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Database: UniProt
Entry: V5I5I7_IXORI
LinkDB: V5I5I7_IXORI
Original site: V5I5I7_IXORI 
ID   V5I5I7_IXORI            Unreviewed;       769 AA.
AC   V5I5I7;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Putative carnitine o-palmitoyltransferase 1 {ECO:0000313|EMBL:JAB84153.1};
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:JAB84153.1};
RN   [1] {ECO:0000313|EMBL:JAB84153.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Salivary gland and midgut {ECO:0000313|EMBL:JAB84153.1};
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; GANP01000315; JAB84153.1; -; mRNA.
DR   AlphaFoldDB; V5I5I7; -.
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:SF112; 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; PS00439; ACYLTRANSF_C_1; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000313|EMBL:JAB84153.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        101..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          173..758
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   ACT_SITE        468
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   769 AA;  88229 MW;  99CE85DCCC5FC670 CRC64;
     MAEARNAVAG LRIREIDDER NSAAVMFRVW LKTAIRKYHR IRNSISNGMW PTSVQNIGIL
     CVIVFLFMLS EIDVAESIKE FFWDTGDTLH VPHALPSTVR AVIVACFISI VLSVVFMKVR
     QIILRGLLAY RGWMYEARKP GEKYLTLMWC MAVRVVSGYQ PSLYSCQRCL PRLPVPPLHD
     TIVRLLDSLK AVCTEDEMKV LSEQAEKFEK TLGPTLQRLL YLRSWYASNY VTDWWEKYIY
     LSSRSSLAVN SNYYCFDQSY YHPSDIQSSR TAVIIHNCLV FKRLIDREEL QPLVLRGTVP
     ICMSQYERLF STTRVPGIDV DEICHFCTSE SKHVILQHKG MFYKLEVYDS TNQILFPTTL
     EHQIEWIMKD AEQHTPTEAE TSLAALTSLD RPTWARIRNK YFLAGVNKES LDAIEKATFF
     VSMNDLEPSG LNERGKYLLH GDGKSIWFDK SLNVQVFKNA HAGMNCEHSM ADAPAMAHMW
     EYALTREVLE KVYDESGRCM PPGKKLKQGS IRRPQRLVWD ISPELEREIA GALANARKNN
     EDLDLYVRDH DSWGKGVIKK CKVSPDAFIQ MALQLTYYKE NKKFVQTYEA SMTRLYLNGR
     TETVRSCTLE AVDFVKAMVE NSVSNEEKIR LLRRAANKHQ MLYRDAMSGK GVDRHLFALF
     VACKGLKYES EFLTNAIMRP WTLSTSQTPH TQLDYSPDAD LEVFTNKICP GGGFGPVSDD
     GYGVSYIIPN NSKIFFHVSS KKSCPNTNSE RFVKTLDESM DEMKALFSF
//
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