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Database: UniProt
Entry: A0A5D2XIM2_GOSMU
LinkDB: A0A5D2XIM2_GOSMU
Original site: A0A5D2XIM2_GOSMU 
ID   A0A5D2XIM2_GOSMU        Unreviewed;       282 AA.
AC   A0A5D2XIM2;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:TYJ13756.1};
GN   ORFNames=E1A91_A10G071600v1 {ECO:0000313|EMBL:TYJ13756.1};
OS   Gossypium mustelinum (Cotton).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=34275 {ECO:0000313|EMBL:TYJ13756.1, ECO:0000313|Proteomes:UP000323597};
RN   [1] {ECO:0000313|EMBL:TYJ13756.1, ECO:0000313|Proteomes:UP000323597}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1408120.09 {ECO:0000313|EMBL:TYJ13756.1};
RA   Chen Z.J., Sreedasyam A., Ando A., Song Q., De L., Hulse-Kemp A., Ding M.,
RA   Ye W., Kirkbride R., Jenkins J., Plott C., Lovell J., Lin Y.-M., Vaughn R.,
RA   Liu B., Li W., Simpson S., Scheffler B., Saski C., Grover C., Hu G.,
RA   Conover J., Carlson J., Shu S., Boston L., Williams M., Peterson D.,
RA   Mcgee K., Jones D., Wendel J., Stelly D., Grimwood J., Schmutz J.;
RT   "WGS assembly of Gossypium mustelinum.";
RL   Submitted (JUL-2019) 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};
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DR   EMBL; CM017645; TYJ13756.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5D2XIM2; -.
DR   Proteomes; UP000323597; Chromosome a10.
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:SF16; INORGANIC PYROPHOSPHATASE 2-LIKE; 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   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR031051-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR031051-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000323597}.
FT   ACT_SITE        11
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR031051-1"
FT   ACT_SITE        13
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR031051-1"
FT   BINDING         11
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR031051-3"
FT   BINDING         13
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR031051-3"
FT   BINDING         22
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR031051-2"
FT   BINDING         97
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR031051-2"
FT   BINDING         182
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR031051-3"
SQ   SEQUENCE   282 AA;  31888 MW;  1EB1740DB50B319F CRC64;
     MAASNVVVVM DFDKTILDCD SDNWVVDKLG ATELFNELLP TMPLNSLMDR MMKELHIQGT
     KIEDIVAVLK RTPIHPRIIQ AIKSAHALGC DLKIVSDANV FFIDTTLKHH GLKECFSEIN
     TNPSFVDEEG RLRIFPYHDF TKHPHGRSHP CPPNMCKGIV IEKIQTSLSA VEEKKTIIYM
     GDGLGDFCPS LKLGDGDYML PRKDFPVWDL VCKNRSLIKA EVCEWSNGEE FDHVLHHFIT
     KITIDKSNIK GNNATQLYSD YKVQTMPGSS NQLFSHTLYV PL
//
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