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PIK1_ORYSJ
ID   PIK1_ORYSJ              Reviewed;        1143 AA.
AC   F2VYU4; D5L9G3;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Disease resistance protein Pik-1 {ECO:0000305};
DE   AltName: Full=Pik-1 blast resistance protein {ECO:0000312|EMBL:ADZ48537.1};
GN   Name=PIK-1 {ECO:0000312|EMBL:ADZ48537.1};
GN   Synonyms=PIK1-KA {ECO:0000312|EMBL:BAL63004.1,
GN   ECO:0000312|EMBL:BAL63005.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=cv. Kusabue;
RX   PubMed=21118257; DOI=10.1111/j.1469-8137.2010.03462.x;
RA   Zhai C., Lin F., Dong Z., He X., Yuan B., Zeng X., Wang L., Pan Q.;
RT   "The isolation and characterization of Pik, a rice blast resistance gene
RT   which emerged after rice domestication.";
RL   New Phytol. 189:321-334(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND FUNCTION.
RC   STRAIN=cv. Kanto 51;
RX   DOI=10.1007/s11032-011-9638-y;
RA   Ashikawa I., Hayashi N., Abe F., Wu J., Matsumoto T.;
RT   "Characterization of the rice blast resistance gene Pik cloned from
RT   Kanto51.";
RL   Mol. Breed. 30:485-494(2012).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH AVR-PIK.
RC   STRAIN=cv. Kanto 51;
RX   PubMed=22805093; DOI=10.1111/j.1365-313x.2012.05110.x;
RA   Kanzaki H., Yoshida K., Saitoh H., Fujisaki K., Hirabuchi A., Alaux L.,
RA   Fournier E., Tharreau D., Terauchi R.;
RT   "Arms race co-evolution of Magnaporthe oryzae AVR-Pik and rice Pik genes
RT   driven by their physical interactions.";
RL   Plant J. 72:894-907(2012).
RN   [4]
RP   FUNCTION, INTERACTION WITH AVR-PIK, AND DOMAIN.
RX   PubMed=23548743; DOI=10.1105/tpc.112.107201;
RA   Cesari S., Thilliez G., Ribot C., Chalvon V., Michel C., Jauneau A.,
RA   Rivas S., Alaux L., Kanzaki H., Okuyama Y., Morel J.B., Fournier E.,
RA   Tharreau D., Terauchi R., Kroj T.;
RT   "The rice resistance protein pair RGA4/RGA5 recognizes the Magnaporthe
RT   oryzae effectors AVR-Pia and AVR1-CO39 by direct binding.";
RL   Plant Cell 25:1463-1481(2013).
CC   -!- FUNCTION: Disease resistance (R) protein that specifically recognizes
CC       the AVR-Pik effector avirulence protein from M.oryzae. Resistance
CC       proteins guard the plant against pathogens that contain an appropriate
CC       avirulence protein via an indirect interaction with this avirulence
CC       protein. That triggers a defense system including the hypersensitive
CC       response, which restricts the pathogen growth. Contribution of Pik-2 is
CC       required to recognize the effector avirulence protein AVR-Pik.
CC       {ECO:0000269|PubMed:21118257, ECO:0000269|PubMed:22805093,
CC       ECO:0000269|PubMed:23548743, ECO:0000269|Ref.2}.
CC   -!- SUBUNIT: Interacts with AVR-Pik through its N-terminal part containing
CC       the HMA-like domain. {ECO:0000269|PubMed:22805093,
CC       ECO:0000269|PubMed:23548743}.
CC   -!- DOMAIN: The HMA-like (RATX1) domain is responsible for the specific
CC       recognition of AVR effectors. {ECO:0000269|PubMed:23548743}.
CC   -!- SIMILARITY: Belongs to the disease resistance NB-LRR family.
CC       {ECO:0000305}.
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DR   EMBL; HM048900; ADZ48537.1; -; Genomic_DNA.
DR   EMBL; AB616658; BAL63004.1; -; mRNA.
DR   EMBL; AB616659; BAL63005.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2VYU4; -.
DR   SMR; F2VYU4; -.
DR   GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR   GO; GO:0002758; P:innate immune response-activating signal transduction; IMP:UniProtKB.
DR   GO; GO:0009626; P:plant-type hypersensitive response; IMP:UniProtKB.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR044974; Disease_R_plants.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR002182; NB-ARC.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR041118; Rx_N.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR23155; PTHR23155; 2.
DR   Pfam; PF00931; NB-ARC; 1.
DR   Pfam; PF18052; Rx_N; 1.
