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Conserved domains on  [gi|240254093|ref|NP_173188|]
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B-block binding subunit of TFIIIC [Arabidopsis thaliana]

Protein Classification

B-block_TFIIIC and Tau138_eWH domain-containing protein( domain architecture ID 12050989)

B-block_TFIIIC and Tau138_eWH domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
B-block_TFIIIC pfam04182
B-block binding subunit of TFIIIC; Yeast transcription factor IIIC (TFIIIC) is a multi-subunit ...
 105-189 5.82e-20

B-block binding subunit of TFIIIC; Yeast transcription factor IIIC (TFIIIC) is a multi-subunit protein complex that interacts with two control elements of class III promoters called the A and B blocks. This family represents the subunit within TFIIIC involved in B-block binding.


:

Pssm-ID: 367858  Cd Length: 75  Bit Score: 85.38  E-value: 5.82e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254093   105 SAIQRRVLERLAVARANGVAQNLLAKEFGIEGRNFFYIVKHLESRGLVVKQPAIvrtkevdgegDSKTTSCISTNMIYLS 184
Cdd:pfam04182    1 GALQFCLLEEIARSRYNGITQSDLAKLTGQDPRSLHYRLKKLEKKGLIVKQQII----------QSNTGKSIHTSLLVLP 70


                   ....*
gi 240254093   185 RYAKP 189
Cdd:pfam04182   71 RFAID 75
Tau138_eWH cd16169
extended winged-helix domain of tau138 and related proteins; Tau138 is one of three subunits ...
 537-618 1.26e-16

extended winged-helix domain of tau138 and related proteins; Tau138 is one of three subunits of the tauB subcomplex of yeast transcription factor IIIC. This extended winged-helix domain of tau138 appears to interact with the TPR (tetratricopeptide repeat) array of tauA subunit tau131, and may therefore play a role in linking tauA, tauB, and TFIIIB to regulate the formation of the RNA polymerase III pre-initiation complex.


:

Pssm-ID: 320085  Cd Length: 97  Bit Score: 76.85  E-value: 1.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254093  537 NEEKFVVRAElHKWLLSLEKDRSS--KVDRKTIDRILNRLQEEGLCNCMNISVPNVtNCGRNRSSVVVFHPSVQSLTRDI 614
Cdd:cd16169    16 KELGGVVNLE-KKFLEEHEKLLGSltRMDKKTLKRDLNKLEEEGKLKVITTSVPAV-GDGRSRTVLYLPDPSVEPLDPLL 93


                  ....
gi 240254093  615 VGEI 618
Cdd:cd16169    94 LSLI 97
 
Name Accession Description Interval E-value
B-block_TFIIIC pfam04182
B-block binding subunit of TFIIIC; Yeast transcription factor IIIC (TFIIIC) is a multi-subunit ...
 105-189 5.82e-20

B-block binding subunit of TFIIIC; Yeast transcription factor IIIC (TFIIIC) is a multi-subunit protein complex that interacts with two control elements of class III promoters called the A and B blocks. This family represents the subunit within TFIIIC involved in B-block binding.


Pssm-ID: 367858  Cd Length: 75  Bit Score: 85.38  E-value: 5.82e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254093   105 SAIQRRVLERLAVARANGVAQNLLAKEFGIEGRNFFYIVKHLESRGLVVKQPAIvrtkevdgegDSKTTSCISTNMIYLS 184
Cdd:pfam04182    1 GALQFCLLEEIARSRYNGITQSDLAKLTGQDPRSLHYRLKKLEKKGLIVKQQII----------QSNTGKSIHTSLLVLP 70


                   ....*
gi 240254093   185 RYAKP 189
Cdd:pfam04182   71 RFAID 75
Tau138_eWH cd16169
extended winged-helix domain of tau138 and related proteins; Tau138 is one of three subunits ...
 537-618 1.26e-16

extended winged-helix domain of tau138 and related proteins; Tau138 is one of three subunits of the tauB subcomplex of yeast transcription factor IIIC. This extended winged-helix domain of tau138 appears to interact with the TPR (tetratricopeptide repeat) array of tauA subunit tau131, and may therefore play a role in linking tauA, tauB, and TFIIIB to regulate the formation of the RNA polymerase III pre-initiation complex.


