RPO2_THECE
ID RPO2_THECE Reviewed; 1122 AA.
AC P31814;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo2 {ECO:0000305};
DE EC=2.7.7.6 {ECO:0000250|UniProtKB:P11513};
DE AltName: Full=DNA-directed RNA polymerase subunit B {ECO:0000303|PubMed:1408768};
GN Name=rpo2 {ECO:0000305}; Synonyms=rpoB {ECO:0000303|PubMed:1408768};
OS Thermococcus celer.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=2264;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35543 / DSM 2476 / JCM 8558 / Vu 13;
RX PubMed=1408768; DOI=10.1093/nar/20.17.4659;
RA Klenk H.-P., Schwass V., Lottspeich F., Zillig W.;
RT "Nucleotide sequence of the genes encoding the three largest subunits of
RT the DNA-dependent RNA polymerase from the archaeum Thermococcus celer.";
RL Nucleic Acids Res. 20:4659-4659(1992).
CC -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the
CC transcription of DNA into RNA using the four ribonucleoside
CC triphosphates as substrates. This subunit is involved in DNA promoter
CC recognition. {ECO:0000250|UniProtKB:B8YB55}.
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:0000250|UniProtKB:P11513};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:B8YB55};
CC Note=Binds 1 Zn(2+) per subunit. {ECO:0000250|UniProtKB:B8YB55};
CC -!- SUBUNIT: Part of the RNA polymerase complex. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B8YB55}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000305}.
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DR EMBL; X67313; CAA47722.1; -; Genomic_DNA.
DR PIR; S25563; S25563.
DR AlphaFoldDB; P31814; -.
DR SMR; P31814; -.
DR PRIDE; P31814; -.
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-KW.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 1.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007646; RNA_pol_Rpb2_4.
DR InterPro; IPR007647; RNA_pol_Rpb2_5.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR InterPro; IPR019969; RNAP_Rpo2.
DR PANTHER; PTHR20856; PTHR20856; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 1.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF04566; RNA_pol_Rpb2_4; 1.
DR Pfam; PF04567; RNA_pol_Rpb2_5; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR TIGRFAMs; TIGR03670; rpoB_arch; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 3: Inferred from homology;
KW Cytoplasm; DNA-binding; DNA-directed RNA polymerase; Metal-binding;
KW Nucleotidyltransferase; Transcription; Transferase; Zinc.
FT CHAIN 1..1122
FT /note="DNA-directed RNA polymerase subunit Rpo2"
FT /id="PRO_0000048099"
FT BINDING 1064
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:B8YB55"
FT BINDING 1067
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:B8YB55"
FT BINDING 1082
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:B8YB55"
FT BINDING 1085
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1122 AA; 127189 MW; 9D5038AA8224785D CRC64;
MASRGPTVVD VTPDDLWLVM EAYWKEKGLV RQHLDSYNAF IDHGMQEVID EFGGVKPDIP
DFEVKFGKVR LGEPEFQEAQ GQRKPLYPMD ARIRNLTYSA PIYLELIPVV NGVSQEAVEV
RIGELPIMLK SKACRLYGLS DEELIKLGED PKDPGGYFIV NGSERVIVSI EDLAPNKTLV
ERDERQNRII AKCFSYRHGY RALITVERRK DGILYVKLPN VPRPVKFVYV MRALGLLSDR
EIVEAVSDDP RIQHVLFDNL EDASDVTTQE EALDYIGKLS LPGQPKEYRL RRAQNIIDNN
LLPHMGVEEK DRKAKAYYLG MMALRVLELS LGLRGEDDKD HYANKRLKLA GDLLMDLFRV
AFGQLVKDMQ YQMTKTYQRK GERYTFENIQ RFVRNSIRPD VLSERIEHAL ATGSWPGGRT
GVSQLLDRTN YISTLSHLRR VTSPLSREQP HFEARDLHGT HWGRICPTET PEGPNCGLVK
NLALMSQITT GVPEEEVREY LERLGVVPIE ERRPNPDLWR LYLNGVLVGT VEDGEGFVNR
IRTDRRSGKI SDIINVALYQ DEDVKEIYVN SDDGRVRRPL IIVENGRPKL TREHVEAIKN
GSLTWSDLVK MGVIEYLDAE EEENALVATW PWEVTEEHTH LELMPAAILG IPASLVPYPE
HNARPRNTYG AGMAKQSLGL GWANFRIRVD TRGHLMHYPQ VPLVNSRIMK AVGFEERPAG
QNFVVAVLSY AGYNMEDAII MNKASIERGL ARSTFFRTYE AEEKRYLGGQ TDRFEIPDPT
IQGYLGERYY RHLDEDGIIF PESKVNGKDV LVGRTSPPRF LEEQSGLGGI ILQERRETSL
TVRPSETGVV DKVIITETGD GTKLVKVTTR DLRIPEFGDK FASRHGQKGV IGLIVPQEDM
PWTESGIVPD LIVNPHGIPS RMTVGQLIEA IGGKVASLKG RRVDGTAFIG EPEEKLRKEL
EELGFKHSGR EVMYDGITGR RLEADVFVGV IYYQRLHHMV ADKMHARSRG PVQVLTKQPT
EGRAREGGLR FGEMERDVLI GHGAAMLLIE RLLEESDKTE VWVCENCGHI ALEDKRRGKV
YCPVCGEEER ISKVEMSYAF KLLLDELKAM GIRPSLKLVD RV
