RPO2C_METVS
ID RPO2C_METVS Reviewed; 611 AA.
AC P41557; A6UQ06;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo2C {ECO:0000305};
DE EC=2.7.7.6 {ECO:0000250|UniProtKB:P11513};
DE AltName: Full=DNA-directed RNA polymerase subunit B' {ECO:0000303|Ref.1};
GN Name=rpo2C {ECO:0000305}; Synonyms=rpoB {ECO:0000303|Ref.1}, rpoB1;
GN OrderedLocusNames=Mevan_0672;
OS Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148
OS / SB).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=406327;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Palm P., Arnold-Ammer I., Lechner K.A., Zillig W.;
RT "DNA sequence of the genes of the large subunits of the DNA dependent RNA-
RT polymerase of Methanococcus vannielii.";
RL Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus vannielii SB.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the
CC transcription of DNA into RNA using the four ribonucleoside
CC triphosphates as substrates. The Rpo2 subunit (Rpo2N and Rpo2C in this
CC organism) is implicated in DNA promoter recognition and in nucleotide
CC binding. {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.
CC {ECO:0000250|UniProtKB:B8YB55}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B8YB55}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA51727.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X73293; CAA51727.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP000742; ABR54578.1; -; Genomic_DNA.
DR PIR; S47161; S47161.
DR RefSeq; WP_011972480.1; NC_009634.1.
DR AlphaFoldDB; P41557; -.
DR SMR; P41557; -.
DR STRING; 406327.Mevan_0672; -.
DR EnsemblBacteria; ABR54578; ABR54578; Mevan_0672.
DR GeneID; 5325059; -.
DR KEGG; mvn:Mevan_0672; -.
DR eggNOG; arCOG01762; Archaea.
DR HOGENOM; CLU_000524_2_2_2; -.
DR OMA; YQKLYHM; -.
DR OrthoDB; 5510at2157; -.
DR Proteomes; UP000001107; 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-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 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; 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; 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..611
FT /note="DNA-directed RNA polymerase subunit Rpo2C"
FT /id="PRO_0000048105"
FT BINDING 547
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:B8YB55"
FT BINDING 550
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:B8YB55"
FT BINDING 565
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:B8YB55"
FT BINDING 568
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
SQ SEQUENCE 611 AA; 68481 MW; FDAC89B41896BE40 CRC64;
MEKQANVYVN GKLIDTSKDP ENLVKSLRIQ RRSGKLSPNT SISFNEESND IHISTDGGRA
VRPLVVVENG FSKLTNELLE KVNNNELTFE YLVKTGVIEF LDAEEEENAR IAMYNDEITF
ENTHVEIDPL VILGIGAGVA PYPEHNSAPR ITMAAAMGKQ SLGIPMANIK WRMDTRGHLL
HYPQVPLVRT KHQEILGFDK RPAGQNFVVA VMSYEGYNME DAFVINKASL ERGLGRSTFF
RSYESFEKRY PGGQLDKFEV PEKGVRGYRA EEAYRNLGDD GLIDLESEVR SGDVILGKTS
PPRFLEEQEI TLQTKSQRRD TSVTIRHGEE GVVDLVILSE TKEGNRLGKV RVRDLRVPEF
GDKFASRHGQ KGVIGLVVPQ EDLPFTEDGV IPDLIINPHA IPSRMTIGQV LEMIGGKVGS
LECRRVDGTI FSGEGEWALR HALENYGFTH SGKETMYDGK TGRKLECEIF VGVAYYQKLH
HLVAGKIHAR SRGPIQVLTR QPTEGRAREG GLRFGEMERD VLVAHGAALL LKERLLDESD
PHEDYVCAKC GEIAIFDYKR GMKFCPVCGE SEDIQDNRKI PPVKIAYAFK LLLDELKSMG
IDPKLKLKDR A