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Database: UniProt
Entry: A0A239PD90_9ACTN
LinkDB: A0A239PD90_9ACTN
Original site: A0A239PD90_9ACTN 
ID   A0A239PD90_9ACTN        Unreviewed;       652 AA.
AC   A0A239PD90;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=GDSL-like Lipase/Acylhydrolase family protein {ECO:0000313|EMBL:SNT64574.1};
GN   ORFNames=SAMN05421812_117109 {ECO:0000313|EMBL:SNT64574.1};
OS   Asanoa hainanensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Asanoa.
OX   NCBI_TaxID=560556 {ECO:0000313|EMBL:SNT64574.1, ECO:0000313|Proteomes:UP000198362};
RN   [1] {ECO:0000313|EMBL:SNT64574.1, ECO:0000313|Proteomes:UP000198362}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.5593 {ECO:0000313|EMBL:SNT64574.1,
RC   ECO:0000313|Proteomes:UP000198362};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FZPH01000017; SNT64574.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239PD90; -.
DR   OrthoDB; 5503950at2; -.
DR   Proteomes; UP000198362; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR   InterPro; IPR037460; SEST-like.
DR   InterPro; IPR013830; SGNH_hydro.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   PANTHER; PTHR37981; LIPASE 2; 1.
DR   PANTHER; PTHR37981:SF1; SGNH_HYDRO DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13472; Lipase_GDSL_2; 1.
DR   SUPFAM; SSF52266; SGNH hydrolase; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR637460-2};
KW   Hydrolase {ECO:0000313|EMBL:SNT64574.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198362};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        35..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        64..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        92..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        155..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        190..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        215..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        238..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        614..635
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          273..544
FT                   /note="SGNH hydrolase-type esterase"
FT                   /evidence="ECO:0000259|Pfam:PF13472"
FT   ACT_SITE        277
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637460-1"
FT   ACT_SITE        536
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637460-1"
FT   DISULFID        299..324
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637460-2"
FT   DISULFID        392..398
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637460-2"
FT   DISULFID        447..499
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637460-2"
SQ   SEQUENCE   652 AA;  69700 MW;  A099EF1071631994 CRC64;
     MDAVDGSALR RLLVFAAALA AFLALAGSGS STLTIQVLFT IFVIAATIWV RGQYLDSLDD
     RQWLVSWRVG LALALVGAAM VVSYAFWPMR GVALAGAIVA YFVAGSAITW LRQGMRSDRR
     RLTLGVTFTG AGVVLAIAGL ALLGRSSGRA VYAELAFLGL AFFALLPVGV ALLSEVVIRR
     LCGSGRKLRL GTGLSGLALL LVSAALLFAY TRSPWLLGAI VVAGLMMVAL VSTTQADVAF
     VLGVIALLGV TPTPEDLPPA LRTDRTASSL LVAIGDSYMS GEGASRYYAG TDVGGDNQCR
     RSPSAWAAMA GQQPPFGRLE FLACSGARTW NVQSAARPVR PEAPVPSAPD GEEATQLDLH
     TRNYADAAFA PAMVVVSLGG NDAGFSTIGL MCLAPGNCGD QAHLWTDSLP QVKLALRDTY
     QHISDVFPRT PVVVVPYPDP IHLTGTCDDV ALSIGERRFL HDYVTNGLNR VLRETAREFG
     FYYLAEMESA LATAHLQLCD ELNGGRPGLH FIGVRSVAGV AEQRFNPKNW SHSSLHPNER
     GHAAMLRTFQ TWLPALDTML IRTTAVGRYD SGRAAPAAVQ AVPQCDLLDT TTAGCRTQGM
     RWAKSQVRTT AWTYGWLLLF PLAGTWAAAV AFFAWQRRRL ATEAAANRTK AD
//
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