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Conserved domains on  [gi|1219862436|ref|NP_001340729|]
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zinc finger protein 846 isoform 4 [Homo sapiens]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204793)

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:0005515|GO:0008270|GO:0003677|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;
8-66 1.06e-27

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 102.67  E-value: 1.06e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1219862436    8 VTFEDVAVDFTQEEWTLLDQAQRDLYRDVMLENYKNLIILGSELFKRSLMSGLEQMEEL 66
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEP 59
zf-H2C2_2 pfam13465
Zinc-finger double domain;
268-292 1.40e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.20  E-value: 1.40e-05
                          10        20
                  ....*....|....*....|....*
gi 1219862436 268 LKLHIRTHSGEKPYKCKECGKAFTH 292
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 super family cl25788
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 249-327 4.81e-05

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


The actual alignment was detected with superfamily member COG5189:

Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 44.71  E-value: 4.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219862436 249 GEKPYVCK--ECGKAFTQSTGLKLHiRTHSGEKPykckecgkaFTHSSYLTDHTRIHSGK-KPYVCMECGKAFTRSTGLI 325
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLKYH-MLHGHQNQ---------KLHENPSPEKMNIFSAKdKPYRCEVCDKRYKNLNGLK 415


                  ..
gi 1219862436 326 LH 327
Cdd:COG5189   416 YH 417
SFP1 super family cl25788
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 197-276 6.74e-05

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


The actual alignment was detected with superfamily member COG5189:

Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 44.32  E-value: 6.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219862436 197 CECKDCWRTFLNQSSLKLHiRSHNgdkhyvckECGKAFSNSSHLIGHGRIHSGEKPYVCKECGKAFTQSTGLKLHiRTHS 276
Cdd:COG5189   352 CPVEGCNKKYKNQNGLKYH-MLHG--------HQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKYH-RKHS 421
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-66 1.06e-27

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 102.67  E-value: 1.06e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1219862436    8 VTFEDVAVDFTQEEWTLLDQAQRDLYRDVMLENYKNLIILGSELFKRSLMSGLEQMEEL 66
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEP 59
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 7-48 1.17e-24

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: 94.07  E-value: 1.17e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1219862436   7 LVTFEDVAVDFTQEEWTLLDQAQRDLYRDVMLENYKNLIILG 48
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 8-45 5.37e-21

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: 84.14  E-value: 5.37e-21
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1219862436   8 VTFEDVAVDFTQEEWTLLDQAQRDLYRDVMLENYKNLI 45
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLV 38
zf-H2C2_2 pfam13465
Zinc-finger double domain;
268-292 1.40e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.20  E-value: 1.40e-05
                          10        20
                  ....*....|....*....|....*
gi 1219862436 268 LKLHIRTHSGEKPYKCKECGKAFTH 292
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 249-327 4.81e-05

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 44.71  E-value: 4.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219862436 249 GEKPYVCK--ECGKAFTQSTGLKLHiRTHSGEKPykckecgkaFTHSSYLTDHTRIHSGK-KPYVCMECGKAFTRSTGLI 325
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLKYH-MLHGHQNQ---------KLHENPSPEKMNIFSAKdKPYRCEVCDKRYKNLNGLK 415


                  ..
gi 1219862436 326 LH 327
Cdd:COG5189   416 YH 417
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 197-276 6.74e-05

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 44.32  E-value: 6.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219862436 197 CECKDCWRTFLNQSSLKLHiRSHNgdkhyvckECGKAFSNSSHLIGHGRIHSGEKPYVCKECGKAFTQSTGLKLHiRTHS 276
Cdd:COG5189   352 CPVEGCNKKYKNQNGLKYH-MLHG--------HQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKYH-RKHS 421
PHA00733 PHA00733
hypothetical protein
 252-299 2.22e-04

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 40.63  E-value: 2.22e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1219862436 252 PYVCKECGKAFTQSTGLKLHIRTHSGEKpyKCKECGKAFTHSSYLTDH 299
Cdd:PHA00733   73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH 118
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
111-332 3.01e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.38  E-value: 3.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219862436 111 KLYDSNHSGKVFNEHPFLMTHMITHIGEKTSEDNQSgkalRKNFPHSFYKKSHAEGKMPKCVKHEKAFNQFPNLTRQNKT 190
Cdd:COG5048   210 SIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSP----SSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKG 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219862436 191 HTqeKLCECKDCWRTFLNQSSLKLHIRSHN----GDKHYVCKE--CGKAFSNSSHLIGHGRIHSGEKPYVCK--ECGKAF 262
Cdd:COG5048   286 FS--LPIKSKQCNISFSRSSPLTRHLRSVNhsgeSLKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKF 363

