ID   A0A0D9X375_9ORYZ        Unreviewed;       921 AA.
AC   A0A0D9X375;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
OS   Leersia perrieri.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX   NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR07G23940.1, ECO:0000313|Proteomes:UP000032180};
RN   [1] {ECO:0000313|EnsemblPlants:LPERR07G23940.1, ECO:0000313|Proteomes:UP000032180}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.A.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:LPERR07G23940.1, ECO:0000313|Proteomes:UP000032180}
RP   NUCLEOTIDE SEQUENCE.
RA   Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA   Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA   Zhang J., Wing R.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:LPERR07G23940.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|ARBA:ARBA00010871}.
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DR   AlphaFoldDB; A0A0D9X375; -.
DR   STRING; 77586.A0A0D9X375; -.
DR   EnsemblPlants; LPERR07G23940.1; LPERR07G23940.1; LPERR07G23940.
DR   Gramene; LPERR07G23940.1; LPERR07G23940.1; LPERR07G23940.
DR   eggNOG; ENOG502QS9K; Eukaryota.
DR   Proteomes; UP000032180; Chromosome 7.
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: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; -; 2.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
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   InterPro; IPR011127; Dala_Dala_lig_N.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
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; 2.
DR   Pfam; PF01820; Dala_Dala_lig_N; 2.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR   PROSITE; PS50975; ATP_GRASP; 2.
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};
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:UP000032180}.
FT   DOMAIN          201..445
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          692..917
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   REGION          14..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   921 AA;  100696 MW;  D2B2404360509E8C CRC64;
     MLIPLPLLVQ APLTTTTPRL RRPSAPPPPR LHRPRIALAS PRLAGAPPPA LLSEREMGVA
     AESEGARPLR VGLVCGGPSA ERGVSLNSAR AVLDHIQGED LLVSCYYIDA AMNAFAISPA
     QLYSNTPSDF DFKLESLAQG FQSLSDFAGH LAANVDIVFP VIHGKFGEDG GIQELLEEAN
     VPFVGSPSKN CLTAFDKYNA SLELSAQGFL TVPNFLVEKD KLAKSELEEW FQSVNLNKEN
     GKVIVKPTRA GSSIGVVVAY GANEAAEKAE GIISEGIDDK VIIEVFLEGG SEFTAIVVDV
     GTANNCEPLV LLPTEIELQS SSNIDIQEDT IFNYRRKYLP TRQVAYHTPP RFPSEVIDCI
     RQGLSILFRS LGLRDFARID GWFLPTPVTS LPSAEKSGKI GSIKCGAVLF TDINVISGME
     QTSFLFQQAS AVGFSHSAFL RTMVQHACLR FPSLVPRRNA WTALSKKKQA AKQAEAIHNG
     TSKKKVFVLF GGDTSERQVS LMSGTNVWLN LQGFDDLDAI PCLLIPGNWD RSSNNQNFNE
     SSRDVWTLPY SLVLRHTTEE VHEACIEALD PERLEITSRL RDQVMDELRQ AFSKHDWFSG
     FDIADKQPIK YSLQQWIDHV KEAKAVVFIA VHGGIGEDGT IQSLLESAGI PYTGPGSIAS
     RTCIDKVATS LAVSHLASYG VHTIPKDVRA TEELLKSSLA DIWNGLKAKL QTETDLEVYA
     NALGRKLHRL PANCLSRAHG VIEMPVPPPE SLIFEPFIET DEIIISTKSV DDSTRHLVWK
     GENEWLEVTV GVVGKRGEMR SLNPSITVKE SGDILSLEEK FQGGTGINLT PPPPTIMSED
     ALQKCKRSIE VLANTLGLEG FSRIDAFVNV RSGEVLLIEA NTVPGMTPST VLIHQALAEE
     PPIYPHKFFR TLLDLAFARA N
//