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Database: UniProt
Entry: A0A914YBQ0_9BILA
LinkDB: A0A914YBQ0_9BILA
Original site: A0A914YBQ0_9BILA 
ID   A0A914YBQ0_9BILA        Unreviewed;       193 AA.
AC   A0A914YBQ0;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   18-JUN-2025, entry version 10.
DE   SubName: Full=ATP-grasp domain-containing protein {ECO:0000313|WBParaSite:PSU_v2.g16713.t1};
OS   Panagrolaimus superbus.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Panagrolaimoidea; Panagrolaimidae;
OC   Panagrolaimus.
OX   NCBI_TaxID=310955 {ECO:0000313|Proteomes:UP000887577, ECO:0000313|WBParaSite:PSU_v2.g16713.t1};
RN   [1] {ECO:0000313|WBParaSite:PSU_v2.g16713.t1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2022) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|ARBA:ARBA00010871}.
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DR   WBParaSite; PSU_v2.g16713.t1; PSU_v2.g16713.t1; PSU_v2.g16713.
DR   Proteomes; UP000887577; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   FunFam; 3.30.470.20:FF:000008; D-alanine--D-alanine ligase; 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; IPR000291; D-Ala_lig_Van_CS.
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.
DR   PROSITE; PS00844; DALA_DALA_LIGASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Reference proteome {ECO:0000313|Proteomes:UP000887577}.
FT   DOMAIN          4..177
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   193 AA;  20640 MW;  610842895039F178 CRC64;
     MSMAVVAQLG LPLSXAQXGS SVGVSKVKDA AGFAEALELA LRYDHKVLVE SAVVGREIEC
     AVLGNEHPQA SLCGEVVVHD EFYAYDTKYI NEDGAEVVVP ADIDAATQAR IQQVALQAYQ
     ALECAGMARV DVFLTAGGDI IINEVNTLPG FTRISMYPKL WGASGVDYTT LITRLIELAQ
     ERHAADRGLH SVV
//
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