ID F9FWJ1_FUSOF Unreviewed; 498 AA.
AC F9FWJ1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=sphingolipid C(9)-methyltransferase {ECO:0000256|ARBA:ARBA00039020};
DE EC=2.1.1.317 {ECO:0000256|ARBA:ARBA00039020};
GN ORFNames=FOXB_10773 {ECO:0000313|EMBL:EGU78746.1};
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU78746.1};
RN [1] {ECO:0000313|EMBL:EGU78746.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU78746.1};
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(2012).
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:EGU78746.1}.
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DR EMBL; AFQF01002754; EGU78746.1; -; Genomic_DNA.
DR AlphaFoldDB; F9FWJ1; -.
DR STRING; 660025.F9FWJ1; -.
DR PaxDb; 5507-FOXG_11716P0; -.
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 Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 498 AA; 56532 MW; FDE92093A83D0723 CRC64;
MALKQNGGAH LSSDIDFIPT PKAPADSPAI KNAPLPADGP GYEQWSNIFL GVALYGVPQW
LSWKLGGGFK LAIFLAIFTT VPVLVVIWTF MSKLSPRIND KVHLPGRPIE FYLTFKTDQL
RARYTGRHKV PMSKFFELYF TGQVDLNADA LEVFEYRHDW ATFNFTSETF NYILFTFFPD
VILHLRSQDE EQVRTNYDSG NDHYAWFLGP RMIYTSGIIS DPDREETLEE MQDNKLAIVC
EKINIKPGDR VLDIGCGWGT LAKFASLNYG ANVTGVTLAR NQVQWGNDGL RKAGVSEEQS
RLLCCDYRDI PEQKFDKITQ LEMAEHVGVR RLTGFFRQCY EMLEDDGAMY VQLSGLRKAW
QYEDFIWGLF LNKYIFPGAD ASTPLSFYVG CLESAGFEVK SVDTVGVHYS GTLWRWYRNW
LGNAEKVKAK YGVRWFRIWE IFLAYSTIAS RQGSATCFQI VVVKNLNSTQ RINGVYSQYG
LQGALEAARA AGKAVLPK
//
