ID   A1CED1_ASPCL            Unreviewed;       147 AA.
AC   A1CED1;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   03-APR-2013, entry version 39.
DE   RecName: Full=DNA-directed RNA polymerase subunit;
DE            EC=2.7.7.6;
GN   ORFNames=ACLA_089220;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC
OS   3887 / NRRL 1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae;
OC   mitosporic Trichocomaceae; Aspergillus.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P.,
RA   Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A.,
RA   Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A.,
RA   Galens K., Fraser-Liggett C.M., Haas B.J., Inman J.M., Kent R.,
RA   Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M.,
RA   Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R.,
RA   Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R.,
RA   Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription
CC       of DNA into RNA using the four ribonucleoside triphosphates as
CC       substrates (By similarity).
CC   -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
CC       + RNA(n+1).
CC   -!- SUBUNIT: Component of the RNA polymerase (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the archaeal rpoM/eukaryotic
CC       RPA12/RPB9/RPC11 RNA polymerase family.
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DR   EMBL; DS027052; EAW11230.1; -; Genomic_DNA.
DR   RefSeq; XP_001272656.1; XM_001272655.1.
DR   ProteinModelPortal; A1CED1; -.
DR   STRING; 5057.CADACLAP00008213; -.
DR   EnsemblFungi; CADACLAT00008423; CADACLAP00008213; CADACLAG00008423.
DR   GeneID; 4705320; -.
DR   KEGG; act:ACLA_089220; -.
DR   HOGENOM; HOG000228133; -.
DR   KO; K03000; -.
DR   OrthoDB; EOG45QMPS; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-dependent; IEA:InterPro.
DR   InterPro; IPR019761; DNA-dir_RNA_pol-M_15_CS.
DR   InterPro; IPR012164; DNA-dir_RNApol_C11.
DR   InterPro; IPR001222; Znf_TFIIS.
DR   Pfam; PF01096; TFIIS_C; 1.
DR   PIRSF; PIRSF005586; RNApol_RpoM; 1.
DR   SMART; SM00440; ZnF_C2C2; 1.
DR   PROSITE; PS01030; RNA_POL_M_15KD; 1.
DR   PROSITE; PS51133; ZF_TFIIS_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; DNA-directed RNA polymerase; Nucleus;
KW   Transcription.
SQ   SEQUENCE   147 AA;  15851 MW;  1DB533F7F20D581B CRC64;
     MSAIGSLIFC TDCGNLLPES TGDPTKVLLC DVCGARNKDT VPNTIVSESK PNAFPSALRA
     KRSAVQTLTA EDKRTEALTQ HTCARCGRKE MYFTTVQLRS ADEGSTVFYT CVCGYKYANP
     VAHLFVALNA DNYSQGNCKQ LGARGRG
//