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Conserved domains on  [gi|1187443692|ref|NP_001337912|]
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zinc finger and SCAN domain-containing protein 25 isoform b [Homo sapiens]

Protein Classification

KRAB_A-box and COG5048 domain-containing protein( domain architecture ID 11577739)

protein containing domains KRAB_A-box, COG5048, and zf-H2C2_2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
160-340 7.84e-12

FOG: Zn-finger [General function prediction only];


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 66.26  E-value: 7.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187443692 160 LPPPQHG-AIPLPDEVKTHSSFWKPFQCPECGKGFSRSSNLVRHQRT-----HEEKSYGCVE--CGKGFTLREYLMKHQR 231
Cdd:COG5048   265 LPTASSQsSSPNESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRSvnhsgESLKPFSCPYslCGKLFSRNDALKRHIL 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187443692 232 THLGKRPYVC--SECWKTFSQ----RHHLEVHQRSHTGEKPYKCGD---CWKSFSRRQHLQVHRRTHTGEKPYTCE---C 299
Cdd:COG5048   345 LHTSISPAKEklLNSSSKFSPllnnEPPQSLQQYKDLKNDKKSETLsnsCIRNFKRDSNLSLHIITHLSFRPYNCKnppC 424

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1187443692 300 GKSFSRNANLAVHRRAHTgEKPYGCQVCGKRFSKGERLVRH 340
Cdd:COG5048   425 SKSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLSNH 464
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 67-95 2.48e-06

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: 43.69  E-value: 2.48e-06
                          10        20
                  ....*....|....*....|....*....
gi 1187443692  67 PFKDMALAFPEEEWRHVTPAQIDCFGEYV 95
Cdd:cd07765     2 TFEDVAVYFSQEEWELLDPAQRDLYRDVM 30
zf-H2C2_2 pfam13465
Zinc-finger double domain;
336-361 4.23e-06

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 4.23e-06
                          10        20
                  ....*....|....*....|....*.
gi 1187443692 336 RLVRHQRIHTGEKPYHCPACGRSFNQ 361
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
160-340 7.84e-12

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 66.26  E-value: 7.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187443692 160 LPPPQHG-AIPLPDEVKTHSSFWKPFQCPECGKGFSRSSNLVRHQRT-----HEEKSYGCVE--CGKGFTLREYLMKHQR 231
Cdd:COG5048   265 LPTASSQsSSPNESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRSvnhsgESLKPFSCPYslCGKLFSRNDALKRHIL 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187443692 232 THLGKRPYVC--SECWKTFSQ----RHHLEVHQRSHTGEKPYKCGD---CWKSFSRRQHLQVHRRTHTGEKPYTCE---C 299
Cdd:COG5048   345 LHTSISPAKEklLNSSSKFSPllnnEPPQSLQQYKDLKNDKKSETLsnsCIRNFKRDSNLSLHIITHLSFRPYNCKnppC 424

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1187443692 300 GKSFSRNANLAVHRRAHTgEKPYGCQVCGKRFSKGERLVRH 340
Cdd:COG5048   425 SKSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLSNH 464
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 67-95 2.48e-06

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: 43.69  E-value: 2.48e-06
                          10        20
                  ....*....|....*....|....*....
gi 1187443692  67 PFKDMALAFPEEEWRHVTPAQIDCFGEYV 95
Cdd:cd07765     2 TFEDVAVYFSQEEWELLDPAQRDLYRDVM 30
zf-H2C2_2 pfam13465
Zinc-finger double domain;
336-361 4.23e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 4.23e-06
                          10        20
                  ....*....|....*....|....*.
gi 1187443692 336 RLVRHQRIHTGEKPYHCPACGRSFNQ 361
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 184-206 7.48e-06

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 42.29  E-value: 7.48e-06
                          10        20
                  ....*....|....*....|...
gi 1187443692 184 FQCPECGKGFSRSSNLVRHQRTH 206
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 68-87 3.05e-03

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 35.14  E-value: 3.05e-03
                          10        20
                  ....*....|....*....|
gi 1187443692  68 FKDMALAFPEEEWRHVTPAQ 87
Cdd:pfam01352   4 FEDVAVDFTQEEWALLDPAQ 23
ZnF_C2H2 smart00355
zinc finger;
184-206 6.36e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 33.98  E-value: 6.36e-03
                           10        20
                   ....*....|....*....|...
gi 1187443692  184 FQCPECGKGFSRSSNLVRHQRTH 206
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
KRAB smart00349
krueppel associated box;
68-87 6.37e-03

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 34.88  E-value: 6.37e-03
                           10        20
                   ....*....|....*....|
gi 1187443692   68 FKDMALAFPEEEWRHVTPAQ 87
Cdd:smart00349   3 FEDVAVYFTQEEWEQLDPAQ 22
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
160-340 7.84e-12

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 66.26  E-value: 7.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187443692 160 LPPPQHG-AIPLPDEVKTHSSFWKPFQCPECGKGFSRSSNLVRHQRT-----HEEKSYGCVE--CGKGFTLREYLMKHQR 231
Cdd:COG5048   265 LPTASSQsSSPNESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRSvnhsgESLKPFSCPYslCGKLFSRNDALKRHIL 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187443692 232 THLGKRPYVC--SECWKTFSQ----RHHLEVHQRSHTGEKPYKCGD---CWKSFSRRQHLQVHRRTHTGEKPYTCE---C 299
Cdd:COG5048   345 LHTSISPAKEklLNSSSKFSPllnnEPPQSLQQYKDLKNDKKSETLsnsCIRNFKRDSNLSLHIITHLSFRPYNCKnppC 424

