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 10-MAY-2017, entry version 141.
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;
OC Schizosaccharomycetaceae; 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
RT 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.,
RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA Shpakovski G.V., Ussery D., Barrell B.G., 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
RP AND 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
CC of DNA into RNA using the four ribonucleoside triphosphates as
CC substrates. Largest and catalytic core component of RNA polymerase
CC I which synthesizes ribosomal RNA precursors. 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
CC the central active site cleft of Pol I. A bridging helix emanates
CC from RPA1 and crosses the cleft near the catalytic site and is
CC thought to promote translocation of Pol I by acting as a ratchet
CC that moves the RNA-DNA hybrid through the active site by switching
CC from straight to bent conformations at each step of nucleotide
CC addition (By similarity). {ECO:0000250|UniProtKB:P10964}.
CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
CC + RNA(n+1).
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex
CC consisting of at least 13 subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {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 ProteinModelPortal; P15398; -.
DR SMR; P15398; -.
DR BioGrid; 277390; 13.
DR IntAct; P15398; 1.
DR MINT; MINT-4687353; -.
DR iPTMnet; P15398; -.
DR MaxQB; P15398; -.
DR PRIDE; P15398; -.
DR EnsemblFungi; SPBC4C3.05c.1; SPBC4C3.05c.1:pep; SPBC4C3.05c.
DR GeneID; 2540873; -.
DR KEGG; spo:SPBC4C3.05c; -.
DR EuPathDB; FungiDB:SPBC4C3.05c; -.
DR PomBase; SPBC4C3.05c; -.
DR HOGENOM; HOG000205401; -.
DR InParanoid; P15398; -.
DR KO; K02999; -.
DR OMA; IREINHV; -.
DR OrthoDB; EOG092C19ZG; -.
DR PhylomeDB; P15398; -.
DR Reactome; R-SPO-73762; RNA Polymerase I Transcription Initiation.
DR PRO; PR:P15398; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; IDA:PomBase.
DR GO; GO:0005736; C:DNA-directed RNA polymerase I complex; ISO:PomBase.
DR GO; GO:0005730; C:nucleolus; IDA:PomBase.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006360; P:transcription from RNA polymerase I promoter; ISO:PomBase.
DR InterPro; IPR015699; DNA-dir_RNA_pol1_lsu.
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; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR PANTHER; PTHR19376:SF44; PTHR19376:SF44; 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 Complete proteome; DNA-directed RNA polymerase; Magnesium;
KW Metal-binding; Nucleotidyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transferase; Zinc.
FT CHAIN 1 1689 DNA-directed RNA polymerase I subunit
FT rpa1.
FT /FTId=PRO_0000073929.
FT REGION 1005 1017 Bridging helix. {ECO:0000250}.
FT METAL 63 63 Zinc. {ECO:0000250}.
FT METAL 66 66 Zinc. {ECO:0000250}.
FT METAL 73 73 Zinc. {ECO:0000250}.
FT METAL 76 76 Zinc. {ECO:0000250}.
FT METAL 643 643 Magnesium; catalytic. {ECO:0000250}.
FT METAL 645 645 Magnesium; catalytic. {ECO:0000250}.
FT METAL 647 647 Magnesium; catalytic. {ECO:0000250}.
FT MOD_RES 159 159 Phosphoserine.
FT {ECO:0000269|PubMed:18257517}.
FT MOD_RES 161 161 Phosphoserine.
FT {ECO:0000269|PubMed:18257517}.
FT MOD_RES 1438 1438 Phosphoserine.
FT {ECO:0000269|PubMed:18257517}.
FT MOD_RES 1441 1441 Phosphoserine.
FT {ECO:0000269|PubMed:18257517}.
FT CONFLICT 69 69 D -> A (in Ref. 1; CAA32887).
FT {ECO:0000305}.
FT CONFLICT 84 84 I -> S (in Ref. 1; CAA32887).
FT {ECO:0000305}.
FT CONFLICT 704 704 T -> I (in Ref. 1; CAA32887).
FT {ECO:0000305}.
FT CONFLICT 1581 1581 A -> T (in Ref. 1; CAA32887).
FT {ECO:0000305}.
FT CONFLICT 1681 1681 T -> N (in Ref. 1; CAA32887).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 358 697 ismart:RPOLA_N [T]
FT MYHIT 672 848 ipfam:RNA_pol_Rpb1_3 [T]
FT MYHIT 1002 1632 ipfam:RNA_pol_Rpb1_5 [T]
FT MYHIT 9 477 ipfam:RNA_pol_Rpb1_1 [T]
FT MYHIT 908 995 ipfam:RNA_pol_Rpb1_4 [T]
FT MYHIT 481 668 ipfam:RNA_pol_Rpb1_2 [T]
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
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