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
//