ROQ1_NICBE
ID ROQ1_NICBE Reviewed; 1306 AA.
AC A0A290U7C4;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2017, sequence version 1.
DT 03-AUG-2022, entry version 11.
DE RecName: Full=Disease resistance protein Roq1 {ECO:0000305};
DE AltName: Full=NAD(+) hydrolase RPV1;
DE EC=3.2.2.6 {ECO:0000305|PubMed:31439792};
DE AltName: Full=Recognition of XopQ 1 protein {ECO:0000303|PubMed:28891100};
GN Name=ROQ1 {ECO:0000303|PubMed:28891100};
OS Nicotiana benthamiana.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4100;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=28891100; DOI=10.1111/tpj.13715;
RA Schultink A., Qi T., Lee A., Steinbrenner A.D., Staskawicz B.;
RT "Roq1 mediates recognition of the Xanthomonas and Pseudomonas effector
RT proteins XopQ and HopQ1.";
RL Plant J. 92:787-795(2017).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=31439792; DOI=10.1126/science.aax1911;
RA Horsefield S., Burdett H., Zhang X., Manik M.K., Shi Y., Chen J., Qi T.,
RA Gilley J., Lai J.S., Rank M.X., Casey L.W., Gu W., Ericsson D.J., Foley G.,
RA Hughes R.O., Bosanac T., von Itzstein M., Rathjen J.P., Nanson J.D.,
RA Boden M., Dry I.B., Williams S.J., Staskawicz B.J., Coleman M.P., Ve T.,
RA Dodds P.N., Kobe B.;
RT "NAD+ cleavage activity by animal and plant TIR domains in cell death
RT pathways.";
RL Science 365:793-799(2019).
CC -!- FUNCTION: Disease resistance (R) protein that specifically recognizes
CC the Xanthomonas and Pseudomonas effector proteins XopQ and HopQ1, and
CC triggers cell death (PubMed:28891100). Acts as a NAD(+) hydrolase
CC (NADase): in response to activation, catalyzes cleavage of NAD(+) into
CC ADP-D-ribose (ADPR) and nicotinamide; NAD(+) cleavage triggering a
CC defense system that promotes cell death (PubMed:31439792).
CC {ECO:0000269|PubMed:28891100, ECO:0000269|PubMed:31439792}.
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:0000305|PubMed:31439792};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
CC Evidence={ECO:0000305|PubMed:31439792};
CC -!- INTERACTION:
CC A0A290U7C4; Q5QA88: xopQ; Xeno; NbExp=2; IntAct=EBI-26584875, EBI-26584891;
CC -!- DOMAIN: The TIR domain mediates NAD(+) hydrolase (NADase) activity.
CC Self-association of TIR domains is required for NADase activity.
CC {ECO:0000255|PROSITE-ProRule:PRU00204}.
CC -!- SIMILARITY: Belongs to the disease resistance TIR-NB-LRR family.
CC {ECO:0000305}.
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DR EMBL; MF773579; ATD14363.1; -; mRNA.
DR PDB; 7JLU; EM; 3.80 A; A=1-1306.
DR PDB; 7JLV; EM; 3.80 A; A/B/D/G=1-1306.
DR PDB; 7JLX; EM; 4.60 A; A/B/C/D=1-1306.
DR PDBsum; 7JLU; -.
DR PDBsum; 7JLV; -.
DR PDBsum; 7JLX; -.
DR AlphaFoldDB; A0A290U7C4; -.
DR SMR; A0A290U7C4; -.
DR IntAct; A0A290U7C4; 1.
DR GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
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; -; 1.
DR Gene3D; 3.40.50.10140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR042197; Apaf_helical.
DR InterPro; IPR045344; C-JID.
DR InterPro; IPR044974; Disease_R_plants.
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; PTHR11017; 4.
DR Pfam; PF20160; C-JID; 1.
DR Pfam; PF00931; NB-ARC; 1.
DR Pfam; PF01582; TIR; 1.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Leucine-rich repeat; NAD; Plant defense; Repeat.
