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Conserved domains on  [gi|1002279662|ref|XP_015644152|]
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putative disease resistance protein RGA1 [Oryza sativa Japonica Group]

Protein Classification

NB-LRR family disease resistance protein( domain architecture ID 16524883)

NB-LRR (nucleotide-binding-leucine rich repeat) family disease resistance protein guards the plant against pathogens via an indirect interaction with an avirulence protein contained in the plant, triggering a defense response that restricts the pathogen growth

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NB-ARC super family cl26397
NB-ARC domain;
282-526 3.19e-32

NB-ARC domain;


The actual alignment was detected with superfamily member pfam00931:

Pssm-ID: 395745 [Multi-domain]  Cd Length: 245  Bit Score: 126.34  E-value: 3.19e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279662  282 RKGDRSRIIEDITRGDycdkDLTVIPIVGPGGIGKTTLTQHIYK---EVHNHFDVKVWVCVSLNFNLYRLKEEISKWIPK 358
Cdd:pfam00931    1 REDMVEKVIGKLSEKD----EPGIVGIHGMGGVGKTTLAAQIFNdfdEVEGHFDSVAWVVVSKTFTISTLQQTILQNLGL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279662  359 LKDDEKY---VDMDDSIEQRLKSKKLLLVLDDMWKcdnEDEWKKFLAPLrKAMTKGNIILVTTRFPVVAEMVKTFDRPIQ 435
Cdd:pfam00931   77 SEDDWDNkeeGELARKIRRALLTKRFLLVLDDVWD---EEDWDKIGIPL-PDRENGCRVLLTTRSEEVAGRVGGPSDPHE 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279662  436 LEGLEPEEFWELFQACVFgdDKSIDDHANLLETGEKIVKKLKGSPLAAKTVGRLLRNHLDLDDWMRVLESKEWESQT--- 512
Cdd:pfam00931  153 VELLEPDEAWELFENKVF--PKTLGECELLEDVAKEIVEKCRGLPLALKVLGGLLSCKKTVEEWKHVYDVLQSELKSnsy 230
                          250
                   ....*....|....
gi 1002279662  513 SENDIMPALKLSYD 526
Cdd:pfam00931  231 SLNSVRSILQLSYE 244
Rx_N pfam18052
Rx N-terminal domain; This entry represents the N-terminal domain found in many plant ...
41-88 4.46e-07

Rx N-terminal domain; This entry represents the N-terminal domain found in many plant resistance proteins. This domain has been predicted to be a coiled-coil, however the structure shows that it adopts a four helical bundle fold.


:

Pssm-ID: 436239  Cd Length: 93  Bit Score: 49.19  E-value: 4.46e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1002279662   41 IKMELLYAQGMLHNTRGRETSNPALQQLLLELRGLAYDADDVLDELDY 88
Cdd:pfam18052   30 LKDELESIQAFLEDAERKQITDEQVKLWLKQLRDVAYDAEDVLDEFLY 77
LRR super family cl34836
Leucine-rich repeat (LRR) protein [Transcription];
820-1026 5.65e-03

Leucine-rich repeat (LRR) protein [Transcription];


The actual alignment was detected with superfamily member COG4886:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 41.07  E-value: 5.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279662  820 LEDLKGSLGIYNLENAQAPEEAELSNKSRLHKLILDCDIKRLTKDSLQEEHILESLKPHSNLRELHINGRGGTTCPSWLG 899
Cdd:COG4886     54 SLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSNLTNLESLDLSGNQLTDLPEELA 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279662  900 vnlSIKGLQTLRLDGvdwNKFPPLGKLLlinehgeeslvctteRSFPNLKRLELVG--IQRLAKWVGNdscfvFSLLKVL 977
Cdd:COG4886    134 ---NLTNLKELDLSN---NQLTDLPEPL---------------GNLTNLKSLDLSNnqLTDLPEELGN-----LTNLKEL 187
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1002279662  978 IIRDCPeLTELPFShstcprseqemnLTQLRTLKELEIVNCpKLSSFPP 1026
Cdd:COG4886    188 DLSNNQ-ITDLPEP------------LGNLTNLEELDLSGN-QLTDLPE 222
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
636-674 6.54e-03

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd04166:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 209  Bit Score: 39.86  E-value: 6.54e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1002279662  636 IRHLSIVIDDMDVND--RATFENIKKDFGTLSKRLDVEKLH 674
Cdd:cd04166    131 IRHVVVAVNKMDLVDydEEVFEEIKADYLAFAASLGIEDIT 171
 
