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Conserved domains on  [gi|564378224|ref|XP_006248929|]
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RB-associated KRAB zinc finger protein isoform X1 [Rattus norvegicus]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204699)

KRAB (Kruppel-associated box) domain-containing zinc finger protein (KRAB-ZFP) plays important roles in cell differentiation and organ development and in regulating viral replication and transcription

CATH:  3.30.160.60|1.10.287.1360
Gene Ontology:  GO:0003677|GO:0008270|GO:0005515|GO:0006355|GO:0001217|GO:0003700
PubMed:  8183940|22803940|2023909|8183939|10748030|27867147|28765213|11361095|30718982|10940247
SCOP:  4003583|4002243

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-68 9.10e-32

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 117.31  E-value: 9.10e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564378224     8 LSFKDVAVAFSQEEWQQLDSEERTTYRDVMLETYSNLVSVGYDVTKPNVIIKLEQGEEPWT 68
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
340-699 1.55e-14

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 76.66  E-value: 1.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378224 340 KPYECSECGKTFCQKTHLTLHQRNHSGERPYPCS--ECGKSFSRKSALNDHQRTHTGEKLYTCNECGKS--YYRKSTLIT 415
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLsnSKASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378224 416 HQRTHTgEKPYQCSECGKFFSRVSYLTIHYRSHLEEKPYECTECGKTF--NLNSAFTRHRKAHAEERVQECG-------- 485
Cdd:COG5048  112 SSSSNS-NDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSvnTPQSNSLHPPLPANSLSKDPSSnlslliss 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378224 486 ----------ECGKPSRLQYLPDHADGLGEKH----------HGCNECGKTFLENSAFSRHQPVPEGEKTYECNICGKVF 545
Cdd:COG5048  191 nvstsipsssENSPLSSSYSIPSSSSDQNLENsssslplttnSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASS 270

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378224 546 SDLSCYTVHYRGHS-EEKPFGCSECGKTFSHNSSLFRHQR--VHTGE--KPYECYE--CGKFFSQKSYLTIHHRIHSGEK 618
Cdd:COG5048  271 QSSSPNESDSSSEKgFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSIS 350

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378224 619 PYEC--SKCGKVFSRMSN-----LTVHYRSHSGEKPYEC--NECGKVFSQKSYLTVHYRTHSGEKPYECN--ECGKKFHH 687
Cdd:COG5048  351 PAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNR 430

                        410
                 ....*....|..
gi 564378224 688 RSAFNSHQRIHK 699
Cdd:COG5048  431 HYNLIPHKKIHT 442
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 314-336 2.84e-03

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: 35.74  E-value: 2.84e-03
                          10        20
                  ....*....|....*....|...
gi 564378224  314 YKCDECGKTFCQKLHLTQHQRTH 336
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-68 9.10e-32

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 117.31  E-value: 9.10e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564378224     8 LSFKDVAVAFSQEEWQQLDSEERTTYRDVMLETYSNLVSVGYDVTKPNVIIKLEQGEEPWT 68
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 7-48 4.46e-20

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: 83.67  E-value: 4.46e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 564378224    7 PLSFKDVAVAFSQEEWQQLDSEERTTYRDVMLETYSNLVSVG 48
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 8-46 9.19e-17

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: 74.12  E-value: 9.19e-17
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 564378224   8 LSFKDVAVAFSQEEWQQLDSEERTTYRDVMLETYSNLVS 46
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
340-699 1.55e-14

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 76.66  E-value: 1.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378224 340 KPYECSECGKTFCQKTHLTLHQRNHSGERPYPCS--ECGKSFSRKSALNDHQRTHTGEKLYTCNECGKS--YYRKSTLIT 415
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLsnSKASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378224 416 HQRTHTgEKPYQCSECGKFFSRVSYLTIHYRSHLEEKPYECTECGKTF--NLNSAFTRHRKAHAEERVQECG-------- 485
Cdd:COG5048  112 SSSSNS-NDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSvnTPQSNSLHPPLPANSLSKDPSSnlslliss 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378224 486 ----------ECGKPSRLQYLPDHADGLGEKH----------HGCNECGKTFLENSAFSRHQPVPEGEKTYECNICGKVF 545
Cdd:COG5048  191 nvstsipsssENSPLSSSYSIPSSSSDQNLENsssslplttnSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASS 270

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378224 546 SDLSCYTVHYRGHS-EEKPFGCSECGKTFSHNSSLFRHQR--VHTGE--KPYECYE--CGKFFSQKSYLTIHHRIHSGEK 618
Cdd:COG5048  271 QSSSPNESDSSSEKgFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSIS 350