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1187443692 300 GKSFSRNANLAVHRRAHTgEKPYGCQVCGKRFSKGERLVRH 340
Cdd:COG5048   425 SKSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
274-378 5.57e-07

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 51.24  E-value: 5.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187443692 274 KSFSRRQHLQVHRRTHTG-EKPYTC-ECGKSFSRNANLAVHRRA--HTGE--KPYGC--QVCGKRFSKGERLVRHQRIHT 345
Cdd:COG5048   268 ASSQSSSPNESDSSSEKGfSLPIKSkQCNISFSRSSPLTRHLRSvnHSGEslKPFSCpySLCGKLFSRNDALKRHILLHT 347

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1187443692 346 GEKPYHCPA--CGRSFNQRSILNRHQKTQHRQEPL 378
Cdd:COG5048   348 SISPAKEKLlnSSSKFSPLLNNEPPQSLQQYKDLK 382
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 67-95 2.48e-06

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: 43.69  E-value: 2.48e-06
                          10        20
                  ....*....|....*....|....*....
gi 1187443692  67 PFKDMALAFPEEEWRHVTPAQIDCFGEYV 95
Cdd:cd07765     2 TFEDVAVYFSQEEWELLDPAQRDLYRDVM 30
zf-H2C2_2 pfam13465
Zinc-finger double domain;
336-361 4.23e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 4.23e-06
                          10        20
                  ....*....|....*....|....*.
gi 1187443692 336 RLVRHQRIHTGEKPYHCPACGRSFNQ 361
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
265-321 5.14e-06

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.15  E-value: 5.14e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187443692 265 KPYKCGDCWKSFSRRQHLQVHRRTHTGEKPYTC---ECGKSFSRNANLAVHRRAHTGEKP 321
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsysGCDKSFSRPLELSRHLRTHHNNPS 91
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 184-206 7.48e-06

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 42.29  E-value: 7.48e-06
                          10        20
                  ....*....|....*....|...
gi 1187443692 184 FQCPECGKGFSRSSNLVRHQRTH 206
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
320-376 1.45e-04

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.53  E-value: 1.45e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1187443692 320 KPYGCQVCGKRFSKGERLVRHQRIHTGEKPYHCPACGRSFNQRSILNRHQKTQHRQE 376
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHN 88
zf-H2C2_2 pfam13465
Zinc-finger double domain;
281-305 1.64e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 1.64e-04
                          10        20
                  ....*....|....*....|....*.
gi 1187443692 281 HLQVHRRTHTGEKPYTC-ECGKSFSR 305
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCpECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 267-289 2.09e-04

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 38.05  E-value: 2.09e-04
                          10        20
                  ....*....|....*....|...
gi 1187443692 267 YKCGDCWKSFSRRQHLQVHRRTH 289
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 239-261 4.23e-04

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 37.28  E-value: 4.23e-04
                          10        20
                  ....*....|....*....|...
gi 1187443692 239 YVCSECWKTFSQRHHLEVHQRSH 261
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
236-298 5.09e-04

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.99  E-value: 5.09e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1187443692 236 KRPYVCSECWKTFSQRHHLEVHQRSHTGEKPYKCGD--CWKSFSRRQHLQVHRRTHTGEKPYTCE 298
Cdd:COG5048    31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNS 95
zf-H2C2_2 pfam13465
Zinc-finger double domain;
253-278 5.10e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 5.10e-04
                          10        20
                  ....*....|....*....|....*.
gi 1187443692 253 HLEVHQRSHTGEKPYKCGDCWKSFSR 278
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
293-361 2.57e-03

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 39.68  E-value: 2.57e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1187443692 293 KPYTCE-CGKSFSRNANLAVHRRAHTGEKPYGCQV--CGKRFSKGERLVRHQRIHTGEKPYHCPACGRSFNQ 361
Cdd:COG5048    32 RPDSCPnCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNS 103
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 68-87 3.05e-03

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 35.14  E-value: 3.05e-03
                          10        20
                  ....*....|....*....|
gi 1187443692  68 FKDMALAFPEEEWRHVTPAQ 87
Cdd:pfam01352   4 FEDVAVDFTQEEWALLDPAQ 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
225-250 3.60e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 3.60e-03
                          10        20
                  ....*....|....*....|....*.
gi 1187443692 225 YLMKHQRTHLGKRPYVCSECWKTFSQ 250
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
ZnF_C2H2 smart00355
zinc finger;
184-206 6.36e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 33.98  E-value: 6.36e-03
                           10        20
                   ....*....|....*....|...
gi 1187443692  184 FQCPECGKGFSRSSNLVRHQRTH 206
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
KRAB smart00349
krueppel associated box;
68-87 6.37e-03

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 34.88  E-value: 6.37e-03
                           10        20
                   ....*....|....*....|
gi 1187443692   68 FKDMALAFPEEEWRHVTPAQ 87
Cdd:smart00349   3 FEDVAVYFTQEEWEQLDPAQ 22
 
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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