ID   RPOM_SCHPO              Reviewed;        1154 AA.
AC   O13993;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2012, sequence version 2.
DT   02-SEP-2026, entry version 146.
DE   RecName: Full=DNA-directed RNA polymerase, mitochondrial;
DE            EC=2.7.7.6;
DE   Flags: Precursor;
GN   Name=rpo41; ORFNames=SPAC26H5.12;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
RN   [3]
RP   FUNCTION.
RX   PubMed=21357609; DOI=10.1093/nar/gkr103;
RA   Jiang H., Sun W., Wang Z., Zhang J., Chen D., Murchie A.I.;
RT   "Identification and characterization of the mitochondrial RNA polymerase
RT   and transcription factor in the fission yeast Schizosaccharomyces pombe.";
RL   Nucleic Acids Res. 39:5119-5130(2011).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       Combines in the mitochondrion with mitochondrial transcription factor
CC       mtf1 as a holoenzyme to recognize and initiate transcription at the
CC       core mitochondrial promoters. {ECO:0000269|PubMed:21357609}.
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:0000255|PROSITE-ProRule:PRU10031,
CC         ECO:0000255|PROSITE-ProRule:PRU10032};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the phage and mitochondrial RNA polymerase
CC       family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB16197.2; -; Genomic_DNA.
DR   PIR; T38431; T38431.
DR   RefSeq; NP_594459.2; NM_001019888.3.
DR   AlphaFoldDB; O13993; -.
DR   SMR; O13993; -.
DR   BioGRID; 279140; 3.
DR   FunCoup; O13993; 143.
DR   STRING; 284812.O13993; -.
DR   iPTMnet; O13993; -.
DR   PaxDb; 284812-O13993; -.
DR   GeneID; 2542687; -.
DR   KEGG; spo:2542687; -.
DR   PomBase; SPAC26H5.12; rpo41.
DR   VEuPathDB; FungiDB:SPAC26H5.12; -.
DR   eggNOG; KOG1038; Eukaryota.
DR   HOGENOM; CLU_003364_1_0_1; -.
DR   InParanoid; O13993; -.
DR   OMA; KWFEVDM; -.
DR   Reactome; R-SPO-163282; Mitochondrial transcription initiation.
DR   PRO; PR:O13993; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0034245; C:mitochondrial DNA-directed RNA polymerase complex; IDA:PomBase.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:PomBase.
DR   GO; GO:0005739; C:mitochondrion; IDA:PomBase.
DR   GO; GO:0003899; F:DNA-directed RNA polymerase activity; EXP:PomBase.
DR   GO; GO:0001018; F:mitochondrial promoter sequence-specific DNA binding; EXP:PomBase.
DR   GO; GO:0006390; P:mitochondrial transcription; IBA:GO_Central.
DR   GO; GO:0006391; P:transcription initiation at mitochondrial promoter; IMP:PomBase.
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; 1.10.287.280; -; 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; 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   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; Mitochondrion; Nucleotidyltransferase;
KW   Reference proteome; Transcription; Transferase; Transit peptide.
FT   TRANSIT         1..30
FT                   /note="Mitochondrion"
FT   CHAIN           31..1154
FT                   /note="DNA-directed RNA polymerase, mitochondrial"
FT                   /id="PRO_0000031077"
FT   REGION          221..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..240
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        821
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        890
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        1061
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1154 AA;  131503 MW;  DE08F7549EF0CD3B CRC64;
     MLRRKIQTYL SRSHIRRGLC GLRFFQTQRL HTDYMPIEAY EPYKNELKSK IGKDFIIDLS
     YKSGTASLFE ACVYNGDFLR SKQLLKSFID HNKGDKILLP MINLYIREII QRGSFELTDV
     LSNAKELLQQ ARLNGDSLTY ALLCQASLNP TQRQLGLPVL HELIHNWRSA NGKVIDILMH
     ESVFSPEEVK LIMDQLNIPI NNFTPSQLQL LGITNSTIVG ESENGKDQNG DSSLKEKQPD
     VETTVTKSAN LNALRSSLSS LLTESIDLPI DEVSLEFGNQ GDTFNLARQK LLEKSAILSA
     AEVWKSEHES VLNRGNLQVP KNVSSLFYSW YVQLEQLFKE EISLIDDLAL NESLDKKNDR
     LIYGPFLKLL SSKKLAALTI MEVAQLSTNP RYDRGARVTT LLGGLGRSFE REFLSEQIQR
     QEKNKSYKDK KRLKELFNDP RKFRQAVKNL RLSNTRDNIV LNPSVDSWPS AIVMKVGSVA
     LCLLLSVAKI EVTAKDLSTG GILKQEVAAF VHTYQYSNGR KVGMIVPHVE FYKLLSRDIE
     KPHLHPQLLP MLVTPKPWTS WIDGGYYYSR QPLVRLKGAL EQVDYLMKAS ENGQLDELFK
     AVSSLGKVSW RINQRLFNVL IRIWNSGEKF LSIPPREVKC DMPPYPKNSI NPRDKVIWHT
     RRKELAALKT GAHSQRCDFN YKLEIARAFL NEKFYFPHSL DFRGRAYPLS SHLHHVSNDV
     CRGLLEFSTG KPLGPKGLNW LKVHLANLFG ISKKDFATRQ AFVDDNMQEV FDSADRPLDG
     NKWWSKADDP FQALAACFEI AEAVRSGDHE SYISHIPIQQ DGTCNGLQHY AALGGDIEGA
     KQVNLWPSDH PSDVYEAVAE IVRGFLKKDA EAGDEMANFL KDKVTRSVVK PTVMTNVYGV
     TYVGARKQIS EKLENIDGME KLKVADYANY LTKKVFEALR SLFTQAHEIQ DWLSACCNLI
     THSLPADYIK EGIKDELTPV VWTTLLNLPI VQPYRNYKSR QIRTNLQTVF IEERDRTATV
     QPHKQATAFP PNFIHSLDAT HMFMTCLKCS EQNINFAAVH DSYWTHACDV DQMNSLLREA
     FVLLHSNNIM ERLKQEFEER YKGFLVSKKA IKANDEDLKA KFGNKSYIPL EFPPLPARGA
     LDLKKVLESK YFFS
//