P15398 · RPA1_SCHPO
- ProteinDNA-directed RNA polymerase I subunit rpa1
- Generpa1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1689 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
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).
Catalytic activity
- a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 63 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 66 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 73 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 76 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 643 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 645 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 647 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | nucleolus | |
Cellular Component | RNA polymerase I complex | |
Molecular Function | DNA binding | |
Molecular Function | DNA-directed 5'-3' RNA polymerase activity | |
Molecular Function | metal ion binding | |
Biological Process | transcription elongation by RNA polymerase I |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDNA-directed RNA polymerase I subunit rpa1
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Taphrinomycotina > Schizosaccharomycetes > Schizosaccharomycetales > Schizosaccharomycetaceae > Schizosaccharomyces
Accessions
- Primary accessionP15398
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000073929 | 1-1689 | DNA-directed RNA polymerase I subunit rpa1 | |||
Sequence: MNIAQPVSSEIKSVKFGIYDVDDVEKISVKQIVNPVLLDNLNHPTNGGLYDLALGPYLKNSVCATCHLDERYCPGHFGHIVLPIPAYHPLFFSQMYNLLRSTCLYCHHFKLSKVKVHLFFCRLKLLDYGLLNESEMVENVSLTEAIIKNSNGTPLEDGSDSEDSGLGHDDIAKDAATLMRIRDEFVAKSIADSRQNAHIDAQLTTLLLHERKKVVRAFYHAISSRKQCDNCQSFSPNFRKEGFAKIFEIPLSGKNLQFMEQTGKIRSDVLRDTSKKHHEDEGYDGDSDSSNESEVEGIDLFEEDPNPLKNKSKSPIAHGAKYMTSTEVRNHLRRLFVKENVVLSRLYAHKRGKPASADMFFLQNIAVPPTRFRPASKMGDEVHENIQNELLTRILQSSIQIASLSKDSTVEVNPDEKEGLERRSRAFELLINAFVQLQHDVNSLIDSNRNPSSGGQSRTVPPGIKQILEKKEGLFRKHMMGKRVNYAARSVISPDPNIETNEIGVPPVFATKLTYPEPVTLYNFNEMRNAVINGPHKWPGASHIQNEDGTLISLMPLTIEQRTALANQLLTPQSNLISSPYSYSRLINTNKKVYRHVRNGDMLILNRQPTLHKPSMMAHKARILPGEKTIRMHYANCNSYNADFDGDEMNMHFPQSTNARSEAQFIANTDSQYLVPTSGDPLRGLIQDHVVMGVWLTCKDTFYTRDEYQQLLFQALKPDETGMYGRIKTLPPAIQRPGIYWTGKQIISSVLLNLKPSDRPGLNLKSKAKVPGKYWSPDSEEGSVLFDDGELLCGILDKSSFGASAFGLVHSVHELYGPDIAGRLLSVLSRLFTAYAQMRGFTCRMDDLRLDEQGDNWRRQLLENGKSFGLEAASEYVGLSTDSPIALLNANLEEVYRDDEKLQGLDAAMKGKMNGLTSSIINKCIPDGLLTKFPYNHMQTMTVSGAKGSNVNVSQISCLLGQQELEGRRVPLMVSGKSLPSFVPYETSAKSGGFIASRFLTGIAPQEYYFHCMAGREGLIDTAVKTSRSGYLQRCLMKHLEGLCVQYDHTVRDSDGSIVQFHYGEDSLDVTKQKHLTQFEFSAKNYKSLIQKYKVKSVLSAVDSETASSYAKKALKKPYKYDPVLDKYPPSRYLGSVSEKFQRAVDEYTQKNPDKLIASKKESKLDDSLLNESKFKALMQLRYQQSLVDPGESVGVLASQSIGEPSTQMTLNTFHFAGFGAKNVTLGIPRLREIIMTASANIQTPTMTLRLNDGVSDKRASAFCKEVNKLVLSEVVRQVRVTEKISGQGSDEQSKTYAIRLDLYSRDEYQDEYGVLQEEIESTFSNRFLKILNRIIKSYLAKSKQRKSGGKDDTVPEVGQALKPLEDIDEAPIEGRAQEALEDEDNDATNEKMVSRSKQHASYEGPDEADKVALRQLKGSNKVEDVNMDEEEDEGFKSDESVSDFKERKLLEKQNTVSISERRELQLKTAKEILSNCKHLDFDYVNGEWATVELVFPINTEKLLMVSLVEKACSETVIHEIPGITRCFSKPPDSALDTVPKVITEGVNLKAIWEFYNEISMNDIYTNDIAAILRIYGVEAARNAIVHEVSSVFGVYGIAVDPRHLSLIADYMTFEGGYKAFNRMGIEYNTSPFAKMSFETTCHFLTEAALRGDVDDLSNPSSRLVVGRVGNFGTGSFDIFTPVVDSPAN | ||||||
Modified residue | 159 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 161 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1438 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1441 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Component of the RNA polymerase I (Pol I) complex consisting of at least 13 subunits.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 269-284 | Basic and acidic residues | ||||
Sequence: VLRDTSKKHHEDEGYD | ||||||
Region | 269-295 | Disordered | ||||
Sequence: VLRDTSKKHHEDEGYDGDSDSSNESEV | ||||||
Region | 1005-1017 | Bridging helix | ||||
Sequence: PQEYYFHCMAGRE | ||||||
Region | 1346-1440 | Disordered | ||||
Sequence: RKSGGKDDTVPEVGQALKPLEDIDEAPIEGRAQEALEDEDNDATNEKMVSRSKQHASYEGPDEADKVALRQLKGSNKVEDVNMDEEEDEGFKSDE | ||||||
Compositional bias | 1363-1425 | Basic and acidic residues | ||||
Sequence: KPLEDIDEAPIEGRAQEALEDEDNDATNEKMVSRSKQHASYEGPDEADKVALRQLKGSNKVED |
Sequence similarities
Belongs to the RNA polymerase beta' chain family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,689
- Mass (Da)189,246
- Last updated1998-07-15 v2
- Checksum2D2D3A2DEC94A497
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 69 | in Ref. 1; CAA32887 | ||||
Sequence: D → A | ||||||
Sequence conflict | 84 | in Ref. 1; CAA32887 | ||||
Sequence: I → S | ||||||
Compositional bias | 269-284 | Basic and acidic residues | ||||
Sequence: VLRDTSKKHHEDEGYD | ||||||
Sequence conflict | 704 | in Ref. 1; CAA32887 | ||||
Sequence: T → I | ||||||
Compositional bias | 1363-1425 | Basic and acidic residues | ||||
Sequence: KPLEDIDEAPIEGRAQEALEDEDNDATNEKMVSRSKQHASYEGPDEADKVALRQLKGSNKVED | ||||||
Sequence conflict | 1581 | in Ref. 1; CAA32887 | ||||
Sequence: A → T | ||||||
Sequence conflict | 1681 | in Ref. 1; CAA32887 | ||||
Sequence: T → N |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X14783 EMBL· GenBank· DDBJ | CAA32887.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M37411 EMBL· GenBank· DDBJ | AAA35326.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CU329671 EMBL· GenBank· DDBJ | CAA16827.1 EMBL· GenBank· DDBJ | Genomic DNA |