ID W6ZE56_COCMI Unreviewed; 608 AA.
AC W6ZE56;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Choline/carnitine acyltransferase domain-containing protein {ECO:0000259|Pfam:PF00755};
GN ORFNames=COCMIDRAFT_8514 {ECO:0000313|EMBL:EUC41801.1};
OS Bipolaris oryzae ATCC 44560.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC41801.1};
RN [1] {ECO:0000313|EMBL:EUC41801.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC41801.1};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005232, ECO:0000256|RuleBase:RU003801}.
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DR EMBL; KI964085; EUC41801.1; -; Genomic_DNA.
DR RefSeq; XP_007691658.1; XM_007693468.1.
DR AlphaFoldDB; W6ZE56; -.
DR STRING; 930090.W6ZE56; -.
DR GeneID; 19126612; -.
DR KEGG; bor:COCMIDRAFT_8514; -.
DR eggNOG; KOG3717; Eukaryota.
DR HOGENOM; CLU_013513_5_1_1; -.
DR OrthoDB; 1429709at2759; -.
DR Proteomes; UP000054032; 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:SF115; CARNITINE O-ACETYLTRANSFERASE, MITOCHONDRIAL; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801}.
FT DOMAIN 33..581
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT ACT_SITE 324
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 608 AA; 69473 MW; 198463CAEC752341 CRC64;
MAPARKQSSL PAGYKEDHTK GAMLRFEESL PRLPVPTLEE TAKRYLKSVH PLLSKTEYEA
TTKAVNEFVA PGGPGEKLQE RLVARREDPK HKNWIYEWWN DAAYLAYRDP VVPYVSYFYS
HRDDKSRRNP TKRAAAMTTA VLEFKKMVDE CTLEPEYMKK LPIAMSSYEY MFNCCRVPKK
PSDTTVKFPY QEHKHIIVIR KNQFWKLAHE VNGKQLNTAE LQQQFDYIYS KAEKSPAVGA
LTSQNRDVWS DVYLKLKAHS PVNAATLQDI ESASFVVCLD DASPITLEER AHQYWHGDGA
NRWYDKPLQF IINENGTSGF MGEHSMMDGT PTHRINDYAN QQIFSNALPF DDPNIRSDLP
SPKPLRFELS PELQQDIEDA QSHFSRQIAA HELRVQAYQG YGKGLIKKFK CSPDAYVQMI
IQLAYHKFYG KNRPTYESAA TRRFQQGRTE TCRSVSDESV AFCNAMADAN ATPEECQQKL
RAALDAHVKY ISDASDGRGV DRHLFGLKKC LKEGEELPAL YKDPAFTYSS TWYISSSQLS
SEYFNGYGWS QVVDDGWGLA YMINENSIQF NVCSKGLGSE KMSFYLNEAA GDMRDIMLPT
LDKEKAKL
//
