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Conserved domains on  [gi|665392642|ref|NP_001285492|]
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uncharacterized protein Dmel_CG11710, isoform C [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ASCH_ASC-1_like cd06554
ASC-1 homology domain, ASC-1-like subfamily. The ASCH domain, a small beta-barrel domain found ...
 367-478 2.65e-52

ASC-1 homology domain, ASC-1-like subfamily. The ASCH domain, a small beta-barrel domain found in all three kingdoms of life, resembles the RNA-binding PUA domain and may also interact with RNA. ASCH has been proposed to function as an RNA-binding domain during coactivation, RNA-processing and the regulation of prokaryotic translation. The domain has been named after the ASC-1 protein, the activating signal cointegrator 1 or thyroid hormone receptor interactor protein 4 (TRIP4). ASC-1 is conserved in many eukaryotes and has been suggested to participate in a protein complex that interacts with RNA. It has been shown that ASC-1 mediates the interaction between various transciption factors and the basal transcriptional machinery.


:

Pssm-ID: 119346  Cd Length: 113  Bit Score: 172.90  E-value: 2.65e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392642 367 QCLSMHQPWASLLVAGIKKHEGRVWYSEHRGRLWIASTSKEPHAEDIAQMEGFYKVLYGdPDIKFPSHYPTSSLLGCVHV 446
Cdd:cd06554    2 KALSIHQPWASLIVRGIKRIEGRSWATNYRGRLWIHASAKLPTKLDIEEVEEFYRILYK-LDIELPTGYPTGCLLGCVDV 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 665392642 447 DSCLPQEEYRELYPNGE-SESPYVFVCTKPEQL 478
Cdd:cd06554   81 VDCLTQEEYREQYPWGKsEESPYAWVLANPRPL 113
zf-C2HC5 pfam06221
Putative zinc finger motif, C2HC5-type; This zinc finger appears to be common in activating ...
 120-168 1.22e-13

Putative zinc finger motif, C2HC5-type; This zinc finger appears to be common in activating signal cointegrator 1/thyroid receptor interacting protein 4.


:

Pssm-ID: 428833  Cd Length: 54  Bit Score: 65.37  E-value: 1.22e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 665392642  120 RRHCDCQAGQHKLIN---NCLGCGRIVCEQEG-SGPCLSCGDPVRTPEEEQQL 168
Cdd:pfam06221   1 RRKCNCQARRHPLFEaapNCLNCGKIICAKEGlHGPCSFCGSPLLSPEERQEL 53
PRK14474 super family cl33002
F0F1 ATP synthase subunit B; Provisional
 160-287 3.08e-03

F0F1 ATP synthase subunit B; Provisional


The actual alignment was detected with superfamily member PRK14474:

Pssm-ID: 184696 [Multi-domain]  Cd Length: 250  Bit Score: 39.41  E-value: 3.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392642 160 RTPEEEQQLAKAAREKGGTKSAAKQGKKSTKELS-------TQALDKALAQRDRLLEydknsEKRttvidDELDyfQENS 232
Cdd:PRK14474  37 RQQRIANRWQDAEQRQQEAGQEAERYRQKQQSLEqqrasfmAQAQEAADEQRQHLLN-----EAR-----EDVA--TARD 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 665392642 233 VWLSDAEREKFEKLHREMEEVkhGSRMKRKIRV---DFAGRELpeeptiskeyEQQVI 287
Cdd:PRK14474 105 EWLEQLEREKQEFFKALQQQT--GQQMVKIIRAalaDLANATL----------EQQIV 150
 
Name Accession Description Interval E-value
ASCH_ASC-1_like cd06554
ASC-1 homology domain, ASC-1-like subfamily. The ASCH domain, a small beta-barrel domain found ...
 367-478 2.65e-52

ASC-1 homology domain, ASC-1-like subfamily. The ASCH domain, a small beta-barrel domain found in all three kingdoms of life, resembles the RNA-binding PUA domain and may also interact with RNA. ASCH has been proposed to function as an RNA-binding domain during coactivation, RNA-processing and the regulation of prokaryotic translation. The domain has been named after the ASC-1 protein, the activating signal cointegrator 1 or thyroid hormone receptor interactor protein 4 (TRIP4). ASC-1 is conserved in many eukaryotes and has been suggested to participate in a protein complex that interacts with RNA. It has been shown that ASC-1 mediates the interaction between various transciption factors and the basal transcriptional machinery.


