ID   A0A317X9D2_9EURO        Unreviewed;       650 AA.
AC   A0A317X9D2;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN   ORFNames=BO94DRAFT_563698 {ECO:0000313|EMBL:PWY94242.1};
OS   Aspergillus sclerotioniger CBS 115572.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1450535 {ECO:0000313|EMBL:PWY94242.1, ECO:0000313|Proteomes:UP000246702};
RN   [1] {ECO:0000313|EMBL:PWY94242.1, ECO:0000313|Proteomes:UP000246702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 115572 {ECO:0000313|EMBL:PWY94242.1,
RC   ECO:0000313|Proteomes:UP000246702};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-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:PWY94242.1}.
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DR   EMBL; MSFK01000005; PWY94242.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317X9D2; -.
DR   STRING; 1450535.A0A317X9D2; -.
DR   OrthoDB; 2149754at2759; -.
DR   Proteomes; UP000246702; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
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:UP000246702}.
FT   DOMAIN          305..542
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   650 AA;  72531 MW;  3AB75F72F3B5E62B CRC64;
     MIGWHTSQST ANCFSLLSLP TEWWQSVDVI LQSESGTHPP AWPEDSRDVQ LWSWDSSWME
     LGTQDWGSPF TLAFFLRALK CANTSTGSAI RLVFPSESGY LVRSDILSLR MVDLEPVEST
     VSFVATPGKP FGPLLIDSNT APIFPHAIMN STVGGILLRT PSAHEDYQDL FRQLDDEFTN
     RLSFPWHLAS PPQRKTLAIV EGGRTGPDHG GLATGIYAAA DALNIDMIVL DVPGHWLEGP
     KYASWRKEFV PVELEPPSLL ADRIVEALSR FNVDGIVTFC DSYQVPVAQA AKRLRLPTHP
     PEAYEIATDK HRTAVSEGRP AYRVHNLEEA FDIVDRENLV YPFIIKPCKG FLSEGVFKVH
     GPEELSHAIS NIHLDRHGTE VVLEAYCDGP KVDINLVLSE GELVFCEVTD DFPKTADEDS
     ETTESTGQLK SFLELTCVMP SKLPTSEIDL LRNSLHQSLL RLGLTTGIYH VEARVQHSSM
     EYGKSDAATA LVDLIPLVNP DEKKPSVWLI EINPRFPGIQ ETVAVESAYG VDYRGIGLLA
     GLRDHDRLRA LAQPFRQGPQ YWTQIVCIPV PIEGTFDSDD VCVELKQRRP DFARQICMSA
     CFVKRGDRVY GLESGINSWV AYFNVFSRIS RQHALGLGET VRRETRFTII
//