ID   RPO6_MIMIV              Reviewed;         396 AA.
AC   Q5UQ32;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=DNA-directed RNA polymerase subunit 6;
DE            EC=2.7.7.6;
GN   OrderedLocusNames=MIMI_R209;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Mimivirus.
OX   NCBI_TaxID=212035;
OH   NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rowbotham-Bradford;
RX   PubMed=15486256; DOI=10.1126/science.1101485;
RA   Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA   La Scola B., Susan M., Claverie J.-M.;
RT   "The 1.2-megabase genome sequence of Mimivirus.";
RL   Science 306:1344-1350(2004).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC         EC=2.7.7.6;
CC   -!- SIMILARITY: Belongs to the archaeal Rpo6/eukaryotic RPB6 RNA polymerase
CC       subunit family. {ECO:0000305}.
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DR   EMBL; AY653733; AAV50482.1; -; Genomic_DNA.
DR   SMR; Q5UQ32; -.
DR   PRIDE; Q5UQ32; -.
DR   BRENDA; 2.7.7.6; 9231.
DR   Proteomes; UP000001134; Genome.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 3.90.940.10; -; 1.
DR   InterPro; IPR006110; Pol_omega/Rpo6/RPB6.
DR   InterPro; IPR036161; RPB6/omega-like_sf.
DR   Pfam; PF01192; RNA_pol_Rpb6; 1.
DR   SUPFAM; SSF63562; SSF63562; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome;
KW   Transcription; Transferase.
FT   CHAIN           1..396
FT                   /note="DNA-directed RNA polymerase subunit 6"
FT                   /id="PRO_0000133807"
FT   REGION          1..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          290..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..48
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..87
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..137
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..370
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   396 AA;  44206 MW;  2C53500721B1EABA CRC64;
     MSSKKGSKTS KTSRSVKQTE EYYDDDAEFQ NSEDEYPPSD EDLDNSGGSD DENTQSGGLS
     DAPDDELGED SATLDIDPDD EAEYDTDGDE KFNPIDEMGE PEDPDDPSEQ EEDEVEDLGS
     EDVDNVEIED DAADIEDLDP ELVDEARNSK SKQCYMKNLN KDFIALDEDD SGIYSKIEYK
     KIPDNERETD PILTYYEIVR ILGTRAQQFN YGAKPLIKGV EGMHPAKMAF VELTAKMTSF
     IVRRHLPGKK YEDWRIDELG MIHTITEELF VPDNFNWDSI TALHKTMISN QQKNSTTDTE
     TLSTQENAST RVSGSNLRSR SGSKSSKSNN SRSASKSNSR TESKSNSRTG SKSNSRTGSK
     SNSRTGSKSK KSSNTKSKSK RNSDNSDDSD YSDYSE