ID A0A319ARJ8_ASPLB Unreviewed; 510 AA.
AC A0A319ARJ8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=sphingolipid C(9)-methyltransferase {ECO:0000256|ARBA:ARBA00039020};
DE EC=2.1.1.317 {ECO:0000256|ARBA:ARBA00039020};
GN ORFNames=BO96DRAFT_355445 {ECO:0000313|EMBL:PYH62909.1};
OS Aspergillus lacticoffeatus (strain CBS 101883).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1450533 {ECO:0000313|EMBL:PYH62909.1, ECO:0000313|Proteomes:UP000247441};
RN [1] {ECO:0000313|EMBL:PYH62909.1, ECO:0000313|Proteomes:UP000247441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101883 {ECO:0000313|EMBL:PYH62909.1,
RC ECO:0000313|Proteomes:UP000247441};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000256|ARBA:ARBA00004760}.
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000256|ARBA:ARBA00004991}.
CC -!- SIMILARITY: Belongs to the CFA/CMAS family.
CC {ECO:0000256|ARBA:ARBA00010815}.
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DR EMBL; KZ821338; PYH62909.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319ARJ8; -.
DR OrthoDB; 5484439at2759; -.
DR Proteomes; UP000247441; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR45197:SF1; SPHINGOLIPID C9-METHYLTRANSFERASE A-RELATED; 1.
DR PANTHER; PTHR45197; SYNTHASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G04190)-RELATED; 1.
DR Pfam; PF02353; CMAS; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Methyltransferase {ECO:0000313|EMBL:PYH62909.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PYH62909.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 85..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 510 AA; 57842 MW; 6E0D3335EAC4EF80 CRC64;
MTTKSKDVEL SDDIQFIETP APAPPKFETG ESCGVALTNA KSINNPPLPA DGPGNESFSN
LLLGGAIIGV PGFLTYLLGG GKKTFVFFTL VTVLPVLVAF WTYTSTFSPR TNEKVKLPGR
PVEHYITFKR DEDRAKWSGR NKIPMQTFSE MYLDGLVDFN GDVLEILEYR HDWASFAFTW
DLFKFIVGTF FVDVLFHTKA QDEEQIRPNY DRGNDHYAWF LGPRMIYTSG IISDPDREET
LEELQDNKMA VVCEKIGLKE GETMLDIGCG WGTLAKFASL NYGAKVTGLT IAENQTAWGN
DALRKAGISE EQSRIVCMDY RDIPRTKYDK ITQLEMGEHV GIRKLTGFFR QCYDMLNDDG
CMYVQLSGLR QAWQYEDFIW GLYLNKYIFR GADASTPLWY YVKCLEGAGF EVKGIDTVGV
HYSGTLWRWY RNWVGNIEAI KAKYGPRWYR IWELFLAWSV IASRQGSATC YQMVVVKNLN
STHRITGVSN QYGLMGALAK SREAGKSRLP
//
