GenomeNet

Database: UniProt
Entry: Q9M0Q5_ARATH
LinkDB: Q9M0Q5_ARATH
Original site: Q9M0Q5_ARATH 
ID   Q9M0Q5_ARATH            Unreviewed;       853 AA.
AC   Q9M0Q5;
DT   01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 160.
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=At4g09360 {ECO:0000313|Araport:AT4G09360,
GN   ECO:0000313|EMBL:CAB78059.1};
GN   ORFNames=T15G18.1 {ECO:0000313|EMBL:AEE82745.1}, T15G18_1
GN   {ECO:0000313|EMBL:AEE82745.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702 {ECO:0000313|EMBL:CAB78059.1};
RN   [1] {ECO:0000313|EMBL:AEE82745.1, ECO:0000313|Proteomes:UP000006548}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX   PubMed=10617198; DOI=10.1038/47134;
RG   EU;
RG   CSHL and WU Arabidopsis Sequencing Project;
RA   Mayer K., Schuller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Dusterhoft A., Stiekema W., Entian K.D., Terryn N., Harris B., Ansorge W.,
RA   Brandt P., Grivell L., Rieger M., Weichselgartner M., de Simone V.,
RA   Obermaier B., Mache R., Muller M., Kreis M., Delseny M., Puigdomenech P.,
RA   Watson M., Schmidtheini T., Reichert B., Portatelle D., Perez-Alonso M.,
RA   Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H.,
RA   Ridley P., Langham S.A., McCullagh B., Bilham L., Robben J.,
RA   Van der Schueren J., Grymonprez B., Chuang Y.J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E.,
RA   Brandt A., Peters S., van Staveren M., Dirske W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Kotter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., Van Montagu M., Rogers J.,
RA   Cronin A., Quail M., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M.,
RA   Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M.,
RA   Benes V., Rechmann S., Borkova D., Blocker H., Scharfe M., Grimm M.,
RA   Lohnert T.H., Dose S., de Haan M., Maarse A., Schafer M., Muller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O.,
RA   Quigley F., Clabauld G., Mundlein A., Felber R., Schnabl S., Hiller R.,
RA   Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C.,
RA   Montfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sehkon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L., Nelson J.,
RA   Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J.,
RA   Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffmann J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [2] {ECO:0000313|EMBL:CAB78059.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Spiegel L.A., Huang E.N., Nascimento L.U., de la Bastide M., Vil D.M.,
RA   Preston R.R., Matero A., Shah R., O'Shaughnessy A., Rodriguez M.,
RA   Shekher M., Schutz K., See L.H., Swaby I., Habermann K., Dedhia N.N.,
RA   Mewes H.W., Lemcke K., Mayer K.F.X.;
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:CAB78059.1}
RP   NUCLEOTIDE SEQUENCE.
RA   EU Arabidopsis sequencing project;
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0007829|PubMed:17272265}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17272265; DOI=10.1074/mcp.M600408-MCP200;
RA   Maor R., Jones A., Nuhse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT   "Multidimensional protein identification technology (MudPIT) analysis of
RT   ubiquitinated proteins in plants.";
RL   Mol. Cell. Proteomics 6:601-610(2007).
RN   [5] {ECO:0000313|EMBL:AEE82745.1}
RP   NUCLEOTIDE SEQUENCE.
RG   TAIR;
RA   Swarbreck D., Lamesch P., Wilks C., Huala E.;
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:AEE82745.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Krishnakumar V., Cheng C.-Y., Chan A.P., Schobel S., Kim M., Ferlanti E.S.,
RA   Belyaeva I., Rosen B.D., Micklem G., Miller J.R., Vaughn M., Town C.D.;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|Proteomes:UP000006548}
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002687; AEE82745.1; -; Genomic_DNA.
DR   EMBL; AL161514; CAB78059.1; -; Genomic_DNA.
DR   PIR; B85095; B85095.
DR   RefSeq; NP_192674.1; NM_117004.1.
DR   AlphaFoldDB; Q9M0Q5; -.
DR   SMR; Q9M0Q5; -.
DR   STRING; 3702.Q9M0Q5; -.
DR   PaxDb; 3702-AT4G09360-1; -.
DR   EnsemblPlants; AT4G09360.1; AT4G09360.1; AT4G09360.
DR   GeneID; 826518; -.
DR   Gramene; AT4G09360.1; AT4G09360.1; AT4G09360.
DR   KEGG; ath:AT4G09360; -.
DR   Araport; AT4G09360; -.
DR   TAIR; AT4G09360; -.
DR   HOGENOM; CLU_001561_0_2_1; -.
DR   OMA; CILISCE; -.
DR   OrthoDB; 687499at2759; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9M0Q5; baseline and differential.
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:InterPro.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
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; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR11017:SF511; ADP-RIBOSYL CYCLASE_CYCLIC ADP-RIBOSE HYDROLASE; 1.
DR   PANTHER; PTHR11017; LEUCINE-RICH REPEAT-CONTAINING PROTEIN; 1.
DR   Pfam; PF20160; C-JID; 1.
DR   Pfam; PF00931; NB-ARC; 1.
DR   PRINTS; PR00364; DISEASERSIST.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF52047; RNI-like; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE   1: Evidence at protein level;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006548}.
FT   DOMAIN          19..154
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   853 AA;  96663 MW;  4D976466C99B5D03 CRC64;
     MDVDMERLNP LLSIESENEV RMIGIWGMGG IGKTTIAKCL YEEYSRRFVH YCFIENVRIF
     AKNGLPYLQE KLLSEIRGKK QETLWSVEKG CRLIKSKLKE KNFLVLDDVD NVDQLHALAK
     ETSWFGPGSR IIITTRDFGL LYSFGVRLLY RVSFLDDNDA IKVFKHVAFD GGQPPFDVYH
     QFSVRASRLA QGLPSALEAF GALGILETVP QKRIKDILKT SYDGLDEEEQ AAFLHVACLF
     NGDSVHRVNA LIDDGDMRIK ALEVKSLIDI SLDGCITLHV LIEQAAREID TAMVEGVALH
     MCEMIHVLPI DGNILNTINN LKFFKAFTHI EVMNSKLQFL PGTANNSGGL GQLRRLDVTG
     SKNLREIPDL SRTMLLEELI MKGCTRLEKT LDIRKGCPSR TWTKATPTNN IEASQRSKEA
     EFSCKPIYRR EDTHRLVASH GNRRAPLLYS EQKIPDELVM VPKKRFPIIS SFYDLKSLSI
     MRFSHIADGT PFRCISFSGF QCLVELNLIN LNIQKIPDNI GLMQSLEKVD LSGNDFRNLP
     ASTKNLSKLK YARLSNCIKL EAFVELTELQ TLKLSGCTNL ESLLELPYAV QDVGRFCLLA
     LELDNCKNLQ ALSEQLSHFS NLIHLDLSSH DFEKLKSVEE LPLNLKHLYA HGCDSLESVD
     LSPKHSIKHL DLSHCFGLQQ DEQQITQFLN DKCSQEVSQR FLCLPGTEVP RNFDNQSHGT
     STKISLFTPT LLSFAACILI SCERSFYLQF PAFSYDWNRK DDEVISINLT PNLNLSSEIE
     EEETVTSHHL VIIHVPSSIN TDKIEDLRLE SSLQFPEEFQ FSPCEIRACG IRMVDEETKC
     LESSPLMPLL EKK
//
DBGET integrated database retrieval system