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Database: UniProt
Entry: A9VCF0_MONBE
LinkDB: A9VCF0_MONBE
Original site: A9VCF0_MONBE 
ID   A9VCF0_MONBE            Unreviewed;       474 AA.
AC   A9VCF0;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN   ORFNames=MONBRDRAFT_29885 {ECO:0000313|EMBL:EDQ84773.1};
OS   Monosiga brevicollis (Choanoflagellate).
OC   Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Monosiga.
OX   NCBI_TaxID=81824 {ECO:0000313|EMBL:EDQ84773.1, ECO:0000313|Proteomes:UP000001357};
RN   [1] {ECO:0000313|EMBL:EDQ84773.1, ECO:0000313|Proteomes:UP000001357}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MX1 / ATCC 50154 {ECO:0000313|Proteomes:UP000001357};
RX   PubMed=18273011; DOI=10.1038/nature06617;
RG   JGI Sequencing;
RA   King N., Westbrook M.J., Young S.L., Kuo A., Abedin M., Chapman J.,
RA   Fairclough S., Hellsten U., Isogai Y., Letunic I., Marr M., Pincus D.,
RA   Putnam N., Rokas A., Wright K.J., Zuzow R., Dirks W., Good M.,
RA   Goodstein D., Lemons D., Li W., Lyons J.B., Morris A., Nichols S.,
RA   Richter D.J., Salamov A., Bork P., Lim W.A., Manning G., Miller W.T.,
RA   McGinnis W., Shapiro H., Tjian R., Grigoriev I.V., Rokhsar D.;
RT   "The genome of the choanoflagellate Monosiga brevicollis and the origin of
RT   metazoans.";
RL   Nature 451:783-788(2008).
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
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DR   EMBL; CH991581; EDQ84773.1; -; Genomic_DNA.
DR   RefSeq; XP_001750423.1; XM_001750371.1.
DR   AlphaFoldDB; A9VCF0; -.
DR   STRING; 81824.A9VCF0; -.
DR   EnsemblProtists; EDQ84773; EDQ84773; MONBRDRAFT_29885.
DR   GeneID; 5895645; -.
DR   KEGG; mbr:MONBRDRAFT_29885; -.
DR   eggNOG; KOG2898; Eukaryota.
DR   InParanoid; A9VCF0; -.
DR   OMA; QIFQWAT; -.
DR   Proteomes; UP000001357; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR   CDD; cd07991; LPLAT_LPCAT1-like; 1.
DR   InterPro; IPR045252; LPCAT1-like.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR23063:SF2; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE 4, ISOFORM D-RELATED; 1.
DR   PANTHER; PTHR23063; PHOSPHOLIPID ACYLTRANSFERASE; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001357};
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        92..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        117..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        146..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          182..294
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
FT   REGION          392..429
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          447..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        392..415
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..474
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   474 AA;  53769 MW;  21BE9A36EEDB36F1 CRC64;
     MIATTKAEGL VAEGFGARLE ETELDVFLNA FDRECVSDFV SQISNEQSYD CTTTFAFSDI
     VPFARNGFEA IVHDSFTQCF EGHPKTRWNQ TWYLALAYYC GVFIRYCILF PLRVTVLILA
     MTIFINLFLI SRLFPATIQR RIGRFAMGIV NNAFCQCTLL TGFAFTAVIH KHGNIPAREP
     GQIYVANHTT VLDIVIMLSH QVYGLTGQGH GGVIGFFQKY VLNFGTDNLW FDRMESRDRT
     TVAQKIKQHA ADTSKAPLLV FPEGTCVNNE FVVMFKRGAF DLGRVIVPVA IKYNNNITDA
     FWNSKKTSFP MHLFHFMTSW ALIADVYYLD PQTRREGETS VQFAARVKEM MANVAGLKSV
     PWDGYYKYFK PKPEYKRRRQ QVFTDQLIRR FNLTPSGTPT TSRSPQGSFS LGKLSNKDQL
     KPDEALPDLN DEARAVLRLR QQARSSLGKP ALGLHEATKS RITEPRRRAI SETA
//
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