ID SSU72_CRYNB Reviewed; 187 AA. AC P0CR77; Q55TK4; Q5KIT2; DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot. DT 28-JUN-2011, sequence version 1. DT 24-JAN-2024, entry version 40. 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=CNBD4490; OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OS (Filobasidiella neoformans). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes; OC Tremellales; Cryptococcaceae; Cryptococcus; OC Cryptococcus neoformans species complex. OX NCBI_TaxID=283643; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B-3501A; 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}. CC -!- SEQUENCE CAUTION: CC Sequence=EAL21073.1; Type=Erroneous gene model prediction; Evidence={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; AAEY01000021; EAL21073.1; ALT_SEQ; Genomic_DNA. DR RefSeq; XP_775720.1; XM_770627.1. DR AlphaFoldDB; P0CR77; -. DR SMR; P0CR77; -. DR GeneID; 4935838; -. DR KEGG; cnb:CNBD4490; -. DR HOGENOM; CLU_062463_1_0_1; -. DR OrthoDB; 63608at2759; -. 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; -; 1. 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 3: Inferred from homology; KW Hydrolase; mRNA processing; Nucleus; Protein phosphatase. FT CHAIN 1..187 FT /note="RNA polymerase II subunit A C-terminal domain FT phosphatase SSU72" FT /id="PRO_0000410300" 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 //