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Database: UniProt
Entry: A0A1Y2WNR6_9PEZI
LinkDB: A0A1Y2WNR6_9PEZI
Original site: A0A1Y2WNR6_9PEZI 
ID   A0A1Y2WNR6_9PEZI        Unreviewed;      1695 AA.
AC   A0A1Y2WNR6;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN   ORFNames=K445DRAFT_370464 {ECO:0000313|EMBL:OTB11245.1};
OS   Daldinia sp. EC12.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Daldinia.
OX   NCBI_TaxID=1001832 {ECO:0000313|EMBL:OTB11245.1, ECO:0000313|Proteomes:UP000243732};
RN   [1] {ECO:0000313|EMBL:OTB11245.1, ECO:0000313|Proteomes:UP000243732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC12 {ECO:0000313|EMBL:OTB11245.1,
RC   ECO:0000313|Proteomes:UP000243732};
RX   PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA   Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA   Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA   Henrissat B., Gladden J.M.;
RT   "Characterization of four endophytic fungi as potential consolidated
RT   bioprocessing hosts for conversion of lignocellulose into advanced
RT   biofuels.";
RL   Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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DR   EMBL; KZ112965; OTB11245.1; -; Genomic_DNA.
DR   STRING; 1001832.A0A1Y2WNR6; -.
DR   OrthoDB; 1949608at2759; -.
DR   Proteomes; UP000243732; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   CDD; cd19537; C_NRPS-like; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 2.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00668; Condensation; 2.
DR   Pfam; PF00550; PP-binding; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 2.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243732}.
FT   DOMAIN          32..111
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1129..1204
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1695 AA;  187405 MW;  7AC8D6A6733AD8BA CRC64;
     MMRKSLPPSG LGVHEAEILV ISEGENNVNK FDDRNEFVSI IVRAISTVLG VSEDEIHYTA
     DTTTFIKLGG NSLSAILISA ECQRKGILIP AGVFLRISTV KEVITTAASL AQHISRPIPT
     IIVTEDTRDD VEGDTSGDEV SSLYTAITTP DPETEDLSLF GCGKDIITAE SLLSKIDPNE
     WTEPQLLLLR ETSQNQKLNI LTLHESYTGD WDAQIICDAF ADTILSESIF KDLLRDLDVL
     PQQFLLRQII QIQSEDDLQR EIRTAVNATG PITKLTVVQF SPPLESNDTP KTTTVIWRIH
     HAFMDGYSAR ILHDKITRIL RGGEFGVPAG PSFRETVRSL RVLREEKSES TRRFWDTKRE
     QFPTAIGELR LSPQRVAKSA EVPPQKSVTI EFPSEKLVAA VTRTGYTSTV FFAAAWALTL
     GKFVDADQVC FGVVFSGRDL PIPGAFDVVG PLINILPLFV QVPAKGDDTS VETFLRRIHA
     DILDLNNVQH SDSTEGFDRK FHSIMATQFE CDEGESPSPI PVDRNRPDMR SGTPLNIVIE
     EECRLQMLYS TAHFADEDMN NLRSVFQNSV NYLLVEDKEK QLVSNINDTL LPYQMEQTIR
     EWSNCASPET FDESKGDDLV TLFENVVAKQ ANEMAIIHGE IQVSYDELDR AAGIIARKLS
     WIEPNEAVCV YADRSVNWLV AIFGVLKAGG VYAPLDPSAP VSVRRANFIR SGARAVLVPS
     RASSQHVVSS RQEEDDVAPF QCLVLSVDDL LVADSTQAGD SYYPRRRIAR PDDLAYICFT
     SGSTGQPKAV QCTHKGLVAF QKDRVVRLGA SKGVVIAQIM SPVFDGSIHE IFSALTHGAT
     LRLASPDHQG DPFSHLRDSD AAILTPSIAK ALDLNQYPRL KNVYLVGEAV PQSLCKTWAR
     ERSLYNMYGP TEATCGATIK QLFPNEAVSL GRPNPSSRVY ILDHNLCLLP PGAVGELYIA
     GIQVSRGYIK LPEQNATCFL KDSVMPETGQ KMYRTGDYAY WNSATGEICI LGRKDRQIKL
     NGFRLDLDDL EARVVKAIPG CGGAAIFRRD DHLIAAYQTT SLNAVSALDV KAYVSNALPP
     YAMPRRIVAF EEFPLTAAGK LDYKTIEKSI STSLADTKIE AQPQRRAMST TEKMVSDVVR
     DLMRLDPSVS VDQESNLTEL GCHSILQLQL ASRISSLIQR HFPVRNVIEN LVVSRLASAI
     DDALGEGPKI EAAVSGQTSN LASGEIKTLG ESGISPIERD WFLKYRRNLG TSSFNVSHVS
     ELDVSFDQHQ ALMSAWDAVL ARHDILRCRF RQSEDGNVER SYVVDPPKAQ YLDDFDVRAE
     INKEFSLETQ DPIRVLVSKR HMLVCVSHII CDYTTLDHLF EEFTSVYSNF DNEDLTIFPQ
     KRYQDTTCWN LEVDQTTTDF WKSYLSGVDF TGTPPYLKAP RTSYHGESLL FRLSKNTMSS
     LQTVSQSLRL TLHQIALAVV SLVLQADNPT KQDLFLGSPY LGRQEEDMHT IGLFLQPLPI
     RIRRRSDQHD GDFKEAPLAT FLQAVQDSSR SALGHAVEWS SLMHILSSSN DENLRAAAAT
     PIPNNPLFDA MVTFHELDTT GKSSSSAIPG VEPLVNWAEG AKFGIMFEFS AVSSSAVTLR
     VEYDAALFSP DEVRLFVARV DAGFRYLCEN STSGTLGELE GKLLDVGVEG FSGGDGGKSG
     GIEVVEFGTP IAALA
//
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