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Conserved domains on  [gi|145340318|ref|NP_193432|]
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disease resistance protein (TIR-NBS class) [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN03210 super family cl33662
Resistant to P. syringae 6; Provisional
 1-449 6.34e-170

Resistant to P. syringae 6; Provisional


The actual alignment was detected with superfamily member PLN03210:

Pssm-ID: 215633 [Multi-domain]  Cd Length: 1153  Bit Score: 516.35  E-value: 6.34e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318    1 MKSSSSQS----YDVFPNFRGEDVRHSLVSHLRKELDRKFINTFNDNRIERSRKITPELLLAIENSRISLVVFSKNYASS 76
Cdd:PLN03210    1 MASSSSSSrnwvYDVFPSFSGEDVRITFLSHFLKELDRKLIIAFKDNEIERSQSLDPELKQAIRDSRIAVVVFSKNYASS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318   77 TWCLDELVKIQECYEKLDQMVIPIFYKVDPSHVRKQTGEFGMVFGETCKGRTENEKRKWMRALAEVAHLAGEDLRNWRSE 156
Cdd:PLN03210   81 SWCLNELLEIVRCKEELGQLVIPVFYGLDPSHVRKQTGDFGEAFEKTCQNKTEDEKIQWKQALTDVANILGYHSQNWPNE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318  157 AEMLENIAKDVSNKL-FPPSNNFSDFVGIEAHIEALISMLRFDSKKARMIGICGPSETGKTTIGRALYSRLKSDFH---- 231
Cdd:PLN03210  161 AKMIEEIANDVLGKLnLTPSNDFEDFVGIEDHIAKMSSLLHLESEEVRMVGIWGSSGIGKTTIARALFSRLSRQFQssvf 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318  232 -HRAFVA-----YKRKIRSDYDQKLYWEEQFLSEILCQKDIKIEECGAVEQRLKHTKVLIVLDDVDDIELLKTLVGRIRW 305
Cdd:PLN03210  241 iDRAFISksmeiYSSANPDDYNMKLHLQRAFLSEILDKKDIKIYHLGAMEERLKHRKVLIFIDDLDDQDVLDALAGQTQW 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318  306 FGSESKIVVITQKRELLKAHNIAHVYEVGFPSEELAHQMFCRYAFGKNSPPHGFNELADEAAKIAGNRPKALKYVGSSFR 385
Cdd:PLN03210  321 FGSGSRIIVITKDKHFLRAHGIDHIYEVCLPSNELALEMFCRSAFKKNSPPDGFMELASEVALRAGNLPLGLNVLGSYLR 400

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145340318  386 RLDKEQWVKMLSEFRSN-----GNKLKISYDELDGKGQD----YVACLTNGSnsqvKAEWIHLALGVSIL-LNI 449
Cdd:PLN03210  401 GRDKEDWMDMLPRLRNGldgkiEKTLRVSYDGLNNKKDKaifrHIACLFNGE----KVNDIKLLLANSDLdVNI 470
BRX pfam08381
Transcription factor regulating root and shoot growth via Pin3; The BREVIS RADIX (BRX) domain ...
 537-592 1.52e-22

Transcription factor regulating root and shoot growth via Pin3; The BREVIS RADIX (BRX) domain was characterized as being a transcription factor in plants regulating the extent of cell proliferation and elongation in the growth zone of the root. BRX is rate limiting for auxin-responsive gene-expression by mediating cross-talk with the brassino-steroid pathway. BRX has a ubiquitous, although quantitatively variable role in modulating the growth rate in both the root and the shoot. The family features a short region of alpha-helix, approximately 60 residues in length, which is found repeated up to three times. BRX is expressed in the vasculature and is rate-limiting for transcriptional auxin action.


