ID A0A318Z160_9EURO Unreviewed; 512 AA.
AC A0A318Z160;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=sphingolipid C(9)-methyltransferase {ECO:0000256|ARBA:ARBA00039020};
DE EC=2.1.1.317 {ECO:0000256|ARBA:ARBA00039020};
GN ORFNames=BP01DRAFT_360792 {ECO:0000313|EMBL:PYH41041.1};
OS Aspergillus saccharolyticus JOP 1030-1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450539 {ECO:0000313|EMBL:PYH41041.1, ECO:0000313|Proteomes:UP000248349};
RN [1] {ECO:0000313|EMBL:PYH41041.1, ECO:0000313|Proteomes:UP000248349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JOP 1030-1 {ECO:0000313|EMBL:PYH41041.1,
RC ECO:0000313|Proteomes:UP000248349};
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; KZ821271; PYH41041.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A318Z160; -.
DR STRING; 1450539.A0A318Z160; -.
DR OrthoDB; 5484439at2759; -.
DR Proteomes; UP000248349; 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:PYH41041.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248349};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PYH41041.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 63..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 88..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 512 AA; 58068 MW; ACEA9AA4DC2FA49B CRC64;
MSPPAPKNVN LPNDIEYIPT PPPQPSAFAA DDHDGGVALT TSPTLHNPSL PVDGPGNESF
SNLWLISALV GIPALLTWTI GGGMKTGVCL GLVTLFPILI AFWTYTSSCS PPTNTKVKLP
CRPIEQYVTF KKEADRAKWH GRNKVPLQTF CEMYLDGEVD FNGDCLDIME YRHDWANFRF
TWELFKYILL TFARDVLFHT KSQDEEQIRP NYDRGNDHYA WFLGPRMVYT SGIISDPDRE
ETLEEMQDNK MAIVCEKLCL KEGETMLDIG CGWGTLAKFA SLNYGAKVTG LTIAQHQTAW
GNEALRTAGV PEAQSRILCM DYRDIPRTQY DKITQIEMGE HVGIRKLSTF FRQCYDLLKD
DGAMYVQLSG LRQAWQYEDL IWGLYLNKYI FRGADASTPL WYYVLAMERA GFEIKSIDTV
GVHYSGTLWR WYRNWSGNAE TIKATYGQRW FRIWELFLAW SVIASRQGSA TCYQFVVVKN
LNSTHRINGV SSQFGLLAAL AASRMAGKSR LT
//
