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Conserved domains on  [gi|1189398126|ref|NP_001338133|]
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R3H domain-containing protein 2 isoform 4 [Homo sapiens]

Protein Classification

R3H domain-containing protein( domain architecture ID 11552619)

R3H domain-containing protein with SUZ and Med15 domains, may bind ssDNA or ssRNA in a sequence-specific manner; similar to Mus musculus R3H domain-containing protein 2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
R3H_encore_like cd02642
R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the ...
 168-229 1.65e-26

R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the germline exit after four mitotic divisions, by facilitating SCF-ubiquitin-proteasome-dependent proteolysis. Maize DBF1-interactor protein 1 (DIP1) containing an R3H domain is a potential regulator of DBF1 activity in stress responses. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


:

Pssm-ID: 100071  Cd Length: 63  Bit Score: 103.07  E-value: 1.65e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189398126  168 DRMMLLKLEQEILEFINDNNNQFKKFPQMTSYHRMLLHRVAAYFGMDHNVDQTG-KAVIINKT 229
Cdd:cd02642      1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
SUZ pfam12752
SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched ...
 250-303 4.33e-12

SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched in positively charged amino acids. It was first characterized in the C.elegans protein Szy-20 where it has been shown to bind RNA and allow their localization to the centrosome. Warning- the domain has a compositionally biased character.


:

Pssm-ID: 463689 [Multi-domain]  Cd Length: 56  Bit Score: 61.95  E-value: 4.33e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1189398126  250 EFQQRFILKRDDASMD--RDDNQIRVPLQDGRRSKSIEEREEEYQRVRERIFARET 303
Cdd:pfam12752    1 PPPKMKILRRPSSGSSssSSAGSSGASSSSGSDSKTLEEREAEYAEARARIFGSSE 56
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 466-774 2.13e-09

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


The actual alignment was detected with superfamily member pfam09606:

Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 61.56  E-value: 2.13e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398126  466 QPVPALQPSPQPVQFSPSSCPQVLLPVSPPQQYNMADDLSNPF--GQMSLSRQGSTEAADPSAALFQTPLISQHPQQTSF 543
Cdd:pfam09606  141 SQMSRVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGqaGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMG 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398126  544 IMASTGQPLPTSNYSTSSHAPPTQQVLPPQGYMQppQQIQVSYYPPGQYPNSNQQYRPLSHPVAY--SPQRGQQLPQPSQ 621
Cdd:pfam09606  221 QQAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQ--SQLGMGINQMQQMPQGVGGGAGQGGPGQPmgPPGQQPGAMPNVM 298

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398126  622 QPGLQPMMPNQQQAAYQGMIGVQQPQNQGLLSSQRSSMGGQMQGLVVQYTPLPSYQVPVGSDSQNVVQP--PFQQPMLVP 699
Cdd:pfam09606  299 SIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGANPMQRgqPGMMSSPSP 378

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398126  700 VS----QSVQG--GLPAAGVPVYYSMIPPAQQNGTSPSVGFLQPPGSEQYQMPQSPSPCSPPQMPQQYSGVSPSG-PGVV 772
Cdd:pfam09606  379 VPgqqvRQVTPnqFMRQSPQPSVPSPQGPGSQPPQSHPGGMIPSPALIPSPSPQMSQQPAQQRTIGQDSPGGSLNtPGQS 458


                   ..
gi 1189398126  773 VM 774
Cdd:pfam09606  459 AV 460
 
Name Accession Description Interval E-value
R3H_encore_like cd02642
R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the ...
 168-229 1.65e-26

R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the germline exit after four mitotic divisions, by facilitating SCF-ubiquitin-proteasome-dependent proteolysis. Maize DBF1-interactor protein 1 (DIP1) containing an R3H domain is a potential regulator of DBF1 activity in stress responses. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100071  Cd Length: 63  Bit Score: 103.07  E-value: 1.65e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189398126  168 DRMMLLKLEQEILEFINDNNNQFKKFPQMTSYHRMLLHRVAAYFGMDHNVDQTG-KAVIINKT 229
Cdd:cd02642      1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
152-229 6.53e-14

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 67.71  E-value: 6.53e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398126   152 IDLHEFLVNTLKKNPRDRMMLLKLEQEILEFINdNNNQFKKFPQMTSYHRMLLHRVAAYFGMDHNVDQTGKA--VIINKT 229
Cdd:smart00393    1 ADFLPVTLDALSYRPRRREELIELELEIARFVK-STKESVELPPMNSYERKIVHELAEKYGLESESFGEGPKrrVVISKK 79
SUZ pfam12752
SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched ...
 250-303 4.33e-12

SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched in positively charged amino acids. It was first characterized in the C.elegans protein Szy-20 where it has been shown to bind RNA and allow their localization to the centrosome. Warning- the domain has a compositionally biased character.


