ID A9V819_MONBE Unreviewed; 515 AA.
AC A9V819;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Acid phosphatase {ECO:0008006|Google:ProtNLM};
GN ORFNames=MONBRDRAFT_33870 {ECO:0000313|EMBL:EDQ86262.1};
OS Monosiga brevicollis (Choanoflagellate).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Monosiga.
OX NCBI_TaxID=81824 {ECO:0000313|EMBL:EDQ86262.1, ECO:0000313|Proteomes:UP000001357};
RN [1] {ECO:0000313|EMBL:EDQ86262.1, ECO:0000313|Proteomes:UP000001357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MX1 / ATCC 50154 {ECO:0000313|Proteomes:UP000001357};
RX PubMed=18273011; DOI=10.1038/nature06617;
RG JGI Sequencing;
RA King N., Westbrook M.J., Young S.L., Kuo A., Abedin M., Chapman J.,
RA Fairclough S., Hellsten U., Isogai Y., Letunic I., Marr M., Pincus D.,
RA Putnam N., Rokas A., Wright K.J., Zuzow R., Dirks W., Good M.,
RA Goodstein D., Lemons D., Li W., Lyons J.B., Morris A., Nichols S.,
RA Richter D.J., Salamov A., Bork P., Lim W.A., Manning G., Miller W.T.,
RA McGinnis W., Shapiro H., Tjian R., Grigoriev I.V., Rokhsar D.;
RT "The genome of the choanoflagellate Monosiga brevicollis and the origin of
RT metazoans.";
RL Nature 451:783-788(2008).
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}.
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DR EMBL; CH991567; EDQ86262.1; -; Genomic_DNA.
DR RefSeq; XP_001748932.1; XM_001748880.1.
DR AlphaFoldDB; A9V819; -.
DR STRING; 81824.A9V819; -.
DR EnsemblProtists; EDQ86262; EDQ86262; MONBRDRAFT_33870.
DR GeneID; 5894231; -.
DR KEGG; mbr:MONBRDRAFT_33870; -.
DR eggNOG; KOG3720; Eukaryota.
DR InParanoid; A9V819; -.
DR OMA; PAWPIRD; -.
DR Proteomes; UP000001357; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR CDD; cd07061; HP_HAP_like; 1.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001357};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..515
FT /note="Acid phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002745375"
FT TRANSMEM 430..453
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 393..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 515 AA; 57072 MW; AA7ACB5C9017E0D9 CRC64;
MSSLRRLAGL GLLLTALPLV LGELKLVQIL FRHGDRTALR DLPGVSQPSD WPEGYGQLTA
LGMQMHYNVG AYFRKRYIQD LSFIDAAYNH EQIVVRSTDA DRTLMSAQAQ LAGWFPVETS
VLGPPDILWR PVPVHTRPVE DDLLLRSWSQ GVCPRYDQLE ANWNQTQGWH DKNNQIVDPL
ACQAVHLPAD QNCTVAQYLS ALEPISQIAP LDLDSLWQIS DTLLCRRMHN LSMPDYANHS
DVGEASYSLL RSLEDWGMYA MFDSVPKRRL SGGPVLQELI SNMQAALQDS SMPRVFLYSG
HDTNLAAVLE ALQTDHFRAR APPYASCLIV ELHVEDDTPF VRIVFKNESA IDAPEHPGHT
LTVKTCEHSD CPLSEFVKVM SPILPTDMTV DCQAATPSPT TRASSSTTTK NVPASTIDPT
SADAANKRDL TVTAVVVAIC LALAVAATFF ILFRRRQRRM RTIGTNIKYT SRSLAAPLSV
VDDDDEEEDV FSSNYPNAPA QRPGRASRNQ SDAFA
//