UniProt: A0A166SWE5

Database: UniProt
Entry: A0A166SWE5_9PEZI

LinkDB:  A0A166SWE5_9PEZI 
Original site:  A0A166SWE5_9PEZI

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (5)   
   InterPro (2)   
   Pfam (1)   
   PROSITE (1)   
   SMART (1)   
All databases (10)   

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ID   A0A166SWE5_9PEZI        Unreviewed;       683 AA.
AC   A0A166SWE5;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Lysophospholipase {ECO:0000256|ARBA:ARBA00013274, ECO:0000256|RuleBase:RU362103};
DE            EC=3.1.1.5 {ECO:0000256|ARBA:ARBA00013274, ECO:0000256|RuleBase:RU362103};
GN   ORFNames=CT0861_12097 {ECO:0000313|EMBL:KZL71292.1};
OS   Colletotrichum tofieldiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL71292.1, ECO:0000313|Proteomes:UP000076552};
RN   [1] {ECO:0000313|EMBL:KZL71292.1, ECO:0000313|Proteomes:UP000076552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0861 {ECO:0000313|EMBL:KZL71292.1,
RC   ECO:0000313|Proteomes:UP000076552};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA   Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA   Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA   O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely related
RT   pathogenic and mutualistic fungi.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC         H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC         ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC         Evidence={ECO:0000256|RuleBase:RU362103};
CC   -!- SIMILARITY: Belongs to the lysophospholipase family.
CC       {ECO:0000256|ARBA:ARBA00008780, ECO:0000256|RuleBase:RU362103}.
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:KZL71292.1}.
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DR   EMBL; LFIV01000075; KZL71292.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166SWE5; -.
DR   STRING; 708197.A0A166SWE5; -.
DR   OrthoDB; 1826981at2759; -.
DR   Proteomes; UP000076552; Unassembled WGS sequence.
DR   GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR   GO; GO:0009395; P:phospholipid catabolic process; IEA:InterPro.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002642; LysoPLipase_cat_dom.
DR   PANTHER; PTHR10728; CYTOSOLIC PHOSPHOLIPASE A2; 1.
DR   PANTHER; PTHR10728:SF33; LYSOPHOSPHOLIPASE 1-RELATED; 1.
DR   Pfam; PF01735; PLA2_B; 1.
DR   SMART; SM00022; PLAc; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS51210; PLA2C; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00555,
KW   ECO:0000256|RuleBase:RU362103};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963, ECO:0000256|PROSITE-
KW   ProRule:PRU00555};
KW   Lipid metabolism {ECO:0000256|PROSITE-ProRule:PRU00555,
KW   ECO:0000256|RuleBase:RU362103};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076552};
KW   Signal {ECO:0000256|RuleBase:RU362103}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT   CHAIN           24..683
FT                   /note="Lysophospholipase"
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT                   /id="PRO_5007748971"
FT   DOMAIN          38..593
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
FT   REGION          625..661
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        645..659
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   683 AA;  72800 MW;  A4C44841D7189F87 CRC64;
     MAILDRYSLA CVLVLAGLAA AQGQGEGGVD PFALVYAECP SGLRVRPASE GLSRTESSWR
     VSRGEKVIPA LNSYLTLANI DGFDVRGYIQ RLNTSNFPVV GLSISGGGTQ SGIGGLGIWQ
     AFDDRNPAAV AARTGGLTQV LTYITGLSGG GALTVSTLAA NDFITIEALR KQINFTVDYT
     VGPDGNQTAY LTEIFENLGA KAETGLPVSV ADAFGQFWGV YLPENRMYGN YSDLTLPGTG
     FSQGESPMPI ISLSEVIPGQ SPSIGGIMWP GRNATNGFNL TSYEVTPFEF GSWRGGRIQA
     FMPTMYLGTS MTNGTAQNTS ECIQGFDKFT FIQGSTANAF DAWFIDEWYD TPIFAKRQLR
     TGPPTSDSIT HLPSSRTTDT AQFFNQTFNE SLWATYPNPF ENYSPAMQDV DELLLIDGSL
     GGETNPIRPL IIPERQVDFI IVYEASSDAE YNWVNGTNLV NTAQSAAQGN IPFPRIPDVA
     TLVTQNLTKQ PTFFGCDAAT SPPTPLVLYL PNSPWSGYIN FTFFKSSFTD NEFDLTADNA
     FNLATYGNGT IDPSWPACLA CATIRGSLTR LGIELPEKCQ ECFRRHYWNG SVATRTVTPE
     DLNPSLRLNS SLSYAEWNQT YWNSQTSTGG SSGGNGGGGG GSGGGGATPS SSPNPSGASA
     TAEIGRAAAA VTVASIIALI ALL
//

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