RPO1C_THEKO
ID RPO1C_THEKO Reviewed; 391 AA.
AC Q5JE34;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo1C {ECO:0000255|HAMAP-Rule:MF_00411};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00411};
DE AltName: Full=DNA-directed RNA polymerase subunit A'' {ECO:0000255|HAMAP-Rule:MF_00411};
GN Name=rpo1C {ECO:0000255|HAMAP-Rule:MF_00411};
GN Synonyms=rpoA2 {ECO:0000255|HAMAP-Rule:MF_00411}; OrderedLocusNames=TK1081;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
CC -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the
CC transcription of DNA into RNA using the four ribonucleoside
CC triphosphates as substrates. Forms part of the jaw domain.
CC {ECO:0000255|HAMAP-Rule:MF_00411}.
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_00411};
CC -!- SUBUNIT: Part of the RNA polymerase complex. {ECO:0000255|HAMAP-
CC Rule:MF_00411}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00411}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00411}.
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DR EMBL; AP006878; BAD85270.1; -; Genomic_DNA.
DR RefSeq; WP_011250032.1; NC_006624.1.
DR PDB; 4QIW; X-ray; 3.50 A; C/M=1-391.
DR PDB; 6KF3; EM; 3.90 A; C=1-391.
DR PDB; 6KF4; EM; 3.97 A; C=1-391.
DR PDB; 6KF9; EM; 3.79 A; C=1-391.
DR PDBsum; 4QIW; -.
DR PDBsum; 6KF3; -.
DR PDBsum; 6KF4; -.
DR PDBsum; 6KF9; -.
DR AlphaFoldDB; Q5JE34; -.
DR SMR; Q5JE34; -.
DR STRING; 69014.TK1081; -.
DR EnsemblBacteria; BAD85270; BAD85270; TK1081.
DR GeneID; 3233696; -.
DR KEGG; tko:TK1081; -.
DR PATRIC; fig|69014.16.peg.1057; -.
DR eggNOG; arCOG04256; Archaea.
DR HOGENOM; CLU_037097_1_0_2; -.
DR InParanoid; Q5JE34; -.
DR OMA; TPMMTVY; -.
DR OrthoDB; 66811at2157; -.
DR PhylomeDB; Q5JE34; -.
DR Proteomes; UP000000536; 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:UniProtKB-UniRule.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR CDD; cd06528; RNAP_A; 1.
DR HAMAP; MF_00411; RNApol_arch_Rpo1C; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR012757; RPO1C.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR TIGRFAMs; TIGR02389; RNA_pol_rpoA2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-binding; DNA-directed RNA polymerase;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase.
FT CHAIN 1..391
FT /note="DNA-directed RNA polymerase subunit Rpo1C"
FT /id="PRO_0000074024"
FT HELIX 10..14
FT /evidence="ECO:0007829|PDB:4QIW"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:4QIW"
FT HELIX 21..31
FT /evidence="ECO:0007829|PDB:4QIW"
FT HELIX 39..56
FT /evidence="ECO:0007829|PDB:4QIW"
FT HELIX 64..73
FT /evidence="ECO:0007829|PDB:4QIW"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:4QIW"
FT HELIX 98..105
FT /evidence="ECO:0007829|PDB:4QIW"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:4QIW"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:4QIW"
FT HELIX 128..139
FT /evidence="ECO:0007829|PDB:4QIW"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:4QIW"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:4QIW"
FT TURN 169..172
FT /evidence="ECO:0007829|PDB:4QIW"
FT HELIX 174..180
FT /evidence="ECO:0007829|PDB:4QIW"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:4QIW"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:4QIW"
FT TURN 216..220
FT /evidence="ECO:0007829|PDB:4QIW"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:4QIW"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:4QIW"
FT STRAND 241..247
FT /evidence="ECO:0007829|PDB:4QIW"
FT HELIX 250..253
FT /evidence="ECO:0007829|PDB:4QIW"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:4QIW"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:4QIW"
FT HELIX 271..275
FT /evidence="ECO:0007829|PDB:4QIW"
FT HELIX 278..294
FT /evidence="ECO:0007829|PDB:4QIW"
FT HELIX 302..313
FT /evidence="ECO:0007829|PDB:4QIW"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:4QIW"
FT STRAND 321..325
FT /evidence="ECO:0007829|PDB:4QIW"
FT TURN 326..328
FT /evidence="ECO:0007829|PDB:4QIW"
FT HELIX 334..337
FT /evidence="ECO:0007829|PDB:4QIW"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:4QIW"
FT HELIX 346..350
FT /evidence="ECO:0007829|PDB:4QIW"
FT HELIX 362..367
FT /evidence="ECO:0007829|PDB:4QIW"
FT HELIX 374..377
FT /evidence="ECO:0007829|PDB:4QIW"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:4QIW"
SQ SEQUENCE 391 AA; 43665 MW; 23AE3E9D670BC913 CRC64;
MVAEKTIKSM VSKAELPDNI KEELYAKLIE YNEKYKLKKD EIQAIIDETV REYQKALIEP
GEAVGTVAAQ SIGEPSTQMT LNTFHYAGVA EINVTLGLPR IIEIVDARKN PSTPIMTVYL
DEEHRYDRDK ALEVARRIEG TTLENLAREE TIDILNMEYV VEIDPERLEK AGLDMEKVVR
KLTGSFKSAE FEAEGYTLVV RPKKVTKLSD LRKIAEKVKK HRLKGLSGVG KTIIRKEGDE
YVIYTEGSNF KQVLKVPGVD PTRTRTNNIW EIAEVLGIEA ARNAIIDEIV STMREQGLEV
DVRHIMLVAD MMTLDGVIRP IGRHGIVGEK ASVLARAAFE ITTQHLFAAA ERGEVDPLNG
VVENVLIGQP VPVGTGIVKL AMSLPLRPKR E