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Database: UniProt/TrEMBL
Entry: D6WV41_TRICA
LinkDB: D6WV41_TRICA
Original site: D6WV41_TRICA 
ID   D6WV41_TRICA            Unreviewed;      1258 AA.
AC   D6WV41;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00012418, ECO:0000256|RuleBase:RU003805};
DE            EC=2.7.7.6 {ECO:0000256|ARBA:ARBA00012418, ECO:0000256|RuleBase:RU003805};
GN   Name=AUGUSTUS-3.0.2_06188 {ECO:0000313|EMBL:EFA08534.1};
GN   ORFNames=TcasGA2_TC006188 {ECO:0000313|EMBL:EFA08534.1};
OS   Tribolium castaneum (Red flour beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX   NCBI_TaxID=7070 {ECO:0000313|EMBL:EFA08534.1, ECO:0000313|Proteomes:UP000007266};
RN   [1] {ECO:0000313|EMBL:EFA08534.1, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA08534.1,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=18362917; DOI=10.1038/nature06784;
RG   Tribolium Genome Sequencing Consortium;
RA   Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA   Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., Friedrich M.,
RA   Grimmelikhuijzen C.J., Klingler M., Lorenzen M., Richards S., Roth S.,
RA   Schroder R., Tautz D., Zdobnov E.M., Muzny D., Gibbs R.A., Weinstock G.M.,
RA   Attaway T., Bell S., Buhay C.J., Chandrabose M.N., Chavez D.,
RA   Clerk-Blankenburg K.P., Cree A., Dao M., Davis C., Chacko J., Dinh H.,
RA   Dugan-Rocha S., Fowler G., Garner T.T., Garnes J., Gnirke A., Hawes A.,
RA   Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V.,
RA   Khan Z.M., Jackson L., Kovar C., Kowis A., Lee S., Lewis L.R., Margolis J.,
RA   Morgan M., Nazareth L.V., Nguyen N., Okwuonu G., Parker D., Richards S.,
RA   Ruiz S.J., Santibanez J., Savard J., Scherer S.E., Schneider B.,
RA   Sodergren E., Tautz D., Vattahil S., Villasana D., White C.S., Wright R.,
RA   Park Y., Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA   Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA   Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA   Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., Brown S.J.,
RA   Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., Lorenzen M., Maselli V.,
RA   Osanai M., Park Y., Robertson H.M., Tu Z., Wang J.J., Wang S., Richards S.,
RA   Song H., Zhang L., Sodergren E., Werner D., Stanke M., Morgenstern B.,
RA   Solovyev V., Kosarev P., Brown G., Chen H.C., Ermolaeva O., Hlavina W.,
RA   Kapustin Y., Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA   Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA   Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., Aranda M.,
RA   Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., Bopp D.,
RA   Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., Ferrier D.E.,
RA   Friedrich M., Gordon C.M., Jindra M., Klingler M., Lan Q., Lattorff H.M.,
RA   Laudet V., von Levetsow C., Liu Z., Lutz R., Lynch J.A., da Fonseca R.N.,
RA   Posnien N., Reuter R., Roth S., Savard J., Schinko J.B., Schmitt C.,
RA   Schoppmeier M., Schroder R., Shippy T.D., Simonnet F., Marques-Souza H.,
RA   Tautz D., Tomoyasu Y., Trauner J., Van der Zee M., Vervoort M.,
RA   Wittkopp N., Wimmer E.A., Yang X., Jones A.K., Sattelle D.B., Ebert P.R.,
RA   Nelson D., Scott J.G., Beeman R.W., Muthukrishnan S., Kramer K.J.,
RA   Arakane Y., Beeman R.W., Zhu Q., Hogenkamp D., Dixit R., Oppert B.,
RA   Jiang H., Zou Z., Marshall J., Elpidina E., Vinokurov K., Oppert C.,
RA   Zou Z., Evans J., Lu Z., Zhao P., Sumathipala N., Altincicek B.,
RA   Vilcinskas A., Williams M., Hultmark D., Hetru C., Jiang H.,
RA   Grimmelikhuijzen C.J., Hauser F., Cazzamali G., Williamson M., Park Y.,
RA   Li B., Tanaka Y., Predel R., Neupert S., Schachtner J., Verleyen P.,
RA   Raible F., Bork P., Friedrich M., Walden K.K., Robertson H.M., Angeli S.,
RA   Foret S., Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA   Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT   "The genome of the model beetle and pest Tribolium castaneum.";
RL   Nature 452:949-955(2008).
RN   [2] {ECO:0000313|EMBL:EFA08534.1, ECO:0000313|Proteomes:UP000007266}
RP   GENOME REANNOTATION.
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA08534.1,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=19820115; DOI=10.1093/nar/gkp807;
RA   Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA   Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT   "BeetleBase in 2010: revisions to provide comprehensive genomic information
RT   for Tribolium castaneum.";
RL   Nucleic Acids Res. 38:D437-D442(2010).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       {ECO:0000256|RuleBase:RU003805}.
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         ECO:0000256|RuleBase:RU003805};
CC   -!- SIMILARITY: Belongs to the phage and mitochondrial RNA polymerase
CC       family. {ECO:0000256|ARBA:ARBA00009493, ECO:0000256|RuleBase:RU003805}.
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DR   EMBL; KQ971357; EFA08534.1; -; Genomic_DNA.
