cell division related protein-like [Arabidopsis thaliana]
J and SANT/Myb-like DNA-binding domain-containing protein( domain architecture ID 13424958)
J and SANT (SWI3, ADA2, N-CoR and TFIIIB)/Myb-like DNA-binding domain-containing protein may play crucial roles in protein translation, folding, unfolding, translocation, and degradation and may bind DNA and function as a transcription factor
List of domain hits
Name | Accession | Description | Interval | E-value | ||||||
ZUO1 super family | cl34965 | Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ... |
98-422 | 7.08e-43 | ||||||
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones]; The actual alignment was detected with superfamily member COG5269: Pssm-ID: 227594 [Multi-domain] Cd Length: 379 Bit Score: 159.04 E-value: 7.08e-43
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SANT | cd00167 | 'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ... |
607-653 | 1.80e-05 | ||||||
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA. : Pssm-ID: 238096 [Multi-domain] Cd Length: 45 Bit Score: 42.18 E-value: 1.80e-05
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SANT | cd00167 | 'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ... |
476-516 | 2.75e-03 | ||||||
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA. : Pssm-ID: 238096 [Multi-domain] Cd Length: 45 Bit Score: 36.01 E-value: 2.75e-03
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Name | Accession | Description | Interval | E-value | ||||||
ZUO1 | COG5269 | Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ... |
98-422 | 7.08e-43 | ||||||
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227594 [Multi-domain] Cd Length: 379 Bit Score: 159.04 E-value: 7.08e-43
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DnaJ | pfam00226 | DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
100-179 | 4.06e-17 | ||||||
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature. Pssm-ID: 395170 [Multi-domain] Cd Length: 63 Bit Score: 75.59 E-value: 4.06e-17
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DnaJ | cd06257 | DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
100-171 | 1.12e-12 | ||||||
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification. Pssm-ID: 99751 [Multi-domain] Cd Length: 55 Bit Score: 62.95 E-value: 1.12e-12
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DnaJ | smart00271 | DnaJ molecular chaperone homology domain; |
100-174 | 9.56e-12 | ||||||
DnaJ molecular chaperone homology domain; Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 60.33 E-value: 9.56e-12
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PRK10767 | PRK10767 | chaperone protein DnaJ; Provisional |
100-179 | 1.16e-11 | ||||||
chaperone protein DnaJ; Provisional Pssm-ID: 236757 [Multi-domain] Cd Length: 371 Bit Score: 66.71 E-value: 1.16e-11
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SANT | cd00167 | 'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ... |
607-653 | 1.80e-05 | ||||||
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA. Pssm-ID: 238096 [Multi-domain] Cd Length: 45 Bit Score: 42.18 E-value: 1.80e-05
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SANT | smart00717 | SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains; |
607-653 | 1.24e-04 | ||||||
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains; Pssm-ID: 197842 [Multi-domain] Cd Length: 49 Bit Score: 39.90 E-value: 1.24e-04
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Myb_DNA-binding | pfam00249 | Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ... |
607-649 | 5.49e-04 | ||||||
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, as well as the SANT domain family. Pssm-ID: 459731 [Multi-domain] Cd Length: 46 Bit Score: 37.87 E-value: 5.49e-04
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SANT | cd00167 | 'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ... |
476-516 | 2.75e-03 | ||||||
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA. Pssm-ID: 238096 [Multi-domain] Cd Length: 45 Bit Score: 36.01 E-value: 2.75e-03
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Name | Accession | Description | Interval | E-value | ||||||
ZUO1 | COG5269 | Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ... |
98-422 | 7.08e-43 | ||||||
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227594 [Multi-domain] Cd Length: 379 Bit Score: 159.04 E-value: 7.08e-43
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DnaJ | pfam00226 | DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
100-179 | 4.06e-17 | ||||||
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature. Pssm-ID: 395170 [Multi-domain] Cd Length: 63 Bit Score: 75.59 E-value: 4.06e-17
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DnaJ | COG0484 | DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ... |
100-179 | 7.76e-14 | ||||||
