ID A0A183IUI6_9BILA Unreviewed; 489 AA.
AC A0A183IUI6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 22-FEB-2023, entry version 23.
DE SubName: Full=SAM domain-containing protein {ECO:0000313|WBParaSite:SBAD_0000755601-mRNA-1};
GN ORFNames=SBAD_LOCUS7283 {ECO:0000313|EMBL:VDP12565.1};
OS Soboliphyme baturini.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Dioctophymatida; Dioctophymatoidea; Soboliphymatidae; Soboliphyme.
OX NCBI_TaxID=241478 {ECO:0000313|Proteomes:UP000050793, ECO:0000313|WBParaSite:SBAD_0000755601-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SBAD_0000755601-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDP12565.1, ECO:0000313|Proteomes:UP000270296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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}.
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DR EMBL; UZAM01010496; VDP12565.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A183IUI6; -.
DR WBParaSite; SBAD_0000755601-mRNA-1; SBAD_0000755601-mRNA-1; SBAD_0000755601.
DR Proteomes; UP000050793; Unplaced.
DR Proteomes; UP000270296; 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; cd09515; SAM_SGMS1-like; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
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.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 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:UP000270296};
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 119..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 217..239
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 251..277
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 297..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 363..381
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..77
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
SQ SEQUENCE 489 AA; 56710 MW; 6D0C9B163882ACAF CRC64;
MNKINKPVAE WCCEEVQSWL VENGFAEYGD LLACHHKVDG RVLLSLTEED LRNPPISLPL
LGDIKRMILA IDRLKPDKGK YDGSGSYYDL QHVCYQHGSG HELSSKTLPP STSSERPRLT
IPLLFCMIML FHSILCFLSL MYHSEVHHNL IISRIEADDT QSRWNCILKT VVAGFHFLCS
IFLTSYVMVI VHDRVPDSKT YPPLPDLLLD NIPHIPWAFD LCELLACLLG LIWCTILVFH
KHRLILLRRF FSLTGTVFIL RCITMLITSL SVPGAHLKCT ARKSEDSYTR LKNALHIWYG
MGMSLFGVRS CGDYMFSGHT TVMTLLNHFI TEYTPDTWNY LHTTSWVINL FAVFFILAGH
EHYSIDVFVA FYISSRLFLY YHSMAYHVKS VTAADTRTRI WFPLFWFLES GSQCGRIPNE
YEWPLPSFAS ICELFDGSYF IKRSKSELEF IQSKYRIQFD RVHEFLFHDH HCFTESAPMK
SKHKAKIKR
//