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Database: UniProt
Entry: A0A5N7ARE0_9EURO
LinkDB: A0A5N7ARE0_9EURO
Original site: A0A5N7ARE0_9EURO 
ID   A0A5N7ARE0_9EURO        Unreviewed;       669 AA.
AC   A0A5N7ARE0;
DT   22-APR-2020, integrated into UniProtKB/TrEMBL.
DT   22-APR-2020, sequence version 1.
DT   05-FEB-2025, entry version 13.
DE   RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN   ORFNames=BDV26DRAFT_302826 {ECO:0000313|EMBL:KAE8371330.1};
OS   Aspergillus bertholletiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=1226010 {ECO:0000313|EMBL:KAE8371330.1, ECO:0000313|Proteomes:UP000326198};
RN   [1] {ECO:0000313|EMBL:KAE8371330.1, ECO:0000313|Proteomes:UP000326198}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 29228 {ECO:0000313|EMBL:KAE8371330.1,
RC   ECO:0000313|Proteomes:UP000326198};
RG   DOE Joint Genome Institute;
RA   Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S.,
RA   Kildgaard S., Isbrandt T., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA   Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA   Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA   Riley R., Salamov A., Simmons B.A., Magnuson J.K., Henrissat B.,
RA   Mortensen U.H., Larsen T.O., Devries R.P., Grigoriev I.V., Machida M.,
RA   Baker S.E., Andersen M.R.;
RT   "Friends and foes A comparative genomics studyof 23 Aspergillus species
RT   from section Flavi.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; ML736437; KAE8371330.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5N7ARE0; -.
DR   OrthoDB; 434648at2759; -.
DR   Proteomes; UP000326198; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR052032; ATP-dep_AA_Ligase.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR041472; BL00235/CARNS1_N.
DR   PANTHER; PTHR43585:SF2; ATP-GRASP ENZYME FSQD; 1.
DR   PANTHER; PTHR43585; FUMIPYRROLE BIOSYNTHESIS PROTEIN C; 1.
DR   Pfam; PF13535; ATP-grasp_4; 1.
DR   Pfam; PF18130; ATPgrasp_N; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000326198}.
FT   DOMAIN          318..561
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   669 AA;  74373 MW;  A508B760AF12CD8F CRC64;
     MAAQDSILSF QSVLATQDSA FPISIYELPK LAQGPSQILC RWGVHTADPV LEPFGFTTVE
     MVLWSTSEPI QKGSFARSVQ MNNHALEKFM LQAIGRAKRG VPIGFQLLLP VSVSYVARSD
     ILEFRMQGCD CVATAAGLMQ SREKLSPWTQ STHGGDEICL EKVLNGAIGV IQAKNAPGVP
     VTEALDQVKT AIVNRLSFRW LLPEPVQPRR LAMVEVRPDH KSIEAIYSLG IQLIVLDQPG
     HWLEPDEGPY AHLRESFVPF DTNVDSHFGD RLTRALEALR VDGVVTRNDR LVTAVARVAE
     TLGFPTSPAV AFEKATNKYA TRLSEIERGF ALCVSGPSDL QEKLHPSDRS EPIRLEYPLV
     VKPCEGDGSH CVSKVSTETQ LFQAVEKVGH RIIRHEGAVP VPSDVLIEPY IDGPEVDVNF
     VLWDGEVLFS DVSDDFPSDA DSPEATAADT FQETAFAHPS RLPPSEQDLL RQVLLDRILH
     MGFRSGIFHV EARVRHSAMK YTKRDGTLDL RYHEMRDETH EPKASVFLVE VNARPPGYYG
     LMSLAWTYGV DYFALHVLHA LSDETRMRAL SQPFLHGPQH DGALMLVLPE RGGVLTSGDP
     AETFRKEHPE VMDNILLRRE PFAMGDFVPG PDAPTMGFLS VLVVRSTMGR AGLLRNMAMI
     RRDWRHTIE
//
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