ID   SSU72_SCHPO             Reviewed;         197 AA.
AC   O42868;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 115.
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=SPAC3G9.04;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   IDENTIFICATION IN THE CPF COMPLEX.
RX   PubMed=14617822; DOI=10.1074/mcp.m300081-mcp200;
RA   Roguev A., Shevchenko A., Schaft D., Thomas H., Stewart A.F.,
RA   Shevchenko A.;
RT   "A comparative analysis of an orthologous proteomic environment in the
RT   yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe.";
RL   Mol. Cell. Proteomics 3:125-132(2004).
RN   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
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, which is composed of cft1, cft2, ysh1, pta1, swd2, pfs2, dis2,
CC       yth1, ssu72, and fip1. {ECO:0000269|PubMed:14617822}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the SSU72 phosphatase family. {ECO:0000305}.
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DR   EMBL; CU329670; CAA15913.1; -; Genomic_DNA.
DR   PIR; T11640; T11640.
DR   RefSeq; NP_594076.1; NM_001019509.2.
DR   AlphaFoldDB; O42868; -.
DR   SMR; O42868; -.
DR   BioGRID; 279872; 183.
DR   STRING; 4896.SPAC3G9.04.1; -.
DR   MaxQB; O42868; -.
DR   PaxDb; O42868; -.
DR   EnsemblFungi; SPAC3G9.04.1; SPAC3G9.04.1:pep; SPAC3G9.04.
DR   GeneID; 2543452; -.
DR   KEGG; spo:SPAC3G9.04; -.
DR   PomBase; SPAC3G9.04; ssu72.
DR   VEuPathDB; FungiDB:SPAC3G9.04; -.
DR   eggNOG; KOG2424; Eukaryota.
DR   HOGENOM; CLU_062463_2_1_1; -.
DR   InParanoid; O42868; -.
DR   OMA; NMLGRNR; -.
DR   PhylomeDB; O42868; -.
DR   PRO; PR:O42868; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0000785; C:chromatin; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IMP:PomBase.
DR   GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IDA:PomBase.
DR   GO; GO:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
DR   GO; GO:0006352; P:DNA-templated transcription, initiation; ISO:PomBase.
DR   GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR   GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IMP:PomBase.
DR   GO; GO:0032215; P:positive regulation of telomere maintenance via semi-conservative replication; IMP:PomBase.
DR   GO; GO:1902801; P:regulation of siRNA-independent facultative heterochromatin assembly; IMP:PomBase.
DR   GO; GO:1904594; P:regulation of termination of RNA polymerase II transcription; IMP:PomBase.
DR   GO; GO:0023052; P:signaling; NAS:PomBase.
DR   GO; GO:0006369; P:termination of RNA polymerase II transcription; IBA:GO_Central.
DR   InterPro; IPR006811; RNA_pol_II_suA.
DR   PANTHER; PTHR20383; PTHR20383; 1.
DR   Pfam; PF04722; Ssu72; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase; mRNA processing; Nucleus; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..197
FT                   /note="RNA polymerase II subunit A C-terminal domain
FT                   phosphatase ssu72"
FT                   /id="PRO_0000255612"
SQ   SEQUENCE   197 AA;  22596 MW;  04BE20BEF08D76BA CRC64;
     MAPKTNLQIS VICASNQNRS MEAHNVLKNA GYQVDSFGTG SAVRLPGPSI DKPNIYQFGY
     PYDEIYKELE AQDSRLYTAN GLLKMLDRNR RIKRAPCRWQ DQDSIYNIVI TCEERCYDAI
     CEDLYRRGET LNRPVYLINV DIKDNHEEAS VGGKAILDLV NKLTEAQDKL EELFPSIMAD
     FQSNHPKLPV LYTIHFF