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P25299

- RNA15_YEAST

UniProt

P25299 - RNA15_YEAST

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Protein
mRNA 3'-end-processing protein RNA15
Gene
RNA15, YGL044C
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

RNA-binding component of the cleavage factor IA (CFIA) complex, which is involved in the endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with the cleavage factor NAB4/CFIB and the cleavage and polyadenylation factor (CPF) complex. Binds to A-rich RNA sequence elements.2 Publications

GO - Molecular functioni

  1. mRNA binding Source: SGD
  2. nucleotide binding Source: InterPro
  3. protein binding Source: IntAct
  4. protein heterodimerization activity Source: SGD
Complete GO annotation...

GO - Biological processi

  1. mRNA cleavage Source: SGD
  2. mRNA polyadenylation Source: SGD
Complete GO annotation...

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30555-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
mRNA 3'-end-processing protein RNA15
Gene namesi
Name:RNA15
Ordered Locus Names:YGL044C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

CYGDiYGL044c.
SGDiS000003012. RNA15.

Subcellular locationi

GO - Cellular componenti

  1. mRNA cleavage factor complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 296296mRNA 3'-end-processing protein RNA15
PRO_0000081807Add
BLAST

Proteomic databases

MaxQBiP25299.
PaxDbiP25299.
PeptideAtlasiP25299.

Expressioni

Gene expression databases

GenevestigatoriP25299.

Interactioni

Subunit structurei

Component of the CFIA complex, which is composed of RNA14, RNA15, PCF11 and CLP1. Interacts directly with RNA14. Interacts with polyadenylate-binding protein PAB1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PCF11P390819EBI-15640,EBI-12980
RNA14P252988EBI-15640,EBI-15632
SUB1P540002EBI-15640,EBI-18492

Protein-protein interaction databases

BioGridi33204. 115 interactions.
DIPiDIP-1489N.
IntActiP25299. 11 interactions.
MINTiMINT-389896.
STRINGi4932.YGL044C.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi18 – 247
Helixi31 – 399
Beta strandi44 – 485
Turni53 – 553
Beta strandi60 – 689
Helixi69 – 7911
Beta strandi85 – 873
Beta strandi90 – 934
Helixi99 – 1013
Helixi139 – 1435
Turni156 – 1583
Helixi161 – 17010
Helixi174 – 19017
Helixi192 – 20110
Helixi203 – 21614
Beta strandi217 – 2193
Helixi221 – 2244
Turni225 – 2273

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KM8NMR-B14-97[»]
2L9BNMR-A127-232[»]
2X1AX-ray2.05A16-111[»]
2X1BX-ray1.80A16-111[»]
2X1FX-ray1.60A16-103[»]
ProteinModelPortaliP25299.
SMRiP25299. Positions 16-101, 138-228.

Miscellaneous databases

EvolutionaryTraceiP25299.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 9679RRM
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi104 – 1096Poly-Gln
Compositional biasi111 – 12818Asn-rich
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG246793.
GeneTreeiENSGT00750000117707.
HOGENOMiHOG000247912.
KOiK14407.
OMAiQILDLCS.
OrthoDBiEOG706125.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR026896. CSTF_C.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF14304. CSTF_C. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25299-1 [UniParc]FASTAAdd to Basket

« Hide

MNRQSGVNAG VQNNPPSRVV YLGSIPYDQT EEQILDLCSN VGPVINLKMM    50
FDPQTGRSKG YAFIEFRDLE SSASAVRNLN GYQLGSRFLK CGYSSNSDIS 100
GVSQQQQQQY NNINGNNNNN GNNNNNSNGP DFQNSGNANF LSQKFPELPS 150
GIDVNINMTT PAMMISSELA KKPKEVQLKF LQKFQEWTRA HPEDAVSLLE 200
LCPQLSFVTA ELLLTNGICK VDDLIPLASR PQEEASATNN NSVNEVVDPA 250
VLNKQKELLK QVLQLNDSQI SILPDDERMA IWDLKQKALR GEFGAF 296
Length:296
Mass (Da):32,791
Last modified:May 1, 1992 - v1
Checksum:i10053B8648A71ECB
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M73462 Genomic DNA. Translation: AAA34984.1.
Z72566 Genomic DNA. Translation: CAA96746.1.
BK006941 Genomic DNA. Translation: DAA08056.1.
PIRiB40257.
RefSeqiNP_011471.1. NM_001180909.1.

