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Database: UniProt
Entry: M7XJ04_RHOT1
LinkDB: M7XJ04_RHOT1
Original site: M7XJ04_RHOT1 
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
//
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