ID   RPO2_MIMIV              Reviewed;        1196 AA.
AC   Q7T6X7;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 2.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=DNA-directed RNA polymerase subunit 2;
DE            EC=2.7.7.6;
GN   Name=RPO2; OrderedLocusNames=MIMI_L244;
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).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=16971431; DOI=10.1128/jvi.00940-06;
RA   Renesto P., Abergel C., Decloquement P., Moinier D., Azza S., Ogata H.,
RA   Fourquet P., Gorvel J.-P., Claverie J.-M., Raoult D.;
RT   "Mimivirus giant particles incorporate a large fraction of anonymous and
RT   unique gene products.";
RL   J. Virol. 80:11678-11685(2006).
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   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:16971431}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC       {ECO:0000305}.
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DR   EMBL; AY653733; AAQ09583.2; -; Genomic_DNA.
DR   SMR; Q7T6X7; -.
DR   PRIDE; Q7T6X7; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00653; RNA_pol_B_RPB2; 1.
DR   Gene3D; 2.40.270.10; -; 1.
DR   Gene3D; 2.40.50.150; -; 1.
DR   Gene3D; 3.90.1110.10; -; 1.
DR   InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR   InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR   InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR   InterPro; IPR007121; RNA_pol_bsu_CS.
DR   InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR   InterPro; IPR007642; RNA_pol_Rpb2_2.
DR   InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR   InterPro; IPR007645; RNA_pol_Rpb2_3.
DR   InterPro; IPR007646; RNA_pol_Rpb2_4.
DR   InterPro; IPR007647; RNA_pol_Rpb2_5.
DR   InterPro; IPR007641; RNA_pol_Rpb2_7.
DR   InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR   PANTHER; PTHR20856; PTHR20856; 1.
DR   Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR   Pfam; PF04561; RNA_pol_Rpb2_2; 1.
DR   Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR   Pfam; PF04566; RNA_pol_Rpb2_4; 1.
DR   Pfam; PF04567; RNA_pol_Rpb2_5; 1.
DR   Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR   Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR   PROSITE; PS01166; RNA_POL_BETA; 1.
PE   1: Evidence at protein level;
KW   DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase;
KW   Reference proteome; Transcription; Transferase; Virion; Zinc; Zinc-finger.
FT   CHAIN           1..1196
FT                   /note="DNA-directed RNA polymerase subunit 2"
FT                   /id="PRO_0000048057"
FT   ZN_FING         1133..1154
FT                   /note="C4-type"
FT   REGION          1074..1095
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1196 AA;  136048 MW;  2B67F08B79D20955 CRC64;
     MSKKSVEIED VNNTYDQEAH FALLDLFFEK DKQVLVKHHI DSFNQFIEEI IPNILQGGDN
     VISEKATENK IIRYRLTFND LGIKPPTLEN EENLLYPLDA IRKQISYSAK YTATVTQWQD
     IVDIDTKKTE TRIIGSPEKD VPIAKIPIMV LSKYCNLTLR PDIAGKHCKY DAGGYFIVNG
     SEKVVLSVES MIPRKPVVFT QRDQNSLLYY VRVQSIPASQ FVGNPQLFTV KMKRDNSIIL
     SIPHFKEVSI FTFIRALGIE TDEDIVDSIL DVKKEKDLLN LLSICMNSSN TPSVTKEEAL
     EIMANQIKST KTFTDTNPEV KAEQRRRYLD KIMTQFVLPH ITSGTGDPEI DKIYKAHYIC
     YMIHKLLKCY LRGAREVEEY RGCDDRDSMV NKRIDLTGRL LGGLFKQFYD KMLNDCNKIF
     RTKNIDDKKP PNIIPHIKPN SIEQGLRQAL STGNFGSQSR KGLSQMLNRM NHLHSLSYMR
     RVITPTVDAS TMKMTSPRHL HNTQYGSMCP LESPEGKPKT GLVKNMAMME GITINMNSQI
     PIIESYLIGK ITTLESANKK RLHQYVKVFL NGNWLGVTRN IIKIHNDLRA MRFRGELSRM
     VGLVLNYKTA EFHIYTDGGR LIRPYLTVTD NKLNFKPEML DEVNSWEEFL AKFPEVIEYV
     DKEEEQNIML AVFPQYIQDA NRIMSKKPIN SRDQLNKINR TNRYDDNVYV RYTHCEIHPC
     MILGLISSNI PFPDHNQSPR GIFQYNQARQ AMGLYISDYR ERTDISYILY HPQIPLVTSR
     ASKYTGTHIF PAGENSIVAI ASYTGLMNQE DSLVINDSAI QKGYMRAQAL KKYMEIIKKN
     PASSQTSIFM KPDRNKVDNL RDANYDKLSE EGYAKVETVI RDGDVVIGVV NPKPTAREDE
     KQYKDASSIY KSLIPGAVDK VITEVNNDGY PIIKMRIRSE RIPNVGDKFS SRAGQKGTIG
     YKAHRADMLF SKSGLIPDII INPNCMPKRM TIGQLIECLL GKLCAVKGVY GDATPFTSVD
     LNAINDELVA AGYEEWGNET MYNGMNGKKL PVKIFIGPTY YQRLKQMVGD KAHSRARGPT
     QLLTRQAPEG RSRDGGLRIG FEMERDALCA HGVAQFLKEK TVDNSDIYTC HVCDSCGQFA
     HKVPEKKYYT CTGCRNTTSI SKIVIPYAFK LLLQELASIN ILGKIRTSKT IATPRG