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Conserved domains on  [gi|564359646|ref|XP_006241545|]
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R3H domain-containing protein 2 isoform X21 [Rattus norvegicus]

Protein Classification

R3H and SUZ domain-containing protein( domain architecture ID 10119061)

R3H and SUZ domain-containing protein may bind single-stranded nucleic acids through its R3H domain and RNA through its SUZ domain, similar to Zea mays DBF1-interactor protein 1 that is a potential regulator of DBF1 activity in stress responses

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 1.22e-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: 103.45  E-value: 1.22e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564359646 168 DRMMLLKLEQEILDFISDNNNQFKKFPQMTSYHRMLLHRVAAYFGMDHNVDQTG-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 ...
250-302 2.15e-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: 62.72  E-value: 2.15e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564359646  250 EFQQRFILKRDDASMDRE--ENQMRVPLQDGRRSKSIEEREEEYQRVRERIFARE 302
Cdd:pfam12752   1 PPPKMKILRRPSSGSSSSssAGSSGASSSSGSDSKTLEEREAEYAEARARIFGSS 55
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
474-743 7.46e-07

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.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 53.23  E-value: 7.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  474 PSSALFQSPLISQHPQQA--SFIMASAGQPLPTSNYSTSSHAPptqQVLPPQGYMQPPQ--QIQVSYYPPGQYPNSNQQ- 548
Cdd:pfam03154 248 PLQPMTQPPPPSQVSPQPlpQPSLHGQMPPMPHSLQTGPSHMQ---HPVPPQPFPLTPQssQSQVPPGPSPAAPGQSQQr 324
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  549 -YRPLSHPVAYSPQ--RGQQLPQAsqqPGLQPMMSSQQQTAYQGMLGVQQPQNQGLLSNQRSNSMGGQMqglvvqytPLP 625
Cdd:pfam03154 325 iHTPPSQSQLQSQQppREQPLPPA---PLSMPHIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSNL--------PPP 393
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  626 SYQVPVGSESQNvvQPPFQQP---MLVPASQSVQGGLPAGGVPVYYSVIPPAQQNGTSPSV---GFLQPPGSEQYQMPQS 699
Cdd:pfam03154 394 PALKPLSSLSTH--HPPSAHPpplQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGlhqVPSQSPFPQHPFVPGG 471
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564359646  700 PAPCSPPQIPQqySGVSPSGPGV-------VVMQLNVPNGPQAPQNPSMVQ 743
Cdd:pfam03154 472 PPPITPPSGPP--TSTSSAMPGIqppssasVSSSGPVPAAVSCPLPPVQIK 520
 
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 1.22e-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: 103.45  E-value: 1.22e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564359646 168 DRMMLLKLEQEILDFISDNNNQFKKFPQMTSYHRMLLHRVAAYFGMDHNVDQTG-KAVIINKT 229
Cdd:cd02642    1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
152-229 3.14e-14

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 68.48  E-value: 3.14e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646   152 IDLHEFLVNTLKKNPRDRMMLLKLEQEILDFISdNNNQFKKFPQMTSYHRMLLHRVAAYFGMDHNVDQTGKA--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 ...
250-302 2.15e-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: 62.72  E-value: 2.15e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564359646  250 EFQQRFILKRDDASMDRE--ENQMRVPLQDGRRSKSIEEREEEYQRVRERIFARE 302
Cdd:pfam12752   1 PPPKMKILRRPSSGSSSSssAGSSGASSSSGSDSKTLEEREAEYAEARARIFGSS 55
R3H pfam01424
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ...
170-228 2.45e-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: 2.45e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564359646  170 MMLLKLEQEILDFISDNNNQFKkFPQMTSYHRMLLHRVAAYFGMDHNV--DQTGKAVIINK 228
Cdd:pfam01424   1 EFLEQLAEKLAEFVKDTGKSLE-LPPMSSYERRIIHELAQKYGLESESegEEPNRRVVVYK 60
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
474-743 7.46e-07

