Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

DNA-directed RNA polymerase I subunit rpa1

Gene

rpa1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Forms the polymerase active center together with the second largest subunit. A single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol I. A bridging helix emanates from RPA1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol I by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition (By similarity).By similarity

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi63 – 631ZincBy similarity
Metal bindingi66 – 661ZincBy similarity
Metal bindingi73 – 731ZincBy similarity
Metal bindingi76 – 761ZincBy similarity
Metal bindingi643 – 6431Magnesium; catalyticBy similarity
Metal bindingi645 – 6451Magnesium; catalyticBy similarity
Metal bindingi647 – 6471Magnesium; catalyticBy similarity

GO - Molecular functioni

GO - Biological processi

  • mRNA export from nucleus Source: PomBase
  • transcription from RNA polymerase I promoter Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Transcription

Keywords - Ligandi

Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-SPO-73762. RNA Polymerase I Transcription Initiation.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-directed RNA polymerase I subunit rpa1 (EC:2.7.7.6)
Alternative name(s):
DNA-directed RNA polymerase I 190 kDa polypeptide
DNA-directed RNA polymerase I largest subunit
Gene namesi
Name:rpa1
Synonyms:nuc1
ORF Names:SPBC4C3.05c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC4C3.05c.
PomBaseiSPBC4C3.05c.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
  • DNA-directed RNA polymerase I complex Source: PomBase
  • nucleolus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

DNA-directed RNA polymerase, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16891689DNA-directed RNA polymerase I subunit rpa1PRO_0000073929Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei159 – 1591Phosphoserine1 Publication
Modified residuei161 – 1611Phosphoserine1 Publication
Modified residuei1438 – 14381Phosphoserine1 Publication
Modified residuei1441 – 14411Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP15398.

PTM databases

iPTMnetiP15398.

Interactioni

Subunit structurei

Component of the RNA polymerase I (Pol I) complex consisting of at least 13 subunits.By similarity

Protein-protein interaction databases

BioGridi277390. 13 interactions.
IntActiP15398. 1 interaction.
MINTiMINT-4687353.

Structurei

3D structure databases

ProteinModelPortaliP15398.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1005 – 101713Bridging helixBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the RNA polymerase beta' chain family.Curated

Phylogenomic databases

HOGENOMiHOG000205401.
InParanoidiP15398.
KOiK02999.
OMAiMGSYGRC.
OrthoDBiEOG72C57M.
PhylomeDBiP15398.

