ID G1Q3Y0_MYOLU Unreviewed; 564 AA.
AC G1Q3Y0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Choline/carnitine acyltransferase domain-containing protein {ECO:0000259|Pfam:PF00755};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000018413.1, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000018413.1, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000018413.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; AAPE02040077; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1Q3Y0; -.
DR STRING; 59463.ENSMLUP00000018413; -.
DR Ensembl; ENSMLUT00000010099.2; ENSMLUP00000018413.1; ENSMLUG00000010099.2.
DR eggNOG; KOG3717; Eukaryota.
DR GeneTree; ENSGT01060000248556; -.
DR HOGENOM; CLU_013513_5_0_1; -.
DR InParanoid; G1Q3Y0; -.
DR OMA; TTQHRDT; -.
DR TreeFam; TF313836; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
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; 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:UP000001074};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801}.
FT DOMAIN 38..560
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT ACT_SITE 343
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
FT BINDING 419
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 423..430
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 452
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 454
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 456
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 465
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 504
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 555
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
SQ SEQUENCE 564 AA; 64224 MW; B5A3761A8555011D CRC64;
MLAFAIRTMV KPLGFLKPSS LRKVASRFKA HQESLPRLPV SPLQQTLDHY LKTLQPMVSE
EEWAHTKKLV EEFQAAGAVG ERLQKGLERR AKKMENWLSQ WWLKMAYLQF RQPLVIYSSP
GLVLPRQDFV DLQGQLRFAA KFIEGVLDFK AMVDNETLPV EYLGRKPLCM NQYNQILFSC
RVPGPKQDSV INFSKTKKPP MHITVVHNYQ FFELDVYHSD GTPLTSDQLF VQPEKIWNSS
LQTNKEPVGI LTSNHRNSWA KAYNTLITDK VNRESVRSIQ KSIFTVCLDT VIPRVSEDMY
RSQVAGQMLH GGGSELNSGN RWFDKTLQFI GAEDGFCGLI YEHAAAEGPP IISLVDHVIE
YTKKAEVVRS PMVPLPMPKK LRFNITPEIN NDIEKAKQNL SIMIQDLDMI VTVFHHFGKD
FPKSEKLSPD TFIQMALQLA YYRVYGQACA TYESASLLMF HLGRTDTIHS ASTESLTFVK
AMDDSNVTEH QKVELLRKAM DAHRAYTNQA IRGEALDRHL LGLKLQAIED LVSMPDIFMD
TSYAIAMHFN LSTSQVPSKT DCVM
//
