RAD-like 6 [Arabidopsis thaliana]
SANT/Myb-like DNA-binding domain-containing protein( domain architecture ID 10073748)
SANT (SWI3, ADA2, N-CoR and TFIIIB)/Myb-like DNA-binding domain-containing protein binds DNA and may function as a transcription factor
List of domain hits
Name | Accession | Description | Interval | E-value | ||
SANT | cd00167 | 'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ... |
11-54 | 1.43e-06 | ||
'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: 1.43e-06
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Name | Accession | Description | Interval | E-value | ||
SANT | cd00167 | 'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ... |
11-54 | 1.43e-06 | ||
'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: 1.43e-06
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SANT | smart00717 | SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains; |
11-54 | 6.13e-06 | ||
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains; Pssm-ID: 197842 [Multi-domain] Cd Length: 49 Bit Score: 40.67 E-value: 6.13e-06
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Myb_DNA-binding | pfam00249 | Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ... |
11-54 | 2.17e-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: 36.33 E-value: 2.17e-04
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Name | Accession | Description | Interval | E-value | ||
SANT | cd00167 | 'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ... |
11-54 | 1.43e-06 | ||
'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: 1.43e-06
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SANT | smart00717 | SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains; |
11-54 | 6.13e-06 | ||
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains; Pssm-ID: 197842 [Multi-domain] Cd Length: 49 Bit Score: 40.67 E-value: 6.13e-06
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Myb_DNA-binding | pfam00249 | Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ... |
11-54 | 2.17e-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: 36.33 E-value: 2.17e-04
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BphC-JF8_C_like | cd09014 | C-terminal, catalytic domain of BphC_JF8, (2,3-dihydroxybiphenyl 1,2-dioxygenase); 2, ... |
4-67 | 3.60e-03 | ||
C-terminal, catalytic domain of BphC_JF8, (2,3-dihydroxybiphenyl 1,2-dioxygenase); 2,3-dihydroxybiphenyl 1,2-dioxygenase (BphC) catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, a key step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). BphC belongs to the type I extradiol dioxygenase family, which requires a metal ion in the active site in its catalytic mechanism. Polychlorinated biphenyl degrading bacteria demonstrate a multiplicity of BphCs. This subfamily of BphC is represented by the enzyme purified from the thermophilic biphenyl and naphthalene degrader, Bacillus sp. JF8. The members in this family of BphC enzymes may use either Mn(II) or Fe(II) as cofactors. The enzyme purified from Bacillus sp. JF8 is Mn(II)-dependent, however, the enzyme from Rhodococcus jostii RHAI has Fe(II) bound to it. BphC_JF8 is thermostable and its optimum activity is at 85 degrees C. The enzymes in this family have an internal duplication. This family represents the C-terminal repeat. Pssm-ID: 319956 Cd Length: 167 Bit Score: 35.43 E-value: 3.60e-03
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Blast search parameters | ||||
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