RPA1_SCHPO
ID RPA1_SCHPO Reviewed; 1689 AA.
AC P15398;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=DNA-directed RNA polymerase I subunit rpa1;
DE EC=2.7.7.6;
DE AltName: Full=DNA-directed RNA polymerase I 190 kDa polypeptide;
DE AltName: Full=DNA-directed RNA polymerase I largest subunit;
GN Name=rpa1; Synonyms=nuc1; ORFNames=SPBC4C3.05c;
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 [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX PubMed=2537310; DOI=10.1083/jcb.108.2.243;
RA Hirano T., Konoha G., Toda T., Yanagida M.;
RT "Essential roles of the RNA polymerase I largest subunit and DNA
RT topoisomerases in the formation of fission yeast nucleolus.";
RL J. Cell Biol. 108:243-253(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=972 / HM123;
RX PubMed=2854522; DOI=10.1016/0378-1119(88)90183-7;
RA Yamagishi M., Nomura M.;
RT "Cloning and sequence determination of the gene encoding the largest
RT subunit of the fission yeast Schizosaccharomyces pombe RNA polymerase I.";
RL Gene 74:503-515(1988).
RN [3]
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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159; SER-161; SER-1438 AND
RP SER-1441, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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 I which
CC synthesizes ribosomal RNA precursors. Forms the polymerase active
CC center together with the second largest subunit. A single stranded DNA
CC template strand of the promoter is positioned within the central active
CC site cleft of Pol I. A bridging helix emanates from RPA1 and crosses
CC the cleft near the catalytic site and is thought to promote
CC translocation of Pol I by acting as a ratchet that moves the RNA-DNA
CC hybrid through the active site by switching from straight to bent
CC conformations at each step of nucleotide addition (By similarity).
CC {ECO:0000250|UniProtKB:P10964}.
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 I (Pol I) complex consisting
CC of at least 13 subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:2537310}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000305}.
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DR EMBL; X14783; CAA32887.1; -; Genomic_DNA.
DR EMBL; M37411; AAA35326.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA16827.1; -; Genomic_DNA.
DR PIR; JS0080; JS0080.
DR RefSeq; NP_596300.1; NM_001022221.2.
DR PDB; 7AOC; EM; 3.84 A; A=1-1689.
DR PDB; 7AOD; EM; 4.50 A; A/M=1-1689.
DR PDB; 7AOE; EM; 3.90 A; A=1-1689.
DR PDBsum; 7AOC; -.
DR PDBsum; 7AOD; -.
DR PDBsum; 7AOE; -.
DR AlphaFoldDB; P15398; -.
DR SMR; P15398; -.
DR BioGRID; 277390; 20.
DR IntAct; P15398; 1.
DR STRING; 4896.SPBC4C3.05c.1; -.
DR iPTMnet; P15398; -.
DR MaxQB; P15398; -.
DR PaxDb; P15398; -.
DR PRIDE; P15398; -.
DR EnsemblFungi; SPBC4C3.05c.1; SPBC4C3.05c.1:pep; SPBC4C3.05c.
DR GeneID; 2540873; -.
DR KEGG; spo:SPBC4C3.05c; -.
DR PomBase; SPBC4C3.05c; -.
DR VEuPathDB; FungiDB:SPBC4C3.05c; -.
DR eggNOG; KOG0262; Eukaryota.
DR HOGENOM; CLU_000487_2_4_1; -.
DR InParanoid; P15398; -.
DR OMA; RFFNRED; -.
DR PhylomeDB; P15398; -.
DR Reactome; R-SPO-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-SPO-73772; RNA Polymerase I Promoter Escape.
DR PRO; PR:P15398; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005730; C:nucleolus; IDA:PomBase.
DR GO; GO:0005736; C:RNA polymerase I complex; ISO:PomBase.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006360; P:transcription by RNA polymerase I; ISO:PomBase.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 1.
DR Gene3D; 4.10.860.120; -; 1.
DR InterPro; IPR015699; DNA-dir_RNA_pol1_lsu.
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; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR PANTHER; PTHR19376:SF11; PTHR19376:SF11; 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 1: Evidence at protein level;
KW 3D-structure; DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transferase; Zinc.
