GenomeNet

Database: UniProt
Entry: A0A135VYC9_9ARCH
LinkDB: A0A135VYC9_9ARCH
Original site: A0A135VYC9_9ARCH 
ID   A0A135VYC9_9ARCH        Unreviewed;        47 AA.
AC   A0A135VYC9;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=AM324_12240 {ECO:0000313|EMBL:KXH77678.1};
OS   Candidatus Thorarchaeota archaeon SMTZ1-83.
OC   Archaea; Asgard group; Candidatus Thorarchaeota.
OX   NCBI_TaxID=1706445 {ECO:0000313|EMBL:KXH77678.1, ECO:0000313|Proteomes:UP000070043};
RN   [1] {ECO:0000313|EMBL:KXH77678.1, ECO:0000313|Proteomes:UP000070043}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMTZ1-83 {ECO:0000313|EMBL:KXH77678.1};
RX   PubMed=26824177;
RA   Seitz K.W., Lazar C.S., Hinrichs K.U., Teske A.P., Baker B.J.;
RT   "Genomic reconstruction of a novel, deeply branched sediment archaeal
RT   phylum with pathways for acetogenesis and sulfur reduction.";
RL   ISME J. 0:0-0(2016).
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:KXH77678.1}.
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; LRSK01000043; KXH77678.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135VYC9; -.
DR   Proteomes; UP000070043; 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         8
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"
FT   BINDING         28
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00615"
SQ   SEQUENCE   47 AA;  5254 MW;  9E0EA906CE4F027B CRC64;
     MVYICHSCHK EVTPEGLKTL PGVKCPYCGG RILYKIRPPV VKRVKGV
//
DBGET integrated database retrieval system