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Database: UniProt
Entry: A0A1F5LVF0_9EURO
LinkDB: A0A1F5LVF0_9EURO
Original site: A0A1F5LVF0_9EURO 
ID   A0A1F5LVF0_9EURO        Unreviewed;       365 AA.
AC   A0A1F5LVF0;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN   ORFNames=PENARI_c002G07915 {ECO:0000313|EMBL:OGE57137.1};
OS   Penicillium arizonense.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1835702 {ECO:0000313|EMBL:OGE57137.1, ECO:0000313|Proteomes:UP000177622};
RN   [1] {ECO:0000313|EMBL:OGE57137.1, ECO:0000313|Proteomes:UP000177622}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 141311 {ECO:0000313|EMBL:OGE57137.1,
RC   ECO:0000313|Proteomes:UP000177622};
RX   PubMed=27739446; DOI=10.1038/srep35112;
RA   Grijseels S., Nielsen J.C., Randelovic M., Nielsen J., Nielsen K.F.,
RA   Workman M., Frisvad J.C.;
RT   "Penicillium arizonense, a new, genome sequenced fungal species, reveals a
RT   high chemical diversity in secreted metabolites.";
RL   Sci. Rep. 6:35112-35112(2016).
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|ARBA:ARBA00010871}.
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:OGE57137.1}.
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DR   EMBL; LXJU01000002; OGE57137.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F5LVF0; -.
DR   STRING; 1835702.A0A1F5LVF0; -.
DR   OrthoDB; 3626832at2759; -.
DR   Proteomes; UP000177622; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:InterPro.
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; IPR011095; Dala_Dala_lig_C.
DR   PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR   PANTHER; PTHR23132:SF25; D-ALANINE--D-ALANINE LIGASE A; 1.
DR   Pfam; PF07478; Dala_Dala_lig_C; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000177622}.
FT   DOMAIN          123..353
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   365 AA;  40055 MW;  7A98EC8FD954674E CRC64;
     MGDSNAYELV QALVSEQRSS YLQLGYSEEQ CAALTHDGEI DAVRTTLERL GHHVTLVPGI
     QFLVQQLAAG KDKGWDLVFN MSQGFHGSAR ESQVPAVLEA YQLPYTFSDA ATMALCQNKA
     ITKIILDRHM IPNAPFTVIP TLDGTADFPE HFAALPSYPL FVKPGTEGSS KGIENFNKVK
     NLEELKLAVR ELAYQFPGQD ILVESFLSGR EFTVSILGTG LHSRVIGIRE HIWQMAPDHS
     NKNGYHTNGT LDFASRDSKA SNGGKILLYN DSHDMDEPQI KAACQVALHT WKVFNCRDSG
     RVDIRFDSDK PGAIPNVLEV NPIAGLLPGH SPLPATAKIN GLSFKQLLSE IIGSALQRTP
     YKNGR
//
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