Name Accession Description Interval E-value
NB-ARC pfam00931
NB-ARC domain;
282-526 3.19e-32

NB-ARC domain;


Pssm-ID: 395745 [Multi-domain]  Cd Length: 245  Bit Score: 126.34  E-value: 3.19e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279662  282 RKGDRSRIIEDITRGDycdkDLTVIPIVGPGGIGKTTLTQHIYK---EVHNHFDVKVWVCVSLNFNLYRLKEEISKWIPK 358
Cdd:pfam00931    1 REDMVEKVIGKLSEKD----EPGIVGIHGMGGVGKTTLAAQIFNdfdEVEGHFDSVAWVVVSKTFTISTLQQTILQNLGL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279662  359 LKDDEKY---VDMDDSIEQRLKSKKLLLVLDDMWKcdnEDEWKKFLAPLrKAMTKGNIILVTTRFPVVAEMVKTFDRPIQ 435
Cdd:pfam00931   77 SEDDWDNkeeGELARKIRRALLTKRFLLVLDDVWD---EEDWDKIGIPL-PDRENGCRVLLTTRSEEVAGRVGGPSDPHE 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279662  436 LEGLEPEEFWELFQACVFgdDKSIDDHANLLETGEKIVKKLKGSPLAAKTVGRLLRNHLDLDDWMRVLESKEWESQT--- 512
Cdd:pfam00931  153 VELLEPDEAWELFENKVF--PKTLGECELLEDVAKEIVEKCRGLPLALKVLGGLLSCKKTVEEWKHVYDVLQSELKSnsy 230
                          250
                   ....*....|....
gi 1002279662  513 SENDIMPALKLSYD 526
Cdd:pfam00931  231 SLNSVRSILQLSYE 244
Rx_N pfam18052
Rx N-terminal domain; This entry represents the N-terminal domain found in many plant ...
41-88 4.46e-07

Rx N-terminal domain; This entry represents the N-terminal domain found in many plant resistance proteins. This domain has been predicted to be a coiled-coil, however the structure shows that it adopts a four helical bundle fold.


Pssm-ID: 436239  Cd Length: 93  Bit Score: 49.19  E-value: 4.46e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1002279662   41 IKMELLYAQGMLHNTRGRETSNPALQQLLLELRGLAYDADDVLDELDY 88
Cdd:pfam18052   30 LKDELESIQAFLEDAERKQITDEQVKLWLKQLRDVAYDAEDVLDEFLY 77
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
820-1026 5.65e-03

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 41.07  E-value: 5.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279662  820 LEDLKGSLGIYNLENAQAPEEAELSNKSRLHKLILDCDIKRLTKDSLQEEHILESLKPHSNLRELHINGRGGTTCPSWLG 899
Cdd:COG4886     54 SLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSNLTNLESLDLSGNQLTDLPEELA 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279662  900 vnlSIKGLQTLRLDGvdwNKFPPLGKLLlinehgeeslvctteRSFPNLKRLELVG--IQRLAKWVGNdscfvFSLLKVL 977
Cdd:COG4886    134 ---NLTNLKELDLSN---NQLTDLPEPL---------------GNLTNLKSLDLSNnqLTDLPEELGN-----LTNLKEL 187
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1002279662  978 IIRDCPeLTELPFShstcprseqemnLTQLRTLKELEIVNCpKLSSFPP 1026
Cdd:COG4886    188 DLSNNQ-ITDLPEP------------LGNLTNLEELDLSGN-QLTDLPE 222
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
636-674 6.54e-03

CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS subfamily. CysN, together with protein CysD, form the ATP sulfurylase (ATPS) complex in some bacteria and lower eukaryotes. ATPS catalyzes the production of ATP sulfurylase (APS) and pyrophosphate (PPi) from ATP and sulfate. CysD, which catalyzes ATP hydrolysis, is a member of the ATP pyrophosphatase (ATP PPase) family. CysN hydrolysis of GTP is required for CysD hydrolysis of ATP; however, CysN hydrolysis of GTP is not dependent on CysD hydrolysis of ATP. CysN is an example of lateral gene transfer followed by acquisition of new function. In many organisms, an ATPS exists which is not GTP-dependent and shares no sequence or structural similarity to CysN.


