ID A0A016T4U3_9BILA Unreviewed; 772 AA.
AC A0A016T4U3;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EYB97589.1};
GN Name=Acey_s0139.g2111 {ECO:0000313|EMBL:EYB97589.1};
GN Synonyms=Acey-cpt-1 {ECO:0000313|EMBL:EYB97589.1};
GN ORFNames=Y032_0139g2111 {ECO:0000313|EMBL:EYB97589.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB97589.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:EYB97589.1}.
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DR EMBL; JARK01001475; EYB97589.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016T4U3; -.
DR STRING; 53326.A0A016T4U3; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004095; F:carnitine O-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR Gene3D; 6.10.250.1760; -; 1.
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 InterPro; IPR032476; CPT_N.
DR PANTHER; PTHR22589; CARNITINE O-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR22589:SF31; CARNITINE O-PALMITOYLTRANSFERASE; 1.
DR Pfam; PF00755; Carn_acyltransf; 1.
DR Pfam; PF16484; CPT_N; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 50..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..47
FT /note="Carnitine O-palmitoyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16484"
FT DOMAIN 175..759
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT ACT_SITE 474
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 772 AA; 89555 MW; 46D0CC7615E49175 CRC64;
MAEAHSAVAL SFTVTHDGVS VSYDQELLHD IWHAFQRGYK RRIGRFKNNF MAGMFPANTI
TISIVIAAIS ILSIFRHDLS FGILPFIEYH ILYFLFGDGL LGFCISLLIS GALIWFVLVQ
LLRLSIKLLL SYKGWMYEQP GKPISTPTKL WLGLLNLMSK SGPMMHSYQG ALPHLPLPSL
NDTIERHLLS MRPILNDEEF EELEHLSEVF RKGLGRRLQR YLQLKSWLST NYVTDWWEEF
VYMRQRSPIM INSNYYGFGA LHEHPTDSQA ARAANVTYTA LLFRRQVDRQ EVTPFSVAPR
TKVPFCTMQY ERLFNSCRVP GEECDRFFHW DDAKHVAVYN RGCWFKVIIH NGKRLLEPCE
IQHQYDAILK QEIEPQPVER HLAVLTAGER THWAKTRRAY FRSGINRTSL NDIERAAFVV
ILDDEEVSYD KNDSSKLDRW AHNLLHGKGY DRWFDKSFNI IISKNAHVGL NAEHSWGDAA
VTAHFSEYMT LKDIMQERYD ENGNCKGEPT IRLKPERLKW DIPEPALNAI EVSMKVAQDL
IDDVEMALLV WTDYGKGFIK KLNVSPDAYL QMCLQYTYYK DQNKFSLTYE ASMTRLYREG
RTETVRSCTT QSSEFVLAMV DPKKTRTERL QLLRKACDRH QELYRDAMCG KGVDRHLFAL
YVIKRYLEEE SPFFDKIFPP MYLLSTSQTP LNQVDSEMYG MDEEQRLRLT TAGGGFGPVA
DRGYGVSYIV AGEHQISFHI SSKRSADNTS SKKFREELQR SLRDMKALFE EK
//
