ID A0A023AZW3_GRENI Unreviewed; 326 AA.
AC A0A023AZW3;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=D-alanine-D-alanine ligase {ECO:0000313|EMBL:EZG44586.1};
DE EC=6.3.2.4 {ECO:0000313|EMBL:EZG44586.1};
GN ORFNames=GNI_145850 {ECO:0000313|EMBL:EZG44586.1};
OS Gregarina niphandrodes (Septate eugregarine).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Gregarinasina;
OC Eugregarinorida; Gregarinidae; Gregarina.
OX NCBI_TaxID=110365 {ECO:0000313|EMBL:EZG44586.1, ECO:0000313|Proteomes:UP000019763};
RN [1] {ECO:0000313|EMBL:EZG44586.1, ECO:0000313|Proteomes:UP000019763}
RP NUCLEOTIDE SEQUENCE.
RA Omoto C.K., Sibley D., Venepally P., Hadjithomas M., Karamycheva S.,
RA Brunk B., Roos D., Caler E., Lorenzi H.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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:EZG44586.1}.
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DR EMBL; AFNH02001082; EZG44586.1; -; Genomic_DNA.
DR RefSeq; XP_011134152.1; XM_011135850.1.
DR AlphaFoldDB; A0A023AZW3; -.
DR EnsemblProtists; EZG44586; EZG44586; GNI_145850.
DR GeneID; 22915129; -.
DR VEuPathDB; CryptoDB:GNI_145850; -.
DR eggNOG; ENOG502S30X; Eukaryota.
DR OMA; RVDFFYV; -.
DR OrthoDB; 3626832at2759; -.
DR Proteomes; UP000019763; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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 HAMAP; MF_00047; Dala_Dala_lig; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR000291; D-Ala_lig_Van_CS.
DR InterPro; IPR005905; D_ala_D_ala.
DR InterPro; IPR011095; Dala_Dala_lig_C.
DR InterPro; IPR011127; Dala_Dala_lig_N.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR NCBIfam; TIGR01205; D_ala_D_alaTIGR; 1.
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 Pfam; PF01820; Dala_Dala_lig_N; 1.
DR PIRSF; PIRSF039102; Ddl/VanB; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00843; DALA_DALA_LIGASE_1; 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 Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EZG44586.1};
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:UP000019763}.
FT DOMAIN 122..322
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 326 AA; 36504 MW; 94760CE499F9FCDF CRC64;
MRKRIIAIVA GGCSSELEVS LRSGQGISSF MDKERYDLYI VEVEGRRWEV ILPDGTKSAI
DRNDFSFTES GEKRTFEFAY ITVHGRPGEN GMLQGYFDLI GMPYSSCSVL VSAMTFSKFT
CNQYLKGFGV RVSESLILRS GFEISDEEVI NKIGLPCFVK PNAGGSSFGV SKVKTREDIQ
QAIRKAFKED NEVMIEASME GTEITCGCYK TRDKETVFPI TEVVSTNEFY DYNAKYRKQS
QNFTPARIPE ETATKVRQLT SSIYDILGCS GLVRIDYIIT KGDNINLLEI NTTPGMTDTS
FIPQQVRAAG LDIKDVMTDI IENKFS
//
