RPAP2_SCHPO
ID RPAP2_SCHPO Reviewed; 197 AA.
AC O42853;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Putative RNA polymerase II subunit B1 CTD phosphatase rtr1;
DE EC=3.1.3.16;
DE AltName: Full=RNA polymerase II-associated protein 2 homolog rtr1;
GN ORFNames=SPAC23A1.16c;
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Putative RNA polymerase II subunit B1 C-terminal domain (CTD)
CC phosphatase involved in RNA polymerase II transcription regulation.
CC {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: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000305|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the RPAP2 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00812, ECO:0000305}.
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DR EMBL; CU329670; CAA16990.1; -; Genomic_DNA.
DR PIR; T38235; T38235.
DR RefSeq; NP_594445.1; NM_001019874.2.
DR AlphaFoldDB; O42853; -.
DR SMR; O42853; -.
DR BioGRID; 278488; 1.
DR STRING; 4896.SPAC23A1.16c.1; -.
DR MaxQB; O42853; -.
DR PaxDb; O42853; -.
DR EnsemblFungi; SPAC23A1.16c.1; SPAC23A1.16c.1:pep; SPAC23A1.16c.
DR GeneID; 2542005; -.
DR KEGG; spo:SPAC23A1.16c; -.
DR PomBase; SPAC23A1.16c; -.
DR VEuPathDB; FungiDB:SPAC23A1.16c; -.
DR eggNOG; KOG4780; Eukaryota.
DR HOGENOM; CLU_1349593_0_0_1; -.
DR InParanoid; O42853; -.
DR OMA; LWIRERA; -.
DR PhylomeDB; O42853; -.
DR PRO; PR:O42853; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; ISM: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:0043175; F:RNA polymerase core enzyme binding; ISM:PomBase.
DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; ISO:PomBase.
DR GO; GO:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
DR GO; GO:0023052; P:signaling; NAS:PomBase.
DR Gene3D; 1.25.40.820; -; 1.
DR InterPro; IPR039693; Rtr1/RPAP2.
DR InterPro; IPR007308; Rtr1/RPAP2_dom.
DR InterPro; IPR038534; Rtr1/RPAP2_sf.
DR PANTHER; PTHR14732; PTHR14732; 1.
DR Pfam; PF04181; RPAP2_Rtr1; 1.
DR PROSITE; PS51479; ZF_RTR1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Metal-binding; Nucleus; Protein phosphatase;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..197
FT /note="Putative RNA polymerase II subunit B1 CTD
FT phosphatase rtr1"
FT /id="PRO_0000317210"
FT ZN_FING 60..139
FT /note="RTR1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
SQ SEQUENCE 197 AA; 23217 MW; 8630B72C41F070E2 CRC64;
MNKKSILKKP KNAQSTQEKQ LITWSKSLID EARSRLQYDF FALEWIEKLV DPVSLETLEE
ARKYLRKSDY DQVVKERKLV NLCGYPVCPY EPKQQTRYKL EDSGMKVYGG LNYYCSKDCF
LKSCQYMVEL SDEPLWIRED AREAMKQHLD PRQDEAFRKE LENKKIEDVR LLLQALPVGY
KAKVGEIVEH PLANEQS
