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Database: UniProt
Entry: Q9EMI5_AMEPV
LinkDB: Q9EMI5_AMEPV
Original site: Q9EMI5_AMEPV 
ID   Q9EMI5_AMEPV            Unreviewed;      1301 AA.
AC   Q9EMI5;
DT   01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=DNA-directed RNA polymerase 147 kDa polypeptide {ECO:0000256|ARBA:ARBA00021673};
DE            EC=2.7.7.6 {ECO:0000256|ARBA:ARBA00012418};
GN   Name=AMV221 {ECO:0000313|EMBL:AAG02927.1};
OS   Amsacta moorei entomopoxvirus (AmEPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Entomopoxvirinae; Betaentomopoxvirus.
OX   NCBI_TaxID=28321 {ECO:0000313|EMBL:AAG02927.1, ECO:0000313|Proteomes:UP000000872};
OH   NCBI_TaxID=340055; Amsacta.
RN   [1] {ECO:0000313|EMBL:AAG02927.1, ECO:0000313|Proteomes:UP000000872}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10936094; DOI=10.1006/viro.2000.0449;
RA   Bawden A.L., Glassberg K.J., Diggans J., Shaw R., Farmerie W., Moyer R.W.;
RT   "Complete genomic sequence of the Amsacta moorei entomopoxvirus: analysis
RT   and comparison with other poxviruses.";
RL   Virology 274:120-139(2000).
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; Evidence={ECO:0000256|ARBA:ARBA00024550};
CC   -!- SIMILARITY: Belongs to the poxviridae DNA-directed RNA polymerase 147
CC       kDa subunit family. {ECO:0000256|ARBA:ARBA00006884}.
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DR   EMBL; AF250284; AAG02927.1; -; Genomic_DNA.
DR   RefSeq; NP_065003.1; NC_002520.1.
DR   GeneID; 1494811; -.
DR   KEGG; vg:1494811; -.
DR   Proteomes; UP000000872; 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:DNA-templated transcription; IEA:InterPro.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.30.1490.180; RNA polymerase ii; 1.
DR   InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR   InterPro; IPR000722; RNA_pol_asu.
DR   InterPro; IPR006592; RNA_pol_N.
DR   InterPro; IPR007066; RNA_pol_Rpb1_3.
DR   InterPro; IPR007083; RNA_pol_Rpb1_4.
DR   InterPro; IPR007081; RNA_pol_Rpb1_5.
DR   InterPro; IPR038120; Rpb1_funnel_sf.
DR   PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR   PANTHER; PTHR19376:SF37; DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1; 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   SMART; SM00663; RPOLA_N; 1.
DR   SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000872};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          198..485
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
SQ   SEQUENCE   1301 AA;  150299 MW;  3E7D097185975BB7 CRC64;
     MTTFKYTLLD NSTIDAIPIV IDSIGNDNEN SVKSPKLGGT KFNVCSTCNL TRENGDMGHP
     GRTPLRDMCI VKSGCIKNVL DTLNTLKLCN SCFMIKNNTI FSEIIEKYNS EYNINLKKEI
     LSLLKNNRQG GVKCNNENCQ NITGTYKYNQ KKSYFYVKKQ KDEIILNKTV YTMLLGIPDI
     IYKCVTVPYA DSQLQPYKAF YANNIIIPVL PSRPPNYFDN KESHVMTTKL GQLVGTSQKS
     RDESEVQKIY NDIDNVKPNS PYKTSNMLVT LNIQVGGNKK GSIVRSNIMA RRADNTARCV
     AGPTMDKIGY IYIPKIVAKT LTSSIYYNRF TENMIKDMLV NDNNKIKYIL LYRYDQLKPT
     TLLKIKPQSR LNNLLKMKYG DRIEVELEDN DVILFSRQPS LHKFNIQAGI CKIWDNNTIA
     TPTPIANSMN LDYDGDEMNV YKLKSSVSVE SLFTMLSVNM IKNNYNFSPI FGLIQDQIIS
     VHMIYNIKEF SLQDVIYILG EYSYYIRDIN KKTYSGKELL SLLFPDNLTY EGMFDNGKIT
     LSNISSKQVV AQSYESFSNI LSQLKNNIYA VYFIDVILYV ARNFINLYSF SVSLKDIIPD
     IYFIDDVQEY INNCCKVIQY VALQYYIKKD HIIKLTYDEM ENIRIQNGNN IISNVKNKIN
     NLFKDEKLNT IMMMKNSGYK ITLDELVTVL GCTGQQGIDS DDIPKPGIMG RVFDSTLPGS
     LDIESLGYVK SSTIKGLKFE ELAFHTKYNS IKKILKITCE TSSAGSIGRK LVKFMEGVKV
     DHLGRSVLNN DIIWYNTNHI KMTGGDISKV EILTPSLEMV NYTLIKEIYN ENKKYLLTNF
     NTEINKEFIF PINIKLEIQS FYNKKSTPIS DIDALKLIDE FIEYVYINIY FYNITIDWFK
     YILYTYLDRN TVEKYNKKYS KELLNYIINK IKLKLLNSLN PGYPIGLEYA NNIQEKFTQQ
     SLSSFHTTKK SGTASTQLGF SDFKDTVELS KKNKRDIVIA FTTHRYKLED IKKQMEYLCL
     KNFNPKINII EETESDMVIS VSIKKYYIND KISLYHYLQM YIEYLENNKI IKGYWITMKL
     KDNDITVIFG VKIKTPYNIN KIYMIKSIPV SVSKGKISNI NLEIEDVKMY NNNLEEQNGY
     RLKFYIDSVT DFINFDTRDV YLELGPWFTY NSFGIQFAEY SIRRRLVSST KEKSMEICYI
     ILSKLMCLSS EMYNIKRIRE GKQNVIKSAI HGSSDAITTA AYNNIIDPNN DIYSQILSSQ
     IMKLGHGYYD CYLNLNRYDS ININSVTEQD INITSEIIEN F
//
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