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Protein

DNA-directed RNA polymerases I and III subunit RPAC1

Gene

RPC40

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I (Pol I) and III (Pol III) which synthesize ribosomal RNA precursors and small RNAs, such as 5S rRNA and tRNAs, respectively. RPC40 is part of the polymerase core and may function as a clamp element that moves to open and close the cleft (PubMed:18160037, PubMed:24153182, PubMed:24153184). Plays an important role in targeting retrotransposons Ty integration upstream of pol III-transcribed genes such as tRNA genes, allowing Ty1, Ty2 and Ty4 to proliferate and yet minimizing genetic damage (PubMed:25931562).1 Publication4 Publications

Miscellaneous

Present with 13000 molecules/cell in log phase SD medium.1 Publication

GO - Molecular functioni

  • DNA binding Source: InterPro
  • protein dimerization activity Source: InterPro
  • RNA polymerase I activity Source: UniProtKB

GO - Biological processi

  • ribosome biogenesis Source: UniProtKB-KW
  • termination of RNA polymerase III transcription Source: Reactome
  • transcription by RNA polymerase I Source: UniProtKB
  • transposon integration Source: SGD
  • tRNA transcription by RNA polymerase III Source: SGD

Keywordsi

Biological processRibosome biogenesis, Transcription

Enzyme and pathway databases

BioCyciYEAST:G3O-34250-MONOMER
ReactomeiR-SCE-73762 RNA Polymerase I Transcription Initiation

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-directed RNA polymerases I and III subunit RPAC1Curated
Short name:
RNA polymerases I and III subunit AC1Curated
Alternative name(s):
C37
DNA-directed RNA polymerases I and III 40 kDa polypeptide1 Publication
Short name:
AC401 Publication
Short name:
C40Curated
Gene namesi
Name:RPC401 Publication
Synonyms:RPC5Imported
Ordered Locus Names:YPR110CImported
ORF Names:P8283.18
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPR110C
SGDiS000006314 RPC40

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

DNA-directed RNA polymerase, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001327422 – 335DNA-directed RNA polymerases I and III subunit RPAC1Add BLAST334

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei17PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP07703
PaxDbiP07703
PRIDEiP07703

PTM databases

iPTMnetiP07703

Interactioni

Subunit structurei

Component of the RNA polymerase I (Pol I) complex consisting of 14 subunits: RPA135, RPA190, RPC40, RPA14, RPB5, RPO26, RPA43, RPB8, RPA12, RPB10, RPC19, RPC10, RPA49 and RPA34 (PubMed:8516295, PubMed:11717393, PubMed:12407181, PubMed:18160037, PubMed:24153184, PubMed:24153182). The complex is composed of a horseshoe-shaped core containing ten subunits (RPA135, RPA190, RPB5, RPO26, RPB8, RPB10, RPC10, RPA12, RPC19 and RPC40) where RPA135 and RPA190 form the DNA-binding cleft. Outside of the core, RPA14 and RPA43 form the stalk that mediates interactions with transcription initiation factors and newly synthesized RNA. Component of the RNA polymerase III (Pol III) complex consisting of at least 17 subunits (PubMed:8516295, PubMed:10384303, PubMed:10393904). Interacts with the RPC19/RPAC2 (PubMed:8516295) and RPC53/RPC4 (PubMed:10393904). Interacts with retrotransposons Ty integrase, targeting Ty1, Ty2 and Ty4 integration upstream of pol III-transcribed genes (PubMed:25931562).1 Publication8 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi36277214 interactors.
DIPiDIP-17N
IntActiP07703 163 interactors.
MINTiP07703
STRINGi4932.YPR110C

