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Database: UniProt
Entry: D7MRE0_ARALL
LinkDB: D7MRE0_ARALL
Original site: D7MRE0_ARALL 
ID   D7MRE0_ARALL            Unreviewed;      1185 AA.
AC   D7MRE0;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase {ECO:0000256|ARBA:ARBA00011982};
DE            EC=3.2.2.6 {ECO:0000256|ARBA:ARBA00011982};
GN   ORFNames=ARALYDRAFT_683354 {ECO:0000313|EMBL:EFH41444.1};
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN   [1] {ECO:0000313|Proteomes:UP000008694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA   Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA   Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA   Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT   change.";
RL   Nat. Genet. 43:476-481(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide;
CC         Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00000404};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
CC         Evidence={ECO:0000256|ARBA:ARBA00000404};
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DR   EMBL; GL348720; EFH41444.1; -; Genomic_DNA.
DR   RefSeq; XP_002865185.1; XM_002865139.1.
DR   AlphaFoldDB; D7MRE0; -.
DR   STRING; 81972.D7MRE0; -.
DR   EnsemblPlants; Al_scaffold_0008_174; Al_scaffold_0008_174; Al_scaffold_0008_174.
DR   GeneID; 9301259; -.
DR   Gramene; Al_scaffold_0008_174; Al_scaffold_0008_174; Al_scaffold_0008_174.
DR   KEGG; aly:9301259; -.
DR   eggNOG; ENOG502SUNR; Eukaryota.
DR   HOGENOM; CLU_001561_0_1_1; -.
DR   OrthoDB; 684198at2759; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
DR   GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 1.10.8.430; Helical domain of apoptotic protease-activating factors; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR   Gene3D; 3.40.50.10140; Toll/interleukin-1 receptor homology (TIR) domain; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR042197; Apaf_helical.
DR   InterPro; IPR045344; C-JID.
DR   InterPro; IPR044974; Disease_R_plants.
DR   InterPro; IPR011713; Leu-rich_rpt_3.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR002182; NB-ARC.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000157; TIR_dom.
DR   InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR11017:SF227; ADP-RIBOSYL CYCLASE_CYCLIC ADP-RIBOSE HYDROLASE-RELATED; 1.
DR   PANTHER; PTHR11017; LEUCINE-RICH REPEAT-CONTAINING PROTEIN; 1.
DR   Pfam; PF20160; C-JID; 1.
DR   Pfam; PF07725; LRR_3; 1.
DR   Pfam; PF00931; NB-ARC; 1.
DR   Pfam; PF01582; TIR; 1.
DR   PRINTS; PR00364; DISEASERSIST.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00255; TIR; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF52200; Toll/Interleukin receptor TIR domain; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50104; TIR; 1.
PE   4: Predicted;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Plant defense {ECO:0000256|ARBA:ARBA00022821};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008694}.
FT   DOMAIN          11..175
FT                   /note="TIR"
FT                   /evidence="ECO:0000259|PROSITE:PS50104"
SQ   SEQUENCE   1185 AA;  135486 MW;  05D8EEB63359F0B0 CRC64;
     MASSSSSSRN WVYDVFPSFS GEDVRITFLS HFLKELDRKL IIAFKDNEIE RSQSLDPELK
     QAIRSSRIAV VVFSEKYPSS SWCLDELLEI VRCKEELGQL VIPVFYGLDP SHVRKQTGQF
     GEAFAKTCQR KTEDETKLWR QSLTDVANVL GYHSQNWPSE AKMIEAIANN VLGKLNFTPS
     KDFEDFVGME DHIAKMSVLL NLESEEVRMV GIWGSSGIGK TSIARALYNQ LSRRFQGSVF
     IDRAFVTKSK SNYESANPDD YNMKLYLLRS FLSEILDKKN VRINHLGAAE ETLNRRKVLI
     FIDDMDDQVV LDTLAGQAQW FGCGSRIIVI TKDKHFLRAH RIDHIYEVCL PSKDLALKIF
     CRSAFKKNSP PEGLMDLASE VALCAGNLPL GLKVLGSYLR GRDKEDLMDM LPRLRNSLDG
     KIEKTLRVSY DGLNDKKDKA IFRHIACLFN GEKANDIKLL LADSGLDVNI GLKNLVDKSL
     IHVRKEIVEM HSLLQEMGKE IVRAQSNEPG EREFLVDAKE ICDLLEDNTG TKKVLGISLD
     MDEIDELHIH ENAFKGMRNL IFLKFYTKKW DQKNEVRWHL PEGFNYLPHK LRLLRLDGYP
     MRHMPSNFRT ENLVELHMPG SKLERLWEGV QELKGLKTIN LHRSKNLKEI PNLSMATNLE
     ELHLGDCSSL VELSSSVQYL NKLKSLVMSG CINLEILPTG INLQSLFSLN LKGCSGLKIF
     PNISTNISWL ILDETSIEEF PSNLRLDNLL LLSMCRMKSQ KLWDRKQPLT PLMAMLPHSL
     EELFLSDIPS LVDIPSSIQN FTHLDCLGIE DCINLETLPT GINFHHLESL NLSGCSRLKT
     FPNISTNIEQ LYLQRTGIEE VPWWIEKFTK LDYITMEKCN NLIRVSLNIY KLKRLMVDFS
     DCGSLTEASW NGSPSEVAMV TDNIHSKFPV LEEAFYSDPD STPPEFWFNF HFLNLDPEAL
     LRQRFIFNSI TLSGEEVPSY FTHQTTEISL TSIPLLQPSL SQQFFKFKAC AVVSFDSLFL
     TWGFGVYIRV NCRFKDRHGN SFDTFGQPHG FSGSKKDNNL FILDCRVPLN KDNAALAQLN
     YDHVDMEIQI RKLDQSYKYG YTFKLKGWGI RVLEECSLLE NRLPHVYEAD EDNLVNMTEH
     SEEYVETVVK RQRETGSDCI LPKGPLKKPL LCPASDTQEE NKTSL
//
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