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Database: UniProt
Entry: F6I3U8_VITVI
LinkDB: F6I3U8_VITVI
Original site: F6I3U8_VITVI 
ID   F6I3U8_VITVI            Unreviewed;      1019 AA.
AC   F6I3U8;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
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   OrderedLocusNames=VIT_18s0041g01340 {ECO:0000313|EMBL:CCB61671.1};
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760 {ECO:0000313|EMBL:CCB61671.1, ECO:0000313|Proteomes:UP000009183};
RN   [1] {ECO:0000313|Proteomes:UP000009183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX   PubMed=17721507; DOI=10.1038/nature06148;
RG   The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA   Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA   Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA   Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA   Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA   Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA   Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA   Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA   Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA   Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in major
RT   angiosperm phyla.";
RL   Nature 449:463-467(2007).
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; FN596744; CCB61671.1; -; Genomic_DNA.
DR   AlphaFoldDB; F6I3U8; -.
DR   PaxDb; 29760-VIT_18s0041g01340-t01; -.
DR   eggNOG; ENOG502R41B; Eukaryota.
DR   HOGENOM; CLU_001561_0_0_1; -.
DR   InParanoid; F6I3U8; -.
DR   Proteomes; UP000009183; Chromosome 18.
DR   ExpressionAtlas; F6I3U8; baseline and differential.
DR   GO; GO:0043531; F:ADP binding; 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; IPR042197; Apaf_helical.
DR   InterPro; IPR045344; C-JID.
DR   InterPro; IPR044974; Disease_R_plants.
DR   InterPro; IPR001611; Leu-rich_rpt.
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   PANTHER; PTHR11017:SF585; AAA+ ATPASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR11017; LEUCINE-RICH REPEAT-CONTAINING PROTEIN; 1.
DR   Pfam; PF20160; C-JID; 1.
DR   Pfam; PF00931; NB-ARC; 1.
DR   Pfam; PF01582; TIR; 1.
DR   PRINTS; PR00364; DISEASERSIST.
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   PROSITE; PS51450; LRR; 2.
DR   PROSITE; PS50104; TIR; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Plant defense {ECO:0000256|ARBA:ARBA00022821};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009183}.
FT   DOMAIN          13..179
FT                   /note="TIR"
FT                   /evidence="ECO:0000259|PROSITE:PS50104"
FT   REGION          966..1019
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        991..1010
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1019 AA;  115826 MW;  69553CB12B42EFEC CRC64;
     MAFPSSSSSS SQGSYDVFLS FRGEDTRNNF TAHLYQELRT KGINTFIDDD KLERGRLISP
     ALVTAIENSM FSIIVLSENY ASSKWCLEEL AKILECMKTR GQRVLPIFYN VDPSDVKKQR
     GKFGAALAEH EKNLTENMER VQIWKDALTQ VANLSGWESR NKNELLLIKE IVKHVFNKLI
     NICSGDTEKL VGIDARIQEI KMRLRLESDD VGMIGIWGMG GIGKTTLARA LYNEISRQFE
     AHSFLEDVGK VLVNKGLIKL QQIFLYDLLE EKDLNTKGFT FIKARLHSKK ALVVLDNVND
     PKILECLVGN WDWFGRGSRI IITARDKHLL IAHGVLCYQV PTFNYDEAYG FIKRHSLKHE
     LLIGDFLELS KEMIDYAKGL PLALKVLCSS LFGMSKKERR NQLDKLKSTL HKKIEEVLRI
     SYDGLDDKEK NIFLDIACFF KGEDKDYVIE ILDGCGFFSS CGIRTLVNKS LISIYGNKLE
     MHDLIQEMGI EIVRQQFVQE LGKRSRLWFH EDIIDVLEKL KCMDLSHSKY LIETPNLSRV
     TNLERLVLED CVSLCKVHPS LRDLKNLNFL SFKNCKMLKS LPSGPYDLKS LATLILSGCS
     KFEQFPENFG YLEMLKKLYA DGTALRELPS SLSSLRNLEI LSFVGCKGPP SASWLFPRRS
     SNSTGFILHN LSGLCSLRKL DLSDCNLSDE TNLSCLVYLS SLKDLYLCEN NFVTLPNLSR
     LSRLERFRLA NCTRLQELPD LPSSIVQVDA RNCTSLKNVS LRNVQSFLLK NRVIWDLNFV
     LALEILTPGS RLPDWIRYQS SGKEVIAELS PNWFNSNFLG FGFANVVPKF SNLGLSRFVY
     CYLSLSRSSD FTHGFRVVPY PHFLCLNRQM LTLDHVYLLY VPLSSFSDWC PWGHIINWHQ
     VTHIKASFQP RSDQFGEVKR YGIGLAYSNE DVNHNNPPMI QFGSISSASS PPPNKSTVVL
     TEIHDEEPSG SVDGSELDNS GYYTADEGEP AETACSKDPS ESEMQPQKRL KCSHFQDIP
//
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