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378224 619 PYEC--SKCGKVFSRMSN-----LTVHYRSHSGEKPYEC--NECGKVFSQKSYLTVHYRTHSGEKPYECN--ECGKKFHH 687
Cdd:COG5048  351 PAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNR 430

                        410
                 ....*....|..
gi 564378224 688 RSAFNSHQRIHK 699
Cdd:COG5048  431 HYNLIPHKKIHT 442
zf-H2C2_2 pfam13465
Zinc-finger double domain;
578-603 5.22e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 5.22e-04
                          10        20
                  ....*....|....*....|....*.
gi 564378224  578 SLFRHQRVHTGEKPYECYECGKFFSQ 603
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 314-336 2.84e-03

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: 35.74  E-value: 2.84e-03
                          10        20
                  ....*....|....*....|...
gi 564378224  314 YKCDECGKTFCQKLHLTQHQRTH 336
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-68 9.10e-32

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 117.31  E-value: 9.10e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564378224     8 LSFKDVAVAFSQEEWQQLDSEERTTYRDVMLETYSNLVSVGYDVTKPNVIIKLEQGEEPWT 68
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 7-48 4.46e-20

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: 83.67  E-value: 4.46e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 564378224    7 PLSFKDVAVAFSQEEWQQLDSEERTTYRDVMLETYSNLVSVG 48
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 8-46 9.19e-17

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: 74.12  E-value: 9.19e-17
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 564378224   8 LSFKDVAVAFSQEEWQQLDSEERTTYRDVMLETYSNLVS 46
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
340-699 1.55e-14

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 76.66  E-value: 1.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378224 340 KPYECSECGKTFCQKTHLTLHQRNHSGERPYPCS--ECGKSFSRKSALNDHQRTHTGEKLYTCNECGKS--YYRKSTLIT 415
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLsnSKASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378224 416 HQRTHTgEKPYQCSECGKFFSRVSYLTIHYRSHLEEKPYECTECGKTF--NLNSAFTRHRKAHAEERVQECG-------- 485
Cdd:COG5048  112 SSSSNS-NDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSvnTPQSNSLHPPLPANSLSKDPSSnlslliss 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378224 486 ----------ECGKPSRLQYLPDHADGLGEKH----------HGCNECGKTFLENSAFSRHQPVPEGEKTYECNICGKVF 545
Cdd:COG5048  191 nvstsipsssENSPLSSSYSIPSSSSDQNLENsssslplttnSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASS 270

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378224 546 SDLSCYTVHYRGHS-EEKPFGCSECGKTFSHNSSLFRHQR--VHTGE--KPYECYE--CGKFFSQKSYLTIHHRIHSGEK 618
Cdd:COG5048  271 QSSSPNESDSSSEKgFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSIS 350

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378224 619 PYEC--SKCGKVFSRMSN-----LTVHYRSHSGEKPYEC--NECGKVFSQKSYLTVHYRTHSGEKPYECN--ECGKKFHH 687
Cdd:COG5048  351 PAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNR 430

                        410
                 ....*....|..
gi 564378224 688 RSAFNSHQRIHK 699
Cdd:COG5048  431 HYNLIPHKKIHT 442
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
255-694 9.23e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 67.80  E-value: 9.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378224 255 MKPFECTQCGKSFCKKSKFIIHQRAHTGEKPYACGV--CGKSFSQKGTLTVHRRSHLEEKPYKCDecgktfcQKLHLTQH 332
Cdd:COG5048   31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNS-------KSLPLSNS 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378224 333 QRTHSGEkpyecSECGKTFCQKTHLTLHQRNHSGERPYPCSECGKSFSRKSALNDHQRTHTGEKLYTC-------NECGK 405
Cdd:COG5048  104 KASSSSL-----SSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSlhpplpaNSLSK 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378224 406 SYYRKSTLITHQRTHTGEKPYQCSECGKFFSRVSYLTIHYRSHLEEKPYECTECGKTFNLNSAFTRHRKAHAEERVQECG 485
Cdd:COG5048  179 DPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSAS 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378224 486 ECGKPSRlqylpdhadglgekhhgcnecGKTFLENSAFSRHQPVPEGEKT--YECNICGKVFSDLSCYTVHYRG--HSEE 561
Cdd:COG5048  259 ESPRSSL---------------------PTASSQSSSPNESDSSSEKGFSlpIKSKQCNISFSRSSPLTRHLRSvnHSGE 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378224 562 --KPFGCSE--CGKTFSHNSSLFRHQRVHTGEKPYECY--ECGKFFSQKSY-----LTIHHRIHSGEKPYEC--SKCGKV 628
Cdd:COG5048  318 slKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRN 397

