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Database: UniProt
Entry: H2NHV7_PONAB
LinkDB: H2NHV7_PONAB
Original site: H2NHV7_PONAB 
ID   H2NHV7_PONAB            Unreviewed;       271 AA.
AC   H2NHV7; A0A2J8UGR1;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   Name=CTDSP2 {ECO:0000313|Ensembl:ENSPPYP00000005367.2};
GN   ORFNames=CR201_G0027726 {ECO:0000313|EMBL:PNJ44452.1};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000005367.2, ECO:0000313|Proteomes:UP000001595};
RN   [1] {ECO:0000313|Ensembl:ENSPPYP00000005367.2, ECO:0000313|Proteomes:UP000001595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wilson R.K., Mardis E.;
RT   "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PNJ44452.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Susie {ECO:0000313|EMBL:PNJ44452.1};
RA   Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA   Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA   Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA   Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA   Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT   "High-resolution comparative analysis of great ape genomes.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSPPYP00000005367.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001512};
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:0000256|ARBA:ARBA00001482};
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DR   EMBL; NDHI03003457; PNJ44452.1; -; Genomic_DNA.
DR   RefSeq; XP_009246233.1; XM_009247958.1.
DR   STRING; 9601.ENSPPYP00000005367; -.
DR   Ensembl; ENSPPYT00000005577.2; ENSPPYP00000005367.2; ENSPPYG00000004711.2.
DR   eggNOG; KOG1605; Eukaryota.
DR   GeneTree; ENSGT01040000240451; -.
DR   HOGENOM; CLU_020262_4_0_1; -.
DR   OMA; ANTIAKX; -.
DR   TreeFam; TF313556; -.
DR   Proteomes; UP000001595; Chromosome 12.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IEA:Ensembl.
DR   GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR   CDD; cd07521; HAD_FCP1-like; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR011948; Dullard_phosphatase.
DR   InterPro; IPR004274; FCP1_dom.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR040078; RNA_Pol_CTD_Phosphatase.
DR   NCBIfam; TIGR02251; HIF-SF_euk; 1.
DR   PANTHER; PTHR12210:SF187; CARBOXY-TERMINAL DOMAIN RNA POLYMERASE II POLYPEPTIDE A SMALL PHOSPHATASE 2; 1.
DR   PANTHER; PTHR12210; DULLARD PROTEIN PHOSPHATASE; 1.
DR   Pfam; PF03031; NIF; 1.
DR   SFLD; SFLDG01124; C0.1:_RNA_Pol_CTD_Phosphatase; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SMART; SM00577; CPDc; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   PROSITE; PS50969; FCP1; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001595}.
FT   DOMAIN          97..255
FT                   /note="FCP1 homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50969"
FT   SITE            163
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640078-3"
FT   SITE            201
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640078-3"
SQ   SEQUENCE   271 AA;  30664 MW;  E4FA4A1657F2B03F CRC64;
     MEHGSIITQA RREDALVLTK QGLVSKSSPK KPRGRNIFKA LFCCFRAQHV GQSSSSTELA
     AYKEEANTIA KSDLLQCLQY QFYQIPGTCL LPEVTEEDQG RICVVIDLDE TLVHSSFKPI
     NNADFIVPIE IEGTTHQVYV LKRPYVDEFL RRMGELFECV LFTASLAKYA DPVTDLLDRC
     GVFRARLFRE SCVFHQGCYV KDLSRLGRDL RKTLILDNSP ASYIFHPENA VPVQSWFDDM
     ADTELLNLIP IFEELSGAED VYTSLGQLRA P
//
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