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
//