ID A0A015LNK5_RHIIW Unreviewed; 647 AA.
AC A0A015LNK5;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Carnitine O-acetyltransferase CAT2 {ECO:0000313|EMBL:EXX74271.1};
GN ORFNames=RirG_052640 {ECO:0000313|EMBL:EXX74271.1};
OS Rhizophagus irregularis (strain DAOM 197198w) (Glomus intraradices).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=1432141 {ECO:0000313|EMBL:EXX74271.1, ECO:0000313|Proteomes:UP000022910};
RN [1] {ECO:0000313|EMBL:EXX74271.1, ECO:0000313|Proteomes:UP000022910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM197198w {ECO:0000313|Proteomes:UP000022910};
RA Lin K., Geurts R., Zhang Z., Limpens E., Saunders D.G., Mu D., Pang E.,
RA Cao H., Cha H., Lin T., Zhou Q., Shang Y., Li Y., Ivanov S., Sharma T.,
RA Velzen R.V., Ruijter N.D., Aanen D.K., Win J., Kamoun S., Bisseling T.,
RA Huang S.;
RT "Single nucleus genome sequencing reveals high similarity among nuclei of
RT an endomycorrhizal fungus.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005232, ECO:0000256|RuleBase:RU003801}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXX74271.1}.
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DR EMBL; JEMT01013053; EXX74271.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A015LNK5; -.
DR STRING; 1432141.A0A015LNK5; -.
DR HOGENOM; CLU_013513_5_1_1; -.
DR OMA; YDAFMCY; -.
DR Proteomes; UP000022910; 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:SF107; CARN_ACYLTRANSF DOMAIN-CONTAINING PROTEIN; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000022910};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801}.
FT DOMAIN 62..636
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT COILED 413..440
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 370
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 647 AA; 73351 MW; C3FE2B7F496DF46B CRC64;
MRTFLSSTSV RTLPSTIIKR YSLTIQNSKS YLICPILSRN YSLQIETDKP KTFSNQHIIP
RLPIPTLQET TERYKKSLLP ILKPEEYTRA ANAVDEFVKA DGLGEVLQKR LHELDKIEKY
SWLENIWLNK AYLEWREPSI INVNWWCEFK DHPNGVLKQV PKGQITDFQI NRTAGLISNT
LSFNDEINNE LLPPESTRQG PLCMNQYKKQ FGTTRIADSP VDRVISPWPA TAKHIIVLFR
DQIFKVQVLG EGGARVTIKD IERQLKSIVE QINNTNELQL PIGLLTGEHR DTWATARKAL
ESQSSENRSN FEAIDTALFS LSLDDYSTDS DIDVSHHNLF HAFNGRNRWF DKCLQLIVQS
NGRAGVNGEH SPADAVIPGR IFDYIVSKEP AQDPPNSSSI PLPTPQHLKW VTYPSLETIL
EKAQSNIQAA NDNVDSVLLH YNEYGSNWLK SAKLSPDAFI QMALQLAYYR RQGGPCPTYE
SASTRGFLHG RTETVRSCSI DSVAFTKAFD DKDFKKEQKL ALLTKAIETH LEYMISATNG
KGVDRHLLGL RCQIQTEEEK SRALIFTDPS YIQSMYFKLS SSNLSPGDYF YGGFGAVVPE
GYGVNYAIGK EGIKFSISSY KKYSETDSTS FRKILKNSLD DLRDFVA
//