(data stored in ACNUC11299 zone)

HOGENOM: CABRI1_4_PE2666

ID   CABRI1_4_PE2666                      STANDARD;      PRT;   1853 AA.
AC   CABRI1_4_PE2666; P35074; A8WZN7; Q61UE8;
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 B1; EC=2.7.7 6;AltName: Full=DNA-directed RNA
DE   polymerase III largest subunit; (CABRI1_4.PE2666).
GN   Name=rpb-1; Synonyms=ama-1; ORFNames=CBG05355;
OS   CAENORHABDITIS BRIGGSAE AF16.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=473542;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CABRI1_4.PE2666.
CC       Caenorhabditis briggsae (strain AF16) chromosome IV, complete sequence.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:RPB1_CAEBR
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAA27891.1; Type=Frameshift; Positions=29;
CC   -!- GENE_FAMILY: HOG000222975 [ FAMILY / ALN / TREE ]
DR   EMBL; AAA27891.1; - ;
DR   UniProtKB/Swiss-Prot; P35074; A8WZN7; Q61UE8; -.
DR   EMBL; CAAC02000467; CAP25847.3; -; Genomic_DNA.
DR   EMBL; L23763; AAA27891.1; ALT_FRAME; Genomic_DNA.
DR   RefSeq; XP_002634760.1; XM_002634714.1.
DR   ProteinModelPortal; P35074; -.
DR   STRING; P35074; -.
DR   GeneID; 8576752; -.
DR   KEGG; cbr:CBG05355; -.
DR   CTD; 8576752; -.
DR   WormBase; CBG05355; CBP01350; WBGene00027817; -.
DR   OMA; SPTSPHY; -.
DR   PhylomeDB; P35074; -.
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; 28.
DR   SMART; SM00663; RPOLA_N; 1.
DR   PROSITE; PS00115; RNA_POL_II_REPEAT; 26.
DR   HOGENOMDNA; CABRI1_4.PE2666; -.
KW   CAP25847.300200367fold_1320000031; AAA27891.1;
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; Reference proteome; Repeat; Transcription;
KW   Transferase; Zinc.
SQ   SEQUENCE   1853 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MALVGVDFQA PLRTVCRVQF GILGPEEIKR MSVAHVEFPE VYENGKPKMG GLMDPRQGVI
     DRRGRCMTCA GNLTDCPGHF GHLELAKPVF HIGFLTKSLK ILRCVCFYCG RLLIDKTNPR
     VMDILKKTSG NPKKRLALIY DLCKSKSVCE GAAEKEDGLP DDMDDPMNEG KKVPAGCGRY
     QPSYRRVGID INAEWKKNVN EDTQERKIML TAERVLEVFK QITDEDILVI GMDPQFARPE
     WMICTVLPVP PLAVRPAVVT FGSAKNQDDL THKLSDIIKT NQQLQRNEAN GAAAHVLTDD
     VRLLQYHVAT LVDNCIPGLP TATQKGGRPL KSIKQRLKGK EGRIRGNLMG KRVDFSARTV
     ITADPNLPID TVGVPRTIAQ NLTFPEIVTP FNVDKLQELV NRGDTQYPGA KYIIRENGAR
     VDLRYHPRAA DLHLQPGYRV ERHMKDGDII VFNRQPTLHK MSMMGHRVKI LPWSTFRMNL
     SVTSPYNADF DGDEMNLHLP QSLETRAEIE EIAMVPRQLI TPQANKPVMG IVQDTLCAVR
     MMTKRDIFID WPFMMDLLMY LPTWDGKVPQ PAILKPKPLW TGKQVFSLII PGNVNVLRTH
     STHPDSEDSG PYKWISPGDT KVLIEHGELL SGIVCSKTVG KSAGNLLHVV ALELGHEIAA
     NFYSHIQTVI NAWLLREGHT IGIGDTIADQ STYLDIQNTI RKAKQDVVDV IEKAHNDDLE
     PTPGNTLRQT FENKVNQILN DARDRTGSSA QKSLSEFNNF KSMVVSGSKG SKINISQVIA
     CVGQQNVEGK RIPFGFRHRT LPHFIKDDYG PESKGFVENS YLAGLTPSEF FFHAMGGREG
     LIDTAVKTAE TGYIQRRLIK AMESVMVNYD GTVRNSLAQM VQLRYGEDGL DGMWVENQNM
     PTMKPNNAVF ERDFRMDLTD NKFLRKNYSE DVVREIQEAQ DGISLVESEW SQLEEDRRLL
     RKIFPRGDAK IVLPCNLQRL IWNAQKIFKV DLRKPVNLSP LHVINGVREL SKKLIIVSGN
     DEISKQAQYN ATLLMNILLR STLCTKKMCT SAKLNTEAFD WLLGEIETRF QQAIAQPGEM
     VGALAAQSLG EPATQMTLNT FHYAGVSAKN VTLGVPRLKE IINVSKQLKT PSLTVFLTGA
     AAKDPEKAKD VLCKLEHTTL KKVTCNTAIY YDPDPKNTVI AEDEEWVSIF YEMPDHDLTR
     TSPWLLRIEL DRKRMVDKKL TMEMIADRIH GGFGQDVHTI YTDDNAEKLV FRLRIAGEDK
     GAEGQEEQVD KMEDDVFLRC IEANMLSDLT LQGIPAISKV YMNQPNTDDK KRIIITPEGG
     FKAVADWILE TDGTALLRVL SERQIDPVRT TSNDICEIFE VLGIEAVRKS IEKEMDNVIS
     FDGSYVNYRH LALLCDVMTA KGHLMAITRH GINRQEVGAL MRCSFEETVD ILMEASVHAE
     VDPVKGVSEN IMLGQLARCG TGCFDLVLDV EKCKHGMEIP QNVVMGAGIY GGGFAGSPSR
     EFSPAHSPWN SGVTPNYSGP WSPTGGMSPS AGFSPAGNLD GGASPFNEGG WSPASPGDPL
     GALSPRTPAY GGMSPGVYSP ASPGFSMTSP HYSPTSPSYS PTSPAHHGQS PVSPSYSPTS
     PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP TSPSYSPTSP SYSPSSPRYS
     PTSPTYSPTS PTYSPTSPTY SPTSPTYSPT SPSYEGYSPS SPKYSPSSPT YSPTSPSYSP
     TSPQYSPTSP QYSPSSPTYT PSSPTYNPTS PRAFSSPQYS PTSPTYSPTS PSYTPSSPQY
     SPTSPTYTPS PADQPGTSNQ YSPSSPTYSP SSPTYSPASP SYSPSSPTYD PQN
//

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