ID A0A2P6TB37_CHLSO Unreviewed; 1526 AA.
AC A0A2P6TB37;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Purple acid phosphatase {ECO:0000256|RuleBase:RU361203};
DE EC=3.1.3.2 {ECO:0000256|RuleBase:RU361203};
GN ORFNames=C2E21_9560 {ECO:0000313|EMBL:PRW05763.1};
OS Chlorella sorokiniana (Freshwater green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX NCBI_TaxID=3076 {ECO:0000313|EMBL:PRW05763.1, ECO:0000313|Proteomes:UP000239899};
RN [1] {ECO:0000313|EMBL:PRW05763.1, ECO:0000313|Proteomes:UP000239899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTEX 1602 {ECO:0000313|Proteomes:UP000239899};
RX PubMed=29178410; DOI=10.1111/tpj.13789;
RA Arriola M.B., Velmurugan N., Zhang Y., Plunkett M.H., Hondzo H.,
RA Barney B.M.;
RT "Genome sequences of Chlorella sorokiniana UTEX 1602 and Micractinium
RT conductrix SAG 241.80: implications to maltose excretion by a green alga.";
RL Plant J. 93:566-586(2018).
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 -!- SIMILARITY: Belongs to the RNase T2 family.
CC {ECO:0000256|ARBA:ARBA00007469, ECO:0000256|RuleBase:RU004328}.
CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. Purple
CC acid phosphatase family. {ECO:0000256|ARBA:ARBA00008723,
CC 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:PRW05763.1}.
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DR EMBL; LHPG02000029; PRW05763.1; -; Genomic_DNA.
DR STRING; 3076.A0A2P6TB37; -.
DR OrthoDB; 5485592at2759; -.
DR Proteomes; UP000239899; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0033897; F:ribonuclease T2 activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00839; MPP_PAPs; 1.
DR CDD; cd13999; STKc_MAP3K-like; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 2.60.40.380; Purple acid phosphatase-like, N-terminal; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR Gene3D; 3.90.730.10; Ribonuclease T2-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041792; MPP_PAP.
DR InterPro; IPR039331; PPA-like.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008963; Purple_acid_Pase-like_N.
DR InterPro; IPR025733; Purple_acid_PPase_C_dom.
DR InterPro; IPR001568; RNase_T2-like.
DR InterPro; IPR036430; RNase_T2-like_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22953; ACID PHOSPHATASE RELATED; 1.
DR PANTHER; PTHR22953:SF153; PURPLE ACID PHOSPHATASE; 1.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF14008; Metallophos_C; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00445; Ribonuclease_T2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF81383; F-box domain; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF49363; Purple acid phosphatase, N-terminal domain; 1.
DR SUPFAM; SSF55895; Ribonuclease Rh-like; 1.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361203};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000239899};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1021..1044
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..54
FT /note="F-box"
FT /evidence="ECO:0000259|PROSITE:PS50181"
FT DOMAIN 1230..1514
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 771..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 997..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1053..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1015
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1526 AA; 164543 MW; FB5FA57A20B5B605 CRC64;
MSLNELPDEL LLHIFEALRE VDPWSWDNKL YTAVPLVCRR WRSLTLSPQL LCKLSIDLHI
MRRADLLPRL RSLCVWMACA AGHIRSLYLN LVFINPLRAD QGEVEGLLAE LQDMGSYVPS
QLDCRSLTRL RLLCISLSQA EAGDYEPLWN LPALERLSLA SCLQLPACLG RLAALRVLSI
SDSPMLEYDF ELAEEEQDPS SDELQRQRAA ALQQALSGLS AAQLTQLALA TNYPADCSQA
LMRLPAAMAQ RLLLAALCLA VAWGPAPTAR AQVSYSSLYH RPAERPALAL DHARLARSPQ
SNAHSPEQVH LAFAGPGAYA VTWVTYPLDR PRLDSSAEQQ AGAAAGTARR LAAAPGSQQQ
QLMAAASDAA GRLDRRRKDR CAPVVQAGGK SVVQYGTASG DYQHTVESPD PPACYSSGNY
VSGAIHRVIF GAGYEGPLPY NNTIFYRVGD PTRGWSDEFS FRTAPLVGLD ALPYRLGLVG
DLGQTDHSLS TLEHMVATNA DSVILTGDLS YADGYQPRWD TWGRLVAPHT SRQVWMYCVG
NHEIELTDGV KDFLSYTTRF YCPYRHSLSE SPLYYSYDVA GAHVIMLSSY SPYSRDSEQY
AWLLRDLASV DRARTPWLVV SFHAPWYNSN YAHQGEGEEM RKAMEPVLYE HGVDFVFCGH
VHAYERHHRV FDNRLDHCAP IHINIGDGGN KEGPDKKYYA QPKYSAYREP SFGHGTLDLL
DATHAEWRWH RNQDDGPESA DFVSVVRDPD CKSLRAERLA AWRANQAAAG SGGVQQAQQG
QQQGQQERST AWLEEQAEEQ ALILEREAEQ RAATAAQRQH LSEEAEQQHG LWCGLSVDML
VLKHGWAPIF CENADRTGAF CGGTTPFGAF RLNRLAAKTF EGKDVTGCND PAFTSSDVPQ
DLLPELNCVW NSYAVPNNNE QLWSSIWSEA TEGGVCTGLS PSEWMRRAVQ LRDQYNPDRA
FKSAGIVEGG ATTAAAITSA FSSAYGRNPH VACNKATTTA SSSSSSSSSS DSGGGGGVNG
AAIGAAVGIA IAVVAAAVIG FAFWRKKRRA RLPRGPADTT GTLGFGGSPT RPHGPPAATA
TLGSLGSLGT VPTRPHGGPP MSLASMMEAG GGAGAAMAGG AAVVGAGGAA QAWQPLPDPG
AGLPPPLPAQ ELDTFVRPGS SAMLGSASAA TASAVLAQDP LMSYIYNSRV SVASRSSART
AGSGGGASSV RTPSSTGIDM HPWEIGFGEL SILRPIGEGS FGRVYLANWR GVFVACKVLL
MGGAGAADPQ RALTLSSPVL NKLEEEASLL ASLRHPNIVN FFGICHDPPC IVTEYAAYGS
LAELLARARA EPAVAEALTW PRRLAMLITA ATGMLYLHNR PAGAIVHRDL KSPNLLVDQA
WNCKVTDFNL SRILEDTTQG SSMAAMNPRW LAPEVMQGQR ATRASDVFSF SVVMWEMLTL
DVPYGSGNPW QLVSHVLSGG RLDLPPPEAL PGGSSPALQA GLPAYVALMK RCWAQAPEDR
PAFDHIVQQL RVLLEQANGG EPAAEY
//