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Database: UniProt
Entry: A0A102DCD7_9SPHN
LinkDB: A0A102DCD7_9SPHN
Original site: A0A102DCD7_9SPHN 
ID   A0A102DCD7_9SPHN        Unreviewed;       303 AA.
AC   A0A102DCD7;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Phosphatase {ECO:0000313|EMBL:KUR78938.1};
GN   ORFNames=AQZ50_06245 {ECO:0000313|EMBL:KUR78938.1};
OS   Novosphingobium sp. Fuku2-ISO-50.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1739114 {ECO:0000313|EMBL:KUR78938.1, ECO:0000313|Proteomes:UP000056630};
RN   [1] {ECO:0000313|EMBL:KUR78938.1, ECO:0000313|Proteomes:UP000056630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fuku2-ISO-50 {ECO:0000313|EMBL:KUR78938.1,
RC   ECO:0000313|Proteomes:UP000056630};
RA   Ruckert C., Winkler A., Glaeser J., Grossart H.-P., Kalinowski J.,
RA   Glaeser S.;
RT   "Draft genome sequence of Novosphingobium sp. Fuku2-ISO-50 (=DSM 27930), a
RT   Novosphingobium acidiphilum related species isolated from a surface water
RT   sample of the southwest basin of Lake Grosse Fuchskuhle.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-(ADP-alpha-D-ribosyl)-thymidine in DNA + H2O = a
CC         thymidine in DNA + ADP-D-ribose; Xref=Rhea:RHEA:71655, Rhea:RHEA-
CC         COMP:13556, Rhea:RHEA-COMP:18051, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:57967, ChEBI:CHEBI:137386, ChEBI:CHEBI:191199;
CC         Evidence={ECO:0000256|ARBA:ARBA00035885};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71656;
CC         Evidence={ECO:0000256|ARBA:ARBA00035885};
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:KUR78938.1}.
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DR   EMBL; LLZR01000008; KUR78938.1; -; Genomic_DNA.
DR   RefSeq; WP_067744217.1; NZ_KQ954287.1.
DR   AlphaFoldDB; A0A102DCD7; -.
DR   STRING; 1739114.AQZ50_06245; -.
DR   OrthoDB; 9780211at2; -.
DR   Proteomes; UP000056630; Unassembled WGS sequence.
DR   CDD; cd02901; Macro_Poa1p-like; 1.
DR   Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR   InterPro; IPR002589; Macro_dom.
DR   InterPro; IPR043472; Macro_dom-like.
DR   PANTHER; PTHR12521:SF0; ADP-RIBOSE GLYCOHYDROLASE OARD1; 1.
DR   PANTHER; PTHR12521; PROTEIN C6ORF130; 1.
DR   Pfam; PF01661; Macro; 1.
DR   SMART; SM00506; A1pp; 1.
DR   SUPFAM; SSF52949; Macro domain-like; 1.
DR   PROSITE; PS51154; MACRO; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000056630}.
FT   DOMAIN          1..148
FT                   /note="Macro"
FT                   /evidence="ECO:0000259|PROSITE:PS51154"
FT   REGION          268..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..303
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   303 AA;  33628 MW;  9A45FFBE9261DE11 CRC64;
     MLIYRRTSIF ESPAQTLVNT VNCVGVMGKG LAHAFKEREP DMFKAYKRIC DQHALEPGKL
     WLWRGKGNWV LNFPTKVHWR NPSRIEWIEQ GLAKFVSAYA DQGITEISFP QLGCGNGNLD
     WADVSLLMEH YLAKLPIPVY IHDYTVDVGL PEHLEPIARA LIDAGVSSGS FDSFIASIGE
     ALTVANGEMT TLDARSSFRA SFRDDNVLAI ETETSSCVLE EDDLRGVWFD MRSGLVTREN
     AGWSVKAGGE PLLSLLSVLP DMRPVQIQRP GRSDPEFAVE PRPNLGGAVS TGQTRGQQEL
     AWH
//
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