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: 53.23  E-value: 7.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  474 PSSALFQSPLISQHPQQA--SFIMASAGQPLPTSNYSTSSHAPptqQVLPPQGYMQPPQ--QIQVSYYPPGQYPNSNQQ- 548
Cdd:pfam03154 248 PLQPMTQPPPPSQVSPQPlpQPSLHGQMPPMPHSLQTGPSHMQ---HPVPPQPFPLTPQssQSQVPPGPSPAAPGQSQQr 324
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  549 -YRPLSHPVAYSPQ--RGQQLPQAsqqPGLQPMMSSQQQTAYQGMLGVQQPQNQGLLSNQRSNSMGGQMqglvvqytPLP 625
Cdd:pfam03154 325 iHTPPSQSQLQSQQppREQPLPPA---PLSMPHIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSNL--------PPP 393
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  626 SYQVPVGSESQNvvQPPFQQP---MLVPASQSVQGGLPAGGVPVYYSVIPPAQQNGTSPSV---GFLQPPGSEQYQMPQS 699
Cdd:pfam03154 394 PALKPLSSLSTH--HPPSAHPpplQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGlhqVPSQSPFPQHPFVPGG 471
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564359646  700 PAPCSPPQIPQqySGVSPSGPGV-------VVMQLNVPNGPQAPQNPSMVQ 743
Cdd:pfam03154 472 PPPITPPSGPP--TSTSSAMPGIqppssasVSSSGPVPAAVSCPLPPVQIK 520
PRK10263 PRK10263
DNA translocase FtsK; Provisional
443-722 1.19e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 49.70  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  443 LNNHMISQaedlsnPFGQMSLSRQGSTEAADPSSALFQSPLISQhPQQASFIMASAGQPLPTSNYSTSSHAPPtqqvlpP 522
Cdd:PRK10263  311 LNGAPITE------PVAVAAAATTATQSWAAPVEPVTQTPPVAS-VDVPPAQPTVAWQPVPGPQTGEPVIAPA------P 377
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  523 QGYMQPPQ--QIQVSYYPPGQYPNSNQQyrPLSHPVAYSPQRGQQLPQASQQPGLQPMMSSQQQTAYQGMLGVQQPQNQg 600
Cdd:PRK10263  378 EGYPQQSQyaQPAVQYNEPLQQPVQPQQ--PYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQS- 454
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  601 LLSNQRSnsmggqmqglvvqYTPLPSYQVPVGSESQNVVQPPFQQPMLVPASQSVQGGLPAGGVPVYYSVIPPAQQNGTS 680
Cdd:PRK10263  455 TFAPQST-------------YQTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPARPPLYYFEEVEEKRARERE 521
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 564359646  681 PSVGFLQP---PGSEQYQMPQSPAPCSPPQIP--QQYSGVSPSGPGV 722
Cdd:PRK10263  522 QLAAWYQPipePVKEPEPIKSSLKAPSVAAVPpvEAAAAVSPLASGV 568
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
561-696 2.77e-04

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 44.80  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  561 QRGQQLPQASQQPGLQPMMSSQQQTAYQGMLGVQQPQNQGLLSNQRSNSMGGQM---QGLVVQYTPLPSYQVPvGSESQN 637
Cdd:TIGR01628 374 QFMQLQPRMRQLPMGSPMGGAMGQPPYYGQGPQQQFNGQPLGWPRMSMMPTPMGpggPLRPNGLAPMNAVRAP-SRNAQN 452
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 564359646  638 VVQPPFQQPMlvPASQSVQGGLPAGGVPVYYSVIPPAQQNGTSPSVGFLQPPGsEQYQM 696
Cdd:TIGR01628 453 AAQKPPMQPV--MYPPNYQSLPLSQDLPQPQSTASQGGQNKKLAQVLASATPQ-MQKQV 508
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
468-757 3.34e-03

N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2.


