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Q4WHY5 (SSU72_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RNA polymerase II subunit A C-terminal domain phosphatase ssu72

Short name=CTD phosphatase ssu72
EC=3.1.3.16
Alternative name(s):
Suppressor of SUA7 protein 2 homolog
Gene names
Name:ssu72
ORF Names:AFUA_2G03760
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length287 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Processively dephosphorylates Ser-5 of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit (rpb1) By similarity.

Component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Ssu72 is required for 3'-end formation of snoRNAs By similarity.

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Subunit structure

Component of the cleavage and polyadenylation factor (CPF) complex By similarity.

Subcellular location

Nucleus By similarity.

Sequence similarities

Belongs to the SSU72 phosphatase family.

Ontologies

Keywords
   Biological processmRNA processing
   Cellular componentNucleus
   Molecular functionHydrolase
Protein phosphatase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionphosphoprotein phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 287287RNA polymerase II subunit A C-terminal domain phosphatase ssu72
PRO_0000255603

Regions

Compositional bias15 – 2814Pro-rich

Sequences

Sequence LengthMass (Da)Tools
Q4WHY5 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 5366D17B18D8BC1D

FASTA28731,559
        10         20         30         40         50         60 
MAHDPRLSSA GTATPNPPPP PPPPPPEPST TGTGETQAAE PSAPAQSSDS FKLKFCTVCA 

        70         80         90        100        110        120 
SNQNRSMEAH LRLSTAPSPF PVISFGTGSL VRLPGPSITQ PNVYNFNTTS YSQMYDELLA 

       130        140        150        160        170        180 
KDERLYRNNG LLNMLDRNRN LKWGPERFQD WVPGMPRVDH VSKGDKGALG TEGGTVDVII 

       190        200        210        220        230        240 
TCEERCWDAV VDDLMNKGAA LNRPVHVFNV DIRDNHEEAL VGGKAILELA TRLNDAATQE 

       250        260        270        280 
RKIHGAEGWE NGNGEARRSF DERVPEILAS WQEKWPNLPA LWTLAWL 

« Hide

References

[1]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAHF01000008 Genomic DNA. Translation: EAL87470.1.
RefSeqXP_749508.1. XM_744415.1.

3D structure databases

ProteinModelPortalQ4WHY5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5085.CADAFUAP00003794.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00003794; CADAFUAP00003794; CADAFUAG00003794.
GeneID3506785.
KEGGafm:AFUA_2G03760.

Phylogenomic databases

eggNOGCOG5211.
HOGENOMHOG000183445.
KOK15544.
OMAWQERWPN.
OrthoDBEOG7GTTG0.

Family and domain databases

InterProIPR006811. RNA_pol_II_suA.
[Graphical view]
PANTHERPTHR20383. PTHR20383. 1 hit.
PfamPF04722. Ssu72. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSSU72_ASPFU
AccessionPrimary (citable) accession number: Q4WHY5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: July 5, 2005
Last modified: April 16, 2014
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families