ID   SSU72_CHAGB             Reviewed;         257 AA.
AC   Q2HFZ9;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 64.
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; ORFNames=CHGG_00855;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
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; CH408029; EAQ92620.1; -; Genomic_DNA.
DR   RefSeq; XP_001220076.1; XM_001220075.1.
DR   AlphaFoldDB; Q2HFZ9; -.
DR   SMR; Q2HFZ9; -.
DR   STRING; 38033.XP_001220076.1; -.
DR   EnsemblFungi; EAQ92620; EAQ92620; CHGG_00855.
DR   GeneID; 4388085; -.
DR   eggNOG; KOG2424; Eukaryota.
DR   HOGENOM; CLU_062463_0_0_1; -.
DR   InParanoid; Q2HFZ9; -.
DR   OMA; NMLGRNR; -.
DR   OrthoDB; 1304061at2759; -.
DR   Proteomes; UP000001056; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
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..257
FT                   /note="RNA polymerase II subunit A C-terminal domain
FT                   phosphatase SSU72"
FT                   /id="PRO_0000255606"
SQ   SEQUENCE   257 AA;  28393 MW;  C629C0EEBBDCD527 CRC64;
     METANGNAGS AATAQNGQQE DASGFKLKFC TVCASNQNRS MEGHLRLAQA NYPVISFGTG
     SLVRLPGPTI TQPNVYKFNE TSYDSIYREL EAKDPRLYRA NGLLNMLGRN RVIKWGPERW
     QDWQVGMPRV KHEKDQGSIG MEAGVPDIVI TCEERCWDAV VDDLLNRGSP LNRPVHVINI
     DIKDNHQDAS IGGGAMVDLA DSLNRAAMEE RDKVGAAVFD AGGAASRASF DERVPEVLGE
     WQERWPGLPS TWTLSWF