RPAP2_ORYSI
ID RPAP2_ORYSI Reviewed; 726 AA.
AC A2Y040;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 60.
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 ORFNames=OsI_18345;
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
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}.
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DR EMBL; CM000130; EAY96450.1; -; Genomic_DNA.
DR AlphaFoldDB; A2Y040; -.
DR SMR; A2Y040; -.
DR STRING; 39946.A2Y040; -.
DR EnsemblPlants; BGIOSGA018860-TA; BGIOSGA018860-PA; BGIOSGA018860.
DR Gramene; BGIOSGA018860-TA; BGIOSGA018860-PA; BGIOSGA018860.
DR HOGENOM; CLU_008740_0_0_1; -.
DR OMA; ACGYPAC; -.
DR Proteomes; UP000007015; Chromosome 5.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblPlants.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:EnsemblPlants.
DR GO; GO:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; IEA:InterPro.
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_0000416293"
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; 78243 MW; 196556A6DD98BC51 CRC64;
MGPTTATDAG ARMKPTTVAS AVHRVQMALY DGAAASREPL LRAAASLLSG PDYADVVTER
SIADACGYPA CPNPLPSEDA RGKAAPRFRI SLREHRVYDL EEARKFCSER CLVASAAFGA
SLPPDRPFGV SPDRLDALVA LFEGGGGGGG DGGLALGFGA SGDGKEVEEG RKVEIMEKEA
AGTGEVTLQE WIGPSDAIEG YVPRRDRVVG GPKKEAKQND ACSAEQSSNI NVDSRNASSG
ESGMVLTENT KAKKKEATKT PLKMFKQDED NDMLSSCISD SIVKQLEDVV LEEKKDKKKN
KAAKGTSRVG KSKPAKRPVG RDGHEVDFTS TIIMGDHGSE MMDHGALGQY NFSSSILANE
QPSSSQYAAI DSVQAYTEEL DELFSNAVNI AKDETSDDSG RCTLRSSLKA VGSKNAGRSV
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
