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Conserved domains on  [gi|322303718|ref|NP_001190179|]
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zinc finger protein 20 isoform 2 [Homo sapiens]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12016853)

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

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List of domain hits

Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
3-44 6.31e-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: 6.31e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 322303718    3 SVAFEDVAVSFTQEEWALLDPSQKNLYRDVMQETFKNLTSVG 44
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
112-522 8.76e-07

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 51.62  E-value: 8.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322303718 112 TGHSSLNTHIRADTGHKSSEYQEYGEN-PYRNKECKKAFSYLDSFQSHDKACTKEKPYD--GKECTETFISHSCIQRHRV 188
Cdd:COG5048    5 SSQSSSSNNSVLSSTPKSTLKSLSNAPrPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQcsYSGCDKSFSRPLELSRHLR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322303718 189 MHSGDGPYKC-KFCGKAFYFLNLCLIHERIHTGVKPYKCKQCGKAFTRSTTLPVHERTHTGVNADECKECGN-------A 260
Cdd:COG5048   85 THHNNPSDLNsKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSssvntpqS 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322303718 261 FSFPSEIRR---------------HKRSHTGEKPYECKQCGKVFISFSSIQYHKMTHTGEKPYECKQCGKAFRCGSHLQK 325
Cdd:COG5048  165 NSLHPPLPAnslskdpssnlslliSSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQS 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322303718 326 HGRTHTGEKPYECRQCGKAFRCTSDLQRHEKTHTE-------DKPYGCKQCGKGFRCASQLQIHERT--HSGE--KPHEC 394
Cdd:COG5048  245 PSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDsssekgfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSC 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322303718 395 KE--CGKVFKYFSSLRIHERTHTGEKPHECK--QCGKAF------RYFSSLHIHERTHTgDKPYECKV--CGKAFTCSSS 462
Cdd:COG5048  325 PYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFspllnnEPPQSLQQYKDLKN-DKKSETLSnsCIRNFKRDSN 403
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 322303718 463 IRYHERTHTGEKPYECK--HCGKAFISNYIRYHE-RTHTGEKPYQCKQCGKAFIRASSCREHE 522
Cdd:COG5048  404 LSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHkKIHTNHAPLLCSILKSFRRDLDLSNHGK 466
 
Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
3-44 6.31e-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: 6.31e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 322303718    3 SVAFEDVAVSFTQEEWALLDPSQKNLYRDVMQETFKNLTSVG 44
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
4-44 3.58e-23

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 92.66  E-value: 3.58e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 322303718     4 VAFEDVAVSFTQEEWALLDPSQKNLYRDVMQETFKNLTSVG 44
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLG 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
4-42 4.97e-20

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: 82.98  E-value: 4.97e-20
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 322303718   4 VAFEDVAVSFTQEEWALLDPSQKNLYRDVMQETFKNLTS 42
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
112-522 8.76e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 51.62  E-value: 8.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322303718 112 TGHSSLNTHIRADTGHKSSEYQEYGEN-PYRNKECKKAFSYLDSFQSHDKACTKEKPYD--GKECTETFISHSCIQRHRV 188
Cdd:COG5048    5 SSQSSSSNNSVLSSTPKSTLKSLSNAPrPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQcsYSGCDKSFSRPLELSRHLR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322303718 189 MHSGDGPYKC-KFCGKAFYFLNLCLIHERIHTGVKPYKCKQCGKAFTRSTTLPVHERTHTGVNADECKECGN-------A 260
Cdd:COG5048   85 THHNNPSDLNsKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSssvntpqS 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322303718 261 FSFPSEIRR---------------HKRSHTGEKPYECKQCGKVFISFSSIQYHKMTHTGEKPYECKQCGKAFRCGSHLQK 325
Cdd:COG5048  165 NSLHPPLPAnslskdpssnlslliSSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQS 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322303718 326 HGRTHTGEKPYECRQCGKAFRCTSDLQRHEKTHTE-------DKPYGCKQCGKGFRCASQLQIHERT--HSGE--KPHEC 394
Cdd:COG5048  245 PSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDsssekgfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSC 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322303718 395 KE--CGKVFKYFSSLRIHERTHTGEKPHECK--QCGKAF------RYFSSLHIHERTHTgDKPYECKV--CGKAFTCSSS 462
Cdd:COG5048  325 PYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFspllnnEPPQSLQQYKDLKN-DKKSETLSnsCIRNFKRDSN 403
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 322303718 463 IRYHERTHTGEKPYECK--HCGKAFISNYIRYHE-RTHTGEKPYQCKQCGKAFIRASSCREHE 522
Cdd:COG5048  404 LSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHkKIHTNHAPLLCSILKSFRRDLDLSNHGK 466
zf-H2C2_2 pfam13465
Zinc-finger double domain;
406-431 8.08e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 8.08e-04
                          10        20
                  ....*....|....*....|....*.
gi 322303718  406 SLRIHERTHTGEKPHECKQCGKAFRY 431
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
3-44 6.31e-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: 6.31e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 322303718    3 SVAFEDVAVSFTQEEWALLDPSQKNLYRDVMQETFKNLTSVG 44
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
4-44 3.58e-23

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 92.66  E-value: 3.58e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 322303718     4 VAFEDVAVSFTQEEWALLDPSQKNLYRDVMQETFKNLTSVG 44
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLG 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
4-42 4.97e-20

