RPO10_HYPBU
ID RPO10_HYPBU Reviewed; 66 AA.
AC A2BK83;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo10 {ECO:0000255|HAMAP-Rule:MF_00250};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00250};
DE AltName: Full=DNA-directed RNA polymerase subunit N {ECO:0000255|HAMAP-Rule:MF_00250};
GN Name=rpo10 {ECO:0000255|HAMAP-Rule:MF_00250};
GN Synonyms=rpoN {ECO:0000255|HAMAP-Rule:MF_00250};
GN OrderedLocusNames=Hbut_0534;
OS Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC Hyperthermus.
OX NCBI_TaxID=415426;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5456 / JCM 9403 / PLM1-5;
RX PubMed=17350933; DOI=10.1155/2007/745987;
RA Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M.,
RA She Q., Garrett R.A., Klenk H.-P.;
RT "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL Archaea 2:127-135(2007).
CC -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the
CC transcription of DNA into RNA using the four ribonucleoside
CC triphosphates as substrates. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00250};
CC Note=Binds 1 zinc ion. {ECO:0000255|HAMAP-Rule:MF_00250};
CC -!- SUBUNIT: Part of the RNA polymerase complex. {ECO:0000255|HAMAP-
CC Rule:MF_00250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00250}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo10/eukaryotic RPB10 RNA
CC polymerase subunit family. {ECO:0000255|HAMAP-Rule:MF_00250}.
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DR EMBL; CP000493; ABM80394.1; -; Genomic_DNA.
DR RefSeq; WP_011821712.1; NC_008818.1.
DR AlphaFoldDB; A2BK83; -.
DR SMR; A2BK83; -.
DR STRING; 415426.Hbut_0534; -.
DR EnsemblBacteria; ABM80394; ABM80394; Hbut_0534.
DR GeneID; 4782386; -.
DR KEGG; hbu:Hbut_0534; -.
DR eggNOG; arCOG04244; Archaea.
DR HOGENOM; CLU_143122_1_1_2; -.
DR OMA; YCCRRMF; -.
DR OrthoDB; 123859at2157; -.
DR Proteomes; UP000002593; Chromosome.
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:transcription, DNA-templated; IEA:UniProtKB-UniRule.
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; 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 Cytoplasm; DNA-directed RNA polymerase; Metal-binding;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..66
FT /note="DNA-directed RNA polymerase subunit Rpo10"
FT /id="PRO_0000304190"
FT BINDING 7
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00250"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00250"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00250"
FT BINDING 45
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00250"
SQ SEQUENCE 66 AA; 7859 MW; 7DD1EBB9F7B5429E CRC64;
MIIPMRCFTC GRPLAQYWEE FRSRVEGGED PRKVLDELGV KRYCCRKTLL AHVPAIYEVR
KFKRVL