ID A0A368G5R0_ANCCA Unreviewed; 608 AA.
AC A0A368G5R0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Choline/Carnitine O-acyltransferase {ECO:0000313|EMBL:RCN37977.1};
DE Flags: Fragment;
GN ORFNames=ANCCAN_16105 {ECO:0000313|EMBL:RCN37977.1};
OS Ancylostoma caninum (Dog hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=29170 {ECO:0000313|EMBL:RCN37977.1, ECO:0000313|Proteomes:UP000252519};
RN [1] {ECO:0000313|EMBL:RCN37977.1, ECO:0000313|Proteomes:UP000252519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Baltimore {ECO:0000313|EMBL:RCN37977.1,
RC ECO:0000313|Proteomes:UP000252519};
RA Mitreva M.;
RT "Draft genome of the hookworm Ancylostoma caninum.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005232, ECO:0000256|RuleBase:RU003801}.
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:RCN37977.1}.
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DR EMBL; JOJR01000429; RCN37977.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368G5R0; -.
DR STRING; 29170.A0A368G5R0; -.
DR Proteomes; UP000252519; Unassembled WGS sequence.
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; 1.
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:SF99; CARN_ACYLTRANSF DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR22589; CARNITINE O-ACYLTRANSFERASE; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000252519};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 57..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 131..606
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT ACT_SITE 427
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RCN37977.1"
SQ SEQUENCE 608 AA; 69531 MW; 12F6F1E6FF95C77E CRC64;
LLRFFFQASV DNRLWPVRPI YFVAGAASLG AIQVKYGDVP LFNVVPVFTN KVVEVVLWTK
ICVVSLAGAY IPIFLLRQFL SYFYFSYKGF IFEDPKKPSI TTRLWGICRQ LLSFSTPMLK
SCDNLLPSPS VPDLDETVAK YLKSVQNILR KDELALVKEQ AQSFLKNEGR RLHMYAWIMS
MMSDNYITPF WEKYAYLYNR EPLLITSSVA HTDLIEIPEH RRATRAYMAA RVTFFEAMSH
LAIDRQAIEP LGSGLLCACH YDKLYSVCRV PGEQIDELVN YGISKHVVAI LDGCFYKVMI
CDGNNRIYSI NQLAKIYAEL LSRNDVVEGP AGMVAALTTD KRDEWARNRE KFFLKHPQNG
ATLKEIESAA FILTLDDGEY GYDPKNPNKL SHFLRNMLTG NGVNRWADKS LNYVVSKNSR
CGGTTEHSIG DGSEFDHIME NFVAMELLTE YPSLEEQQRI EKLTEADRGL TLAKRLPIEV
NAEMGVAIQR CYTQYEKLRE DVDVAATVFR EYGKGFIKKC GVSPDGFMQM AIQLANYRDQ
GRFVLTYEPA SARFYKNSRT ETLRTVTDES CEFVYAMVNG KTTKEEKIKR LRVACELHTR
RNREAMVS
//
