ID A0A2A2HC40_9EURY Unreviewed; 43 AA.
AC A0A2A2HC40;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo12 {ECO:0000256|HAMAP-Rule:MF_00615};
DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_00615};
DE AltName: Full=DNA-directed RNA polymerase subunit P {ECO:0000256|HAMAP-Rule:MF_00615};
GN Name=rpo12 {ECO:0000256|HAMAP-Rule:MF_00615};
GN Synonyms=rpoP {ECO:0000256|HAMAP-Rule:MF_00615};
GN ORFNames=ASJ82_06555 {ECO:0000313|EMBL:PAV06803.1}, MSCUN_02000
GN {ECO:0000313|EMBL:PWL08874.1};
OS Methanosphaera cuniculi.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX NCBI_TaxID=1077256 {ECO:0000313|EMBL:PAV06803.1, ECO:0000313|Proteomes:UP000217528};
RN [1] {ECO:0000313|EMBL:PWL08874.1, ECO:0000313|Proteomes:UP000246004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4103 {ECO:0000313|EMBL:PWL08874.1,
RC ECO:0000313|Proteomes:UP000246004};
RA Poehlein A., Seedorf H., Daniel R.;
RT "Genome sequence of Methanosphaera cuniculi DSM 4103.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PAV06803.1, ECO:0000313|Proteomes:UP000217528}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1R-7 {ECO:0000313|EMBL:PAV06803.1,
RC ECO:0000313|Proteomes:UP000217528};
RX PubMed=28826405; DOI=10.1186/s12864-017-4036-4;
RA Gilmore S.P., Henske J.K., Sexton J.A., Solomon K.V., Seppala S., Yoo J.I.,
RA Huyett L.M., Pressman A., Cogan J.Z., Kivenson V., Peng X., Tan Y.,
RA Valentine D.L., O'Malley M.A.;
RT "Genomic analysis of methanogenic archaea reveals a shift towards energy
RT conservation.";
RL BMC Genomics 18:639-639(2017).
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_00615}.
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_00615};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00615};
CC Note=Binds 1 zinc ion. {ECO:0000256|HAMAP-Rule:MF_00615};
CC -!- SUBUNIT: Part of the RNA polymerase complex. {ECO:0000256|HAMAP-
CC Rule:MF_00615}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00615}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo12/eukaryotic RPC10 RNA
CC polymerase subunit family. {ECO:0000256|HAMAP-Rule:MF_00615}.
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:PAV06803.1}.
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DR EMBL; LMVN01000026; PAV06803.1; -; Genomic_DNA.
DR EMBL; LWMS01000006; PWL08874.1; -; Genomic_DNA.
DR RefSeq; WP_069592306.1; NZ_LWMS01000006.1.
DR AlphaFoldDB; A0A2A2HC40; -.
DR OrthoDB; 129238at2157; -.
DR Proteomes; UP000217528; Unassembled WGS sequence.
DR Proteomes; UP000246004; 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; 2.20.28.30; RNA polymerase ii, chain L; 1.
DR HAMAP; MF_00615; RNApol_arch_Rpo12; 1.
DR InterPro; IPR006591; RNAP_P/RPABC4.
DR InterPro; IPR029040; RPABC4/Spt4.
DR InterPro; IPR023464; Rpo12.
DR Pfam; PF03604; DNA_RNApol_7kD; 1.
DR SMART; SM00659; RPOLCX; 1.
DR SUPFAM; SSF63393; RNA polymerase subunits; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00615};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|HAMAP-Rule:MF_00615};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00615};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00615};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00615};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00615};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00615}.
FT BINDING 7
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00615"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00615"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00615"
SQ SEQUENCE 43 AA; 5111 MW; E01828C2B94F1F4B CRC64;
MYKCINCGQT VDIKKYSESK CPKCRYRILF KEVPVVKRTV KAR
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