ID A0A2B4S6W9_STYPI Unreviewed; 1389 AA.
AC A0A2B4S6W9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Purple acid phosphatase {ECO:0000256|RuleBase:RU361203};
DE EC=3.1.3.2 {ECO:0000256|RuleBase:RU361203};
GN Name=POGK {ECO:0000313|EMBL:PFX24793.1};
GN ORFNames=AWC38_SpisGene10603 {ECO:0000313|EMBL:PFX24793.1};
OS Stylophora pistillata (Smooth cauliflower coral).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Pocilloporidae; Stylophora.
OX NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX24793.1, ECO:0000313|Proteomes:UP000225706};
RN [1] {ECO:0000313|Proteomes:UP000225706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA Tambutte S., Allemand D., Aranda M.;
RT "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT digitifera provides evidence for extensive differences between species of
RT corals.";
RL bioRxiv 0:0-0(2017).
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|RuleBase:RU361203};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. Purple
CC acid phosphatase family. {ECO:0000256|RuleBase:RU361203}.
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:PFX24793.1}.
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DR EMBL; LSMT01000167; PFX24793.1; -; Genomic_DNA.
DR EnsemblMetazoa; XM_022936267.1; XP_022792002.1; LOC111331203.
DR Proteomes; UP000225706; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd00839; MPP_PAPs; 1.
DR Gene3D; 3.60.21.10; -; 2.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 2.60.40.380; Purple acid phosphatase-like, N-terminal; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR004875; DDE_SF_endonuclease_dom.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR006600; HTH_CenpB_DNA-bd_dom.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041792; MPP_PAP.
DR InterPro; IPR008963; Purple_acid_Pase-like_N.
DR InterPro; IPR015914; Purple_acid_Pase_N.
DR InterPro; IPR025733; Purple_acid_PPase_C_dom.
DR PANTHER; PTHR45778:SF51; PURPLE ACID PHOSPHATASE; 1.
DR PANTHER; PTHR45778; PURPLE ACID PHOSPHATASE-RELATED; 1.
DR Pfam; PF03184; DDE_1; 1.
DR Pfam; PF03221; HTH_Tnp_Tc5; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF14008; Metallophos_C; 1.
DR Pfam; PF16656; Pur_ac_phosph_N; 2.
DR SMART; SM00674; CENPB; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 2.
DR SUPFAM; SSF49363; Purple acid phosphatase, N-terminal domain; 2.
DR PROSITE; PS51253; HTH_CENPB; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|RuleBase:RU361203};
KW Reference proteome {ECO:0000313|Proteomes:UP000225706};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 1036..1104
FT /note="HTH CENPB-type"
FT /evidence="ECO:0000259|PROSITE:PS51253"
FT REGION 1355..1389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1357..1389
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1389 AA; 157170 MW; 317C4D0C9018D5D3 CRC64;
MSVPFFKMAA LRAFAAVWIS IFWVTGIDCK HDHPVPTYFG KLHPNGTIVD ARNPANKLRF
SLPPKPITTQ DAGAVLKVSP SSEIENGEEV NVMWSGVTLP NSKDVVALYC PPDTEPNHYL
DFINVSSIAT YSKGYGEFGV RLWNLRKECI FRYYRIGNYS MLEAESNVVT FEGGAAIPLQ
GHLALTGNPT EMRVMWVSGL METSIVKYGT DPSAMVIIVG NVSKTYTAAD MCNSPANDVN
NFVDPGYIHD VLLKNLTPGT RYYYSYGSMK AYIWEQWHAI IEPYATILPY MVGVGNHEQD
HLKGGSKDPS GAPGEGFHPW WVEGYAYGTD SGGECGVPMY YRFHMPDNGN AVWWYSFDYG
SIHFMMMSTE HNFTQGSRQY EWMEQDLKNV NRSLTPWVVI AGHRAMYTSQ KEEWDYIVSL
GMQHAFDSLL YKYKVDLAFW AHYHSYERTC PVYQRQCTPG APVHIVVGTA GKELDLEEYF
PVSWSLYHEN DYGYGRLTQA NRSALLWEWV ENTSGKLPMH SVTSHDFKMA AVRAFAAVWI
SIFWVTGINC KHDHPVPTYF GKLHPNGTIV DARNPANKLR FSFPPKSITT QDSTADLKVS
PSSEIKNGEE VNVMWSGVTS PNKEDVVVLY CPPDAEPERY LDYVNVSTIA TYPKGYGEFR
VRLWNVRKDC VFRYFRIGNY SLLAVESNLV TFKGGAEMPL QGHLALTGNP TEMRVMWVSG
STELSIVKYG TDPSAMVIMV GNVSKTYTAA DMCNAPANDV NIFVDPGFIH DVLLTDLTPG
TRYYYSYGSM KMMSPIQHFN TAPPVGSASK FTALVYGDMG ISPIPRAYKT ADYATEEANN
GTAAFVIHNG DISYARGYAY IWEQWHAIIE PYATIIPYMV GIGNHEQDHV KGGSKDPSGA
PGEGFHPWWS GGWGHDSFGE CGVPMFYRFH MPDNGNAVWW YSFDYGSIHF TMMSTEHNFT
QGSRQYEWIE QDLKSVNRSL TPCMAFKIKV IAEAEAVENN SEIAREYGLS ESMVRRWRRD
QATILSGELK MSAKRATMGR FTPKYPELDQ QVMEWFSQQR EQGIAVSGLI LRLKAKELSD
DPAFKASRGW YEKWKRRHSV SMRTKTTLAQ RLPADLEENI VCFHRFVIAA RRRADYPLSR
IYNMDETPMR FELPSNRTLE FSGSRTVPVK SCGAEKRSFT VVLAVAADGA KVPPKVIFKG
VRTPRDLVVP HPLRVSFHKK GWMDEQGIRE WIRQSLPRAE RSLLVWDSFR AHLTDSVKDD
LKQRNIDVAV IPGGLTPVVQ PLDKCLNKPF KDNVRRKYLA WMTSGPFEFT PAGKKKAPSR
NLVLRWIKEA WAEIPEEMVV KSFKTCGISN ALDGTEDDVV YSEETPEVDD EYIEENEFDT
DSENETDGE
//
