ID A0A093XGG7_TALMA Unreviewed; 517 AA.
AC A0A093XGG7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=sphingolipid C(9)-methyltransferase {ECO:0000256|ARBA:ARBA00039020};
DE EC=2.1.1.317 {ECO:0000256|ARBA:ARBA00039020};
GN ORFNames=GQ26_0290670 {ECO:0000313|EMBL:KFX44323.1};
OS Talaromyces marneffei PM1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX44323.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|Proteomes:UP000029285};
RX PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA Lin X.;
RT "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT of Dimorphic Transition in Penicillium marneffei.";
RL PLoS Genet. 10:e1004662-e1004662(2014).
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:KFX44323.1}.
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DR EMBL; JPOX01000029; KFX44323.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093XGG7; -.
DR eggNOG; ENOG502QS47; Eukaryota.
DR HOGENOM; CLU_026434_5_0_1; -.
DR Proteomes; UP000029285; 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:KFX44323.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KFX44323.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 53..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 517 AA; 58640 MW; 3CDC57511CC9F53A CRC64;
MARTHSESSE DFEFIETPPA PASPVPEDCG VRTTSFPAIK NAPLPADSAG SDSFSNVLLI
ILLIGVPFYI ARQFRGGLYT TIFFAIFTTI PILMVFWTVA SAASPRKNEK AKYPGRPVEH
YLEFHSEHDR VKYHGKSKIP MTTFFEKYFD GDVDFKGDAL DILEYRHDWA SFRFTWQLYK
HFLTGFLPEM LIHSRSQDEE QVRDHYDRGD DFYAWFLGPR MIYTSGIISD INKEETLEEL
QDNKLSVVCE KIDLKPGDTM LDLGCGWGTL AKFASVHYGA HVTGITLGRN QTKWGNNGLR
KAGIDESQSK ILCMDYRDAP SITGGYKKIT CLEMAEHVGV RHFGSFLSQV YDMLDDDGVF
FLQIAGLRKS WQYEDLIWGL FMNKYIFPGA DASTPLGFVV DSLEGSGFEI KSIDTVGVHY
SATLWRWYRN WMANREKVEA KYGKRWFRIW EYFLASSTIT SRQGGATCWQ ITLVKNINST
HRVEGIPSQY GLAGARQAAI DHVGHGKLPS AHVSTKE
//
