RPO10_METTH
ID RPO10_METTH Reviewed; 55 AA.
AC O26147;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 141.
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};
DE AltName: Full=RPB10 {ECO:0000303|PubMed:10841539};
GN Name=rpo10 {ECO:0000255|HAMAP-Rule:MF_00250};
GN Synonyms=rpoN {ECO:0000255|HAMAP-Rule:MF_00250}; OrderedLocusNames=MTH_40;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
RN [2]
RP STRUCTURE BY NMR IN COMPLEX WITH ZINC, AND COFACTOR.
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=10841539; DOI=10.1073/pnas.97.12.6316;
RA Mackereth C.D., Arrowsmith C.H., Edwards A.M., McIntosh L.P.;
RT "Zinc-bundle structure of the essential RNA polymerase subunit RPB10 from
RT Methanobacterium thermoautotrophicum.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:6316-6321(2000).
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 ECO:0000269|PubMed:10841539};
CC Note=Binds 1 zinc ion. {ECO:0000255|HAMAP-Rule:MF_00250,
CC ECO:0000269|PubMed:10841539};
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; AE000666; AAB84548.1; -; Genomic_DNA.
DR PIR; A69152; A69152.
DR RefSeq; WP_010875681.1; NC_000916.1.
DR PDB; 1EF4; NMR; -; A=1-55.
DR PDBsum; 1EF4; -.
DR AlphaFoldDB; O26147; -.
DR BMRB; O26147; -.
DR SMR; O26147; -.
DR STRING; 187420.MTH_40; -.
DR EnsemblBacteria; AAB84548; AAB84548; MTH_40.
DR GeneID; 1470002; -.
DR KEGG; mth:MTH_40; -.
DR PATRIC; fig|187420.15.peg.39; -.
DR HOGENOM; CLU_143122_1_1_2; -.
DR OMA; YCCRRMF; -.
DR EvolutionaryTrace; O26147; -.
DR Proteomes; UP000005223; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-directed RNA polymerase; Metal-binding;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..55
FT /note="DNA-directed RNA polymerase subunit Rpo10"
FT /id="PRO_0000121353"
FT BINDING 6
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00250,
FT ECO:0000269|PubMed:10841539, ECO:0007744|PDB:1EF4"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00250,
FT ECO:0000269|PubMed:10841539, ECO:0007744|PDB:1EF4"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00250,
FT ECO:0000269|PubMed:10841539, ECO:0007744|PDB:1EF4"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00250,
FT ECO:0000269|PubMed:10841539, ECO:0007744|PDB:1EF4"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:1EF4"
FT HELIX 14..26
FT /evidence="ECO:0007829|PDB:1EF4"
FT HELIX 30..37
FT /evidence="ECO:0007829|PDB:1EF4"
FT HELIX 42..48
FT /evidence="ECO:0007829|PDB:1EF4"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:1EF4"
SQ SEQUENCE 55 AA; 6434 MW; A858F89CB5409C95 CRC64;
MIPVRCLSCG KPVSAYFNEY QRRVADGEDP KDVLDDLGLK RYCCRRMLIS HVETW
