ID A0A2G5V558_9PELO Unreviewed; 921 AA.
AC A0A2G5V558;
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=Cni-pho-1 {ECO:0000313|EMBL:PIC46882.1};
GN Synonyms=Cnig_chr_II.g6426 {ECO:0000313|EMBL:PIC46882.1};
GN ORFNames=B9Z55_006426 {ECO:0000313|EMBL:PIC46882.1};
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:PIC46882.1, 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:PIC46882.1}.
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DR EMBL; PDUG01000002; PIC46882.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5V558; -.
DR STRING; 1611254.A0A2G5V558; -.
DR Proteomes; UP000230233; Chromosome ii.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd07061; HP_HAP_like; 2.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 2.
DR InterPro; IPR033379; Acid_Pase_AS.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 1.
DR PANTHER; PTHR11567:SF207; INTESTINAL ACID PHOSPHATASE; 1.
DR Pfam; PF00328; His_Phos_2; 2.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 2.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 2.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..921
FT /note="Acid phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013828559"
FT TRANSMEM 899..918
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 921 AA; 104357 MW; 3E58995552BBAF85 CRC64;
MKVVFYSVPI LLLLQVSLSS GDVMNGTMKL MMVQALWRHG DRTPTETYHN DKFTEQDWVF
GGGGWGQLTP IGMRQHMQLG QKLRARYVNG QPYQFLNRRY DQQEIFVRST DKNRTLLSAF
SNMVGMYGSN NENASLPGYD YPDVPGWPAG FVPIPIHTIP DAEDHLLSVD NACALQDTIW
EMAKTTDIVS SYFNRSDVKS LMGNLTNYCG EDINPENLWI LFNALKIEKQ YYPLKFQQTT
PWYSDSLFEQ IDIVNSQVQD FQNGLGLEGV IKNGIDIGKY LRKIRGGTLV NDIYNHMNRK
TQCTSNNGKE CTYTNRLKFF AYSAHDTTLY ALFSLLGVAH LAVQPRGYPL YSACVIMEQW
QDIQTNQTYF KMIYHRHEND TLNNVITSGI PGCNGNDYCP LSVLKNYSDV YKPEMEMNQD
SAFNVKSFSP PNIILLLHID ACQQMSICTS GCVPDCYLKT EFQSFQYDMG VNFTMVSAIS
IVGLFALTGF ATSYTDGTKE LVFVQTLWRH GDRSPTKTFP TDPYQESAWT FGGGGWGQLS
PTGMRQHLNL GKMLRDRYVT NYQFFPTKYN AKQIYVRSTD VNRTIISAMS NLLGQYGQDD
GSSVPDVDYP AVAGWPKGFV PIAVHTVDDD TDHLGNMEST CPFREQVWNL AKTSDEVKNF
TNSDKVQSML AKLTNYTGQT VDIDNLWIIT NALYIEQIYF NDSIRAKNSW FTDDLYAQAD
AINDQVQLYQ NGIFKNMPNM VNGHDVGVLT RKIRGGPILN DMVMHMNIKL ACQGMTTPNC
TWINNLKNYV YSAHDTTIYA FFSALLIEEY AVKPSGGYPL YSAAVLLELY VDSADKKPYF
KMIYHEQDGS GFKTITQGIQ GCSSDYCSLD VLRNFSATIQ PDQPIDQWCY SDLNKYSGLN
TVSMLLLAVI LAVQYNFFGL F
//