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P39081 (PCF11_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein PCF11
Alternative name(s):
protein 1 of CF I
Gene names
Name:PCF11
Ordered Locus Names:YDR228C
ORF Names:YD9934.13C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length626 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 cleavage factor NAB4/CFIB and the cleavage and polyadenylation factor (CPF) complex. Independently involved in RNA polymerase II transcript termination. Binds RNA. Seems to bridge RNA polymerase II and the native transcript and may be involved in dismantling the RNA polymerase II elongation complex. Ref.5 Ref.10

Subunit structure

Component of the CFIA complex, which is composed of RNA14, RNA15, PCF11 and CLP1. Interacts with RNA14, RNA15 and RTT103. Interacts directly with the phosphorylated CTD domain of RPB1/RNA polymerase II. Ref.4 Ref.6 Ref.7 Ref.9

Subcellular location

Nucleus Potential.

Miscellaneous

Present with 2800 molecules/cell in log phase SD medium.

Sequence similarities

Contains 1 CID domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 626626Protein PCF11
PRO_0000058247

Regions

Domain4 – 139136CID
Region1 – 130130Interaction with RBP1 CTD (CID)
Compositional bias234 – 25320Poly-Gln
Compositional bias470 – 4734Poly-Thr

Experimental info

Mutagenesis661A → D: Loss of interaction with RBP1 CTD. Ref.7
Mutagenesis68 – 703DSI → AAA: Loss of interaction with RBP1 CTD. Ref.7
Sequence conflict286 – 2883NSL → ILS in AAC33145. Ref.3
Sequence conflict5151I → V in AAC33145. Ref.3

Secondary structure

........................ 626
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P39081 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: 66F91BA9577E82F1

FASTA62671,898
        10         20         30         40         50         60 
MDHDTEVIVK DFNSILEELT FNSRPIITTL TKLAEENISC AQYFVDAIES RIEKCMPKQK 

        70         80         90        100        110        120 
LYAFYALDSI CKNVGSPYTI YFSRNLFNLY KRTYLLVDNT TRTKLINMFK LWLNPNDTGL 

       130        140        150        160        170        180 
PLFEGSALEK IEQFLIKASA LHQKNLQAML PTPTVPLLLR DIDKLTCLTS ERLKNQPNDE 

       190        200        210        220        230        240 
KLKMKLLVLS QLKQELKREK LTLNALKQVQ MQLRQVFSQD QQVLQERMRY HELQQQQQQQ 

       250        260        270        280        290        300 
QQQQQQQQQQ QQQYHETKDM VGSYTQNSNS AIPLFGNNSD TTNQQNSLSS SLFGNISGVE 

       310        320        330        340        350        360 
SFQEIEKKKS LNKINNLYAS LKAEGLIYTP PKESIVTLYK KLNGHSNYSL DSHEKQLMKN 

       370        380        390        400        410        420 
LPKIPLLNDI LSDCKAYFAT VNIDVLNNPS LQLSEQTLLQ ENPIVQNNLI HLLYRSKPNK 

       430        440        450        460        470        480 
CSVCGKRFGN SESEKLLQNE HLDWHFRINT RIKGSQNTAN TGISNSNLNT TTTRKNIQSR 

       490        500        510        520        530        540 
NWYLSDSQWA AFKDDEITST KHKNDYTDPH ANKNIDKSAL NIHADENDEG SVDNTLGSDR 

       550        560        570        580        590        600 
SNELEIRGKY VVVPETSQDM AFKCPICKET VTGVYDEESG EWVWKNTIEV NGKYFHSTCY 