FT CHAIN 1..1306
FT /note="Disease resistance protein Roq1"
FT /id="PRO_0000448793"
FT DOMAIN 10..179
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT DOMAIN 198..417
FT /note="NB-ARC"
FT /evidence="ECO:0000255"
FT REPEAT 200..224
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 252..275
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 417..440
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 599..622
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 645..669
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 670..693
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 716..739
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 741..763
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 784..807
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 808..831
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 832..857
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 878..902
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 904..926
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 927..949
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 961..983
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 987..1010
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 1013..1036
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 1045..1070
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT ACT_SITE 86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT BINDING 19..24
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:V9M398"
FT BINDING 52
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:V9M398"
SQ SEQUENCE 1306 AA; 150462 MW; 44C8C3485CAD0D16 CRC64;
MLTSSSHHGR SYDVFLSFRG EDTRKTFVGH LFNALIEKGI HTFMDDKELK RGKSISSELM
KAIGESRFAV VVFSKNYASS TWCLEELVKI LEIHEKFELI VVPVFYDVDP STVRKQNGEY
AVCFTKFEAN LVDDRDKVLR WREALTKVAN ISGHDLRNTY NGDESKCIQQ ILKDIFDKFC
FSISITNRDL VGIESQIKKL SSLLRMDLKG VRLVGIWGMG GVGKTTAARA LFNRYYQNFE
SACFLEDVKE YLQHHTLLYL QKTLLSKLLK VEFVDCTDTE EMCVILKRRL CSKKVLVVLD
DVNHNDQLDK LVGAEDWFGS GSRIVITTRD MKLLKNHDVH ETYEIKVLEK DEAIELFNLH
AFKRSSPEKE FKELLNLVVD YTGGLPLALK VLGSLLYKED LDVWISTIDR LKDNPEGEIM
ATLKISFDGL RDYEKSIFLD IACFFRGYNQ RDMTALFHAS GFHPVLGVKT LVEKSLIFIL
EDKIQMHDLM QEMGRQIAVQ ESPMRRIYRP EDVKDACIGD MRKEAIEGLL LTEPEQFEEG
ELEYMYSAEA LKKTRRLRIL VKEYYNRGFD EPVAYLPNSL LWLEWRNYSS NSFPSNFEPS
KLVYLTMKGS SIIELWNGAK RLAFLTTLDL SYCHKLIQTP DFRMITNLER LILSSCDALV
EVHPSVGFLK NLILLNMDHC ISLERLPAII QSECLEVLDL NYCFNLKMFP EVERNMTHLK
KLDLTSTGIR ELPASIEHLS SLENLQMHSC NQLVSLPSSI WRFRNLKISE CEKLGSLPEI
HGNSNCTREL ILKLVSIKEL PTSIGNLTSL NFLEICNCKT ISSLSSSIWG LTSLTTLKLL
DCRKLKNLPG IPNAINHLSG HGLQLLLTLE QPTIYERLDL LRIIDMSWCS CISSLPHNIW
MLKFLRILCI SYCSRLEYLP ENLGHLEHLE ELLADGTGIL RLPSSVARLN KLEVLSFRKK
FAIGPKVQYS SSMLNLPDDV FGSLGSLGSV VKLNLSGNGF CNLPETMNQL FCLEYLDITF
CQRLEALPEL PPSIKELYVD EHLALRIMED LVIKCKELNL IAVTKIEYQN FYRWLDSIWS
DVSELLENSQ KQQLDDMLQL IPFSYLSTAK REEVLKIVIH GTRIPEWFRW QDRSATTMSV
NLPEYWYTEN FLGFAICCSC CFYHSARSYD VEFEGSMHHY NYDSSYWKEY EEPSYDFYER
DSIEITAKLT PRHKGMRTEE LKKVCSFSMN VLRRATAVPN MCFAFFPFNS LCHISNLQAN
NPNDYGIFET CLSPGDIRHR GKQWGFNLVY KDETGGSVTH EMLINR
