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Q75E60 (SSU72_ASHGO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 59. 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
Ordered Locus Names:ABL190W
OrganismAshbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) [Reference proteome]
Taxonomic identifier284811 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium

Protein attributes

Sequence length281 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 – 281281RNA polymerase II subunit A C-terminal domain phosphatase SSU72
PRO_0000255602

Sequences

Sequence LengthMass (Da)Tools
Q75E60 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 3D3D5DBD42239466

FASTA28131,588
        10         20         30         40         50         60 
MAPKRGSSPA IAGHCSLILS RGLPSVRVTD SNRQKKLIRH LHTFLLYLPA DTSCGYRPEC 

        70         80         90        100        110        120 
GAASFRTRQS SLMVSSEMPN TSTLRLCTVC ASNNNRSMES HRVLKEAGYD VSSYGTGSAV 

       130        140        150        160        170        180 
RLPGLSIDKP NVYPFGTPYN DIYNDLLAQS AERYKSNGLL EMLDRNRRIK KAPEKWHDSQ 

       190        200        210        220        230        240 
KVFDFVFTCE ERCFDSVCED LMNRGGQLNK IVHVINLDIR DDNENAKIGG RAMLELVKAL 

       250        260        270        280 
NSKMQECDQQ GVPFEDTIMD VVADWQQAHP QLPLLYSPAY Y 

« Hide

References

« Hide 'large scale' references
[1]"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
Science 304:304-307(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.
[2]"Genomes of Ashbya fungi isolated from insects reveal four mating-type loci, numerous translocations, lack of transposons, and distinct gene duplications."
Dietrich F.S., Voegeli S., Kuo S., Philippsen P.
G3 (Bethesda) 3:1225-1239(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016815 Genomic DNA. Translation: AAS50581.1.
RefSeqNP_982757.1. NM_208110.1.

3D structure databases

ProteinModelPortalQ75E60.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING33169.AGOS_ABL190W.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiAAS50581; AAS50581; AGOS_ABL190W.
GeneID4618836.
KEGGago:AGOS_ABL190W.

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_ASHGO
AccessionPrimary (citable) accession number: Q75E60
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 59 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