ID A0A564QBT7_9EURY Unreviewed; 62 AA. AC A0A564QBT7; DT 16-OCT-2019, integrated into UniProtKB/TrEMBL. DT 16-OCT-2019, sequence version 1. DT 22-APR-2020, entry version 4. DE RecName: Full=DNA-directed RNA polymerase subunit N {ECO:0000256|HAMAP-Rule:MF_00250}; DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_00250}; GN Name=rpoN {ECO:0000256|HAMAP-Rule:MF_00250}; GN ORFNames=SYNGOMJ08_00320 {ECO:0000313|EMBL:VUT27769.1}; OS Candidatus Syntrophoarchaeum sp. GoM_oil. OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia; OC Methanosarcinales; ANME-2 cluster; Candidatus Syntrophoarchaeum; OC unclassified Candidatus Syntrophoarchaeum. OX NCBI_TaxID=2588693 {ECO:0000313|EMBL:VUT27769.1, ECO:0000313|Proteomes:UP000384390}; RN [1] {ECO:0000313|EMBL:VUT27769.1, ECO:0000313|Proteomes:UP000384390} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Gfbio:sag-sample:67c8463b-6cbd-4d56-a398-d795175a9500 RC {ECO:0000313|EMBL:VUT27769.1}; RA Weber M., Kostadinov I., Kostadinov D I.; RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of CC DNA into RNA using the four ribonucleoside triphosphates as substrates. CC {ECO:0000256|HAMAP-Rule:MF_00250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA- CC COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:83400; CC EC=2.7.7.6; Evidence={ECO:0000256|HAMAP-Rule:MF_00250}; CC -!- SIMILARITY: Belongs to the archaeal RpoN/eukaryotic RPB10 RNA CC polymerase subunit family. {ECO:0000256|HAMAP-Rule:MF_00250}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CABGHI010000005; VUT27769.1; -; Genomic_DNA. DR Proteomes; UP000384390; Unassembled WGS sequence. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule. DR HAMAP; MF_00250; RNApol_arch_N; 1. DR InterPro; IPR023580; RNA_pol_su_RPB10. DR InterPro; IPR020789; RNA_pol_suN_Zn-BS. DR InterPro; IPR000268; RNAP_N/Rpb10. DR PANTHER; PTHR23431; PTHR23431; 1. DR Pfam; PF01194; RNA_pol_N; 1. DR PIRSF; PIRSF005653; RNA_pol_N/8_sub; 1. DR SUPFAM; SSF46924; SSF46924; 1. DR PROSITE; PS01112; RNA_POL_N_8KD; 1. PE 3: Inferred from homology; KW DNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_00250, KW ECO:0000313|EMBL:VUT27769.1}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00250}; KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00250, KW ECO:0000313|EMBL:VUT27769.1}; KW Transcription {ECO:0000256|HAMAP-Rule:MF_00250}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00250, ECO:0000313|EMBL:VUT27769.1}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00250}. FT METAL 6 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00250" FT METAL 9 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00250" FT METAL 43 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00250" FT METAL 44 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00250" SQ SEQUENCE 62 AA; 7204 MW; 8248EE3004D10D80 CRC64; MIPVRCFTCG KVVGGLWEEY KERRDAGEDP GKVLDDLGVE RYCCRRMLLA HLEIVDKFVP YQ //