ID A0A1H4XQI2_9PSEU Unreviewed; 489 AA.
AC A0A1H4XQI2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=GDSL-like Lipase/Acylhydrolase family protein {ECO:0000313|EMBL:SED07827.1};
GN ORFNames=SAMN04489727_6310 {ECO:0000313|EMBL:SED07827.1};
OS Amycolatopsis tolypomycina.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=208445 {ECO:0000313|EMBL:SED07827.1, ECO:0000313|Proteomes:UP000199622};
RN [1] {ECO:0000313|EMBL:SED07827.1, ECO:0000313|Proteomes:UP000199622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44544 {ECO:0000313|EMBL:SED07827.1,
RC ECO:0000313|Proteomes:UP000199622};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FNSO01000004; SED07827.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4XQI2; -.
DR STRING; 208445.SAMN04489727_6310; -.
DR OrthoDB; 9801375at2; -.
DR Proteomes; UP000199622; Unassembled WGS sequence.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd01831; Endoglucanase_E_like; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR018366; CBM2_CS.
DR InterPro; IPR040794; CE2_N.
DR InterPro; IPR037461; CtCE2-like_dom.
DR InterPro; IPR001087; GDSL.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR PANTHER; PTHR37834; GDSL-LIKE LIPASE/ACYLHYDROLASE DOMAIN PROTEIN (AFU_ORTHOLOGUE AFUA_2G00620); 1.
DR PANTHER; PTHR37834:SF2; PUTATIVE-RELATED; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF17996; CE2_N; 1.
DR Pfam; PF00657; Lipase_GDSL; 1.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF52266; SGNH hydrolase; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00561; CBM2_A; 1.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SED07827.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..489
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011604667"
FT DOMAIN 32..141
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 139..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 489 AA; 51463 MW; 5DCADD7EEA47E83C CRC64;
MSPTRHGKRA AVAAAVTLVS AVATGITVGT APAQAAAGCR VTYQVASQWQ GGFTADVDVT
NLGDPVTGWQ LTWSFGAGQR VTQLWNGTVA QSGAQVTVGN AGWNGTLGAG ASAGLGFLGS
WTGANPVPTD FALNGTRCNG PTPTPTPTTT TTTPPADSLA RTHTVGRVKV AGDVAQYTWP
GIYFEGRFRG TGVGVVLNDA TNDYDVQVDG TTVATLVTPG RTTYQVRGLT DAEHRVRLVK
RTESPWAAGE FGGFVASPGG EILAKPAARS RQIEFIGDSL TAGYGNLSTT RDCSGNGGID
RNTDTDLSYG ALTARGLDAD YQINAQSGRG MVRNYNGGDP GTDFRTAYDR TLQNAAADVW
HNPATWRPQL VVVALGTNDF STAINPGEPW TPDSLVAAYQ SAYQGFLGKL RAQYGAEAII
VVGATNLYAQ PAQQVVTDRN ARGDSRVRFW NFDDPGLDHL GCDWHFSLAD HRLISGSLAR
YVAGLPLTW
//
