GenomeNet

Database: UniProt
Entry: F4S8K1_MELLP
LinkDB: F4S8K1_MELLP
Original site: F4S8K1_MELLP 
ID   F4S8K1_MELLP            Unreviewed;       574 AA.
AC   F4S8K1;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE            EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN   ORFNames=MELLADRAFT_94935 {ECO:0000313|EMBL:EGF99004.1};
OS   Melampsora larici-populina (strain 98AG31 / pathotype 3-4-7) (Poplar leaf
OS   rust fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Melampsoraceae; Melampsora.
OX   NCBI_TaxID=747676 {ECO:0000313|Proteomes:UP000001072};
RN   [1] {ECO:0000313|Proteomes:UP000001072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=98AG31 / pathotype 3-4-7 {ECO:0000313|Proteomes:UP000001072};
RX   PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA   Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA   Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA   Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA   Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA   Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA   Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA   Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA   Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA   Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA   Grigoriev I.V., Szabo L.J., Martin F.;
RT   "Obligate biotrophy features unraveled by the genomic analysis of rust
RT   fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
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   ---------------------------------------------------------------------------
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; GL883165; EGF99004.1; -; Genomic_DNA.
DR   RefSeq; XP_007417696.1; XM_007417634.1.
DR   AlphaFoldDB; F4S8K1; -.
DR   STRING; 747676.F4S8K1; -.
DR   EnsemblFungi; EGF99004; EGF99004; MELLADRAFT_94935.
DR   GeneID; 18937071; -.
DR   KEGG; mlr:MELLADRAFT_94935; -.
DR   VEuPathDB; FungiDB:MELLADRAFT_94935; -.
DR   eggNOG; KOG1325; Eukaryota.
DR   HOGENOM; CLU_014602_1_0_1; -.
DR   InParanoid; F4S8K1; -.
DR   OrthoDB; 1826981at2759; -.
DR   Proteomes; UP000001072; 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; 2.
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; 2.
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:UP000001072};
KW   Signal {ECO:0000256|RuleBase:RU362103}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT   CHAIN           22..574
FT                   /note="Lysophospholipase"
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT                   /id="PRO_5005129571"
FT   DOMAIN          34..569
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
SQ   SEQUENCE   574 AA;  62616 MW;  20E975E645C5C4B4 CRC64;
     MLSYFYITLL ILFSSTLICH TQTPAHSYAP IRTKCPSGSF MRYAGTVERR NQRLGDKEAY
     YMEQRRQKVI PGAYRAYLSN VENSLRSRSR RLPRYVSKIL RGDNIDRPHV SVAVSGGGLR
     ASYFGAGVLN ALDGRNSTSV KVGTGGLLQA FDYITGLSGA ACLVMSLAQA NFPDMYELSL
     GPRDPRVVPE ESDAFIGSTR GWLTDISYIT PGALNLAQDG LWWAEISGDV EEKAAAGFKV
     SLADMYARIL AYHYVNGTSH ENYFDPGAPH GQAETLSSLA RAVPTLRNYS QPLALITSIA
     ESPGEGRDNI LQGAAVPITN NQYEFSMFEV GSWDSNLATF IDTAYLGSQP GRKDCVKNYD
     NLGFMVAASA NVLKKADNLL GALSTKGYFP ILPRIEGFLS LVPNPFKENL PFAPLLVPAR
     KVDVILALDA SDDLDMGYPT GDALLATAQR SRIFPNKAYP FPDVKNVSRL HRTRPSFVGC
     TDLPGTPLII YIPNAPPVPK VQTAALELSR ATSLAVLDSS TQLAFTKDPL WSGCLACAVV
     DRARARAKKR RVGLCADCFS RYCYDGQAGK YTDV
//
DBGET integrated database retrieval system