ID FCP1_SCHPO Reviewed; 723 AA. AC Q9P376; DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 155. DE RecName: Full=RNA polymerase II subunit A C-terminal domain phosphatase; DE EC=3.1.3.16; DE AltName: Full=CTD phosphatase fcp1; GN Name=fcp1; ORFNames=SPAC19B12.05c; OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=284812; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=972 / ATCC 24843; RX PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., RA Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). RN [2] RP FUNCTION, COFACTOR, SUBUNIT, CATALYTIC ACTIVITY, ACTIVE SITE, AND RP MUTAGENESIS OF ASP-170 AND ASP-172. RX PubMed=11934898; DOI=10.1074/jbc.m202056200; RA Hausmann S., Shuman S.; RT "Characterization of the CTD phosphatase Fcp1 from fission yeast. RT Preferential dephosphorylation of serine 2 versus serine 5."; RL J. Biol. Chem. 277:21213-21220(2002). CC -!- FUNCTION: Processively dephosphorylates 'Ser-2' and 'Ser-5' of the CC heptad repeats YSPTSPS in the C-terminal domain of the largest RNA CC polymerase II subunit. This promotes the activity of RNA polymerase II. CC {ECO:0000269|PubMed:11934898}. 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:0000269|PubMed:11934898}; 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:0000269|PubMed:11934898}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:11934898}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:11934898}; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000269|PubMed:11934898}; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11934898}. CC -!- SUBCELLULAR LOCATION: Nucleus {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; CU329670; CAC00553.1; -; Genomic_DNA. DR RefSeq; NP_594768.1; NM_001020195.2. DR PDB; 3EF0; X-ray; 2.10 A; A=149-329, A=394-580. DR PDB; 3EF1; X-ray; 2.15 A; A=140-580. DR PDB; 4XPZ; X-ray; 1.45 A; A=149-329, A=394-580. DR PDB; 4XQ0; X-ray; 1.85 A; A=149-329, A=394-580. DR PDBsum; 3EF0; -. DR PDBsum; 3EF1; -. DR PDBsum; 4XPZ; -. DR PDBsum; 4XQ0; -. DR AlphaFoldDB; Q9P376; -. DR SMR; Q9P376; -. DR BioGRID; 278698; 17. DR STRING; 284812.Q9P376; -. DR iPTMnet; Q9P376; -. DR MaxQB; Q9P376; -. DR PaxDb; 4896-SPAC19B12-05c-1; -. DR EnsemblFungi; SPAC19B12.05c.1; SPAC19B12.05c.1:pep; SPAC19B12.05c. DR GeneID; 2542225; -. DR KEGG; spo:SPAC19B12.05c; -. DR PomBase; SPAC19B12.05c; fcp1. DR VEuPathDB; FungiDB:SPAC19B12.05c; -. DR eggNOG; KOG0323; Eukaryota. DR HOGENOM; CLU_007683_0_0_1; -. DR InParanoid; Q9P376; -. DR OMA; DQTVIHC; -. DR PhylomeDB; Q9P376; -. DR Reactome; R-SPO-113418; Formation of the Early Elongation Complex. DR Reactome; R-SPO-674695; RNA Polymerase II Pre-transcription Events. DR Reactome; R-SPO-6796648; TP53 Regulates Transcription of DNA Repair Genes. DR Reactome; R-SPO-75955; RNA Polymerase II Transcription Elongation. DR EvolutionaryTrace; Q9P376; -. DR PRO; PR:Q9P376; -. DR Proteomes; UP000002485; Chromosome I. DR GO; GO:0005634; C:nucleus; IDA:PomBase. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IDA:PomBase. DR GO; GO:0023052; P:signaling; NAS:PomBase. 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; 2. DR InterPro; IPR001357; BRCT_dom. DR InterPro; IPR036420; BRCT_dom_sf. DR InterPro; IPR039189; Fcp1. DR InterPro; IPR004274; FCP1_dom. DR InterPro; IPR011947; FCP1_euk. DR InterPro; IPR036412; HAD-like_sf. DR InterPro; IPR023214; HAD_sf. DR InterPro; IPR040078; RNA_Pol_CTD_Phosphatase. 