ID M7XJ04_RHOT1 Unreviewed; 483 AA.
AC M7XJ04;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-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=RHTO_06933 {ECO:0000313|EMBL:EMS23874.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS23874.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS23874.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS23874.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(2012).
CC -!- SIMILARITY: Belongs to the CFA/CMAS family.
CC {ECO:0000256|ARBA:ARBA00010815}.
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DR EMBL; KB722646; EMS23874.1; -; Genomic_DNA.
DR RefSeq; XP_016274993.1; XM_016420592.1.
DR AlphaFoldDB; M7XJ04; -.
DR GeneID; 27370946; -.
DR eggNOG; ENOG502QS47; Eukaryota.
DR HOGENOM; CLU_026434_5_0_1; -.
DR OrthoDB; 5484439at2759; -.
DR Proteomes; UP000016926; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
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; SYNTHASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G04190)-RELATED; 1.
DR PANTHER; PTHR45197:SF1; 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:EMS23874.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EMS23874.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 31..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 483 AA; 55330 MW; D5C373A7260A7285 CRC64;
MAATYDPTVG LKVTHRAAIA NAPFPVEGNG SFSNVQLAAA VLIVPYFLSR FVPYFSFRTT
YVFLLLVTGI PTTIAYWLLM SRANVRVRDS GIFPGKDIEH YITSKDAELR EKYNGQKKIP
MQVFHDAYFE GKIDIKGDML ELLEWRHDWM SFPMTLELMK YVLTKLIPDV IFHSAGQDEE
QVTDHYDRGD DFHEWFLGPR MIYTSGIIHD VDRKETLEEL QDNKLAVVCQ KLQLKPTDTL
LDIGCGWGTL VTYAAKNYGC DATGVTLSKN QAEFGTKRIA ANGVDASRAR ILRTDFRNLD
KSKKFTKIVS LEMAEHVGIR RYNTFLRDVY NLLDDDGILV FQVAGIRPSW QYEDLIWGLF
MNKYVFPGAD ASCALNWVIG RLENAGFEVT NVDVLGVHYS ATLHRWYENW IKNKENVLAK
YGERWYRVWL YFLASSVITS RQGGASVFQI TLHKNLNGYH RVDDIPSHTN IFPKLEKEPQ
LVV
//