       610        620 
HETSQNSSKS NSGKVGLDDL KKLVTK 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Insertion site specificity of the transposon Tn3."
Davies C.J., Hutchison C.A. III
Nucleic Acids Res. 23:507-514(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 286-626.
[4]"PCF11 encodes a third protein component of yeast cleavage and polyadenylation factor I."
Amrani N., Minet M., Wyers F., Dufour M.-E., Aggerbeck L.P., Lacroute F.
Mol. Cell. Biol. 17:1102-1109(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE CFIA COMPLEX, INTERACTION WITH RNA14 AND RNA15.
[5]"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.
[6]"Cleavage/polyadenylation factor IA associates with the carboxyl-terminal domain of RNA polymerase II in Saccharomyces cerevisiae."
Barilla D., Lee B.A., Proudfoot N.J.
Proc. Natl. Acad. Sci. U.S.A. 98:445-450(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RBP1.
[7]"Independent functions of yeast Pcf11p in pre-mRNA 3' end processing and in transcription termination."
Sadowski M., Dichtl B., Huebner W., Keller W.
EMBO J. 22:2167-2177(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RBP1, MUTAGENESIS OF ALA-66 AND 68-ASP--ILE-70.
[8]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]"The yeast Rat1 exonuclease promotes transcription termination by RNA polymerase II."
Kim M., Krogan N.J., Vasiljeva L., Rando O.J., Nedea E., Greenblatt J.F., Buratowski S.
Nature 432:517-522(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RTT103.
[10]"CTD-dependent dismantling of the RNA polymerase II elongation complex by the pre-mRNA 3'-end processing factor, Pcf11."
Zhang Z., Fu J., Gilmour D.S.
Genes Dev. 19:1572-1580(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, RNA-BINDING.
[11]"Recognition of RNA polymerase II carboxy-terminal domain by 3'-RNA-processing factors."
Meinhart A., Cramer P.
Nature 430:223-226(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-140.
[12]"Key features of the interaction between Pcf11 CID and RNA polymerase II CTD."
Noble C.G., Hollingworth D., Martin S.R., Ennis-Adeniran V., Smerdon S.J., Kelly G., Taylor I.A., Ramos A.
Nat. Struct. Mol. Biol. 12:144-151(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-138.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z48612 Genomic DNA. Translation: CAA88508.1.
U13239 Genomic DNA. Translation: AAC33145.1.
BK006938 Genomic DNA. Translation: DAA12070.1.
PIRS59435.
RefSeqNP_010514.3. NM_001180536.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SZ9X-ray2.10A/B/C1-140[»]
1SZAX-ray2.20A/B/C1-140[»]
2BF0X-ray2.30X1-138[»]
2NPIX-ray2.95C/D454-563[»]
4C0BX-ray2.77C/D454-563[»]
4C0HX-ray2.70C/D454-563[»]
4OI4X-ray2.40B/D/U454-563[»]
ProteinModelPortalP39081.
SMRP39081. Positions 2-140, 473-499.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32280. 85 interactions.
DIPDIP-944N.
IntActP39081. 78 interactions.
MINTMINT-389878.
STRING4932.YDR228C.

Proteomic databases

MaxQBP39081.
PaxDbP39081.
PeptideAtlasP39081.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR228C; YDR228C; YDR228C.
GeneID851814.
KEGGsce:YDR228C.

Organism-specific databases

CYGDYDR228c.
SGDS000002636. PCF11.

Phylogenomic databases

eggNOGNOG268273.
GeneTreeENSGT00440000034259.
HOGENOMHOG000115468.
KOK14400.
OMAHADENDE.
OrthoDBEOG76QFSS.

Enzyme and pathway databases

BioCycYEAST:G3O-29807-MONOMER.

Gene expression databases

GenevestigatorP39081.

Family and domain databases

Gene3D1.25.40.90. 1 hit.
InterProIPR021605. CFIA_Pcf11.
IPR006569. CID_dom.
IPR008942. ENTH_VHS.
[Graphical view]
PfamPF11526. CFIA_Pcf11. 1 hit.
[Graphical view]
SMARTSM00582. RPR. 1 hit.
[Graphical view]
SUPFAMSSF48464. SSF48464. 1 hit.
PROSITEPS51391. CID. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP39081.
NextBio969674.
PROP39081.

Entry information

Entry namePCF11_YEAST
AccessionPrimary (citable) accession number: P39081
Secondary accession number(s): D6VSL0, Q04932
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 15, 1998
Last modified: July 9, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references