ID A0A316VY27_9BASI Unreviewed; 596 AA.
AC A0A316VY27;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=sphingolipid C(9)-methyltransferase {ECO:0000256|ARBA:ARBA00039020};
DE EC=2.1.1.317 {ECO:0000256|ARBA:ARBA00039020};
GN ORFNames=IE81DRAFT_304030 {ECO:0000313|EMBL:PWN41201.1};
OS Ceraceosorus guamensis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX NCBI_TaxID=1522189 {ECO:0000313|EMBL:PWN41201.1, ECO:0000313|Proteomes:UP000245783};
RN [1] {ECO:0000313|EMBL:PWN41201.1, ECO:0000313|Proteomes:UP000245783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4658 {ECO:0000313|EMBL:PWN41201.1,
RC ECO:0000313|Proteomes:UP000245783};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
CC -!- SIMILARITY: Belongs to the CFA/CMAS family.
CC {ECO:0000256|ARBA:ARBA00010815}.
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DR EMBL; KZ819397; PWN41201.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316VY27; -.
DR STRING; 1522189.A0A316VY27; -.
DR InParanoid; A0A316VY27; -.
DR OrthoDB; 5484439at2759; -.
DR Proteomes; UP000245783; 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:PWN41201.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245783};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PWN41201.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 23..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 596 AA; 66683 MW; B0A237AFF493486A CRC64;
MSEQTQQAAL DALAYQRAQL QAQEAHLAQQ VAPSSPSTAS VGSPVNPSTP ARSSMGAAAA
NGSPLATSNP FTTSAGPQSP TIPRKDPKRA SIAAGAGFNP LEAAASGAQS TRYAPGGKVR
LTDYATIANA PLPAEGNGTF SNLHLALLVF FTPAILLRVI PFFKASWVPW WLYWILVIVI
GAPVTIGYWT FMSICGPRKN EKVNLPGKPV EDYITIHDAE LKRKYHGRNK IPMQPFHDAY
FDGKIDIKGD MLDLLEHRLD WSHMHFTPEL FKFVLTVLVP DVIRHTEKQD MEQVRDHYDR
GDDFYEWFLG PQMIYTSGMI SDPRRKETLE ELQDNKMAAV CNKLQLQPSD KVLDIGCGWG
TLTAFAAKNF GCDVTGVTLA KNQTKFGNER IAKAGLSSDK ARVLCMDYRD IPVEKGYYNK
IVSLEMAEHV GIRHYSKFLA DIHERLDDDG TFLLQVAGIR PTWQYWDLIW GLFMNKYIFR
GADASCAIGW VINKLEAAGF EVQSADVLGV HYSATILRWY ENWKSNEAKI KAKYGEKLWR
IWLYFLASSV IIAREGGSSV FQITSKKNLN ATDRVSFWEG RIQPSKYQSV YTPAQY
//
