ID   A0A0V0WF85_9BILA        Unreviewed;       972 AA.
AC   A0A0V0WF85;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Putative acid phosphatase 5 {ECO:0000313|EMBL:KRX74524.1};
GN   Name=pho-5 {ECO:0000313|EMBL:KRX74524.1};
GN   ORFNames=T06_2845 {ECO:0000313|EMBL:KRX74524.1};
OS   Trichinella sp. T6.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX74524.1, ECO:0000313|Proteomes:UP000054673};
RN   [1] {ECO:0000313|EMBL:KRX74524.1, ECO:0000313|Proteomes:UP000054673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS34 {ECO:0000313|EMBL:KRX74524.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) 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:KRX74524.1}.
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DR   EMBL; JYDK01000144; KRX74524.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0WF85; -.
DR   STRING; 92179.A0A0V0WF85; -.
DR   Proteomes; UP000054673; Unassembled WGS sequence.
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:SF110; ACID PHOSPHATASE 1, ISOFORM B; 1.
DR   PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 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   Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..972
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006871615"
SQ   SEQUENCE   972 AA;  113079 MW;  59EEE4E2467DBA25 CRC64;
     MINYQLLHLL FIFLFIQIAC SCSPKFGLQR DQSAKKALEK VMRTCRTRTC KNELSALGKY
     NAESESKDDE SSEQWNTYQT CVEDCWNSSR TVQKNEDAAD KFLEENNFTV KDAIELYNKL
     NPNNAVMLKI FFWILSLELY NPSEVHSALT LEMVQVIWRH GHRTPTRFIA SDTTNREDTW
     IPGPRELTKK GMKQQFLLGR ILSNRYMNEI PVVDKSKAWQ QIYIRSSNFN RTILSALSNL
     AAFMSNVTSL QPAFNEWPKR WIPIPIHTED DWILKPLSYC PTAAKSQMDN VVLTEEYQEI
     EENNTEFFKF LQNVTGISKI NLANIYTVHD SLQIIKEGSP EDWEPEDHPW PAWVNEEIYQ
     KIDYLRRYGN GYLFANENVR RLRAGPLLQE IISRMRDKAE SLTNQKQNSS SWIHRLKYYA
     YSAHDLNILI LMQMFGVKEW LAKNVDMPGF ASCLVFELWK TDDNQLEVKI FLRRGPLDSN
     FEQIQVQGCP LLPNGCPLNL FEEINEKYVV HDWNTECGLS SAETSYHSFS IVGLCIALKN
     DLVTMARYFA ELLLILLHIT HTSSIPTLEL VQVIWRHGHR TPVRRVTSLK ANDTNKWIPD
     LGELTKKGMK QQFLLGTILA NRYMNQIPLI ETNTAWQHIY IRSSNYNRTI VSALSNLAGF
     MHNSTSGLPN VHDWPQKWSP IPVHTEEEWK LRMLRECPAA VEVKKEKVIA TAEYQAYETN
     NTEFFKFLRN MTGIPNINLE NIYLIDDSLQ LIKEGSPEDW VPEDHPWPIW ATEEVYEKIK
     TLRQHGNGFL FADEEIRRLR GGPLLQEIIE RMRQKEASLT NKNLISPKWI RNLKYYAYSA
     HDLNILLLLQ MFKVEEWLQK NVSMPDFASC LSIELWRTDN NTMEVKVFQR LGPTEMVFQP
     VQVGGCPKLP SACPLEQFEE VFQKYFIKKS WINECTAQSA ATSSLHHSFL SAGVFCLIYW
     ILSEKIFTKL TI
//