RPA2_DROME
ID RPA2_DROME Reviewed; 1129 AA.
AC P20028; Q9VPP3;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=DNA-directed RNA polymerase I subunit RPA2;
DE Short=RNA polymerase I subunit 2;
DE EC=2.7.7.6 {ECO:0000250|UniProtKB:P22138};
DE AltName: Full=RPA135;
GN Name=RpI135; ORFNames=CG4033;
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].
RX PubMed=2482932; DOI=10.1007/bf00259609;
RA Kontermann R., Sitzler S., Seifarth W., Petersen G., Bautz E.K.F.;
RT "Primary structure and functional aspects of the gene coding for the
RT second-largest subunit of RNA polymerase III of Drosophila.";
RL Mol. Gen. Genet. 219:373-380(1989).
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=Embryo;
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 DISRUPTION PHENOTYPE.
RX PubMed=25858587; DOI=10.1074/jbc.m114.607036;
RA Kim W., Kim H.D., Jung Y., Kim J., Chung J.;
RT "Drosophila Low Temperature Viability Protein 1 (LTV1) Is Required for
RT Ribosome Biogenesis and Cell Growth Downstream of Drosophila Myc (dMyc).";
RL J. Biol. Chem. 290:13591-13604(2015).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Second largest core component of RNA polymerase I which synthesizes
CC ribosomal RNA precursors. Proposed to contribute to the polymerase
CC catalytic activity and forms the polymerase active center together with
CC the largest subunit. Pol I is composed of mobile elements and RPA2 is
CC part of the core element with the central large cleft and probably a
CC clamp element that moves to open and close the cleft (By similarity).
CC {ECO:0000250|UniProtKB:P22138}.
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:0000250|UniProtKB:P22138};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21249;
CC Evidence={ECO:0000250|UniProtKB:P22138};
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting
CC of at least 13 subunits. {ECO:0000250|UniProtKB:P22138}.
CC -!- INTERACTION:
CC P20028; Q9VH20: TAF1B; NbExp=4; IntAct=EBI-3403932, EBI-104191;
CC P20028; A1Z7A5: udd; NbExp=4; IntAct=EBI-3403932, EBI-126425;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P22138}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in decreased cell
CC size likely as a result of its role in the synthesis of ribosomal RNA
CC precursors. {ECO:0000269|PubMed:25858587}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000305}.
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DR EMBL; X17298; CAA35185.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF51503.1; -; Genomic_DNA.
DR EMBL; AY075569; AAL68376.1; -; mRNA.
DR PIR; JQ0354; JQ0354.
DR RefSeq; NP_476708.1; NM_057360.4.
DR AlphaFoldDB; P20028; -.
DR SMR; P20028; -.
DR BioGRID; 59466; 8.
DR DIP; DIP-61427N; -.
DR IntAct; P20028; 6.
DR STRING; 7227.FBpp0077714; -.
DR PaxDb; P20028; -.
DR PRIDE; P20028; -.
DR DNASU; 33210; -.
DR EnsemblMetazoa; FBtr0078054; FBpp0077714; FBgn0003278.
DR GeneID; 33210; -.
DR KEGG; dme:Dmel_CG4033; -.
DR CTD; 33210; -.
DR FlyBase; FBgn0003278; RpI135.
DR VEuPathDB; VectorBase:FBgn0003278; -.
DR eggNOG; KOG0216; Eukaryota.
DR GeneTree; ENSGT00950000183132; -.
DR HOGENOM; CLU_000524_5_1_1; -.
DR InParanoid; P20028; -.
DR OMA; FFGVVHY; -.
DR OrthoDB; 42570at2759; -.
DR PhylomeDB; P20028; -.
DR Reactome; R-DME-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-DME-73772; RNA Polymerase I Promoter Escape.
DR SignaLink; P20028; -.
DR BioGRID-ORCS; 33210; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 33210; -.
DR PRO; PR:P20028; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0003278; Expressed in eye disc (Drosophila) and 43 other tissues.
