ID   A0A2P5F9B0_TREOI        Unreviewed;       960 AA.
AC   A0A2P5F9B0;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=D-alanine--D-alanine ligase {ECO:0000313|EMBL:PON94377.1};
GN   ORFNames=TorRG33x02_098510 {ECO:0000313|EMBL:PON94377.1};
OS   Trema orientale (Charcoal tree) (Celtis orientalis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Cannabaceae; Trema.
OX   NCBI_TaxID=63057 {ECO:0000313|EMBL:PON94377.1, ECO:0000313|Proteomes:UP000237000};
RN   [1] {ECO:0000313|Proteomes:UP000237000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. RG33-2 {ECO:0000313|Proteomes:UP000237000};
RA   Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA   Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA   Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA   Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA   Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA   Smit S., Geurts R.;
RT   "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT   legume Parasponia.";
RL   Submitted (JUN-2016) 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:PON94377.1}.
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DR   EMBL; JXTC01000052; PON94377.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P5F9B0; -.
DR   STRING; 63057.A0A2P5F9B0; -.
DR   InParanoid; A0A2P5F9B0; -.
DR   OrthoDB; 659795at2759; -.
DR   Proteomes; UP000237000; 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   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, ECO:0000313|EMBL:PON94377.1};
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:UP000237000}.
FT   DOMAIN          217..460
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          891..949
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   960 AA;  105433 MW;  3F43E50F149E4D1A CRC64;
     MASIAFGSGL ALLRGAQNDV AGELLLRFPN LLRSNFVLRS DCFSTARTRR RGGVGVPRAA
     AAAAEAEEVV VVDRVVEGKE KGGVLRVGVV CGGPSAERGI SLNSARSVID HIQGDGLHVS
     CFYIDTDYNA YAISSAQVYS NTPADFDFKL ESLAQGFQSL SDFAEHLSAS VDIVFPVIHG
     QFGEDGGIQE LLERYNIPFV GTGSSECRQA FDKYNASLEL SRRGFVTVPS YLVQSSEANE
     SELSEWFVRN QLDSNSGRVV VKPARAGSSI GVKVAYGVAD SLKKANAIIS EGIDDKVLIE
     VFLEGGSEFT AIVLDVGSGL DCHPVVLLPT EVELQFHGKV DMREKDAIFN YRRKYLPTQQ
     VAYHTPPRFP IDVIESIREG ASLLFKELGL RDFARIDGWF LPNSVHVSSF SERNFGKTKF
     GTIVFTDINL ISGMEQTSFL FQQASKVGFS HSNVLRSIIY HACSRFPKLT SFRSASHILP
     KRSTSSPLSE ALPKHERTRK VFVIFGGDTS ERQVSLMSGT NVWLNLQAFE DLEVVPCLLA
     PTSEYSASIN SNQKEIDVST RTVWSLPYSL VLRHTTEEVL AACIEAIEPA RAELTSHLRN
     KVMKDLMEGL KAHSWFKGFD ISDEPPVRYS LKQWIKQAKE LQATVFIAVH GGIGEDGTLQ
     SLLEDEGVPY TGPGVIASKT CMDKVATSLA LSHLANSGVL TINKDVRKKE DLLRMPTLEI
     WHDLTLKLQC KTLCVKPARD GCSTGVARLC CAEDLSVYVE ALRGGLLRIP PNSLSKAHGM
     IEMPNPPPEL LIFEPFIETD EIIVSSKSTD EYGHQLKWKG QSRWVEVTVG VIGKRGSMHS
     LSPSITVKES GDILSLEEKF QGGTGINLTP PPLSIISNEA LERCKQHIEL IANNLQLEGF
     SRIDAFVNVD SGEVLIIEVN TVPGMTPSTV LIHQALSEQP PMYPHRFFRT LLDLGTERPL
//