NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|4585643|ref|NP_003408|]
View 

zinc finger protein 264 [Homo sapiens]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204794)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-74 1.10e-31

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 116.92  E-value: 1.10e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4585643      14 VTFDDVAVTFTKEEWGQLDLAQRTLYQEVMLENCGLLVSLGCPVPKAELICHLEHGQEPWT 74
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
257-561 5.05e-10

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 62.02  E-value: 5.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4585643  257 RPYECMECGKAFNRKSYLTQHQRIHSGEKPYKCN--ECGKAFTHRSNFVLHNRRHTGEKSFVCTecgQVFRHRPGFLRHY 334
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNS---KSLPLSNSKASSS 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4585643  335 VVHSG--ENPYECLECGKVFKHRSYlmwHQQTHTGEKPYE--------CSECGKVFLESAALIH-HYVIHTGEKPFECLE 403
Cdd:COG5048 109 SLSSSssNSNDNNLLSSHSLPPSSR---DPQLPDLLSISNlrnnplpgNNSSSVNTPQSNSLHPpLPANSLSKDPSSNLS 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4585643  404 CGKAFNHRSYLKRHQ----RIHTGEKPFVCSECGK------AFTHCSTFILHKR--------AHTGEKPFECKECG---- 461
Cdd:COG5048 186 LLISSNVSTSIPSSSenspLSSSYSIPSSSSDQNLenssssLPLTTNSQLSPKSllsqspssLSSSDSSSSASESPrssl 265

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4585643  462 --KAFSNRKDLIRHFSIHTG-EKPYECVECGKAFTRMSGLTRHKR--IHSGE--KPYECVE--CGKSFCWSTNLIRHAII 532
Cdd:COG5048 266 ptASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILL 345

                       330       340       350
                ....*....|....*....|....*....|.
gi 4585643  533 HTGEKPYKC--SECGKAFSRSSSLTQHQRMH 561
Cdd:COG5048 346 HTSISPAKEklLNSSSKFSPLLNNEPPQSLQ 376
zf-H2C2_2 pfam13465
Zinc-finger double domain;
221-240 9.99e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.88  E-value: 9.99e-03
                          10        20
                  ....*....|....*....|
gi 4585643    221 HEKIHSGVKPYECTECGKTF 240
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSF 24
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-74 1.10e-31

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 116.92  E-value: 1.10e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4585643      14 VTFDDVAVTFTKEEWGQLDLAQRTLYQEVMLENCGLLVSLGCPVPKAELICHLEHGQEPWT 74
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 13-54 3.17e-22

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: 89.45  E-value: 3.17e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 4585643     13 SVTFDDVAVTFTKEEWGQLDLAQRTLYQEVMLENCGLLVSLG 54
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 14-53 1.37e-18

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: 79.13  E-value: 1.37e-18
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 4585643   14 VTFDDVAVTFTKEEWGQLDLAQRTLYQEVMLENCGLLVSL 53
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
257-561 5.05e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 62.02  E-value: 5.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4585643  257 RPYECMECGKAFNRKSYLTQHQRIHSGEKPYKCN--ECGKAFTHRSNFVLHNRRHTGEKSFVCTecgQVFRHRPGFLRHY 334
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNS---KSLPLSNSKASSS 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4585643  335 VVHSG--ENPYECLECGKVFKHRSYlmwHQQTHTGEKPYE--------CSECGKVFLESAALIH-HYVIHTGEKPFECLE 403
Cdd:COG5048 109 SLSSSssNSNDNNLLSSHSLPPSSR---DPQLPDLLSISNlrnnplpgNNSSSVNTPQSNSLHPpLPANSLSKDPSSNLS 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4585643  404 CGKAFNHRSYLKRHQ----RIHTGEKPFVCSECGK------AFTHCSTFILHKR--------AHTGEKPFECKECG---- 461
Cdd:COG5048 186 LLISSNVSTSIPSSSenspLSSSYSIPSSSSDQNLenssssLPLTTNSQLSPKSllsqspssLSSSDSSSSASESPrssl 265

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4585643  462 --KAFSNRKDLIRHFSIHTG-EKPYECVECGKAFTRMSGLTRHKR--IHSGE--KPYECVE--CGKSFCWSTNLIRHAII 532
Cdd:COG5048 266 ptASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILL 345

