ID A0A0G4FHS1_VITBC Unreviewed; 467 AA.
AC A0A0G4FHS1;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=acid phosphatase {ECO:0000256|ARBA:ARBA00012646};
DE EC=3.1.3.2 {ECO:0000256|ARBA:ARBA00012646};
GN ORFNames=Vbra_9215 {ECO:0000313|EMBL:CEM13067.1};
OS Vitrella brassicaformis (strain CCMP3155).
OC Eukaryota; Sar; Alveolata; Colpodellida; Vitrellaceae; Vitrella.
OX NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEM13067.1, ECO:0000313|Proteomes:UP000041254};
RN [1] {ECO:0000313|EMBL:CEM13067.1, ECO:0000313|Proteomes:UP000041254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhu J., Qi W., Song R.;
RL Submitted (NOV-2014) 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};
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DR EMBL; CDMY01000442; CEM13067.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4FHS1; -.
DR STRING; 1169540.A0A0G4FHS1; -.
DR VEuPathDB; CryptoDB:Vbra_9215; -.
DR InParanoid; A0A0G4FHS1; -.
DR OMA; PRNKYIS; -.
DR OrthoDB; 230039at2759; -.
DR PhylomeDB; A0A0G4FHS1; -.
DR Proteomes; UP000041254; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd07378; MPP_ACP5; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR024927; Acid_PPase.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR PANTHER; PTHR10161; TARTRATE-RESISTANT ACID PHOSPHATASE TYPE 5; 1.
DR PANTHER; PTHR10161:SF14; TARTRATE-RESISTANT ACID PHOSPHATASE TYPE 5; 1.
DR Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000041254};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..467
FT /note="acid phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005189120"
FT TRANSMEM 388..412
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 30..270
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT REGION 422..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 467 AA; 51314 MW; E9875AD34444A559 CRC64;
MAALFTMLAA TVVASAAVSG AAESPSLTFV SLGDWGKLGT GQRNVAKQMG IEAQRLKASF
VLAIGDNFYE HGVRSVNDPL WQTTYHDVYG PIDSLQVPFY AVLGNHDWYG NASAQIDYHY
REPKPEWLSR ITLASLPFPL YAAATGRRWW MPHNWYSVAY PLTSEGQPMT GDSSEATEEQ
QYAVFVFIDT WVADPSNRQL AAMRHEQLHW LAKTLHGAAT DPHVGWIIVV GHYPIYTSGQ
HGDTDFLVSD VLPLLKEYQV DAYLCGHDHD LELLSEHTPE QPLPKNVTEL TSDTEGVTFV
VTGAGGKKRS FSKPLHKQHI YGWPSYGFTS HVLTSSQMTT HFISSDGSLL FTYTQPRRIR
TAVKEESELA PLIEDTPASE AKEVWAQWQW VAGAAGMGGL LAGAAVTWAV LFSGRKCGGW
QRVADEPSPS PMDASRAPFD ECTDAGADAP KTRHTDTDAN KSRAQAG
//