ID A0A2G5V5A5_9PELO Unreviewed; 431 AA.
AC A0A2G5V5A5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Acid phosphatase {ECO:0008006|Google:ProtNLM};
GN Name=Cnig_chr_II.g6469 {ECO:0000313|EMBL:PIC46963.1};
GN ORFNames=B9Z55_006469 {ECO:0000313|EMBL:PIC46963.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC46963.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000032};
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIC46963.1}.
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DR EMBL; PDUG01000002; PIC46963.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5V5A5; -.
DR STRING; 1611254.A0A2G5V5A5; -.
DR Proteomes; UP000230233; Chromosome ii.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 1.
DR PANTHER; PTHR11567:SF191; INTESTINAL ACID PHOSPHATASE; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..431
FT /note="Acid phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013687280"
SQ SEQUENCE 431 AA; 50059 MW; 670C386D902E73CF CRC64;
MLIALLLSVR IISILSVSEE DFNLVFVQAL WRHGDRAAQY PYLNDKFTEN DWNSIGSGIG
QLTYKGVRQH IDLGESIRKR YIKSGFLPEN FDEEVVRLNL VKLNFSLVLK FQVVFRSTNR
NRTILSAKAN FLGMYPKKDE EEIKLPIIVP ENYGNDCINN VMCKCPRRDI LQKMAKDLDE
YKEVVEDEST ISLFSKLSKV AGETINVENF WRLPDTLRCE KRNFPDSFKQ KTPWYSEELL
EEMETLNTKI NRFTSGLYAS PEKSNRLDIG KEIRKLRCGP LISDIFGRMR QKLDCIYSQN
RAGRSSDCSE KIRKMKYYAY SSHDMTLYSL LTAMGLEDLT SMEIGGWPSY ASSLFVELFI
RKQDNNPYFR IIYRNPSSSY APSEFFNLTS LIPKCHESTF CHLNILENVF KEFNIGMPVS
EFCHVTNDLE L
//