                       330       340       350
                ....*....|....*....|....*....|.
gi 4585643  533 HTGEKPYKC--SECGKAFSRSSSLTQHQRMH 561
Cdd:COG5048 346 HTSISPAKEklLNSSSKFSPLLNNEPPQSLQ 376
zf-H2C2_2 pfam13465
Zinc-finger double domain;
413-438 8.96e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 8.96e-06
                          10        20
                  ....*....|....*....|....*.
gi 4585643    413 YLKRHQRIHTGEKPFVCSECGKAFTH 438
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
221-240 9.99e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.88  E-value: 9.99e-03
                          10        20
                  ....*....|....*....|
gi 4585643    221 HEKIHSGVKPYECTECGKTF 240
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSF 24
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-74 1.10e-31

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 116.92  E-value: 1.10e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4585643      14 VTFDDVAVTFTKEEWGQLDLAQRTLYQEVMLENCGLLVSLGCPVPKAELICHLEHGQEPWT 74
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 13-54 3.17e-22

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: 89.45  E-value: 3.17e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 4585643     13 SVTFDDVAVTFTKEEWGQLDLAQRTLYQEVMLENCGLLVSLG 54
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 14-53 1.37e-18

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: 79.13  E-value: 1.37e-18
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 4585643   14 VTFDDVAVTFTKEEWGQLDLAQRTLYQEVMLENCGLLVSL 53
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
257-561 5.05e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 62.02  E-value: 5.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4585643  257 RPYECMECGKAFNRKSYLTQHQRIHSGEKPYKCN--ECGKAFTHRSNFVLHNRRHTGEKSFVCTecgQVFRHRPGFLRHY 334
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNS---KSLPLSNSKASSS 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4585643  335 VVHSG--ENPYECLECGKVFKHRSYlmwHQQTHTGEKPYE--------CSECGKVFLESAALIH-HYVIHTGEKPFECLE 403
Cdd:COG5048 109 SLSSSssNSNDNNLLSSHSLPPSSR---DPQLPDLLSISNlrnnplpgNNSSSVNTPQSNSLHPpLPANSLSKDPSSNLS 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4585643  404 CGKAFNHRSYLKRHQ----RIHTGEKPFVCSECGK------AFTHCSTFILHKR--------AHTGEKPFECKECG---- 461
Cdd:COG5048 186 LLISSNVSTSIPSSSenspLSSSYSIPSSSSDQNLenssssLPLTTNSQLSPKSllsqspssLSSSDSSSSASESPrssl 265

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4585643  462 --KAFSNRKDLIRHFSIHTG-EKPYECVECGKAFTRMSGLTRHKR--IHSGE--KPYECVE--CGKSFCWSTNLIRHAII 532
Cdd:COG5048 266 ptASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILL 345

                       330       340       350
                ....*....|....*....|....*....|.
gi 4585643  533 HTGEKPYKC--SECGKAFSRSSSLTQHQRMH 561
Cdd:COG5048 346 HTSISPAKEklLNSSSKFSPLLNNEPPQSLQ 376
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
184-568 5.88e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.55  E-value: 5.88e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4585643  184 SHNSCESGKDPMIQEEENN--FKCSECGKVFNKKHLLAGHEKIHSGVKPYECT--ECGKTFIKSTHLLQHHMIHTGERPY 259
Cdd:COG5048  13 NSVLSSTPKSTLKSLSNAPrpDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSD 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4585643  260 ECmeCGKAFNRKSYLTQHQRIHSGE---KPYKCNECGKAFTHR--------SNFVLHNRRHTGEKSFVCT---------- 318
Cdd:COG5048  93 LN--SKSLPLSNSKASSSSLSSSSSnsnDNNLLSSHSLPPSSRdpqlpdllSISNLRNNPLPGNNSSSVNtpqsnslhpp 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4585643  319 -----ECGQVFRHRPGFLRHYVVHSGENPYECLECgkvfkHRSYLMWHQQTH----TGEKPYECSECGKVFLESaaLIHH 389
Cdd:COG5048 171 lpansLSKDPSSNLSLLISSNVSTSIPSSSENSPL-----SSSYSIPSSSSDqnleNSSSSLPLTTNSQLSPKS--LLSQ 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4585643  390 YVIHTGeKPFECLECGKAFNHRSYLKRHQRIH----------TGEKPFVCSECGKAFTHCSTFILHKRA--HTGE--KPF 455
Cdd:COG5048 244 SPSSLS-SSDSSSSASESPRSSLPTASSQSSSpnesdsssekGFSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPF 322

