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SSU72_CRYNJ
ID   SSU72_CRYNJ             Reviewed;         187 AA.
AC   P0CR76; Q55TK4; Q5KIT2;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 44.
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=CND01850;
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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; AE017344; AAW42937.1; -; Genomic_DNA.
DR   RefSeq; XP_570244.1; XM_570244.1.
DR   AlphaFoldDB; P0CR76; -.
DR   SMR; P0CR76; -.
DR   STRING; 5207.AAW42937; -.
DR   PaxDb; P0CR76; -.
DR   eggNOG; KOG2424; Eukaryota.
DR   HOGENOM; CLU_062463_2_1_1; -.
DR   InParanoid; P0CR76; -.
DR   OMA; PNCYEFG; -.
DR   OrthoDB; 1174597at2759; -.
DR   Proteomes; UP000002149; Chromosome 4.
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: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: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   3: Inferred from homology;
KW   Hydrolase; mRNA processing; Nucleus; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..187
FT                   /note="RNA polymerase II subunit A C-terminal domain
FT                   phosphatase SSU72"
FT                   /id="PRO_0000255607"
SQ   SEQUENCE   187 AA;  21310 MW;  B9175977D9B09F89 CRC64;
     MCHKVEEDRY FVWFVRAITK NSFRVVSAGT GSAVRLPGPA IDKPNVYRFG TPYDDIYRDL
     ESQDPQLYTR NGILPMLDRN RKVKKAPEKW QELKSVLADV VITCEERCYD AVCDDLLTRS
     GEYNRPIHII NIEIKDNPEE AHIAGQSILE LARAIEASDD LDSDIDAILN AHGDKHPHTL
     LHTVGFY
 
 
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