Genome annotation databases

EnsemblFungiiYGL044C; YGL044C; YGL044C.
GeneIDi852838.
KEGGisce:YGL044C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M73462 Genomic DNA. Translation: AAA34984.1 .
Z72566 Genomic DNA. Translation: CAA96746.1 .
BK006941 Genomic DNA. Translation: DAA08056.1 .
PIRi B40257.
RefSeqi NP_011471.1. NM_001180909.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KM8 NMR - B 14-97 [» ]
2L9B NMR - A 127-232 [» ]
2X1A X-ray 2.05 A 16-111 [» ]
2X1B X-ray 1.80 A 16-111 [» ]
2X1F X-ray 1.60 A 16-103 [» ]
ProteinModelPortali P25299.
SMRi P25299. Positions 16-101, 138-228.
ModBasei Search...

Protein-protein interaction databases

BioGridi 33204. 115 interactions.
DIPi DIP-1489N.
IntActi P25299. 11 interactions.
MINTi MINT-389896.
STRINGi 4932.YGL044C.

Proteomic databases

MaxQBi P25299.
PaxDbi P25299.
PeptideAtlasi P25299.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YGL044C ; YGL044C ; YGL044C .
GeneIDi 852838.
KEGGi sce:YGL044C.

Organism-specific databases

CYGDi YGL044c.
SGDi S000003012. RNA15.

Phylogenomic databases

eggNOGi NOG246793.
GeneTreei ENSGT00750000117707.
HOGENOMi HOG000247912.
KOi K14407.
OMAi QILDLCS.
OrthoDBi EOG706125.

Enzyme and pathway databases

BioCyci YEAST:G3O-30555-MONOMER.

Miscellaneous databases

EvolutionaryTracei P25299.
NextBioi 972414.

Gene expression databases

Genevestigatori P25299.

Family and domain databases

Gene3Di 3.30.70.330. 1 hit.
InterProi IPR026896. CSTF_C.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view ]
Pfami PF14304. CSTF_C. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view ]
SMARTi SM00360. RRM. 1 hit.
[Graphical view ]
PROSITEi PS50102. RRM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mutations in the yeast RNA14 and RNA15 genes result in an abnormal mRNA decay rate; sequence analysis reveals an RNA-binding domain in the RNA15 protein."
    Minvielle-Sebastia L., Winsor B., Bonneaud N., Lacroute F.
    Mol. Cell. Biol. 11:3075-3087(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 28383 / FL100 / VTT C-80102.
  2. "The characterization of two new clusters of duplicated genes suggests a 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes."
    Feuermann M., de Montigny J., Potier S., Souciet J.-L.
    Yeast 13:861-869(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "RNA14 and RNA15 proteins as components of a yeast pre-mRNA 3'-end processing factor."
    Minvielle-Sebastia L., Preker P.J., Keller W.
    Science 266:1702-1705(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Yeast Pab1 interacts with Rna15 and participates in the control of the poly(A) tail length in vitro."
    Amrani N., Minet M., Le Gouar M., Lacroute F., Wyers F.
    Mol. Cell. Biol. 17:3694-3701(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PAB1.
  7. "Five subunits are required for reconstitution of the cleavage and polyadenylation activities of Saccharomyces cerevisiae cleavage factor I."
    Gross S., Moore C.
    Proc. Natl. Acad. Sci. U.S.A. 98:6080-6085(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE CFIA COMPLEX.
  8. "Rna15 interaction with the A-rich yeast polyadenylation signal is an essential step in mRNA 3'-end formation."
    Gross S., Moore C.L.
    Mol. Cell. Biol. 21:8045-8055(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA-BINDING.
  9. "Purification of the Saccharomyces cerevisiae cleavage/polyadenylation factor I. Separation into two components that are required for both cleavage and polyadenylation of mRNA 3' ends."
    Kessler M.M., Zhao J., Moore C.L.
    J. Biol. Chem. 271:27167-27175(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: COMPOSITION OF THE CFIA COMPLEX.
  10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRNA15_YEAST
AccessioniPrimary (citable) accession number: P25299
Secondary accession number(s): D6VU95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: June 11, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 6350 molecules/cell in log phase SD medium.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3

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