DR   RefSeq; XP_967600.2; XM_962507.3.
DR   AlphaFoldDB; D6WV41; -.
DR   STRING; 7070.D6WV41; -.
DR   EnsemblMetazoa; TC006188_001; TC006188_001; TC006188.
DR   GeneID; 655952; -.
DR   KEGG; tca:655952; -.
DR   eggNOG; KOG1038; Eukaryota.
DR   HOGENOM; CLU_003364_2_0_1; -.
DR   InParanoid; D6WV41; -.
DR   OMA; WWAKSDE; -.
DR   OrthoDB; 143789at2759; -.
DR   PhylomeDB; D6WV41; -.
DR   Proteomes; UP000007266; Linkage group 8.
DR   GO; GO:0034245; C:mitochondrial DNA-directed RNA polymerase complex; IBA:GO_Central.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IBA:GO_Central.
DR   GO; GO:0001018; F:mitochondrial promoter sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProt.
DR   GO; GO:0006390; P:mitochondrial transcription; IBA:GO_Central.
DR   Gene3D; 1.10.287.280; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 1.10.1320.10; DNA-directed RNA polymerase, N-terminal domain; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR046950; DNA-dir_Rpol_C_phage-type.
DR   InterPro; IPR002092; DNA-dir_Rpol_phage-type.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR037159; RNA_POL_N_sf.
DR   InterPro; IPR029262; RPOL_N.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR10102; DNA-DIRECTED RNA POLYMERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR10102:SF0; DNA-DIRECTED RNA POLYMERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00940; RNA_pol; 1.
DR   Pfam; PF14700; RPOL_N; 1.
DR   SMART; SM01311; RPOL_N; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   PROSITE; PS00900; RNA_POL_PHAGE_1; 1.
DR   PROSITE; PS00489; RNA_POL_PHAGE_2; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW   ECO:0000256|RuleBase:RU003805};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU003805};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007266};
KW   Transcription {ECO:0000256|RuleBase:RU003805};
KW   Transferase {ECO:0000256|RuleBase:RU003805}.
FT   DOMAIN          411..731
FT                   /note="DNA-directed RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01311"
SQ   SEQUENCE   1258 AA;  143509 MW;  CAA40D757934C698 CRC64;
     MYRLFNTRIS SFRKLTNLSS GFNSENVNFK VRDGGGLLNT QLNNYCIACA RNQSTNTNPN
     LAPKKIRKRS KSKKSYYDLL VVTETNAKQQ KTSIKKLTWN DLKLLASTNL NLSELHKLKD
     LTKDNQHVQE HTYNNLAVID PIAAEETPNE KERVVTITDI PQPPEQPQPP VEELLDTIPK
     IDFLQPEIID EPPEISEVSD PAPKINLSKK ARYEISVKTL GSYLEMCSTL QTPNRGLNAL
     IFHNQRATRG KDLTFATMKS IKVYNAVLKG FAAKGETSRL EEVLAMVRKE NVKLNLQSYI
     AILECYGRAN FHDHYLKQIR IYAKEAVTNG FTFDRMLNEG TFLNDERAVV LATMQKFDPS
     YRPKYAEPIV QYDNELVNSL NHDSQLELPE EGRLIDETGL FTPGFMQSAV AKQLELEKTG
     QIVVKSIENR GKVSDEVTKY REIMNQHIRD WEETAAKAFN RDLSALAAQK SPLNPEIYMR
     SIPLKDFVTI LVNEAKQIAE GSETYSPTVN QLYRDLGSKV YARYKILRKQ KTGVLDKVQS
     IHSRYCQSYA HQHEELGVLP ETVHHVNPRQ QWQWFEYSMK GTGATLTMDH RTWSPSTLQT
     IGKFLYKIVM HDLKVDVNAM KANIKHKNNH PAFYTVFRTQ GRVLKEEVKP HPVLARLFRA
     SMPETLTFPA NELPMFCPPV PWTCVDNGGY LIVPCEVVRL PPQATSQKQR LYQSEVQQLY
     PPLDALNQLA AVAWKVNTDV LDVILEVFNN GGSAKLDVPE PPTALARPQA ITNDMDKAQK
     FKLFRQKLQY RRKKAEMYSL WCDCLYRLSL ANHFRSDIFW LPHNMDFRGR VYPVPPHLNH
     LGSDLARSML VFAESRPLGP DGLNWLKLHL INLTGLKKRD SITDRLAYAD TIMDDILDSA
     DSPLTGRQWW AESEEPWQTL ACCIEIAKAT RSGNPETYRS HFPVHQDGSC NGLQHYAALG
     RDSAGAYSVN LCPSEVPQDV YSAVVALVEQ QRLVDAANGV EVAKALHGFV KRKVIKQTIM
     TTVYGVTKYG ARLQIARQLK DIDDFPKDLV WAASSYLTGR TFDSLRSMFT STREIQDWFT
     DCARLISMSG QHVEWVTPMG LPIVQPYIRY KNLGTSLVYK PYHMDEFEKP NVMKQKNAFP
     PNFIHSLDSS HMMLTSLFCE RAGITFVSVH DCYWTHPSTV DIMNKICREQ FVALHSLPIL
     ENLSMFLTEK YSFRNDDLIG DGSISDLTKT KLNKVLRKLP KTGDFDITQV LKSVYFFS
//
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