ID A0A498G9E8_9EURY Unreviewed; 44 AA.
AC A0A498G9E8;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 22-FEB-2023, entry version 15.
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=D3D02_04845 {ECO:0000313|EMBL:RLM90111.1};
OS Halobellus sp. Atlit-38R.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Halobellus.
OX NCBI_TaxID=2282131 {ECO:0000313|EMBL:RLM90111.1, ECO:0000313|Proteomes:UP000277703};
RN [1] {ECO:0000313|EMBL:RLM90111.1, ECO:0000313|Proteomes:UP000277703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Atlit-38R {ECO:0000313|EMBL:RLM90111.1,
RC ECO:0000313|Proteomes:UP000277703};
RA Turgeman-Grott I.;
RT "Pervasive acquisition of CRISPR memory from multiple replicons driven by
RT inter-species mating of archaea.";
RL Submitted (SEP-2018) 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_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:RLM90111.1}.
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DR EMBL; QXIJ01000003; RLM90111.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498G9E8; -.
DR OrthoDB; 129238at2157; -.
DR Proteomes; UP000277703; 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}; Reference proteome {ECO:0000313|Proteomes:UP000277703};
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 8
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00615"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00615"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00615"
SQ SEQUENCE 44 AA; 5115 MW; DE2930EAA4CADFAC CRC64;
MSYKCSRCKR DVELDEYGGV RCPYCGHRVL LKERAPDVKE VPVE
//