ID A0A1V6Q778_9EURO Unreviewed; 517 AA.
AC A0A1V6Q778;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=sphingolipid C(9)-methyltransferase {ECO:0000256|ARBA:ARBA00039020};
DE EC=2.1.1.317 {ECO:0000256|ARBA:ARBA00039020};
GN ORFNames=PENANT_c011G06471 {ECO:0000313|EMBL:OQD85094.1};
OS Penicillium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD85094.1, ECO:0000313|Proteomes:UP000191672};
RN [1] {ECO:0000313|Proteomes:UP000191672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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}.
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:OQD85094.1}.
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DR EMBL; MDYN01000011; OQD85094.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6Q778; -.
DR STRING; 416450.A0A1V6Q778; -.
DR OrthoDB; 5484439at2759; -.
DR Proteomes; UP000191672; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; 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 Reference proteome {ECO:0000313|Proteomes:UP000191672};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 54..72
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 79..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 517 AA; 58799 MW; 34DBDBD5EBE67436 CRC64;
MTTIHPDSTE EFEFIQTPAA PEQIKPAFDC GVPTTLYPAI KNAPVPADSP GSDSFSNGLM
IFLVVVVPWW LARQVGGGFY TTIFFAIFTT IPVLMAFWTV SSSISPRKTE KAKYCGRPVE
HYLHFHSEHD RATYRGKSKI PMEVFYEKYF NGEVDFKGDA LECLEYRHDW ANFKFTMGLF
KHFLFGFIPE MLMHTRSQDE EQVRDHYDRG DDFYAWFLGP RMIYTSGVIS DINKEETLEE
LQDNKLAIVC EKIGVKPGDK VLDLGCGWGT LAKYASAHYG AHVTGITLGR NQTAWGNNGL
RKAGIEEDQS RILCSDYRDA PRVEGGYQQI TCLEMAEHVG VRHFSSFLSQ VYDMLDDNGT
FFLQIAGLRK SWQYEDLIWG LFMNKYIFPG ADASTPLGFV VDRLEGAGFE IKAVDTIGVH
YSATLWRWYR NWMGNRDKVE AKYGKRWFRI WEYFLAASTI TSRQGGATCW QLTLVKNINS
THRIDGIATQ HGLTGARQNA IDRAGTLPKA HIIKKDL
//
