ID   A0A061EXN2_THECC        Unreviewed;       804 AA.
AC   A0A061EXN2;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=D-alanine--D-alanine ligase family protein isoform 2 {ECO:0000313|EMBL:EOY07029.1};
GN   ORFNames=TCM_021565 {ECO:0000313|EMBL:EOY07029.1};
OS   Theobroma cacao (Cacao) (Cocoa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX   NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY07029.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOY07029.1, ECO:0000313|Proteomes:UP000026915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX   PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA   Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA   Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA   Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA   Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA   Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA   Kuhn D.N.;
RT   "The genome sequence of the most widely cultivated cacao type and its use
RT   to identify candidate genes regulating pod color.";
RL   Genome Biol. 14:R53.1-R53.24(2013).
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|ARBA:ARBA00010871}.
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DR   EMBL; CM001883; EOY07029.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061EXN2; -.
DR   EnsemblPlants; EOY07029; EOY07029; TCM_021565.
DR   Gramene; EOY07029; EOY07029; TCM_021565.
DR   Proteomes; UP000026915; Chromosome 5.
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; -; 1.
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; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
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:EOY07029.1};
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:UP000026915}.
FT   DOMAIN          57..300
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          731..789
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   804 AA;  88942 MW;  AA8D8CCEE5422AA4 CRC64;
     MVGLVKMVAF RSYWKNIMFH LLAQDPRSVV KHLTRFRNFI SHIIMTSLFI LINYDASLSL
     SKHGFVTIPS FLVQGSEVNE SELSKWFASN QLDFNSGKVV VKPTRAGSSI GVTVAYGVTD
     SLKKAKEIIS QGIDDRVLVE LFLEGGSEFT AIVLDVGHGF DCQPVVLLPT EVELQFHGSG
     DVRERDAIFN YRRKYLPTQQ VAYHTPPRFP IDIIKSIREG ASLLFRRLGL RDFARIDGWF
     LPSTTKALSS SEDKYGMTEL GTILFTDINL ISGMEQTSFL FQQASKVGFS HSNILRSIIH
     RACLRFPELA TYSSESGQLR RTSKCLKPTE TSKGLEGIHK VFVIFGGDTS ERQVSLMSGT
     NVWLNLQAFD DLDVTPCLLA SSIDHSSTTD SDKKESDVSS REVWLLPYSL VLRHTTEEVL
     DACMEAIEPA RAALTSHLRN QVMNELMEGL KKHGWFMGFD ITDQQPVRYS LKEWIKFAKE
     VEATVFISVH GGIGEDGTLQ SLLEAEEIPY SGPGVKASKI CMDKVATSLA LNHLGDMGVL
     TINKDVKRKK ELLKMPILQT WHDLTSKLQC ETLCIKPARD GCSTGVARLC CAEDLAVYAK
     AVDDCLLRIP PNSFSKAHGM IEMPNPPPEL LIFEPFVETD EIVVSSKTAT ANSQHLLWKG
     HSRWVEVTVG VIGKRGSMHS LSPSITVKET GDILSLEEKF QGGTGINLTP PPVSIMSNEV
     LGRCKQRIEL IANTLQLEGF SRMDAFVNVD SGEVLVIEVN TVPGMTPSTV LIHQGTGRAA
     SHVSSPVLPF TSRFGVRESA VKVV
//