FCP1_SCHPO
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 03-AUG-2022, entry version 148.
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}.
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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; 4896.SPAC19B12.05c.1; -.
DR iPTMnet; Q9P376; -.
DR MaxQB; Q9P376; -.
DR PaxDb; Q9P376; -.
DR PRIDE; Q9P376; -.
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; PDVKDIM; -.
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:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:PomBase.
DR GO; GO:0023052; P:signaling; NAS:PomBase.
DR Gene3D; 3.40.50.1000; -; 1.
DR Gene3D; 3.40.50.10190; -; 1.
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 PANTHER; PTHR23081; PTHR23081; 1.
DR Pfam; PF03031; NIF; 1.
DR Pfam; PF12738; PTCB-BRCT; 1.
DR SFLD; SFLDG01124; C0.1:_RNA_Pol_CTD_Phosphatase; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR02250; FCP1_euk; 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
