RPA1_DROME
ID RPA1_DROME Reviewed; 1642 AA.
AC P91875; Q8MRE2; Q9V732;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=DNA-directed RNA polymerase I subunit RPA1;
DE Short=RNA polymerase I subunit A1;
DE EC=2.7.7.6;
DE AltName: Full=DNA-directed RNA polymerase I largest subunit;
DE AltName: Full=DNA-directed RNA polymerase I subunit A;
GN Name=RpI1; Synonyms=RPA1; ORFNames=CG10122;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Oregon-R;
RX PubMed=9065685; DOI=10.1007/s004380050354;
RA Knackmuss S., Bautz E.K.F., Petersen G.;
RT "Identification of the gene coding for the largest subunit of RNA
RT polymerase I (A) of Drosophila melanogaster.";
RL Mol. Gen. Genet. 253:529-534(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Ovary;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1364 AND SER-1365, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Largest and catalytic core component of RNA polymerase I which
CC synthesizes ribosomal RNA precursors. Forms the polymerase active
CC center together with the second largest subunit. A single stranded DNA
CC template strand of the promoter is positioned within the central active
CC site cleft of Pol I. A bridging helix emanates from RPA1 and crosses
CC the cleft near the catalytic site and is thought to promote
CC translocation of Pol I by acting as a ratchet that moves the RNA-DNA
CC hybrid through the active site by switching from straight to bent
CC conformations at each step of nucleotide addition (By similarity).
CC {ECO:0000250}.
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;
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting
CC of at least 13 subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000305}.
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DR EMBL; Y09103; CAA70321.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF58234.1; -; Genomic_DNA.
DR EMBL; AY121632; AAM51959.1; -; mRNA.
DR PIR; T13803; T13803.
DR RefSeq; NP_523743.1; NM_079019.3.
DR AlphaFoldDB; P91875; -.
DR SMR; P91875; -.
DR BioGRID; 62365; 6.
DR IntAct; P91875; 1.
DR STRING; 7227.FBpp0086640; -.
DR iPTMnet; P91875; -.
DR PaxDb; P91875; -.
DR PRIDE; P91875; -.
DR EnsemblMetazoa; FBtr0087511; FBpp0086640; FBgn0019938.
DR GeneID; 36617; -.
DR KEGG; dme:Dmel_CG10122; -.
DR CTD; 36617; -.
DR FlyBase; FBgn0019938; RpI1.
DR VEuPathDB; VectorBase:FBgn0019938; -.
DR eggNOG; KOG0262; Eukaryota.
DR GeneTree; ENSGT00920000149138; -.
DR HOGENOM; CLU_000487_2_2_1; -.
DR InParanoid; P91875; -.
DR PhylomeDB; P91875; -.
DR Reactome; R-DME-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-DME-73772; RNA Polymerase I Promoter Escape.
DR SignaLink; P91875; -.
DR BioGRID-ORCS; 36617; 1 hit in 1 CRISPR screen.
DR ChiTaRS; RpI1; fly.
DR GenomeRNAi; 36617; -.
DR PRO; PR:P91875; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0019938; Expressed in eye disc (Drosophila) and 26 other tissues.
DR Genevisible; P91875; DM.
DR GO; GO:0005736; C:RNA polymerase I complex; ISS:FlyBase.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006360; P:transcription by RNA polymerase I; ISS:FlyBase.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 1.
DR Gene3D; 4.10.860.120; -; 1.
DR InterPro; IPR015699; DNA-dir_RNA_pol1_lsu.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR000722; RNA_pol_asu.
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; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR PANTHER; PTHR19376:SF11; PTHR19376:SF11; 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 SMART; SM00663; RPOLA_N; 1.
PE 1: Evidence at protein level;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transferase; Zinc.
