ID A0A453AKZ3_AEGTS Unreviewed; 943 AA.
AC A0A453AKZ3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
OS Aegilops tauschii subsp. strangulata (Goatgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET2Gv20178300.16, ECO:0000313|Proteomes:UP000015105};
RN [1] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=25035499; DOI=10.1126/science.1250092;
RG International Wheat Genome Sequencing Consortium,;
RA Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL Science 345:1250092-1250092(2014).
RN [2] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL Nat. Plants 3:946-955(2017).
RN [3] {ECO:0000313|EnsemblPlants:AET2Gv20178300.16}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2019) to UniProtKB.
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
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DR AlphaFoldDB; A0A453AKZ3; -.
DR STRING; 200361.A0A453AKZ3; -.
DR EnsemblPlants; AET2Gv20178300.16; AET2Gv20178300.16; AET2Gv20178300.
DR Gramene; AET2Gv20178300.16; AET2Gv20178300.16; AET2Gv20178300.
DR Proteomes; UP000015105; Chromosome 2D.
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:UP000015105}.
FT DOMAIN 209..447
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 674..939
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 15..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 943 AA; 103127 MW; D6D68988A7ECA184 CRC64;
RMLLSFAQPR LLPRLPSPAT ATATTARPRA PRRALSSAAK TAAAGRLRAV VSERAVEGMA
PAAAGQEGRP LRVGLVCGGP SAERGISLNS ARSVLDHIQG EDLLVSCYYI DCGMNAFAIS
PAQLYSNTPS DFDFKLESLA QEFSTLSEFA EHLAANVDIV FPVIHGKFGE DGGIQELLEK
ANVPFVGTPS NECLRAFDKH NASLELDAQG FLTVPNFLVE KDKLATSELE EWFRSINLNK
ENGKVIVKPT RAGSSIGVVV AYGANEAAEK AEGIFSEGID NKVIIEVFLE GGCEFTAIVL
DVGTANNSEP IVLLPTEVEL QSSISSDIQE DTIFNYRRKY LPTQQVAYHT PPRFPAEVID
CIRKGVSLLF RHFGLRDFAR IDGWFLPSPA TSLPSSENGV KFGNTEYGAV LFTDINLISG
MEQTSFLFQQ ASKVGFSHSR ILRTIVQHAC SRFPSLVTSN NAWTALSRKM QSAKQALIIP
NGTCKQKAFV IFGGDTSERQ VSLMSGTNVW LNLQGFDDLD VTPCLLAPSN GYSSHNEDFS
ESSRDVWTLP YSLVLRHTTE EVHAACFEAI EPERVEITSR LRNQVMKELE RALSKQDWFA
GFDITDEQPI KYSLQQWIDY VKEAKAVVFI AVHGGIGEDG TIQSLLESAG VPYTGPGPIA
SRTCMDKVAT SLAVDHLASY GIHTIPKDVR AREELLKSSL VDIWNDLKAK LQTETVCVKP
ARDGCSTGVA RLRCPEDLEV YANALRGTLP RLPANCLSKA HGVIEMPVPP PESLIFEPFI
ETDEIIISNK SWNDSTRHLV WKGENEWLEV TVGVVGKRGE MHSLNPSITV KESGDILSLE
EKFQGGTGIN LTPPPATIMS EDALQKCKSC IEMTANTLGL EGFSRIDAFV NVHSGEVLLI
EVNTVPGMTP STVLIHQALT EEPPIYPHKF FRTLLDLAFA RAG
//