RPC1_SCHPO
ID RPC1_SCHPO Reviewed; 1405 AA.
AC O94666; Q0QYE3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 140.
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 largest subunit;
DE AltName: Full=RPC158;
GN Name=rpc1; ORFNames=SPBC651.08c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=16877568; DOI=10.1093/nar/gkl421;
RA Proshkina G.M., Shematorova E.K., Proshkin S.A., Zaros C., Thuriaux P.,
RA Shpakovski G.V.;
RT "Ancient origin, functional conservation and fast evolution of DNA-
RT dependent RNA polymerase III.";
RL Nucleic Acids Res. 34:3615-3624(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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; DQ156227; ABA54855.1; -; mRNA.
DR EMBL; CU329671; CAB37604.1; -; Genomic_DNA.
DR PIR; T40607; T40607.
DR RefSeq; NP_595506.1; NM_001021416.2.
DR AlphaFoldDB; O94666; -.
DR SMR; O94666; -.
DR BioGRID; 277609; 5.
DR STRING; 4896.SPBC651.08c.1; -.
DR MaxQB; O94666; -.
DR PaxDb; O94666; -.
DR PRIDE; O94666; -.
DR EnsemblFungi; SPBC651.08c.1; SPBC651.08c.1:pep; SPBC651.08c.
DR GeneID; 2541094; -.
DR KEGG; spo:SPBC651.08c; -.
DR PomBase; SPBC651.08c; rpc1.
DR VEuPathDB; FungiDB:SPBC651.08c; -.
DR eggNOG; KOG0261; Eukaryota.
DR HOGENOM; CLU_000487_3_0_1; -.
DR InParanoid; O94666; -.
DR OMA; AVCPPYN; -.
DR PhylomeDB; O94666; -.
DR Reactome; R-SPO-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR Reactome; R-SPO-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR PRO; PR:O94666; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005666; C:RNA polymerase III complex; ISO:PomBase.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; ISO:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006383; P:transcription by RNA polymerase III; ISO:PomBase.
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 2: Evidence at transcript level;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Transcription;
KW Transferase; Zinc.
FT CHAIN 1..1405
FT /note="DNA-directed RNA polymerase III subunit rpc1"
FT /id="PRO_0000073951"
FT REGION 838..850
FT /note="Bridging helix"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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"
FT BINDING 497
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1405 AA; 157562 MW; 104B1AC4145A3B7B CRC64;
MKDPIDDQIP KRIKHLQFGI NGPEEFVKDG TVEVSRRDLY TMTDRSPAEH GALDLHMGTS
NKQINCATCG ESMADCMGHF GYVKLALPVF HIGYFKATLT ILQNICKDCS SVLLSDQEKR
QFLKDLRRPG IDNLRRSQIC KRINDHCKKM RRCSKCDAMQ GVVKKAGPLK IIHERFRYVR
KSQDDEENFR HSFDEALKTI PELKMHLSKA HDDLNPLKVL NLFKQITPVD CELLGMDPEH
GRPENLLWRY VPAPPVCIRP SVAQEGATTE DDLTVKITEI IWTSSLIRAA LSKGTPISNL
MEQWEFMQLS IAMYINSEMP GLRPSDMPSK PIRGFCQRLK GKQGRFRGNL SGKRVDFSGR
TVISPDPNLR IDQVAVPYRI AKILTFPERV TTQNKKHLQD CIRNGPDVHP GANYVIDRES
GFKRFLRFGN RNRIADDLKI GDIVERHLHD NDVVLFNRQP SLHKLSIMAH LVKVRPWRTL
RFNECVCGPY NADFDGDEMN LHVPQTEEAK TEALELMGIK NNLVSPRNGE PIIAATQDFI
TAAYLLSLKD TFLDRKSISN ICCYMMDAST HIDLPPPAII KPRCLWTGKQ VFTVLMKPNR
FSKVLVNLDA KTRSFSRIKS KTPEMCPKDG YLMIRNSEII AGVVDKSVVG DGKKDSLFYV
ILRDYGALEA AEAITRLSKM CARFLGNRGF SIGIEDVQPG KSLSSQKEIL VNKAYATSDD
FIMQYAKGIL ECQPGMDQEA TLEAKISSTL SKVRDDVGEI CMDELGPANS PLIMATCGSK
GSKINVSQMV ACVGQQIISG KRVPDGFQDR SLPHFHKNSK HPLAKGFVSN SFYSGLTPTE
FLFHAISGRE GLVDTAVKTA ETGYMSRRLM KSLEDLSSAY DGTVRSSNSD VVQFVYGDDG
LDPTYMEGDG QAVEFKRTWI HSVNLNYDRH DSAMLPYEII DYVNRALDDP KFLTNCNRDF
IETIRTFVIE NIAKYLASVR ERRDLAPMLE EPDMDDLDDM EGDEFAPVAK RKSVENIIRV
TEKQLRSFVD RCWEKYMRAK VEPGTAVGAI GAQSIGEPGT QMTLKTFHFA GVAAQTTLGV
PRIKEIINAA KTISTPIITG QLINDRDERS ARVVKGRIEK TYLKDVTSYI EEVYGPVTTY
LSIQVNFDTI SKLQLDITLA DIAAAIWNTP KLKIPSQQVT VNNTLQQIHV HTSSDGKSSE
TEVYYRLQTY KRVLPDVVVA GIPTINRSVI NQESGKIELF MEGTGLQAVM NTEGIVGTKT
STNHVMEMKD VLGIEAARYS IISEIGYTMA KHGLTVDPRH IMLLGDVMTC KGEVLGITRF
GVAKMKDSVL ALASFEKTTD HLFNAAARFA KDSIEGISEC IVLGKLAPIG TNVFQLIRRT
EEEEEQKPKE LLFDTPSLHQ LEITA
