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
//