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Database: UniProt
Entry: M3XIE6_LATCH
LinkDB: M3XIE6_LATCH
Original site: M3XIE6_LATCH 
ID   M3XIE6_LATCH            Unreviewed;       631 AA.
AC   M3XIE6;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   SubName: Full=Carnitine O-acetyltransferase {ECO:0000313|Ensembl:ENSLACP00000022502.1};
GN   Name=CRAT {ECO:0000313|Ensembl:ENSLACP00000022502.1};
OS   Latimeria chalumnae (Coelacanth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Coelacanthiformes; Coelacanthidae; Latimeria.
OX   NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000022502.1, ECO:0000313|Proteomes:UP000008672};
RN   [1] {ECO:0000313|Proteomes:UP000008672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT   "The draft genome of Latimeria chalumnae.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLACP00000022502.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005232, ECO:0000256|RuleBase:RU003801}.
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DR   EMBL; AFYH01046078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01046079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01046080; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01046081; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01046082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005993311.1; XM_005993249.2.
DR   AlphaFoldDB; M3XIE6; -.
DR   STRING; 7897.ENSLACP00000022502; -.
DR   Ensembl; ENSLACT00000024956.1; ENSLACP00000022502.1; ENSLACG00000013470.2.
DR   GeneID; 102359761; -.
DR   KEGG; lcm:102359761; -.
DR   CTD; 449545; -.
DR   eggNOG; KOG3717; Eukaryota.
DR   GeneTree; ENSGT01060000248556; -.
DR   HOGENOM; CLU_013513_5_0_1; -.
DR   InParanoid; M3XIE6; -.
DR   OMA; ENHSKGP; -.
DR   OrthoDB; 1429709at2759; -.
DR   Proteomes; UP000008672; Unassembled WGS sequence.
DR   Bgee; ENSLACG00000013470; Expressed in mesonephros and 1 other cell type or tissue.
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.
DR   PROSITE; PS00439; ACYLTRANSF_C_1; 1.
DR   PROSITE; PS00440; ACYLTRANSF_C_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU003801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW   Transferase {ECO:0000256|RuleBase:RU003801}.
FT   DOMAIN          43..613
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   ACT_SITE        348
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
FT   BINDING         424
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT   BINDING         428..435
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT   BINDING         457
FT                   /ligand="(R)-carnitine"
FT                   /ligand_id="ChEBI:CHEBI:16347"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT   BINDING         459
FT                   /ligand="(R)-carnitine"
FT                   /ligand_id="ChEBI:CHEBI:16347"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT   BINDING         461
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT   BINDING         470
FT                   /ligand="(R)-carnitine"
FT                   /ligand_id="ChEBI:CHEBI:16347"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT   BINDING         509
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT   BINDING         560
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
SQ   SEQUENCE   631 AA;  71426 MW;  E6419CDCFB76FA41 CRC64;
     MLLAVRNIMG KQALLKPICL VKPVSLTKIP GRYLAHQEGL PRLPVPPLQQ TLERYLLALE
     PIISLEELDH TRGIVKEFGA LGGVGERLQK GLERRARKNE NWLSDWWLQT AYLEYRLPVV
     IHSSPGVILP KQDFQDRQGQ LRFAAKLIAG VLDFKAMIDN ETLPVEYLGG KPLCMNQYYQ
     ILSSCRIPGS RRDSVVNYAR TSKPPTHITV VHNFQFFELD VYNSDGSPLT VDQIYIQLEK
     IWNSSLQTNK EPLGILTSQH RNTWGNAYNN LLKDKTNKES MRIIQKSIFT VCLDAPVPRV
     SDELYKSRVA AQMLHGGGSR WNSGNRWFDK TLQFIVAEDG SCGLVYEHAP AEGPPIVALV
     DHVMEYTKKS EVVRSPMLPL AMPKKLRFNI TPEIKKDIEN AKQNLNIMIQ DLDIKVFVFS
     QFGKSFPKSQ KMSPDAFIQM ALQLAYYRIY GCVCATYESA SLRMFHLGRT DTIRSASYDS
     MKFVEAMDDP SKQNQEKVEL LHKAVKYHRT YTDMAIQGQA IDRHLLGLKF QAIEDLVSMP
     EIFMDTAYAV AFHFHLSTSQ VPAKVDCVMC FGPVVPDGYG VCYNPMDDHI NFCVSAFNSC
     AETNASELAE KLESALSNMQ SLLQQTPKSK L
//
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