ID   A0A182MZ77_9DIPT        Unreviewed;       667 AA.
AC   A0A182MZ77;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Choline/carnitine acyltransferase domain-containing protein {ECO:0000259|Pfam:PF00755};
OS   Anopheles dirus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7168 {ECO:0000313|EnsemblMetazoa:ADIR000682-PA, ECO:0000313|Proteomes:UP000075884};
RN   [1] {ECO:0000313|Proteomes:UP000075884}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WRAIR2 {ECO:0000313|Proteomes:UP000075884};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   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 Anopheles dirus WRAIR2.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:ADIR000682-PA}
RP   IDENTIFICATION.
RC   STRAIN=WRAIR2 {ECO:0000313|EnsemblMetazoa:ADIR000682-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-carnitine + 4,8-dimethylnonanoyl-CoA = CoA + O-4,8-
CC         dimethylnonanoyl-(R)-carnitine; Xref=Rhea:RHEA:44860,
CC         ChEBI:CHEBI:16347, ChEBI:CHEBI:57287, ChEBI:CHEBI:77061,
CC         ChEBI:CHEBI:84654; Evidence={ECO:0000256|ARBA:ARBA00024283};
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000256|ARBA:ARBA00005005}.
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005232, ECO:0000256|RuleBase:RU003801}.
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   AlphaFoldDB; A0A182MZ77; -.
DR   STRING; 7168.A0A182MZ77; -.
DR   EnsemblMetazoa; ADIR000682-RA; ADIR000682-PA; ADIR000682.
DR   VEuPathDB; VectorBase:ADIR000682; -.
DR   OrthoDB; 1429709at2759; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000075884; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.20.1280.180; -; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 1.10.275.20; Choline/Carnitine o-acyltransferase; 1.
DR   Gene3D; 3.30.559.70; Choline/Carnitine o-acyltransferase, domain 2; 1.
DR   InterPro; IPR000542; Carn_acyl_trans.
DR   InterPro; IPR042572; Carn_acyl_trans_N.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR039551; Cho/carn_acyl_trans.
DR   InterPro; IPR042231; Cho/carn_acyl_trans_2.
DR   PANTHER; PTHR22589; CARNITINE O-ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR22589:SF16; CARNITINE O-PALMITOYLTRANSFERASE 2, MITOCHONDRIAL; 1.
DR   Pfam; PF00755; Carn_acyltransf; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   PROSITE; PS00440; ACYLTRANSF_C_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU003801};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          52..647
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   ACT_SITE        375
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   667 AA;  74298 MW;  C9C855565F4AEC68 CRC64;
     MLRVPKTQWA ASVANAVRSK STTARSTSGD EYQFLQRSKI PMLHFQPSLP RLPIPELDKT
     CARYLAAQQP LLAPEAFQRT TEAVKQFSET DGPKLQTLLK EFDGKNKHTS YISEPWFDMY
     LRDRVPLPLN YNPLLMMNPD PRPEYNDQLL RTTNLVVSSL RFMRSLRAKT LEPEVFHMNP
     AKSDTNMFRT VTSLMPSLIS TYVAYTFKAF PLDMSQYQGL FGGTRIPELG KDRIYRNESA
     RHVLVLRKGN MYAVDVLDAA GDIEQPATLF ARFERILSDA KPPAADPLGL LTTENRDTWA
     TARTHLTQLG NNAKSLELVD SALFCLCLDE STINPDNPIP AIREFLFGDG TNRWFDKSFS
     LIVAKDGTAG INFEHSWGDG VAVLRYFQEI YKETTTTPFV HPGLQGANDQ SSSAIAPIEF
     TLDDRVKSAI RTAENNHNAV IDSLDMNYMK YEGINKGVCK KQRISPDSVM QLGFQLAYYK
     QHGSFVATYE SCSTAAFRHG RTETMRPCTL ATRAFCEAVE RRAGPNGKSA AELRAMMDQC
     STVHGQLTKE AAMGQGFDRH LFGLRHTAQQ NGLPLPALYQ DPAYAALNHN ILSTSTLSSP
     ALLAGGFGPV VKDGYGIGYN IQDGYLGSVV TSYKPHRNGR EFVDCLRAAY EDISKVLTAS
     GPSPKEK
//