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1219862436 263 TQSTGLKLH--IRTHSGEKPYKCKE-----CGKAFTHSSYLTDHTRIHSGKKPYVCM--ECGKAFTRSTGLILHMRIHT 332
Cdd:COG5048   364 SPLLNNEPPqsLQQYKDLKNDKKSEtlsnsCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHT 442
zf-H2C2_2 pfam13465
Zinc-finger double domain;
295-320 3.78e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 3.78e-04
                          10        20
                  ....*....|....*....|....*.
gi 1219862436 295 YLTDHTRIHSGKKPYVCMECGKAFTR 320
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
211-236 1.62e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 1.62e-03
                          10        20
                  ....*....|....*....|....*.
gi 1219862436 211 SLKLHIRSHNGDKHYVCKECGKAFSN 236
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-66 1.06e-27

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 102.67  E-value: 1.06e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1219862436    8 VTFEDVAVDFTQEEWTLLDQAQRDLYRDVMLENYKNLIILGSELFKRSLMSGLEQMEEL 66
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEP 59
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 7-48 1.17e-24

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: 94.07  E-value: 1.17e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1219862436   7 LVTFEDVAVDFTQEEWTLLDQAQRDLYRDVMLENYKNLIILG 48
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 8-45 5.37e-21

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: 84.14  E-value: 5.37e-21
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1219862436   8 VTFEDVAVDFTQEEWTLLDQAQRDLYRDVMLENYKNLI 45
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLV 38
zf-H2C2_2 pfam13465
Zinc-finger double domain;
268-292 1.40e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.20  E-value: 1.40e-05
                          10        20
                  ....*....|....*....|....*
gi 1219862436 268 LKLHIRTHSGEKPYKCKECGKAFTH 292
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 249-327 4.81e-05

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 44.71  E-value: 4.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219862436 249 GEKPYVCK--ECGKAFTQSTGLKLHiRTHSGEKPykckecgkaFTHSSYLTDHTRIHSGK-KPYVCMECGKAFTRSTGLI 325
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLKYH-MLHGHQNQ---------KLHENPSPEKMNIFSAKdKPYRCEVCDKRYKNLNGLK 415


                  ..
gi 1219862436 326 LH 327
Cdd:COG5189   416 YH 417
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 197-276 6.74e-05

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 44.32  E-value: 6.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219862436 197 CECKDCWRTFLNQSSLKLHiRSHNgdkhyvckECGKAFSNSSHLIGHGRIHSGEKPYVCKECGKAFTQSTGLKLHiRTHS 276
Cdd:COG5189   352 CPVEGCNKKYKNQNGLKYH-MLHG--------HQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKYH-RKHS 421
PHA00733 PHA00733
hypothetical protein
 252-299 2.22e-04

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 40.63  E-value: 2.22e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1219862436 252 PYVCKECGKAFTQSTGLKLHIRTHSGEKpyKCKECGKAFTHSSYLTDH 299
Cdd:PHA00733   73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH 118
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
111-332 3.01e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.38  E-value: 3.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219862436 111 KLYDSNHSGKVFNEHPFLMTHMITHIGEKTSEDNQSgkalRKNFPHSFYKKSHAEGKMPKCVKHEKAFNQFPNLTRQNKT 190
Cdd:COG5048   210 SIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSP----SSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKG 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219862436 191 HTqeKLCECKDCWRTFLNQSSLKLHIRSHN----GDKHYVCKE--CGKAFSNSSHLIGHGRIHSGEKPYVCK--ECGKAF 262
Cdd:COG5048   286 FS--LPIKSKQCNISFSRSSPLTRHLRSVNhsgeSLKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKF 363