Pssm-ID: 411776 [Multi-domain]  Cd Length: 511  Bit Score: 41.07  E-value: 3.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646 468 STEAADPSSALFQSPLISQHPQQasfimasagQPLPTSNYSTSSHAPPTQQ--VLPPQGyMQPPQQ----IQVSYYPPGQ 541
Cdd:cd22540    2 ATAAVSPSEYLQPAASTTQDSQP---------SPLALLAATCSKIGPPAVEaaVTPPAP-PQPTPRklvpIKPAPLPLGP 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646 542 YPN------SNQQYRPLSHPVAYSPQRGQQLPQASQQPGLQPMMSSQQQTAYQGMLGVQQPQNQGLLSNqrsnsmGGQMQ 615
Cdd:cd22540   72 GKNsigflsAKGNIIQLQGSQLSSSAPGGQQVFAIQNPTMIIKGSQTRSSTNQQYQISPQIQAAGQINN------SGQIQ 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646 616 GL----VVQYTPLPSYQVPVGSESQNVVQPPFQQP----MLVPASQSVQGGLPAGGVPVyySVIPpaQQNGTSPSVGFLQ 687
Cdd:cd22540  146 IIpgtnQAIITPVQVLQQPQQAHKPVPIKPAPLQTsntnSASLQVPGNVIKLQSGGNVA--LTLP--VNNLVGTQDGATQ 221
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564359646 688 -----PPGSEQYQMPQSPAPCSPPQIPQQysgvspSGPGVVVMQLNVPNGPQAPQNPSMVQWGHCKYYSVDQRGQ 757
Cdd:cd22540  222 lqlaaAPSKPSKKIRKKSAQAAQPAVTVA------EQVETVLIETTADNIIQAGNNLLIVQSPGTGQPAVLQQVQ 290
 
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 1.22e-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: 103.45  E-value: 1.22e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564359646 168 DRMMLLKLEQEILDFISDNNNQFKKFPQMTSYHRMLLHRVAAYFGMDHNVDQTG-KAVIINKT 229
Cdd:cd02642    1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
152-229 3.14e-14

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 68.48  E-value: 3.14e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646   152 IDLHEFLVNTLKKNPRDRMMLLKLEQEILDFISdNNNQFKKFPQMTSYHRMLLHRVAAYFGMDHNVDQTGKA--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 ...
250-302 2.15e-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: 62.72  E-value: 2.15e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564359646  250 EFQQRFILKRDDASMDRE--ENQMRVPLQDGRRSKSIEEREEEYQRVRERIFARE 302
Cdd:pfam12752   1 PPPKMKILRRPSSGSSSSssAGSSGASSSSGSDSKTLEEREAEYAEARARIFGSS 55
R3H cd02325
R3H domain. The name of the R3H domain comes from the characteristic spacing of the most ...
172-228 8.93e-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: 58.01  E-value: 8.93e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 564359646 172 LLKLEQEILDFISDNNNQFKKFPQMTSYHRMLLHRVAAYFGMDHNVDQTG--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 2.45e-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: 2.45e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564359646  170 MMLLKLEQEILDFISDNNNQFKkFPQMTSYHRMLLHRVAAYFGMDHNV--DQTGKAVIINK 228
Cdd:pfam01424   1 EFLEQLAEKLAEFVKDTGKSLE-LPPMSSYERRIIHELAQKYGLESESegEEPNRRVVVYK 60
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
474-743 7.46e-07

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: 53.23  E-value: 7.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  474 PSSALFQSPLISQHPQQA--SFIMASAGQPLPTSNYSTSSHAPptqQVLPPQGYMQPPQ--QIQVSYYPPGQYPNSNQQ- 548
Cdd:pfam03154 248 PLQPMTQPPPPSQVSPQPlpQPSLHGQMPPMPHSLQTGPSHMQ---HPVPPQPFPLTPQssQSQVPPGPSPAAPGQSQQr 324
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  549 -YRPLSHPVAYSPQ--RGQQLPQAsqqPGLQPMMSSQQQTAYQGMLGVQQPQNQGLLSNQRSNSMGGQMqglvvqytPLP 625
Cdd:pfam03154 325 iHTPPSQSQLQSQQppREQPLPPA---PLSMPHIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSNL--------PPP 393
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  626 SYQVPVGSESQNvvQPPFQQP---MLVPASQSVQGGLPAGGVPVYYSVIPPAQQNGTSPSV---GFLQPPGSEQYQMPQS 699
Cdd:pfam03154 394 PALKPLSSLSTH--HPPSAHPpplQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGlhqVPSQSPFPQHPFVPGG 471
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564359646  700 PAPCSPPQIPQqySGVSPSGPGV-------VVMQLNVPNGPQAPQNPSMVQ 743
Cdd:pfam03154 472 PPPITPPSGPP--TSTSSAMPGIqppssasVSSSGPVPAAVSCPLPPVQIK 520
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
467-656 7.87e-07