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440252 [Multi-domain] Cd Length: 139 Bit Score: 68.96 E-value: 7.76e-14
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DnaJ | cd06257 | DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
100-171 | 1.12e-12 | ||||||
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification. Pssm-ID: 99751 [Multi-domain] Cd Length: 55 Bit Score: 62.95 E-value: 1.12e-12
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DnaJ | smart00271 | DnaJ molecular chaperone homology domain; |
100-174 | 9.56e-12 | ||||||
DnaJ molecular chaperone homology domain; Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 60.33 E-value: 9.56e-12
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PRK10767 | PRK10767 | chaperone protein DnaJ; Provisional |
100-179 | 1.16e-11 | ||||||
chaperone protein DnaJ; Provisional Pssm-ID: 236757 [Multi-domain] Cd Length: 371 Bit Score: 66.71 E-value: 1.16e-11
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CbpA | COG2214 | Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription]; |
100-179 | 9.19e-11 | ||||||
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription]; Pssm-ID: 441816 [Multi-domain] Cd Length: 91 Bit Score: 58.58 E-value: 9.19e-11
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PRK14281 | PRK14281 | chaperone protein DnaJ; Provisional |
97-179 | 2.02e-10 | ||||||
chaperone protein DnaJ; Provisional Pssm-ID: 237657 [Multi-domain] Cd Length: 397 Bit Score: 63.29 E-value: 2.02e-10
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PRK14290 | PRK14290 | chaperone protein DnaJ; Provisional |
100-185 | 6.01e-10 | ||||||
chaperone protein DnaJ; Provisional Pssm-ID: 172778 [Multi-domain] Cd Length: 365 Bit Score: 61.49 E-value: 6.01e-10
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PRK14278 | PRK14278 | chaperone protein DnaJ; Provisional |
100-179 | 1.98e-09 | ||||||
chaperone protein DnaJ; Provisional Pssm-ID: 237654 [Multi-domain] Cd Length: 378 Bit Score: 60.07 E-value: 1.98e-09
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PRK14294 | PRK14294 | chaperone protein DnaJ; Provisional |
100-179 | 4.83e-09 | ||||||
chaperone protein DnaJ; Provisional Pssm-ID: 237664 [Multi-domain] Cd Length: 366 Bit Score: 58.62 E-value: 4.83e-09
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PRK14282 | PRK14282 | chaperone protein DnaJ; Provisional |
100-208 | 6.90e-09 | ||||||
chaperone protein DnaJ; Provisional Pssm-ID: 184603 [Multi-domain] Cd Length: 369 Bit Score: 58.27 E-value: 6.90e-09
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PRK14291 | PRK14291 | chaperone protein DnaJ; Provisional |
98-233 | 7.45e-09 | ||||||
chaperone protein DnaJ; Provisional Pssm-ID: 237661 [Multi-domain] Cd Length: 382 Bit Score: 58.24 E-value: 7.45e-09
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PRK14297 | PRK14297 | molecular chaperone DnaJ; |
98-186 | 1.07e-08 | ||||||
molecular chaperone DnaJ; Pssm-ID: 184611 [Multi-domain] Cd Length: 380 Bit Score: 57.49 E-value: 1.07e-08
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PRK14298 | PRK14298 | chaperone protein DnaJ; Provisional |
100-179 | 2.05e-08 | ||||||
chaperone protein DnaJ; Provisional Pssm-ID: 184612 [Multi-domain] Cd Length: 377 Bit Score: 56.78 E-value: 2.05e-08
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PRK14284 | PRK14284 | chaperone protein DnaJ; Provisional |
100-179 | 2.97e-08 | ||||||
chaperone protein DnaJ; Provisional Pssm-ID: 237658 [Multi-domain] Cd Length: 391 Bit Score: 56.39 E-value: 2.97e-08
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PRK14299 | PRK14299 | chaperone protein DnaJ; Provisional |
100-180 | 3.60e-08 | ||||||
chaperone protein DnaJ; Provisional Pssm-ID: 237667 [Multi-domain] Cd Length: 291 Bit Score: 55.33 E-value: 3.60e-08
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PRK14289 | PRK14289 | molecular chaperone DnaJ; |
98-179 | 5.36e-08 | ||||||
molecular chaperone DnaJ; Pssm-ID: 237660 [Multi-domain] Cd Length: 386 Bit Score: 55.61 E-value: 5.36e-08
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PRK14277 | PRK14277 | chaperone protein DnaJ; Provisional |
100-179 | 5.92e-08 | ||||||
chaperone protein DnaJ; Provisional Pssm-ID: 184599 [Multi-domain] Cd Length: 386 Bit Score: 55.19 E-value: 5.92e-08
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PRK14295 | PRK14295 | molecular chaperone DnaJ; |
97-179 | 9.54e-08 | ||||||
molecular chaperone DnaJ; Pssm-ID: 237665 [Multi-domain] Cd Length: 389 Bit Score: 54.85 E-value: 9.54e-08
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PRK14285 | PRK14285 | chaperone protein DnaJ; Provisional |
97-179 | 1.28e-07 | ||||||
chaperone protein DnaJ; Provisional Pssm-ID: 172773 [Multi-domain] Cd Length: 365 Bit Score: 54.23 E-value: 1.28e-07
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PRK14276 | PRK14276 | chaperone protein DnaJ; Provisional |