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4585643  456 ECKE--CGKAFSNRKDLIRHFSIHTGEKPYECV--ECGKAFTRMS-----GLTRHKRIHSGEKPYECVE-CGKSFCWST- 524
Cdd:COG5048 323 SCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLnneppQSLQQYKDLKNDKKSETLSnSCIRNFKRDs 402

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*.
gi 4585643  525 NLIRHAIIHTGEKP--YKCSECGKAFSRSSSLTQHQRMHTGKNPIS 568
Cdd:COG5048 403 NLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLL 448
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
229-434 8.99e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.09  E-value: 8.99e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4585643  229 KPYECTECGKTFIKSTHLLQH--HMIHTGE--RPYECME--CGKAFNRKSYLTQHQRIHSGEKPYKC--NECGKAFTHRS 300
Cdd:COG5048 288 LPIKSKQCNISFSRSSPLTRHlrSVNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLL 367

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4585643  301 NfvlhnrrhtgeksfvctecgqvfRHRPGFLRHYVVHSGENPYECL--ECGKVFKHRSYLMWHQQTHTGEKPYECSecgk 378
Cdd:COG5048 368 N-----------------------NEPPQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCK---- 420

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4585643  379 vflesaalihhyvihtgekpfeCLECGKAFNHRSYLKRHQRIHTGEKPFVCSECGK 434
Cdd:COG5048 421 ----------------------NPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS 454
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
285-580 1.21e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 51.24  E-value: 1.21e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4585643  285 KPYKCNECGKAFTHRSNFVLHNRRHTGEKSFVCTECGQVF-RHRPGFLRHYVVHSGENPYECLEcgkvfkHRSYLMWHQQ 363
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKsFSRPLELSRHLRTHHNNPSDLNS------KSLPLSNSKA 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4585643  364 THTgEKPYECSECGKVFLESAALIHHYVIHTgEKPFECLEC--GKAFNHRSYLKRHQRIHTGEKPFVCS--ECGKAFTHC 439
Cdd:COG5048 106 SSS-SLSSSSSNSNDNNLLSSHSLPPSSRDP-QLPDLLSISnlRNNPLPGNNSSSVNTPQSNSLHPPLPanSLSKDPSSN 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4585643  440 STFILHKRAHTGEKPFECKECGKAFSNRKDLIRHFSIHTGEKPYECVECGKAF--------------------------- 492
Cdd:COG5048 184 LSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpksllsqspsslsssdssssasesprs 263

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4585643  493 ---TRMSGLTRHKRIHSGE-----KPYECVECGKSFCWSTNLIRH--AIIHTGE--KPYKCSE--CGKAFSRSSSLTQHQ 558
Cdd:COG5048 264 slpTASSQSSSPNESDSSSekgfsLPIKSKQCNISFSRSSPLTRHlrSVNHSGEslKPFSCPYslCGKLFSRNDALKRHI 343

                       330       340
                ....*....|....*....|..
gi 4585643  559 RMHTGKNPISVTDVGRPFTSGQ 580
Cdd:COG5048 344 LLHTSISPAKEKLLNSSSKFSP 365
zf-H2C2_2 pfam13465
Zinc-finger double domain;
413-438 8.96e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 8.96e-06
                          10        20
                  ....*....|....*....|....*.
gi 4585643    413 YLKRHQRIHTGEKPFVCSECGKAFTH 438
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
273-298 5.18e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 5.18e-05
                          10        20
                  ....*....|....*....|....*.
gi 4585643    273 YLTQHQRIHSGEKPYKCNECGKAFTH 298
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
525-550 8.54e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 8.54e-05
                          10        20
                  ....*....|....*....|....*.
gi 4585643    525 NLIRHAIIHTGEKPYKCSECGKAFSR 550
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
276-503 1.55e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.69  E-value: 1.55e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4585643  276 QHQRIHSGEKPYKCNECGKAFTHRSNFVLHNRRHTGEKSFVCTECGQVFRHRPGFLRHYVVHSGE-------NPYECLEC 348
Cdd:COG5048 216 SDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQC 295

