ID A0A1Y2GHY0_9FUNG Unreviewed; 760 AA.
AC A0A1Y2GHY0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 28-JUN-2023, entry version 18.
DE RecName: Full=Sphingomyelin synthase-like domain-containing protein {ECO:0000259|Pfam:PF14360};
GN ORFNames=BCR41DRAFT_387827 {ECO:0000313|EMBL:ORZ11390.1};
OS Lobosporangium transversale.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Lobosporangium.
OX NCBI_TaxID=64571 {ECO:0000313|EMBL:ORZ11390.1, ECO:0000313|Proteomes:UP000193648};
RN [1] {ECO:0000313|EMBL:ORZ11390.1, ECO:0000313|Proteomes:UP000193648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3116 {ECO:0000313|EMBL:ORZ11390.1,
RC ECO:0000313|Proteomes:UP000193648};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the sphingomyelin synthase family.
CC {ECO:0000256|ARBA:ARBA00005441}.
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:ORZ11390.1}.
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DR EMBL; MCFF01000028; ORZ11390.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2GHY0; -.
DR STRING; 64571.A0A1Y2GHY0; -.
DR InParanoid; A0A1Y2GHY0; -.
DR OrthoDB; 2880501at2759; -.
DR Proteomes; UP000193648; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IEA:InterPro.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01610; PAP2_like; 1.
DR InterPro; IPR045221; Sphingomyelin_synth-like.
DR InterPro; IPR025749; Sphingomyelin_synth-like_dom.
DR PANTHER; PTHR21290:SF25; SPHINGOMYELIN SYNTHASE-RELATED PROTEIN 1; 1.
DR PANTHER; PTHR21290; SPHINGOMYELIN SYNTHETASE; 1.
DR Pfam; PF14360; PAP2_C; 1.
PE 3: Inferred from homology;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000193648};
KW Sphingolipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 155..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 319..336
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 621..641
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 292..360
FT /note="Sphingomyelin synthase-like"
FT /evidence="ECO:0000259|Pfam:PF14360"
FT REGION 413..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 760 AA; 85986 MW; E7038E496E42CAC3 CRC64;
MDHHIQIEHF GDESDRSQSQ FQFPYTSYYD TNNSIELDLE AVERDRFDRL SNSSTLVGGT
SPLRHPYSPE FNSNNSYFID DFKSNGNTIA TIATTTTTDT DINATTTITS ASVAAPAITV
YKARRRKYDG TDENEKKKTN GSLWYRFFYS EGGRLTCAVV YFVVICIGMA FCNQLSDHRW
VNTGYTDVLL RDRGFDVIEA QADIQPANTF VMTSVVFTVL GIGLICPNWT MRGIVLRRIL
WVIGTLSAFR ALTLSVTTLP TPKEECRPSL KTGFWDMFIV ALQMIPGTVE ACTDDIFSGH
TVFMVSCAIQ WRLYCRNKWV TYFSYLYISI GLYYVIATRL HYTVDVVLAI FITFAGWSVY
ICMIDVVMEE EYFGIKSHHE KYAVFNTAAA EYEFVTQEQD RAIDEEDEEV KVTISSTTTS
TTSTLTPNPT KSQTISSRRK QLEYHMNRLR GPRIGYGRGE YDRVAFVPMQ FNLWLKNVVR
WCDGLDLRMN PYIAENPSTG EQEEEEGLSS LSSSSRWNEL VVRYRAELAS ITGARCDCKK
TDGELENNLN GYNELGRHRE MVQVYRSGSG LESVHIHNYM EERGQQQHGR WRSMALRTSP
RSRSPDLKAA KAKKMERNRK LFVLKIALVI FVNVILLIKV IETVQNNSSA AASSSQWPTE
MKTYPGGTIY NNNNSYPNSP TSHATAPSGP SSLLTPSTQD EEHQVQASPE ESEVGNDSNK
AGAIAVALDD YKVIKEAVHH RGIQRRNSVG KRNLKQAEAI
//