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Database: UniProt
Entry: A0A0W7WA01_9MICO
LinkDB: A0A0W7WA01_9MICO
Original site: A0A0W7WA01_9MICO 
ID   A0A0W7WA01_9MICO        Unreviewed;       678 AA.
AC   A0A0W7WA01;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Nucleotide pyrophosphatase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AUL38_09655 {ECO:0000313|EMBL:KUF07378.1};
OS   Leucobacter sp. G161.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Leucobacter.
OX   NCBI_TaxID=663704 {ECO:0000313|EMBL:KUF07378.1, ECO:0000313|Proteomes:UP000053012};
RN   [1] {ECO:0000313|EMBL:KUF07378.1, ECO:0000313|Proteomes:UP000053012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G161 {ECO:0000313|EMBL:KUF07378.1,
RC   ECO:0000313|Proteomes:UP000053012};
RA   Ge S., Dong X.;
RT   "High quality draft genome sequence of Leucobacter sp. G161, a distinct and
RT   effective chromium reducer.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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:KUF07378.1}.
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DR   EMBL; LOHP01000057; KUF07378.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0W7WA01; -.
DR   STRING; 663704.AUL38_09655; -.
DR   OrthoDB; 1956004at2; -.
DR   Proteomes; UP000053012; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 2.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR002591; Phosphodiest/P_Trfase.
DR   PANTHER; PTHR10151:SF120; BIS(5'-ADENOSYL)-TRIPHOSPHATASE; 1.
DR   PANTHER; PTHR10151; ECTONUCLEOTIDE PYROPHOSPHATASE/PHOSPHODIESTERASE; 1.
DR   Pfam; PF01663; Phosphodiest; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053012};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..678
FT                   /note="Nucleotide pyrophosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006936070"
FT   TRANSMEM        651..670
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          590..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        611..636
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   678 AA;  71075 MW;  C699645E48C6F90A CRC64;
     MAVAAAALLL GATGVGGAVA SPAQADTPAA EGAKTPKTLV VGIDGASFDI MSPESTPTVT
     AIRNGGLTGT SNLPGNPMAP TVSGPGWSTI ATGTWPTKHN VVNNNFTNPQ YDKFPDYLTR
     VEQNLPDRST NVVGTWGPIS TTIFGAAVDS RAQFANDTLT TQAAVETLAA PATDDLFVHL
     DEVDGAGHGS GATSQAYREA LLKADGQIAQ MVETIKSRAS YHSEDWMIVI TSDHGHKPTG
     GHGDSTKLER KTFVAAQGSH FAPGTERHDV KISDIAPSVL SHIGIANDPA WELDGSVIHD
     IQPDDFDSLR PLLQPAVQEQ GPENLLGWTN TAPEGWSIDN SKMPSGGAPE FSGWTFMTDD
     FFSNVELGQY RENNVHSRNV FAVADSDEWA DVSPKGGNTF DSTLKSPAYE LNGSEKLDIS
     FVSDYAVDDP QKAIVWVAFD EASGIAPHEL VTYQPEGSRL NPVNRVERFT LDLPRGENGE
     LPQTASLHFE YAATNAAFWV IDQVRVSQAD VPAAPAEFAL SGTTVEAGKP LTATGTGFAA
     HEELAFELRS APQALGTTNA DEAGAFSHEL TIPATTPAGE HTVVAVRADG TELSQPVSVT
     AAPSTGGENP GEEKPGEEKP GEEKPDAEKD PAAKDPAASE QPDLAATGGS IAGIAIAATA
     ILGAGAYLVV RSRRRVTE
//
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