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; PF03031; NIF; 1. DR Pfam; PF12738; PTCB-BRCT; 1. DR SFLD; SFLDG01124; C0.1:_RNA_Pol_CTD_Phosphatase; 1. DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 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 1: Evidence at protein level; KW 3D-structure; Cobalt; Hydrolase; Magnesium; Manganese; Metal-binding; KW Nucleus; Protein phosphatase; Reference proteome. FT CHAIN 1..723 FT /note="RNA polymerase II subunit A C-terminal domain FT phosphatase" FT /id="PRO_0000212567" FT DOMAIN 160..341 FT /note="FCP1 homology" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336" FT DOMAIN 486..579 FT /note="BRCT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033" FT REGION 345..380 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 631..723 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 352..366 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 638..654 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 671..686 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 170 FT /evidence="ECO:0000269|PubMed:11934898" FT ACT_SITE 172 FT /evidence="ECO:0000269|PubMed:11934898" FT MUTAGEN 170 FT /note="D->A,N,E: No activity." FT /evidence="ECO:0000269|PubMed:11934898" FT MUTAGEN 172 FT /note="D->A,N,E: No activity." FT /evidence="ECO:0000269|PubMed:11934898" FT HELIX 151..162 FT /evidence="ECO:0007829|PDB:4XPZ" FT STRAND 165..169 FT /evidence="ECO:0007829|PDB:4XPZ" FT TURN 172..174 FT /evidence="ECO:0007829|PDB:4XPZ" FT STRAND 175..179 FT /evidence="ECO:0007829|PDB:4XPZ" FT HELIX 183..188 FT /evidence="ECO:0007829|PDB:4XPZ" FT TURN 194..196 FT /evidence="ECO:0007829|PDB:4XPZ" FT HELIX 197..199 FT /evidence="ECO:0007829|PDB:4XPZ" FT STRAND 203..209 FT /evidence="ECO:0007829|PDB:4XPZ" FT TURN 210..213 FT /evidence="ECO:0007829|PDB:4XPZ" FT STRAND 214..222 FT /evidence="ECO:0007829|PDB:4XPZ" FT HELIX 226..234 FT /evidence="ECO:0007829|PDB:4XPZ" FT STRAND 237..242 FT /evidence="ECO:0007829|PDB:4XPZ" FT HELIX 247..257 FT /evidence="ECO:0007829|PDB:4XPZ" FT TURN 262..266 FT /evidence="ECO:0007829|PDB:4XPZ" FT TURN 271..273 FT /evidence="ECO:0007829|PDB:4XPZ" FT HELIX 282..284 FT /evidence="ECO:0007829|PDB:4XPZ" FT STRAND 293..298 FT /evidence="ECO:0007829|PDB:4XPZ" FT HELIX 301..303 FT /evidence="ECO:0007829|PDB:4XPZ" FT STRAND 309..311 FT /evidence="ECO:0007829|PDB:4XPZ" FT TURN 327..329 FT /evidence="ECO:0007829|PDB:4XPZ" FT HELIX 398..415 FT /evidence="ECO:0007829|PDB:4XPZ" FT HELIX 417..427 FT /evidence="ECO:0007829|PDB:4XPZ" FT HELIX 434..436 FT /evidence="ECO:0007829|PDB:3EF0" FT HELIX 445..470 FT /evidence="ECO:0007829|PDB:4XPZ" FT TURN 471..473 FT /evidence="ECO:0007829|PDB:4XPZ" FT HELIX 479..488 FT /evidence="ECO:0007829|PDB:4XPZ" FT STRAND 495..502 FT /evidence="ECO:0007829|PDB:4XPZ" FT TURN 508..510 FT /evidence="ECO:0007829|PDB:3EF0" FT HELIX 512..519 FT /evidence="ECO:0007829|PDB:4XPZ" FT STRAND 526..530 FT /evidence="ECO:0007829|PDB:4XPZ" FT STRAND 533..538 FT /evidence="ECO:0007829|PDB:4XPZ" FT STRAND 540..542 FT /evidence="ECO:0007829|PDB:4XQ0" FT HELIX 543..551 FT /evidence="ECO:0007829|PDB:4XPZ" FT STRAND 555..557 FT /evidence="ECO:0007829|PDB:4XPZ" FT HELIX 559..568 FT /evidence="ECO:0007829|PDB:4XPZ" FT HELIX 574..577 FT /evidence="ECO:0007829|PDB:4XPZ" FT STRAND 578..580 FT /evidence="ECO:0007829|PDB:3EF1" SQ SEQUENCE 723 AA; 81965 MW; A127A06CD2FD3435 CRC64; MSKRLTPIHL PNSLNYPIEI ASCLVPQGSY VKKGTPLLLY RFFTKVKEDQ EDGSEVYVDR EFVEQFECPV EGELVEWAVK KEESIENFSK IVAKLHEPCT HEVNYGGLCA ICGKNITSQD YMGYSDMARA NISMTHNTGD LTVSLEEASR LESENVKRLR QEKRLSLIVD LDQTIIHATV DPTVGEWMSD PGNVNYDVLR DVRSFNLQEG PSGYTSCYYI KFRPGLAQFL QKISELYELH IYTMGTKAYA KEVAKIIDPT GKLFQDRVLS RDDSGSLAQK SLRRLFPCDT SMVVVIDDRG DVWDWNPNLI KVVPYEFFVG IGDINSNFLA KSTPLPEQEQ LIPLEIPKDE PDSVDEINEE NEETPEYDSS NSSYAQDSST IPEKTLLKDT FLQNREALEE QNKERVTALE LQKSERPLAK QQNALLEDEG KPTPSHTLLH NRDHELERLE KVLKDIHAVY YEEENDISSR SGNHKHANVG LIIPKMKQKV LKGCRLLFSG VIPLGVDVLS SDIAKWAMSF GAEVVLDFSV PPTHLIAAKI RTEKVKKAVS MGNIKVVKLN WLTESLSQWK RLPESDYLLY PSYDLPDRNL SEHSYSSSSD DEQRISELND RELDEIDWQA ADQDVENALK DLSDDNDFDT GSISASQSQP EALEVNTPIK RKADLIQPSY NYDGEKRRKE NDNHEGYDLL PNSSTKGEES AENENELDDL ADIMEAELSK DTA //