ID A0A1B8DWP0_9PEZI Unreviewed; 1036 AA.
AC A0A1B8DWP0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=PKS/NRPS-like protein {ECO:0000313|EMBL:OBT63538.1};
GN ORFNames=VE03_07039 {ECO:0000313|EMBL:OBT63538.1};
OS Pseudogymnoascus sp. 23342-1-I1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1524831 {ECO:0000313|EMBL:OBT63538.1, ECO:0000313|Proteomes:UP000091879};
RN [1] {ECO:0000313|EMBL:OBT63538.1, ECO:0000313|Proteomes:UP000091879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=23342-1-I1 {ECO:0000313|EMBL:OBT63538.1,
RC ECO:0000313|Proteomes:UP000091879};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000091879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=23342-1-I1 {ECO:0000313|Proteomes:UP000091879};
RX PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT white-nose syndrome of bats.";
RL Nat. Commun. 9:35-35(2018).
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005232}.
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DR EMBL; KV455023; OBT63538.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B8DWP0; -.
DR STRING; 1524831.A0A1B8DWP0; -.
DR OrthoDB; 1750147at2759; -.
DR Proteomes; UP000091879; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
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 Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
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 InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR PANTHER; PTHR22589:SF115; CARNITINE O-ACETYLTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR22589; CARNITINE O-ACYLTRANSFERASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00755; Carn_acyltransf; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR PROSITE; PS00439; ACYLTRANSF_C_1; 1.
DR PROSITE; PS00440; ACYLTRANSF_C_2; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000091879};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 398..475
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT ACT_SITE 792
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 1036 AA; 115289 MW; 9E8A95625F6FF267 CRC64;
MAVLKTQNTS PSARLEENVL PPQDIVTPQI GFLFTGQGSQ WFNMGRELIG TTTAFGVSMR
KSDEFLSISQ SSWNLLDELH RSNHSSQVDK GHIAIPATTA IQIALVDLLE SLDILPHVVL
GHSTGEIAAA YASKILTHQD AIMVAFQLGQ VLHRRGLFDG CGKMLAVGLG ESEIQPYLDL
LDCRDVYIAC ENSPLSTTVS GSSATVDQLQ KNLQSLGIFN KGLIVPAAYH SPQMECIESE
YMASIHTIEP SSPESVNFYS STTGRRKLED FGPSYWINNV VSKVLYRSAL QKIIASTPSS
SQLLLIEIGP QPHLRRPTEE CICECNTNTT QLAYFSSLLR GKDACRAAYE LSHGISLRGY
PVHSGNLAKL GETYEAINAE KEISQGHKCF PINSNNNQAL KTIYQDLSDE ILKLTGNSRS
ECQAELPISD YGLDSLLAVE FADWINQKYA LHFSVGEIFD ASSLLALVQS IGMLTQDYAS
NIDEPPPPKK VVASQGLNGL PRLPLPNLRS TLENYYSSVE CFGTDSELLT TQQTIGNFIN
SEEGCKLQDR LLARVHDPIL DCWLADLYNG SNFLDRNVPL VPFGSFFYTH KLSKFQHTQA
ERAAVVTKAA LQYKEDLESG IISPDILQGQ PSCTYLFKYL FNTSRKPCIG SDIIGRFLGN
NYIVVLWRGR AFKVPLYDNG SQLSFVQLKG IFERIMQKAD GDSLQVGILT SDERTSWAKI
RKSLQVLHPQ NLQYLHAIEA AAFLVCLDEA SPETASERAH HFHFGTGGNR WNDKSVQFVV
CTNGVSGFVG DHSMLDAGTV LGLNRFVTRA ILQHRHEPDI SPSVVVDISA YLDEKKLVIS
PYIDLEISRV IQDFNENIKD ANHVFFTLSN FGGSICRLNN YPPKSLFQLI VALASKLYFG
AIVPLWETVS LGNFHRGRVE INQVITPPVL RFLNAAQDLC IPISERQRLL LEATKLHAAS
VMRAVRGRGV DRHITSLRQM VKEGEAVPRL FTDPLYERTR PRKIMSHCHE TGMAEKGFLL
RDPESIWVHY EVEDER
//
