RPO10_SACS2
ID RPO10_SACS2 Reviewed; 66 AA.
AC Q980Z8;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
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 ECO:0000303|PubMed:11427726}; OrderedLocusNames=SSO5140;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2] {ECO:0007744|PDB:2PMZ, ECO:0007744|PDB:3HKZ}
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF THE RNA POLYMERASE COMPLEX IN
RP COMPLEX WITH ZINC, COFACTOR, AND SUBUNIT.
RX PubMed=18235446; DOI=10.1038/nature06530;
RA Hirata A., Klein B.J., Murakami K.S.;
RT "The X-ray crystal structure of RNA polymerase from Archaea.";
RL Nature 451:851-854(2008).
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:18235446, ECO:0007744|PDB:2PMZ,
CC ECO:0007744|PDB:3HKZ};
CC Note=Binds 1 zinc ion. {ECO:0000255|HAMAP-Rule:MF_00250,
CC ECO:0000269|PubMed:18235446, ECO:0007744|PDB:2PMZ,
CC ECO:0007744|PDB:3HKZ};
CC -!- SUBUNIT: Part of the 13-subunit RNA polymerase complex.
CC {ECO:0000269|PubMed:18235446}.
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; AE006641; AAK40429.1; -; Genomic_DNA.
DR PIR; F90146; F90146.
DR RefSeq; WP_009988875.1; NC_002754.1.
DR PDB; 2PMZ; X-ray; 3.40 A; N/Y=1-66.
DR PDB; 3HKZ; X-ray; 3.40 A; N/W=1-66.
DR PDBsum; 2PMZ; -.
DR PDBsum; 3HKZ; -.
DR AlphaFoldDB; Q980Z8; -.
DR SMR; Q980Z8; -.
DR DIP; DIP-60643N; -.
DR IntAct; Q980Z8; 10.
DR STRING; 273057.SSO5140; -.
DR EnsemblBacteria; AAK40429; AAK40429; SSO5140.
DR GeneID; 44129030; -.
DR KEGG; sso:SSO5140; -.
DR PATRIC; fig|273057.12.peg.68; -.
DR eggNOG; arCOG04244; Archaea.
DR HOGENOM; CLU_143122_1_1_2; -.
DR InParanoid; Q980Z8; -.
DR OMA; YCCRRMF; -.
DR PhylomeDB; Q980Z8; -.
DR BRENDA; 2.7.7.6; 6163.
DR EvolutionaryTrace; Q980Z8; -.
DR Proteomes; UP000001974; 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; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
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..66
FT /note="DNA-directed RNA polymerase subunit Rpo10"
FT /id="PRO_0000121362"
FT BINDING 7
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00250,
FT ECO:0000269|PubMed:18235446, ECO:0007744|PDB:2PMZ,
FT ECO:0007744|PDB:3HKZ"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00250,
FT ECO:0000269|PubMed:18235446, ECO:0007744|PDB:2PMZ,
FT ECO:0007744|PDB:3HKZ"
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:18235446, ECO:0007744|PDB:2PMZ,
FT ECO:0007744|PDB:3HKZ"
FT BINDING 45
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00250,
FT ECO:0000269|PubMed:18235446, ECO:0007744|PDB:2PMZ,
FT ECO:0007744|PDB:3HKZ"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 21..26
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 31..36
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 44..50
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:2PMZ"
SQ SEQUENCE 66 AA; 7591 MW; C6774B541A1CFA13 CRC64;
MLIPIRCFTC GSLIADKWQS FITRVNAGEN PGKVLDDLGV KRYCCRRMLL SHVDIINEVI
HYTRPI