DR   SMART; SM00369; LRR_TYP; 3.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50846; HMA_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Coiled coil; Leucine-rich repeat; Nucleotide-binding;
KW   Plant defense; Repeat.
FT   CHAIN           1..1143
FT                   /note="Disease resistance protein Pik-1"
FT                   /id="PRO_0000444663"
FT   DOMAIN          189..258
FT                   /note="HMA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   DOMAIN          282..570
FT                   /note="NB-ARC"
FT                   /evidence="ECO:0000255"
FT   REPEAT          681..706
FT                   /note="LRR 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          708..731
FT                   /note="LRR 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          732..754
FT                   /note="LRR 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          756..777
FT                   /note="LRR 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          778..800
FT                   /note="LRR 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          802..823
FT                   /note="LRR 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          824..848
FT                   /note="LRR 7"
FT                   /evidence="ECO:0000255"
FT   REPEAT          945..968
FT                   /note="LRR 8"
FT                   /evidence="ECO:0000255"
FT   REPEAT          979..1002
FT                   /note="LRR 9"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1004..1027
FT                   /note="LRR 10"
FT                   /evidence="ECO:0000255"
FT   REGION          1..190
FT                   /note="Structured coiled coil (CC) domain"
FT                   /evidence="ECO:0000303|PubMed:21118257"
FT   REGION          191..264
FT                   /note="HMA-like domain"
FT                   /evidence="ECO:0000269|PubMed:23548743"
FT   CONFLICT        465
FT                   /note="S -> P (in Ref. 2; BAL63004/BAL63005)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        495
FT                   /note="G -> R (in Ref. 2; BAL63004/BAL63005)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1143 AA;  126799 MW;  3CD263EFA3BF5966 CRC64;
     MEAAAMAVTA ATGALAPVLV KLAALLDDGE CNLLEGSRSD AEFIRSELEA VHSLLTPNIL
     GRMGDDDAAC KDGLIAEVRE LSYDLDDAVD DFLELNFEQR RSASPFGELK ARVEERVSNR
     FSDWKLPAAS LPPSSVHRRA GLPPPDAGLV GMHKRKEELI ELLEQGSSDA SRWRKRKPHV
     PLRIMGGEMQ KIVFKIPMVD DKSRTKAMSL VASTVGVHSV AIAGDLRDEV VVVGDGIDSI
     NLVSALRKKV GHAELLQVSQ VKEDVKEITA MLAPVKSICE FHEVKTICIL GLPGGGKTTI
     ARVLYHALGT QFQCRVFASI SPSSSPSPNL TETLADIFAQ AQLGVTDTLS TPYGGSGTGR
     ALQQHLIDNI SAFLLNKKYL IVIDDIWHWE EWEVIRKSIP KNDLGGRIIM TTRLNSIAEK
     CHTDDNDVFV YEVGDLDNND ALSLSWGIAT KSGAGNRIGT GEDNSCYDIV NMCYGMPLAL
     IWLSSALVGE IEELGGAEVK KCRDLRHIED GILDIPSLQP LAESLCLGYN HLPLYLRTLL
     LYCSAYHWSN RIERGRLVRR WIAEGFVSEE KEAEGYFGEL INRGWITQHG DNNSYNYYEI
     HPVMLAFLRC KSKEYNFLTC LGLGSDTSTS ASSPRLIRRL SLQGGYPVDC LSSMSMDVSH
     TCSLVVLGDV ARPKGIPFYM FKRLRVLDLE DNKDIQDSHL QGICEQLSLR VRYLGLKGTR
     IRKLPQEMRK LKHLEILYVG STRISELPQE IGELKHLRIL DVRNTDITEL PLQIRELQHL
     HTLDVRNTPI SELPPQVGKL QNLKIMCVRS TGVRELPKEI GELNHLQTLD VRNTRVRELP
     WQAGQISQSL RVLAGDSGDG VRLPEGVCEA LINGIPGATR AKCREVLSIA IIDRFGPPLV
     GIFKVPGSHM RIPKMIKDHF RVLSCLDIRL CHKLEDDDQK FLAEMPNLQT LVLRFEALPR
     QPITINGTGF QMLESFRVDS RLPRIAFHED AMPNLKLLEF KFYAGPASND AIGITNLKSL
     QKVVFRCSPW YKSDAPGISA TIDVVKKEAE EHPNRPITLL INAGYKEIST ESHGSSENIA
     GSSGIDTEPA QAQHDNLPAV RDDYKGKGIL LDGRCPTCGR ATKIEEETQD RVADIEIQTE
     TTS
 
 
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