:

Pssm-ID: 429960 [Multi-domain]  Cd Length: 56  Bit Score: 91.11  E-value: 1.52e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 145340318  537 EKEKIEYCEPHVYITPAIFSDGTRAPKYVESSRRVTQVHHAKTWWPENCEKVYENH 592
Cdd:pfam08381   1 EREWVEQDEPGVYITLVILPDGTKELKRVRFSRRRFSEKQAEVWWEENRDRVYEKY 56
BRX super family cl07125
Transcription factor regulating root and shoot growth via Pin3; The BREVIS RADIX (BRX) domain ...
 433-485 1.26e-16

Transcription factor regulating root and shoot growth via Pin3; The BREVIS RADIX (BRX) domain was characterized as being a transcription factor in plants regulating the extent of cell proliferation and elongation in the growth zone of the root. BRX is rate limiting for auxin-responsive gene-expression by mediating cross-talk with the brassino-steroid pathway. BRX has a ubiquitous, although quantitatively variable role in modulating the growth rate in both the root and the shoot. The family features a short region of alpha-helix, approximately 60 residues in length, which is found repeated up to three times. BRX is expressed in the vasculature and is rate-limiting for transcriptional auxin action.


The actual alignment was detected with superfamily member pfam08381:

Pssm-ID: 429960 [Multi-domain]  Cd Length: 56  Bit Score: 74.16  E-value: 1.26e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 145340318  433 KAEWI-HLALGVSILLNIRSDGTTILKHLSYNRSM--AQQAKIWWYENLERVCKKY 485
Cdd:pfam08381   1 EREWVeQDEPGVYITLVILPDGTKELKRVRFSRRRfsEKQAEVWWEENRDRVYEKY 56
 
Name Accession Description Interval E-value
PLN03210 PLN03210
Resistant to P. syringae 6; Provisional
 1-449 6.34e-170

Resistant to P. syringae 6; Provisional


Pssm-ID: 215633 [Multi-domain]  Cd Length: 1153  Bit Score: 516.35  E-value: 6.34e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318    1 MKSSSSQS----YDVFPNFRGEDVRHSLVSHLRKELDRKFINTFNDNRIERSRKITPELLLAIENSRISLVVFSKNYASS 76
Cdd:PLN03210    1 MASSSSSSrnwvYDVFPSFSGEDVRITFLSHFLKELDRKLIIAFKDNEIERSQSLDPELKQAIRDSRIAVVVFSKNYASS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318   77 TWCLDELVKIQECYEKLDQMVIPIFYKVDPSHVRKQTGEFGMVFGETCKGRTENEKRKWMRALAEVAHLAGEDLRNWRSE 156
Cdd:PLN03210   81 SWCLNELLEIVRCKEELGQLVIPVFYGLDPSHVRKQTGDFGEAFEKTCQNKTEDEKIQWKQALTDVANILGYHSQNWPNE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318  157 AEMLENIAKDVSNKL-FPPSNNFSDFVGIEAHIEALISMLRFDSKKARMIGICGPSETGKTTIGRALYSRLKSDFH---- 231
Cdd:PLN03210  161 AKMIEEIANDVLGKLnLTPSNDFEDFVGIEDHIAKMSSLLHLESEEVRMVGIWGSSGIGKTTIARALFSRLSRQFQssvf 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318  232 -HRAFVA-----YKRKIRSDYDQKLYWEEQFLSEILCQKDIKIEECGAVEQRLKHTKVLIVLDDVDDIELLKTLVGRIRW 305
Cdd:PLN03210  241 iDRAFISksmeiYSSANPDDYNMKLHLQRAFLSEILDKKDIKIYHLGAMEERLKHRKVLIFIDDLDDQDVLDALAGQTQW 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318  306 FGSESKIVVITQKRELLKAHNIAHVYEVGFPSEELAHQMFCRYAFGKNSPPHGFNELADEAAKIAGNRPKALKYVGSSFR 385
Cdd:PLN03210  321 FGSGSRIIVITKDKHFLRAHGIDHIYEVCLPSNELALEMFCRSAFKKNSPPDGFMELASEVALRAGNLPLGLNVLGSYLR 400

