ID   RPAB2_PONAB             Reviewed;         127 AA.
AC   Q5R592;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the archaeal Rpo6/eukaryotic RPB6 RNA polymerase
CC       subunit family. {ECO:0000305}.
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DR   EMBL; CR860972; CAH93074.1; -; mRNA.
DR   RefSeq; NP_001127626.1; NM_001134154.1.
DR   AlphaFoldDB; Q5R592; -.
DR   SMR; Q5R592; -.
DR   STRING; 9601.ENSPPYP00000013173; -.
DR   Ensembl; ENSPPYT00000060617; ENSPPYP00000028000; ENSPPYG00000011809.
DR   GeneID; 100174705; -.
DR   KEGG; pon:100174705; -.
DR   CTD; 5435; -.
DR   eggNOG; KOG3405; Eukaryota.
DR   GeneTree; ENSGT00390000010415; -.
DR   HOGENOM; CLU_112527_2_0_1; -.
DR   InParanoid; Q5R592; -.
DR   OMA; QEEDGYN; -.
DR   OrthoDB; 1488436at2759; -.
DR   TreeFam; TF103041; -.
DR   Proteomes; UP000001595; Chromosome 22.
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   2: Evidence at transcript level;
KW   Acetylation; DNA-directed RNA polymerase; Nucleus; Phosphoprotein;
KW   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_0000133801"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..33
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"
SQ   SEQUENCE   127 AA;  14478 MW;  6362B0D7EB3F0921 CRC64;
     MSDNEDNFDG DDFDDVEEDE GLDDLENAEE EGQENVEILP SGERPQANQK RITTPYMTKY
     ERARVLGTRA LQIAMCAPVM VELEGETDPL LIAMKELKAR KIPIIIRRYL PDGSYEDWGV
     DELIITD