FT CHAIN 1..1689
FT /note="DNA-directed RNA polymerase I subunit rpa1"
FT /id="PRO_0000073929"
FT REGION 269..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1017
FT /note="Bridging helix"
FT /evidence="ECO:0000250"
FT REGION 1346..1440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1363..1425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 643
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 645
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 647
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1438
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1441
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 69
FT /note="D -> A (in Ref. 1; CAA32887)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="I -> S (in Ref. 1; CAA32887)"
FT /evidence="ECO:0000305"
FT CONFLICT 704
FT /note="T -> I (in Ref. 1; CAA32887)"
FT /evidence="ECO:0000305"
FT CONFLICT 1581
FT /note="A -> T (in Ref. 1; CAA32887)"
FT /evidence="ECO:0000305"
FT CONFLICT 1681
FT /note="T -> N (in Ref. 1; CAA32887)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1689 AA; 189246 MW; 2D2D3A2DEC94A497 CRC64;
MNIAQPVSSE IKSVKFGIYD VDDVEKISVK QIVNPVLLDN LNHPTNGGLY DLALGPYLKN
SVCATCHLDE RYCPGHFGHI VLPIPAYHPL FFSQMYNLLR STCLYCHHFK LSKVKVHLFF
CRLKLLDYGL LNESEMVENV SLTEAIIKNS NGTPLEDGSD SEDSGLGHDD IAKDAATLMR
IRDEFVAKSI ADSRQNAHID AQLTTLLLHE RKKVVRAFYH AISSRKQCDN CQSFSPNFRK
EGFAKIFEIP LSGKNLQFME QTGKIRSDVL RDTSKKHHED EGYDGDSDSS NESEVEGIDL
FEEDPNPLKN KSKSPIAHGA KYMTSTEVRN HLRRLFVKEN VVLSRLYAHK RGKPASADMF
FLQNIAVPPT RFRPASKMGD EVHENIQNEL LTRILQSSIQ IASLSKDSTV EVNPDEKEGL
ERRSRAFELL INAFVQLQHD VNSLIDSNRN PSSGGQSRTV PPGIKQILEK KEGLFRKHMM
GKRVNYAARS VISPDPNIET NEIGVPPVFA TKLTYPEPVT LYNFNEMRNA VINGPHKWPG
ASHIQNEDGT LISLMPLTIE QRTALANQLL TPQSNLISSP YSYSRLINTN KKVYRHVRNG
DMLILNRQPT LHKPSMMAHK ARILPGEKTI RMHYANCNSY NADFDGDEMN MHFPQSTNAR
SEAQFIANTD SQYLVPTSGD PLRGLIQDHV VMGVWLTCKD TFYTRDEYQQ LLFQALKPDE
TGMYGRIKTL PPAIQRPGIY WTGKQIISSV LLNLKPSDRP GLNLKSKAKV PGKYWSPDSE
EGSVLFDDGE LLCGILDKSS FGASAFGLVH SVHELYGPDI AGRLLSVLSR LFTAYAQMRG
FTCRMDDLRL DEQGDNWRRQ LLENGKSFGL EAASEYVGLS TDSPIALLNA NLEEVYRDDE
KLQGLDAAMK GKMNGLTSSI INKCIPDGLL TKFPYNHMQT MTVSGAKGSN VNVSQISCLL
GQQELEGRRV PLMVSGKSLP SFVPYETSAK SGGFIASRFL TGIAPQEYYF HCMAGREGLI
DTAVKTSRSG YLQRCLMKHL EGLCVQYDHT VRDSDGSIVQ FHYGEDSLDV TKQKHLTQFE
FSAKNYKSLI QKYKVKSVLS AVDSETASSY AKKALKKPYK YDPVLDKYPP SRYLGSVSEK
FQRAVDEYTQ KNPDKLIASK KESKLDDSLL NESKFKALMQ LRYQQSLVDP GESVGVLASQ
SIGEPSTQMT LNTFHFAGFG AKNVTLGIPR LREIIMTASA NIQTPTMTLR LNDGVSDKRA
SAFCKEVNKL VLSEVVRQVR VTEKISGQGS DEQSKTYAIR LDLYSRDEYQ DEYGVLQEEI
ESTFSNRFLK ILNRIIKSYL AKSKQRKSGG KDDTVPEVGQ ALKPLEDIDE APIEGRAQEA
LEDEDNDATN EKMVSRSKQH ASYEGPDEAD KVALRQLKGS NKVEDVNMDE EEDEGFKSDE
SVSDFKERKL LEKQNTVSIS ERRELQLKTA KEILSNCKHL DFDYVNGEWA TVELVFPINT
EKLLMVSLVE KACSETVIHE IPGITRCFSK PPDSALDTVP KVITEGVNLK AIWEFYNEIS
MNDIYTNDIA AILRIYGVEA ARNAIVHEVS SVFGVYGIAV DPRHLSLIAD YMTFEGGYKA
FNRMGIEYNT SPFAKMSFET TCHFLTEAAL RGDVDDLSNP SSRLVVGRVG NFGTGSFDIF
TPVVDSPAN