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: 53.12  E-value: 7.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  467 GSTEAADPSSALFQSPLISQHPQQASFIM------------ASAGQPLPTSNYSTSSHAPPTQQVLPPQGYMQPPQQIQv 534
Cdd:pfam09770 166 APKKAAAPAPAPQPAAQPASLPAPSRKMMsleeveaamraqAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQ- 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  535 syyPPGQYPNSNQQYRPLSHPVAYspqrgQQLPQASQQPGLQPMMSSQQQTAYQGMLGVQQPQNQGLlsnQRSNSMGGQM 614
Cdd:pfam09770 245 ---QPQQQPQQPQQHPGQGHPVTI-----LQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQPTQIL---QNPNRLSAAR 313
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 564359646  615 QGLVVQYTPLPSYQVPVGSESQNVVQPPfQQPMLVPASQSVQ 656
Cdd:pfam09770 314 VGYPQNPQPGVQPAPAHQAHRQQGSFGR-QAPIITHPQQLAQ 354
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
472-817 1.28e-06

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: 52.46  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  472 ADPSSALFQSPLISQHPQ-QASFIMASAGQPLPTSNYSTSSHAP-PTQQVLPPQGY---MQPPQQiQVSYYPPGQYPNSN 546
Cdd:pfam03154 156 SDSDSSAQQQILQTQPPVlQAQSGAASPPSPPPPGTTQAATAGPtPSAPSVPPQGSpatSQPPNQ-TQSTAAPHTLIQQT 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  547 QQYRPLSHPVAYSPQRGQQLPQASQQPGLQPMmssqqqtayqgmlgvQQPQNQGLLSnqrsnSMGGQMQ-GLVVQYTPLP 625
Cdd:pfam03154 235 PTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPL---------------PQPSLHGQMP-----PMPHSLQtGPSHMQHPVP 294
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  626 SYQVPVGSE-SQNVVQPPFQQPMLVPASQSVQgglpaggvpvyysvIPPAQQNGTSPSVGFLQPPGSEQYQMPQ-SPAPC 703
Cdd:pfam03154 295 PQPFPLTPQsSQSQVPPGPSPAAPGQSQQRIH--------------TPPSQSQLQSQQPPREQPLPPAPLSMPHiKPPPT 360
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  704 SP-PQIPQQYSGVSP---SGPGVVVMQLNVPNGPQAPQNPSMvqwghckyysvdqRGQKPGDLYSPDGD--PQTNaQMGS 777
Cdd:pfam03154 361 TPiPQLPNPQSHKHPphlSGPSPFQMNSNLPPPPALKPLSSL-------------STHHPPSAHPPPLQlmPQSQ-QLPP 426
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 564359646  778 SPVTSP--TQSPAPSPVTSLSSVCTGLSPLPVLTPFPR----PGGP 817
Cdd:pfam03154 427 PPAQPPvlTQSQSLPPPAASHPPTSGLHQVPSQSPFPQhpfvPGGP 472
PRK10263 PRK10263
DNA translocase FtsK; Provisional
443-722 1.19e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 49.70  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  443 LNNHMISQaedlsnPFGQMSLSRQGSTEAADPSSALFQSPLISQhPQQASFIMASAGQPLPTSNYSTSSHAPPtqqvlpP 522
Cdd:PRK10263  311 LNGAPITE------PVAVAAAATTATQSWAAPVEPVTQTPPVAS-VDVPPAQPTVAWQPVPGPQTGEPVIAPA------P 377
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  523 QGYMQPPQ--QIQVSYYPPGQYPNSNQQyrPLSHPVAYSPQRGQQLPQASQQPGLQPMMSSQQQTAYQGMLGVQQPQNQg 600
Cdd:PRK10263  378 EGYPQQSQyaQPAVQYNEPLQQPVQPQQ--PYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQS- 454
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  601 LLSNQRSnsmggqmqglvvqYTPLPSYQVPVGSESQNVVQPPFQQPMLVPASQSVQGGLPAGGVPVYYSVIPPAQQNGTS 680
Cdd:PRK10263  455 TFAPQST-------------YQTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPARPPLYYFEEVEEKRARERE 521
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 564359646  681 PSVGFLQP---PGSEQYQMPQSPAPCSPPQIP--QQYSGVSPSGPGV 722
Cdd:PRK10263  522 QLAAWYQPipePVKEPEPIKSSLKAPSVAAVPpvEAAAAVSPLASGV 568
PHA03379 PHA03379
EBNA-3A; Provisional
476-744 4.74e-05

