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Database: UniProt
Entry: V5HC06_IXORI
LinkDB: V5HC06_IXORI
Original site: V5HC06_IXORI 
ID   V5HC06_IXORI            Unreviewed;       721 AA.
AC   V5HC06;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Putative carnitine o-palmitoyltransferase 1 {ECO:0000313|EMBL:JAB70758.1};
OS   Ixodes ricinus (Common tick) (Acarus ricinus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX   NCBI_TaxID=34613 {ECO:0000313|EMBL:JAB70758.1};
RN   [1] {ECO:0000313|EMBL:JAB70758.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Salivary gland and midgut {ECO:0000313|EMBL:JAB70758.1};
RX   PubMed=25765539;
RA   Kotsyfakis M., Schwarz A., Erhart J., Ribeiro J.M.;
RT   "Tissue- and time-dependent transcription in Ixodes ricinus salivary glands
RT   and midguts when blood feeding on the vertebrate host.";
RL   Sci. Rep. 5:9103-9103(2015).
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005232}.
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DR   EMBL; GANP01013710; JAB70758.1; -; mRNA.
DR   AlphaFoldDB; V5HC06; -.
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; CARNITINE O-ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR22589:SF112; CHOLINE_CARNITINE ACYLTRANSFERASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00755; Carn_acyltransf; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   PROSITE; PS00439; ACYLTRANSF_C_1; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:JAB70758.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..721
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004737881"
FT   TRANSMEM        53..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          125..710
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   ACT_SITE        420
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   721 AA;  82689 MW;  6EA009247D4334AD CRC64;
     MWPTSVQNIG ILCVIVFLFM LSEIDVAESI KEFFWDTGDT LHVPHALPST VRAVIVACFI
     SIVLSVVFMK VRQIILRGLL AYRGWMYEAR KPGEKYLTLM WCMAVRVVSG YQPSLYSCQR
     CLPRLPVPPL HDTIVRLLDS LKAVCTEDEM KVLSEQAEKF EKTLGPTLQR LLYLRSWYAS
     NYVTDWWEKY IYLSSRSSLA VNSNYYCFDQ SYYHPSDIQS SRTAVIIHNC LVFKRLIDRE
     ELQPLVLRGT VPICMSQYER LFSTTRVPGI DVDEICHFCT SESKHVILQH KGMFYKLEVY
     DSTNQILFPT TLEHQIEWIM KDAEQHTPTE AETSLAALTS LDRPTWARIR NKYFLAGVNK
     ESLDAIEKAT FFVSMNDLEP SGLNERGKYL LHGDGKSIWF DKSLNVQVFK NAHAGMNCEH
     SMADAPAMAH MWEYALTREV LEKVYDESGR CMPPGKKLKQ GSIRRPQRLV WDISPELERE
     IAGALANARK NNEDLDLYVR DHDSWGKGVI KKCKVSPDAF IQMALQLTYY KENKKFVQTY
     EASMTRLYLN GRTETVRSCT LEAVDFVKAM VENSVSNEEK IRLLRRAANK HQMLYRDAMS
     GKGVDRHLFA LFVACKGLKY ESEFLTNAIM RPWTLSTSQT PHTQLDYSPD ADLEVFTNKI
     CPGGGFGPVS DDGYGVSYII PNNSKIFFHV SSKKSCPNTN SERFVKTLDE SMDEMKALFS
     F
//
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