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: 82.98  E-value: 4.97e-20
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 322303718   4 VAFEDVAVSFTQEEWALLDPSQKNLYRDVMQETFKNLTS 42
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
112-522 8.76e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 51.62  E-value: 8.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322303718 112 TGHSSLNTHIRADTGHKSSEYQEYGEN-PYRNKECKKAFSYLDSFQSHDKACTKEKPYD--GKECTETFISHSCIQRHRV 188
Cdd:COG5048    5 SSQSSSSNNSVLSSTPKSTLKSLSNAPrPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQcsYSGCDKSFSRPLELSRHLR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322303718 189 MHSGDGPYKC-KFCGKAFYFLNLCLIHERIHTGVKPYKCKQCGKAFTRSTTLPVHERTHTGVNADECKECGN-------A 260
Cdd:COG5048   85 THHNNPSDLNsKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSssvntpqS 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322303718 261 FSFPSEIRR---------------HKRSHTGEKPYECKQCGKVFISFSSIQYHKMTHTGEKPYECKQCGKAFRCGSHLQK 325
Cdd:COG5048  165 NSLHPPLPAnslskdpssnlslliSSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQS 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322303718 326 HGRTHTGEKPYECRQCGKAFRCTSDLQRHEKTHTE-------DKPYGCKQCGKGFRCASQLQIHERT--HSGE--KPHEC 394
Cdd:COG5048  245 PSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDsssekgfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSC 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322303718 395 KE--CGKVFKYFSSLRIHERTHTGEKPHECK--QCGKAF------RYFSSLHIHERTHTgDKPYECKV--CGKAFTCSSS 462
Cdd:COG5048  325 PYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFspllnnEPPQSLQQYKDLKN-DKKSETLSnsCIRNFKRDSN 403
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 322303718 463 IRYHERTHTGEKPYECK--HCGKAFISNYIRYHE-RTHTGEKPYQCKQCGKAFIRASSCREHE 522
Cdd:COG5048  404 LSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHkKIHTNHAPLLCSILKSFRRDLDLSNHGK 466
zf-H2C2_2 pfam13465
Zinc-finger double domain;
406-431 8.08e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 8.08e-04
                          10        20
                  ....*....|....*....|....*.
gi 322303718  406 SLRIHERTHTGEKPHECKQCGKAFRY 431
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
266-291 1.17e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.17e-03
                          10        20
                  ....*....|....*....|....*.
gi 322303718  266 EIRRHKRSHTGEKPYECKQCGKVFIS 291
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
489-514 1.49e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.49e-03
                          10        20
                  ....*....|....*....|....*.
gi 322303718  489 YIRYHERTHTGEKPYQCKQCGKAFIR 514
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
464-487 2.20e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 2.20e-03
                          10        20
                  ....*....|....*....|....
gi 322303718  464 RYHERTHTGEKPYECKHCGKAFIS 487
Cdd:pfam13465   3 KRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
379-403 2.22e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 2.22e-03
                          10        20
                  ....*....|....*....|....*
gi 322303718  379 LQIHERTHSGEKPHECKECGKVFKY 403
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
444-498 2.51e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.47  E-value: 2.51e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 322303718 444 GDKPYECKV--CGKAFTCSSSIRYH---------------ERTHTG----EKPYECKHCGKAFIS-NYIRYHeRTHT 498
Cdd:COG5189  346 DGKPYKCPVegCNKKYKNQNGLKYHmlhghqnqklhenpsPEKMNIfsakDKPYRCEVCDKRYKNlNGLKYH-RKHS 421
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
304-387 2.67e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.09  E-value: 2.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322303718 304 GEKPYECK--QCGKAFRCGSHLQKHgRTHTgekpyecrQCGKAFRCTSDLQRHEKTHTEDKPYGCKQCGKGFRCASQLQI 381
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLKYH-MLHG--------HQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416

                 ....*.
gi 322303718 382 HeRTHS 387
Cdd:COG5189  417 H-RKHS 421
zf-H2C2_2 pfam13465
Zinc-finger double domain;
322-347 3.26e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 3.26e-03
                          10        20
                  ....*....|....*....|....*.
gi 322303718  322 HLQKHGRTHTGEKPYECRQCGKAFRC 347
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
438-459 4.21e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 4.21e-03
                          10        20
                  ....*....|....*....|..
gi 322303718  438 HERTHTGDKPYECKVCGKAFTC 459
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
214-235 4.51e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 4.51e-03
                          10        20
                  ....*....|....*....|..
gi 322303718  214 HERIHTGVKPYKCKQCGKAFTR 235
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
388-471 5.35e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 39.32  E-value: 5.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322303718 388 GEKPHECK--ECGKVFKYFSSLRIHERT-HTGEKPHECKQCGKafryfsslhiHERTHTGDKPYECKVCGKAFTCSSSIR 464
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLKYHMLHgHQNQKLHENPSPEK----------MNIFSAKDKPYRCEVCDKRYKNLNGLK 415

                 ....*..
gi 322303718 465 YHeRTHT 471
Cdd:COG5189  416 YH-RKHS 421
zf-H2C2_2 pfam13465
Zinc-finger double domain;
296-319 6.42e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 6.42e-03
                          10        20
                  ....*....|....*....|....
gi 322303718  296 QYHKMTHTGEKPYECKQCGKAFRC 319
Cdd:pfam13465   3 KRHMRTHTGEKPYKCPECGKSFKS 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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