ID U1GR67_ENDPU Unreviewed; 858 AA.
AC U1GR67;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Choline/carnitine acyltransferase domain-containing protein {ECO:0000259|Pfam:PF00755};
GN ORFNames=EPUS_03242 {ECO:0000313|EMBL:ERF74858.1};
OS Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF74858.1, ECO:0000313|Proteomes:UP000019373};
RN [1] {ECO:0000313|Proteomes:UP000019373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT "Genome characteristics reveal the impact of lichenization on lichen-
RT forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL BMC Genomics 15:34-34(2014).
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005232}.
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DR EMBL; KE720866; ERF74858.1; -; Genomic_DNA.
DR RefSeq; XP_007787862.1; XM_007789672.1.
DR AlphaFoldDB; U1GR67; -.
DR GeneID; 19238288; -.
DR eggNOG; KOG3719; Eukaryota.
DR HOGENOM; CLU_013513_4_0_1; -.
DR OMA; HILVMRR; -.
DR OrthoDB; 1429709at2759; -.
DR Proteomes; UP000019373; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 1.10.275.20; Choline/Carnitine o-acyltransferase; 1.
DR Gene3D; 3.30.559.70; Choline/Carnitine o-acyltransferase, domain 2; 1.
DR InterPro; IPR000542; Carn_acyl_trans.
DR InterPro; IPR042572; Carn_acyl_trans_N.
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:SF29; MITOCHONDRIAL CARNITINE O-ACETYLTRANSFERASE-RELATED; 1.
DR Pfam; PF00755; Carn_acyltransf; 2.
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 Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000019373};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 75..608
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT DOMAIN 665..738
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 381
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 858 AA; 95375 MW; 5B1DDFDC7B1C48D6 CRC64;
MPTTATEARH FTMPKSLNES MNSTQMAPDA GPRSTEAATE TKTSYPEKVQ EPLHGQKPNF
RPGITYAAQD KLPKLPIPEL GSTLKKYCEA LLPLQTSREQ EDTKAAAKEF LENEGKELQE
RLERYATGKT SYIEQFWYDS YLNYDNPVVL NLNPFFLLED DPTPARNNQV TRAASLVISA
LCFVRAVRKE ELPPDTLKGV PLDMYQYSRM FGTARVPTQN GCVIGQDSSA KHIVVLCKGQ
FYWFDVLDDN NDLIMTEKDV VQNLQVIVED AEQIPIQEAA KAAVGVLSTE NRKVWSGLRD
VLTRDEGSNN AECLNIVDSS LFMLCLDYTE PTNVSDLCGN MLCGTNEVVK GLQVGTCTNR
WYDKLQIIVC KNGSAGINFE HTGVDGHTVL RFASDVYTDT ILRFARTING QAPTLWASNS
PDPSKRDPDS FGDVSTTPRK LEWDMIPELS IALRFAETRL ADLIHQNEFQ TLDFAGYGKN
FMTSMGFSPD AFVQMAFQAA YYGLYGRIEN TYEPAMTKIY LHGRTEAIRS VTPEAVEFVK
TFWADNSPQK KVDTLKKATQ KHTAITKECG KAQGHDRHLY ALYCVWQRAV DGEGAEREES
PGFSSNGYIS GTESDMGGSP RRALDGEARP VSPPARNGNN TRPGRSTSSN NNRSSSNHRA
SKGGPSQMPA LFMDPGWEKI NNTILSTSNC GNPSLRHFGF GPISGDGFGI GYIIKDDSIS
ICASSKHRQT RRFVDSLESY LLEIRKLLRA TKRESSHAKQ TRAREVDERH ELGGRTKSFG
RLVRSDGTDK KVVGSQMPLG DGVDGELESD DGLGGYGFFD AGMLLQVRKA NQEKEQKPHQ
VAEQKRRAVG KKLALSEY
//
