ID A0A1V6QLB8_9EURO Unreviewed; 377 AA.
AC A0A1V6QLB8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN ORFNames=PENANT_c002G06115 {ECO:0000313|EMBL:OQD89787.1};
OS Penicillium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD89787.1, ECO:0000313|Proteomes:UP000191672};
RN [1] {ECO:0000313|Proteomes:UP000191672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQD89787.1}.
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DR EMBL; MDYN01000002; OQD89787.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6QLB8; -.
DR STRING; 416450.A0A1V6QLB8; -.
DR OrthoDB; 3626832at2759; -.
DR Proteomes; UP000191672; 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:SF0; D-ALANINE-D-ALANINE LIGASE FAMILY; 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 Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000191672}.
FT DOMAIN 122..365
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 377 AA; 41235 MW; C3FE8152123B1CFE CRC64;
MTRSKSNLLI ALIYEDPQIY RDLGYPASHI SHLEVCTPAE DVIVTLHRLG HRVIPIPDVQ
MLARKLGAGE GAQWDLAVNI AVGVYGAARE AQVPAMLEAF GVPFTFSDTA TMALCLDKGK
TKMVLEHYGI PTSPFAIINL DRHPDKLITP NIINSLTKGS KHASSLLDPA SYPLFAKPLA
EDTSKGIKQI SVIHNVNQLC QAVEELRSST RAIPAILVEK FLAGREFTVG ILGTGDDAWV
LGVDEIVWKD QLNGDRDSDV DVDVVPFATE KAKTREDWDG ITDEIPANRA DPLVERACTV
ALRAWRAIGC RDGGRVDIRF DASAGVANVL EINPLAGLKP EWAQLPTIAA HNGMSFQTLF
EHILRSALKR APAQWRM
//
