ID A0A1I7I4X2_9CLOT Unreviewed; 811 AA.
AC A0A1I7I4X2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Lipase (Class 3) {ECO:0000313|EMBL:SFU67997.1};
GN ORFNames=SAMN04487886_109914 {ECO:0000313|EMBL:SFU67997.1};
OS Clostridium sp. DSM 8431.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1761781 {ECO:0000313|EMBL:SFU67997.1, ECO:0000313|Proteomes:UP000198524};
RN [1] {ECO:0000313|EMBL:SFU67997.1, ECO:0000313|Proteomes:UP000198524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8431 {ECO:0000313|EMBL:SFU67997.1,
RC ECO:0000313|Proteomes:UP000198524};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FPBY01000099; SFU67997.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7I4X2; -.
DR OrthoDB; 6372180at2; -.
DR Proteomes; UP000198524; Unassembled WGS sequence.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR CDD; cd00519; Lipase_3; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002921; Fungal_lipase-like.
DR PANTHER; PTHR45856; ALPHA/BETA-HYDROLASES SUPERFAMILY PROTEIN; 1.
DR PANTHER; PTHR45856:SF11; LIPASE_3 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000198524};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..811
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038529847"
FT DOMAIN 495..630
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
FT REGION 63..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 811 AA; 90848 MW; 3BFA63579D8B0674 CRC64;
MKRKKLIGKL LLLTMSVLLV SNINMKAINN TNEKETEKNY DEDNTVVSTS IADNPVLSDI
SKIEINSKDE IPSKNSNKNI GKEEGKDNDN DGLSDGLEEI FGADPEKLDT DDDGLDDYLE
VKMGLSPNSV DTDNNGINDI DEDIDKDGLV NGEEIKNGTS PTEEDTDKDG IKDSDEVNRF
KTSPVKADTD GDNIYDGDER KLGLDPNKIS TDGITNDNER KINQNLSEEG MSTILLENPK
DFKVSINGQV SGCIDRDVFV SEYDITPIEN VRGVKDGAIE ISSQKEKMDE LTLKFNYEEY
KEADIDNLCI CNYKDEEFKL LDTNIDKDNK ILSSDITDEG IYLVVNKEEY EETPVVLNEE
SYSFAKSEAA VNTDTDYDGI ENSSDSNPTN NSFSGKLKTK FATSKVSYTM DYRNFFATNK
QYNRNIAEIS SLFSTVIYPG STYNGLDISG FMALHGIKDI TNYNLSTRYN DSDLSEIYIG
HKNVTYNGVT KEIIVIVVRG TNGSIEEWTS NFDVGSTLEK SRFVDWKVTA NHKGFDTAAT
RILKFLDEYE NKSFIDKNAS KTYWVTGHSR GASIANVLGA RLDDGSKDVY AYTFASPATT
TASNAEDTNA YPGIFNVLNK DDLIPYLPTK QWGFKHYGKS YKISIASNYE KEWETLTDIW
DYDNDYFGMD DTVNALAGIM KTRNDAYVYT CKCHGDGSSN NITIRNYGMS KNSREEAIAK
IPSNALSYCA ITRYTGKWIA GWDFTVCQQP EYFMQLLAAF MANKINAYRF GVELNIADRY
EKAKTGIIKS GIGGLAHPHY PESYYLLAKH I
//