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Database: UniProt
Entry: A0A0Q5R1N0_9SPHN
LinkDB: A0A0Q5R1N0_9SPHN
Original site: A0A0Q5R1N0_9SPHN 
ID   A0A0Q5R1N0_9SPHN        Unreviewed;       343 AA.
AC   A0A0Q5R1N0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=PNPLA domain-containing protein {ECO:0000259|PROSITE:PS51635};
GN   ORFNames=ASG11_04765 {ECO:0000313|EMBL:KQS03640.1};
OS   Sphingomonas sp. Leaf357.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736350 {ECO:0000313|EMBL:KQS03640.1, ECO:0000313|Proteomes:UP000051080};
RN   [1] {ECO:0000313|EMBL:KQS03640.1, ECO:0000313|Proteomes:UP000051080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf357 {ECO:0000313|EMBL:KQS03640.1,
RC   ECO:0000313|Proteomes:UP000051080};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQS03640.1, ECO:0000313|Proteomes:UP000051080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf357 {ECO:0000313|EMBL:KQS03640.1,
RC   ECO:0000313|Proteomes:UP000051080};
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   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01161}.
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:KQS03640.1}.
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DR   EMBL; LMPM01000001; KQS03640.1; -; Genomic_DNA.
DR   RefSeq; WP_055775810.1; NZ_LMPM01000001.1.
DR   AlphaFoldDB; A0A0Q5R1N0; -.
DR   STRING; 1736350.ASG11_04765; -.
DR   OrthoDB; 9807112at2; -.
DR   Proteomes; UP000051080; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 2.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR021095; DUF3734.
DR   InterPro; IPR002641; PNPLA_dom.
DR   PANTHER; PTHR14226:SF57; BLR7027 PROTEIN; 1.
DR   PANTHER; PTHR14226; NEUROPATHY TARGET ESTERASE/SWISS CHEESE D.MELANOGASTER; 1.
DR   Pfam; PF12536; DUF3734; 1.
DR   Pfam; PF01734; Patatin; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS51635; PNPLA; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01161};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963, ECO:0000256|PROSITE-
KW   ProRule:PRU01161};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|PROSITE-
KW   ProRule:PRU01161}; Reference proteome {ECO:0000313|Proteomes:UP000051080}.
FT   DOMAIN          15..218
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000259|PROSITE:PS51635"
FT   MOTIF           46..50
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT   MOTIF           205..207
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        48
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        205
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
SQ   SEQUENCE   343 AA;  36870 MW;  37C3A0083488BAD4 CRC64;
     MTNGMGPQRD FDVVLALSGG NALGAFEAGA YQALHEHDLF PDWIVGASIG AINGALIAGS
     AMADRLGTLR DFWQPESFGL GAPGTPWLPS AMDVARRCTA AMSTMMLGRA GLFGPLLSSL
     TPWTDDQPSL FETEQLAATL DRLVDFDLLN RGECRYTSTA VDLATGDDVV FDSRSGTIDS
     RHVRASAALP MLFPPLEIDG RWLIDGGISA NLPLDPILSS PGARPQLCLA VDLLPLGQVL
     PATVGEAASR MQDLIFAAQS RRTLERWRMA HAGNDEISLT LVRIAYADQG DEVAGKAMDF
     SGPTIERRWA AGYKTMLNVI ERLHDGSLQP VQHGFHVPEL ETT
//
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