ID A0A498H4I8_9EURY Unreviewed; 604 AA.
AC A0A498H4I8;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 18-JUN-2025, entry version 26.
DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000256|RuleBase:RU363031};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU363031};
GN ORFNames=ABH15_02170 {ECO:0000313|EMBL:RXE56968.1};
OS Methanoculleus taiwanensis.
OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC Methanomicrobia; Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX NCBI_TaxID=1550565 {ECO:0000313|EMBL:RXE56968.1, ECO:0000313|Proteomes:UP000290932};
RN [1] {ECO:0000313|EMBL:RXE56968.1, ECO:0000313|Proteomes:UP000290932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CYW4 {ECO:0000313|EMBL:RXE56968.1,
RC ECO:0000313|Proteomes:UP000290932};
RX PubMed=25575827; DOI=.1099/ijs.0.000062;
RA Weng C.Y., Chen S.C., Lai M.C., Wu S.Y., Lin S., Yang T.F., Chen P.C.;
RT "Methanoculleus taiwanensis sp. nov., a methanogen isolated from deep
RT marine sediment at the deformation front area near Taiwan.";
RL Int. J. Syst. Evol. Microbiol. 65:1044-1049(2015).
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:RXE56968.1}.
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DR EMBL; LHQS01000001; RXE56968.1; -; Genomic_DNA.
DR RefSeq; WP_128692720.1; NZ_LHQS01000001.1.
DR AlphaFoldDB; A0A498H4I8; -.
DR OrthoDB; 6009at2157; -.
DR Proteomes; UP000290932; 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:UP000290932};
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..120
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04567"
FT DOMAIN 136..507
FT /note="DNA-directed RNA polymerase subunit 2 hybrid-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF00562"
FT DOMAIN 509..600
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04560"
SQ SEQUENCE 604 AA; 67447 MW; FB5D0CF8E669D2D3 CRC64;
MKMSRVFVDG ALIGLVEDPV ALVANIRRMR RRGEVSTEIN VSYKEFNNDV IVHTDRGRAR
RPLIVVENGK TQVAPEDIER LRAGEIDFND FVRRGVIEFI DAEEEEDLFI AITEDVLTPE
HTHLEIDPAL ILGIGAAHVP FPEHNASPRV TMGAGMVKQA LGFAAANMKL RPDTRGHMLH
YVQKPLTYTQ TSDVIGSDDR PAGQNFVVAI ISYEGFNIED ALIINKASID RGVGRSHFFR
TYDGEERRYP GGQVDRIEIP DEEVSGAHGT EYYANLDDDG VISPETVVRE KDVIIGKTSP
PRFLEEPTSE LIAVEKRRDT SVTMRSNEHG IVDTVIITEG ENSSRLVKVR TRDLRVPEVG
DKFASRHGQK GVIGLIQPQE DMPFTESGMT PDLVINPHAV PSRMTIGHML EMLGGKVGSL
EGHRINATAF RGEREAAMRS SLKELGFSHT GREVMYDGIT GRRFAADIYI GVIYYQKLYH
MVSSKMHARS RGPVQVLTRQ PTEGRAREGG LRFGEMERDV MIGHGAAMAL KERLLDESDK
VSEWVCAKCG MVAMLDRKRK ITRCLACGGE TDIYPVEMSY AFKLLLDEMK SMGIAPRLRL
EDMV
//