Pssm-ID: 463689 [Multi-domain]  Cd Length: 56  Bit Score: 61.95  E-value: 4.33e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1189398126  250 EFQQRFILKRDDASMD--RDDNQIRVPLQDGRRSKSIEEREEEYQRVRERIFARET 303
Cdd:pfam12752    1 PPPKMKILRRPSSGSSssSSAGSSGASSSSGSDSKTLEEREAEYAEARARIFGSSE 56
R3H pfam01424
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ...
 170-228 2.81e-10

R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA.


Pssm-ID: 460206  Cd Length: 60  Bit Score: 56.73  E-value: 2.81e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189398126  170 MMLLKLEQEILEFINDNNNQFKkFPQMTSYHRMLLHRVAAYFGMDHNV--DQTGKAVIINK 228
Cdd:pfam01424    1 EFLEQLAEKLAEFVKDTGKSLE-LPPMSSYERRIIHELAQKYGLESESegEEPNRRVVVYK 60
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 466-774 2.13e-09

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 61.56  E-value: 2.13e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398126  466 QPVPALQPSPQPVQFSPSSCPQVLLPVSPPQQYNMADDLSNPF--GQMSLSRQGSTEAADPSAALFQTPLISQHPQQTSF 543
Cdd:pfam09606  141 SQMSRVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGqaGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMG 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398126  544 IMASTGQPLPTSNYSTSSHAPPTQQVLPPQGYMQppQQIQVSYYPPGQYPNSNQQYRPLSHPVAY--SPQRGQQLPQPSQ 621
Cdd:pfam09606  221 QQAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQ--SQLGMGINQMQQMPQGVGGGAGQGGPGQPmgPPGQQPGAMPNVM 298

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398126  622 QPGLQPMMPNQQQAAYQGMIGVQQPQNQGLLSSQRSSMGGQMQGLVVQYTPLPSYQVPVGSDSQNVVQP--PFQQPMLVP 699
Cdd:pfam09606  299 SIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGANPMQRgqPGMMSSPSP 378

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398126  700 VS----QSVQG--GLPAAGVPVYYSMIPPAQQNGTSPSVGFLQPPGSEQYQMPQSPSPCSPPQMPQQYSGVSPSG-PGVV 772
Cdd:pfam09606  379 VPgqqvRQVTPnqFMRQSPQPSVPSPQGPGSQPPQSHPGGMIPSPALIPSPSPQMSQQPAQQRTIGQDSPGGSLNtPGQS 458


                   ..
gi 1189398126  773 VM 774
Cdd:pfam09606  459 AV 460
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 464-611 1.33e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 42.76  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398126  464 ISQPVPALQPSPQPVQFSPSSCPQVLLPVSPPQQYNMADDLSNPFGQMSLSRQGSTEAADPSAAlfQTPLISQHPQQTSF 543
Cdd:PRK10263   353 PAQPTVAWQPVPGPQTGEPVIAPAPEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPA--QQPYYAPAPEQPAQ 430

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189398126  544 IMASTGQPlPTSNYSTSSHAPPTQQVLPPQGYMQPPQQIQVSYYPPGQYpnsnQQYRPLSHPVAYSPQ 611
Cdd:PRK10263   431 QPYYAPAP-EQPVAGNAWQAEEQQSTFAPQSTYQTEQTYQQPAAQEPLY----QQPQPVEQQPVVEPE 493
 
Name Accession Description Interval E-value
R3H_encore_like cd02642
R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the ...
 168-229 1.65e-26

R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the germline exit after four mitotic divisions, by facilitating SCF-ubiquitin-proteasome-dependent proteolysis. Maize DBF1-interactor protein 1 (DIP1) containing an R3H domain is a potential regulator of DBF1 activity in stress responses. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100071  Cd Length: 63  Bit Score: 103.07  E-value: 1.65e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189398126  168 DRMMLLKLEQEILEFINDNNNQFKKFPQMTSYHRMLLHRVAAYFGMDHNVDQTG-KAVIINKT 229
Cdd:cd02642      1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
152-229 6.53e-14

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 67.71  E-value: 6.53e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398126   152 IDLHEFLVNTLKKNPRDRMMLLKLEQEILEFINdNNNQFKKFPQMTSYHRMLLHRVAAYFGMDHNVDQTGKA--VIINKT 229
Cdd:smart00393    1 ADFLPVTLDALSYRPRRREELIELELEIARFVK-STKESVELPPMNSYERKIVHELAEKYGLESESFGEGPKrrVVISKK 79
SUZ pfam12752
SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched ...
 250-303 4.33e-12

SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched in positively charged amino acids. It was first characterized in the C.elegans protein Szy-20 where it has been shown to bind RNA and allow their localization to the centrosome. Warning- the domain has a compositionally biased character.


