RPC2_DICDI
ID RPC2_DICDI Reviewed; 1608 AA.
AC Q54IZ9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
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 subunit B;
DE Contains:
DE RecName: Full=Ddi rpc2 intein;
GN Name=polr3b; Synonyms=rpc2; ORFNames=DDB_G0288449;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP IDENTIFICATION OF INTEIN, AND NOMENCLATURE.
RX PubMed=17069655; DOI=10.1186/1741-7007-4-38;
RA Goodwin T.J., Butler M.I., Poulter R.T.;
RT "Multiple, non-allelic, intein-coding sequences in eukaryotic RNA
RT polymerase genes.";
RL BMC Biol. 4:38-38(2006).
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- PTM: This protein undergoes a protein self splicing that involves a
CC post-translational excision of the intervening region (intein) followed
CC by peptide ligation. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000111; EAL63250.1; -; Genomic_DNA.
DR RefSeq; XP_636731.1; XM_631639.1.
DR AlphaFoldDB; Q54IZ9; -.
DR SMR; Q54IZ9; -.
DR STRING; 44689.DDB0216313; -.
DR PaxDb; Q54IZ9; -.
DR PRIDE; Q54IZ9; -.
DR EnsemblProtists; EAL63250; EAL63250; DDB_G0288449.
DR GeneID; 8626608; -.
DR KEGG; ddi:DDB_G0288449; -.
DR dictyBase; DDB_G0288449; rpc2.
DR eggNOG; KOG0215; Eukaryota.
DR HOGENOM; CLU_000524_5_1_1; -.
DR InParanoid; Q54IZ9; -.
DR OMA; LAYCSWC; -.
DR Reactome; R-DDI-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR Reactome; R-DDI-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR PRO; PR:Q54IZ9; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005736; C:RNA polymerase I complex; ISS:dictyBase.
DR GO; GO:0005666; C:RNA polymerase III complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; ISS:dictyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR GO; GO:0006360; P:transcription by RNA polymerase I; ISS:dictyBase.
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; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR006141; Intein_N.
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 SMART; SM00306; HintN; 1.
DR SUPFAM; SSF51294; SSF51294; 1.
DR TIGRFAMs; TIGR01443; intein_Cterm; 1.
DR TIGRFAMs; TIGR01445; intein_Nterm; 1.
DR PROSITE; PS50818; INTEIN_C_TER; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage; DNA-directed RNA polymerase; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Protein splicing; Reference proteome;
KW Transcription; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..505
FT /note="DNA-directed RNA polymerase III subunit rpc2, 1st
FT part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000328068"
FT CHAIN 506..969
FT /note="Ddi rpc2 intein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000328069"
FT CHAIN 970..1608
FT /note="DNA-directed RNA polymerase III subunit rpc2, 2nd
FT part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000328070"
FT ZN_FING 1557..1572
FT /note="C4-type"
FT BINDING 1557
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1560
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1569
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1572
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1608 AA; 183030 MW; 16D3C2AC009EAF5A CRC64;
MDPESVGYCN NPDFLHKGSM DELYNISKLT DDIKPVEEKW KLVPAFMKCR GLVKQHIDSF
NFFINVEMKK IVKANERLTA ENDPSYFVRF TDINVGSPTS TEDNLDSVQL TPQRCRLRDM
TYSAPIFVNI EYTRNKQIIS KRDVHIGNIP IMLRSSNCVL SKKTPEQMAA LGECPMDPGG
YFIVRGQEKV ILNHEQLSKN RIIIEMDSKG LPSASVTSST HERKSRTGVT LKNEKLYLKH
NTFGEDIPVA IVLKGMGVET DQEMAQLVGS DDVFLNAITP SLEECQKCGV HTAAQALDYL
GSRIKVFRRP YGVQNKKTKS EEARDILAGV VLNHVPVRRY NFRLKVIYLS LMIRRIIMAS
KDKSCLDDKD YYGNKRIELS GQLISLLFED CFKKFQSELK KSVDQAIAKA NRAENLDLPK
LIRTDTITNG FTHAISSGQW NLKRFRMERS GVSQVLSRLS YISCMGMMTR IQSQFEKTRK
VAGPRSLQPS QWGMLCPSDT PEGEACLHPD TIITMSNGQQ KPIRQLKDGD SIITLDPITM
EAHSTRIYSH FIKSSSQYGK QLLKITTITG KEIICTNDHR FLTSNGNWKQ SKDLLLNDKL
FLISSSNQLE FNNNNNENNN ENNNDIIEIL NENQLINQGV VPIKIIQELK SIELLPLLNN
NEKLITISRI IGSIDKIGSN KQNEPIIQYQ FNLISDFDQF LKDLQYLGFI NPIYKLNEEQ
QQQQQQKIDH QQQQQQQVEQ QQKSIIIDFI GSSFGYFIQS LLNEKNWIEK SNNQFVKKEF
LSSFISNVNR IQFNIIEEIN QQNNDSNFKI LLNYKQQKQQ QNEKEERAVV DHDNEIFNIK
SLQILLNQFN VISSIDFEES NLIIINSSLK KFIDLINIKF NQKLNNQIIQ IREYLNYINY
NNNNNNNEEI NIKKKDFGYF KKLKIKRNSF EIEIEKIEQL NYQDCPEISD FTTESDYHSM
ISNGFVSHNC GLVKNFALMS HVTTDDSEGP LLRLAYNLGV QDILLVTGEE LNSRNAYLVL
LNGQIIGIHN SPDYFVTTLR KMRRAGRIRE FVSICKNKAQ QTISVACDGG RLCRPVIIVD
DQRPRLTQEH IEDLKDGLRT FDDFIREGII EYLDVNEEND SFLAWREAAI QPWTTHLEIE
PFTMLGCVAG LIPYPHHNQS PRNTYQCAMG KQAIGAIAYN QLTRIDTLLY LLVHTQRPLC
QTRTIDLLNW YKLPAGHNAT VAVMSYSGYD IEDALVMNKA SLDRGFGRCI VLKKQVTSIK
KHGNDTSDRI FPPTPNDLRQ PKYGLLDSDG IAKPGELAQK GQILVNKYSP LNTIDATPNP
ELIPDSAYKS SYMGYKYDNP AFIDKVLLTS GDDEQLLIKM LMRSTRRPEL GDKFSSRHGQ
KGVCGIIVKQ EDMPFSDLGI CPDIIMNPHG FPSRMTIGKM IELLAGKAGV LSGKFGFGTC
FGGDRVENIS KVLISKGFSY GGKDYVTSGV TGEPLACFIF FGPIFYQKLK HMVMDKMHAR
ARGPTVTLTR QPTEGRARGG GLRLGEMERD CLIGYGASAL IMERLMISSD RFTVYACKNC
GFLGYEGYCQ YCKSSVDIST IQIPYACKLL FQELQAMNIV PRLKLVDS