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145340318  386 RLDKEQWVKMLSEFRSN-----GNKLKISYDELDGKGQD----YVACLTNGSnsqvKAEWIHLALGVSIL-LNI 449
Cdd:PLN03210  401 GRDKEDWMDMLPRLRNGldgkiEKTLRVSYDGLNNKKDKaifrHIACLFNGE----KVNDIKLLLANSDLdVNI 470
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
 9-171 2.88e-66

TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular signalling domain found in MyD88, interleukin 1 receptor and the Toll receptor. It contains three highly-conserved regions, and mediates protein-protein interactions between the Toll-like receptors (TLRs) and signal-transduction components. TIR-like motifs are also found in plant proteins thought to be involved in resistance to disease. When activated, TIR domains recruit cytoplasmic adaptor proteins MyD88 and TOLLIP (Toll interacting protein). In turn, these associate with various kinases to set off signalling cascades.


Pssm-ID: 396246 [Multi-domain]  Cd Length: 165  Bit Score: 214.92  E-value: 2.88e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318    9 YDVFPNFRGEDVRHSLVSHLRKELDRKFINTFNDNR-IERSRKITPELLLAIENSRISLVVFSKNYASSTWCLDELVKIQ 87
Cdd:pfam01582   1 YDVFLSFRGSDTREWFVSHLLKELKQKGIKLFIDDRdLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSGWCLDELVKIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318   88 ECYEKLDQMVIPIFYKVDPSHVRKQTGEFGMVFGETCKGRTENEKRKWMRALAEVAHLagEDLRNWRSEAEMLENIAKDV 167
Cdd:pfam01582  81 ECALDLGQKVIPIFYEVDPSDVRKQTGSFGKAFKKHKKVLTEEKVLKWRGALNEVANI--WHSKSVSDESKFWKKIAYDI 158


                  ....
gi 145340318  168 SNKL 171
Cdd:pfam01582 159 SNKL 162
TIR smart00255
Toll - interleukin 1 - resistance;
9-145 6.93e-46

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 159.41  E-value: 6.93e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318     9 YDVFPNFRG-EDVRHSLVSHLRKELDRKFINTFNDNRIERSRKITpELLLAIENSRISLVVFSKNYASSTWCLDELVKIQ 87
Cdd:smart00255   2 YDVFISYSGkEDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLE-EIDEAIEKSRIAIVVLSPNYAESEWCLDELVAAL 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318    88 ECYEKLDQM-VIPIFYKVDPSHVRKQTGEFGMVFGETCKGRTENEK-RKWMRALAEVAHL 145
Cdd:smart00255  81 ENALEEGGLrVIPIFYEVIPSDVRKQPGKFRKVFKKNYLKWPEDEKeQFWKKALYAVPSK 140
BRX pfam08381
Transcription factor regulating root and shoot growth via Pin3; The BREVIS RADIX (BRX) domain ...
 537-592 1.52e-22

Transcription factor regulating root and shoot growth via Pin3; The BREVIS RADIX (BRX) domain was characterized as being a transcription factor in plants regulating the extent of cell proliferation and elongation in the growth zone of the root. BRX is rate limiting for auxin-responsive gene-expression by mediating cross-talk with the brassino-steroid pathway. BRX has a ubiquitous, although quantitatively variable role in modulating the growth rate in both the root and the shoot. The family features a short region of alpha-helix, approximately 60 residues in length, which is found repeated up to three times. BRX is expressed in the vasculature and is rate-limiting for transcriptional auxin action.


