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Conserved domains on  [gi|10337601|ref|NP_066294|]
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protein SSX3 [Homo sapiens]

Protein Classification

KRAB and SSXRD domain-containing protein( domain architecture ID 12204788)

KRAB and SSXRD domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
23-82 2.98e-16

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 69.16  E-value: 2.98e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10337601     23 KAFDDIAKYFSKEEWEKMKVSEKIVY-VYMKRKYEAMTKLGFKAILPSFMRNKRVTDFQGN 82
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYrDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
SSXRD pfam09514
SSXRD motif; SSX1 can repress transcription, and this has been attributed to a putative ...
 158-187 6.30e-07

SSXRD motif; SSX1 can repress transcription, and this has been attributed to a putative Kruppel associated box (KRAB) repression domain at the N-terminus. However, from the analysis of these deletion constructs further repression activity was found at the C-terminus of SSX1. Which has been called the SSXRD (SSX Repression Domain). The potent repression exerted by full-length SSX1 appears to localize to this region.


:

Pssm-ID: 430657  Cd Length: 31  Bit Score: 43.91  E-value: 6.30e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 10337601   158 KRGEHAWTHRLRERKqLVIYEEISDPEEDD 187
Cdd:pfam09514   3 RKEVEVWMYRLRERK-GVVYEEISDPQEDD 31
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
23-82 2.98e-16

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 69.16  E-value: 2.98e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10337601     23 KAFDDIAKYFSKEEWEKMKVSEKIVY-VYMKRKYEAMTKLGFKAILPSFMRNKRVTDFQGN 82
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYrDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
SSXRD pfam09514
SSXRD motif; SSX1 can repress transcription, and this has been attributed to a putative ...
 158-187 6.30e-07

SSXRD motif; SSX1 can repress transcription, and this has been attributed to a putative Kruppel associated box (KRAB) repression domain at the N-terminus. However, from the analysis of these deletion constructs further repression activity was found at the C-terminus of SSX1. Which has been called the SSXRD (SSX Repression Domain). The potent repression exerted by full-length SSX1 appears to localize to this region.


Pssm-ID: 430657  Cd Length: 31  Bit Score: 43.91  E-value: 6.30e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 10337601   158 KRGEHAWTHRLRERKqLVIYEEISDPEEDD 187
Cdd:pfam09514   3 RKEVEVWMYRLRERK-GVVYEEISDPQEDD 31
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 24-61 2.88e-05

KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta , KRAB-A interacting protein , and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation.


Pssm-ID: 143639  Cd Length: 40  Bit Score: 39.84  E-value: 2.88e-05
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 10337601  24 AFDDIAKYFSKEEWEKMKVSEKIVYVYMKR-KYEAMTKL 61
Cdd:cd07765   2 TFEDVAVYFSQEEWELLDPAQRDLYRDVMLeNYENLVSL 40
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
23-82 2.98e-16

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 69.16  E-value: 2.98e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10337601     23 KAFDDIAKYFSKEEWEKMKVSEKIVY-VYMKRKYEAMTKLGFKAILPSFMRNKRVTDFQGN 82
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYrDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
SSXRD pfam09514
SSXRD motif; SSX1 can repress transcription, and this has been attributed to a putative ...
 158-187 6.30e-07

SSXRD motif; SSX1 can repress transcription, and this has been attributed to a putative Kruppel associated box (KRAB) repression domain at the N-terminus. However, from the analysis of these deletion constructs further repression activity was found at the C-terminus of SSX1. Which has been called the SSXRD (SSX Repression Domain). The potent repression exerted by full-length SSX1 appears to localize to this region.


Pssm-ID: 430657  Cd Length: 31  Bit Score: 43.91  E-value: 6.30e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 10337601   158 KRGEHAWTHRLRERKqLVIYEEISDPEEDD 187
Cdd:pfam09514   3 RKEVEVWMYRLRERK-GVVYEEISDPQEDD 31
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 24-61 2.88e-05

KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta , KRAB-A interacting protein , and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation.


Pssm-ID: 143639  Cd Length: 40  Bit Score: 39.84  E-value: 2.88e-05
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 10337601  24 AFDDIAKYFSKEEWEKMKVSEKIVYVYMKR-KYEAMTKL 61
Cdd:cd07765   2 TFEDVAVYFSQEEWELLDPAQRDLYRDVMLeNYENLVSL 40
 
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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