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
//