Pssm-ID: 429960 [Multi-domain]  Cd Length: 56  Bit Score: 91.11  E-value: 1.52e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 145340318  537 EKEKIEYCEPHVYITPAIFSDGTRAPKYVESSRRVTQVHHAKTWWPENCEKVYENH 592
Cdd:pfam08381   1 EREWVEQDEPGVYITLVILPDGTKELKRVRFSRRRFSEKQAEVWWEENRDRVYEKY 56
BRX pfam08381
Transcription factor regulating root and shoot growth via Pin3; The BREVIS RADIX (BRX) domain ...
 433-485 1.26e-16

Transcription factor regulating root and shoot growth via Pin3; The BREVIS RADIX (BRX) domain was characterized as being a transcription factor in plants regulating the extent of cell proliferation and elongation in the growth zone of the root. BRX is rate limiting for auxin-responsive gene-expression by mediating cross-talk with the brassino-steroid pathway. BRX has a ubiquitous, although quantitatively variable role in modulating the growth rate in both the root and the shoot. The family features a short region of alpha-helix, approximately 60 residues in length, which is found repeated up to three times. BRX is expressed in the vasculature and is rate-limiting for transcriptional auxin action.


Pssm-ID: 429960 [Multi-domain]  Cd Length: 56  Bit Score: 74.16  E-value: 1.26e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 145340318  433 KAEWI-HLALGVSILLNIRSDGTTILKHLSYNRSM--AQQAKIWWYENLERVCKKY 485
Cdd:pfam08381   1 EREWVeQDEPGVYITLVILPDGTKELKRVRFSRRRfsEKQAEVWWEENRDRVYEKY 56
COG4916 COG4916
Uncharacterized conserved protein [Function unknown];
9-219 1.23e-03

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443944 [Multi-domain]  Cd Length: 236  Bit Score: 40.87  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318   9 YDVFPNFRGEDvRHsLVSHLRKELDRKFINTFNDNRiERSRKITPELLLAIEN-----SRISLVVFSKNYASSTWCLDEL 83
Cdd:COG4916    1 YDVALSFAGED-RE-FVERVAEALKARGIKVFYDEN-EEAELWGKDLDEYLQDiyrseSRFVVVFLSKDYVEKKWTGLER 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318  84 VKIQECYEKLDQM-VIPIfyKVDPSHVrkqTGEFGMVFGETCKGRTEnekrkwmralAEVAHLAGEDLRNWRSEAEMlEN 162
Cdd:COG4916   78 RAALARAMQRKKEyILPI--RLDDTEI---PGILATIGYIDLRNRTP----------EEIADLILEKLAKGRPKPSR-AL 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 145340318 163 IAKDVSNKLFPPSNNFSDFVGIEAHIEALISMLRFDSKKARMIGICGPSETGKTTIG 219
Cdd:COG4916  142 SLAPTETVGSPARPNDAPGVFSTASAKTCVSGNLTGLLAVLDLEEVQGFLIGVRGDT 198
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 182-323 3.55e-03

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 38.67  E-value: 3.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318 182 VGIEAHIEALISMLRFDSKKArmIGICGPSETGKTTIGRALYSRLKSDFHHraFVAYKrkiRSDYDQKLYWEEQFLSEIL 261
Cdd:cd00009    1 VGQEEAIEALREALELPPPKN--LLLYGPPGTGKTTLARAIANELFRPGAP--FLYLN---ASDLLEGLVVAELFGHFLV 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318 262 CQKDIKIEecgaveqrlKHTKVLIVLDDVDDI------ELLKTLVGRIRWFGSESKIVVI--TQKRELLK 323
Cdd:cd00009   74 RLLFELAE---------KAKPGVLFIDEIDSLsrgaqnALLRVLETLNDLRIDRENVRVIgaTNRPLLGD 134
 
Name Accession Description Interval E-value
PLN03210 PLN03210
Resistant to P. syringae 6; Provisional
 1-449 6.34e-170

