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 27-MAR-2024, entry version 66. 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}. 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; 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 AGR; Xenbase:XB-GENE-17334852; -. DR AGR; Xenbase:XB-GENE-5725684; -. DR CTD; 431913; -. DR Xenbase; XB-GENE-5725684; ssu72.L. DR OMA; PNCYEFG; -. DR OrthoDB; 63608at2759; -. DR Proteomes; UP000186698; Chromosome 7L. DR Proteomes; UP000186698; Chromosome 7S. DR Bgee; 431913; Expressed in blastula and 19 other cell types or 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 Gene3D; 3.40.50.2300; -; 2. DR InterPro; IPR006811; RNA_pol_II_suA. DR PANTHER; PTHR20383; RNA POLYMERASE II SUBUNIT A C-TERMINAL DOMAIN PHOSPHATASE; 1. DR PANTHER; PTHR20383:SF9; RNA POLYMERASE II SUBUNIT A C-TERMINAL DOMAIN PHOSPHATASE SSU72; 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 //