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Database: UniProt
Entry: J9VIM7_CRYNH
LinkDB: J9VIM7_CRYNH
Original site: J9VIM7_CRYNH 
ID   J9VIM7_CRYNH            Unreviewed;       759 AA.
AC   J9VIM7;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Carnitine acetyltransferase {ECO:0000313|EMBL:AFR94307.1};
GN   ORFNames=CNAG_05042 {ECO:0000313|EMBL:AFR94307.1};
OS   Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS   CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=235443 {ECO:0000313|EMBL:AFR94307.1, ECO:0000313|Proteomes:UP000010091};
RN   [1] {ECO:0000313|EMBL:AFR94307.1, ECO:0000313|Proteomes:UP000010091}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487
RC   {ECO:0000313|Proteomes:UP000010091};
RX   PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA   Janbon G., Ormerod K.L., Paulet D., Byrnes E.J.III., Yadav V.,
RA   Chatterjee G., Mullapudi N., Hon C.C., Billmyre R.B., Brunel F., Bahn Y.S.,
RA   Chen W., Chen Y., Chow E.W., Coppee J.Y., Floyd-Averette A., Gaillardin C.,
RA   Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S., Hamlin J.L.,
RA   Hsueh Y.P., Ianiri G., Jones S., Kodira C.D., Kozubowski L., Lam W.,
RA   Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K., Proux C.,
RA   Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A., Zeng Q.,
RA   Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA   Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA   Cuomo C.A., Dietrich F.S.;
RT   "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT   grubii reveals complex RNA expression and microevolution leading to
RT   virulence attenuation.";
RL   PLoS Genet. 10:E1004261-E1004261(2014).
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005232, ECO:0000256|RuleBase:RU003801}.
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DR   EMBL; CP003823; AFR94307.1; -; Genomic_DNA.
DR   RefSeq; XP_012048682.1; XM_012193292.1.
DR   AlphaFoldDB; J9VIM7; -.
DR   GeneID; 23888398; -.
DR   KEGG; cng:CNAG_05042; -.
DR   VEuPathDB; FungiDB:CNAG_05042; -.
DR   HOGENOM; CLU_013513_5_0_1; -.
DR   OrthoDB; 1429709at2759; -.
DR   Proteomes; UP000010091; Chromosome 4.
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: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; 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   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          69..736
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   REGION          173..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..198
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        464
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   759 AA;  84184 MW;  38B8A4A5EAAC9E12 CRC64;
     MIIPSSIHRI QSVHTPLRTL RATSLFTVSA PTHPASITAR NVSRRMFAAS TYRSNQPKTF
     ENQSKLPRLP VPDLEASLEG YLKSLGPLLE EKYDKASLSN EVEKRQLYVK DFASTGGLGR
     VLQERLKDLD HVSPNNWLND TLWLALAYHT WRAPLLVNSN WWLCFAEDPL SPPPPSLPSS
     TKESNATRAQ TATIKVPNPS PLTDVPAGGQ GGGKEWLVSG SIDPPVQYEK VVKKEWITPW
     QIRRAAWIAR RFAEFRTKLE REEIKPDEIK GVKFCMNQYA NMFNLSRIPL PNCDAFSTPS
     PLSTHLSLLV DDYYYAIDIF SPPSSSADGV PEPLPAGEIE KRFQAAVDDA KRRKERGERA
     VEVGVLGADD RDNWTKNREH LLLLSPSNRS TLTSLSTSLL ALSLDPYTLP SVPPPSGDPL
     RLPAVDAQVR NCATGIDGGR NRWFDKAVSV LVETNGRAGI MGEHSPVDAL IPSIVVEYVL
     DKPVDGSQFM SSAPVPVATG KSGEGWEKLD WAVDEAILQE IEQVKQRNQK LIDDSDASQL
     WWGEYASEWI KKIAKQAPDA YIQQALQLAW FLDQGYPTAT YETASTRTML HGRTDVIRSL
     TSESRAFVKA MVNPESTAEE RYRLLSSACQ AHNALTKRSS SGHGYDRHLM GLKVQLRAGE
     THPLFEDEVY AKSQEWKLST SGLSAGGKFT ATGFGAAWPD GYGINYMAGP HLIKFGIESK
     FSCEKTSTQR FKHNIVQVLR DMRAVCEAVG GVDASRAKL
//
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