SSU72_CANGA
ID SSU72_CANGA Reviewed; 204 AA.
AC Q6FMU7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=CAGL0K05071g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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}.
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DR EMBL; CR380957; CAG61408.1; -; Genomic_DNA.
DR RefSeq; XP_448447.1; XM_448447.1.
DR AlphaFoldDB; Q6FMU7; -.
DR SMR; Q6FMU7; -.
DR STRING; 5478.XP_448447.1; -.
DR EnsemblFungi; CAG61408; CAG61408; CAGL0K05071g.
DR GeneID; 2890504; -.
DR KEGG; cgr:CAGL0K05071g; -.
DR CGD; CAL0134219; CAGL0K05071g.
DR VEuPathDB; FungiDB:CAGL0K05071g; -.
DR eggNOG; KOG2424; Eukaryota.
DR HOGENOM; CLU_062463_0_1_1; -.
DR InParanoid; Q6FMU7; -.
DR OMA; NMLGRNR; -.
DR Proteomes; UP000002428; Chromosome K.
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..204
FT /note="RNA polymerase II subunit A C-terminal domain
FT phosphatase SSU72"
FT /id="PRO_0000255605"
SQ SEQUENCE 204 AA; 23379 MW; 4660A18012F677A7 CRC64;
MDQKQALKFC TVCASNNNRS MESHRILQEA GYEVSSYGTG SAVRLPGLSF DKPNVYPFGT
PYNDIYNDLL SQSAERYKAN GLLQMLDRNR RLKKAPEKWQ EGTKTFDFVF TCEERCFDAV
CEDLMNRGGR LNKIVHVINI DIRDDNENAK IGGRAILELA NMLNEKVSEC EQNDTLFEDC
ILDILTKWQE AHPQLPCLYA PSYY