Family and domain databases

InterProiIPR015699. DNA-dir_RNA_pol1_lsu.
IPR000722. RNA_pol_asu.
IPR006592. RNA_pol_N.
IPR007080. RNA_pol_Rpb1_1.
IPR007066. RNA_pol_Rpb1_3.
IPR007083. RNA_pol_Rpb1_4.
IPR007081. RNA_pol_Rpb1_5.
[Graphical view]
PANTHERiPTHR19376:SF11. PTHR19376:SF11. 3 hits.
PfamiPF04997. RNA_pol_Rpb1_1. 1 hit.
PF00623. RNA_pol_Rpb1_2. 1 hit.
PF04983. RNA_pol_Rpb1_3. 1 hit.
PF05000. RNA_pol_Rpb1_4. 1 hit.
PF04998. RNA_pol_Rpb1_5. 1 hit.
[Graphical view]
SMARTiSM00663. RPOLA_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P15398-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNIAQPVSSE IKSVKFGIYD VDDVEKISVK QIVNPVLLDN LNHPTNGGLY
60 70 80 90 100
DLALGPYLKN SVCATCHLDE RYCPGHFGHI VLPIPAYHPL FFSQMYNLLR
110 120 130 140 150
STCLYCHHFK LSKVKVHLFF CRLKLLDYGL LNESEMVENV SLTEAIIKNS
160 170 180 190 200
NGTPLEDGSD SEDSGLGHDD IAKDAATLMR IRDEFVAKSI ADSRQNAHID
210 220 230 240 250
AQLTTLLLHE RKKVVRAFYH AISSRKQCDN CQSFSPNFRK EGFAKIFEIP
260 270 280 290 300
LSGKNLQFME QTGKIRSDVL RDTSKKHHED EGYDGDSDSS NESEVEGIDL
310 320 330 340 350
FEEDPNPLKN KSKSPIAHGA KYMTSTEVRN HLRRLFVKEN VVLSRLYAHK
360 370 380 390 400
RGKPASADMF FLQNIAVPPT RFRPASKMGD EVHENIQNEL LTRILQSSIQ
410 420 430 440 450
IASLSKDSTV EVNPDEKEGL ERRSRAFELL INAFVQLQHD VNSLIDSNRN
460 470 480 490 500
PSSGGQSRTV PPGIKQILEK KEGLFRKHMM GKRVNYAARS VISPDPNIET
510 520 530 540 550
NEIGVPPVFA TKLTYPEPVT LYNFNEMRNA VINGPHKWPG ASHIQNEDGT
560 570 580 590 600
LISLMPLTIE QRTALANQLL TPQSNLISSP YSYSRLINTN KKVYRHVRNG
610 620 630 640 650
DMLILNRQPT LHKPSMMAHK ARILPGEKTI RMHYANCNSY NADFDGDEMN
660 670 680 690 700
MHFPQSTNAR SEAQFIANTD SQYLVPTSGD PLRGLIQDHV VMGVWLTCKD
710 720 730 740 750
TFYTRDEYQQ LLFQALKPDE TGMYGRIKTL PPAIQRPGIY WTGKQIISSV
760 770 780 790 800
LLNLKPSDRP GLNLKSKAKV PGKYWSPDSE EGSVLFDDGE LLCGILDKSS
810 820 830 840 850
FGASAFGLVH SVHELYGPDI AGRLLSVLSR LFTAYAQMRG FTCRMDDLRL
860 870 880 890 900
DEQGDNWRRQ LLENGKSFGL EAASEYVGLS TDSPIALLNA NLEEVYRDDE
910 920 930 940 950
KLQGLDAAMK GKMNGLTSSI INKCIPDGLL TKFPYNHMQT MTVSGAKGSN
960 970 980 990 1000
VNVSQISCLL GQQELEGRRV PLMVSGKSLP SFVPYETSAK SGGFIASRFL
1010 1020 1030 1040 1050
TGIAPQEYYF HCMAGREGLI DTAVKTSRSG YLQRCLMKHL EGLCVQYDHT
1060 1070 1080 1090 1100
VRDSDGSIVQ FHYGEDSLDV TKQKHLTQFE FSAKNYKSLI QKYKVKSVLS
1110 1120 1130 1140 1150
AVDSETASSY AKKALKKPYK YDPVLDKYPP SRYLGSVSEK FQRAVDEYTQ
1160 1170 1180 1190 1200
KNPDKLIASK KESKLDDSLL NESKFKALMQ LRYQQSLVDP GESVGVLASQ
1210 1220 1230 1240 1250
SIGEPSTQMT LNTFHFAGFG AKNVTLGIPR LREIIMTASA NIQTPTMTLR
1260 1270 1280 1290 1300
LNDGVSDKRA SAFCKEVNKL VLSEVVRQVR VTEKISGQGS DEQSKTYAIR
1310 1320 1330 1340 1350
LDLYSRDEYQ DEYGVLQEEI ESTFSNRFLK ILNRIIKSYL AKSKQRKSGG
1360 1370 1380 1390 1400
KDDTVPEVGQ ALKPLEDIDE APIEGRAQEA LEDEDNDATN EKMVSRSKQH
1410 1420 1430 1440 1450
ASYEGPDEAD KVALRQLKGS NKVEDVNMDE EEDEGFKSDE SVSDFKERKL
1460 1470 1480 1490 1500
LEKQNTVSIS ERRELQLKTA KEILSNCKHL DFDYVNGEWA TVELVFPINT
1510 1520 1530 1540 1550
EKLLMVSLVE KACSETVIHE IPGITRCFSK PPDSALDTVP KVITEGVNLK
1560 1570 1580 1590 1600
AIWEFYNEIS MNDIYTNDIA AILRIYGVEA ARNAIVHEVS SVFGVYGIAV
1610 1620 1630 1640 1650
DPRHLSLIAD YMTFEGGYKA FNRMGIEYNT SPFAKMSFET TCHFLTEAAL
1660 1670 1680
RGDVDDLSNP SSRLVVGRVG NFGTGSFDIF TPVVDSPAN
Length:1,689
Mass (Da):189,246
Last modified:July 15, 1998 - v2
Checksum:i2D2D3A2DEC94A497
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 691D → A in CAA32887 (PubMed:2537310).Curated
Sequence conflicti84 – 841I → S in CAA32887 (PubMed:2537310).Curated
Sequence conflicti704 – 7041T → I in CAA32887 (PubMed:2537310).Curated
Sequence conflicti1581 – 15811A → T in CAA32887 (PubMed:2537310).Curated
Sequence conflicti1681 – 16811T → N in CAA32887 (PubMed:2537310).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14783 Genomic DNA. Translation: CAA32887.1.
M37411 Genomic DNA. Translation: AAA35326.1.
CU329671 Genomic DNA. Translation: CAA16827.1.
PIRiJS0080.
RefSeqiNP_596300.1. NM_001022221.2.

