ID A0A3E2GSV4_SCYLI Unreviewed; 1928 AA.
AC A0A3E2GSV4;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=sphingolipid C(9)-methyltransferase {ECO:0000256|ARBA:ARBA00039020};
DE EC=2.1.1.317 {ECO:0000256|ARBA:ARBA00039020};
DE Flags: Fragment;
GN ORFNames=B7463_g12188 {ECO:0000313|EMBL:RFU24150.1};
OS Scytalidium lignicola (Hyphomycete).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Scytalidium.
OX NCBI_TaxID=5539 {ECO:0000313|EMBL:RFU24150.1, ECO:0000313|Proteomes:UP000258309};
RN [1] {ECO:0000313|EMBL:RFU24150.1, ECO:0000313|Proteomes:UP000258309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 105466 {ECO:0000313|EMBL:RFU24150.1,
RC ECO:0000313|Proteomes:UP000258309};
RA Buettner E., Gebauer A.M., Hofrichter M., Liers C., Kellner H.;
RT "Draft genome sequence of Scytalidium lignicola DSM 105466, a ubiquitous
RT saprotrophic fungus.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the PAN1 actin cytoskeleton-regulatory complex
CC required for the internalization of endosomes during actin-coupled
CC endocytosis. The complex links the site of endocytosis to the cell
CC membrane-associated actin cytoskeleton. Mediates uptake of external
CC molecules and vacuolar degradation of plasma membrane proteins. Plays a
CC role in the proper organization of the cell membrane-associated actin
CC cytoskeleton and promotes its destabilization.
CC {ECO:0000256|ARBA:ARBA00025194}.
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000256|ARBA:ARBA00004760}.
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000256|ARBA:ARBA00004991}.
CC -!- SUBUNIT: Component of the PAN1 actin cytoskeleton-regulatory complex.
CC {ECO:0000256|ARBA:ARBA00011159}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004413};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm,
CC cytoskeleton, actin patch {ECO:0000256|ARBA:ARBA00004134}. Endosome
CC membrane {ECO:0000256|ARBA:ARBA00004125}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004125}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004125}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
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:RFU24150.1}.
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DR EMBL; NCSJ02000497; RFU24150.1; -; Genomic_DNA.
DR STRING; 5539.A0A3E2GSV4; -.
DR OMA; PQRTGMQ; -.
DR Proteomes; UP000258309; Unassembled WGS sequence.
DR GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd00052; EH; 2.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EH_dom.
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 Pfam; PF12763; EF-hand_4; 2.
DR SMART; SM00027; EH; 2.
DR SUPFAM; SSF47473; EF-hand; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50031; EH; 2.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000258309};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 53..72
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 81..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 502..528
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 540..561
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 741..829
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 1011..1100
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 1044..1079
