RPC2_DROME
ID RPC2_DROME Reviewed; 1137 AA.
AC P25167; Q8MRD5; Q9V649;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=DNA-directed RNA polymerase III subunit RPC2;
DE Short=RNA polymerase III subunit C2;
DE EC=2.7.7.6;
DE AltName: Full=DNA-directed RNA polymerase III 128 kDa polypeptide;
DE Short=C128;
GN Name=RpIII128; Synonyms=RP128; ORFNames=CG8344;
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=1910149; DOI=10.1007/bf00260636;
RA Seifarth W., Petersen G., Kontermann R., Riva M., Huet J.-C., Bautz E.K.F.;
RT "Identification of the genes coding for the second-largest subunits of RNA
RT polymerases I and III of Drosophila melanogaster.";
RL Mol. Gen. Genet. 228:424-432(1991).
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).
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 III which synthesizes
CC small RNAs, such as 5S rRNA and tRNAs. Proposed to contribute to the
CC polymerase catalytic activity and forms the polymerase active center
CC together with the largest subunit. Pol III is composed of mobile
CC elements and RPC2 is part of the core element with the central large
CC cleft and probably a clamp element that moves to open and close the
CC cleft (By similarity). {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 III (Pol III) complex
CC consisting of 17 subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM51972.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X58826; CAA41631.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF58590.1; -; Genomic_DNA.
DR EMBL; AY121645; AAM51972.1; ALT_INIT; mRNA.
DR PIR; S16894; RNFF32.
DR RefSeq; NP_523706.1; NM_078982.3.
DR AlphaFoldDB; P25167; -.
DR SMR; P25167; -.
DR BioGRID; 62073; 6.
DR IntAct; P25167; 5.
DR STRING; 7227.FBpp0087085; -.
DR PaxDb; P25167; -.
DR PRIDE; P25167; -.
DR DNASU; 36289; -.
DR EnsemblMetazoa; FBtr0087977; FBpp0087085; FBgn0004463.
DR GeneID; 36289; -.
DR KEGG; dme:Dmel_CG8344; -.
DR CTD; 36289; -.
DR FlyBase; FBgn0004463; RpIII128.
DR VEuPathDB; VectorBase:FBgn0004463; -.
DR eggNOG; KOG0215; Eukaryota.
DR GeneTree; ENSGT00950000183132; -.
DR HOGENOM; CLU_000524_5_1_1; -.
DR InParanoid; P25167; -.
DR OMA; LAYCSWC; -.
DR OrthoDB; 42570at2759; -.
DR PhylomeDB; P25167; -.
DR Reactome; R-DME-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR Reactome; R-DME-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR SignaLink; P25167; -.
DR BioGRID-ORCS; 36289; 0 hits in 1 CRISPR screen.
DR ChiTaRS; RpIII128; fly.
DR GenomeRNAi; 36289; -.
DR PRO; PR:P25167; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0004463; Expressed in eye disc (Drosophila) and 24 other tissues.
DR Genevisible; P25167; DM.
DR GO; GO:0005666; C:RNA polymerase III 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:0042797; P:tRNA transcription by RNA polymerase III; 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; IPR007646; RNA_pol_Rpb2_4.
DR InterPro; IPR007647; RNA_pol_Rpb2_5.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR PANTHER; PTHR20856; PTHR20856; 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; PF04566; RNA_pol_Rpb2_4; 1.
DR Pfam; PF04567; RNA_pol_Rpb2_5; 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 2: Evidence at transcript level;
KW DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase;
KW Nucleus; Reference proteome; Transcription; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1137
FT /note="DNA-directed RNA polymerase III subunit RPC2"
FT /id="PRO_0000048094"
FT ZN_FING 1084..1099
FT /note="C4-type"
FT BINDING 1086
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1089
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1098
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CONFLICT 150
FT /note="Missing (in Ref. 1; CAA41631)"
FT /evidence="ECO:0000305"
FT CONFLICT 490
FT /note="D -> Y (in Ref. 1; CAA41631)"
FT /evidence="ECO:0000305"
FT CONFLICT 668
FT /note="P -> T (in Ref. 1; CAA41631)"
FT /evidence="ECO:0000305"
FT CONFLICT 708..709
FT /note="QK -> HN (in Ref. 1; CAA41631)"
FT /evidence="ECO:0000305"
FT CONFLICT 898..899
FT /note="EI -> R (in Ref. 1; CAA41631)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1137 AA; 128515 MW; 043EC430D998E1FD CRC64;
MVELKMGDHN VEATTWDPGD SKDWSVPIKP LTEKWKLVPA FLQVKGLVKQ HIDSFNHFIN
VDIKKIVKAN ELVTSGADPL FYLKYLDVRV GKPDIDDGFN ITKATTPHEC RLRDTTYSAP
ITVDIEYTRG TQRIKRNNLL IGRMPLMLRC SNCALTGKSE FELSKLNECP LDPGGYFVVR
GQEKVILIQE QLSWNKMLTE DFNGVVQCQV TSSTHEKKSR TLVLSKHGKY YLKHNSMTDD
IPIVVIFKAL GVVSDQEIQS LIGIDSKSQN RFGASLIDAY NLKVFTQQRA LEYMGSKLVV
KRFQSATTKT PSEEARELLL TTILAHVPVD NFNLQMKAIY VSMMVRRVMA AELDKTLFDD
RDYYGNKRLE LAGSLLSMMF EDLFKRMNWE LKTIADKNIP KVKAAQFDVV KHMRAAQITA
GLESAISSGN WTIKRFKMER AGVTQVLSRL SYISALGMMT RVNSQFEKTR KVSGPRSLQP
SQWGMLCPSD TPEGEACGLV KNLALMTHIT TEVEERPVMI VAFNAGVEDI REVSGNPINN
PNVFLVFING NVLGLTLNHK HLVRNLRYMR RKGRMGSYVS VHTSYTQRCI YIHTDGGRLC
RPYVIVENRR PLVKQHHLDE LNRGIRKFDD FLLDGLIEYL DVNEENDSFI AWNEDQIEDR
TTHLEIEPFT LLGVCAGLVP YPHHNQSPRN TYQCAMGKQA MGMIGYNQKN RIDSLMYNLV
YPHAPMVKSK TIELTNFDKL PAGQNATVAV MSYSGYDIED ALILNKASID RGYGRCLVYK
NSKCTVKRYA NQTFDRIMGP MKDALTNKVI FKHDVLDTDG IVAPGEQVQN KQIMINKEMP
AVTSMNPLQG QSAQVPYTAV PISYKGPEPS YIERVMVSAN AEEDFLIKIL LRQTRIPEIG
DKFSSRHGQK GVTGLIVEQE DMPFNDFGIC PDMIMNPHGF PSRMTVGKTL ELLGGKAGLL
EGKFHYGTAF GGSKVEDIQA ELERHGFNYV GKDFFYSGIT GTPLEAYIYS GPVYYQKLKH
MVQDKMHARA RGPKAVLTRQ PTQGRSREGG LRLGEMERDC LISYGASMLI MERLMISSDA
FEVDVCRTCG RMAYCSWCHF CQSSANVSKI SMPYACKLLF QELTSMNVVP KMILENY
