ID A0A183E0K5_9BILA Unreviewed; 846 AA.
AC A0A183E0K5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 18-JUN-2025, entry version 37.
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=GPUH_LOCUS14494 {ECO:0000313|EMBL:VDN24263.1};
OS Gongylonema pulchrum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Spiruroidea; Gongylonematidae; Gongylonema.
OX NCBI_TaxID=637853 {ECO:0000313|WBParaSite:GPUH_0001451501-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:GPUH_0001451501-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN24263.1, ECO:0000313|Proteomes:UP000271098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU363031};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000256|ARBA:ARBA00006835, ECO:0000256|RuleBase:RU000434}.
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DR EMBL; UYRT01081333; VDN24263.1; -; Genomic_DNA.
DR WBParaSite; GPUH_0001451501-mRNA-1; GPUH_0001451501-mRNA-1; GPUH_0001451501.
DR OrthoDB; 10248617at2759; -.
DR Proteomes; UP000271098; Unassembled WGS sequence.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032549; F:ribonucleoside 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:000006; DNA-directed RNA polymerase subunit beta; 1.
DR FunFam; 2.40.270.10:FF:000011; DNA-directed RNA polymerase subunit beta; 1.
DR FunFam; 2.40.50.150:FF:000002; DNA-directed RNA polymerase subunit beta; 1.
DR FunFam; 3.90.1070.20:FF:000001; 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; 3.90.1110.10; RNA polymerase Rpb2, domain 2; 2.
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; IPR014724; RNA_pol_RPB2_OB-fold.
DR PANTHER; PTHR20856; DNA-DIRECTED RNA POLYMERASE I SUBUNIT 2; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 2.
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 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 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}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000271098};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU363031};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363031}.
FT DOMAIN 1..240
FT /note="RNA polymerase beta subunit protrusion"
FT /evidence="ECO:0000259|Pfam:PF04563"
FT DOMAIN 40..117
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04561"
FT DOMAIN 118..199
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04561"
FT DOMAIN 240..303
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04565"
FT DOMAIN 338..400
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04566"
FT DOMAIN 421..466
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04567"
FT DOMAIN 473..834
FT /note="DNA-directed RNA polymerase subunit 2 hybrid-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF00562"
SQ SEQUENCE 846 AA; 95458 MW; 2DBD5ADD75DE1697 CRC64;
MLANMSDRDL SELNECPLDP GGYFVINGSE KVLIAQEKMA TNTVYVFAMK DGKYTYKTEC
RSCLENSSRP TSTLWVNMLP RGGGSNKKSA MGPKIIAILP YIKQEIPVMI VFRALGFEQN
VALNFIGARG AKPGVTKEQR IKYAKEILQK EMLPHVGISD FCETKKAYFL GYMVHRLLLA
ALGRRELDDR DHMGNKRLDL AGPLLAFLFR ALFRNLLKEV RLTAQKYINK NGDFMLDLCV
LNRLTYTATL SHLRRCNSPI GREGKLAKPR QLHNTQWGMV CPAETPEGQA VGLVKNLALM
AYISVGSLPE PILEFLEEWS MENLEEVAPS AIAEATKIFV NGAWVGIHRD PEQLMTTLKK
LRREMDIIVS EVSMVRDIRD REIRIFTDAG RVCRPLLIVE NQKLALKKKH IDQLKDNSYS
WSELVAGGVV ELIDAMEEET IMLAMMPEDL KAGGYCDTYT HCEIHPAMIL GVCASIIPFP
DHNQSPRNTY QSAMGKQAMG VYTTNYHVRM DTLAHVLYYP QKPLVTTPGI NAIVAILSYT
GYNQEDSIIM NQSGIDRGLF RSVFYRSYRD QEANLDNPNE ELIEKPTRDK CSGMRHSLYD
KLEDDGIISP GMRVSGDDVI IGKTISLPDD EDDLDATVKR YTKKDASTFL RSSETGIVDQ
VMLTLNTDGN KFVKIRVRSV RLPQIGDKFA SRHGQKGTMG MMYRQEDMPF TNEGITPDII
INPHAVPSRM TIGHLIECLQ GKLSANKGEI GDATPFNDTV NVQKISNLLQ EYGYHLRGNE
IMYNGHTGRK LTTQVFLGPT YYQRLKHMVD DKIHSRARGP VQMMNRQPME GRARYSFCLG
FWPCAL
//
