RPO3_THEKO
ID RPO3_THEKO Reviewed; 259 AA.
AC Q5JJF4;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo3 {ECO:0000255|HAMAP-Rule:MF_00320};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00320};
DE AltName: Full=DNA-directed RNA polymerase subunit D {ECO:0000255|HAMAP-Rule:MF_00320};
GN Name=rpo3 {ECO:0000255|HAMAP-Rule:MF_00320};
GN Synonyms=rpoD {ECO:0000255|HAMAP-Rule:MF_00320}; OrderedLocusNames=TK1503;
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. {ECO:0000255|HAMAP-Rule:MF_00320}.
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_00320};
CC -!- SUBUNIT: Part of the RNA polymerase complex. {ECO:0000255|HAMAP-
CC Rule:MF_00320}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00320}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo3/eukaryotic RPB3 RNA polymerase
CC subunit family. {ECO:0000255|HAMAP-Rule:MF_00320}.
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DR EMBL; AP006878; BAD85692.1; -; Genomic_DNA.
DR PDB; 4QIW; X-ray; 3.50 A; D/O=1-259.
DR PDB; 4QJV; X-ray; 1.60 A; A/C=1-259.
DR PDB; 6KF3; EM; 3.90 A; D=1-259.
DR PDB; 6KF4; EM; 3.97 A; D=1-259.
DR PDB; 6KF9; EM; 3.79 A; D=1-259.
DR PDBsum; 4QIW; -.
DR PDBsum; 4QJV; -.
DR PDBsum; 6KF3; -.
DR PDBsum; 6KF4; -.
DR PDBsum; 6KF9; -.
DR AlphaFoldDB; Q5JJF4; -.
DR SMR; Q5JJF4; -.
DR IntAct; Q5JJF4; 1.
DR MINT; Q5JJF4; -.
DR STRING; 69014.TK1503; -.
DR EnsemblBacteria; BAD85692; BAD85692; TK1503.
DR KEGG; tko:TK1503; -.
DR PATRIC; fig|69014.16.peg.1463; -.
DR eggNOG; arCOG04241; Archaea.
DR HOGENOM; CLU_038421_3_1_2; -.
DR InParanoid; Q5JJF4; -.
DR OMA; ECLRHPE; -.
DR PhylomeDB; Q5JJF4; -.
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:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 2.170.120.12; -; 1.
DR Gene3D; 3.30.1360.10; -; 1.
DR HAMAP; MF_00320; RNApol_arch_Rpo3; 1.
DR InterPro; IPR001514; DNA-dir_RNA_pol_30-40kDasu_CS.
DR InterPro; IPR011262; DNA-dir_RNA_pol_insert.
DR InterPro; IPR011263; DNA-dir_RNA_pol_RpoA/D/Rpb3.
DR InterPro; IPR036603; RBP11-like.
DR InterPro; IPR022842; RNAP_Rpo3/Rpb3/RPAC1.
DR InterPro; IPR036643; RNApol_insert_sf.
DR Pfam; PF01000; RNA_pol_A_bac; 1.
DR Pfam; PF01193; RNA_pol_L; 1.
DR SMART; SM00662; RPOLD; 1.
DR SUPFAM; SSF55257; SSF55257; 1.
DR SUPFAM; SSF56553; SSF56553; 1.
DR PROSITE; PS00446; RNA_POL_D_30KD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-directed RNA polymerase;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase.
FT CHAIN 1..259
FT /note="DNA-directed RNA polymerase subunit Rpo3"
FT /id="PRO_0000132763"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:4QJV"
FT STRAND 13..20
FT /evidence="ECO:0007829|PDB:4QJV"
FT HELIX 23..35
FT /evidence="ECO:0007829|PDB:4QJV"
FT STRAND 39..50
FT /evidence="ECO:0007829|PDB:4QJV"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:4QJV"
FT HELIX 56..64
FT /evidence="ECO:0007829|PDB:4QJV"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:4QJV"
FT STRAND 87..100
FT /evidence="ECO:0007829|PDB:4QJV"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:4QJV"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:4QJV"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:4QJV"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:4QJV"
FT STRAND 128..138
FT /evidence="ECO:0007829|PDB:4QJV"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:4QJV"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:4QJV"
FT STRAND 149..162
FT /evidence="ECO:0007829|PDB:4QJV"
FT HELIX 168..177
FT /evidence="ECO:0007829|PDB:4QJV"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:4QJV"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:4QJV"
FT HELIX 201..206
FT /evidence="ECO:0007829|PDB:4QJV"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:4QJV"
FT STRAND 211..226
FT /evidence="ECO:0007829|PDB:4QJV"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:4QJV"
FT HELIX 232..255
FT /evidence="ECO:0007829|PDB:4QJV"
SQ SEQUENCE 259 AA; 29392 MW; D62F88135F5F9494 CRC64;
MVEFKILEKR PDSIKFIVSG VDVPFANALR RTILSEVPTF AVDEVEFLEN DSALFDEIIA
HRLAMIPLTT PHERFSLDAL ELDDYTVTLS LEAEGPGMVY SGDLKSSDGD VKPANPNIPI
VKLAEGQRLT FNAYARLGRG KDHAKWQPGF VYYKYLTKIH VSKDVPDWEE LKELAERRGL
PVEESDEEIV ITTIKAFYLP RKFEEHMGKG IREEIVPGSF VFTVETNGEL PVEEIVSIAL
KILMRKSDRF INELHKLAD
