ID   SSU72_XENLA             Reviewed;         194 AA.
AC   Q6NRQ7; Q4KLW8;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=RNA polymerase II subunit A C-terminal domain phosphatase SSU72;
DE            Short=CTD phosphatase SSU72;
DE            EC=3.1.3.16;
GN   Name=ssu72;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in the C-terminal domain of RNA polymerase II
CC       dephosphorylation, RNA processing and termination. {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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC       Note=Predominantly in the cytosol. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SSU72 phosphatase family. {ECO:0000305}.
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DR   EMBL; BC070675; AAH70675.1; -; mRNA.
DR   EMBL; BC098966; AAH98966.1; -; mRNA.
DR   RefSeq; NP_001084864.1; NM_001091395.1.
DR   RefSeq; NP_001089572.1; NM_001096103.1.
DR   AlphaFoldDB; Q6NRQ7; -.
DR   SMR; Q6NRQ7; -.
DR   DNASU; 431913; -.
DR   DNASU; 734628; -.
DR   GeneID; 431913; -.
DR   GeneID; 734628; -.
DR   KEGG; xla:431913; -.
DR   KEGG; xla:734628; -.
DR   CTD; 431913; -.
DR   CTD; 734628; -.
DR   Xenbase; XB-GENE-5725684; ssu72.L.
DR   Xenbase; XB-GENE-17334852; ssu72.S.
DR   OMA; PNCYEFG; -.
DR   OrthoDB; 1304061at2759; -.
DR   Proteomes; UP000186698; Chromosome 7L.
DR   Proteomes; UP000186698; Chromosome 7S.
DR   Bgee; 431913; Expressed in blastula and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Hydrolase; mRNA processing; Nucleus;
KW   Protein phosphatase; Reference proteome.
FT   CHAIN           1..194
FT                   /note="RNA polymerase II subunit A C-terminal domain
FT                   phosphatase SSU72"
FT                   /id="PRO_0000330017"
FT   COILED          160..186
FT                   /evidence="ECO:0000255"
FT   CONFLICT        31
FT                   /note="F -> I (in Ref. 1; AAH98966)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        91
FT                   /note="I -> V (in Ref. 1; AAH98966)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        178
FT                   /note="E -> D (in Ref. 1; AAH98966)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   194 AA;  22681 MW;  92B269CB832A2EC6 CRC64;
     MPTAPLRVAV VCSSNQNRSM EAHNILSKRS FNVRSFGTGT HVKLPGPAPD KPNVYDFKTT
     YEQMYSDLLK KDKELYTQNG ILHMLDRNRR IKPRPERFQN CKDYFDLVIT CEERVYDQVV
     EELNSREQET CQPVHVINVD IQDNHEEATL GAFLICELCQ CIQHTEDMEN EIDELLQEFE
     DKSGRTFLHT ICFY