Resistant to P. syringae 6; Provisional


Pssm-ID: 215633 [Multi-domain]  Cd Length: 1153  Bit Score: 516.35  E-value: 6.34e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318    1 MKSSSSQS----YDVFPNFRGEDVRHSLVSHLRKELDRKFINTFNDNRIERSRKITPELLLAIENSRISLVVFSKNYASS 76
Cdd:PLN03210    1 MASSSSSSrnwvYDVFPSFSGEDVRITFLSHFLKELDRKLIIAFKDNEIERSQSLDPELKQAIRDSRIAVVVFSKNYASS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318   77 TWCLDELVKIQECYEKLDQMVIPIFYKVDPSHVRKQTGEFGMVFGETCKGRTENEKRKWMRALAEVAHLAGEDLRNWRSE 156
Cdd:PLN03210   81 SWCLNELLEIVRCKEELGQLVIPVFYGLDPSHVRKQTGDFGEAFEKTCQNKTEDEKIQWKQALTDVANILGYHSQNWPNE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318  157 AEMLENIAKDVSNKL-FPPSNNFSDFVGIEAHIEALISMLRFDSKKARMIGICGPSETGKTTIGRALYSRLKSDFH---- 231
Cdd:PLN03210  161 AKMIEEIANDVLGKLnLTPSNDFEDFVGIEDHIAKMSSLLHLESEEVRMVGIWGSSGIGKTTIARALFSRLSRQFQssvf 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318  232 -HRAFVA-----YKRKIRSDYDQKLYWEEQFLSEILCQKDIKIEECGAVEQRLKHTKVLIVLDDVDDIELLKTLVGRIRW 305
Cdd:PLN03210  241 iDRAFISksmeiYSSANPDDYNMKLHLQRAFLSEILDKKDIKIYHLGAMEERLKHRKVLIFIDDLDDQDVLDALAGQTQW 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318  306 FGSESKIVVITQKRELLKAHNIAHVYEVGFPSEELAHQMFCRYAFGKNSPPHGFNELADEAAKIAGNRPKALKYVGSSFR 385
Cdd:PLN03210  321 FGSGSRIIVITKDKHFLRAHGIDHIYEVCLPSNELALEMFCRSAFKKNSPPDGFMELASEVALRAGNLPLGLNVLGSYLR 400

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145340318  386 RLDKEQWVKMLSEFRSN-----GNKLKISYDELDGKGQD----YVACLTNGSnsqvKAEWIHLALGVSIL-LNI 449
Cdd:PLN03210  401 GRDKEDWMDMLPRLRNGldgkiEKTLRVSYDGLNNKKDKaifrHIACLFNGE----KVNDIKLLLANSDLdVNI 470
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
 9-171 2.88e-66

TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular signalling domain found in MyD88, interleukin 1 receptor and the Toll receptor. It contains three highly-conserved regions, and mediates protein-protein interactions between the Toll-like receptors (TLRs) and signal-transduction components. TIR-like motifs are also found in plant proteins thought to be involved in resistance to disease. When activated, TIR domains recruit cytoplasmic adaptor proteins MyD88 and TOLLIP (Toll interacting protein). In turn, these associate with various kinases to set off signalling cascades.


Pssm-ID: 396246 [Multi-domain]  Cd Length: 165  Bit Score: 214.92  E-value: 2.88e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318    9 YDVFPNFRGEDVRHSLVSHLRKELDRKFINTFNDNR-IERSRKITPELLLAIENSRISLVVFSKNYASSTWCLDELVKIQ 87
Cdd:pfam01582   1 YDVFLSFRGSDTREWFVSHLLKELKQKGIKLFIDDRdLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSGWCLDELVKIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318   88 ECYEKLDQMVIPIFYKVDPSHVRKQTGEFGMVFGETCKGRTENEKRKWMRALAEVAHLagEDLRNWRSEAEMLENIAKDV 167
Cdd:pfam01582  81 ECALDLGQKVIPIFYEVDPSDVRKQTGSFGKAFKKHKKVLTEEKVLKWRGALNEVANI--WHSKSVSDESKFWKKIAYDI 158


                  ....
gi 145340318  168 SNKL 171
Cdd:pfam01582 159 SNKL 162
TIR smart00255
Toll - interleukin 1 - resistance;
9-145 6.93e-46