Pssm-ID: 119346  Cd Length: 113  Bit Score: 172.90  E-value: 2.65e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392642 367 QCLSMHQPWASLLVAGIKKHEGRVWYSEHRGRLWIASTSKEPHAEDIAQMEGFYKVLYGdPDIKFPSHYPTSSLLGCVHV 446
Cdd:cd06554    2 KALSIHQPWASLIVRGIKRIEGRSWATNYRGRLWIHASAKLPTKLDIEEVEEFYRILYK-LDIELPTGYPTGCLLGCVDV 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 665392642 447 DSCLPQEEYRELYPNGE-SESPYVFVCTKPEQL 478
Cdd:cd06554   81 VDCLTQEEYREQYPWGKsEESPYAWVLANPRPL 113
zf-C2HC5 pfam06221
Putative zinc finger motif, C2HC5-type; This zinc finger appears to be common in activating ...
 120-168 1.22e-13

Putative zinc finger motif, C2HC5-type; This zinc finger appears to be common in activating signal cointegrator 1/thyroid receptor interacting protein 4.


Pssm-ID: 428833  Cd Length: 54  Bit Score: 65.37  E-value: 1.22e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 665392642  120 RRHCDCQAGQHKLIN---NCLGCGRIVCEQEG-SGPCLSCGDPVRTPEEEQQL 168
Cdd:pfam06221   1 RRKCNCQARRHPLFEaapNCLNCGKIICAKEGlHGPCSFCGSPLLSPEERQEL 53
ASCH smart01022
The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to ...
 369-421 5.16e-08

The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to function as an RNA-binding domain during coactivation, RNA-processing and possibly during prokaryotic translation regulation.


Pssm-ID: 214979  Cd Length: 99  Bit Score: 50.80  E-value: 5.16e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 665392642   369 LSMHQPWASLLVAGIKKHEGRVWYSEH--RGRLWIASTSKEPHAEDIAQMEGFYK 421
Cdd:smart01022   1 LSFKDELADLILSGKKTATIRLENEPLpkVGDLLIVLDGEGKPVCVIEVTSVEII 55
ASCH pfam04266
ASCH domain; The ASCH domain adopts a beta-barrel fold similar to the pfam01472 domain. It is ...
 369-407 9.26e-08

ASCH domain; The ASCH domain adopts a beta-barrel fold similar to the pfam01472 domain. It is thought to function as an RNA-binding domain during coactivation, RNA-processing and possibly during prokaryotic translation regulation.


Pssm-ID: 398105  Cd Length: 102  Bit Score: 50.07  E-value: 9.26e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 665392642  369 LSMHQPWASLLVAGIKKHEGRVWYSEHR--GRLWIASTSKE 407
Cdd:pfam04266   1 LSFGQEYADLILSGKKTAEIRVWDEPLPvvGDLLILLDSTG 41
PRK14474 PRK14474
F0F1 ATP synthase subunit B; Provisional
 160-287 3.08e-03

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184696 [Multi-domain]  Cd Length: 250  Bit Score: 39.41  E-value: 3.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392642 160 RTPEEEQQLAKAAREKGGTKSAAKQGKKSTKELS-------TQALDKALAQRDRLLEydknsEKRttvidDELDyfQENS 232
Cdd:PRK14474  37 RQQRIANRWQDAEQRQQEAGQEAERYRQKQQSLEqqrasfmAQAQEAADEQRQHLLN-----EAR-----EDVA--TARD 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 665392642 233 VWLSDAEREKFEKLHREMEEVkhGSRMKRKIRV---DFAGRELpeeptiskeyEQQVI 287
Cdd:PRK14474 105 EWLEQLEREKQEFFKALQQQT--GQQMVKIIRAalaDLANATL----------EQQIV 150
 
Name Accession Description Interval E-value
ASCH_ASC-1_like cd06554
ASC-1 homology domain, ASC-1-like subfamily. The ASCH domain, a small beta-barrel domain found ...
 367-478 2.65e-52

ASC-1 homology domain, ASC-1-like subfamily. The ASCH domain, a small beta-barrel domain found in all three kingdoms of life, resembles the RNA-binding PUA domain and may also interact with RNA. ASCH has been proposed to function as an RNA-binding domain during coactivation, RNA-processing and the regulation of prokaryotic translation. The domain has been named after the ASC-1 protein, the activating signal cointegrator 1 or thyroid hormone receptor interactor protein 4 (TRIP4). ASC-1 is conserved in many eukaryotes and has been suggested to participate in a protein complex that interacts with RNA. It has been shown that ASC-1 mediates the interaction between various transciption factors and the basal transcriptional machinery.


Pssm-ID: 119346  Cd Length: 113  Bit Score: 172.90  E-value: 2.65e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392642 367 QCLSMHQPWASLLVAGIKKHEGRVWYSEHRGRLWIASTSKEPHAEDIAQMEGFYKVLYGdPDIKFPSHYPTSSLLGCVHV 446
Cdd:cd06554    2 KALSIHQPWASLIVRGIKRIEGRSWATNYRGRLWIHASAKLPTKLDIEEVEEFYRILYK-LDIELPTGYPTGCLLGCVDV 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 665392642 447 DSCLPQEEYRELYPNGE-SESPYVFVCTKPEQL 478
Cdd:cd06554   81 VDCLTQEEYREQYPWGKsEESPYAWVLANPRPL 113
zf-C2HC5 pfam06221
Putative zinc finger motif, C2HC5-type; This zinc finger appears to be common in activating ...
 120-168 1.22e-13

Putative zinc finger motif, C2HC5-type; This zinc finger appears to be common in activating signal cointegrator 1/thyroid receptor interacting protein 4.


Pssm-ID: 428833  Cd Length: 54  Bit Score: 65.37  E-value: 1.22e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 665392642  120 RRHCDCQAGQHKLIN---NCLGCGRIVCEQEG-SGPCLSCGDPVRTPEEEQQL 168
Cdd:pfam06221   1 RRKCNCQARRHPLFEaapNCLNCGKIICAKEGlHGPCSFCGSPLLSPEERQEL 53
ASCH smart01022
The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to ...
 369-421 5.16e-08

The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to function as an RNA-binding domain during coactivation, RNA-processing and possibly during prokaryotic translation regulation.


Pssm-ID: 214979  Cd Length: 99  Bit Score: 50.80  E-value: 5.16e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 665392642   369 LSMHQPWASLLVAGIKKHEGRVWYSEH--RGRLWIASTSKEPHAEDIAQMEGFYK 421
Cdd:smart01022   1 LSFKDELADLILSGKKTATIRLENEPLpkVGDLLIVLDGEGKPVCVIEVTSVEII 55
ASCH pfam04266
ASCH domain; The ASCH domain adopts a beta-barrel fold similar to the pfam01472 domain. It is ...
 369-407 9.26e-08

ASCH domain; The ASCH domain adopts a beta-barrel fold similar to the pfam01472 domain. It is thought to function as an RNA-binding domain during coactivation, RNA-processing and possibly during prokaryotic translation regulation.


Pssm-ID: 398105  Cd Length: 102  Bit Score: 50.07  E-value: 9.26e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 665392642  369 LSMHQPWASLLVAGIKKHEGRVWYSEHR--GRLWIASTSKE 407
Cdd:pfam04266   1 LSFGQEYADLILSGKKTAEIRVWDEPLPvvGDLLILLDSTG 41
PRK14474 PRK14474
F0F1 ATP synthase subunit B; Provisional
 160-287 3.08e-03

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184696 [Multi-domain]  Cd Length: 250  Bit Score: 39.41  E-value: 3.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392642 160 RTPEEEQQLAKAAREKGGTKSAAKQGKKSTKELS-------TQALDKALAQRDRLLEydknsEKRttvidDELDyfQENS 232
Cdd:PRK14474  37 RQQRIANRWQDAEQRQQEAGQEAERYRQKQQSLEqqrasfmAQAQEAADEQRQHLLN-----EAR-----EDVA--TARD 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 665392642 233 VWLSDAEREKFEKLHREMEEVkhGSRMKRKIRV---DFAGRELpeeptiskeyEQQVI 287
Cdd:PRK14474 105 EWLEQLEREKQEFFKALQQQT--GQQMVKIIRAalaDLANATL----------EQQIV 150
 
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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