ID A0A2H9PLP2_9ARCH Unreviewed; 65 AA. AC A0A2H9PLP2; DT 28-FEB-2018, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 1. DT 22-FEB-2023, entry version 16. DE RecName: Full=DNA-directed RNA polymerase subunit Rpo10 {ECO:0000256|HAMAP-Rule:MF_00250}; DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_00250}; DE AltName: Full=DNA-directed RNA polymerase subunit N {ECO:0000256|HAMAP-Rule:MF_00250}; GN Name=rpo10 {ECO:0000256|HAMAP-Rule:MF_00250}; GN Synonyms=rpoN {ECO:0000256|HAMAP-Rule:MF_00250}; GN ORFNames=COY27_05365 {ECO:0000313|EMBL:PIZ50946.1}; OS Candidatus Woesearchaeota archaeon CG_4_10_14_0_2_um_filter_33_13. OC Archaea; Candidatus Woesearchaeota. OX NCBI_TaxID=1974449 {ECO:0000313|EMBL:PIZ50946.1, ECO:0000313|Proteomes:UP000230948}; RN [1] {ECO:0000313|Proteomes:UP000230948} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Probst A.J., Ladd B., Jarett J.K., Geller-Mcgrath D.E., Sieber C.M.K., RA Emerson J.B., Anantharaman K., Thomas B.C., Malmstrom R., Stieglmeier M., RA Klingl A., Woyke T., Ryan C.M., Banfield J.F.; RT "Depth-based differentiation of microbial function through sediment-hosted RT aquifers and enrichment of novel symbionts in the deep terrestrial RT subsurface."; RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the CC transcription of DNA into RNA using the four ribonucleoside CC triphosphates as substrates. {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:14527, Rhea:RHEA- CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; CC EC=2.7.7.6; Evidence={ECO:0000256|HAMAP-Rule:MF_00250}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00250}; CC Note=Binds 1 zinc ion. {ECO:0000256|HAMAP-Rule:MF_00250}; CC -!- SUBUNIT: Part of the RNA polymerase complex. {ECO:0000256|HAMAP- CC Rule:MF_00250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00250}. CC -!- SIMILARITY: Belongs to the archaeal Rpo10/eukaryotic RPB10 RNA CC polymerase subunit family. {ECO:0000256|HAMAP-Rule:MF_00250}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:PIZ50946.1}. 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; PFNQ01000043; PIZ50946.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2H9PLP2; -. DR Proteomes; UP000230948; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006351; P:DNA-templated transcription; IEA:UniProtKB-UniRule. DR Gene3D; 1.10.10.60; Homeodomain-like; 1. DR HAMAP; MF_00250; RNApol_arch_Rpo10; 1. DR InterPro; IPR023580; RNA_pol_su_RPB10. DR InterPro; IPR020789; RNA_pol_suN_Zn-BS. DR InterPro; IPR000268; RPABC5/Rpb10. DR PANTHER; PTHR23431:SF3; DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC5; 1. DR PANTHER; PTHR23431; DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC5 FAMILY MEMBER; 1. DR Pfam; PF01194; RNA_pol_N; 1. DR PIRSF; PIRSF005653; RNA_pol_N/8_sub; 1. DR SUPFAM; SSF46924; RNA polymerase subunit RPB10; 1. DR PROSITE; PS01112; RNA_POL_N_8KD; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00250}; KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478, KW ECO:0000256|HAMAP-Rule:MF_00250}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00250}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP- KW Rule:MF_00250}; KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP- KW Rule:MF_00250}; Transferase {ECO:0000256|HAMAP-Rule:MF_00250}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00250}. FT BINDING 7 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00250" FT BINDING 10 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00250" FT BINDING 44 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00250" FT BINDING 45 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00250" SQ SEQUENCE 65 AA; 7394 MW; A1397D24804E74FD CRC64; MIIPIRCFSC GKPIGHLYEE YRERVDKGED AKKVLDSLEV ERYCCRAVFL GQVDLIDIAG AFKKG //