ID A0A914IYF5_9BILA Unreviewed; 1750 AA.
AC A0A914IYF5;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 18-JUN-2025, entry version 13.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
OS Panagrolaimus sp. JU765.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Panagrolaimoidea; Panagrolaimidae;
OC Panagrolaimus.
OX NCBI_TaxID=591449 {ECO:0000313|WBParaSite:JU765_v2.g1446.t1};
RN [1] {ECO:0000313|WBParaSite:JU765_v2.g1446.t1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2022) to UniProtKB.
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:RU004279}.
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:RU004279};
CC -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting
CC of 12 subunits. Interacts with sig-7. {ECO:0000256|ARBA:ARBA00064942}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|ARBA:ARBA00006460, ECO:0000256|RuleBase:RU004279}.
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DR WBParaSite; JU765_v2.g1446.t1; JU765_v2.g1446.t1; JU765_v2.g1446.
DR Proteomes; UP000887576; Unplaced.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IEA:TreeGrafter.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd02584; RNAP_II_Rpb1_C; 1.
DR CDD; cd02733; RNAP_II_RPB1_N; 1.
DR FunFam; 2.40.40.20:FF:000019; DNA-directed RNA polymerase II subunit RPB1; 1.
DR FunFam; 1.10.132.30:FF:000001; DNA-directed RNA polymerase subunit; 1.
DR FunFam; 1.10.150.390:FF:000001; DNA-directed RNA polymerase subunit; 1.
DR FunFam; 1.10.274.100:FF:000001; DNA-directed RNA polymerase subunit; 1.
DR FunFam; 3.30.1360.140:FF:000001; DNA-directed RNA polymerase subunit; 1.
DR FunFam; 3.30.1490.180:FF:000001; DNA-directed RNA polymerase subunit; 1.
DR FunFam; 4.10.860.120:FF:000005; DNA-directed RNA polymerase subunit; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.150.390; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.1360.140; -; 1.
DR Gene3D; 6.10.250.2940; -; 1.
DR Gene3D; 6.20.50.80; -; 1.
DR Gene3D; 3.30.1490.180; RNA polymerase ii; 1.
DR Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 2.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR000684; RNA_pol_II_repeat_euk.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR007075; RNA_pol_Rpb1_6.
DR InterPro; IPR007073; RNA_pol_Rpb1_7.
DR InterPro; IPR038593; RNA_pol_Rpb1_7_sf.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR NCBIfam; NF006336; PRK08566.1; 1.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF37; DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR Pfam; PF04992; RNA_pol_Rpb1_6; 1.
DR Pfam; PF04990; RNA_pol_Rpb1_7; 1.
DR SMART; SM00663; RPOLA_N; 1.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
DR PROSITE; PS00115; RNA_POL_II_REPEAT; 3.
PE 3: Inferred from homology;
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|RuleBase:RU004279};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004279}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000887576};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 234..537
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1704..1750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1710..1750
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1750 AA; 194977 MW; D135BCFEB1273ED9 CRC64;
MSLLGADFRA PLRTVKRVQF GILSPDEIRR MSVGQLEYPE VYENGKPKIG GLMDPRQGVI
DKRSRCMTCT GTMNDCSGHF AHIELAKPVF HIGFLSKTLK VMNCVCFYCS KLLIDKDSPK
IKEIIRKTKG NLRKRLTMIY DLCKGRSICR VDGGVEDDEM QTDASSKKGG CGRYQPSYRR
TGLDISAEWK KNLNEENQEK KIVLTAEKVL EVFKNVSDAD CRVLGFDPEY GRPDWMVCTV
MPVPPLAVRP AVVTSGSARN HDDLTHKLAD IVKTNNQLKR NETHGAAAHV IAEDVRLLQY
HVATFVDNQI PGVPLACQKG GRPLKSIKQR LKGKEGRIRG NLMGKRVDFS ARTVITPDPN
LPIDYVGVPR TIAQNLTFPE LVTPFNIDNL QEVVKRGDKS YPGAKYIIRE NGERVDLRYH
PRAADLHLEP GYRVERHMRD GDTVVFNRQP TLHKMSMMGH KIKVLPWSTF RLNLSVTTPY
NADFDGDEMN LHFPQSLETR AEIQEIAMVP RQLITPQANK PVMGIVQDTL CAVRMMTKRD
VFIELPRLMD LLMYLPSWNG IIPYPAILKP KPLWTGKQLF SLIIPGNVNV IRTHFTHDDN
EDKTDLKWIS PADTRVLIEN GVLLSGIICS KTVGRSAGNL LHIVALELGH EIAADFYSHI
QTVVNAWLIA EGHTIGIGDT IADESTYKEI QETIRKAKAD VVEVIEKAHN DELEATPGNT
LRQTFENNVN RILNDARDRT GSTAQKSLSE FNNFKAMVVA GSKGSKINIS QVIACVGQQN
VEGKRIPFGF RHRSLPHFIK DDYGPESRGF VENSYLAGLT PAEFFFHAMG GREGLIDTAV
KTAETGYIQR RLIKAMESVM VNYDGTVRNA VGQLIQLRYG EDGLDGMWVE NQSLPTMKLT
DAVFEKKCCL NAANEKEIRK LFTDEIVHEI QSDLDLQDKL DEEWKQLVED RRTLREIFPR
GETKVVLPCN LQRLIWNAQK IFHVDLKKPC DLCPSTIIDG IKKLSERLIV VGGDDSISKQ
AQINATLLIK ILIRSTLCSK QIAQTYKLNT EAFEWILGEI ESRFNQAIVQ PGEMVGPLAA
QSLGEPATQM TLNTFHYAGV SAKNVTLGVP RLKEIINVSK SPKTPSLTVF LTGDAAKNAE
SAKDVLCKLE HTTLRKVTAN TAIYYNPNPT QTCIEEDQEW VSIFYELDPK NIDNVSPWLL
RIELDRKRMT DKKLSMETIA DKIAMGFGGD LHVIYTDDNA EKLVIYLRLQ NPLIEEEAEE
QVGKMGDETF LRCVEQNLLS DLTLQGIESI SKVYMHKPQS DDKKRVVQTP EGGFQTIAEW
VLETDGTALL KVLSEQNVDA VRTYSNDICE VFHRNXXXXG SYVNYRHLAL LCDVMTAKGH
LMAITRHGIN RQEVGALMRC SFEETVDILM EAAVHSEVDP VKGVSENIML GQLAKVGTGC
FDLVLDAEKC EQAMEIPANK AYENMSDFIE MGGNVSPASP QMSPEPWNYY SSRVYVSPSG
GMTPANAVFS PAQFDSEGVY SPSYNEGWSP RGDVSPAHSI GAMSPGAMSP RDYSSLASPA
YRSPASPFYR YSPASPGFET RYSPTSPMYS PTSPAYSPKS PAYSPTSHSP TSPAYSPISP
TYSPMSATYS PIYATYSPMS ATYSPIYATY SPTYSRTSPS YSPTSPSYRP ISPSYSPISP
SYSPTYSPTS PNYLPSSPQY SPISPPYVPS SPNYSSSSPQ YSPASPVLSP SSPQYSPTSP
TYSPLSPKYP
//
