RPC1_DICDI
ID RPC1_DICDI Reviewed; 1450 AA.
AC Q86AQ5; Q54ZZ2;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=DNA-directed RNA polymerase III subunit rpc1;
DE Short=RNA polymerase III subunit C1;
DE EC=2.7.7.6;
DE AltName: Full=DNA-directed RNA polymerase III subunit A;
GN Name=polr3a; Synonyms=rpc1; ORFNames=DDB_G0277199;
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=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
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).
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 III which
CC synthesizes small RNAs, such as 5S rRNA and tRNAs. Forms the polymerase
CC active center together with the second largest subunit. A single-
CC stranded DNA template strand of the promoter is positioned within the
CC central active site cleft of Pol III. A bridging helix emanates from
CC RPC1 and crosses the cleft near the catalytic site and is thought to
CC promote translocation of Pol III by acting as a ratchet that moves the
CC RNA-DNA hybrid through the active site by switching from straight to
CC bent 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 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}.
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DR EMBL; AAFI02000019; EAL68785.1; -; Genomic_DNA.
DR RefSeq; XP_642724.1; XM_637632.1.
DR AlphaFoldDB; Q86AQ5; -.
DR SMR; Q86AQ5; -.
DR STRING; 44689.DDB0216293; -.
DR PaxDb; Q86AQ5; -.
DR EnsemblProtists; EAL68785; EAL68785; DDB_G0277199.
DR GeneID; 8620917; -.
DR KEGG; ddi:DDB_G0277199; -.
DR dictyBase; DDB_G0277199; rpc1.
DR eggNOG; KOG0261; Eukaryota.
DR HOGENOM; CLU_000487_3_0_1; -.
DR InParanoid; Q86AQ5; -.
DR OMA; AVCPPYN; -.
DR PhylomeDB; Q86AQ5; -.
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:Q86AQ5; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005666; C:RNA polymerase III complex; ISS:dictyBase.
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:0006383; P:transcription by RNA polymerase III; ISS:dictyBase.
DR CDD; cd02736; RNAP_III_Rpc1_C; 1.
DR CDD; cd02583; RNAP_III_RPC1_N; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 1.
DR Gene3D; 4.10.860.120; -; 1.
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; IPR035698; RNAP_III_Rpc1_C.
DR InterPro; IPR035697; RNAP_III_RPC1_N.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 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 3: Inferred from homology;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Transcription;
KW Transferase; Zinc.
FT CHAIN 1..1450
FT /note="DNA-directed RNA polymerase III subunit rpc1"
FT /id="PRO_0000330754"
FT REGION 832..844
FT /note="Bridging helix"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 491
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 493
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 495
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1450 AA; 163727 MW; 4F56DE7F372097A2 CRC64;
MIELLKEDDA PKKIGHIQFG LLSEDDIVRL SHVQIVNREL FDLVKRKPTP YGVLDNKLGT
SDKQAMCTTC GLSIVDCVGH FGYIKLQLPV FHIGYLKNIM NILQMICKSC STILLNEEKK
QYYLRKMRNK KMDNLQRKSL LKKIFLECRK TKECLKCGST NGMIKKSGAF KIIHEKYKGK
TESLQDYYAL YDDAIKYNPE MKSHIKKAQD DLNPLVALNL FKKISYQDIE IMNMDPVIGR
PERLILTYML VPPVSIRPSV PMDGGSGTNE DDLTMKLSEI LHINEHIRSN VDRAEMSAIM
EDWDYLQASC AIYINSDVPG LPLQMKPTKA VRGLSQRLKG KTGRFRGNLS GKRVDFSGRT
VISPDPNLNI DEVAVPQLIA LTMTYPERVT DYNIERLQKY VINGPDRHPG ANYIIYADGV
KKWLKFGNRE KFAAELKIGD IVERHIIDGD IMLFNRQPSL HKLSIMSHKA RVMPWRTLRF
NECVCTPYNA DFDGDEMNIH LPQTEEARAE ATILMGVTNN LITPRNGEPL VAATQDFLTA
SYLISRRDAF YERYRFALMC THFADANEHI DLPPPAILKP VELWTGKQIF EVLLRPSVKS
HVLCNFETRS RTYSKNLYMC PKDGYVYFRN SELMCGSIDK SIIGGGNKNS LFHILMRDFS
PTIAANCMTR LAKLCARFLG DQGFSIGIPD IKPAEDLDRK KREIIETAYK KCAVFLKDYE
SGSLQLSSGC SMEQTFEAKM NQTLSQIRDD CGKLCVNDLP NYNSPLIMGL CGSKGSNINI
AQMICCVGQQ IVNGTRIPNG FTNRTTPHFK HFAKNPKSKG FVSNSFYTGM IPTEFFFHTM
GGREGLVDTA VKTAETGYMQ RRLMKALEDL STHYDYTVRD SIGGIVQFIY GDDGLDPAGM
EAKDRPVDFL RAMMSVKSTR QCRNEPEMKP FEIRKLVESI IDSSKFEACT DLFKNEIRVF
FNGNEKTKGY IQELISLRKQ FKLSSFDLND NEDEIIIEDN SPMDISTTTT TTTTTTTNNA
VKITNITTDI EMNESNKEEN DKIEKERIEK EKESKRLKLL GERFANEHVV NQIHRITKTQ
IELFLDICLD KYSRARIEPG TAVGAIGAQS IGEPGTQMTL KTFHFAGVAS MNVTLGVPRI
KEIINAAKNI STPIITASLN CDYDIRSARI VAGRIEKTTL GHVATHIKEV VKRAGCYLSI
KIDKNFVDSL QLEINSKTIS QSIASTKGLK LKPEQITTNG DYKLRIVPPA NIREGSLYYL
QFLKNNLPAV IVKGIPTVNR VVISKVDEKQ ERYQLLVEGY DLRAVMATPG IKGTHTTSNH
IMECENTLGI ETARNTIMSE IDMIMTSHGM SIDIRHVMLL ADLMSFKGEI LGITRFGIAK
MKESVLMLAS FEKTTDHLFD AAVHHRQDDI VGVSECIIMG VVIPLGTGLF KLLRKSNKNN
LPKKSLLLQD