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 47.36  E-value: 4.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646 476 SALFQSPLISQHPQQASFiMASAGQPLPTSNYSTSSHAPPTQQVLPPQGYMQPPQQIQVSYYPPGQYPNSNQ-------- 547
Cdd:PHA03379 511 ASLSQVPGVAFAPVMPQP-MPVEPVPVPTVALERPVCPAPPLIAMQGPGETSGIVRVRERWRPAPWTPNPPRspsqmsvr 589
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646 548 --------QYRPLSHPVAYSPqrgQQLPQAS-QQPGLQPMMSSQQ-----------QTAYQGMLGVQQPQNQGlLSNQRS 607
Cdd:PHA03379 590 drlarlraEAQPYQASVEVQP---PQLTQVSpQQPMEYPLEPEQQmfpgspfsqvaDVMRAGGVPAMQPQYFD-LPLQQP 665
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646 608 NSMGGQMQGLVVQYTPLPsyqvPVGSESQNVVQPPFQQPMLVPASqSVQG--GLPAGG--VPVYYSVIPPAQQNGTSPSV 683
Cdd:PHA03379 666 ISQGAPLAPLRASMGPVP----PVPATQPQYFDIPLTEPINQGAS-AAHFlpQQPMEGplVPERWMFQGATLSQSVRPGV 740
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646 684 GFLQPPGSEQYQ-----MPQSPAPCSPPQ----IPQQ--YSGVSPSgPGVVVMQ---------LNVPNGPQAPQNPSMVQ 743
Cdd:PHA03379 741 AQSQYFDLPLTQpinhgAPAAHFLHQPPMegpwVPEQwmFQGAPPS-QGTDVVQhqldalgyvLHVLNHPGVPVSPAVNQ 819

                 .
gi 564359646 744 W 744
Cdd:PHA03379 820 Y 820
PRK10263 PRK10263
DNA translocase FtsK; Provisional
338-692 4.92e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 47.39  E-value: 4.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  338 EPRPWSSTDSDGSVRSMrPPVTKASSfsgISILTRGDSIGSSKGGSAGRLSRPGMTL---GAPE------VCNQVTSPQS 408
Cdd:PRK10263  536 EPEPIKSSLKAPSVAAV-PPVEAAAA---VSPLASGVKKATLATGAAATVAAPVFSLansGGPRpqvkegIGPQLPRPKR 611
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  409 VR-----GLLPCTVQQQQQQQQQQQQLPALPPVPQQQPPLNNHMIS--QAEDLSNPFGQMSLSRQGST-------EAADP 474
Cdd:PRK10263  612 IRvptrrELASYGIKLPSQRAAEEKAREAQRNQYDSGDQYNDDEIDamQQDELARQFAQTQQQRYGEQyqhdvpvNAEDA 691
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  475 SSALfQSPLISQ--HPQQASFimaSAGQPLPTSNYSTSSHAPPTQQVLPPQGYMQP---PQQIQVSyyPPGQYPNSNQQY 549
Cdd:PRK10263  692 DAAA-EAELARQfaQTQQQRY---SGEQPAGANPFSLDDFEFSPMKALLDDGPHEPlftPIVEPVQ--QPQQPVAPQQQY 765
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  550 RPLSHPVAysPQRGQQLPqasQQPGLQPMMSSQQQTAYQGMLGVQQPQNqgllsnqrsnsmggqmqglvvQYTPLPSYQV 629
Cdd:PRK10263  766 QQPQQPVA--PQPQYQQP---QQPVAPQPQYQQPQQPVAPQPQYQQPQQ---------------------PVAPQPQYQQ 819
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564359646  630 PvgsESQNVVQPPFQQPMLVPASQsvqgglpaggvPVYYSVIPPAQQNGTS----------PSVGFLQPPGSE 692
Cdd:PRK10263  820 P---QQPVAPQPQYQQPQQPVAPQ-----------PQDTLLHPLLMRNGDSrplhkpttplPSLDLLTPPPSE 878
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
449-749 2.33e-04