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1219862436 263 TQSTGLKLH--IRTHSGEKPYKCKE-----CGKAFTHSSYLTDHTRIHSGKKPYVCM--ECGKAFTRSTGLILHMRIHT 332
Cdd:COG5048   364 SPLLNNEPPqsLQQYKDLKNDKKSEtlsnsCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHT 442
zf-H2C2_2 pfam13465
Zinc-finger double domain;
295-320 3.78e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 3.78e-04
                          10        20
                  ....*....|....*....|....*.
gi 1219862436 295 YLTDHTRIHSGKKPYVCMECGKAFTR 320
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 281-303 7.08e-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: 36.51  E-value: 7.08e-04
                          10        20
                  ....*....|....*....|...
gi 1219862436 281 YKCKECGKAFTHSSYLTDHTRIH 303
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 253-275 1.25e-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: 1.25e-03
                          10        20
                  ....*....|....*....|...
gi 1219862436 253 YVCKECGKAFTQSTGLKLHIRTH 275
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
279-338 1.25e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.45  E-value: 1.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1219862436 279 KPYKCKECGKAFTHSSYLTDHTRIHSGKKPYVCMECGKAFTRSTGLIL--HMRIHTGEKPYE 338
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELsrHLRTHHNNPSDL 93
zf-H2C2_2 pfam13465
Zinc-finger double domain;
211-236 1.62e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 1.62e-03
                          10        20
                  ....*....|....*....|....*.
gi 1219862436 211 SLKLHIRSHNGDKHYVCKECGKAFSN 236
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
209-337 1.71e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.06  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219862436 209 QSSLKLHIRSHNGDKHYVCkecgkafSNSSHLIGHGRIHSGEKPYVCKECGKAFTQSTGLKLHIRTHSG-EKPYKCKECG 287
Cdd:COG5048   224 SSSLPLTTNSQLSPKSLLS-------QSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCN 296

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1219862436 288 KAFTHSSYLTDHTR--IHSGK--KPYVCME--CGKAFTRSTGLILHMRIHTGEKPY 337
Cdd:COG5048   297 ISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPA 352
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
207-280 2.28e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 39.68  E-value: 2.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1219862436 207 LNQSSLKLHIRSHNGDKHYVCKECGKAFSNSSHLIGHGRIHSGEKPYVCKECGKAFTQSTGLKL--HIRTHSGEKP 280
Cdd:COG5048    16 LSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELsrHLRTHHNNPS 91
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
169-311 2.74e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 39.29  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219862436 169 PKCVKHEKAFNQFPNLTRQNKT--HTQEKL----CECKDCWRTFLNQSSLKLHIRSHNGDKHYVCK--ECGKAFSNSSHL 240
Cdd:COG5048   290 IKSKQCNISFSRSSPLTRHLRSvnHSGESLkpfsCPYSLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNN 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219862436 241 IGHGRIH-----SGEKPYVC--KECGKAFTQSTGLKLHIRTHSGEKP--YKCKECGKAFTHSSYLTDHTRIHSGKKPYVC 311
Cdd:COG5048   370 EPPQSLQqykdlKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLC 449
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 225-247 4.89e-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: 4.89e-03
                          10        20
                  ....*....|....*....|...
gi 1219862436 225 YVCKECGKAFSNSSHLIGHGRIH 247
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 309-331 5.45e-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: 33.81  E-value: 5.45e-03
                          10        20
                  ....*....|....*....|...
gi 1219862436 309 YVCMECGKAFTRSTGLILHMRIH 331
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
110-312 6.10e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 38.14  E-value: 6.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219862436 110 EKLYDSNHSGKVFNEH-PFLMTHMITHIGEKTSEDNQSGKALRKNFPHSfykkSHAEGKMPKCVKHEKAFNQFPNLTRQN 188
Cdd:COG5048   149 NPLPGNNSSSVNTPQSnSLHPPLPANSLSKDPSSNLSLLISSNVSTSIP----SSSENSPLSSSYSIPSSSSDQNLENSS 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219862436 189 ---KTHTQEKLCECKDcwrTFLNQSSLKLHIRSHNGDKHYVCKECGKAFSNSSHLIGHGRIHSG-EKPYVCKECGKAFTQ 264
Cdd:COG5048   225 sslPLTTNSQLSPKSL---LSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSR 301

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1219862436 265 STGLKLHIRT--HSGE--KPYKCKE--CGKAFTHSSYLTDHTRIHSGKKPYVCM 312
Cdd:COG5048   302 SSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEK 355
zf-H2C2_2 pfam13465
Zinc-finger double domain;
239-264 7.34e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.50  E-value: 7.34e-03
                          10        20
                  ....*....|....*....|....*.
gi 1219862436 239 HLIGHGRIHSGEKPYVCKECGKAFTQ 264
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
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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