DR Genevisible; P20028; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0006360; P:transcription by RNA polymerase I; ISS:FlyBase.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 1.
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; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR InterPro; IPR009674; Rpa2_dom_4.
DR PANTHER; PTHR20856; PTHR20856; 1.
DR Pfam; PF06883; RNA_pol_Rpa2_4; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 1.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 1: Evidence at protein level;
KW DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase;
KW Nucleus; Reference proteome; Transcription; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1129
FT /note="DNA-directed RNA polymerase I subunit RPA2"
FT /id="PRO_0000048075"
FT ZN_FING 1061..1093
FT /note="C4-type"
FT /evidence="ECO:0000250|UniProtKB:P22138"
FT CONFLICT 369
FT /note="A -> S (in Ref. 1; CAA35185)"
FT /evidence="ECO:0000305"
FT CONFLICT 617
FT /note="M -> L (in Ref. 1; CAA35185)"
FT /evidence="ECO:0000305"
FT CONFLICT 727
FT /note="N -> I (in Ref. 1; CAA35185)"
FT /evidence="ECO:0000305"
FT CONFLICT 855
FT /note="K -> T (in Ref. 1; CAA35185)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1129 AA; 128444 MW; DB39B863EF48487B CRC64;
MLEEMQQMKT IPVLTNSRPE FKQIPKKLSR HLANLGGPHV DSFDEMLTVG LDNSAKHMIP
NHWLSPAGEK ISMKVESIWI AKPKVPQDVI DVRTREIYPT DSRQLHVSYS GMCSVRLGWS
VNGVQKTPIN MDLGEVPIML RSKACNLGQA TPEEMVKHGE HDSEWGGIFV IRGNEKIVRM
LIMTRRNHPI CVKRSSWKDR GQNFSDLGML VQTVREDESS LSNVVHYLNN GTAKFMFSHV
KRLSYVPVCL ILKCLMDYTD EEIYNRLVQG YESDQYYVSC VQAMLREVQN ENVYTHAQCK
SFIGNLFRAR FPEVPEWQPD DDVTDFILRE RVMIHLDTYE DKFQLIVFMI QKLFQCAQGK
YKVENVDSAM MQEVLLPGHL YQKYLSERVE SWVSQVRRCL QKKLTSPDAL VTSAVMTQCM
RQAGGVGRAI ESFLATGNIA SRTGLGLMQN SGLVIMAENI NRMRYMSHFR AIHRGSYFTT
MRTTEARQLL PDAWGFICPV HTPDGTPCGL LNHLTLTCEI SMRPDPKLVK AIPKHLIDMG
MMPLSNRRYL GEKLYVVFLD GKHLGHIHQS EAEKIVDELR YGKIFGTLPQ MMEIGFIPFK
KNGQFPGLYI ATGPARMMRP VWNLKWKRVE YIGTLEQLYM EIAIDAKEMY PDFTTHLELA
KTHFMSNLAN LIPMPDYNQS PRNMYQCQMG KQTMGTPCLN WPKQAANKLY RLQTPGTPLF
RPVHYDNIQL DDFAMGTNAI VAVISYTGYD MEDAMIINKA AYERGFAYGS IYKTKFLTLD
KKSSYFARHP HMPELIKHLD TDGLPHPGSK LSYGSPLYCY FDGEVATYKV VKMDEKEDCI
VESIRQLGSF DLSPKKMVAI TLRVPRPATI GDKFASRAGQ KGICSQKYPA EDLPFTESGL
IPDIVFNPHG FPSRMTIAMM IETMAGKGAA IHGNVYDATP FRFSEENTAI DYFGKMLEAG
GYNYYGTERL YSGVDGREMT ADIFFGVVHY QRLRHMVFDK WQVRSTGAVE ARTHQPIKGR
KRGGGVRFGE MERDALISHG AAFLLQDRLF HNSDKTHTLV CHKCGSILAP LQRIVKRNET
GGLSSQPDTC RLCGDNSSVS MIEIPFSFKY LVTELSSVNI NARFKLNEI
