ID A0A087XQQ3_POEFO Unreviewed; 1907 AA.
AC A0A087XQQ3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN Name=POLR2A {ECO:0000313|Ensembl:ENSPFOP00000008106.2};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000008106.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000008106.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) 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=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; AYCK01004356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007551323.1; XM_007551261.2.
DR STRING; 48698.ENSPFOP00000008106; -.
DR Ensembl; ENSPFOT00000008118.2; ENSPFOP00000008106.2; ENSPFOG00000007890.2.
DR GeneID; 103137507; -.
DR KEGG; pfor:103137507; -.
DR CTD; 5430; -.
DR eggNOG; KOG0260; Eukaryota.
DR GeneTree; ENSGT00930000151033; -.
DR OMA; MVQYDRT; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000028760; 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; 29.
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; 21.
PE 3: Inferred from homology;
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:UP000028760};
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 244..547
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1544..1907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1563..1582
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1607..1901
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1907 AA; 211031 MW; 853321A78DF113A2 CRC64;
MHGPPSGDSA CPLRTIKRVQ FGVISPDELK RMSVTEGGIK YPETTEGGRP KLGGLMDPRQ
GVIERSGRCQ TCAGNMTECP GHFGHIELAK PVFHVGFISK IMKILRCVCF FCSKLLVDSN
NPKIKEILVK SKGQPRKRLT HVYELCKGKN ICEGGEEMDN KFGMEPQETE EDITKEKGHG
GCGRYQPRIR RSGLELYAEW KHVNEDSQEK KILLSPERVH EIFKRISDEE DIILGMDPKF
ARPEWMIVTV LPVPPLAVRP AVVMQGSARN QDDLTHKLAD IVKINNQLRR NEQSGAAAHV
IAEDVKLLQF HVATMVDNEL PGLPRAMQKS GRPLKSIKQR LKGKEGRVRG NLMGKRVDFS
ARTVITPDPN LQIDQVGVPR SIAANMTFPE IVTPFNIDRL QELVRRGNSQ YPGAKYIIRD
NGDRIDLRFH PKPSDLHLQI GYKVERHMCD GDIIIFNRQP TLHKMSMMGH RVRILPWSTF
RLNLSVTTPY NADFDGDEMN LHLPQSLETR AEIQELAMVP RMIVTPQSNR PVMGIVQDTL
TAVRKFTKRD VFLERGEVMN LLMFLSTWDG KMPQPAILKP RPLWTGKQIF SLIIPGHINV
IRTHSTHPDD EDSGPYKHIS PGDTKVIVEN GELIMGILCK KSLGTSAGSL VHISYLEMGH
DITRLFYSNI QTVVNNWLLI EGHSIGIGDS IADAKTYLDI QNTIKKAKQD VIEVIEKAHN
NELEPTPGNT LRQTFENQVN RILNDARDKT GSSAQKSLSE YNNFKSMVVA GSKGSKINIS
QVIAVVGQQN VEGKRIPFGF KHRTLPHFIK DDYGPESRGF VENSYLAGLT PTEFFFHAMG
GREGLIDTAV KTAETGYIQR RLIKSMESVM VKYDATVRNS INQVVQLRYG EDGLAGENVE
FQNLATLKPS NKAFEKKFRF DCTNERALRR VLQEDVVKDV LTNAHVQSVL EKEFEKMRED
REILRAIFPT GDSKVVLPCN LARMIWNAQK IFRINTRTPT DLNPLRVVEG VHELSKKLVI
VNGDDPLSRQ AQENATLLFN IHLRSTLCSK RMTEEFRLST EAYDWLLGEI ETKFNQSIAH
PGEMVGALAA QSLGEPATQM TLNTFHYAGV SAKNVTLGVP RLKELINISK RPKTPSLTVF
LLGQAARDAE RAKDILCRLE HTTLRKVTAN TAIYYDPNPQ NTVVAEDQEW VNVYYEMPDF
DVTRISPWLL RIELDRKHMT DRKLTMEQIA EKINAGFGDD LNCIFNDDNA EKLVLRIRIM
NSDENKFQED EEVVDKMDDD VFLRCIESNM LTDMTLQGIE QISKVYMHLP QTDNKKKIII
TEDGEFKALQ EWILETDGVS LMRVLSEKDV DPVRTTSNDI VEIFTVLGIE AVRKALEREL
YHVISFDGSY VNYRHLALLC DTMTCRGHLM AITRHGINRQ DTGPLMKCSF EETVDVLMEA
SSHGECDPMK GVSENIMLGQ LAPAGTGCFD LLLDAEKCKY GMEIPTNIPG ISVAGPTGMF
FGSVPSPMSG MSPAMTPWNT GATPAYGAWS PSVGSGMTPG AAGFSPSAAS DASGFSPGYS
PAWSPTPGSP GSPGPVSPYI PSPGGAMSPN YSPTSPAYEP RSPGGYTPQS PGYSPTSPSY
SPTSPSYSPT SPNYSPTSPS YSPTSPSYSP TSPSYSPTSP SYSPTSPSYS PTSPSYSPTS
PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP TSPSYSPTSP SYSPTSPSYS
PTSPSYSPTS PNYTPTSPSY SPTSPSYSPT SPSYSPTSPN YTPTSPNYSP TSPSYSPTSP
SYSPSSPRYT PQSPTYTPSS PSYSPSSPSY SPTSPKYTPT SPSYSPSSPE YTPTSPKYSP
TSPKYSPTSP KYSPTSPTYS PTTPKYSPTS PTYSPAISPD DSDEENN
//
