RPAP2_CAEEL
ID RPAP2_CAEEL Reviewed; 455 AA.
AC P30641;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Putative RNA polymerase II subunit B1 CTD phosphatase rpap-2;
DE EC=3.1.3.16;
DE AltName: Full=RNA polymerase II-associated protein 2;
GN Name=rpap-2 {ECO:0000312|WormBase:R08D7.2};
GN ORFNames=R08D7.2 {ECO:0000312|WormBase:R08D7.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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; Z12017; CAA78048.1; -; Genomic_DNA.
DR PIR; S41037; S24458.
DR RefSeq; NP_498983.1; NM_066582.4.
DR AlphaFoldDB; P30641; -.
DR SMR; P30641; -.
DR STRING; 6239.R08D7.2.2; -.
DR EPD; P30641; -.
DR PaxDb; P30641; -.
DR PeptideAtlas; P30641; -.
DR EnsemblMetazoa; R08D7.2.1; R08D7.2.1; WBGene00011143.
DR GeneID; 176267; -.
DR KEGG; cel:CELE_R08D7.2; -.
DR UCSC; R08D7.2.1; c. elegans.
DR CTD; 176267; -.
DR WormBase; R08D7.2; CE00290; WBGene00011143; rpap-2.
DR eggNOG; KOG4780; Eukaryota.
DR GeneTree; ENSGT00390000017965; -.
DR HOGENOM; CLU_584284_0_0_1; -.
DR InParanoid; P30641; -.
DR OMA; EHPLWIT; -.
DR OrthoDB; 975479at2759; -.
DR Reactome; R-CEL-6807505; RNA polymerase II transcribes snRNA genes.
DR PRO; PR:P30641; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00011143; Expressed in germ line (C elegans) and 4 other tissues.
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..455
FT /note="Putative RNA polymerase II subunit B1 CTD
FT phosphatase rpap-2"
FT /id="PRO_0000065430"
FT ZN_FING 36..121
FT /note="RTR1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
SQ SEQUENCE 455 AA; 52438 MW; 1FDFADAA58980F3E CRC64;
METEIPVNEK ETSFRRRVYT TIETLIDIEN TDQLQEHLPH LHCLGWDEVV EERYVNKQCG
FPSCQKAPPK ITRNQMFEID RKEGKIFEFR KQRAKFCSEM CYQKSSFVRK QLDEHPLWIT
GLTEARTQKV YEVPDESFVS PIAEKSEPVD SQFKKEPSIW LVTDSIIAKV QDMKLSEEAE
EPKSLDPEDQ DIEPFKLTDD DKDFIKSIKE FRNSNFGPPS TSKLLKTAPK PVLSAKDRKK
EDEVLAKLRA KYGNKNALQK KPPILIEAQE IHSKLKTMEK AKEAWLVDLI KSWFTPETRK
LVREGARPTG GAAEQILMDF LSGKKVDAEK LVNLPNLDKY NVKEKRLNIF LHSIRNHWMD
LEARLHLTPT RRDILSRVAS TFQLDSENIT GWTKREINSI VIALFIVICL VDVELGDDYF
KKDNASPELT AISNELCGLD SFQITGLHAA IKSQC
