ID V2XXJ5_MONRO Unreviewed; 430 AA.
AC V2XXJ5;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Lipid particle protein {ECO:0000313|EMBL:ESK84109.1};
GN ORFNames=Moror_11421 {ECO:0000313|EMBL:ESK84109.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK84109.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK84109.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK84109.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
CC -!- SIMILARITY: Belongs to the putative lipase ROG1 family.
CC {ECO:0000256|ARBA:ARBA00007920}.
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:ESK84109.1}.
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; AWSO01001369; ESK84109.1; -; Genomic_DNA.
DR RefSeq; XP_007856573.1; XM_007858382.1.
DR AlphaFoldDB; V2XXJ5; -.
DR KEGG; mrr:Moror_11421; -.
DR HOGENOM; CLU_027968_0_0_1; -.
DR OrthoDB; 48091at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR007751; DUF676_lipase-like.
DR InterPro; IPR044294; Lipase-like.
DR PANTHER; PTHR12482:SF62; DUF676 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR12482; UNCHARACTERIZED; 1.
DR Pfam; PF05057; DUF676; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 276..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 3..201
FT /note="DUF676"
FT /evidence="ECO:0000259|Pfam:PF05057"
SQ SEQUENCE 430 AA; 47954 MW; 847C148CAF828B8A CRC64;
MDSVHLLTLV HGMWGNPSHL RELERTIKER EVTDIPLHVI VARTNAEDST YDGIDWGGER
VAKEVIDEVE QLQSDGKKVV KFSITGYSLG GLVSRYVVGI LYQKGFFKDV APVNFNTIAT
PHLGLPRYPS ILSSLYSTLG PKLLSRTGEQ FYCVDKWSNT GKPLLEVMAD PEFVFYKALA
SFQHARIYAN AIYDTTVPYV TAAIETEDPF ADHAKNGIEI KLDENYKPII KSYSLPPVPP
APTPKPVILS PSWFQQRKNK KPSLPPFLKF RFPLNIVFYA MLPILIPVIL ALTVIRLSRD
ARSSRARIKE LEKDATHGQS LARVLAQLER EVEGAVVELM DEAGSGSTST LQGTEISIKV
GKKSKEPAAL SPLQHKIAEQ LNTLPLKKEL AFIDGVFNSH GTIIMRDVKR FPFQIAGEGV
VRHWADSLII
//
