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Database: UniProt
Entry: A0A2A2M0D2_9BILA
LinkDB: A0A2A2M0D2_9BILA
Original site: A0A2A2M0D2_9BILA 
ID   A0A2A2M0D2_9BILA        Unreviewed;       502 AA.
AC   A0A2A2M0D2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   22-FEB-2023, entry version 14.
DE   RecName: Full=Sphingomyelin synthase-like domain-containing protein {ECO:0000259|Pfam:PF14360};
GN   ORFNames=WR25_23162 {ECO:0000313|EMBL:PAV91697.1};
OS   Diploscapter pachys.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX   NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV91697.1, ECO:0000313|Proteomes:UP000218231};
RN   [1] {ECO:0000313|EMBL:PAV91697.1, ECO:0000313|Proteomes:UP000218231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PF1309 {ECO:0000313|EMBL:PAV91697.1};
RA   Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA   Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT   "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL   Curr. Biol. 0:0-0(2017).
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:PAV91697.1}.
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DR   EMBL; LIAE01006299; PAV91697.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A2M0D2; -.
DR   STRING; 2018661.A0A2A2M0D2; -.
DR   Proteomes; UP000218231; 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:SF27; PHOSPHATIDYLCHOLINE:CERAMIDE CHOLINEPHOSPHOTRANSFERASE 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:UP000218231};
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        223..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        264..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        396..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        421..443
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          364..436
FT                   /note="Sphingomyelin synthase-like"
FT                   /evidence="ECO:0000259|Pfam:PF14360"
FT   REGION          1..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..31
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..110
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..184
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   502 AA;  56243 MW;  F9AC046C2C3B516E CRC64;
     MHNPGDDGRK PESGAHVNAA VDEEQDSEAA TTTIRDSDTV GQRETSPDPR LAAFHSADAA
     FSDDDDDEVF LADNKAEPEP VRVHQPQSHS KNGQSEQNEK DLEAGRSGRN EPEVSIKPPR
     TIITVRPPSP DLIVAMDDDG PSGSGVRESG IRPAIDGSTG PGRPRRVCGT GSSAASSSSD
     SETADDAPLL AGSSERSQPV RIEMPGEKPA SPHDRFPKER GKAIACTILL VFAAVFNTIV
     LSYVHEKLPD DPPLPDIVFD HTPYFPLGLD ICEYLMMVSF ASVLLLMLFH RHRWIMLRRL
     TFIGSLLYLM RCVTMLSTQV PKADKNWHCA PKYGENATFW NVVWRGIEIV TGVGLNVQGR
     KTLCGDYIYS GHTIVLVCSA LFMGEYSPRR WRIVHALYWL AAIVGGAFLV VSRGHYTIDV
     ILSYFICTRM FWVYHTMAAN PTLRMSSHNH HRKEYWFYFF HYLERSVMKP VPRRFDMPIP
     IDRLTSLIPR NTRRQNNRIA IE
//
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