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Database: UniProt
Entry: A0A1Y2E9U5_9PEZI
LinkDB: A0A1Y2E9U5_9PEZI
Original site: A0A1Y2E9U5_9PEZI 
ID   A0A1Y2E9U5_9PEZI        Unreviewed;       470 AA.
AC   A0A1Y2E9U5;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Condensation domain-domain-containing protein {ECO:0000313|EMBL:ORY68358.1};
DE   Flags: Fragment;
GN   ORFNames=BCR38DRAFT_422904 {ECO:0000313|EMBL:ORY68358.1};
OS   Pseudomassariella vexata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Pseudomassariaceae; Pseudomassariella.
OX   NCBI_TaxID=1141098 {ECO:0000313|EMBL:ORY68358.1, ECO:0000313|Proteomes:UP000193689};
RN   [1] {ECO:0000313|EMBL:ORY68358.1, ECO:0000313|Proteomes:UP000193689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 129021 {ECO:0000313|EMBL:ORY68358.1,
RC   ECO:0000313|Proteomes:UP000193689};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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:ORY68358.1}.
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DR   EMBL; MCFJ01000003; ORY68358.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2E9U5; -.
DR   STRING; 1141098.A0A1Y2E9U5; -.
DR   InParanoid; A0A1Y2E9U5; -.
DR   OrthoDB; 2639360at2759; -.
DR   Proteomes; UP000193689; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   CDD; cd19542; CT_NRPS-like; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   Pfam; PF00668; Condensation; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193689}.
FT   DOMAIN          1..72
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   NON_TER         470
FT                   /evidence="ECO:0000313|EMBL:ORY68358.1"
SQ   SEQUENCE   470 AA;  52333 MW;  8F70D3D771A312A1 CRC64;
     MELKLQRLWS EVLGVGLEAI SPEDNFFRLG GDSVTAMKLA AAFRRQKLKL SVKQIFSFQT
     IALQAASTKC LSMLDEPLRS QHGPMAPFSL STALSSAELS SMISRFPVDE VLDVLPATHF
     QHMIISRGVK SSHAALNYPV LNLGRSVEVE RLQDACRSVV AHLEVLRTVF VEHGNRTWQI
     VLRHLDPPFY TIDQASSRDD LPRSIITQAS TCVGGSYPML SFTLVYQQSS ELQLVVGLSH
     AQYDGFCMPQ FLKSLSHAYY GVQLPRTVPF STYMYSRAAR HAESVSFWKK YLEGSRLINL
     SSHLSTTSQS GVPSRVIETS GMLEHIELPT LPNGITVSSF LQAAWALTLL HATNVQDMVY
     AIVVAGRNST IHEIDDVVGP CVNIIPVRLI FSPNWTALDL VKAVQSQVLT IGEQDSLGFN
     EIVQQCTDWP SISTFDAFFQ SQNVDEHPEH NISGSQTQLQ WMENPYVEQD
//
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