GenomeNet

Database: UniProt
Entry: A0A5A8CQM4_CAFRO
LinkDB: A0A5A8CQM4_CAFRO
Original site: A0A5A8CQM4_CAFRO 
ID   A0A5A8CQM4_CAFRO        Unreviewed;       624 AA.
AC   A0A5A8CQM4;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   08-OCT-2025, entry version 17.
DE   RecName: Full=O-acyltransferase {ECO:0000256|PIRNR:PIRNR000439};
GN   ORFNames=FNF29_01777 {ECO:0000313|EMBL:KAA0155402.1};
OS   Cafeteria roenbergensis (Marine flagellate).
OC   Eukaryota; Sar; Stramenopiles; Bigyra; Opalozoa; Bicosoecida;
OC   Cafeteriaceae; Cafeteria.
OX   NCBI_TaxID=33653 {ECO:0000313|EMBL:KAA0155402.1, ECO:0000313|Proteomes:UP000323011};
RN   [1] {ECO:0000313|EMBL:KAA0155402.1, ECO:0000313|Proteomes:UP000323011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BVI {ECO:0000313|EMBL:KAA0155402.1,
RC   ECO:0000313|Proteomes:UP000323011};
RA   Fischer M.G., Hackl T., Roman M.;
RT   "Genomes of Cafeteria roenbergensis.";
RL   Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|PIRNR:PIRNR000439}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC       ECO:0000256|PIRNR:PIRNR000439}.
CC   -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC       Sterol o-acyltransferase subfamily. {ECO:0000256|ARBA:ARBA00009010,
CC       ECO:0000256|PIRNR:PIRNR000439}.
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:KAA0155402.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; VLTN01000007; KAA0155402.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5A8CQM4; -.
DR   Proteomes; UP000323011; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR   InterPro; IPR004299; MBOAT_fam.
DR   InterPro; IPR014371; Oat_ACAT_DAG_ARE.
DR   PANTHER; PTHR10408; STEROL O-ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR10408:SF9; STEROL O-ACYLTRANSFERASE 2-RELATED; 1.
DR   Pfam; PF03062; MBOAT; 1.
DR   PIRSF; PIRSF000439; Oat_ACAT_DAG_ARE; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|PIRNR:PIRNR000439};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW   ECO:0000256|PIRNR:PIRNR000439};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000439};
KW   Reference proteome {ECO:0000313|Proteomes:UP000323011};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000439};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        25..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        137..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        207..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        413..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        455..481
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        548..568
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        588..606
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          256..370
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        260..288
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        321..333
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        340..351
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        546
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000439-1"
SQ   SEQUENCE   624 AA;  67073 MW;  F69E3E9E5CD08A24 CRC64;
     MSGNDLVATL EQLGLGVLVD TNAGLLMPAL AVLALLGVVY FSALACMGDA MPRQPRARTK
     REVLRNADSI LDSGGFSMLP WLDSMHDVSG TGAADGWFMA LAAIVIYWIL GTIVVNVERS
     GSPFSDDGVF WWRLVSGLWS LGLAFLAFAA VFSLAFVFQS AVVIAGVRPP MAVQIAFQVV
     LENGMLAAAV WYAYYGDAKD WPWTQKAGLL LEVAVLVLKA HSYLAVNGAL SRGSLAGFAA
     SSTALDAMVE LEGGAEEADA AARAERSAVE ARQRATRDQH DGDSHADDGT SSDSEEEDAR
     QGGSGHNTRS SSTRRRRRRP AAAAAATESP ASPVTRRSAA KAAKAADQAT ASPHDDSSAP
     RLTQTPSHGA DISYPDNVTL ADFVRFACAP TVVYSPNFPS TAAFRPLYLL EKVVFAAILL
     FAALETAIQF VLPVVADLGR AHAAGSPLPA GLVMARMVVP LTALMLLLFF LVFDVLFNAF
     AEFTLFGDRR FYGDWWNSTS FAEFSRKWNR PVHTWLLHHV YLPLQEAGLG SAVARYGTFA
     VSIAAHELLL HGFFGFAAPW LLVFSLFQFP LFTIMRLPIF KGKRLGNLVF WFGMALGVPL
     VGSLYLNDFC KSEPGSCIMT PAAA
//
DBGET integrated database retrieval system