ID   C5DNP3_LACTC            Unreviewed;      1289 AA.
AC   C5DNP3;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   02-SEP-2026, entry version 81.
DE   RecName: Full=DNA-directed RNA polymerase {ECO:0000256|PROSITE-ProRule:PRU10031, ECO:0000256|RuleBase:RU003805};
DE            EC=2.7.7.6 {ECO:0000256|PROSITE-ProRule:PRU10031, ECO:0000256|RuleBase:RU003805};
GN   OrderedLocusNames=KLTH0G18744g {ECO:0000313|EMBL:CAR25404.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR25404.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR25404.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
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=RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) +
CC         diphosphate; 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:ARBA00048552,
CC         ECO:0000256|PROSITE-ProRule:PRU10031, ECO:0000256|RuleBase:RU003805};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
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; CU928171; CAR25404.1; -; Genomic_DNA.
DR   FunCoup; C5DNP3; 304.
DR   STRING; 559295.C5DNP3; -.
DR   KEGG; lth:KLTH0G18744g; -.
DR   eggNOG; KOG1038; Eukaryota.
DR   HOGENOM; CLU_003364_1_0_1; -.
DR   InParanoid; C5DNP3; -.
DR   OMA; KWFEVDM; -.
DR   OrthoDB; 276422at2759; -.
DR   Proteomes; UP000002036; Chromosome G.
DR   GO; GO:0034245; C:mitochondrial DNA-directed RNA polymerase complex; IEA:TreeGrafter.
DR   GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0001018; F:mitochondrial promoter sequence-specific DNA binding; IEA:TreeGrafter.
DR   GO; GO:0006390; P:mitochondrial transcription; IEA:UniProtKB-ARBA.
DR   FunFam; 1.10.1320.10:FF:000005; DNA-directed RNA polymerase; 1.
DR   FunFam; 1.10.150.20:FF:000041; DNA-directed RNA polymerase; 1.
DR   FunFam; 1.10.287.280:FF:000001; DNA-directed RNA polymerase; 1.
DR   Gene3D; 1.10.287.260; -; 1.
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   InterPro; IPR024075; DNA-dir_RNA_pol_helix_hairp_sf.
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   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   Pfam; PF26713; TPR_RPO41_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   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU003805};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002036};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU003805};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003805};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          352..672
FT                   /note="DNA-directed RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01311"
FT   ACT_SITE        886
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10031"
FT   ACT_SITE        955
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10032"
SQ   SEQUENCE   1289 AA;  145974 MW;  8DB3C8E07781D20C CRC64;
     MLRFSRSCSR MLVSKRLTSQ LRCVSQTAFL RKPSGNIDGL SGATGREDIG FLKSSSVSMS
     PHFGPFDHSH AVVSAAESRD IMNLWSLLEA CLHSGYMERA FSILKSLYAL KSHQAYFIDD
     YNKFLMKYAE TLHDIKDLDK KLFHDIQETF PACEYNDKTL AILIHHALKL SSSAEAKLEH
     CKIYFKMAVS GQRSILSNVD VLTVPNYKSL VHDLKLVSLN ELPAAVRPLI ESGNIVTGEM
     LSSQQSSEIN AKALSHGEVA LDRNIEPLDK DAKELLAVDT IGMKVVRHTL LGLSFTEDQK
     KQITSFNFDT SSNLLNFDQE KESIDFFEMF RNLKSEEERR SFESALDEFN QDRQHQLENR
     ATDAAKERWR HDFEEAKSRG DLSIQKKLNI KLWEWFNLML PLVKEEVRRC AAVANKTAQD
     TSLSPQEKKQ NKARQEYGPY LTLVDPEKMC VITILELLKL NSTGGIIEGM RTARAVISVG
     KAIEMEFRAE MLLKNESHVF KDVNKKSHEF KLMVQRARAT FRSIKIEESK VLWPQEARAK
     IGSILISMLI HVAKVKVEGV DPVTNEKIKG EAPAFSHGYQ YHNGSKLGVL KIHRSLIHQL
     NGERLVAAVQ PQLLPMLVKP RAWNSWNSGG YYYTQSTLIR SKDSPEQVAY LKAVSDAGAI
     DNVYRGLNVL GETPWTVNRK MFNVMSQVWN SGKPFLDIPG IQEKLTLTPQ PPRDADPSVH
     REWKLKNKEL ANEFSGNRSA RCDANYKLEI ARAFLGEKFY FPHNLDFRGR AYPLSPHFNH
     LGNDMSRGLM TFWHGKRLGS TGLRWLKVHL SNLFGFDKAP LEDRVRFAED HIDDIRDSAE
     HPLDGKCWWK EADKPWQALA TCMELNEALK MSNPDDFVSH QPVHQDGTCN GLQHYAALGG
     DIEGATQVNL VPSDRPQDVY SHVAKLVVAR LEKAAANGDE TAALLKDKIK RKVVKQTVMT
     NVYGVTYIGA THQIDKQLST LFNDHKRSYE LSKYLTKHVF ASVRELFEGA HLIQDWLGEC
     AKRISKSIRL DVDEKTLKNG NKPDFMSSVI WTTPLGLPIV QPYRENGKKQ VATNLQTVFI
     SDPFAINPIN ARRQKAGFPP NFIHSLDASH MLLSAAKCGE KGLDFAAVHD SYWTHACDVD
     TMNVVLREQF IKLHEVDLIE RLKDEFDERY KNYLQILKID KKSEVAMKVT DLKKKLSQKL
     GRPFTLADEI YMEKKRIQLL SSEDASEQAE GANMVTTVSL VAGAGDISNL EKTSDASCLV
     VLAPLTLPQI PPKGDFDVRE LEKSKYFFS
//