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: 45.00  E-value: 2.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  449 SQAEDLSNPFGQMSLSRQGSTEAADPSSALfqsPLISQHPQQASFIMASAGQPLPTSnystsshapptQQVLPPQGymqp 528
Cdd:pfam09606 255 SQLGMGINQMQQMPQGVGGGAGQGGPGQPM---GPPGQQPGAMPNVMSIGDQNNYQQ-----------QQTRQQQQ---- 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  529 pqqiqvsyyppgqypnsnqqyrplshpvayspQRGQQLPQASQQPGLQPMMSSQQQTA--YQGMLGVQQPQNQGllsNQR 606
Cdd:pfam09606 317 --------------------------------QQGGNHPAAHQQQMNQSVGQGGQVVAlgGLNHLETWNPGNFG---GLG 361
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  607 SNSMGGQMQGLVVQYTPLPSYQVPVGSESQNVVQPPFQQpmlVPASQsvqgglpaggvpvyysviPPAQQNGTSPSVGFL 686
Cdd:pfam09606 362 ANPMQRGQPGMMSSPSPVPGQQVRQVTPNQFMRQSPQPS---VPSPQ------------------GPGSQPPQSHPGGMI 420
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564359646  687 QPPG---SEQYQMPQSPApcSPPQIPQQYSGVSPSGPGVVVMqlNVPNGPQAPQNPSMVQWGHCKY 749
Cdd:pfam09606 421 PSPAlipSPSPQMSQQPA--QQRTIGQDSPGGSLNTPGQSAV--NSPLNPQEEQLYREKYRQLTKY 482
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
552-796 2.74e-04

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: 45.03  E-value: 2.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  552 LSHPVAYSPQRGQQlPQASQQPGLQPMMSSQQQTAYQGMLGVQQPQNQGLLSN-QRSNSMGGQMQGLVVQYTPLP---SY 627
Cdd:pfam09770 104 RQQPAARAAQSSAQ-PPASSLPQYQYASQQSQQPSKPVRTGYEKYKEPEPIPDlQVDASLWGVAPKKAAAPAPAPqpaAQ 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  628 QVPVGSESQNVV-------------QPPFQQPMLVPASQsvqgglpaggvPVYYSVIPPAQQNGTSPSVGFLQPPGSEQY 694
Cdd:pfam09770 183 PASLPAPSRKMMsleeveaamraqaKKPAQQPAPAPAQP-----------PAAPPAQQAQQQQQFPPQIQQQQQPQQQPQ 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  695 QMPQSPAPCSPPQI------PQQYSGVSPSGPGVVVMQLNVPNGPQAP----QNPSMVQWGHCKYYSVDQRGQKPgdlys 764
Cdd:pfam09770 252 QPQQHPGQGHPVTIlqrpqsPQPDPAQPSIQPQAQQFHQQPPPVPVQPtqilQNPNRLSAARVGYPQNPQPGVQP----- 326
                         250       260       270
                  ....*....|....*....|....*....|..
gi 564359646  765 pdGDPQTNAQMGSSPVTSPTQSPAPSPVTSLS 796
Cdd:pfam09770 327 --APAHQAHRQQGSFGRQAPIITHPQQLAQLS 356
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
561-696 2.77e-04

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 44.80  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  561 QRGQQLPQASQQPGLQPMMSSQQQTAYQGMLGVQQPQNQGLLSNQRSNSMGGQM---QGLVVQYTPLPSYQVPvGSESQN 637
Cdd:TIGR01628 374 QFMQLQPRMRQLPMGSPMGGAMGQPPYYGQGPQQQFNGQPLGWPRMSMMPTPMGpggPLRPNGLAPMNAVRAP-SRNAQN 452
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 564359646  638 VVQPPFQQPMlvPASQSVQGGLPAGGVPVYYSVIPPAQQNGTSPSVGFLQPPGsEQYQM 696
Cdd:TIGR01628 453 AAQKPPMQPV--MYPPNYQSLPLSQDLPQPQSTASQGGQNKKLAQVLASATPQ-MQKQV 508
PHA03377 PHA03377
EBNA-3C; Provisional
446-713 8.81e-04

