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Database: UniProt
Entry: A0A167N6P2_PHYB8
LinkDB: A0A167N6P2_PHYB8
Original site: A0A167N6P2_PHYB8 
ID   A0A167N6P2_PHYB8        Unreviewed;       704 AA.
AC   A0A167N6P2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Choline/carnitine acyltransferase domain-containing protein {ECO:0000259|Pfam:PF00755};
GN   ORFNames=PHYBLDRAFT_167469 {ECO:0000313|EMBL:OAD75150.1};
OS   Phycomyces blakesleeanus (strain ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC
OS   33097 / NRRL 1555).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Phycomycetaceae; Phycomyces.
OX   NCBI_TaxID=763407 {ECO:0000313|EMBL:OAD75150.1, ECO:0000313|Proteomes:UP000077315};
RN   [1] {ECO:0000313|Proteomes:UP000077315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 1555(-) {ECO:0000313|Proteomes:UP000077315};
RG   DOE Joint Genome Institute;
RA   Corrochano L.M., Kuo A., Marcet-Houben M., Polaino S., Salamov A.,
RA   Villalobos J.M., Alvarez M.I., Avalos J., Benito E.P., Benoit I.,
RA   Burger G., Camino L.P., Canovas D., Cerda-Olmedo E., Cheng J.-F.,
RA   Dominguez A., Elias M., Eslava A.P., Glaser F., Grimwood J., Gutierrez G.,
RA   Heitman J., Henrissat B., Iturriaga E.A., Lang B.F., Lavin J.L., Lee S.,
RA   Li W., Lindquist E., Lopez-Garcia S., Luque E.M., Marcos A.T., Martin J.,
RA   McCluskey K., Medina H.R., Miralles-Duran A., Miyazaki A., Munoz-Torres E.,
RA   Oguiza J.A., Ohm R., Olmedo M., Orejas M., Ortiz-Castellanos L.,
RA   Pisabarro A.G., Rodriguez-Romero J., Ruiz-Herrera J., Ruiz-Vazquez R.,
RA   Sanz C., Schackwitz W., Schmutz J., Shahriari M., Shelest E.,
RA   Silva-Franco F., Soanes D., Syed K., Tagua V.G., Talbot N.J., Thon M.,
RA   De vries R.P., Wiebenga A., Yadav J.S., Braun E.L., Baker S., Garre V.,
RA   Horwitz B., Torres-Martinez S., Idnurm A., Herrera-Estrella A.,
RA   Gabaldon T., Grigoriev I.V.;
RT   "Expansion of signal transduction pathways in fungi by whole-genome
RT   duplication.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005232, ECO:0000256|RuleBase:RU003801}.
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DR   EMBL; KV440978; OAD75150.1; -; Genomic_DNA.
DR   RefSeq; XP_018293190.1; XM_018435646.1.
DR   AlphaFoldDB; A0A167N6P2; -.
DR   STRING; 763407.A0A167N6P2; -.
DR   GeneID; 28996552; -.
DR   VEuPathDB; FungiDB:PHYBL_167469; -.
DR   InParanoid; A0A167N6P2; -.
DR   OrthoDB; 1429709at2759; -.
DR   Proteomes; UP000077315; 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; CARNITINE O-ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR22589:SF29; MITOCHONDRIAL CARNITINE O-ACETYLTRANSFERASE-RELATED; 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   Reference proteome {ECO:0000313|Proteomes:UP000077315};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801}.
FT   DOMAIN          30..625
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   ACT_SITE        334
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   704 AA;  79810 MW;  905013C8FB0E1EA6 CRC64;
     MANVKAHKNA LNFEPSGGET FRYQEQLPKL PIPELKDTLA RYLTSIQPLQ SVEEHERSKV
     AVKDFLENDG PKLQSKLLTY ATDKSSYIEE FWYDSYLQHS DPVVLNLNPF FVLEDDPTPL
     RNDQVIRASS LIYSTLKFID ALHDKTLEPD VFRGTPLCMS QFSRLFGTAR VPTDNGCYMA
     PGNESRHIVV MAHSQSYHFE VFDEFGETAL TEKEIAANLR AILRDAARIP VSDIAKTAIG
     VLTTEKRRNW ARLRAELKSD PTNRQSLKVI DSALFIVCLD HVEPTTIEDL SSNMLCGTYR
     LDQGLQVGTC TNRWYDKLQI IVCKNGSAGI NFEHTGVDGH TVLRYVSDIY TDTILRFAKT
     INSQTKSIFH SHKQKDSAAN RARRDSFGTG LSFDINPRRI EWNMTEPITL GVRYAETRLS
     DLILQNEVRV LEFNNYGKYF ITDMKMSPDA FVQMAFQAAY YGLYGKSECT YEPAMTKTFL
     HGRTEAIRSV TNASVNFVET YYSKAADHDK LESLRKALKS HTNLTRQCAQ GLGQDRHLFA
     LECLWNRMNK DTKKPLIFTD SGWKVLGHTM ISTSNCGNPA LRLFGFGPTV SDGFGIGYII
     KEDGISFAAS SKHRQTERLL KTLEKYLLDI QIMLQKEKYP GGISQRQRIL AMENADELNN
     GYSYFDNGEN FGSDKESSSG SIDGYLSRSP TRKVGKRLML RETD
//
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