SSU72_ASHGO
ID SSU72_ASHGO Reviewed; 281 AA.
AC Q75E60;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=ABL190W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016815; AAS50581.1; -; Genomic_DNA.
DR RefSeq; NP_982757.1; NM_208110.1.
DR AlphaFoldDB; Q75E60; -.
DR SMR; Q75E60; -.
DR STRING; 33169.AAS50581; -.
DR EnsemblFungi; AAS50581; AAS50581; AGOS_ABL190W.
DR GeneID; 4618836; -.
DR KEGG; ago:AGOS_ABL190W; -.
DR eggNOG; KOG2424; Eukaryota.
DR HOGENOM; CLU_062463_0_1_1; -.
DR InParanoid; Q75E60; -.
DR OMA; NMLGRNR; -.
DR Proteomes; UP000000591; Chromosome II.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
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:0006369; P:termination of RNA polymerase II transcription; IBA:GO_Central.
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..281
FT /note="RNA polymerase II subunit A C-terminal domain
FT phosphatase SSU72"
FT /id="PRO_0000255602"
SQ SEQUENCE 281 AA; 31588 MW; 3D3D5DBD42239466 CRC64;
MAPKRGSSPA IAGHCSLILS RGLPSVRVTD SNRQKKLIRH LHTFLLYLPA DTSCGYRPEC
GAASFRTRQS SLMVSSEMPN TSTLRLCTVC ASNNNRSMES HRVLKEAGYD VSSYGTGSAV
RLPGLSIDKP NVYPFGTPYN DIYNDLLAQS AERYKSNGLL EMLDRNRRIK KAPEKWHDSQ
KVFDFVFTCE ERCFDSVCED LMNRGGQLNK IVHVINLDIR DDNENAKIGG RAMLELVKAL
NSKMQECDQQ GVPFEDTIMD VVADWQQAHP QLPLLYSPAY Y
