SSU72_KLULA
ID SSU72_KLULA Reviewed; 207 AA.
AC Q6CQ61;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=RNA polymerase II subunit A C-terminal domain phosphatase SSU72;
DE Short=CTD phosphatase SSU72;
DE EC=3.1.3.16;
DE AltName: Full=Suppressor of SUA7 protein 2 homolog;
GN Name=SSU72; OrderedLocusNames=KLLA0D19514g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Processively dephosphorylates Ser-5 of the heptad repeats
CC YSPTSPS in the C-terminal domain of the largest RNA polymerase II
CC subunit (RPB1). {ECO:0000250}.
CC -!- FUNCTION: Component of the cleavage and polyadenylation factor (CPF)
CC complex, which plays a key role in polyadenylation-dependent pre-mRNA
CC 3'-end formation and cooperates with cleavage factors including the
CC CFIA complex and NAB4/CFIB. SSU72 is required for 3'-end formation of
CC snoRNAs (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- SUBUNIT: Component of the cleavage and polyadenylation factor (CPF)
CC complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SSU72 phosphatase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR382124; CAH01024.1; -; Genomic_DNA.
DR RefSeq; XP_453928.1; XM_453928.1.
DR AlphaFoldDB; Q6CQ61; -.
DR SMR; Q6CQ61; -.
DR STRING; 28985.XP_453928.1; -.
DR EnsemblFungi; CAH01024; CAH01024; KLLA0_D19514g.
DR GeneID; 2893209; -.
DR KEGG; kla:KLLA0_D19514g; -.
DR eggNOG; KOG2424; Eukaryota.
DR HOGENOM; CLU_062463_0_1_1; -.
DR InParanoid; Q6CQ61; -.
DR OMA; NMLGRNR; -.
DR Proteomes; UP000000598; Chromosome D.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IEA:EnsemblFungi.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:EnsemblFungi.
DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IEA:EnsemblFungi.
DR GO; GO:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; IEA:EnsemblFungi.
DR GO; GO:0006378; P:mRNA polyadenylation; IEA:EnsemblFungi.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IEA:EnsemblFungi.
DR GO; GO:0032215; P:positive regulation of telomere maintenance via semi-conservative replication; IEA:EnsemblFungi.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IEA:EnsemblFungi.
DR GO; GO:1902801; P:regulation of siRNA-independent facultative heterochromatin assembly; IEA:EnsemblFungi.
DR GO; GO:1904594; P:regulation of termination of RNA polymerase II transcription; IEA:EnsemblFungi.
DR GO; GO:0009302; P:sno(s)RNA transcription; IEA:EnsemblFungi.
DR GO; GO:0030847; P:termination of RNA polymerase II transcription, exosome-dependent; IEA:EnsemblFungi.
DR GO; GO:0030846; P:termination of RNA polymerase II transcription, poly(A)-coupled; IEA:EnsemblFungi.
DR GO; GO:0031564; P:transcription antitermination; IEA:EnsemblFungi.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IEA:EnsemblFungi.
DR GO; GO:0001174; P:transcriptional start site selection at RNA polymerase II promoter; IEA:EnsemblFungi.
DR InterPro; IPR006811; RNA_pol_II_suA.
DR PANTHER; PTHR20383; PTHR20383; 1.
DR Pfam; PF04722; Ssu72; 1.
PE 3: Inferred from homology;
KW Hydrolase; mRNA processing; Nucleus; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..207
FT /note="RNA polymerase II subunit A C-terminal domain
FT phosphatase SSU72"
FT /id="PRO_0000255610"
SQ SEQUENCE 207 AA; 23838 MW; 8E050E3873B90B6E CRC64;
MSESMRNSGL KFCTVCASNN NRSMESHRVL EEAGYDVSSY GTGSAVRLPG LSIDKPNVYS
FGTPYDDIYN DLISQSEDRY KQNGVLEMLD RNRKLKKAPE KWHDGRKVFD FVFTCEERCF
DSVCEDLMNR GGQLNLIAHI INIDIKDDNE NAKIGGRAIL RLADMLRDKV FECEKNGTQF
EDFIMDVFTE WQEKYPKLPL TYSAAYY
