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RLM1B_ARATH
ID   RLM1B_ARATH             Reviewed;        1017 AA.
AC   Q9CAK1; Q7FKS0;
DT   24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Disease resistance protein RML1B {ECO:0000305};
DE            EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
DE   AltName: Full=Protein RESISTANCE TO LEPTOSPHAERIA MACULANS 1B {ECO:0000303|PubMed:16623885};
GN   Name=RLM1B {ECO:0000303|PubMed:16623885};
GN   OrderedLocusNames=At1g63880 {ECO:0000312|Araport:AT1G63880};
GN   ORFNames=T12P18.10 {ECO:0000312|EMBL:AAG52448.1};
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16623885; DOI=10.1111/j.1365-313x.2006.02688.x;
RA   Staal J., Kaliff M., Bohman S., Dixelius C.;
RT   "Transgressive segregation reveals two Arabidopsis TIR-NB-LRR resistance
RT   genes effective against Leptosphaeria maculans, causal agent of blackleg
RT   disease.";
RL   Plant J. 46:218-230(2006).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19220763; DOI=10.1111/j.1469-8137.2009.02763.x;
RA   Persson M., Staal J., Oide S., Dixelius C.;
RT   "Layers of defense responses to Leptosphaeria maculans below the RLM1- and
RT   camalexin-dependent resistances.";
RL   New Phytol. 182:470-482(2009).
CC   -!- FUNCTION: TIR-NB-LRR receptor-like protein that confers resistance to
CC       the pathogen Leptosphaeria maculans (blackleg disease).
CC       {ECO:0000269|PubMed:16623885, ECO:0000269|PubMed:19220763}.
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:0000255|PROSITE-ProRule:PRU00204};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00204};
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   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions, but mutant plants are susceptible to the pathogen
CC       Leptosphaeria maculans. {ECO:0000269|PubMed:16623885,
CC       ECO:0000269|PubMed:19220763}.
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DR   EMBL; AC010852; AAG52448.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE34163.1; -; Genomic_DNA.
DR   EMBL; AK119065; BAC43641.2; -; mRNA.
DR   PIR; H96663; H96663.
DR   RefSeq; NP_176572.1; NM_105062.3.
DR   AlphaFoldDB; Q9CAK1; -.
DR   SMR; Q9CAK1; -.
DR   STRING; 3702.AT1G63880.1; -.
DR   PaxDb; Q9CAK1; -.
DR   PRIDE; Q9CAK1; -.
DR   ProteomicsDB; 228135; -.
DR   EnsemblPlants; AT1G63880.1; AT1G63880.1; AT1G63880.
DR   GeneID; 842692; -.
DR   Gramene; AT1G63880.1; AT1G63880.1; AT1G63880.
DR   KEGG; ath:AT1G63880; -.
DR   Araport; AT1G63880; -.
DR   TAIR; locus:2195468; AT1G63880.
DR   HOGENOM; CLU_001561_0_1_1; -.
DR   InParanoid; Q9CAK1; -.
DR   OrthoDB; 258604at2759; -.
DR   PhylomeDB; Q9CAK1; -.
DR   PRO; PR:Q9CAK1; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9CAK1; baseline and differential.
DR   Genevisible; Q9CAK1; AT.
DR   GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0050832; P:defense response to fungus; IMP:TAIR.
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; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR042197; Apaf_helical.
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; PTHR11017; 1.
DR   Pfam; PF07725; LRR_3; 1.
DR   Pfam; PF00931; NB-ARC; 1.
DR   Pfam; PF01582; TIR; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00255; TIR; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF52200; SSF52200; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50104; TIR; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Hydrolase; Leucine-rich repeat; NAD; Nucleotide-binding;
KW   Plant defense; Reference proteome; Repeat.
FT   CHAIN           1..1017
FT                   /note="Disease resistance protein RML1B"
FT                   /id="PRO_0000433376"
FT   DOMAIN          12..176
FT                   /note="TIR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT   DOMAIN          191..447
FT                   /note="NB-ARC"
FT                   /evidence="ECO:0000255"
FT   REPEAT          539..562
FT                   /note="LRR 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          583..605
FT                   /note="LRR 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          606..628
FT                   /note="LRR 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          629..652
FT                   /note="LRR 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          654..675
FT                   /note="LRR 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          676..698
FT                   /note="LRR 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          699..724
FT                   /note="LRR 7"
FT                   /evidence="ECO:0000255"
FT   REPEAT          738..760
FT                   /note="LRR 8"
FT                   /evidence="ECO:0000255"
FT   REPEAT          761..782
FT                   /note="LRR 9"
FT                   /evidence="ECO:0000255"
FT   REPEAT          784..809
FT                   /note="LRR 10"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        87
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT   CONFLICT        312
FT                   /note="E -> G (in Ref. 3; BAC43641)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1017 AA;  115415 MW;  9C1AF3178F70F7D4 CRC64;
     MASPSSFSSQ NYKFNVFASF HGPDVRKTLL SHIRLQFNRN GITMFDDQKI VRSATIGPSL
     VEAIKESRIS IVILSKKYAS SSWCLDELVE ILECKKAMGQ IVMTIFYGVD PSDVRKQIGK
     FGIAFNETCA RKTEEERQKW SKALNQVSNI AGEDFLRWDN EAIMIEKIAR DVLDKLNATP
     SRDFDGMVGI EAHLREIKSL LDLDNVEVKI VAIAGPAGIG KTTIARALYG LLSKRFQLSC
     FVDNLRGSYH SGFDEYGFKL HLQEQFLSKV LNQSGMRICH LGAIKENLSD QRVLIILDDV
     NKLKQLEALA NETTWFGPGS RIVVTTENKE LLQQHGINNT YHVGFPSDED ALKILCSYAF
     KQTSPRHGFE ELSESVTKLC GKLPLGLCVV GSSLRGKKED EWEDVVTRLE TILDQDIEDV
     LRVGYESLDE NAQTLFLHIA IFFNKEDGDL VKTMFAESDL DVKYGLKILE NRSLIKMKIF
     SNGDTKIVMH RLLQQMGKRA IQKQEPWERQ ILIDAREICH VLEHAKGTGW NVHGMSFDIS
     RISEVSIRKK AFKRMPNLQF LKVYKSKDDG NNRMHVPEEM DFPCLLRLLD WKAYPSKSLP
     PTFNPEHLVE LNMHSSQLEY LWQGTQPLKN LKKMDLSQSK NLKQLPDLSN ATNLEYLYLM
     GCESLIEIPS SISHLHKLEM LATVGCINLE VIPAHMNLES LQTVYLGGCS RLRNIPVMST
     NIRYLFITNT AVEGVPLCPG LKTLDVSGSR NFKGLLTHLP TSLTTLNLCY TDIERIPDCF
     KSLHQLKGVN LRGCRRLASL PELPRSLLTL VADDCESLET VFCPLNTLKA SFSFANCFKL
     DREARRAIIQ QSFFMGKAVL PGREVPAVFD HRAKGYSLTI RPDGNPYTSF VFCVVVSRNQ
     KSDKTIPPSL LWRRIIAQDE GYPVEVWNRI GDVFKYRTEH LLIFHFDFLE FDNRDIVFEF
     SSESHDFDII ECGAKVLAEK SIKESYESGS DQAFEDDVVF EPSKAFGDEK YGDCCIL
 
 
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