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Database: UniProt
Entry: A0A3B4XG83_SERLL
LinkDB: A0A3B4XG83_SERLL
Original site: A0A3B4XG83_SERLL 
ID   A0A3B4XG83_SERLL        Unreviewed;       624 AA.
AC   A0A3B4XG83;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Carnitine O-acetyltransferase-like {ECO:0000313|Ensembl:ENSSLDP00000015176.1};
OS   Seriola lalandi dorsalis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000015176.1, ECO:0000313|Proteomes:UP000261360};
RN   [1] {ECO:0000313|Ensembl:ENSSLDP00000015176.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005232}.
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DR   AlphaFoldDB; A0A3B4XG83; -.
DR   STRING; 1841481.ENSSLDP00000015176; -.
DR   Ensembl; ENSSLDT00000015751.1; ENSSLDP00000015176.1; ENSSLDG00000011790.1.
DR   GeneTree; ENSGT01060000248556; -.
DR   Proteomes; UP000261360; Unplaced.
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:SF50; CARNITINE O-ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR22589; CARNITINE O-ACYLTRANSFERASE; 1.
DR   Pfam; PF00755; Carn_acyltransf; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          40..605
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   ACT_SITE        344
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   624 AA;  69721 MW;  D47191866A7BE4DE CRC64;
     MLTFPTAKLG VMKPCTLGKP VAATLVAGRN LTQQNIVPSL PVPPLKQTCE LYLSFLEPIV
     EAEELKQTEI LVEEFLKAGG VGERLQRGLE RKASNTENWL TDDYVKFEYL DRRKPVVVYS
     NHGMVLPHMN FRNKQEQIRF AAEVTSGCLN VKTMVDNDTL PVEYMGGKPL CMKQYDRVLS
     SCRIPGPKTD TLVFHAKTSN APKHISVVHN CQFFVLDVYN SDGTLLTVDQ LYVQLERICK
     ASPQTTTEPV GILTTQNRDV WSRTYSSLIQ DETNKESLSA IERSIFTVCL DRATPQEPDE
     MRSSAILQIL HGGGSQCNSG NRWFDKGLQF VIGEDGTCGA NGSHSAADGT ACMGLADHTV
     AFMMKPKMTQ SRTEPLPLPK KLQFKITPEI KKDIEEAKQM ARDLNLRVTV FEHFGKNYLK
     AHKMSPDAFV QMALQLAYYR MYQQCCSTFE PASLRMFKLG RVAGIHSTSK ASATFVKAFD
     DPNIKNSVKV DLLDKAIKAH KWYTHMAVNG QAIEGHLLGL RMQTGEENIS MPELFTDSSF
     TKAFNYQIST SQVISKSSSL PCVGPETPDI YDVCYSVLSD RISLIVSRFE PPNTCKVKNA
     ECLIEAMVDA LLDMRTMLEL QEAV
//
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