RPAB1_BOVIN
ID RPAB1_BOVIN Reviewed; 210 AA.
AC Q2T9T3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=DNA-directed RNA polymerases I, II, and III subunit RPABC1;
DE Short=RNA polymerases I, II, and III subunit ABC1;
DE AltName: Full=DNA-directed RNA polymerase II subunit E;
DE AltName: Full=RPB5 homolog;
GN Name=POLR2E;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Common component of RNA polymerases I, II and III which synthesize
CC ribosomal RNA precursors, mRNA precursors and many functional non-
CC coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively.
CC Pol II is the central component of the basal RNA polymerase II
CC transcription machinery. Pols are composed of mobile elements that move
CC relative to each other. In Pol II, POLR2E/RPB5 is part of the lower jaw
CC surrounding the central large cleft and thought to grab the incoming
CC DNA template. Seems to be the major component in this process (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I), RNA polymerase II
CC (Pol II) and RNA polymerase III (Pol III) complexes consisting of at
CC least 13, 12 and 17 subunits, respectively. In RNA Pol II, this subunit
CC is present in 2-fold molar excess over the other subunits. Component of
CC the PAQosome complex which is responsible for the biogenesis of several
CC protein complexes and which consists of R2TP complex members RUVBL1,
CC RUVBL2, RPAP3 and PIH1D1, URI complex members PFDN2, PFDN6, PDRG1, UXT
CC and URI1 as well as ASDURF, POLR2E and DNAAF10/WDR92. Interacts with
CC URI1. {ECO:0000250|UniProtKB:P19388}.
CC -!- INTERACTION:
CC Q2T9T3; G3MZY8: POLR2A; NbExp=3; IntAct=EBI-15586877, EBI-6551200;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo5/eukaryotic RPB5 RNA polymerase
CC subunit family. {ECO:0000305}.
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DR EMBL; BC111280; AAI11281.1; -; mRNA.
DR RefSeq; NP_001033182.1; NM_001038093.2.
DR PDB; 5FLM; EM; 3.40 A; E=1-210.
DR PDB; 5OIK; EM; 3.70 A; E=1-210.
DR PDBsum; 5FLM; -.
DR PDBsum; 5OIK; -.
DR AlphaFoldDB; Q2T9T3; -.
DR SMR; Q2T9T3; -.
DR BioGRID; 169601; 1.
DR DIP; DIP-61190N; -.
DR IntAct; Q2T9T3; 2.
DR STRING; 9913.ENSBTAP00000027684; -.
DR PaxDb; Q2T9T3; -.
DR PRIDE; Q2T9T3; -.
DR GeneID; 512971; -.
DR KEGG; bta:512971; -.
DR CTD; 5434; -.
DR eggNOG; KOG3218; Eukaryota.
DR InParanoid; Q2T9T3; -.
DR OrthoDB; 1255823at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005665; C:RNA polymerase II, core complex; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISS:UniProtKB.
DR Gene3D; 3.40.1340.10; -; 1.
DR Gene3D; 3.90.940.20; -; 1.
DR HAMAP; MF_00025; RNApol_Rpo5_RPB5; 1.
DR InterPro; IPR014381; Arch_Rpo5/euc_Rpb5.
DR InterPro; IPR005571; RNA_pol_Rpb5_N.
DR InterPro; IPR036710; RNA_pol_Rpb5_N_sf.
DR InterPro; IPR000783; RNA_pol_subH/Rpb5_C.
DR InterPro; IPR020608; RNA_pol_subH/Rpb5_CS.
DR InterPro; IPR035913; RPB5-like_sf.
DR PANTHER; PTHR10535; PTHR10535; 1.
DR Pfam; PF01191; RNA_pol_Rpb5_C; 1.
DR Pfam; PF03871; RNA_pol_Rpb5_N; 1.
DR PIRSF; PIRSF000747; RPB5; 1.
DR SUPFAM; SSF53036; SSF53036; 1.
DR SUPFAM; SSF55287; SSF55287; 1.
DR PROSITE; PS01110; RNA_POL_H_23KD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; DNA-directed RNA polymerase; Isopeptide bond;
KW Nucleus; Reference proteome; Transcription; Ubl conjugation.
FT CHAIN 1..210
FT /note="DNA-directed RNA polymerases I, II, and III subunit
FT RPABC1"
FT /id="PRO_0000240448"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P19388"
FT CROSSLNK 81
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P19388"
FT HELIX 3..23
FT /evidence="ECO:0007829|PDB:5FLM"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:5FLM"
FT HELIX 37..44
FT /evidence="ECO:0007829|PDB:5FLM"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:5FLM"
FT HELIX 84..97
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 101..110
FT /evidence="ECO:0007829|PDB:5FLM"
FT HELIX 112..120
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:5FLM"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:5FLM"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:5FLM"
FT HELIX 153..162
FT /evidence="ECO:0007829|PDB:5FLM"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:5FLM"
FT HELIX 178..183
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 203..209
FT /evidence="ECO:0007829|PDB:5FLM"
SQ SEQUENCE 210 AA; 24481 MW; 10BE1DB4A7FA3F58 CRC64;
MDDEEETYRL WKIRKTIMQL CHDRGYLVTQ DGLDQTLEEF KAQFGGKPSE GRPRRTDLTV
LVAHNDDPTD QMFVFFPEEP KVGIKTIKVY CQRMQEENIT RALIVVQQGM TPSAKQSLVD
MAPKYILEQF LQQELLINIT EHELVPEHVV MTKEEVTELL ARYKLRENQL PRIQAGDPVA
RYFGIKRGQV VKIIRPSETA GRYITYRLVQ
