36594; -.
DR   EMBL; X56564; CAA39916.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAB57941.1; -; Genomic_DNA.
DR   PIR; S26849; S26849.
DR   RefSeq; NP_595673.1; NM_001021568.1.
DR   PDB; 3H0G; X-ray; 3.65 A; A/M=1-1752.
DR   PDBsum; 3H0G; -.
DR   ProteinModelPortal; P36594; -.
DR   IntAct; P36594; 9.
DR   MINT; MINT-1214221; -.
DR   STRING; P36594; -.
DR   EnsemblFungi; SPBC28F2.12-1; SPBC28F2.12-1; SPBC28F2.12.
DR   GeneID; 2540292; -.
DR   GenomeReviews; CU329671_GR; rpb1.
DR   KEGG; spo:SPBC28F2.12; -.
DR   NMPDR; fig|4896.1.peg.1539; -.
DR   GeneDB_Spombe; SPBC28F2.12; -.
DR   eggNOG; fuNOG04507; -.
DR   GeneTree; EFGT00050000000243; -.
DR   OMA; SPTSPHY; -.
DR   OrthoDB; EOG4J14H5; -.
DR   PhylomeDB; P36594; -.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-003699-MON; -.
DR   ArrayExpress; P36594; -.
DR   GO; GO:0005829; C:cytosol; IDA:GeneDB_Spombe.
DR   GO; GO:0005665; C:DNA-directed RNA polymerase II, core complex; TAS:GeneDB_Spombe.
DR   GO; GO:0003677; F:DNA binding; IDA:GeneDB_Spombe.
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:0005515; F:protein binding; IPI:GeneDB_Spombe.
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; 17.
DR   SMART; SM00663; RPOLA_N; 1.
DR   PROSITE; PS00115; RNA_POL_II_REPEAT; 24.
DR   HOGENOMDNA; SCHPO_2.PE627; -.
KW   SPBC28F2.12ccc7236820036002503210000011;
KW   P36594;
KW   3D-structure; Complete proteome; DNA-binding;
KW   DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Transcription; Transferase; Zinc.
SQ   SEQUENCE   1752 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSGIQFSPSS VPLRRVEEVQ FGILSPEEIR SMSVAKIEFP ETMDESGQRP RVGGLLDPRL
     GTIDRQFKCQ TCGETMADCP GHFGHIELAK PVFHIGFLSK IKKILECVCW NCGKLKIDSS
     NPKFNDTQRY RDPKNRLNAV WNVCKTKMVC DTGLSAGSDN FDLSNPSANM GHGGCGAAQP
     TIRKDGLRLW GSWKRGKDES DLPEKRLLSP LEVHTIFTHI SSEDLAHLGL NEQYARPDWM
     IITVLPVPPP SVRPSISVDG TSRGEDDLTH KLSDIIKANA NVRRCEQEGA PAHIVSEYEQ
     LLQFHVATYM DNEIAGQPQA LQKSGRPLKS IRARLKGKEG RLRGNLMGKR VDFSARTVIT
     GDPNLSLDEL GVPRSIAKTL TYPETVTPYN IYQLQELVRN GPDEHPGAKY IIRDTGERID
     LRYHKRAGDI PLRYGWRVER HIRDGDVVIF NRQPSLHKMS MMGHRIRVMP YSTFRLNLSV
     TSPYNADFDG DEMNMHVPQS EETRAEIQEI TMVPKQIVSP QSNKPVMGIV QDTLAGVRKF
     SLRDNFLTRN AVMNIMLWVP DWDGILPPPV ILKPKVLWTG KQILSLIIPK GINLIRDDDK
     QSLSNPTDSG MLIENGEIIY GVVDKKTVGA SQGGLVHTIW KEKGPEICKG FFNGIQRVVN
     YWLLHNGFSI GIGDTIADAD TMKEVTRTVK EARRQVAECI QDAQHNRLKP EPGMTLRESF
     EAKVSRILNQ ARDNAGRSAE HSLKDSNNVK QMVAAGSKGS FINISQMSAC VGQQIVEGKR
     IPFGFKYRTL PHFPKDDDSP ESRGFIENSY LRGLTPQEFF FHAMAGREGL IDTAVKTAET
     GYIQRRLVKA MEDVMVRYDG TVRNAMGDII QFAYGEDGLD ATLVEYQVFD SLRLSTKQFE
     KKYRIDLMED RSLSLYMENS IENDSSVQDL LDEEYTQLVA DRELLCKFIF PKGDARWPLP
     VNVQRIIQNA LQIFHLEAKK PTDLLPSDII NGLNELIAKL TIFRGSDRIT RDVQNNATLL
     FQILLRSKFA VKRVIMEYRL NKVAFEWIMG EVEARFQQAV VSPGEMVGTL AAQSIGEPAT
     QMTLNTFHYA GVSSKNVTLG VPRLKEILNV AKNIKTPSLT IYLMPWIAAN MDLAKNVQTQ
     IEHTTLSTVT SATEIHYDPD PQDTVIEEDK DFVEAFFAIP DEEVEENLYK QSPWLLRLEL
     DRAKMLDKKL SMSDVAGKIA ESFERDLFTI WSEDNADKLI IRCRIIRDDD RKAEDDDNMI
     EEDVFLKTIE GHMLESISLR GVPNITRVYM MEHKIVRQIE DGTFERADEW VLETDGINLT
     EAMTVEGVDA TRTYSNSFVE ILQILGIEAT RSALLKELRN VIEFDGSYVN YRHLALLCDV
     MTSRGHLMAI TRHGINRAET GALMRCSFEE TVEILMDAAA SGEKDDCKGI SENIMLGQLA
     PMGTGAFDIY LDQDMLMNYS LGTAVPTLAG SGMGTSQLPE GAGTPYERSP MVDSGFVGSP
     DAAAFSPLVQ GGSEGREGFG DYGLLGAASP YKGVQSPGYT SPFSSAMSPG YGLTSPSYSP
     SSPGYSTSPA YMPSSPSYSP TSPSYSPTSP SYSPTSPSYS PTSPSYSATS PSYSPTSPSY
     SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP TSPSYSPTSP SYSPTSPSYS PTSPSYSPTS
     PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP TSPSYSPTSP SYSPTSPSYS
     PTSPSYSPTS PS
//

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