Genome annotation databases

EnsemblFungiiSPBC4C3.05c.1; SPBC4C3.05c.1:pep; SPBC4C3.05c.
GeneIDi2540873.
KEGGispo:SPBC4C3.05c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14783 Genomic DNA. Translation: CAA32887.1.
M37411 Genomic DNA. Translation: AAA35326.1.
CU329671 Genomic DNA. Translation: CAA16827.1.
PIRiJS0080.
RefSeqiNP_596300.1. NM_001022221.2.

3D structure databases

ProteinModelPortaliP15398.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277390. 13 interactions.
IntActiP15398. 1 interaction.
MINTiMINT-4687353.

PTM databases

iPTMnetiP15398.

Proteomic databases

MaxQBiP15398.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC4C3.05c.1; SPBC4C3.05c.1:pep; SPBC4C3.05c.
GeneIDi2540873.
KEGGispo:SPBC4C3.05c.

Organism-specific databases

EuPathDBiFungiDB:SPBC4C3.05c.
PomBaseiSPBC4C3.05c.

Phylogenomic databases

HOGENOMiHOG000205401.
InParanoidiP15398.
KOiK02999.
OMAiMGSYGRC.
OrthoDBiEOG72C57M.
PhylomeDBiP15398.

Enzyme and pathway databases

ReactomeiR-SPO-73762. RNA Polymerase I Transcription Initiation.

Miscellaneous databases

NextBioi20801989.
PROiP15398.

Family and domain databases

InterProiIPR015699. DNA-dir_RNA_pol1_lsu.
IPR000722. RNA_pol_asu.
IPR006592. RNA_pol_N.
IPR007080. RNA_pol_Rpb1_1.
IPR007066. RNA_pol_Rpb1_3.
IPR007083. RNA_pol_Rpb1_4.
IPR007081. RNA_pol_Rpb1_5.
[Graphical view]
PANTHERiPTHR19376:SF11. PTHR19376:SF11. 3 hits.
PfamiPF04997. RNA_pol_Rpb1_1. 1 hit.
PF00623. RNA_pol_Rpb1_2. 1 hit.
PF04983. RNA_pol_Rpb1_3. 1 hit.
PF05000. RNA_pol_Rpb1_4. 1 hit.
PF04998. RNA_pol_Rpb1_5. 1 hit.
[Graphical view]
SMARTiSM00663. RPOLA_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Essential roles of the RNA polymerase I largest subunit and DNA topoisomerases in the formation of fission yeast nucleolus."
    Hirano T., Konoha G., Toda T., Yanagida M.
    J. Cell Biol. 108:243-253(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
  2. "Cloning and sequence determination of the gene encoding the largest subunit of the fission yeast Schizosaccharomyces pombe RNA polymerase I."
    Yamagishi M., Nomura M.
    Gene 74:503-515(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 972 / HM123.
  3. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159; SER-161; SER-1438 AND SER-1441, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiRPA1_SCHPO
AccessioniPrimary (citable) accession number: P15398
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: July 15, 1998
Last modified: January 20, 2016
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.