ID   RPO1_MIMIV              Reviewed;        1495 AA.
AC   Q7T6X5;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 2.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=DNA-directed RNA polymerase subunit 1;
DE            EC=2.7.7.6;
GN   Name=RPO1; OrderedLocusNames=MIMI_R501;
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; AAQ09585.2; -; Genomic_DNA.
DR   RefSeq; YP_003987013.1; NC_014649.1.
DR   SMR; Q7T6X5; -.
DR   PRIDE; Q7T6X5; -.
DR   GeneID; 9925132; -.
DR   KEGG; vg:9925132; -.
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; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.274.100; -; 1.
DR   Gene3D; 3.30.1360.140; -; 1.
DR   Gene3D; 4.10.860.120; -; 1.
DR   InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR   InterPro; IPR000722; RNA_pol_asu.
DR   InterPro; IPR006592; RNA_pol_N.
DR   InterPro; IPR007080; RNA_pol_Rpb1_1.
DR   InterPro; IPR007066; RNA_pol_Rpb1_3.
DR   InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR   InterPro; IPR007083; RNA_pol_Rpb1_4.
DR   InterPro; IPR007081; RNA_pol_Rpb1_5.
DR   InterPro; IPR007075; RNA_pol_Rpb1_6.
DR   InterPro; IPR007073; RNA_pol_Rpb1_7.
DR   InterPro; IPR038593; RNA_pol_Rpb1_7_sf.
DR   InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR   InterPro; IPR038120; Rpb1_funnel_sf.
DR   PANTHER; PTHR19376; PTHR19376; 1.
DR   Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR   Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR   Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR   Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR   Pfam; PF04992; RNA_pol_Rpb1_6; 1.
DR   Pfam; PF04990; RNA_pol_Rpb1_7; 1.
DR   SMART; SM00663; RPOLA_N; 1.
PE   1: Evidence at protein level;
KW   DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome;
KW   Transcription; Transferase; Virion.
FT   CHAIN           1..1495
FT                   /note="DNA-directed RNA polymerase subunit 1"
FT                   /id="PRO_0000073917"
SQ   SEQUENCE   1495 AA;  169839 MW;  9439FE6F7B1A91DF CRC64;
     MEANKNTYSR LGDTIETVER IEFCINSNES IIRHSAIVDP NGITEAETFN SNNNEPVQGG
     VIDKRLGVTE SHLECSTCGE TALRCPGHFG HIKFVEPVFH MGYLIYLKHI LSCICIRCNK
     LLVYKNEKEI AALIKNKQGK QRFAEIRSIC KKVTHCQKEN YGCGTPAHKI SIDKRNGNIF
     LLAEPVKRTD EYDETGETRK RPQQILTPQL CYDILKSVSD EDCIIMGFDP AKSRPEDMII
     LNFPVPPVQV RPSIRAEILS SPTMDDDLTH KLIDIIKSNE NLKNTKGDGS LIKYTSINDD
     FMLLQLHVAT FFANDMAGLA RSQQKNKKVT KSMSERLRGK EGRIRGNLMG KRVDMSARTV
     ITSDPNIALN EVGVPLIIAK NLTFDEIVTE HNIEYLTQLV KNGKRVYPGA NFVIKHVIDA
     EGNESGHIYH LKYVDKPISL KPGDIVKRQL IDGDIVIFNR QPSLHKLSMM GHKCHVIPDN
     NLLTFRVNVS VTDPYNADFD GDEMNLHVPQ SIQTATEILL IANASRRFVS PATSNIAIKA
     KQDTLMGSYV QTEPDMEIDW RDAMSILMST SVKLDNDIPK YQNVSGKFLY SQIIPEGLNI
     TKRKNDKEFQ LKIKNGELTD GTLGKSEISS ILQRIWFQYG SKETQEFIDD AQRMILQFLM
     RYGYTVSIKD TVIGEKVNQY IYDLIETKRK ETLAFITEYD NDPYVMTKDA FEIKLQENLK
     SVQDEIKNTV MRNFDKNSGI FIAISSGSSG EPMNAGQIAG CIGQVIVEGK RIQIRFNGRT
     LPMFPKFDDS AFSRGFCRNS FIEGLGPFEF FFQVMAGREG IINTAIKTAD TGYIQRKLVK
     MLEDIKQEYD GTVRNANGKL ISCVYGDNGI NTENQVDQKI DLISANDNKV RNDYVYTEDE
     IKYLIKNHKT DKRYTTDLNN SLYRKLISMR DQLRRIQRLV NLTSAEFKET YKMPVDIQQF
     IFNIINRDVR NNNVVVDPYY VLKMIKDMYY GSDSKIMKYN NRTSRIKKED EKRIKFLMKI
     YLYDVLAPKK CTHVYKFSKQ EFDEIVDYFK KTIMLAKVEG GEMVGFVAAQ SIGEPVTQTN
     LKSFHKSGTG KTVSGGLVRV KELLGISKNI KTPITEIILE EKYKNDKITA SRIASYLKYT
     TLRDVVEKAD VIYDPEPFSK DGLMKKDGVD NIFDQEQGKT GCQTDIKNLP WVLRIMLSKE
     KMIERNINML EIKTSFCRNW GTRNEDKTSK KEFNKVIDKI TQCAIVTNYD NSQVPIVHVR
     FDANNYNLNT LIQFQEMVIN TYKIKGISNI TESNNIIEES YVDFDDEGNV VKKKQYVIIA
     EGINLSEMSQ INGIDLLRTK CNDIVTIYEM YGVEAARTAF IKEFTAAIES SGGFSNYQHI
     EILADAITHM GGLIPVNRHG ANKLDTDPFS RASFEKTVEQ LLAAAVFGES DHMRSVSARI
     MVGALINGGT GCFDLLLDHK KIQQSLVESE EVVAPVVPIK KKTVLDDLIS KKKSK