ID Q9PT70_XENLA Unreviewed; 867 AA. AC Q9PT70; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 79. DE RecName: Full=RNA polymerase II subunit A C-terminal domain phosphatase {ECO:0000256|RuleBase:RU366066}; DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU366066}; GN Name=fcp1 {ECO:0000313|EMBL:CAB65510.1}; 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 {ECO:0000313|EMBL:CAB65510.1}; RN [1] {ECO:0000313|EMBL:CAB65510.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Ovary {ECO:0000313|EMBL:CAB65510.1}; RA Golini E., Marazziti D., Matteoni R., Tocchini-Valentini G.P.; RT "Molecular cloning of the Xenopus laevis FCP1 serine phosphatase cDNA."; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: This promotes the activity of RNA polymerase II. CC {ECO:0000256|RuleBase:RU366066}. 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 Evidence={ECO:0000256|ARBA:ARBA00001512, CC ECO:0000256|RuleBase:RU366066}; 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 Evidence={ECO:0000256|ARBA:ARBA00001482, CC ECO:0000256|RuleBase:RU366066}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123, CC ECO:0000256|RuleBase:RU366066}. 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; AJ132385; CAB65510.1; -; mRNA. DR AlphaFoldDB; Q9PT70; -. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IEA:UniProtKB-UniRule. DR CDD; cd17729; BRCT_CTDP1; 1. DR CDD; cd07521; HAD_FCP1-like; 1. DR Gene3D; 3.40.50.10190; BRCT domain; 1. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1. DR Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 1. DR InterPro; IPR001357; BRCT_dom. DR InterPro; IPR036420; BRCT_dom_sf. DR InterPro; IPR039189; Fcp1. DR InterPro; IPR015388; FCP1_C. DR InterPro; IPR004274; FCP1_dom. DR InterPro; IPR011947; FCP1_euk. DR InterPro; IPR036412; HAD-like_sf. DR InterPro; IPR023214; HAD_sf. DR NCBIfam; TIGR02250; FCP1_euk; 1. DR PANTHER; PTHR23081; RNA POLYMERASE II CTD PHOSPHATASE; 1. DR PANTHER; PTHR23081:SF36; RNA POLYMERASE II SUBUNIT A C-TERMINAL DOMAIN PHOSPHATASE; 1. DR Pfam; PF00533; BRCT; 1. DR Pfam; PF09309; FCP1_C; 1. DR Pfam; PF03031; NIF; 1. DR SMART; SM00292; BRCT; 1. DR SMART; SM00577; CPDc; 1. DR SUPFAM; SSF52113; BRCT domain; 1. DR SUPFAM; SSF56784; HAD-like; 1. DR PROSITE; PS50172; BRCT; 1. DR PROSITE; PS50969; FCP1; 1. PE 2: Evidence at transcript level; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366066}; KW Nucleus {ECO:0000256|RuleBase:RU366066}. FT DOMAIN 59..224 FT /note="FCP1 homology" FT /evidence="ECO:0000259|PROSITE:PS50969" FT DOMAIN 519..618 FT /note="BRCT" FT /evidence="ECO:0000259|PROSITE:PS50172" FT REGION 226..249 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 281..416 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 433..477 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 671..697 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 711..744 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 763..867 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 281..295 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 315..329 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 337..351 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 366..416 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 461..477 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 672..687 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 815..845 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 867 AA; 97438 MW; BB126AB8B6A4F2E1 CRC64; MKGLCAECGQ DLTQLQSKNG KQQVPYSTAT VSMVHSVPEL MVSSEKAEQL GREDQFRLHR NQKLVLMVDL DQTLIHTTEQ HCQHMSRKGI FHFQLGRGEP MLHTRLRPHC KEFLEKIAKL YELHVFTFGS RLYAHTIAGF LDPEKKLFSH RILSRDECID PYSKTGNLRN LFPCGDSMVC IIDDREDVWK FAPNLITVKK MCIFQGTGDI NAPPGSREAQ MKSKVSCSKA SEVTEKSEAS AQDSEHAKDI LVEKHSNGRR KAMKELNGGC TANSELTKKD TECSDELHEH DSTSSHLTDV LNSKKVKSLA DTPPSLEQDE RTNVSIPQPK TGAAKDLDFD LSSDSDSEGE TRKISSPSSA SGSENECKRS WRKSNKKDED CIASQELCTD DDSKKARPEN HSNLERPIFE SKDTLPVEDD EMEVQSASLC DLGNGCTDKK EVETESQNSE QSGITVGESL DQSMEEEDED SEDTDEDDHL IYLEEILVRV HTDYYAKYDR ILKKEVDDVP DIRNIVPELK SKVLENVIIT FSGLHPTNFP IERTREFYHA RALGANISKN LILKPDDSDR VTHLIAARSG TEKVRQAQNC KHLHVVNPEW LWSCLERWEK VEEQLFPLKD DYMKSQRTIS PTTFPDVHSA FQTPLFHPTP IHPKTQPGPE VHLYNPVTGK LIRKGSQGSS QSPYIQAPSP PLTLPVHGEH SSFRVVQPHQ EQLFDDEEPP TANQDEEQSG PSRRKRQPSM SESMPLYTLC KEDLESMDKE VDDILGEGSD DSDSEKKKTV KVKKSQSAAQ GDKLKNPEER TETPSSSSSE KSLSGTRPRG HKAKLEEEEE DAESVSSKES SNEDEEGSSS EADEMAAAIE AELNDFI //