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Database: UniProt
Entry: A0A0F0IFZ7_ASPPU
LinkDB: A0A0F0IFZ7_ASPPU
Original site: A0A0F0IFZ7_ASPPU 
ID   A0A0F0IFZ7_ASPPU        Unreviewed;       565 AA.
AC   A0A0F0IFZ7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=AMP-binding enzyme {ECO:0000313|EMBL:KJK66744.1};
GN   ORFNames=P875_00127919 {ECO:0000313|EMBL:KJK66744.1};
OS   Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK66744.1, ECO:0000313|Proteomes:UP000033540};
RN   [1] {ECO:0000313|EMBL:KJK66744.1, ECO:0000313|Proteomes:UP000033540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC   {ECO:0000313|Proteomes:UP000033540};
RA   Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA   Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT   "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL   Submitted (FEB-2015) 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:KJK66744.1}.
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DR   EMBL; JZEE01000233; KJK66744.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0IFZ7; -.
DR   STRING; 1403190.A0A0F0IFZ7; -.
DR   Proteomes; UP000033540; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR025110; AMP-bd_C.
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   PANTHER; PTHR24096:SF149; 4-COUMARATE--COA LIGASE 1-RELATED; 1.
DR   PANTHER; PTHR24096; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000033540}.
FT   DOMAIN          32..394
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          448..525
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   565 AA;  62537 MW;  3FE14E621C7FD1C5 CRC64;
     MIFDSKLPLP AVPSCDAFNY IFHQGRRNYS TDRVLYRVDG SDETLTFGEL EQKSRQFADA
     IREYYDIEPN DVVAILAKDK IQYPIAYYGI LAAGAVVAPI PVQKEMSETD VAARLEQAKA
     KLVITDSELL RLTEVASMLA GCISVMTLDA NDQNWPCVDS LLPMGNPDAQ IFELKTPQEV
     DQHNAFINRT SGSTGTMKSV LTSHAHYIAT MEATVGTIPA DTDPDRDVWV SPLSLGFFIN
     AKLHMGLNIL LGIPVVLMKH TLDETTVDVV ARHHITFLFI TPPIAARLAR ADLRHIDVSS
     VKWLLTAGAP MHENLRRTVS RQFGGVHLTL EWATSETMLL AMQVDERSKQ PGSSGTLVNG
     IQARVINVET GRECSYGEEG EILVRNAIAR FKGYKDNEVA NRDFDSEGWF HTGDYGYLDQ
     NCNVYIVDRI KELLKVGEGY GSHVSAAEIE AILFEHPAVS SVVVVGVRNT ETQVDEPTAF
     VIAKPEYRSR TAQVTRDIER YARAKLTGLR RLTGGVHCIS SYPTTGFKIN RRALKSMAPS
     KMPKMPVVPS CLLPTMSAIS AMRMV
//
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