ID A0A023BDT6_GRENI Unreviewed; 587 AA.
AC A0A023BDT6;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Histidine phosphatase superfamily (Branch 2) protein {ECO:0000313|EMBL:EZG89693.1};
GN ORFNames=GNI_001110 {ECO:0000313|EMBL:EZG89693.1};
OS Gregarina niphandrodes (Septate eugregarine).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Gregarinasina;
OC Eugregarinorida; Gregarinidae; Gregarina.
OX NCBI_TaxID=110365 {ECO:0000313|EMBL:EZG89693.1, ECO:0000313|Proteomes:UP000019763};
RN [1] {ECO:0000313|EMBL:EZG89693.1, ECO:0000313|Proteomes:UP000019763}
RP NUCLEOTIDE SEQUENCE.
RA Omoto C.K., Sibley D., Venepally P., Hadjithomas M., Karamycheva S.,
RA Brunk B., Roos D., Caler E., Lorenzi H.;
RL Submitted (DEC-2013) 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:EZG89693.1}.
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DR EMBL; AFNH02000010; EZG89693.1; -; Genomic_DNA.
DR RefSeq; XP_011128458.1; XM_011130156.1.
DR AlphaFoldDB; A0A023BDT6; -.
DR EnsemblProtists; EZG89693; EZG89693; GNI_001110.
DR GeneID; 22910319; -.
DR VEuPathDB; CryptoDB:GNI_001110; -.
DR eggNOG; ENOG502QWYC; Eukaryota.
DR OMA; CASELCP; -.
DR OrthoDB; 207924at2759; -.
DR Proteomes; UP000019763; Unassembled WGS sequence.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
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; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
DR PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000019763};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..587
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012316850"
SQ SEQUENCE 587 AA; 64998 MW; 98DDA65FA457A608 CRC64;
MFPLLLLAWV AGAYEYPNYC SKVGDEDFVQ ARTIPELSQE AVRLKTELVH VSTILRHGAR
TPAGRYLCWR GYAPQWNCDV EESLRPLLTA RAFAHTRTEI TDLIPPVPGD ADIKAAGASD
AQVADTEAHD LDLFPETATP QLMFRKHYDS DPAANSLGGT CGKGHLLAEG FEQHAHIGQL
FAQYYQKNST PLIATDAKNQ IWFRSSDMQR TILSGATFLT HFIRASNLTV GGEIDLHTMD
EGNDFIFPNA HACPELQQLK EDLLSSQTFA ELQAKYEGVE KSIAVLTGLE DVKALWPGEF
FDCIMTAVCG DEWASLPSNL RPMWLSSEVD TSDAASNQQI GSNLAGNNQM GTNQAASMRW
SDAFHETVGK TSAAVNEYAS YQYTWNGSRY SRAATVKFMV EFKTELCRAL MKHVTADHEP
AQAARILADI IPTDDLQEFY RRVVASRTSI TTPFDAKKLV VYAAHDTTLL PFLASLGNED
MFDATWPPYA SQMIFELHAA TKDTPHLRDQ PDDDDQSDDV DNQTAYFFRL IYNGVSITDR
IPACSKRRVG TSDLCGLKAF FHATSWAAPS KVTALCGSPT VIPDVVY
//