Pssm-ID: 463689 [Multi-domain]  Cd Length: 56  Bit Score: 61.95  E-value: 4.33e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1189398126  250 EFQQRFILKRDDASMD--RDDNQIRVPLQDGRRSKSIEEREEEYQRVRERIFARET 303
Cdd:pfam12752    1 PPPKMKILRRPSSGSSssSSAGSSGASSSSGSDSKTLEEREAEYAEARARIFGSSE 56
R3H cd02325
R3H domain. The name of the R3H domain comes from the characteristic spacing of the most ...
 172-228 3.36e-11

R3H domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. R3H domains are found in proteins together with ATPase domains, SF1 helicase domains, SF2 DEAH helicase domains, Cys-rich repeats, ring-type zinc fingers, and KH domains. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100064  Cd Length: 59  Bit Score: 59.55  E-value: 3.36e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1189398126  172 LLKLEQEILEFINDNNNQFKKFPQMTSYHRMLLHRVAAYFGMDHNVDQTG--KAVIINK 228
Cdd:cd02325      1 REEREEELEAFAKDAAGKSLELPPMNSYERKLIHDLAEYYGLKSESEGEGpnRRVVITK 59
R3H pfam01424
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ...
 170-228 2.81e-10

R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA.


Pssm-ID: 460206  Cd Length: 60  Bit Score: 56.73  E-value: 2.81e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189398126  170 MMLLKLEQEILEFINDNNNQFKkFPQMTSYHRMLLHRVAAYFGMDHNV--DQTGKAVIINK 228
Cdd:pfam01424    1 EFLEQLAEKLAEFVKDTGKSLE-LPPMSSYERRIIHELAQKYGLESESegEEPNRRVVVYK 60
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 466-774 2.13e-09

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 61.56  E-value: 2.13e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398126  466 QPVPALQPSPQPVQFSPSSCPQVLLPVSPPQQYNMADDLSNPF--GQMSLSRQGSTEAADPSAALFQTPLISQHPQQTSF 543
Cdd:pfam09606  141 SQMSRVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGqaGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMG 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398126  544 IMASTGQPLPTSNYSTSSHAPPTQQVLPPQGYMQppQQIQVSYYPPGQYPNSNQQYRPLSHPVAY--SPQRGQQLPQPSQ 621
Cdd:pfam09606  221 QQAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQ--SQLGMGINQMQQMPQGVGGGAGQGGPGQPmgPPGQQPGAMPNVM 298

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398126  622 QPGLQPMMPNQQQAAYQGMIGVQQPQNQGLLSSQRSSMGGQMQGLVVQYTPLPSYQVPVGSDSQNVVQP--PFQQPMLVP 699
Cdd:pfam09606  299 SIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGANPMQRgqPGMMSSPSP 378

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398126  700 VS----QSVQG--GLPAAGVPVYYSMIPPAQQNGTSPSVGFLQPPGSEQYQMPQSPSPCSPPQMPQQYSGVSPSG-PGVV 772
Cdd:pfam09606  379 VPgqqvRQVTPnqFMRQSPQPSVPSPQGPGSQPPQSHPGGMIPSPALIPSPSPQMSQQPAQQRTIGQDSPGGSLNtPGQS 458


                   ..
gi 1189398126  773 VM 774
Cdd:pfam09606  459 AV 460
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 474-637 1.18e-05

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 49.65  E-value: 1.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398126  474 SPQPVQFSPSSCPQVllPVSPPQQYNMADDLSNPFGQMSLSRQGSTEAADPSAALFQTPLISQHPQQTSFIMAsTGQPLP 553
Cdd:pfam09770  207 AKKPAQQPAPAPAQP--PAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVTILQRPQSPQPDPA-QPSIQP 283

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398126  554 tsnystsshAPPTQQVLPPQGYMQPPQQIQ---VSYYPPGQYPNSNQQYRPLSHPVAYSPQRGQQLPQPSQQPGLQPM-- 628
Cdd:pfam09770  284 ---------QAQQFHQQPPPVPVQPTQILQnpnRLSAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPIITHPQQLaq 354


                   ....*....
gi 1189398126  629 MPNQQQAAY 637
Cdd:pfam09770  355 LSEEEKAAY 363
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 469-685 2.51e-05

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 48.49  E-value: 2.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398126  469 PALQPSPQPVQFSPSSCPQVLLPVSPPQQ-----------YNMADDLSNPFGQMSLSRQGSTEAADPSAALFQTPLISQH 537
Cdd:pfam09770  107 PAARAAQSSAQPPASSLPQYQYASQQSQQpskpvrtgyekYKEPEPIPDLQVDASLWGVAPKKAAAPAPAPQPAAQPASL 186

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398126  538 PQQTSFIM-------ASTGQPLPTSNYSTSSHAPPTQQVLPPQGYMQPPQQIQVSYY-PPGQYPNSNQQYRPLSHPVAYS 609
Cdd:pfam09770  187 PAPSRKMMsleeveaAMRAQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQqQPQQQPQQPQQHPGQGHPVTIL 266

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189398126  610 PQRGQQLPQPSQQPGLQPMMPNQQQAAYQGMIGVQQPQNQGLLSSQRSSMGGQMQGLVVQYTPLPSYQVPVGSDSQ 685
Cdd:pfam09770  267 QRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQPTQILQNPNRLSAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQ 342
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 467-611 3.54e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 44.76  E-value: 3.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398126  467 PVPALQPSPQPVQFSPSSCPQVLLPVSPP--QQYNMADDLSNPFGQMSLSRQGSTEAADPSAALFQTPLISQHPQQT--S 542
Cdd:pfam03154  189 PGTTQAATAGPTPSAPSVPPQGSPATSQPpnQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPlpQ 268

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189398126  543 FIMASTGQPLPTSNYSTSSHAPptqQVLPPQGYMQPPQ--QIQVSYYPPGQYPNSNQQ--YRPLSHPVAYSPQ 611
Cdd:pfam03154  269 PSLHGQMPPMPHSLQTGPSHMQ---HPVPPQPFPLTPQssQSQVPPGPSPAAPGQSQQriHTPPSQSQLQSQQ 338
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 464-611 1.33e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 42.76  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398126  464 ISQPVPALQPSPQPVQFSPSSCPQVLLPVSPPQQYNMADDLSNPFGQMSLSRQGSTEAADPSAAlfQTPLISQHPQQTSF 543
Cdd:PRK10263   353 PAQPTVAWQPVPGPQTGEPVIAPAPEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPA--QQPYYAPAPEQPAQ 430

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189398126  544 IMASTGQPlPTSNYSTSSHAPPTQQVLPPQGYMQPPQQIQVSYYPPGQYpnsnQQYRPLSHPVAYSPQ 611
Cdd:PRK10263   431 QPYYAPAP-EQPVAGNAWQAEEQQSTFAPQSTYQTEQTYQQPAAQEPLY----QQPQPVEQQPVVEPE 493
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 524-675 2.16e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 42.38  E-value: 2.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398126  524 PSAALFqTPLISqhPQQTSfimasTGQPLPTSNYSTSSH-APPTQQVLPPQGYMQPPQQiqvsYYPPGQYPNSNQQYRPL 602
Cdd:PRK10263   740 PHEPLF-TPIVE--PVQQP-----QQPVAPQQQYQQPQQpVAPQPQYQQPQQPVAPQPQ----YQQPQQPVAPQPQYQQP 807

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189398126  603 SHPVAYSPQRGqqlpqpsqqpglQPMMPNQQQAAYqgmigvQQPQNQGLLSSQRSSM------GGQMQGLVVQYTPLPS 675
Cdd:PRK10263   808 QQPVAPQPQYQ------------QPQQPVAPQPQY------QQPQQPVAPQPQDTLLhpllmrNGDSRPLHKPTTPLPS 868
PHA03377 PHA03377
EBNA-3C; Provisional
 447-734 3.08e-03

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 41.58  E-value: 3.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398126  447 PALPPTPQQQPPLNNHMISQPVPALQpsPQPVQFSPSSCPQVLLPVSPPQQYNMADdlsnPFGQMSLSRQGSTEAADPSA 526
Cdd:PHA03377   672 PATQSTPPRPSWLPSVFVLPSVDAGR--AQPSEESHLSSMSPTQPISHEEQPRYED----PDDPLDLSLHPDQAPPPSHQ 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398126  527 ALFQTPLISQHPQqtsfimastgqplptSNYSTSSHAPPTQqvLPPQGYMQPP-QQIQVSYYPPGQYP-NSNQQYRPLSH 604
Cdd:PHA03377   746 APYSGHEEPQAQQ---------------APYPGYWEPRPPQ--APYLGYQEPQaQGVQVSSYPGYAGPwGLRAQHPRYRH 808

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189398126  605 PVAYSPQRGQQLPQPSQQPGLQPMMPNQqqaaYQGMIGVQQPQNQGLLSSQRSSMGGQMQGLVVQYTPLPsyQVPVGSDS 684
Cdd:PHA03377   809 SWAYWSQYPGHGHPQGPWAPRPPHLPPQ----WDGSAGHGQDQVSQFPHLQSETGPPRLQLSQVPQLPYS--QTLVSSSA 882

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1189398126  685 QNVVQPPFQQPMlvpvsQSVQGGLPAAGVPVYYSMIPPAQQNGTS-PSVGF 734
Cdd:PHA03377   883 PSWSSPQPRAPI-----RPIPTRFPPPPMPLQDSMAVGCDSSGTAcPSMPF 928
 
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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