ID I1N349_SOYBN Unreviewed; 955 AA.
AC I1N349;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 2.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN Name=100775955 {ECO:0000313|EnsemblPlants:KRH00379};
GN ORFNames=GLYMA_18G209600 {ECO:0000313|EMBL:KRH00379.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH00379.1};
RN [1] {ECO:0000313|EMBL:KRH00379.1, ECO:0000313|EnsemblPlants:KRH00379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH00379};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH00379.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH00379}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH00379};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH00379.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH00379.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
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DR EMBL; CM000851; KRH00379.1; -; Genomic_DNA.
DR RefSeq; XP_003551592.1; XM_003551544.3.
DR AlphaFoldDB; I1N349; -.
DR SMR; I1N349; -.
DR STRING; 3847.I1N349; -.
DR PaxDb; 3847-GLYMA18G44100-1; -.
DR EnsemblPlants; KRH00379; KRH00379; GLYMA_18G209600.
DR GeneID; 100775955; -.
DR Gramene; KRH00379; KRH00379; GLYMA_18G209600.
DR KEGG; gmx:100775955; -.
DR eggNOG; ENOG502QS9K; Eukaryota.
DR HOGENOM; CLU_010120_0_0_1; -.
DR InParanoid; I1N349; -.
DR OMA; RQVAYHT; -.
DR OrthoDB; 659795at2759; -.
DR Proteomes; UP000008827; Chromosome 18.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IBA:GO_Central.
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; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR InterPro; IPR011761; ATP-grasp.
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:UP000008827}.
FT DOMAIN 211..455
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 886..951
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 955 AA; 104450 MW; 998CDF80882ADD9A CRC64;
MATSSLAGNC TLLRHSETQS CSLLSSPGGS SVKLFWSKKH EASTCHAARV AAVPRASARE
VAVVGGGVVE KGREKGRVLK VGLICGGPSA ERGISLNSAR SVLDHLQGDD LHVSCYYIDC
NLNAFAISSA QVYSNTPADF DFKLESLAQS FQTLSDLAKH LATAVDIVFP VIHGQFGEDG
GIQELLEKYN VPFVGTGSKE CCQAFDKHKA SLELRKHGFI TVPSFLVQGY ETKKSELSEW
FEKHQLDPDL GKVVVKPTRG GSSIGVRVAY GVNDSLVKAN EIMSEGIDNK VLIEIYLEGG
SEFTAIVLDV GSASDSFPVV LLPTEVELQF RGANDVKEND AIFNYRRKYL PTQQVAYHTP
PRFPLDVIEN IRKGASLIFQ QLCLQDFARI DGWFLPNSSS KLSPSPESEF GRTESGTIIF
TDINLISGME QTSFLFQQAS KVGFSHTNIL RSIIHHACLR FPNLASVSGI SGQLPSRSKS
LQQSKSFSRH EGTRKVFVIF GGNTSERQVS LMSGTNVWLN LLAFHDLEVT PCLLSPTSEC
ASSVDIGKKA DDVMNRTVLS LPYSLVLRHT TEEVLDACME AIEPERAAIT SDLRKKVMND
LMEGLKDHNW FTGFDIADDL PAKFSLRQWI KLAKEVQATI FIAVHGGIGE DGTLQSLLDA
EGVPYTGPGA MASKICMDKV ATSVAIKHLA NSGVLTINKN VRQKDDLSNK PISDTWHDLT
RKLQCQTLCV KPAKDGCSTG VARLCCSEDL AIYVRALEDC LLRIPPNSLS KAHGMIEMPN
PPPEYLIFEP FIETDEIIVT SKFEDATGHG LTWKGHSRWV EITVGVIGKR GSMHSLSPSV
TVKESGDILS LEEKFQGGTG INLTPPPLSI MSENALKRCK QHIELIANTL QLEGFSRIDA
FVNVDSGEVL IIEVNTVPGM TPSTVLIHQA LVEQPPLYPH QFFRKLLDLA SERSM
//