Pssm-ID: 206729 [Multi-domain]  Cd Length: 209  Bit Score: 39.86  E-value: 6.54e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1002279662  636 IRHLSIVIDDMDVND--RATFENIKKDFGTLSKRLDVEKLH 674
Cdd:cd04166    131 IRHVVVAVNKMDLVDydEEVFEEIKADYLAFAASLGIEDIT 171
 
Name Accession Description Interval E-value
NB-ARC pfam00931
NB-ARC domain;
282-526 3.19e-32

NB-ARC domain;


Pssm-ID: 395745 [Multi-domain]  Cd Length: 245  Bit Score: 126.34  E-value: 3.19e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279662  282 RKGDRSRIIEDITRGDycdkDLTVIPIVGPGGIGKTTLTQHIYK---EVHNHFDVKVWVCVSLNFNLYRLKEEISKWIPK 358
Cdd:pfam00931    1 REDMVEKVIGKLSEKD----EPGIVGIHGMGGVGKTTLAAQIFNdfdEVEGHFDSVAWVVVSKTFTISTLQQTILQNLGL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279662  359 LKDDEKY---VDMDDSIEQRLKSKKLLLVLDDMWKcdnEDEWKKFLAPLrKAMTKGNIILVTTRFPVVAEMVKTFDRPIQ 435
Cdd:pfam00931   77 SEDDWDNkeeGELARKIRRALLTKRFLLVLDDVWD---EEDWDKIGIPL-PDRENGCRVLLTTRSEEVAGRVGGPSDPHE 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279662  436 LEGLEPEEFWELFQACVFgdDKSIDDHANLLETGEKIVKKLKGSPLAAKTVGRLLRNHLDLDDWMRVLESKEWESQT--- 512
Cdd:pfam00931  153 VELLEPDEAWELFENKVF--PKTLGECELLEDVAKEIVEKCRGLPLALKVLGGLLSCKKTVEEWKHVYDVLQSELKSnsy 230
                          250
                   ....*....|....
gi 1002279662  513 SENDIMPALKLSYD 526
Cdd:pfam00931  231 SLNSVRSILQLSYE 244
Rx_N pfam18052
Rx N-terminal domain; This entry represents the N-terminal domain found in many plant ...
41-88 4.46e-07

Rx N-terminal domain; This entry represents the N-terminal domain found in many plant resistance proteins. This domain has been predicted to be a coiled-coil, however the structure shows that it adopts a four helical bundle fold.


Pssm-ID: 436239  Cd Length: 93  Bit Score: 49.19  E-value: 4.46e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1002279662   41 IKMELLYAQGMLHNTRGRETSNPALQQLLLELRGLAYDADDVLDELDY 88
Cdd:pfam18052   30 LKDELESIQAFLEDAERKQITDEQVKLWLKQLRDVAYDAEDVLDEFLY 77
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
820-1026 5.65e-03

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 41.07  E-value: 5.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279662  820 LEDLKGSLGIYNLENAQAPEEAELSNKSRLHKLILDCDIKRLTKDSLQEEHILESLKPHSNLRELHINGRGGTTCPSWLG 899
Cdd:COG4886     54 SLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSNLTNLESLDLSGNQLTDLPEELA 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279662  900 vnlSIKGLQTLRLDGvdwNKFPPLGKLLlinehgeeslvctteRSFPNLKRLELVG--IQRLAKWVGNdscfvFSLLKVL 977
Cdd:COG4886    134 ---NLTNLKELDLSN---NQLTDLPEPL---------------GNLTNLKSLDLSNnqLTDLPEELGN-----LTNLKEL 187
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1002279662  978 IIRDCPeLTELPFShstcprseqemnLTQLRTLKELEIVNCpKLSSFPP 1026
Cdd:COG4886    188 DLSNNQ-ITDLPEP------------LGNLTNLEELDLSGN-QLTDLPE 222
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
636-674 6.54e-03

CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS subfamily. CysN, together with protein CysD, form the ATP sulfurylase (ATPS) complex in some bacteria and lower eukaryotes. ATPS catalyzes the production of ATP sulfurylase (APS) and pyrophosphate (PPi) from ATP and sulfate. CysD, which catalyzes ATP hydrolysis, is a member of the ATP pyrophosphatase (ATP PPase) family. CysN hydrolysis of GTP is required for CysD hydrolysis of ATP; however, CysN hydrolysis of GTP is not dependent on CysD hydrolysis of ATP. CysN is an example of lateral gene transfer followed by acquisition of new function. In many organisms, an ATPS exists which is not GTP-dependent and shares no sequence or structural similarity to CysN.


Pssm-ID: 206729 [Multi-domain]  Cd Length: 209  Bit Score: 39.86  E-value: 6.54e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1002279662  636 IRHLSIVIDDMDVND--RATFENIKKDFGTLSKRLDVEKLH 674
Cdd:cd04166    131 IRHVVVAVNKMDLVDydEEVFEEIKADYLAFAASLGIEDIT 171
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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