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RPAP2_ORYSJ
ID   RPAP2_ORYSJ             Reviewed;         726 AA.
AC   Q6AVZ9; A0A0N7KK38; Q0DKZ3;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Putative RNA polymerase II subunit B1 CTD phosphatase RPAP2 homolog;
DE            EC=3.1.3.16;
DE   AltName: Full=RNA polymerase II-associated protein 2 homolog;
GN   OrderedLocusNames=Os05g0134300, LOC_Os05g04370;
GN   ORFNames=OsJ_17019, P0519E07.4;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA   Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA   Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA   Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT   "A fine physical map of the rice chromosome 5.";
RL   Mol. Genet. Genomics 274:337-345(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
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: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RPAP2 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00812, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAF16480.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC087552; AAT94046.1; -; Genomic_DNA.
DR   EMBL; AP008211; BAF16480.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014961; BAS92137.1; -; Genomic_DNA.
DR   EMBL; CM000142; EEE62232.1; -; Genomic_DNA.
DR   RefSeq; XP_015640837.1; XM_015785351.1.
DR   AlphaFoldDB; Q6AVZ9; -.
DR   SMR; Q6AVZ9; -.
DR   STRING; 4530.OS05T0134300-01; -.
DR   PaxDb; Q6AVZ9; -.
DR   PRIDE; Q6AVZ9; -.
DR   EnsemblPlants; Os05t0134300-01; Os05t0134300-01; Os05g0134300.
DR   GeneID; 4337724; -.
DR   Gramene; Os05t0134300-01; Os05t0134300-01; Os05g0134300.
DR   KEGG; osa:4337724; -.
DR   eggNOG; KOG4780; Eukaryota.
DR   HOGENOM; CLU_008740_0_0_1; -.
DR   InParanoid; Q6AVZ9; -.
DR   OMA; ACGYPAC; -.
DR   OrthoDB; 1506260at2759; -.
DR   Proteomes; UP000000763; Chromosome 5.
DR   Proteomes; UP000007752; Chromosome 5.
DR   Proteomes; UP000059680; Chromosome 5.
DR   Genevisible; Q6AVZ9; OS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IEA:InterPro.
DR   GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IBA:GO_Central.
DR   GO; GO:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
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   Hydrolase; Metal-binding; Nucleus; Protein phosphatase; Reference proteome;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..726
FT                   /note="Putative RNA polymerase II subunit B1 CTD
FT                   phosphatase RPAP2 homolog"
FT                   /id="PRO_0000416292"
FT   ZN_FING         43..131
FT                   /note="RTR1-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT   REGION          209..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          294..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..242
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT   BINDING         71
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT   BINDING         107
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT   BINDING         111
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
SQ   SEQUENCE   726 AA;  78331 MW;  4AF8D7356FB0361B CRC64;
     MGPTTATDTG ARMKPTTVAS AVHRVQMALY DGAAASREPL LRAAASLLSG PDYADVVTER
     SIADACGYPA CPNPLPSEDA RGKAAPRFRI SLREHRVYDL EEARKFCSER CLVASAAFGA
     SLPPDRPFGV SPDRLDALVA LFEGGGGGGD DGGLALGFGA SGDGKEVEEG RKVEIMEKEA
     AGTGEVTLQE WIGPSDAIEG YVPRRDRVVG GPKKEAKQND ACSAEQSSNI NVDSRNASSG
     ESGMVLTENT KAKKKEATKT PLKMFKQDED NDMLSSCISD SIVKQLEDVV LEEKKDKKKN
     KAAKGTSRVG KSKPAKRPVG RDGHEVDFTS TIIMGDRGSE MMDHGALGQY NFSSSILANE
     QPSSSQYAAI DSVQAYTEEL DELFSNAVNI AKDETSDDSG RCTLRSSLKA VGSKNAGHSV
     KWADENGSVL ETSRAFVSHS SKSQESMDSS VRRESAEACA AALIEAAEAI SSGTSEVEDA
     VSKAGIIILP DMVNQQQYNN DYDNDKDAGE NEIFEIDRGV VKWPKKTVLL DTDMFDVDDS
     WHDTPPEGFS LTLSSFATMW AALFGWVSRS SLAYVYGLDE SSMEDLLIAG GRECPQKRVL
     NDGHSSEIRR ALDTCVCNAL PVLVSNLRMQ IPVSKLEITL GYLLDTMSFV DALPSLRSRQ
     WQLMVLVLLD ALSLHRLPAL APIMSDSKLL QKLLNSAQVS REEYDSMIDL LLPFGRSTQS
     QASLPS
 
 
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