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4585643  349 GKVFKHRSYLMWHQQT--HTGE--KPYECSE--CGKVFLESAALIHHYVIHTGEKPFEC--LECGKAFNHRSYLKRHQRI 420
Cdd:COG5048 296 NISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSL 375

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4585643  421 H-----TGEKPFVC--SECGKAFTHCSTFILHKRAHTGEKP--FECKECGKAFSNRKDLIRHFSIHTGEKPYECvECGKA 491
Cdd:COG5048 376 QqykdlKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLC-SILKS 454

                       250
                ....*....|..
gi 4585643  492 FTRMSGLTRHKR 503
Cdd:COG5048 455 FRRDLDLSNHGK 466
zf-H2C2_2 pfam13465
Zinc-finger double domain;
357-380 2.88e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 2.88e-04
                          10        20
                  ....*....|....*....|....
gi 4585643    357 YLMWHQQTHTGEKPYECSECGKVF 380
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 539-561 3.20e-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: 3.20e-04
                          10        20
                  ....*....|....*....|...
gi 4585643    539 YKCSECGKAFSRSSSLTQHQRMH 561
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
245-270 5.96e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 5.96e-04
                          10        20
                  ....*....|....*....|....*.
gi 4585643    245 HLLQHHMIHTGERPYECMECGKAFNR 270
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
498-520 1.27e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.27e-03
                          10        20
                  ....*....|....*....|...
gi 4585643    498 LTRHKRIHSGEKPYECVECGKSF 520
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 479-562 1.43e-03

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 41.63  E-value: 1.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4585643  479 GEKPYEC--VECGKAFTRMSGLTRHkRIHSgekpyecvECGKSFCWSTNLIRHAIIHTGEKPYKCSECGKAFSRSSSLTQ 556
Cdd:COG5189 346 DGKPYKCpvEGCNKKYKNQNGLKYH-MLHG--------HQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                ....*.
gi 4585643  557 HqRMHT 562
Cdd:COG5189 417 H-RKHS 421
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 399-421 1.85e-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: 36.12  E-value: 1.85e-03
                          10        20
                  ....*....|....*....|...
gi 4585643    399 FECLECGKAFNHRSYLKRHQRIH 421
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 259-281 2.85e-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: 35.35  E-value: 2.85e-03
                          10        20
                  ....*....|....*....|...
gi 4585643    259 YECMECGKAFNRKSYLTQHQRIH 281
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
445-466 4.12e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.12e-03
                          10        20
                  ....*....|....*....|..
gi 4585643    445 HKRAHTGEKPFECKECGKAFSN 466
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
469-494 4.25e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.25e-03
                          10        20
                  ....*....|....*....|....*.
gi 4585643    469 DLIRHFSIHTGEKPYECVECGKAFTR 494
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 343-365 4.31e-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: 4.31e-03
                          10        20
                  ....*....|....*....|...
gi 4585643    343 YECLECGKVFKHRSYLMWHQQTH 365
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
198-333 5.72e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 39.68  E-value: 5.72e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4585643  198 EEENNFKCSE--CGKVFNKKHLLAGHEKIHSGVKPYEC--TECGKTFIKSTH-----LLQHHMIHTGERPYECM--ECGK 266
Cdd:COG5048 317 ESLKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETLsnSCIR 396

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4585643  267 AFNRKSYLTQH--QRIHSGEKPYKCNECGKAFTHRSNFVLHNRRHTgEKSFVCTECGQVFRHRPGFLRH 333
Cdd:COG5048 397 NFKRDSNLSLHiiTHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLSNH 464
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 287-309 9.00e-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: 9.00e-03
                          10        20
                  ....*....|....*....|...
gi 4585643    287 YKCNECGKAFTHRSNFVLHNRRH 309
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
221-240 9.99e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.88  E-value: 9.99e-03
                          10        20
                  ....*....|....*....|
gi 4585643    221 HEKIHSGVKPYECTECGKTF 240
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSF 24
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH