ID   RPAB2_BOVIN             Reviewed;         127 AA.
AC   Q32PE0;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=DNA-directed RNA polymerases I, II, and III subunit RPABC2;
DE            Short=RNA polymerases I, II, and III subunit ABC2;
DE   AltName: Full=DNA-directed RNA polymerase II subunit F;
DE   AltName: Full=RPB6 homolog;
GN   Name=POLR2F;
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 (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA-dependent RNA polymerases catalyze 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, POLR2F/RPB6 is part of the clamp
CC       element and together with parts of RPB1 and RPB2 forms a pocket to
CC       which the RPB4-RPB7 subcomplex binds (By 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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the archaeal Rpo6/eukaryotic RPB6 RNA polymerase
CC       subunit family. {ECO:0000305}.
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DR   EMBL; BC108153; AAI08154.1; -; mRNA.
DR   PDB; 5FLM; EM; 3.40 A; F=1-127.
DR   PDB; 5OIK; EM; 3.70 A; F=1-127.
DR   PDBsum; 5FLM; -.
DR   PDBsum; 5OIK; -.
DR   AlphaFoldDB; Q32PE0; -.
DR   SMR; Q32PE0; -.
DR   DIP; DIP-61191N; -.
DR   IntAct; Q32PE0; 2.
DR   STRING; 9913.ENSBTAP00000006328; -.
DR   PaxDb; Q32PE0; -.
DR   eggNOG; KOG3405; Eukaryota.
DR   InParanoid; Q32PE0; -.
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; 3.90.940.10; -; 1.
DR   InterPro; IPR020708; DNA-dir_RNA_polK_14-18kDa_CS.
DR   InterPro; IPR006110; Pol_omega/Rpo6/RPB6.
DR   InterPro; IPR028363; RPB6.
DR   InterPro; IPR036161; RPB6/omega-like_sf.
DR   InterPro; IPR006111; Rpo6/Rpb6.
DR   Pfam; PF01192; RNA_pol_Rpb6; 1.
DR   PIRSF; PIRSF500154; RPB6; 1.
DR   PIRSF; PIRSF000778; RpoK/RPB6; 1.
DR   SMART; SM01409; RNA_pol_Rpb6; 1.
DR   SUPFAM; SSF63562; SSF63562; 1.
DR   PROSITE; PS01111; RNA_POL_K_14KD; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; DNA-directed RNA polymerase; Nucleus;
KW   Phosphoprotein; Reference proteome; Transcription.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P61218"
FT   CHAIN           2..127
FT                   /note="DNA-directed RNA polymerases I, II, and III subunit
FT                   RPABC2"
FT                   /id="PRO_0000291376"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..31
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P61218"
FT   MOD_RES         2
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000250|UniProtKB:O88828"
FT   HELIX           59..74
FT                   /evidence="ECO:0007829|PDB:5FLM"
FT   HELIX           89..99
FT                   /evidence="ECO:0007829|PDB:5FLM"
FT   STRAND          104..109
FT                   /evidence="ECO:0007829|PDB:5FLM"
FT   STRAND          115..119
FT                   /evidence="ECO:0007829|PDB:5FLM"
FT   TURN            120..122
FT                   /evidence="ECO:0007829|PDB:5FLM"
SQ   SEQUENCE   127 AA;  14448 MW;  4FE678833B2D2A33 CRC64;
     MSDNEDNFDG DDFDDVEEDE GLDDLENAEE EGQVNVEILP SGERPQANQK RITTPYMTKY
     ERARVLGTRA LQIAMCAPVM VELEGETDPL LIAMKELKAR KIPIIIRRYL PDGSYEDWGV
     DELIITD