ID N9P825_9GAMM Unreviewed; 503 AA.
AC N9P825;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=PNPLA domain-containing protein {ECO:0000259|PROSITE:PS51635};
GN ORFNames=F890_02128 {ECO:0000313|EMBL:ENX29563.1};
OS Acinetobacter sp. CIP 64.7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1144673 {ECO:0000313|EMBL:ENX29563.1, ECO:0000313|Proteomes:UP000013258};
RN [1] {ECO:0000313|EMBL:ENX29563.1, ECO:0000313|Proteomes:UP000013258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 64.7 {ECO:0000313|EMBL:ENX29563.1,
RC ECO:0000313|Proteomes:UP000013258};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter sp. CIP 64.7.";
RL Submitted (FEB-2013) 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:ENX29563.1}.
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DR EMBL; APRY01000043; ENX29563.1; -; Genomic_DNA.
DR RefSeq; WP_005251456.1; NZ_KB850179.1.
DR AlphaFoldDB; N9P825; -.
DR PATRIC; fig|1144673.3.peg.2049; -.
DR HOGENOM; CLU_009031_5_1_6; -.
DR OrthoDB; 7055653at2; -.
DR Proteomes; UP000013258; Unassembled WGS sequence.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd07206; Pat_TGL3-4-5_SDP1; 1.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002641; PNPLA_dom.
DR InterPro; IPR021771; Triacylglycerol_lipase_N.
DR PANTHER; PTHR14226; NEUROPATHY TARGET ESTERASE/SWISS CHEESE D.MELANOGASTER; 1.
DR PANTHER; PTHR14226:SF10; TRIACYLGLYCEROL LIPASE 4-RELATED; 1.
DR Pfam; PF11815; DUF3336; 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};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098}.
FT DOMAIN 158..345
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
SQ SEQUENCE 503 AA; 57707 MW; AA87A0EB970207B8 CRC64;
MLFKDFTQDI NPHQAYRIKK LKQQLQQAES YEEWKYIALK IDEESGAQEW KFDNSSPYFD
AEVIAHRLGK LRRYRQQKRT RDLMYILREG LSYDIANIAH PLLFTEAYVG TKRIIEDYVE
EVSQGLAYIA SIDCTCLSME EKIEYFQHCQ RAYGQPALMF SGGSTLGLFH TGVCKALMEQ
DLLPKVMSGS SAGAIMTAML GVSKPSQYID ILKGHNFFHE AFHFRTMSEL MKGNGGLADV
KYLKKFLVEN LGDLTFEEAL KTSGLHINIA VAPYDAGQDA RILNAYTSPD LLVWSAVLAS
CAVPVMFPPV RLTSKRYDGQ YTPYMGSTRW VDGSVRSDFP QEKMARLYNI NYTIASQTNP
HIVPFMQDDI SRFRKGTLTW PQRIVRRQGA VITKGMMDFA REHAGSLPPV RRLLDHGYGV
VDQRYYGDVN IVGKYSLRHY SYMLQNPRPY LFKILQREGE RATWPKISLI ETQERVGKTI
QHCLELLNYQ HTLNPIPEYI ATT
//
