ID A0A0N4VBC4_ENTVE Unreviewed; 1846 AA.
AC A0A0N4VBC4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=EVEC_LOCUS7312 {ECO:0000313|EMBL:VDD92561.1};
OS Enterobius vermicularis (Human pinworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Enterobius.
OX NCBI_TaxID=51028 {ECO:0000313|Proteomes:UP000038041, ECO:0000313|WBParaSite:EVEC_0000782801-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EVEC_0000782801-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDD92561.1, ECO:0000313|Proteomes:UP000274131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (OCT-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:RU004279}.
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:0000256|ARBA:ARBA00024550,
CC ECO:0000256|RuleBase:RU004279};
CC -!- SUBCELLULAR LOCATION: 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 EMBL; UXUI01008867; VDD92561.1; -; Genomic_DNA.
DR STRING; 51028.A0A0N4VBC4; -.
DR WBParaSite; EVEC_0000782801-mRNA-1; EVEC_0000782801-mRNA-1; EVEC_0000782801.
DR Proteomes; UP000038041; Unplaced.
DR Proteomes; UP000274131; Unassembled WGS sequence.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0031981; C:nuclear lumen; IEA:UniProt.
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: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 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 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 Pfam; PF05001; RNA_pol_Rpb1_R; 17.
DR PRINTS; PR01217; PRICHEXTENSN.
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; 9.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|RuleBase:RU004279};
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:UP000274131};
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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 237..548
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1539..1846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 941..968
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1548..1846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1846 AA; 203198 MW; ECC2DA2BD4FD6EA4 CRC64;
MSLLGVDFRA PLRTVKRVQF GILSPDEIKR MSVGEIEFSE IYENGQPKVG GLMDPRQGVV
DRKGHCMTCA GNLADCPGHF AHLELAKPVF HIGFLAKTLK LLRCVCFYCS RLMIEKDSPR
VKEILKKTAG NPRKRLALIY DICKSKTVCD GGDELQPVAE EGDDAEKEVK AGGCGRYQPS
YKRMGLDITA EWKKHVNEDT QERKIVLSAE RALEIFKSVS DADCVILGFD PRFSRPDWMI
VQVLPVSPLA VRPAVVTFGS ARNQDDLTHK LSDIVKTNNQ LRRDEANGAA AHVIAEDVKL
LQYHVATLVD NNIPGIPTAT QKGGRPLKSI KQRLKGKEGR IRGNLMGKRV DFSARTVITP
DPNLPIDTIG VPRTIAQNMT FPEIVTPFNI DKLQELVNRG DSQYPGAKYI IRDTGARVDL
RYHPRAADLH LQPGYRVERH MKDGDIIVFN RQPSLHKMSM MGHKVKILPW STFRMNLSVT
TPYNADFDGD EMNLHLPQSL ETRAEIAEIA MVPRQVSKDG WKQLITPQAN KPVMGIVQDT
LCAVRMMTKR DSFIEKPRMM DLLMQMPNWD GVIPQPAILK PKPLWTGKQV FTLIIPGNVN
VMRTHSTHPD DEDNGPYKWI SPGDTKVLIE HGELLSGIIC SRTVGRSAGN LLHVVALELG
HEVAAQFYSH IQTTVNAWLL AEGHTIGIGD TIADQQTYEV IQQTIKKAKQ DVVDVIEKAH
NDELEPTPGN TLRQTFENMV NRILNDARDR TGGSAQRSLS EFNKFKAMVV AGSKGSKINI
SQVIACVGQQ NVEGKRIPFG FRHRTLPHFI KDDYGPESKG FVENSYLAGL TPSEFFFHAM
GGREGLIDTA VKTAETGYIQ RRLIKAMESV MVNYDGTVRN SLGQLVQLRY GEDGLDGMWV
ENQSMPSMKP TNALFEKDFK LDLTDEKALR RMYTENVIRE LQGSAEALKE IESEWAQLEE
DRRLLRKIFP RGDAKIVLPC NLQRMIWNAQ KIFRVELRKP TDLNPLKVIE GVRELSKKLV
IVGGEDRISK QAQYNATLLM NILLRSTLCS KRMGEKHKLN QEGFEWLIGE IESRFKQAIA
QPGEMVGPLA AQSLGEPATQ MTLNTFHYAG VSAKNVTLGV PRLKEIINVS KKPKTPSLTV
FLNGPAAKDA ERAKDVLCKL EHTTLRKVTA NTAIYYDPDP KNTVIEEDEE WVSIFYEMPD
FDPSRASPWL LRIELDRRRM TDKKLTMEAI ADKIHQGFGD DLNVIYTDDN AEKLVFRLRI
TNQDGDKGSE EEQIDKMEDD VFLRCIEANM LSDLTLQGIE QITKVYMHKP HTDDKKRVII
TPDGGFKAIP DWLLETDGMF YRNIKVLSEP NVDPVRTTSN DICEIFEVLG IEAVRKAIER
EMDQVISFDG SYVNYRHLAL LCDVMTSKGH LMAVTRHGIN RQEVGALMRC SFEETVDILM
EAAVHAEQDP VKGVSENIML GQLARAGTGC FDLVLDADKC KLGMEIQVGS LLNTGGGFFG
GGASPASSSM SPAQTPWNAG TTPAYGAAWS PAAGSGMTPG GAGFSPSGHS EGSFSPYGSG
AWSPGSPSGS MSGMSPSGAY SPTSDYGSGF EGLQSPGYSP TSPSSAFGGV MSPRYSPTSP
SYSPTSPSYS PTSPSYSPTS PSYSPTSPSY SPTSPTYSPT SPSYSPTSPS YSPTSPGYSA
SSPRYSPTSP TYSPTSPTYS PTSPTYSPTS PTYSPTSPTY SPASPAYSPT SPRYSPTSPT
YSPTSPAYSP SSPQYSPSSP QYSPSSPQYT PSSPIVGDAS PAYSPSSPQY SPSSPRYSPS
SPQYSPSSPQ YSPSSPGGAG TTYSPTSPQY SPSSPQYSPS SPQSLS
//