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 578..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1139..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1396..1416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1440..1616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1629..1688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1700..1928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1440..1454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1455..1470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1478..1496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1533..1566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1576..1597
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1599..1616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1637..1688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1722..1740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1904..1928
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RFU24150.1"
FT NON_TER 1928
FT /evidence="ECO:0000313|EMBL:RFU24150.1"
SQ SEQUENCE 1928 AA; 211481 MW; 8B7CE3BB8A29FBEF CRC64;
MSVNGSESEF EFIETPKAAT PTFEKFEDCG VRTTSYPAIK NAPLPADASG SDTFSNTLLF
SILFIVPAYM AWKIGGGLKT TIFFAIFTSF PILMAFWTLT SSLSPRKNEK AKFPGRPVEH
YLTFKNEADK LKYSGRNKIP METFHNMYFD GDVDFNGDAL EVMEYRHDWA SFRFTLSLFK
YVLFNFAPEV IMHTRSQDEE QVRDHYDRGD DFYAWFLGPR MIYTSGIISD VNKEETLEQL
QDNKLAIVCE KIDLKEGESL LDIGCGWGTL AKYASVNYGA KVTGVTLGRN QTAWGNNGLR
KAGVTEEQSK ILCMDYRDIP VPEGNYNKIT CLEMAEHVGI RHLTGFLKQV NEMLDDDGVF
FLQVAGLRKY WQYEDLIWGL FMNKYVFPGA DASTPLGFYI SCLESAGFEV KGIDTVGVHY
SATLWRWYRN WMGNRQKVEA KYGKRWFRIW EFFLAYSTIT SRQGGATCYQ ITLVKNLNST
HRVEGISSQF GLSDWISGMG SLTWVTVVCW LGLAIIISQV AGLSFVIAPL HAWHLDRQPF
LPSPLYFILS PSLLASVIIM YSGSNSYLGG NAGRPGPQYG NTFQGNQQTG QSLGYNSQPQ
NFGAAPQLQP NFTGYPLQAQ QTGFQPQQQL SQPGFLGPQP TGQFQQAPQQ QNFQTGVPPI
PQIPQQFQQQ QQQQPPPQAQ FQSQPQPPQV QHQAPQPTGF AQVAASFQNA APPTPAKPKG
RRQGGGAKIP NIRLSFITAS DQAKFEGLFK SAVGDGQALS GDKARDLLLR SKLDGTALSQ
IWQLSDTTKS GQLLFPEFAL AMYLCNQKLI GKTLPSGLPE NIKNEVSSMV DIISFGVADD
APAPAPAGNV PDFNARTTAA SPPAIQQPQP LQSNSALLTA QLTGFPQPQQ GGFPGQQQSL
QFQPTGFQSL SNPQALGYNG PRPPMPPIPT GFNQGLSPAV TGPGGMVAPL NSQPTGRPGQ
WGLVNAPASG LPNIDALQAR MMPQQGREQG SYTTVGLSGN AVIPWAVTKD EKTRYDSLFR
AWDGFNKGFI GGDVAIEVFG QSGLPKTDLE RVWTLADHGN KGRLNMDEFA VAMHLIYRKL
NGYPLPAQLP PELVPPSTRN FNDSIGAVKS LLHQESDFRK NSGATLLPQK TGVSYLKSHS
FRGDSGAMSG RKDATVYKNN DDDVGYKSSA RRRIGNHSPR PDSPASVKSD DELTLDQLRK
KVHEKQILLD AMDFKDEKVA DQEDALDRKD RREAEDLYHR IRRIQEDIDA HPDAALHNVD
SGAERRALKR QLQTLTDRLP EIASQVRKTE RSIADAKLEL FRLRDAKAHP GSASSIIGTG
PGGTVTESDR LKARAKAMMQ QRTAALTGRK IESNDEDLAA PKRLEEESIK IRTEKENNER
LVQDVEDSVR DFSRGLEDSL KDGAEDSSSE HERRRWEDGL GVEDEVKEFI FDLQRSSRAA
RIRKDDRADS RSARSTESSR APSGSHIETP LSSRRAEEPP RTASTPASTG GTYSQYKTPE
ERAAFIKQQA EQRMAERLAA LGIRAPSKPG ETAAQRLERE KSERAAKLRQ AEEEDARREA
ERQARIAEEQ GIPPPVPETT ASPAAAAKKP PPPPSRKAAK SDAAEREAAR KAEEERVLVE
QKAQLIATQN MEDEAAQQEA ELAKEREAAQ SRLKALEEQV KAGKLKKEEE KRKKKAAVAE
AKEKEARLAA RRAEIEAAQA RERELQRQLE AIEDESSSDD DLEQVTPQAS TPTQGSQELE
RKEVSPPPAA PVVRAMTPPA PIPTVSTVTS PPVDSETRNP FFKKLAQPGE TPSVAAPAPT
PAAVSNNPFH RLPSQEHTAK AVELPPPQPM GTRSRGRPEE DEWSVVGSDN DDDSSDDEGP
GAGNARQLAS ILFGTMAPPR PLSATGNGSA PVSPAIGSPG GEPSFAATPP PAPPLPGAGG
APPPPSTS
//