FT CHAIN 1..1642
FT /note="DNA-directed RNA polymerase I subunit RPA1"
FT /id="PRO_0000073926"
FT REGION 939..951
FT /note="Bridging helix"
FT /evidence="ECO:0000250"
FT REGION 1337..1428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1337..1363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1371..1388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1389..1419
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 565
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 567
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 569
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MOD_RES 1364
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1365
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 407
FT /note="S -> C (in Ref. 1; CAA70321)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="D -> AY (in Ref. 1; CAA70321)"
FT /evidence="ECO:0000305"
FT CONFLICT 461..462
FT /note="EL -> DV (in Ref. 1; CAA70321)"
FT /evidence="ECO:0000305"
FT CONFLICT 758
FT /note="L -> V (in Ref. 1; CAA70321)"
FT /evidence="ECO:0000305"
FT CONFLICT 1042
FT /note="A -> V (in Ref. 1; CAA70321)"
FT /evidence="ECO:0000305"
FT CONFLICT 1085
FT /note="I -> V (in Ref. 1; CAA70321)"
FT /evidence="ECO:0000305"
FT CONFLICT 1315..1316
FT /note="RA -> PPP (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1341
FT /note="D -> E (in Ref. 2; AAF58234)"
FT /evidence="ECO:0000305"
FT CONFLICT 1494
FT /note="N -> T (in Ref. 2; AAF58234)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1642 AA; 185410 MW; B05DB5C4A5149F9A CRC64;
MGSKRAMDVH MFPSDLEFAV FTDQEIRKLS VVKVITGITF DALGHAIPGG LYDIRMGSYG
RCMDPCGTCL KLQDCPGHMG HIELGTPVYN PFFIKFVQRL LCIFCLHCYK LQMKDHECEI
IMLQLRLIDA GYIIEAQELE LFKSEIVCQN TENLVAIKNG DMVHPHIAAM YKLLEKNEKN
SSNSTKTSCS LRTAITHSAL QRLGKKCRHC NKSMRFVRYM HRRLVFYVTL ADIKERVGTG
AETGGQNKVI FADECRRYLR QIYANYPELL KLLVPVLGLS NTDLTQGDRS PVDLFFMDTL
PVTPPRARPL NMVGDMLKGN PQTDIYINII ENNHVLNVVL KYMKGGQEKL TEEAKAAYQT
LKGETAHEKL YTAWLALQMS VDVLLDVNMS REMKSGEGLK QIIEKKSGLI RSHMMGKRVN
YAARTVITPD PNINVDEIGI PDIFAKKLSY PVPVTEWNVT ELRKMVMNGP DVHPGANYIQ
DKNGFTTYIP ADNASKRESL AKLLLSNPKD GIKIVHRHVL NGDVLLLNRQ PSLHKPSIMG
HKARILHGEK TFRLHYSNCK AYNADFDGDE MNAHYPQSEV ARAEAYNLVN VASNYLVPKD
GTPLGGLIQD HVISGVKLSI RGRFFNREDY QQLVFQGLSQ LKKDIKLLPP TILKPAVLWS
GKQILSTIII NIIPEGYERI NLDSFAKIAG KNWNVSRPRP PICGTNPEGN DLSESQVQIR
NGELLVGVLD KQQYGATTYG LIHCMYELYG GDVSTLLLTA FTKVFTFFLQ LEGFTLGVKD
ILVTDVADRK RRKIIRECRN VGNSAVAAAL ELEDEPPHDE LVEKMEAAYV KDSKFRVLLD
RKYKSLLDGY TNDINSTCLP RGLITKFPSN NLQLMVLSGA KGSMVNTMQI SCLLGQIELE
GKRPPLMISG KSLPSFTSFE TSPKSGGFID GRFMTGIQPQ DFFFHCMAGR EGLIDTAVKT
SRSGYLQRCL IKHLEGLSVH YDLTVRDSDN SVVQFLYGED GLDILKSKFF NDKFCADFLT
QNATAILRPA QLQLMKDEEQ LAKVQRHEKH IRSWEKKKPA KLRAAFTHFS EELREEVEVK
RPNEINSKTG RRRFDEGLLK LWKKADAEDK ALYRKKYARC PDPTVAVYKQ DLYYGSVSER
TRKLITDYAK RKPALKETIA DIMRVKTIKS LAAPGEPVGL IAAQSIGEPS TQMTLNTFHF
AGRGEMNVTL GIPRLREILM LASSNIKTPS MDIPIKPGQQ HQAEKLRINL NSVTLANLLE
YVHVSTGLTL DPERSYEYDM RFQFLPREVY KEDYGVRPKH IIKYMHQTFF KQLIRAILKV
SNASRTTKIV VIDDKKDADK DDDNDLDNGD EVGRSKAKAN DDDSSDDNDD DDATGVKLKQ
RKTDEKDYDD PDDVEELHDA NDDDDEAEDE DDEEKGQDGN DNDGDDKAVE RLLSNDMVKA
YTYDKENHLW CQVKLNLSVR YQKPDLTSII RELAGKSVVH QVQHIKRAII YKGNDDDQLL
KTDGINIGEM FQHNKILDLN RLYSNDIHAI ARTYGIEAAS QVIVKEVSNV FKVYGITVDR
RHLSLIADYM TFDGTFQPLS RKGMEHSSSP LQQMSFESSL QFLKSAAGFG RADELSSPSS
RLMVGLPVRN GTGAFELLTK IC