Pssm-ID: 320085  Cd Length: 97  Bit Score: 76.85  E-value: 1.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254093  537 NEEKFVVRAElHKWLLSLEKDRSS--KVDRKTIDRILNRLQEEGLCNCMNISVPNVtNCGRNRSSVVVFHPSVQSLTRDI 614
Cdd:cd16169    16 KELGGVVNLE-KKFLEEHEKLLGSltRMDKKTLKRDLNKLEEEGKLKVITTSVPAV-GDGRSRTVLYLPDPSVEPLDPLL 93


                  ....
gi 240254093  615 VGEI 618
Cdd:cd16169    94 LSLI 97
 
Name Accession Description Interval E-value
B-block_TFIIIC pfam04182
B-block binding subunit of TFIIIC; Yeast transcription factor IIIC (TFIIIC) is a multi-subunit ...
 105-189 5.82e-20

B-block binding subunit of TFIIIC; Yeast transcription factor IIIC (TFIIIC) is a multi-subunit protein complex that interacts with two control elements of class III promoters called the A and B blocks. This family represents the subunit within TFIIIC involved in B-block binding.


Pssm-ID: 367858  Cd Length: 75  Bit Score: 85.38  E-value: 5.82e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254093   105 SAIQRRVLERLAVARANGVAQNLLAKEFGIEGRNFFYIVKHLESRGLVVKQPAIvrtkevdgegDSKTTSCISTNMIYLS 184
Cdd:pfam04182    1 GALQFCLLEEIARSRYNGITQSDLAKLTGQDPRSLHYRLKKLEKKGLIVKQQII----------QSNTGKSIHTSLLVLP 70


                   ....*
gi 240254093   185 RYAKP 189
Cdd:pfam04182   71 RFAID 75
Tau138_eWH cd16169
extended winged-helix domain of tau138 and related proteins; Tau138 is one of three subunits ...
 537-618 1.26e-16

extended winged-helix domain of tau138 and related proteins; Tau138 is one of three subunits of the tauB subcomplex of yeast transcription factor IIIC. This extended winged-helix domain of tau138 appears to interact with the TPR (tetratricopeptide repeat) array of tauA subunit tau131, and may therefore play a role in linking tauA, tauB, and TFIIIB to regulate the formation of the RNA polymerase III pre-initiation complex.


Pssm-ID: 320085  Cd Length: 97  Bit Score: 76.85  E-value: 1.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254093  537 NEEKFVVRAElHKWLLSLEKDRSS--KVDRKTIDRILNRLQEEGLCNCMNISVPNVtNCGRNRSSVVVFHPSVQSLTRDI 614
Cdd:cd16169    16 KELGGVVNLE-KKFLEEHEKLLGSltRMDKKTLKRDLNKLEEEGKLKVITTSVPAV-GDGRSRTVLYLPDPSVEPLDPLL 93


                  ....
gi 240254093  615 VGEI 618
Cdd:cd16169    94 LSLI 97
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 104-156 3.09e-04

MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a non-specific resistance system. The expression of the mar operon is controlled by a repressor, MarR. A large number of compounds induce transcription of the mar operon. This is thought to be due to the compound binding to MarR, and the resulting complex stops MarR binding to the DNA. With the MarR repression lost, transcription of the operon proceeds. The structure of MarR is known and shows MarR as a dimer with each subunit containing a winged-helix DNA binding motif.


Pssm-ID: 432797 [Multi-domain]  Cd Length: 60  Bit Score: 40.26  E-value: 3.09e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 240254093   104 ISAIQRRVLerLAVARANGVAQNLLAKEFGIEGRNFFYIVKHLESRGLVVKQP 156
Cdd:pfam12802    3 LTPAQFRVL--LALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVEREP 53
 
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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