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564378224 629 FSRMSNLTVHYRSHSGEKPYECN--ECGKVFSQKSYLTVHYRTHSGEKPYECNECgKKFHHRSAFNSH 694
Cdd:COG5048  398 FKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSIL-KSFRRDLDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
284-445 2.49e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.38  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378224 284 KPYACGVCGKSFSQKGTLTVHRRSHLEE----KPYKCDE--CGKTFCQKLHLTQHQRTHSGEKPYEC--SECGKTFCQKT 355
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRSVNHSgeslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378224 356 ----HLTLHQRNHSGERPYPC---SECGKSFSRKSALNDHQRTHT--GEKLYTCNECGKSYYRKSTLITHQRTHTGEKPY 426
Cdd:COG5048  368 nnepPQSLQQYKDLKNDKKSEtlsNSCIRNFKRDSNLSLHIITHLsfRPYNCKNPPCSKSFNRHYNLIPHKKIHTNHAPL 447

                        170
                 ....*....|....*....
gi 564378224 427 QCSECGKFFSRVSYLTIHY 445
Cdd:COG5048  448 LCSILKSFRRDLDLSNHGK 466
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
352-583 6.56e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 46.23  E-value: 6.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378224 352 CQKTHLTLHQRNHSGERPYPCSECGKSFSRKSALNDHQRTHTGEKL-YTCNECGKSYYRKSTLITHQRT--HTGE--KPY 426
Cdd:COG5048  243 QSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGFSLpIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPF 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378224 427 QCSE--CGKFFSRVSYLTIHYRSHLEEKPYECTECGKTFNLNSAFTRHRKAHAEERVQEcgecgKPSRLQYLPDhadglg 504
Cdd:COG5048  323 SCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNNEPPQSLQQYKDL-----KNDKKSETLS------ 391

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378224 505 ekhhgcNECGKTFLENSAFSRH--QPVPEGEKTYECNICGKVFSDLSCYTVHYRGHSEEKPFGCSECGKTFSHNSSLFRH 582
Cdd:COG5048  392 ------NSCIRNFKRDSNLSLHiiTHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHG 465


                 .
gi 564378224 583 Q 583
Cdd:COG5048  466 K 466
zf-H2C2_2 pfam13465
Zinc-finger double domain;
578-603 5.22e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 5.22e-04
                          10        20
                  ....*....|....*....|....*.
gi 564378224  578 SLFRHQRVHTGEKPYECYECGKFFSQ 603
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
328-351 7.51e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 7.51e-04
                          10        20
                  ....*....|....*....|....
gi 564378224  328 HLTQHQRTHSGEKPYECSECGKTF 351
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
413-437 1.31e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.31e-03
                          10        20
                  ....*....|....*....|....*
gi 564378224  413 LITHQRTHTGEKPYQCSECGKFFSR 437
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 370-392 1.37e-03

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: 36.51  E-value: 1.37e-03
                          10        20
                  ....*....|....*....|...
gi 564378224  370 YPCSECGKSFSRKSALNDHQRTH 392
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 648-670 1.53e-03

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: 36.51  E-value: 1.53e-03
                          10        20
                  ....*....|....*....|...
gi 564378224  648 YECNECGKVFSQKSYLTVHYRTH 670
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
634-659 2.32e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.32e-03
                          10        20
                  ....*....|....*....|....*.
gi 564378224  634 NLTVHYRSHSGEKPYECNECGKVFSQ 659
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
356-381 2.44e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.44e-03
                          10        20
                  ....*....|....*....|....*.
gi 564378224  356 HLTLHQRNHSGERPYPCSECGKSFSR 381
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 314-336 2.84e-03

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: 35.74  E-value: 2.84e-03
                          10        20
                  ....*....|....*....|...
gi 564378224  314 YKCDECGKTFCQKLHLTQHQRTH 336
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 398-420 4.17e-03

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: 34.97  E-value: 4.17e-03
                          10        20
                  ....*....|....*....|...
gi 564378224  398 YTCNECGKSYYRKSTLITHQRTH 420
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
662-685 4.81e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.81e-03
                          10        20
                  ....*....|....*....|....
gi 564378224  662 YLTVHYRTHSGEKPYECNECGKKF 685
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 620-642 5.07e-03

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: 34.97  E-value: 5.07e-03
                          10        20
                  ....*....|....*....|...
gi 564378224  620 YECSKCGKVFSRMSNLTVHYRSH 642
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 342-364 7.22e-03

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: 34.58  E-value: 7.22e-03
                          10        20
                  ....*....|....*....|...
gi 564378224  342 YECSECGKTFCQKTHLTLHQRNH 364
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 566-586 7.73e-03

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: 34.20  E-value: 7.73e-03
                          10        20
                  ....*....|....*....|.
gi 564378224  566 CSECGKTFSHNSSLFRHQRVH 586
Cdd:pfam00096   3 CPDCGKSFSRKSNLKRHLRTH 23
 
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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