ID L5KWH8_PTEAL Unreviewed; 271 AA.
AC L5KWH8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=PAL_GLEAN10004888 {ECO:0000313|EMBL:ELK15336.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK15336.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB030539; ELK15336.1; -; Genomic_DNA.
DR RefSeq; XP_006909039.1; XM_006908977.2.
DR AlphaFoldDB; L5KWH8; -.
DR STRING; 9402.L5KWH8; -.
DR GeneID; 102896091; -.
DR KEGG; pale:102896091; -.
DR CTD; 10106; -.
DR eggNOG; KOG1605; Eukaryota.
DR InParanoid; L5KWH8; -.
DR OrthoDB; 5473812at2759; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
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:InterPro.
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:UP000010552}.
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; 30616 MW; B2D247DBE10F869E CRC64;
MEHGSIITQA RREDALVLTK QGLVSKSSPK KPRGRNIFKA LFCCFHAQHV GQSGSSAELS
TYKEEANTIA KSDLLQCLQY QFYQIPGTCL LPEVTEQDQG RICVVIDLDE TLVHSSFKPI
NNADFIVPVE IEGTTHQVYV LKRPYVDEFL RRMGELFECV LFTASLAKYA DPVTDLLDRC
GVFRARLFRE SCVFHQGCYV KDLSRLGRDL RKTLILDNSP ASYIFHPENA VPVQSWFDDM
ADTELLNLIP IFEELSGAED VYTSLGQLRA P
//
