RPO10_SACSH
ID RPO10_SACSH Reviewed; 66 AA.
AC B8YB63;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo10 {ECO:0000255|HAMAP-Rule:MF_00250, ECO:0000303|PubMed:19419240};
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, ECO:0000303|PubMed:19419240};
GN Synonyms=rpoN {ECO:0000255|HAMAP-Rule:MF_00250};
OS Saccharolobus shibatae (Sulfolobus shibatae).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=2286;
RN [1] {ECO:0007744|PDB:2WAQ, ECO:0007744|PDB:2WB1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS)
RP OF THE RNA POLYMERASE COMPLEX IN COMPLEX WITH ZINC, COFACTOR, SUBUNIT, AND
RP NOMENCLATURE.
RC STRAIN=ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12;
RX PubMed=19419240; DOI=10.1371/journal.pbio.1000102;
RA Korkhin Y., Unligil U.M., Littlefield O., Nelson P.J., Stuart D.I.,
RA Sigler P.B., Bell S.D., Abrescia N.G.;
RT "Evolution of complex RNA polymerases: the complete archaeal RNA polymerase
RT structure.";
RL PLoS Biol. 7:e1000102-e1000102(2009).
RN [2] {ECO:0007744|PDB:2Y0S}
RP X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) OF THE RNA POLYMERASE COMPLEX IN
RP COMPLEX WITH ZINC, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12;
RX PubMed=21265742; DOI=10.1042/bst0390025;
RA Wojtas M., Peralta B., Ondiviela M., Mogni M., Bell S.D., Abrescia N.G.;
RT "Archaeal RNA polymerase: the influence of the protruding stalk in crystal
RT packing and preliminary biophysical analysis of the Rpo13 subunit.";
RL Biochem. Soc. Trans. 39:25-30(2011).
RN [3] {ECO:0007744|PDB:4AYB, ECO:0007744|PDB:4V8S}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF THE RNA POLYMERASE COMPLEX IN
RP COMPLEX WITH ZINC WITH AND WITHOUT DNA, COFACTOR, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12;
RX PubMed=22848102; DOI=10.1093/nar/gks692;
RA Wojtas M.N., Mogni M., Millet O., Bell S.D., Abrescia N.G.;
RT "Structural and functional analyses of the interaction of archaeal RNA
RT polymerase with DNA.";
RL Nucleic Acids Res. 40:9941-9952(2012).
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:19419240, ECO:0007744|PDB:2WAQ,
CC ECO:0007744|PDB:2WB1, ECO:0007744|PDB:2Y0S};
CC Note=Binds 1 Zn(2+) per monomer. {ECO:0000255|HAMAP-Rule:MF_00250,
CC ECO:0000269|PubMed:19419240, ECO:0007744|PDB:2WAQ,
CC ECO:0007744|PDB:2WB1, ECO:0007744|PDB:2Y0S};
CC -!- SUBUNIT: Part of the 13-subunit RNA polymerase complex.
CC {ECO:0000269|PubMed:19419240, ECO:0000269|PubMed:21265742,
CC ECO:0000269|PubMed:22848102}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00250,
CC ECO:0000269|PubMed:22848102}.
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; FJ515675; ACL36498.1; -; Genomic_DNA.
DR PDB; 2WAQ; X-ray; 3.35 A; N=1-66.
DR PDB; 2WB1; X-ray; 3.52 A; N/O=1-66.
DR PDB; 2Y0S; X-ray; 3.80 A; N/O=1-66.
DR PDB; 4AYB; X-ray; 3.20 A; N=1-66.
DR PDB; 4V8S; X-ray; 4.32 A; AO/BN=1-66.
DR PDBsum; 2WAQ; -.
DR PDBsum; 2WB1; -.
DR PDBsum; 2Y0S; -.
DR PDBsum; 4AYB; -.
DR PDBsum; 4V8S; -.
DR SMR; B8YB63; -.
DR GeneID; 8762169; -.
DR BRENDA; 2.7.7.6; 6162.
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; 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; Transcription; Transferase; Zinc.
FT CHAIN 1..66
FT /note="DNA-directed RNA polymerase subunit Rpo10"
FT /id="PRO_0000453815"
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:19419240, ECO:0007744|PDB:2WAQ,
FT ECO:0007744|PDB:2WB1, ECO:0007744|PDB:2Y0S"
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:19419240, ECO:0007744|PDB:2WAQ,
FT ECO:0007744|PDB:2WB1, ECO:0007744|PDB:2Y0S,
FT ECO:0007744|PDB:4AYB, ECO:0007744|PDB:4V8S"
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:19419240, ECO:0007744|PDB:2WAQ,
FT ECO:0007744|PDB:2WB1, ECO:0007744|PDB:2Y0S,
FT ECO:0007744|PDB:4V8S"
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:19419240, ECO:0007744|PDB:2WAQ,
FT ECO:0007744|PDB:2WB1, ECO:0007744|PDB:2Y0S,
FT ECO:0007744|PDB:4V8S"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 18..26
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 31..37
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 44..50
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:2WAQ"
SQ SEQUENCE 66 AA; 7606 MW; 7A684255ABB45AE0 CRC64;
MMIPIRCFTC GSLIADKWQP FITRVNAGEN PGKVLDDLGV KRYCCRRMLL SHIDIISEVI
HYTRPI
