ID A0A1R3HKP9_COCAP Unreviewed; 271 AA.
AC A0A1R3HKP9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=HAD-superfamily hydrolase, subfamily IB, PSPase-like protein {ECO:0000313|EMBL:OMO70834.1};
GN ORFNames=CCACVL1_18632 {ECO:0000313|EMBL:OMO70834.1};
OS Corchorus capsularis (Jute).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO70834.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO70834.1, ECO:0000313|Proteomes:UP000188268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC TISSUE=Whole seedling {ECO:0000313|EMBL:OMO70834.1};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT "Corchorus capsularis genome sequencing.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRSR:PIRSR031051-3};
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:OMO70834.1}.
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DR EMBL; AWWV01011761; OMO70834.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3HKP9; -.
DR STRING; 210143.A0A1R3HKP9; -.
DR EnsemblPlants; OMO70834; OMO70834; CCACVL1_18632.
DR Gramene; OMO70834; OMO70834; CCACVL1_18632.
DR OMA; RMMKEIH; -.
DR OrthoDB; 372892at2759; -.
DR Proteomes; UP000188268; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006384; HAD_hydro_PyrdxlP_Pase-like.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR016965; Pase_PHOSPHO-typ.
DR NCBIfam; TIGR01489; DKMTPPase-SF; 1.
DR NCBIfam; TIGR01488; HAD-SF-IB; 1.
DR PANTHER; PTHR20889:SF12; LP01149P; 1.
DR PANTHER; PTHR20889; PHOSPHATASE, ORPHAN 1, 2; 1.
DR Pfam; PF06888; Put_Phosphatase; 1.
DR PIRSF; PIRSF031051; PyrdxlP_Pase_PHOSPHO2; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:OMO70834.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR031051-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR031051-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000188268}.
FT ACT_SITE 10
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-1"
FT ACT_SITE 12
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-1"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-3"
FT BINDING 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-3"
FT BINDING 21
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-2"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-2"
FT BINDING 178
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-3"
SQ SEQUENCE 271 AA; 30646 MW; 05038A20DA66D63E CRC64;
MADGIVCVFD FDKTIIDVDS DNWVVDELGF TDLFNQLLPT MPWNSLMDRM MKEIHAQGKT
IDDIAEVLKR IPIHPRVVPA IKEAHALGCE LRIVSDANLF FIETILEHLG LREYFSEINT
NPGYVDGEGR LRIFPYHDFN KCSHGCNLCP PNMCKVGMII ERIQASLEGK KRIIYLGDGS
GDYCPSLKLG EADIMMPRKN FPVWDLICRN PMLIKAEIHE WTDGEDLERV LLQIINMISL
NNAQLISVDC KLQIISASAH EALPQALPVP Q
//