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 43.50  E-value: 8.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  446 HMISQAEDLSNPFG-------QMSLSRQGSTEAADPSSALfQSPLISQHPQQA--------SFIMASAGQPLPTSNYSTS 510
Cdd:PHA03377  631 RMFLRERLLEQSTGpkpksfwEMRAGRDGSGIQQEPSSRR-QPATQSTPPRPSwlpsvfvlPSVDAGRAQPSEESHLSSM 709
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  511 SHAPPTQQVLPPQgYMQPPQQIQVSYYPPGQYPNSNQqyrplshpvaySPQRGQQLPQASQQPGLQPMMSSQQQTAYQGm 590
Cdd:PHA03377  710 SPTQPISHEEQPR-YEDPDDPLDLSLHPDQAPPPSHQ-----------APYSGHEEPQAQQAPYPGYWEPRPPQAPYLG- 776
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  591 lgVQQPQNQGLLSNQ---RSNSMGGQMQGLVVQYTPLPSYQVPVGSESQN--VVQPPFQQPMLVPASQSVQGGLpAGGVP 665
Cdd:PHA03377  777 --YQEPQAQGVQVSSypgYAGPWGLRAQHPRYRHSWAYWSQYPGHGHPQGpwAPRPPHLPPQWDGSAGHGQDQV-SQFPH 853
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 564359646  666 VYYSVIPPAQQNGTSPSVGFLQPP--------GSEQYQMPQSPAPCS--PPQIPQQYS 713
Cdd:PHA03377  854 LQSETGPPRLQLSQVPQLPYSQTLvsssapswSSPQPRAPIRPIPTRfpPPPMPLQDS 911
PHA03378 PHA03378
EBNA-3B; Provisional
480-734 2.09e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 41.98  E-value: 2.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646 480 QSPLISQHPQQASFIMASAGQPLPTSNYSTSSHAPPTQQVLPPQGYMQPPQQIQVSYYPPGQYPNS-NQQYRPLSHPVAY 558
Cdd:PHA03378 708 AAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGApTPQPPPQAPPAPQ 787
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646 559 SPQRGQQLPQASQQPGLQPMMSSQQQTAYQGMlGVQQPQNQGLLSNQRSNSMGGQMQGLVVQYTPLPSYQVPVGSESQNV 638
Cdd:PHA03378 788 QRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQG-PTKQILRQLLTGGVKRGRPSLKKPAALERQAAAGPTPSPGSGTSDKI 866
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646 639 VQPP-FQQPMLVPASQSVQGGLPAggvPVYYSVIP--PAQQNGTSPSVGFLQP---PGSEQYQMPQSPAPcSPPQipqqy 712
Cdd:PHA03378 867 VQAPvFYPPVLQPIQVMRQLGSVR---AAAASTVTqaPTEYTGERRGVGPMHPtdiPPSKRAKTDAYVES-QPPH----- 937
                        250       260
                 ....*....|....*....|..
gi 564359646 713 SGVSPSgpgVVVMQLNVPNGPQ 734
Cdd:PHA03378 938 GGQSHS---FSVIWENVSQGQQ 956
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
424-790 2.47e-03