Structurei

Secondary structure

1335
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 7Combined sources5
Beta strandi23 – 26Combined sources4
Helixi33 – 39Combined sources7
Beta strandi41 – 46Combined sources6
Beta strandi49 – 58Combined sources10
Helixi61 – 73Combined sources13
Beta strandi77 – 88Combined sources12
Beta strandi90 – 92Combined sources3
Helixi94 – 103Combined sources10
Beta strandi106 – 108Combined sources3
Helixi110 – 112Combined sources3
Beta strandi118 – 120Combined sources3
Helixi122 – 125Combined sources4
Turni128 – 130Combined sources3
Beta strandi132 – 139Combined sources8
Helixi153 – 156Combined sources4
Beta strandi157 – 159Combined sources3
Beta strandi161 – 163Combined sources3
Helixi164 – 166Combined sources3
Beta strandi168 – 170Combined sources3
Helixi175 – 178Combined sources4
Turni179 – 181Combined sources3
Beta strandi185 – 188Combined sources4
Beta strandi192 – 195Combined sources4
Beta strandi201 – 211Combined sources11
Turni213 – 215Combined sources3
Helixi217 – 219Combined sources3
Beta strandi222 – 237Combined sources16
Helixi242 – 248Combined sources7
Turni253 – 255Combined sources3
Beta strandi256 – 258Combined sources3
Turni260 – 262Combined sources3
Beta strandi264 – 268Combined sources5
Helixi270 – 272Combined sources3
Helixi278 – 281Combined sources4
Helixi283 – 286Combined sources4
Beta strandi289 – 304Combined sources16
Beta strandi306 – 308Combined sources3
Helixi310 – 329Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4C2MX-ray2.80C/R1-335[»]
4C3HX-ray3.27C1-335[»]
4C3IX-ray3.0C1-335[»]
4C3JX-ray3.35C1-335[»]
4YM7X-ray5.50AC/BC/CC/DC/EC/FC1-335[»]
5FJ8electron microscopy3.90C1-335[»]
5FJ9electron microscopy4.60C1-335[»]
5FJAelectron microscopy4.65C1-335[»]
5G5Lelectron microscopy4.80C1-335[»]
5LMXelectron microscopy4.90C1-335[»]
5M3Felectron microscopy3.80C1-335[»]
5M3Melectron microscopy4.00C1-335[»]
5M5Welectron microscopy3.80C1-335[»]
5M5Xelectron microscopy4.00C1-335[»]
5M5Yelectron microscopy4.00C1-335[»]
5M64electron microscopy4.60C1-335[»]
5N5Yelectron microscopy7.70C1-335[»]
5N5Zelectron microscopy7.70C1-335[»]
5N60electron microscopy7.70C1-335[»]
5N61electron microscopy3.40C1-335[»]
5OA1electron microscopy4.40C1-335[»]
5W5Yelectron microscopy3.80C1-335[»]
5W64electron microscopy4.20C1-335[»]
5W65electron microscopy4.30C1-335[»]
5W66electron microscopy3.90C1-335[»]
6EU0electron microscopy4.00C1-335[»]
6EU1electron microscopy3.40C1-335[»]
6EU2electron microscopy3.40C1-335[»]
6EU3electron microscopy3.30C1-335[»]
6F40electron microscopy3.70C1-335[»]
6F41electron microscopy4.30C1-335[»]
6F42electron microscopy5.50C1-335[»]
6F44electron microscopy4.20C1-335[»]
ProteinModelPortaliP07703
SMRiP07703
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00550000075060
HOGENOMiHOG000230845
InParanoidiP07703
KOiK03027
OMAiRGKDHAK
OrthoDBiEOG092C3EZ0

Family and domain databases

CDDicd07032 RNAP_I_II_AC40, 1 hit
Gene3Di2.170.120.121 hit
InterProiView protein in InterPro
IPR001514 DNA-dir_RNA_pol_30-40kDasu_CS
IPR011262 DNA-dir_RNA_pol_insert
IPR011263 DNA-dir_RNA_pol_RpoA/D/Rpb3
IPR036603 RBP11-like
IPR033901 RNAPI/II_AC40
IPR036643 RNApol_insert_sf
PANTHERiPTHR11800:SF13 PTHR11800:SF13, 1 hit
PfamiView protein in Pfam
PF01000 RNA_pol_A_bac, 1 hit
PF01193 RNA_pol_L, 1 hit
SMARTiView protein in SMART
SM00662 RPOLD, 1 hit
SUPFAMiSSF55257 SSF55257, 2 hits
SSF56553 SSF56553, 1 hit
PROSITEiView protein in PROSITE
PS00446 RNA_POL_D_30KD, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07703-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNIVGIEYN RVTNTTSTDF PGFSKDAENE WNVEKFKKDF EVNISSLDAR
60 70 80 90 100
EANFDLINID TSIANAFRRI MISEVPSVAA EYVYFFNNTS VIQDEVLAHR
110 120 130 140 150
IGLVPLKVDP DMLTWVDSNL PDDEKFTDEN TIVLSLNVKC TRNPDAPKGS
160 170 180 190 200
TDPKELYNNA HVYARDLKFE PQGRQSTTFA DCPVVPADPD ILLAKLRPGQ
210 220 230 240 250
EISLKAHCIL GIGGDHAKFS PVSTASYRLL PQINILQPIK GESARRFQKC
260 270 280 290 300
FPPGVIGIDE GSDEAYVKDA RKDTVSREVL RYEEFADKVK LGRVRNHFIF
310 320 330
NVESAGAMTP EEIFFKSVRI LKNKAEYLKN CPITQ
Length:335
Mass (Da):37,687
Last modified:April 1, 1988 - v1
Checksum:i76A5D6784403E990
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15499 Genomic DNA Translation: AAA34999.1
U32445 Genomic DNA Translation: AAB68080.1
BK006949 Genomic DNA Translation: DAA11525.1
PIRiA25968
RefSeqiNP_015435.1, NM_001184207.1

Genome annotation databases

EnsemblFungiiYPR110C; YPR110C; YPR110C
GeneIDi856226
KEGGisce:YPR110C

Similar proteinsi

Entry informationi

Entry nameiRPAC1_YEAST
AccessioniPrimary (citable) accession number: P07703
Secondary accession number(s): D6W4A9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: March 28, 2018
This is version 183 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome