|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03210 super family |
cl33662 |
Resistant to P. syringae 6; Provisional |
1-449 |
1.72e-168 |
|
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: 517.12 E-value: 1.72e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 1 MKSSSSQS----YDVFPNFRGEDVRHSLVSHLRKELDRKFINTFNDNRIERSRKITPELLLAIENSRISLVVFSKNYASS 76
Cdd:PLN03210 1 MASSSSSSrnwvYDVFPSFSGEDVRITFLSHFLKELDRKLIIAFKDNEIERSQSLDPELKQAIRDSRIAVVVFSKNYASS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 77 TWCLDELVKIQECYEKLDQMVIPIFYKVDPSHVRKQTGEFGMVFGETCKGRTENEKRKWMRALAEVAHLAGEDLRNWRSE 156
Cdd:PLN03210 81 SWCLNELLEIVRCKEELGQLVIPVFYGLDPSHVRKQTGDFGEAFEKTCQNKTEDEKIQWKQALTDVANILGYHSQNWPNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 157 AEMLENIAKDVSNKL-FPPSNNFSDFVGIEAHIEALISMLRFDSKKARMIGICGPSETGKTTIGRALYSRLKSDFH---- 231
Cdd:PLN03210 161 AKMIEEIANDVLGKLnLTPSNDFEDFVGIEDHIAKMSSLLHLESEEVRMVGIWGSSGIGKTTIARALFSRLSRQFQssvf 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 232 -HRAFVA-----YKRKIRSDYDQKLYWEEQFLSEILCQKDIKIEECGAVEQRLKHTKVLIVLDDVDDIELLKTLVGRIRW 305
Cdd:PLN03210 241 iDRAFISksmeiYSSANPDDYNMKLHLQRAFLSEILDKKDIKIYHLGAMEERLKHRKVLIFIDDLDDQDVLDALAGQTQW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 306 FGSESKIVVITQKRELLKAHNIAHVYEVGFPSEELAHQMFCRYAFGKNSPPHGFNELADEAAKIAGNRPKALKYVGSSFR 385
Cdd:PLN03210 321 FGSGSRIIVITKDKHFLRAHGIDHIYEVCLPSNELALEMFCRSAFKKNSPPDGFMELASEVALRAGNLPLGLNVLGSYLR 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063723127 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 |
2.91e-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: 90.34 E-value: 2.91e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063723127 537 EKEKIEYCEPHVYITPAIFSDGTRAPKYVESSRRVTQVHHAKTWWPENCEKVYENH 592
Cdd:pfam08381 1 EREWVEQDEPGVYITLVILPDGTKELKRVRFSRRRFSEKQAEVWWEENRDRVYEKY 56
|
|
| BRX |
pfam08381 |
Transcription factor regulating root and shoot growth via Pin3; The BREVIS RADIX (BRX) domain ... |
717-770 |
3.97e-19 |
|
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: 81.48 E-value: 3.97e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063723127 717 DEKNFEYCEQGVYITLGILSGGIIVLKHLEFSRRM--AQQAKVWWSENWIKVYQEH 770
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 |
2.28e-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: 73.77 E-value: 2.28e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063723127 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 |
1.72e-168 |
|
Resistant to P. syringae 6; Provisional
Pssm-ID: 215633 [Multi-domain] Cd Length: 1153 Bit Score: 517.12 E-value: 1.72e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 1 MKSSSSQS----YDVFPNFRGEDVRHSLVSHLRKELDRKFINTFNDNRIERSRKITPELLLAIENSRISLVVFSKNYASS 76
Cdd:PLN03210 1 MASSSSSSrnwvYDVFPSFSGEDVRITFLSHFLKELDRKLIIAFKDNEIERSQSLDPELKQAIRDSRIAVVVFSKNYASS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 77 TWCLDELVKIQECYEKLDQMVIPIFYKVDPSHVRKQTGEFGMVFGETCKGRTENEKRKWMRALAEVAHLAGEDLRNWRSE 156
Cdd:PLN03210 81 SWCLNELLEIVRCKEELGQLVIPVFYGLDPSHVRKQTGDFGEAFEKTCQNKTEDEKIQWKQALTDVANILGYHSQNWPNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 157 AEMLENIAKDVSNKL-FPPSNNFSDFVGIEAHIEALISMLRFDSKKARMIGICGPSETGKTTIGRALYSRLKSDFH---- 231
Cdd:PLN03210 161 AKMIEEIANDVLGKLnLTPSNDFEDFVGIEDHIAKMSSLLHLESEEVRMVGIWGSSGIGKTTIARALFSRLSRQFQssvf 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 232 -HRAFVA-----YKRKIRSDYDQKLYWEEQFLSEILCQKDIKIEECGAVEQRLKHTKVLIVLDDVDDIELLKTLVGRIRW 305
Cdd:PLN03210 241 iDRAFISksmeiYSSANPDDYNMKLHLQRAFLSEILDKKDIKIYHLGAMEERLKHRKVLIFIDDLDDQDVLDALAGQTQW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 306 FGSESKIVVITQKRELLKAHNIAHVYEVGFPSEELAHQMFCRYAFGKNSPPHGFNELADEAAKIAGNRPKALKYVGSSFR 385
Cdd:PLN03210 321 FGSGSRIIVITKDKHFLRAHGIDHIYEVCLPSNELALEMFCRSAFKKNSPPDGFMELASEVALRAGNLPLGLNVLGSYLR 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063723127 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 |
3.84e-65 |
|
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: 214.15 E-value: 3.84e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 9 YDVFPNFRGEDVRHSLVSHLRKELDRKFINTFNDNR-IERSRKITPELLLAIENSRISLVVFSKNYASSTWCLDELVKIQ 87
Cdd:pfam01582 1 YDVFLSFRGSDTREWFVSHLLKELKQKGIKLFIDDRdLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSGWCLDELVKIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 88 ECYEKLDQMVIPIFYKVDPSHVRKQTGEFGMVFGETCKGRTENEKRKWMRALAEVAHLagEDLRNWRSEAEMLENIAKDV 167
Cdd:pfam01582 81 ECALDLGQKVIPIFYEVDPSDVRKQTGSFGKAFKKHKKVLTEEKVLKWRGALNEVANI--WHSKSVSDESKFWKKIAYDI 158
|
....
gi 1063723127 168 SNKL 171
Cdd:pfam01582 159 SNKL 162
|
|
| TIR |
smart00255 |
Toll - interleukin 1 - resistance; |
9-145 |
4.32e-45 |
|
Toll - interleukin 1 - resistance;
Pssm-ID: 214587 [Multi-domain] Cd Length: 140 Bit Score: 158.26 E-value: 4.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 9 YDVFPNFRG-EDVRHSLVSHLRKELDRKFINTFNDNRIERSRKITpELLLAIENSRISLVVFSKNYASSTWCLDELVKIQ 87
Cdd:smart00255 2 YDVFISYSGkEDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLE-EIDEAIEKSRIAIVVLSPNYAESEWCLDELVAAL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 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 |
2.91e-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: 90.34 E-value: 2.91e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063723127 537 EKEKIEYCEPHVYITPAIFSDGTRAPKYVESSRRVTQVHHAKTWWPENCEKVYENH 592
Cdd:pfam08381 1 EREWVEQDEPGVYITLVILPDGTKELKRVRFSRRRFSEKQAEVWWEENRDRVYEKY 56
|
|
| BRX |
pfam08381 |
Transcription factor regulating root and shoot growth via Pin3; The BREVIS RADIX (BRX) domain ... |
717-770 |
3.97e-19 |
|
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: 81.48 E-value: 3.97e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063723127 717 DEKNFEYCEQGVYITLGILSGGIIVLKHLEFSRRM--AQQAKVWWSENWIKVYQEH 770
Cdd:pfam08381 1 EREWVEQDEPGVYITLVILPDGTKELKRVRFSRRRfsEKQAEVWWEENRDRVYEKY 56
|
|
| BRX |
pfam08381 |
Transcription factor regulating root and shoot growth via Pin3; The BREVIS RADIX (BRX) domain ... |
433-485 |
2.28e-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: 73.77 E-value: 2.28e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063723127 433 KAEWI-HLALGVSILLNIRSDGTTILKHLSYNRSM--AQQAKIWWYENLERVCKKY 485
Cdd:pfam08381 1 EREWVeQDEPGVYITLVILPDGTKELKRVRFSRRRfsEKQAEVWWEENRDRVYEKY 56
|
|
| CDC6 |
COG1474 |
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair]; |
179-315 |
1.43e-03 |
|
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
Pssm-ID: 441083 [Multi-domain] Cd Length: 389 Bit Score: 41.76 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 179 SDFVGIEAHIEALISMLR--FDSKKARMIGICGPSETGKTTIGRALYSRLKSDFHHRAF---VAYK--RKIRSDYdqkly 251
Cdd:COG1474 26 DRLPHREEEIEELASALRpaLRGERPSNVLIYGPTGTGKTAVAKYVLEELEEEAEERGVdvrVVYVncRQASTRY----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 252 weeQFLSEILCQ--KDIKIEECG--------AVEQRLKHTK--VLIVLDDVDDI------ELLKTLVgRIRWFGSESKIV 313
Cdd:COG1474 101 ---RVLSRILEElgSGEDIPSTGlstdelfdRLYEALDERDgvLVVVLDEIDYLvddegdDLLYQLL-RANEELEGARVG 176
|
..
gi 1063723127 314 VI 315
Cdd:COG1474 177 VI 178
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
182-323 |
4.73e-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: 38.28 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 182 VGIEAHIEALISMLRFDSKKArmIGICGPSETGKTTIGRALYSRLKSDFHHraFVAYKrkiRSDYDQKLYWEEQFLSEIL 261
Cdd:cd00009 1 VGQEEAIEALREALELPPPKN--LLLYGPPGTGKTTLARAIANELFRPGAP--FLYLN---ASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 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 |
1.72e-168 |
|
Resistant to P. syringae 6; Provisional
Pssm-ID: 215633 [Multi-domain] Cd Length: 1153 Bit Score: 517.12 E-value: 1.72e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 1 MKSSSSQS----YDVFPNFRGEDVRHSLVSHLRKELDRKFINTFNDNRIERSRKITPELLLAIENSRISLVVFSKNYASS 76
Cdd:PLN03210 1 MASSSSSSrnwvYDVFPSFSGEDVRITFLSHFLKELDRKLIIAFKDNEIERSQSLDPELKQAIRDSRIAVVVFSKNYASS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 77 TWCLDELVKIQECYEKLDQMVIPIFYKVDPSHVRKQTGEFGMVFGETCKGRTENEKRKWMRALAEVAHLAGEDLRNWRSE 156
Cdd:PLN03210 81 SWCLNELLEIVRCKEELGQLVIPVFYGLDPSHVRKQTGDFGEAFEKTCQNKTEDEKIQWKQALTDVANILGYHSQNWPNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 157 AEMLENIAKDVSNKL-FPPSNNFSDFVGIEAHIEALISMLRFDSKKARMIGICGPSETGKTTIGRALYSRLKSDFH---- 231
Cdd:PLN03210 161 AKMIEEIANDVLGKLnLTPSNDFEDFVGIEDHIAKMSSLLHLESEEVRMVGIWGSSGIGKTTIARALFSRLSRQFQssvf 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 232 -HRAFVA-----YKRKIRSDYDQKLYWEEQFLSEILCQKDIKIEECGAVEQRLKHTKVLIVLDDVDDIELLKTLVGRIRW 305
Cdd:PLN03210 241 iDRAFISksmeiYSSANPDDYNMKLHLQRAFLSEILDKKDIKIYHLGAMEERLKHRKVLIFIDDLDDQDVLDALAGQTQW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 306 FGSESKIVVITQKRELLKAHNIAHVYEVGFPSEELAHQMFCRYAFGKNSPPHGFNELADEAAKIAGNRPKALKYVGSSFR 385
Cdd:PLN03210 321 FGSGSRIIVITKDKHFLRAHGIDHIYEVCLPSNELALEMFCRSAFKKNSPPDGFMELASEVALRAGNLPLGLNVLGSYLR 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063723127 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 |
3.84e-65 |
|
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: 214.15 E-value: 3.84e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 9 YDVFPNFRGEDVRHSLVSHLRKELDRKFINTFNDNR-IERSRKITPELLLAIENSRISLVVFSKNYASSTWCLDELVKIQ 87
Cdd:pfam01582 1 YDVFLSFRGSDTREWFVSHLLKELKQKGIKLFIDDRdLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSGWCLDELVKIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 88 ECYEKLDQMVIPIFYKVDPSHVRKQTGEFGMVFGETCKGRTENEKRKWMRALAEVAHLagEDLRNWRSEAEMLENIAKDV 167
Cdd:pfam01582 81 ECALDLGQKVIPIFYEVDPSDVRKQTGSFGKAFKKHKKVLTEEKVLKWRGALNEVANI--WHSKSVSDESKFWKKIAYDI 158
|
....
gi 1063723127 168 SNKL 171
Cdd:pfam01582 159 SNKL 162
|
|
| TIR |
smart00255 |
Toll - interleukin 1 - resistance; |
9-145 |
4.32e-45 |
|
Toll - interleukin 1 - resistance;
Pssm-ID: 214587 [Multi-domain] Cd Length: 140 Bit Score: 158.26 E-value: 4.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 9 YDVFPNFRG-EDVRHSLVSHLRKELDRKFINTFNDNRIERSRKITpELLLAIENSRISLVVFSKNYASSTWCLDELVKIQ 87
Cdd:smart00255 2 YDVFISYSGkEDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLE-EIDEAIEKSRIAIVVLSPNYAESEWCLDELVAAL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 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 |
2.91e-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: 90.34 E-value: 2.91e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063723127 537 EKEKIEYCEPHVYITPAIFSDGTRAPKYVESSRRVTQVHHAKTWWPENCEKVYENH 592
Cdd:pfam08381 1 EREWVEQDEPGVYITLVILPDGTKELKRVRFSRRRFSEKQAEVWWEENRDRVYEKY 56
|
|
| BRX |
pfam08381 |
Transcription factor regulating root and shoot growth via Pin3; The BREVIS RADIX (BRX) domain ... |
717-770 |
3.97e-19 |
|
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: 81.48 E-value: 3.97e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063723127 717 DEKNFEYCEQGVYITLGILSGGIIVLKHLEFSRRM--AQQAKVWWSENWIKVYQEH 770
Cdd:pfam08381 1 EREWVEQDEPGVYITLVILPDGTKELKRVRFSRRRfsEKQAEVWWEENRDRVYEKY 56
|
|
| BRX |
pfam08381 |
Transcription factor regulating root and shoot growth via Pin3; The BREVIS RADIX (BRX) domain ... |
433-485 |
2.28e-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: 73.77 E-value: 2.28e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063723127 433 KAEWI-HLALGVSILLNIRSDGTTILKHLSYNRSM--AQQAKIWWYENLERVCKKY 485
Cdd:pfam08381 1 EREWVeQDEPGVYITLVILPDGTKELKRVRFSRRRfsEKQAEVWWEENRDRVYEKY 56
|
|
| PLN03194 |
PLN03194 |
putative disease resistance protein; Provisional |
3-147 |
1.78e-11 |
|
putative disease resistance protein; Provisional
Pssm-ID: 215626 [Multi-domain] Cd Length: 187 Bit Score: 63.69 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 3 SSSSQSYDVFPNFRGEDVRHSLVSHLRKELDRKFINTFNDNR-IERSRKITPELLLAIENSRISLVVFSKNYASSTWCLD 81
Cdd:PLN03194 21 SSSAKPCDVFINHRGIDTKRTIATLLYDHLSRLNLRPFLDNKnMKPGDKLFDKINSAIRNCKVGVAVFSPRYCESYFCLH 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063723127 82 ELVKIQECYEKldqmVIPIFYKVDPSHVRkqtgefgMVFGETCkgrTENEKRKWMRALAEVAHLAG 147
Cdd:PLN03194 101 ELALIMESKKR----VIPIFCDVKPSQLR-------VVDNGTC---PDEEIRRFNWALEEAKYTVG 152
|
|
| NB-ARC |
pfam00931 |
NB-ARC domain; |
184-414 |
1.09e-07 |
|
NB-ARC domain;
Pssm-ID: 395745 [Multi-domain] Cd Length: 245 Bit Score: 53.54 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 184 IEAHIEALISMLrFDSKKARMIGICGPSETGKTTIGRALYSRLKSDFHH---RAFVAYKRKIRSDYDQKLYWEEQFLSEI 260
Cdd:pfam00931 1 REDMVEKVIGKL-SEKDEPGIVGIHGMGGVGKTTLAAQIFNDFDEVEGHfdsVAWVVVSKTFTISTLQQTILQNLGLSED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 261 LCQKDIKIEECGAVEQRLKHTKVLIVLDDVDDIELLKTLVGRIRWFGSESKIVVITQKRELLKAHNIAH-VYEVGFPSEE 339
Cdd:pfam00931 80 DWDNKEEGELARKIRRALLTKRFLLVLDDVWDEEDWDKIGIPLPDRENGCRVLLTTRSEEVAGRVGGPSdPHEVELLEPD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063723127 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 |
2.13e-06 |
|
TIR domain; This is a family of Toll-like receptors.
Pssm-ID: 463954 [Multi-domain] Cd Length: 118 Bit Score: 47.31 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 11 VFPNFRGEDvrHSLVSHLRKELDRKFINTFNDNR-IERSRKITPELLLAIENSRISLVVFSKNYASSTWCLDELVKIQEc 89
Cdd:pfam13676 1 VFISYAGED--RAWAEWLADALEAAGYRVWLDRWdIRPGDDWVEEIEEAIENSDRVLVVLSPNYLESPWCRAEWEAALA- 77
|
90
....*....|....*....
gi 1063723127 90 YEKLDQMVIPIFYKVDPSH 108
Cdd:pfam13676 78 DPEGRKRLIPVRLECDLEL 96
|
|
| AAA_18 |
pfam13238 |
AAA domain; |
205-251 |
4.05e-04 |
|
AAA domain;
Pssm-ID: 433052 [Multi-domain] Cd Length: 128 Bit Score: 40.87 E-value: 4.05e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1063723127 205 IGICGPSETGKTTIGRALYSRLKSDFHHRaFVAYKRKIRSDYDQKLY 251
Cdd:pfam13238 1 ILITGTPGVGKTTLAKELSKRLGFGDNVR-DLALENGLVLGDDPETR 46
|
|
| CDC6 |
COG1474 |
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair]; |
179-315 |
1.43e-03 |
|
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
Pssm-ID: 441083 [Multi-domain] Cd Length: 389 Bit Score: 41.76 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 179 SDFVGIEAHIEALISMLR--FDSKKARMIGICGPSETGKTTIGRALYSRLKSDFHHRAF---VAYK--RKIRSDYdqkly 251
Cdd:COG1474 26 DRLPHREEEIEELASALRpaLRGERPSNVLIYGPTGTGKTAVAKYVLEELEEEAEERGVdvrVVYVncRQASTRY----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 252 weeQFLSEILCQ--KDIKIEECG--------AVEQRLKHTK--VLIVLDDVDDI------ELLKTLVgRIRWFGSESKIV 313
Cdd:COG1474 101 ---RVLSRILEElgSGEDIPSTGlstdelfdRLYEALDERDgvLVVVLDEIDYLvddegdDLLYQLL-RANEELEGARVG 176
|
..
gi 1063723127 314 VI 315
Cdd:COG1474 177 VI 178
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
199-229 |
1.63e-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: 1.63e-03
10 20 30
....*....|....*....|....*....|.
gi 1063723127 199 SKKARMIGICGPSETGKTTIGRALYSRLKSD 229
Cdd:COG0572 4 SGKPRIIGIAGPSGSGKTTFARRLAEQLGAD 34
|
|
| COG4916 |
COG4916 |
Uncharacterized conserved protein [Function unknown]; |
9-219 |
2.00e-03 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443944 [Multi-domain] Cd Length: 236 Bit Score: 40.48 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 9 YDVFPNFRGEDvRHsLVSHLRKELDRKFINTFNDNRiERSRKITPELLLAIEN-----SRISLVVFSKNYASSTWCLDEL 83
Cdd:COG4916 1 YDVALSFAGED-RE-FVERVAEALKARGIKVFYDEN-EEAELWGKDLDEYLQDiyrseSRFVVVFLSKDYVEKKWTGLER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 84 VKIQECYEKLDQM-VIPIfyKVDPSHVrkqTGEFGMVFGETCKGRTEnekrkwmralAEVAHLAGEDLRNWRSEAEMlEN 162
Cdd:COG4916 78 RAALARAMQRKKEyILPI--RLDDTEI---PGILATIGYIDLRNRTP----------EEIADLILEKLAKGRPKPSR-AL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063723127 163 IAKDVSNKLFPPSNNFSDFVGIEAHIEALISMLRFDSKKARMIGICGPSETGKTTIG 219
Cdd:COG4916 142 SLAPTETVGSPARPNDAPGVFSTASAKTCVSGNLTGLLAVLDLEEVQGFLIGVRGDT 198
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
182-323 |
4.73e-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: 38.28 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 182 VGIEAHIEALISMLRFDSKKArmIGICGPSETGKTTIGRALYSRLKSDFHHraFVAYKrkiRSDYDQKLYWEEQFLSEIL 261
Cdd:cd00009 1 VGQEEAIEALREALELPPPKN--LLLYGPPGTGKTTLARAIANELFRPGAP--FLYLN---ASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 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 |
5.73e-03 |
|
Poxvirus A32 protein; The A32 protein is thought to be involved in viral DNA packaging.
Pssm-ID: 282513 Cd Length: 241 Bit Score: 39.35 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723127 194 MLRFDSKKA-----RMIgICGPSETGKTTIGRALYSRLKSDFHHRAFV------AYKRKIRSDYDQKLYWEEQfLSEILC 262
Cdd:pfam04665 1 EVRFDRNSLladpfRMA-LVGGSGSGKTTYLLSLFRTLVRKYKHIFLFtpvynsAYDGYIWPDHINKVTSNEE-LEYSLS 78
|
90 100 110
....*....|....*....|....*....|....
gi 1063723127 263 QKDIKIEECGAVEQRLKHT-KVLIVLDDVDDIEL 295
Cdd:pfam04665 79 RYKQKIENYAKSASNQKENfRFLLILDDLGDKQT 112
|
|
| PRK05541 |
PRK05541 |
adenylylsulfate kinase; Provisional |
199-232 |
6.35e-03 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 235498 Cd Length: 176 Bit Score: 38.50 E-value: 6.35e-03
10 20 30
....*....|....*....|....*....|....
gi 1063723127 199 SKKARMIGICGPSETGKTTIGRALYSRLKSDFHH 232
Cdd:PRK05541 4 KPNGYVIWITGLAGSGKTTIAKALYERLKLKYSN 37
|
|
| |
