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Database: UniProt
Entry: A0A0M3I0R0_ASCLU
LinkDB: A0A0M3I0R0_ASCLU
Original site: A0A0M3I0R0_ASCLU 
ID   A0A0M3I0R0_ASCLU        Unreviewed;       757 AA.
AC   A0A0M3I0R0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Carn_acyltransf domain-containing protein {ECO:0000313|WBParaSite:ALUE_0000975001-mRNA-1};
OS   Ascaris lumbricoides (Giant roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6252 {ECO:0000313|Proteomes:UP000036681, ECO:0000313|WBParaSite:ALUE_0000975001-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:ALUE_0000975001-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005232, ECO:0000256|RuleBase:RU003801}.
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DR   AlphaFoldDB; A0A0M3I0R0; -.
DR   WBParaSite; ALUE_0000975001-mRNA-1; ALUE_0000975001-mRNA-1; ALUE_0000975001.
DR   Proteomes; UP000036681; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR   Gene3D; 3.30.559.70; Choline/Carnitine o-acyltransferase, domain 2; 1.
DR   InterPro; IPR000542; Carn_acyl_trans.
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:SF31; CARNITINE O-PALMITOYLTRANSFERASE; 1.
DR   Pfam; PF00755; Carn_acyltransf; 2.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 3.
DR   PROSITE; PS00440; ACYLTRANSF_C_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU003801}; Membrane {ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000256|RuleBase:RU003801};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        5..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          86..395
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   DOMAIN          414..730
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   ACT_SITE        392
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   757 AA;  87067 MW;  3238C4F25B9BB106 CRC64;
     LHIFIFRCGI ISQILSLLVC GALIWFVAIQ TLRLSLKAFL SYKGWMYESP HSKKISIATK
     LWLMALHFIS KSDPMLHSFQ GALPHLPLPS LEETLEKHLR SMRPICSDEE YNELVELTDK
     FCKGIGRRLQ RYLVIKWILS INYVTDWWEE FVYLRQRSPI MINSNYYGFD TLREHPTHSQ
     SARAANITYA ALTFRRMVER QQIKPFAISP RTKVPFCTMQ YERLFNSCRV PGEESDRFLH
     WDDSQHVAVF CKGCWFKLPV HTGKRLYEPC ELQVAFQSIL DSALTPAPGE ENLAALTAGE
     RTAWALARKK YFSAGVNKTS LHAIERSAFV VVLDQEEFDY DPVRFIPPMN EPSKLDSWAC
     NLLHGKAKDR WFDKSFNFVV YKNGRMGINA EHSWYCAYKC LFNEPSKLDS WACNLLHGKA
     KDRWFDKSFN FVVYKNGRMG INAEHSWGDA AIMAHFMEYC LITDLCQQGY DDKGNTFGTP
     VQSSRPERLR WNLGDEVQAA VHNSLSTATA LIEDVEMALL VWTEYGKGLI KNLHVSPDAF
     LQMTLQLTYF RNQGRFSLTY EAAMTRLYRE GRTETVRSCT VESCDFVRAM LDPKQTREER
     CRLLRRASER HQELYRAAMC GKGVDRHLFA LYVVKRYLEE ESPFLDKIFP PTYLLSTSQT
     PLNQCTEEAK CMTPQQKANF VSAGGGFGPV ADEGYGVSYN IAGENQISFH ISSKKSAKNT
     SSVGFRNDLV KSLREMRDLF VDEIRNADTF EVVEGAL
//
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