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Protein

RNA polymerase II subunit A C-terminal domain phosphatase SSU72

Gene

SSU72

Organism
Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Protein phosphatase
Biological processmRNA processing

Names & Taxonomyi

Protein namesi
Recommended name:
RNA polymerase II subunit A C-terminal domain phosphatase SSU72 (EC:3.1.3.16)
Short name:
CTD phosphatase SSU72
Alternative name(s):
Suppressor of SUA7 protein 2 homolog
Gene namesi
Name:SSU72
Ordered Locus Names:YALI0F18194g
OrganismiYarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
Taxonomic identifieri284591 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDipodascaceaeYarrowia
Proteomesi
  • UP000001300 Componenti: Chromosome F

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

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002556131 – 193RNA polymerase II subunit A C-terminal domain phosphatase SSU72Add BLAST193

Proteomic databases

PRIDEiQ6C195

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi4952.XP_505567.1

Structurei

3D structure databases

ProteinModelPortaliQ6C195
SMRiQ6C195
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SSU72 phosphatase family.Curated

Phylogenomic databases

HOGENOMiHOG000183445
InParanoidiQ6C195
KOiK15544
OMAiPNCYEFG
OrthoDBiEOG092C4UKX

Family and domain databases

InterProiView protein in InterPro
IPR036196 Ptyr_pPase_sf
IPR006811 RNA_pol_II_suA
PANTHERiPTHR20383 PTHR20383, 1 hit
PfamiView protein in Pfam
PF04722 Ssu72, 1 hit
SUPFAMiSSF52788 SSF52788, 1 hit

Sequencei

Sequence statusi: Complete.

Q6C195-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTELKMCTVC ASNQNRSMEA HKVLKEAGFD VESYGTGSAV RLPGPAYDKP
60 70 80 90 100
NIYAFGTPYD DIYNELSAQD ERLYTANGLL TMLDRNRKIK TAPERWVEHK
110 120 130 140 150
NVFDVVFTCE ERCFEAVCDD LMDRGEKLQR PVHVINVDIR DNHEDSVIGA
160 170 180 190
QGILKLARSL ADSKDLDAQI MGIMDSWQEQ HPKLPLMHAV GYF
Length:193
Mass (Da):21,900
Last modified:August 16, 2004 - v1
Checksum:iB670E9811714D5B0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR382132 Genomic DNA Translation: CAG78376.1
RefSeqiXP_505567.1, XM_505567.1

Genome annotation databases

EnsemblFungiiCAG78376; CAG78376; YALI0_F18194g
GeneIDi2908669
KEGGiyli:YALI0F18194g

Similar proteinsi

Entry informationi

Entry nameiSSU72_YARLI
AccessioniPrimary (citable) accession number: Q6C195
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: August 16, 2004
Last modified: May 23, 2018
This is version 72 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

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health