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Database: UniProt
Entry: S2J5N2_MUCC1
LinkDB: S2J5N2_MUCC1
Original site: S2J5N2_MUCC1 
ID   S2J5N2_MUCC1            Unreviewed;       485 AA.
AC   S2J5N2;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EPB83517.1};
GN   ORFNames=HMPREF1544_09738 {ECO:0000313|EMBL:EPB83517.1};
OS   Mucor circinelloides f. circinelloides (strain 1006PhL) (Mucormycosis
OS   agent) (Calyptromyces circinelloides).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX   NCBI_TaxID=1220926 {ECO:0000313|EMBL:EPB83517.1, ECO:0000313|Proteomes:UP000014254};
RN   [1] {ECO:0000313|Proteomes:UP000014254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1006PhL {ECO:0000313|Proteomes:UP000014254};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., Earl A., Findley K., Lee S.C., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome sequence of Mucor circinelloides f. circinelloides 1006PhL.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol
CC         + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20;
CC         Evidence={ECO:0000256|ARBA:ARBA00001039};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acyl-CoA + a long chain fatty alcohol = a wax ester +
CC         CoA; Xref=Rhea:RHEA:38443, ChEBI:CHEBI:10036, ChEBI:CHEBI:17135,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:77636; EC=2.3.1.75;
CC         Evidence={ECO:0000256|ARBA:ARBA00029340};
CC   -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004771}.
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC   -!- SIMILARITY: Belongs to the long-chain O-acyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00009587}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the long-chain O-
CC       acyltransferase family. {ECO:0000256|ARBA:ARBA00024360}.
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DR   EMBL; KE124068; EPB83517.1; -; Genomic_DNA.
DR   AlphaFoldDB; S2J5N2; -.
DR   STRING; 1220926.S2J5N2; -.
DR   VEuPathDB; FungiDB:HMPREF1544_09738; -.
DR   eggNOG; ENOG502S5A5; Eukaryota.
DR   InParanoid; S2J5N2; -.
DR   OMA; KAMYPLG; -.
DR   OrthoDB; 1359873at2759; -.
DR   UniPathway; UPA00282; -.
DR   Proteomes; UP000014254; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0019432; P:triglyceride biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR045034; O-acyltransferase_WSD1-like.
DR   InterPro; IPR009721; O-acyltransferase_WSD1_C.
DR   InterPro; IPR004255; O-acyltransferase_WSD1_N.
DR   PANTHER; PTHR31650:SF1; DIACYGLYCEROL O-ACYLTRANSFERASE TGS4-RELATED; 1.
DR   PANTHER; PTHR31650; O-ACYLTRANSFERASE (WSD1-LIKE) FAMILY PROTEIN; 1.
DR   Pfam; PF06974; WS_DGAT_C; 1.
DR   Pfam; PF03007; WS_DGAT_cat; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014254};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        216..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          13..157
FT                   /note="O-acyltransferase WSD1-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03007"
FT   DOMAIN          332..461
FT                   /note="O-acyltransferase WSD1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06974"
FT   COILED          456..483
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   485 AA;  55697 MW;  03F114CFFFBCFBD6 CRC64;
     MTTVKKSDKQ VGGLDTLFLK VEHPRRLMTV TSIWTFKQRL DQKQVYKVLE KLCEEYPRFA
     KTPAHEGFFR PATWVEPVGW KFQDNIVTHT LEEPTRQALQ KYCAEQVVTP FDYTKPLWEL
     HAISGLEDDR YAFFWKAHHA LADGEGFIRS LLSTTSLGAT LKKLEEQSIV SHRRKKEKPT
     TKNDTSKPES IWQKLPTCIS AVMGFIWLIL YKIYVYSVVT IHDLYCIMLC VLPVTRKDLY
     YKGLQSHEKE MAWSDDVSIK DIKTVREAFG GTLNDVMLLV ITRCLKSYLE SIGKRNDNYI
     SFIIPVSLRE PSDWSFQNVV SGSWGFFSMK DLDTRHLLKQ VQTEMLAIKN SYGPRMLYET
     WQWFFSHAPG LSPSMSVYNH VCDIPHGVFT NVPGPTVPIQ FAGEEIQEYR TFPPQSGKGS
     IGMALISYSG KVSVGAITDV HRDYPQVANG VCSRFAEEFQ LILDEAKMEI SKKNANLNLR
     EKKDK
//
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