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Database: UniProt
Entry: A0A2G7FWF3_9EURO
LinkDB: A0A2G7FWF3_9EURO
Original site: A0A2G7FWF3_9EURO 
ID   A0A2G7FWF3_9EURO        Unreviewed;      1551 AA.
AC   A0A2G7FWF3;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   13-SEP-2023, entry version 23.
DE   SubName: Full=Nonribosomal peptide synthase GliP-like protein {ECO:0000313|EMBL:PIG84655.1};
GN   ORFNames=AARAC_001984 {ECO:0000313|EMBL:PIG84655.1};
OS   Aspergillus arachidicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=656916 {ECO:0000313|EMBL:PIG84655.1, ECO:0000313|Proteomes:UP000231358};
RN   [1] {ECO:0000313|EMBL:PIG84655.1, ECO:0000313|Proteomes:UP000231358}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 117610 {ECO:0000313|EMBL:PIG84655.1,
RC   ECO:0000313|Proteomes:UP000231358};
RA   Moore G., Beltz S.B., Mack B.M.;
RT   "Genome sequence for an aflatoxigenic pathogen of Argentinian peanut,
RT   Aspergillus arachidicola.";
RL   Submitted (MAY-2017) 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:PIG84655.1}.
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DR   EMBL; NEXV01000376; PIG84655.1; -; Genomic_DNA.
DR   STRING; 656916.A0A2G7FWF3; -.
DR   OrthoDB; 1949608at2759; -.
DR   Proteomes; UP000231358; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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   InterPro; IPR006162; Ppantetheine_attach_site.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   PANTHER; PTHR45527:SF11; NONRIBOSOMAL PEPTIDE SYNTHETASE 5; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00668; Condensation; 2.
DR   Pfam; PF00550; PP-binding; 2.
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.
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:UP000231358}.
FT   DOMAIN          1..75
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1044..1119
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          79..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..108
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1551 AA;  171327 MW;  964B6583026B517C CRC64;
     MNPSSQLLVQ QLAAVLEIDT AELDLDSGFV QNGGNSLSAV EFVSRCKSLG VSLSIASILS
     STNLRALFPN LLSSESNFIP IPDPSDDSDD LSNPSSSTGG SPRVATPISS NVSTAAEDDY
     PTQGSVLTQY ATDTLSEMQA SLLHGSLKSP GTNIIYHYET YQTDAIPILK KAWKTVIEGE
     PIFHSSLLDG SARNQEFFTW TEVTVETEAE YREQLQTLWL KSVSSSFKVV HWKRTPPNSS
     QSTVIWAVHH ALVDGYSAML LFCKVRRAVA GLPIVSGPSF SDVEKRIRIW RQEHKSEGDE
     YWAGHAAQLD QAQGELLLPA PTQEGTSSTI TESEEVYVAP SVSTTQLHCV AKRLGVTLST
     CYYAAWSLVL SLYADSASVV FGAVLAGRNL PLEGADEVVG PLVNTLPLCL TLDRQQSAQD
     FLKNLFSRMV ELAEYQWTTP DNGYTRNFSS AMAMQVPGPE CKDGVSPIQP PYTRQTTDVP
     LSINILTDGA ARFVYHTSQY NQPDIVRLGK YFQRALQLLL RPHRPIEECL QGLLGCVDLQ
     TLMGFGNCSS ALTTTVAIKE DLVTLFESAV SRNPMDVAVQ KGNCHLTYQE LDTHAGRVAA
     TLRSYIQDGD VVCLHADRSV NWIVGIMGIL KAGGVYCALD KALPQEARET IFSASGSRLF
     LVPSLSDQSF CPTDCDRLLV VEDLVKDDDV PITHRDSPRP QTDAYLCFTS GSTGKPKGVM
     CLHQGLVAFQ RDLEVRLFAQ PGRRVAQIMS VAFDGSIHEI FSALSYGATL VLQSGDDPFA
     HLSDVDSTIL TPSMARVLNP ADFERLSTVY LVGEPVTQDV CDRWAEQKTL YNMYGPTEGT
     CGATIKQLHP RQRVTIGPPN PSTRIYIMNQ HQELVPPGVI GEIYIAGVQV ARHYIGMPEQ
     TAQRFVADPV IRIGERMYKT GDRGYWSEDG EVVCLGRTDR QIKLRGFRLD LDDLETRMIR
     AFPAVTAVAL TRQGNHLIAA ILPASTDVDA FSMRVAQVLP PYATPRKILV LDEFPTTKAG
     KRDYQAIAKL SAQAPASTGR TLTSPMEKLV GDAFRDILQL GKDVALHTHS SFRELGGHSL
     LQLLLATRIS QGVNRQVPLY VVAQHDRIDH LAAAIDSGPG LQQLYQINES TSSFNVNFMA
     KIDDCLVDRA RLVHACNEVM ARHRVLRSRY IFSRAAGRVV RQYSPLAPRV QAVKTVNPWV
     EVNRPFSLSR SAPIRAVVSD SYFILTISHI VADLTTLQIL LREISSHYEG GSLPSIPHTY
     MNSTLWYEKP TSCDLDFWTD CLGQLPDTTH LLGHGGYRRG YRGRSALCEI PTTTYQSMRH
     YLRQSSITAQ QLSLATIALC LDNPSVPMPT ETDIVLGIPY INRKSQEDLD VVGLFLEPLP
     VRISFGQETH NNEKASYLDT VQRSVRSSVG HAIHWDQLLE HLQVPTTPPD HPLFDVVVTF
     HSQSHSNGLE LSAPGLQTCY TYAEGAKFRL LCEFSALSED RLLLRLEYDT DCFTEENIKL
     LQARIPLALS LLVQNVPYDM IRQTLARPPE TQPVKVLRPD VVFGTPLSDI Q
//
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