ID A0A366MAB4_9EURY Unreviewed; 603 AA.
AC A0A366MAB4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 18-JUN-2025, entry version 25.
DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000256|RuleBase:RU363031};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU363031};
GN Name=rpoB1 {ECO:0000313|EMBL:RBQ22499.1};
GN ORFNames=ALNOE001_19310 {ECO:0000313|EMBL:RBQ22499.1};
OS Candidatus Methanobinarius endosymbioticus.
OC Archaea; Methanobacteriati; Methanobacteriota; Methanomada group;
OC Methanobacteria; Methanobacteriales; Methanobacteriaceae;
OC Candidatus Methanobinarius.
OX NCBI_TaxID=2006182 {ECO:0000313|EMBL:RBQ22499.1, ECO:0000313|Proteomes:UP000253099};
RN [1] {ECO:0000313|EMBL:RBQ22499.1, ECO:0000313|Proteomes:UP000253099}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NOE {ECO:0000313|EMBL:RBQ22499.1};
RA Lind A.E., Lewis W.H., Spang A., Guy L., Embley M.T., Ettema T.J.G.;
RT "Genomic insight into two independent archaeal endosymbiosis events.";
RL Submitted (JUN-2018) 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:0000256|ARBA:ARBA00025096}.
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000256|RuleBase:RU363031}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) +
CC diphosphate; 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:0000256|ARBA:ARBA00048552,
CC ECO:0000256|RuleBase:RU363031};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBUNIT: Part of the RNA polymerase complex.
CC {ECO:0000256|ARBA:ARBA00025838}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000256|ARBA:ARBA00006835, ECO:0000256|RuleBase:RU363031}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RBQ22499.1}.
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DR EMBL; NIZT01000064; RBQ22499.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366MAB4; -.
DR Proteomes; UP000253099; Unassembled WGS sequence.
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 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:DNA-templated transcription; IEA:InterPro.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR FunFam; 2.40.270.10:FF:000011; DNA-directed RNA polymerase subunit beta; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1070.20; -; 1.
DR Gene3D; 2.40.270.10; DNA-directed RNA polymerase, subunit 2, domain 6; 1.
DR Gene3D; 3.90.1800.10; RNA polymerase alpha subunit dimerisation domain; 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 NCBIfam; TIGR03670; rpoB_arch; 1.
DR PANTHER; PTHR20856; DNA-DIRECTED RNA POLYMERASE I SUBUNIT 2; 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 SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|RuleBase:RU363031};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU363031};
KW Reference proteome {ECO:0000313|Proteomes:UP000253099};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU363031};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363031};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 6..67
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04566"
FT DOMAIN 88..121
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04567"
FT DOMAIN 135..507
FT /note="DNA-directed RNA polymerase subunit 2 hybrid-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF00562"
FT DOMAIN 509..599
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04560"
SQ SEQUENCE 603 AA; 67466 MW; A98B52871387325C CRC64;
MTKAKIYING ELIGTCEDPD DFVAEMREKR RIGEVSEEMN ITYYDGTDEI YIFNDPGRAR
RPLILVKDGV PLLEDEHIDK IAEGEIKWDD LINSGVIEYL DAEEEENSYI AMGLNYLNED
HTHLEIDPST MLGICAGIIP FSDHNSSPRN TMEAGMTKQA LGLYVSNYGL RTDTRAHLLH
HPQTPLVKTR IIDATNYDER PSGQNFVVAV MSFEGYNMED SLILNKSSLE RGMSRSSFFR
SYEASERRYP GGQEDKFEVP EKGVRGYRSE EAYRHLDDDG VVNPESYVES GDVLIGKTSP
PRFLEEIDEF GTVAERRRET SVTVRHGEKG IVDAVLLTET VEGSKLAKIR VRDTRQPEFG
DKFASRHGQK GVVGLILSPE DVPFTEDGVV PDLIVNPHAI PSRMSVGQVI EMVAGKAGCM
EGERVDGTPF NGDLEAELKE SLKANGFESA GCESLYNGMT GERIEAEIFV GVAFYQKLHH
MTTDKVYARS RGPVQVLTRQ PTEGRAREGG LRFGEMERDC LIAHGAALAL KERLLDESDK
YEAIICGDCG MISVYDKIRD KKYCPICGDV DSYPVEISYA FKLLLDELKS LCIFPKLVLE
DKA
//