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 159.41  E-value: 6.93e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318     9 YDVFPNFRG-EDVRHSLVSHLRKELDRKFINTFNDNRIERSRKITpELLLAIENSRISLVVFSKNYASSTWCLDELVKIQ 87
Cdd:smart00255   2 YDVFISYSGkEDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLE-EIDEAIEKSRIAIVVLSPNYAESEWCLDELVAAL 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318    88 ECYEKLDQM-VIPIFYKVDPSHVRKQTGEFGMVFGETCKGRTENEK-RKWMRALAEVAHL 145
Cdd:smart00255  81 ENALEEGGLrVIPIFYEVIPSDVRKQPGKFRKVFKKNYLKWPEDEKeQFWKKALYAVPSK 140
BRX pfam08381
Transcription factor regulating root and shoot growth via Pin3; The BREVIS RADIX (BRX) domain ...
 537-592 1.52e-22

Transcription factor regulating root and shoot growth via Pin3; The BREVIS RADIX (BRX) domain was characterized as being a transcription factor in plants regulating the extent of cell proliferation and elongation in the growth zone of the root. BRX is rate limiting for auxin-responsive gene-expression by mediating cross-talk with the brassino-steroid pathway. BRX has a ubiquitous, although quantitatively variable role in modulating the growth rate in both the root and the shoot. The family features a short region of alpha-helix, approximately 60 residues in length, which is found repeated up to three times. BRX is expressed in the vasculature and is rate-limiting for transcriptional auxin action.


Pssm-ID: 429960 [Multi-domain]  Cd Length: 56  Bit Score: 91.11  E-value: 1.52e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 145340318  537 EKEKIEYCEPHVYITPAIFSDGTRAPKYVESSRRVTQVHHAKTWWPENCEKVYENH 592
Cdd:pfam08381   1 EREWVEQDEPGVYITLVILPDGTKELKRVRFSRRRFSEKQAEVWWEENRDRVYEKY 56
BRX pfam08381
Transcription factor regulating root and shoot growth via Pin3; The BREVIS RADIX (BRX) domain ...
 433-485 1.26e-16

Transcription factor regulating root and shoot growth via Pin3; The BREVIS RADIX (BRX) domain was characterized as being a transcription factor in plants regulating the extent of cell proliferation and elongation in the growth zone of the root. BRX is rate limiting for auxin-responsive gene-expression by mediating cross-talk with the brassino-steroid pathway. BRX has a ubiquitous, although quantitatively variable role in modulating the growth rate in both the root and the shoot. The family features a short region of alpha-helix, approximately 60 residues in length, which is found repeated up to three times. BRX is expressed in the vasculature and is rate-limiting for transcriptional auxin action.


Pssm-ID: 429960 [Multi-domain]  Cd Length: 56  Bit Score: 74.16  E-value: 1.26e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 145340318  433 KAEWI-HLALGVSILLNIRSDGTTILKHLSYNRSM--AQQAKIWWYENLERVCKKY 485
Cdd:pfam08381   1 EREWVeQDEPGVYITLVILPDGTKELKRVRFSRRRfsEKQAEVWWEENRDRVYEKY 56
PLN03194 PLN03194
putative disease resistance protein; Provisional
 3-147 1.61e-11

putative disease resistance protein; Provisional


Pssm-ID: 215626 [Multi-domain]  Cd Length: 187  Bit Score: 63.69  E-value: 1.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318   3 SSSSQSYDVFPNFRGEDVRHSLVSHLRKELDRKFINTFNDNR-IERSRKITPELLLAIENSRISLVVFSKNYASSTWCLD 81
Cdd:PLN03194  21 SSSAKPCDVFINHRGIDTKRTIATLLYDHLSRLNLRPFLDNKnMKPGDKLFDKINSAIRNCKVGVAVFSPRYCESYFCLH 100

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145340318  82 ELVKIQECYEKldqmVIPIFYKVDPSHVRkqtgefgMVFGETCkgrTENEKRKWMRALAEVAHLAG 147
Cdd:PLN03194 101 ELALIMESKKR----VIPIFCDVKPSQLR-------VVDNGTC---PDEEIRRFNWALEEAKYTVG 152
NB-ARC pfam00931
NB-ARC domain;
184-414 8.35e-08

NB-ARC domain;


Pssm-ID: 395745 [Multi-domain]  Cd Length: 245  Bit Score: 53.92  E-value: 8.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318  184 IEAHIEALISMLrFDSKKARMIGICGPSETGKTTIGRALYSRLKSDFHH---RAFVAYKRKIRSDYDQKLYWEEQFLSEI 260
Cdd:pfam00931   1 REDMVEKVIGKL-SEKDEPGIVGIHGMGGVGKTTLAAQIFNDFDEVEGHfdsVAWVVVSKTFTISTLQQTILQNLGLSED 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318  261 LCQKDIKIEECGAVEQRLKHTKVLIVLDDVDDIELLKTLVGRIRWFGSESKIVVITQKRELLKAHNIAHV-YEVGFPSEE 339
Cdd:pfam00931  80 DWDNKEEGELARKIRRALLTKRFLLVLDDVWDEEDWDKIGIPLPDRENGCRVLLTTRSEEVAGRVGGPSDpHEVELLEPD 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145340318  340 LAHQMFCRYAFGKNS-PPHGFNELADEAAKIAGNRPKALKYVGSSFRRLDKEQ-WVKMLSEFRSNGNKLKISYDELD 414
Cdd:pfam00931 160 EAWELFENKVFPKTLgECELLEDVAKEIVEKCRGLPLALKVLGGLLSCKKTVEeWKHVYDVLQSELKSNSYSLNSVR 236
TIR_2 pfam13676
TIR domain; This is a family of Toll-like receptors.
 11-108 1.24e-06

TIR domain; This is a family of Toll-like receptors.


Pssm-ID: 463954 [Multi-domain]  Cd Length: 118  Bit Score: 47.70  E-value: 1.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318   11 VFPNFRGEDvrHSLVSHLRKELDRKFINTFNDNR-IERSRKITPELLLAIENSRISLVVFSKNYASSTWCLDELVKIQEc 89
Cdd:pfam13676   1 VFISYAGED--RAWAEWLADALEAAGYRVWLDRWdIRPGDDWVEEIEEAIENSDRVLVVLSPNYLESPWCRAEWEAALA- 77

                          90
                  ....*....|....*....
gi 145340318   90 YEKLDQMVIPIFYKVDPSH 108
Cdd:pfam13676  78 DPEGRKRLIPVRLECDLEL 96
AAA_18 pfam13238
AAA domain;
205-251 3.49e-04

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 40.87  E-value: 3.49e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 145340318  205 IGICGPSETGKTTIGRALYSRLKSDFHHRaFVAYKRKIRSDYDQKLY 251
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELSKRLGFGDNVR-DLALENGLVLGDDPETR 46
COG4916 COG4916
Uncharacterized conserved protein [Function unknown];
9-219 1.23e-03

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443944 [Multi-domain]  Cd Length: 236  Bit Score: 40.87  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318   9 YDVFPNFRGEDvRHsLVSHLRKELDRKFINTFNDNRiERSRKITPELLLAIEN-----SRISLVVFSKNYASSTWCLDEL 83
Cdd:COG4916    1 YDVALSFAGED-RE-FVERVAEALKARGIKVFYDEN-EEAELWGKDLDEYLQDiyrseSRFVVVFLSKDYVEKKWTGLER 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318  84 VKIQECYEKLDQM-VIPIfyKVDPSHVrkqTGEFGMVFGETCKGRTEnekrkwmralAEVAHLAGEDLRNWRSEAEMlEN 162
Cdd:COG4916   78 RAALARAMQRKKEyILPI--RLDDTEI---PGILATIGYIDLRNRTP----------EEIADLILEKLAKGRPKPSR-AL 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 145340318 163 IAKDVSNKLFPPSNNFSDFVGIEAHIEALISMLRFDSKKARMIGICGPSETGKTTIG 219
Cdd:COG4916  142 SLAPTETVGSPARPNDAPGVFSTASAKTCVSGNLTGLLAVLDLEEVQGFLIGVRGDT 198
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 199-229 1.28e-03

Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440337 [Multi-domain]  Cd Length: 206  Bit Score: 40.59  E-value: 1.28e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 145340318 199 SKKARMIGICGPSETGKTTIGRALYSRLKSD 229
Cdd:COG0572    4 SGKPRIIGIAGPSGSGKTTFARRLAEQLGAD 34
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
179-315 1.37e-03

Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 41.37  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318 179 SDFVGIEAHIEALISMLR--FDSKKARMIGICGPSETGKTTIGRALYSRLKSDFHHRAF---VAYK--RKIRSDYdqkly 251
Cdd:COG1474   26 DRLPHREEEIEELASALRpaLRGERPSNVLIYGPTGTGKTAVAKYVLEELEEEAEERGVdvrVVYVncRQASTRY----- 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318 252 weeQFLSEILCQ--KDIKIEECG--------AVEQRLKHTK--VLIVLDDVDDI------ELLKTLVgRIRWFGSESKIV 313
Cdd:COG1474  101 ---RVLSRILEElgSGEDIPSTGlstdelfdRLYEALDERDgvLVVVLDEIDYLvddegdDLLYQLL-RANEELEGARVG 176


                 ..
gi 145340318 314 VI 315
Cdd:COG1474  177 VI 178
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 182-323 3.55e-03

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 38.67  E-value: 3.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318 182 VGIEAHIEALISMLRFDSKKArmIGICGPSETGKTTIGRALYSRLKSDFHHraFVAYKrkiRSDYDQKLYWEEQFLSEIL 261
Cdd:cd00009    1 VGQEEAIEALREALELPPPKN--LLLYGPPGTGKTTLARAIANELFRPGAP--FLYLN---ASDLLEGLVVAELFGHFLV 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318 262 CQKDIKIEecgaveqrlKHTKVLIVLDDVDDI------ELLKTLVGRIRWFGSESKIVVI--TQKRELLK 323
Cdd:cd00009   74 RLLFELAE---------KAKPGVLFIDEIDSLsrgaqnALLRVLETLNDLRIDRENVRVIgaTNRPLLGD 134
Pox_A32 pfam04665
Poxvirus A32 protein; The A32 protein is thought to be involved in viral DNA packaging.
 194-295 5.21e-03

Poxvirus A32 protein; The A32 protein is thought to be involved in viral DNA packaging.


Pssm-ID: 282513  Cd Length: 241  Bit Score: 38.96  E-value: 5.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340318  194 MLRFDSKKA-----RMIgICGPSETGKTTIGRALYSRLKSDFHHRAFV------AYKRKIRSDYDQKLYWEEQfLSEILC 262
Cdd:pfam04665   1 EVRFDRNSLladpfRMA-LVGGSGSGKTTYLLSLFRTLVRKYKHIFLFtpvynsAYDGYIWPDHINKVTSNEE-LEYSLS 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 145340318  263 QKDIKIEECGAVEQRLKHT-KVLIVLDDVDDIEL 295
Cdd:pfam04665  79 RYKQKIENYAKSASNQKENfRFLLILDDLGDKQT 112
PRK05541 PRK05541
adenylylsulfate kinase; Provisional
 199-232 5.32e-03

adenylylsulfate kinase; Provisional


Pssm-ID: 235498  Cd Length: 176  Bit Score: 38.50  E-value: 5.32e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 145340318 199 SKKARMIGICGPSETGKTTIGRALYSRLKSDFHH 232
Cdd:PRK05541   4 KPNGYVIWITGLAGSGKTTIAKALYERLKLKYSN 37
 
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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