PIKM1_ORYSJ
ID PIKM1_ORYSJ Reviewed; 1143 AA.
AC B5UBC1; D5L9G0; D5L9G3;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Disease resistance protein Pikm1-TS {ECO:0000305};
GN Name=PIKM1-TS {ECO:0000312|EMBL:BAG71909.1};
GN Synonyms=PI-KM1 {ECO:0000312|EMBL:ADE80944.1, ECO:0000312|EMBL:ADE80945.1,
GN ECO:0000312|EMBL:ADE80946.1, ECO:0000312|EMBL:ADE80948.1,
GN ECO:0000312|EMBL:ADE80951.1};
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] {ECO:0000312|EMBL:BAG71909.1, ECO:0000312|EMBL:BAG72135.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP INDUCTION BY PATHOGEN INFECTION.
RC STRAIN=cv. Tsuyuake;
RX PubMed=18940787; DOI=10.1534/genetics.108.095034;
RA Ashikawa I., Hayashi N., Yamane H., Kanamori H., Wu J., Matsumoto T.,
RA Ono K., Yano M.;
RT "Two adjacent nucleotide-binding site-leucine-rich repeat class genes are
RT required to confer Pikm-specific rice blast resistance.";
RL Genetics 180:2267-2276(2008).
RN [2] {ECO:0000312|EMBL:ADE80944.1, ECO:0000312|EMBL:ADE80945.1, ECO:0000312|EMBL:ADE80946.1, ECO:0000312|EMBL:ADE80948.1, ECO:0000312|EMBL:ADE80951.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Cypress, cv. Kanto 51, cv. Katy, and cv. Lemont;
RX DOI=10.1016/j.plantsci.2010.02.014;
RA Costanzo S., Jia Y.;
RT "Sequence variation at the rice blast resistance gene Pi-km locus:
RT Implications for the development of allele specific markers.";
RL Plant Sci. 178:523-530(2010).
RN [3]
RP INTERACTION WITH AVR-PIK, AND FUNCTION.
RC STRAIN=cv. Tsuyuake;
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).
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 (PubMed:18940787,
CC PubMed:22805093). Contribution of Pikm-2 is required to recognize the
CC effector avirulence protein AVR-Pik (PubMed:18940787).
CC {ECO:0000269|PubMed:18940787, ECO:0000269|PubMed:22805093}.
CC -!- SUBUNIT: Interacts with AVR-Pik through its N-terminal part containing
CC the HMA-like domain. {ECO:0000250|UniProtKB:F2VYU4,
CC ECO:0000269|PubMed:22805093}.
CC -!- TISSUE SPECIFICITY: Constitutively expressed.
CC {ECO:0000269|PubMed:18940787}.
CC -!- INDUCTION: By M.oryzae pathogen infection.
CC {ECO:0000269|PubMed:18940787}.
CC -!- DOMAIN: The HMA-like (RATX1) domain is responsible for the specific
CC recognition of AVR effectors. {ECO:0000250|UniProtKB:F2VYU4}.
CC -!- SIMILARITY: Belongs to the disease resistance NB-LRR family.
CC {ECO:0000305}.
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DR EMBL; AB462256; BAG71909.1; -; Genomic_DNA.
DR EMBL; AB462324; BAG72135.1; -; mRNA.
DR EMBL; GU811849; ADE80944.1; -; Genomic_DNA.
DR EMBL; GU811850; ADE80945.1; -; Genomic_DNA.
DR EMBL; GU811851; ADE80946.1; -; Genomic_DNA.
DR EMBL; GU811853; ADE80948.1; -; Genomic_DNA.
DR EMBL; GU811856; ADE80951.1; -; Genomic_DNA.
DR PDB; 6FU9; X-ray; 1.20 A; A/C=186-264.
DR PDB; 6FUB; X-ray; 1.30 A; A=186-264.
DR PDB; 6FUD; X-ray; 1.30 A; A=186-264.
DR PDBsum; 6FU9; -.
DR PDBsum; 6FUB; -.
DR PDBsum; 6FUD; -.
DR AlphaFoldDB; B5UBC1; -.
DR SMR; B5UBC1; -.
DR GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0051707; P:response to other organism; IEA:UniProt.
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 3D-structure; ATP-binding; Coiled coil; Leucine-rich repeat;
KW Nucleotide-binding; Plant defense; Repeat.
FT CHAIN 1..1143
FT /note="Disease resistance protein Pikm1-TS"
FT /id="PRO_0000444667"
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:0000250|UniProtKB:F2VYU4"
FT REGION 191..264
FT /note="HMA-like domain"
FT /evidence="ECO:0000250|UniProtKB:F2VYU4"
FT CONFLICT 229
FT /note="Q -> E (in Ref. 2; ADE80948/ADE80951)"
FT /evidence="ECO:0000305"
FT CONFLICT 252..257
FT /note="PAMFLE -> HAELLQ (in Ref. 2; ADE80951)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="V -> A (in Ref. 2; ADE80948)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="W -> L (in Ref. 2; ADE80951)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="S -> P (in Ref. 2; ADE80951)"
FT /evidence="ECO:0000305"
FT CONFLICT 495
FT /note="G -> R (in Ref. 2; ADE80951)"
FT /evidence="ECO:0000305"
FT CONFLICT 982
FT /note="V -> L (in Ref. 2; ADE80951)"
FT /evidence="ECO:0000305"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:6FU9"
FT HELIX 201..212
FT /evidence="ECO:0007829|PDB:6FU9"
FT STRAND 217..224
FT /evidence="ECO:0007829|PDB:6FU9"
FT STRAND 229..236
FT /evidence="ECO:0007829|PDB:6FU9"
FT HELIX 239..249
FT /evidence="ECO:0007829|PDB:6FU9"
FT STRAND 254..260
FT /evidence="ECO:0007829|PDB:6FU9"
SQ SEQUENCE 1143 AA; 126855 MW; 38B9546EE4892EE6 CRC64;
MEAAAMAVTA ATGALAPVLV KLAALLDDGE CNLLEGSRSD AEFIRSELEA VHSLLTPNIL
GRMGDDDAAC KDGLIAEVRE LSYDLDDAVD DFLELNFEQR RSASPFGELK ARVEERVSNR
FSDWKLPAAS LPPSSVHRRA GLPPPDAGLV GMHKRKEELI ELLEQGSSDA SRWRKRKPHV
PLRIMGGEMQ KIVFKIPMVD DKSRTKAMSL VASTVGVHSV AIAGDLRDQV VVVGDGIDSI
NLVSALRKKV GPAMFLEVSQ VKEDVKEITA MLAPVKSICE FHEVKTICIL GLPGGGKTTI
ARVLYHALGT QFQCRVFASI SPSSSPSPNL TETLADIFAQ AQLGVTDTLS TPYGGSGTGR
ALQQHLIDNI SAFLLNKKYL IVIDDIWHWE EWEVIRKSIP KNDLGGRIIM TTRLNSIAEK
CHTDDNDVFV YEVGDLDNND AWSLSWGIAT 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 RVPRIAFHED AMPNLKLLEF KFYAGPASND AIGITNLKSL
QKVVFRCSPW YKSDAPGISA TIDVVKKEAE EHPNRPITLL INAGYKEIST ESHGSSENIA
GSSGIDTEPA QAQHDNLPAV RDDYKGKGIL LDGRCPTCGR ATKIEEETQD RVADIEIQTE
TTS