98-179 | 1.54e-07 | ||||||
chaperone protein DnaJ; Provisional Pssm-ID: 237653 [Multi-domain] Cd Length: 380 Bit Score: 53.94 E-value: 1.54e-07
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PRK14280 | PRK14280 | molecular chaperone DnaJ; |
100-179 | 2.56e-07 | ||||||
molecular chaperone DnaJ; Pssm-ID: 237656 [Multi-domain] Cd Length: 376 Bit Score: 53.19 E-value: 2.56e-07
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PRK14286 | PRK14286 | chaperone protein DnaJ; Provisional |
101-179 | 2.64e-07 | ||||||
chaperone protein DnaJ; Provisional Pssm-ID: 172774 [Multi-domain] Cd Length: 372 Bit Score: 53.07 E-value: 2.64e-07
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PRK14301 | PRK14301 | chaperone protein DnaJ; Provisional |
98-179 | 2.81e-07 | ||||||
chaperone protein DnaJ; Provisional Pssm-ID: 237668 [Multi-domain] Cd Length: 373 Bit Score: 53.21 E-value: 2.81e-07
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PTZ00037 | PTZ00037 | DnaJ_C chaperone protein; Provisional |
109-201 | 3.90e-07 | ||||||
DnaJ_C chaperone protein; Provisional Pssm-ID: 240236 [Multi-domain] Cd Length: 421 Bit Score: 52.90 E-value: 3.90e-07
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PRK14292 | PRK14292 | chaperone protein DnaJ; Provisional |
100-179 | 5.13e-06 | ||||||
chaperone protein DnaJ; Provisional Pssm-ID: 237662 [Multi-domain] Cd Length: 371 Bit Score: 49.12 E-value: 5.13e-06
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PRK10266 | PRK10266 | curved DNA-binding protein; |
100-179 | 1.19e-05 | ||||||
curved DNA-binding protein; Pssm-ID: 182347 [Multi-domain] Cd Length: 306 Bit Score: 47.89 E-value: 1.19e-05
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PRK14283 | PRK14283 | chaperone protein DnaJ; Provisional |
98-179 | 1.72e-05 | ||||||
chaperone protein DnaJ; Provisional Pssm-ID: 184604 [Multi-domain] Cd Length: 378 Bit Score: 47.51 E-value: 1.72e-05
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SANT | cd00167 | 'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ... |
607-653 | 1.80e-05 | ||||||
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA. Pssm-ID: 238096 [Multi-domain] Cd Length: 45 Bit Score: 42.18 E-value: 1.80e-05
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SANT | smart00717 | SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains; |
607-653 | 1.24e-04 | ||||||
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains; Pssm-ID: 197842 [Multi-domain] Cd Length: 49 Bit Score: 39.90 E-value: 1.24e-04
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PRK14288 | PRK14288 | molecular chaperone DnaJ; |
114-179 | 1.70e-04 | ||||||
molecular chaperone DnaJ; Pssm-ID: 172776 [Multi-domain] Cd Length: 369 Bit Score: 44.29 E-value: 1.70e-04
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DjlA | COG1076 | DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones]; |
100-171 | 2.74e-04 | ||||||
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440694 [Multi-domain] Cd Length: 75 Bit Score: 39.78 E-value: 2.74e-04
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PRK14293 | PRK14293 | molecular chaperone DnaJ; |
100-179 | 4.69e-04 | ||||||
molecular chaperone DnaJ; Pssm-ID: 237663 [Multi-domain] Cd Length: 374 Bit Score: 43.05 E-value: 4.69e-04
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Myb_DNA-binding | pfam00249 | Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ... |
607-649 | 5.49e-04 | ||||||
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, as well as the SANT domain family. Pssm-ID: 459731 [Multi-domain] Cd Length: 46 Bit Score: 37.87 E-value: 5.49e-04
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PRK14287 | PRK14287 | chaperone protein DnaJ; Provisional |
98-179 | 8.00e-04 | ||||||
chaperone protein DnaJ; Provisional Pssm-ID: 237659 [Multi-domain] Cd Length: 371 Bit Score: 42.30 E-value: 8.00e-04
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PRK14296 | PRK14296 | chaperone protein DnaJ; Provisional |
98-179 | 9.14e-04 | ||||||
chaperone protein DnaJ; Provisional Pssm-ID: 237666 [Multi-domain] Cd Length: 372 Bit Score: 42.24 E-value: 9.14e-04
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SANT | cd00167 | 'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ... |
476-516 | 2.75e-03 | ||||||
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA. Pssm-ID: 238096 [Multi-domain] Cd Length: 45 Bit Score: 36.01 E-value: 2.75e-03
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PRK14300 | PRK14300 | chaperone protein DnaJ; Provisional |
97-179 | 4.11e-03 | ||||||
chaperone protein DnaJ; Provisional Pssm-ID: 172788 [Multi-domain] Cd Length: 372 Bit Score: 40.00 E-value: 4.11e-03
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Blast search parameters | ||||
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