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Database: UniProt
Entry: A0A0Q7SJQ3_9CAUL
LinkDB: A0A0Q7SJQ3_9CAUL
Original site: A0A0Q7SJQ3_9CAUL 
ID   A0A0Q7SJQ3_9CAUL        Unreviewed;       270 AA.
AC   A0A0Q7SJQ3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=3'(2'),5'-bisphosphate nucleotidase CysQ {ECO:0000313|EMBL:KQY84576.1};
GN   ORFNames=ASD25_05885 {ECO:0000313|EMBL:KQY84576.1};
OS   Brevundimonas sp. Root1423.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Brevundimonas.
OX   NCBI_TaxID=1736462 {ECO:0000313|EMBL:KQY84576.1, ECO:0000313|Proteomes:UP000051815};
RN   [1] {ECO:0000313|Proteomes:UP000051815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1423 {ECO:0000313|Proteomes:UP000051815};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQY84576.1, ECO:0000313|Proteomes:UP000051815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1423 {ECO:0000313|EMBL:KQY84576.1,
RC   ECO:0000313|Proteomes:UP000051815};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC       {ECO:0000256|ARBA:ARBA00009759}.
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:KQY84576.1}.
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DR   EMBL; LMFL01000023; KQY84576.1; -; Genomic_DNA.
DR   RefSeq; WP_056617616.1; NZ_LMFL01000023.1.
DR   AlphaFoldDB; A0A0Q7SJQ3; -.
DR   Proteomes; UP000051815; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR   CDD; cd01638; CysQ; 1.
DR   Gene3D; 3.40.190.80; -; 1.
DR   Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1.
DR   InterPro; IPR020583; Inositol_monoP_metal-BS.
DR   InterPro; IPR000760; Inositol_monophosphatase-like.
DR   InterPro; IPR020550; Inositol_monophosphatase_CS.
DR   PANTHER; PTHR20854; INOSITOL MONOPHOSPHATASE; 1.
DR   PANTHER; PTHR20854:SF4; INOSITOL-1-MONOPHOSPHATASE-RELATED; 1.
DR   Pfam; PF00459; Inositol_P; 1.
DR   PRINTS; PR00377; IMPHPHTASES.
DR   SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR   PROSITE; PS00629; IMP_1; 1.
DR   PROSITE; PS00630; IMP_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051815}.
SQ   SEQUENCE   270 AA;  28946 MW;  80E12B9661ED8180 CRC64;
     MTDLAADLAL IRDAALAAGE LALAEREAGL KIWSKSGGSP VTSADMAVDQ LLKDTVLAAR
     PDHSWLSEET ADTDARIGQR RLIVVDPIDG TVAYMKGKPW WCIPIAIVED GQPVAAVIHA
     PALGETFTAT RGGGAFLNGR PITASDTTDL DDASVLADAR LMEGPHWPEP WPAMRFEKRN
     AIAYRMALVA AGAFDAAIAL TPKWDWDVCA GALIVEEAGG RVSDHHGVAW RFNQPDPRQN
     SLICSAPALH PLIVRRTAPI PLAPRQTDRT
//
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