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Database: UniProt
Entry: A0A8E0QS26_9EURO
LinkDB: A0A8E0QS26_9EURO
Original site: A0A8E0QS26_9EURO 
ID   A0A8E0QS26_9EURO        Unreviewed;       663 AA.
AC   A0A8E0QS26;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   02-APR-2025, entry version 10.
DE   RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN   ORFNames=Aud_006841 {ECO:0000313|EMBL:GIC90407.1};
OS   Aspergillus udagawae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=91492 {ECO:0000313|EMBL:GIC90407.1, ECO:0000313|Proteomes:UP000036893};
RN   [1] {ECO:0000313|Proteomes:UP000036893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 46973 {ECO:0000313|Proteomes:UP000036893};
RA   Kusuya Y., Takahashi-Nakaguchi A., Takahashi H., Yaguchi T.;
RT   "Draft Genome Sequence of the Pathogenic Filamentous Fungus Aspergillus
RT   udagawae Strain IFM 46973T.";
RL   Genome Announc. 3:e00834-15(2015).
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:GIC90407.1}.
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DR   EMBL; BBXM02000005; GIC90407.1; -; Genomic_DNA.
DR   RefSeq; XP_043147673.1; XM_043291738.1.
DR   GeneID; 66994318; -.
DR   Proteomes; UP000036893; 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; 3.30.1490.20; ATP-grasp fold, A domain; 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; 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}.
FT   DOMAIN          323..551
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   663 AA;  73410 MW;  2308E9F2FA1916B5 CRC64;
     MATQERLQVR SKNNEGLFRE YSFILSSPPT ESSWQSLDFL FWEEPGYHGP DLLNAPDDIR
     IFQLDQDDAS KEITPASLGS PKAFGFLLQI LRASASGAKC AVKLIVPLHS GFIVRSDIIP
     LRLRDSEYVE SALSFALPLQ TYSGKKIAIS SRLDLTTYFA PATAGLILRQ GSTHVSDAGH
     QALFRNVESD LENRLSFPWI QPGTPRRRTL ALVDANSSHP EDGLGFYRAA RELGINVVVL
     ENSGHWLEDP AQAQWREAFI PTRLTNPPEE DVGDHILASL RAYGKPVDGI VTFADSFWYY
     IAQIAHEIGV DTAPPDSMRI ATNKFLTSKY VGHEAYLASN VDEALKIAEE VELPYPLIVK
     PCDGWSSEGV SRVESPDAFP AAIKSIDTSR HGTEFVMEPY CDGPEVDVNL VLLDGQVLFA
     EICDDLPKSA DVNGPTVGSL TNFHELNSVY PSALPSQELD LLINSFVGTL LSLGIRNGVM
     HLEGRVENSS MEYREQNGMM DLQPRAPQAT RPEPSAWLIE INPRPLGMTG SHIIESTYGI
     DYWGLAVVLG VGDKDRARAL SKPYRCGPQY TCIMVFIPAD FPPSSQGIFD TDDICADLLA
     RRPDLAKHIS RCATLVKRGQ KVAHPTTGRH TFLAYFNVFS RAGRQEALDL ARQVREEVRY
     SFL
//
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