ID A0A068YDP1_ECHMU Unreviewed; 642 AA.
AC A0A068YDP1;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Carnitine O palmitoyltransferase 2 {ECO:0000313|EMBL:CDS42888.1};
GN ORFNames=EmuJ_001061200 {ECO:0000313|EMBL:CDS42888.1};
OS Echinococcus multilocularis (Fox tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus.
OX NCBI_TaxID=6211 {ECO:0000313|EMBL:CDS42888.1};
RN [1] {ECO:0000313|EMBL:CDS42888.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23485966; DOI=10.1038/nature12031;
RA Tsai I.J., Zarowiecki M., Holroyd N., Garciarrubio A., Sanchez-Flores A.,
RA Brooks K.L., Tracey A., Bobes R.J., Fragoso G., Sciutto E., Aslett M.,
RA Beasley H., Bennett H.M., Cai J., Camicia F., Clark R., Cucher M.,
RA De Silva N., Day T.A., Deplazes P., Estrada K., Fernandez C., Holland P.W.,
RA Hou J., Hu S., Huckvale T., Hung S.S., Kamenetzky L., Keane J.A., Kiss F.,
RA Koziol U., Lambert O., Liu K., Luo X., Luo Y., Macchiaroli N., Nichol S.,
RA Paps J., Parkinson J., Pouchkina-Stantcheva N., Riddiford N., Rosenzvit M.,
RA Salinas G., Wasmuth J.D., Zamanian M., Zheng Y., Cai X., Soberon X.,
RA Olson P.D., Laclette J.P., Brehm K., Berriman M., Garciarrubio A.,
RA Bobes R.J., Fragoso G., Sanchez-Flores A., Estrada K., Cevallos M.A.,
RA Morett E., Gonzalez V., Portillo T., Ochoa-Leyva A., Jose M.V., Sciutto E.,
RA Landa A., Jimenez L., Valdes V., Carrero J.C., Larralde C.,
RA Morales-Montor J., Limon-Lason J., Soberon X., Laclette J.P.;
RT "The genomes of four tapeworm species reveal adaptations to parasitism.";
RL Nature 496:57-63(2013).
RN [2] {ECO:0000313|EMBL:CDS42888.1}
RP NUCLEOTIDE SEQUENCE.
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005232}.
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DR EMBL; LN902842; CDS42888.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068YDP1; -.
DR STRING; 6211.A0A068YDP1; -.
DR eggNOG; KOG3719; Eukaryota.
DR OMA; YADGYYK; -.
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:SF16; CARNITINE O-PALMITOYLTRANSFERASE 2, MITOCHONDRIAL; 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, ECO:0000313|EMBL:CDS42888.1}.
FT DOMAIN 32..630
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
SQ SEQUENCE 642 AA; 71709 MW; A7DA022987549A8B CRC64;
MRVNRALLAR CASHMISTKS GCSSIRKEVI SQTEAFEELY TLVEHFRRSF GSELQGKLRE
LHYSNPNYMS KILLDSHLKD RKPVAVNHNS VYIFKQCSLG TGYNDSVLRA ANLVYSSLRF
LESLRRNKLR PDIHHTIPAI TNSGNFEHLI SILPSFLATQ GAHLFKAFPL DMSHYKFMFH
STRIPDFGID RLETYPEACH VVVLSRGEFY TFDAFDDQNK MVSAEQLVSN LAFIRNRPRG
STEKPSVGLL TTMNRDCAAL ARQRLRQVDG DTEGINTRNL ALIDAAIMVL IMCDDFSEYL
PQLVSTTLAG PGGSRWFDKS FSLLVDRSGT AALNFDCGWT DASAALRFAE SIFRDSETRP
SADPWLLDFP HRLPRATVRR LEWHLDEAFY EKVLLPQRDA YDALRDSLQV DCLAEMGDRT
LTRRLCVRAG VCADAMMQLA FLMAHEKVHG EAGLNGGSTE SRSTRTFRGG YTTLLRPFTT
EMSKFLRLFR LSDIVGYLDE GDLLDALHCC SRAHQKLLRG AAVAQDWDSH LFALKQLAEA
EGKKLPEFFT NKAYARISTV DLYTAPLTSG VANAATTGTT TGLLIGAFAP TSPHGYGISY
GITDEGCSAC CTTWRDSSIS KGSQFVESFQ QSLHQIAAIL QS
//