RPO10_SULAC
ID RPO10_SULAC Reviewed; 66 AA.
AC P39472; Q4JCG5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 118.
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, ECO:0000269|Ref.4};
DE AltName: Full=DNA-directed RNA polymerase subunit N {ECO:0000255|HAMAP-Rule:MF_00250, ECO:0000303|PubMed:7597027};
GN Name=rpo10 {ECO:0000255|HAMAP-Rule:MF_00250};
GN Synonyms=rpoN {ECO:0000255|HAMAP-Rule:MF_00250,
GN ECO:0000303|PubMed:7597027}; OrderedLocusNames=Saci_0087;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=7597027; DOI=10.1073/pnas.92.13.5768;
RA Langer D., Hain J., Thuriaux P., Zillig W.;
RT "Transcription in archaea: similarity to that in eucarya.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:5768-5772(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
RN [3]
RP PROTEIN SEQUENCE OF 1-23, AND SUBUNIT.
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=1729711; DOI=10.1073/pnas.89.1.407;
RA Klenk H.-P., Palm P., Lottspeich F., Zillig W.;
RT "Component H of the DNA-dependent RNA polymerases of Archaea is homologous
RT to a subunit shared by the three eucaryal nuclear RNA polymerases.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:407-410(1992).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX DOI=10.1016/S0723-2020(11)80337-1;
RA Lanzendorfer M., Langer D., Hain J., Klenk H.-P., Holz I., Arnold-Ammer I.,
RA Zillig W.;
RT "Structure and Function of the DNA-Dependent RNA Polymerase of
RT Sulfolobus.";
RL Syst. Appl. Microbiol. 16:656-664(1994).
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 ECO:0000269|Ref.4}.
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 ECO:0000269|Ref.4};
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 13-subunit RNA polymerase complex.
CC {ECO:0000269|PubMed:1729711, ECO:0000269|Ref.4}.
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; X80194; CAA56484.1; -; Genomic_DNA.
DR EMBL; CP000077; AAY79514.1; -; Genomic_DNA.
DR PIR; S47027; S47027.
DR RefSeq; WP_011277015.1; NC_007181.1.
DR PDB; 7OK0; EM; 2.90 A; N=1-66.
DR PDB; 7OQ4; EM; 3.27 A; N=1-66.
DR PDB; 7OQY; EM; 2.61 A; N=1-66.
DR PDBsum; 7OK0; -.
DR PDBsum; 7OQ4; -.
DR PDBsum; 7OQY; -.
DR AlphaFoldDB; P39472; -.
DR SMR; P39472; -.
DR STRING; 330779.Saci_0087; -.
DR EnsemblBacteria; AAY79514; AAY79514; Saci_0087.
DR GeneID; 3473863; -.
DR KEGG; sai:Saci_0087; -.
DR PATRIC; fig|330779.12.peg.81; -.
DR eggNOG; arCOG04244; Archaea.
DR HOGENOM; CLU_143122_1_1_2; -.
DR OMA; YCCRRMF; -.
DR Proteomes; UP000001018; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:UniProtKB.
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; Direct protein sequencing;
KW DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase;
KW Reference proteome; Transcription; Transferase; Zinc.
FT CHAIN 1..66
FT /note="DNA-directed RNA polymerase subunit Rpo10"
FT /id="PRO_0000121361"
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"
FT CONFLICT 17
FT /note="K -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 19
FT /note="E -> I (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 18..25
FT /evidence="ECO:0007829|PDB:7OQY"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 31..38
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 43..50
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:7OQY"
SQ SEQUENCE 66 AA; 7662 MW; A31441B268749D5F CRC64;
MIIPIRCFTC GAVVADKWEP FSNRVMGGED PEKVLTELGV NRYCCRRMLL SHVNIIREII
HYTRPI