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: 41.92  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  424 QQQQQQLPALPPVPQQQPPLN------------NHMISQAEDLSNPFG-QMSLSRQGSTEAADPSSALFQSPLISQ-HPQ 489
Cdd:pfam09606  64 QGGQGNGGMGGGQQGMPDPINalqnlagqgtrpQMMGPMGPGPGGPMGqQMGGPGTASNLLASLGRPQMPMGGAGFpSQM 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  490 QASFIMASAGQPLPTSNYSTSSHAPPTQQVLPPQG--------YMQPPQQIQVSYYPPGQYPNSNQqyrplshPVAYSPQ 561
Cdd:pfam09606 144 SRVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNGgpgqgqagGMNGGQQGPMGGQMPPQMGVPGM-------PGPADAG 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  562 -RGQQLPQASQQPGLQPMMSSQQQTAYQGMLGVQQPQNQ--GLLSNQRSNSMGG----QMQGLVVQYTPLPSYQVPVGSE 634
Cdd:pfam09606 217 aQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQSqlGMGINQMQQMPQGvgggAGQGGPGQPMGPPGQQPGAMPN 296
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  635 SQNVVQPPFQQPMLVPASQSVQGGLPAGGVPVyySVIPPAQQNGTSPSVGFLQPPGSEQ--YQMPQSPAPCSPPQiPQQY 712
Cdd:pfam09606 297 VMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQ--QMNQSVGQGGQVVALGGLNHLETWNpgNFGGLGANPMQRGQ-PGMM 373
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  713 SGVSPSgPGVVVMQLNVPNGPQAPQNPSMVQWGHCKYysvdQRGQK--PGDLYSPDGDPQTNAQMGSSPVTS---PTQSP 787
Cdd:pfam09606 374 SSPSPV-PGQQVRQVTPNQFMRQSPQPSVPSPQGPGS----QPPQShpGGMIPSPALIPSPSPQMSQQPAQQrtiGQDSP 448

                  ...
gi 564359646  788 APS 790
Cdd:pfam09606 449 GGS 451
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
468-757 3.34e-03

N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2.


Pssm-ID: 411776 [Multi-domain]  Cd Length: 511  Bit Score: 41.07  E-value: 3.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646 468 STEAADPSSALFQSPLISQHPQQasfimasagQPLPTSNYSTSSHAPPTQQ--VLPPQGyMQPPQQ----IQVSYYPPGQ 541
Cdd:cd22540    2 ATAAVSPSEYLQPAASTTQDSQP---------SPLALLAATCSKIGPPAVEaaVTPPAP-PQPTPRklvpIKPAPLPLGP 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646 542 YPN------SNQQYRPLSHPVAYSPQRGQQLPQASQQPGLQPMMSSQQQTAYQGMLGVQQPQNQGLLSNqrsnsmGGQMQ 615
Cdd:cd22540   72 GKNsigflsAKGNIIQLQGSQLSSSAPGGQQVFAIQNPTMIIKGSQTRSSTNQQYQISPQIQAAGQINN------SGQIQ 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646 616 GL----VVQYTPLPSYQVPVGSESQNVVQPPFQQP----MLVPASQSVQGGLPAGGVPVyySVIPpaQQNGTSPSVGFLQ 687
Cdd:cd22540  146 IIpgtnQAIITPVQVLQQPQQAHKPVPIKPAPLQTsntnSASLQVPGNVIKLQSGGNVA--LTLP--VNNLVGTQDGATQ 221
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564359646 688 -----PPGSEQYQMPQSPAPCSPPQIPQQysgvspSGPGVVVMQLNVPNGPQAPQNPSMVQWGHCKYYSVDQRGQ 757
Cdd:cd22540  222 lqlaaAPSKPSKKIRKKSAQAAQPAVTVA------EQVETVLIETTADNIIQAGNNLLIVQSPGTGQPAVLQQVQ 290
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
454-624 3.93e-03

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 40.95  E-value: 3.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  454 LSNPFGQMSLSRQGSTEAADPSSALFQSPLISQHPQQASfimasAGQPLptsNYstsshaPPTQQVLPPQGYMQPPQQIQ 533
Cdd:TIGR01628 371 LQDQFMQLQPRMRQLPMGSPMGGAMGQPPYYGQGPQQQF-----NGQPL---GW------PRMSMMPTPMGPGGPLRPNG 436
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359646  534 VSYYPPGQYPNSNQQYRPLSHPVA---YSPQ-RGQQLPQASQQPGLQPMMSSQQQTAYQgMLGVQQPQnqgllsnQRSNS 609
Cdd:TIGR01628 437 LAPMNAVRAPSRNAQNAAQKPPMQpvmYPPNyQSLPLSQDLPQPQSTASQGGQNKKLAQ-VLASATPQ-------MQKQV 508
                         170
                  ....*....|....*
gi 564359646  610 MGGQMQGLVVQYTPL 624
Cdd:TIGR01628 509 LGERLFPLVEAIEPA 523
 
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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