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Conserved domains on  [gi|34785715|gb|AAH57313|]
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Zfp715 protein [Mus musculus]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204378)

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 smart00349
krueppel associated box;
48-105 4.48e-26

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 101.52  E-value: 4.48e-26
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 34785715     48 MSFEDVTVNFSQEEWQHLDSAQRCLYQEVMLEIYSHLLAVGYSIPSPGVIFRMEKGKE 105
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEE 58
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
410-812 3.07e-14

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 75.89  E-value: 3.07e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785715 410 TPFICDICGKAFLRKSELTSHKQCHNGEKPYKCND--CEKSFKFPSQLKVHHQIHTGEKPYECR-ECGKSFSKTAKLKVH 486
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSkSLPLSNSKASSSSLS 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785715 487 QRIHTGEKPYVCSQCGKAFNQKSILDRHEKLHPGEKPYKCNDCGKS-------FNYPSQLKVHCHSHTgekPYKCHECGK 559
Cdd:COG5048 112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSsvntpqsNSLHPPLPANSLSKD---PSSNLSLLI 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785715 560 SFNFPCELKVHYQNHTGEKPYKcrecwKLFSKMSQLKAHYRVhtgerPYKCSHCGKAFSTKEQVQEHERIHTGEKPFVCT 639
Cdd:COG5048 189 SSNVSTSIPSSSENSPLSSSYS-----IPSSSSDQNLENSSS-----SLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSAS 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785715 640 ECGKAFSSRSSFRKHQLIHT-------KEKPFVSQKCETGL-QEATLIPHQQ--LHIGE--KPYKCP--DCGKLFNYPSQ 705
Cdd:COG5048 259 ESPRSSLPTASSQSSSPNESdsssekgFSLPIKSKQCNISFsRSSPLTRHLRsvNHSGEslKPFSCPysLCGKLFSRNDA 338
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785715 706 LKSHYQIHTGEKPCKCP--DCGKSFS------KTSQLKAHSRIHTgERPYVCSV--CGKAFKQLSTLSRHEKIHMVEKP- 774
Cdd:COG5048 339 LKRHILLHTSISPAKEKllNSSSKFSpllnnePPQSLQQYKDLKN-DKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPy 417
                       410       420       430
                ....*....|....*....|....*....|....*....
gi 34785715 775 -YKCSFCGKSFCSPSELKVHLLIHTGERPYkCSSCWKAF 812
Cdd:COG5048 418 nCKNPPCSKSFNRHYNLIPHKKIHTNHAPL-LCSILKSF 455
zf-H2C2_2 pfam13465
Zinc-finger double domain;
818-838 6.64e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 6.64e-03
                          10        20
                  ....*....|....*....|.
gi 34785715   818 LQEHERIHTGERPYVCTHCGK 838
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGK 22
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
48-105 4.48e-26

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 101.52  E-value: 4.48e-26
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 34785715     48 MSFEDVTVNFSQEEWQHLDSAQRCLYQEVMLEIYSHLLAVGYSIPSPGVIFRMEKGKE 105
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEE 58
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
48-88 2.46e-19

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: 81.75  E-value: 2.46e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 34785715    48 MSFEDVTVNFSQEEWQHLDSAQRCLYQEVMLEIYSHLLAVG 88
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
48-84 2.93e-15

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: 70.27  E-value: 2.93e-15
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 34785715  48 MSFEDVTVNFSQEEWQHLDSAQRCLYQEVMLEIYSHL 84
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENL 37
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
410-812 3.07e-14

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 75.89  E-value: 3.07e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785715 410 TPFICDICGKAFLRKSELTSHKQCHNGEKPYKCND--CEKSFKFPSQLKVHHQIHTGEKPYECR-ECGKSFSKTAKLKVH 486
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSkSLPLSNSKASSSSLS 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785715 487 QRIHTGEKPYVCSQCGKAFNQKSILDRHEKLHPGEKPYKCNDCGKS-------FNYPSQLKVHCHSHTgekPYKCHECGK 559
Cdd:COG5048 112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSsvntpqsNSLHPPLPANSLSKD---PSSNLSLLI 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785715 560 SFNFPCELKVHYQNHTGEKPYKcrecwKLFSKMSQLKAHYRVhtgerPYKCSHCGKAFSTKEQVQEHERIHTGEKPFVCT 639
Cdd:COG5048 189 SSNVSTSIPSSSENSPLSSSYS-----IPSSSSDQNLENSSS-----SLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSAS 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785715 640 ECGKAFSSRSSFRKHQLIHT-------KEKPFVSQKCETGL-QEATLIPHQQ--LHIGE--KPYKCP--DCGKLFNYPSQ 705
Cdd:COG5048 259 ESPRSSLPTASSQSSSPNESdsssekgFSLPIKSKQCNISFsRSSPLTRHLRsvNHSGEslKPFSCPysLCGKLFSRNDA 338
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785715 706 LKSHYQIHTGEKPCKCP--DCGKSFS------KTSQLKAHSRIHTgERPYVCSV--CGKAFKQLSTLSRHEKIHMVEKP- 774
Cdd:COG5048 339 LKRHILLHTSISPAKEKllNSSSKFSpllnnePPQSLQQYKDLKN-DKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPy 417
                       410       420       430
                ....*....|....*....|....*....|....*....
gi 34785715 775 -YKCSFCGKSFCSPSELKVHLLIHTGERPYkCSSCWKAF 812
Cdd:COG5048 418 nCKNPPCSKSFNRHYNLIPHKKIHTNHAPL-LCSILKSF 455
zf-H2C2_2 pfam13465
Zinc-finger double domain;
483-507 1.26e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 1.26e-04
                          10        20
                  ....*....|....*....|....*
gi 34785715   483 LKVHQRIHTGEKPYVCSQCGKAFNQ 507
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
818-838 6.64e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 6.64e-03
                          10        20
                  ....*....|....*....|.
gi 34785715   818 LQEHERIHTGERPYVCTHCGK 838
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGK 22
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
48-105 4.48e-26

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 101.52  E-value: 4.48e-26
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 34785715     48 MSFEDVTVNFSQEEWQHLDSAQRCLYQEVMLEIYSHLLAVGYSIPSPGVIFRMEKGKE 105
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEE 58
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
48-88 2.46e-19

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: 81.75  E-value: 2.46e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 34785715    48 MSFEDVTVNFSQEEWQHLDSAQRCLYQEVMLEIYSHLLAVG 88
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
48-84 2.93e-15

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: 70.27  E-value: 2.93e-15
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 34785715  48 MSFEDVTVNFSQEEWQHLDSAQRCLYQEVMLEIYSHL 84
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENL 37
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
410-812 3.07e-14

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 75.89  E-value: 3.07e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785715 410 TPFICDICGKAFLRKSELTSHKQCHNGEKPYKCND--CEKSFKFPSQLKVHHQIHTGEKPYECR-ECGKSFSKTAKLKVH 486
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSkSLPLSNSKASSSSLS 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785715 487 QRIHTGEKPYVCSQCGKAFNQKSILDRHEKLHPGEKPYKCNDCGKS-------FNYPSQLKVHCHSHTgekPYKCHECGK 559
Cdd:COG5048 112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSsvntpqsNSLHPPLPANSLSKD---PSSNLSLLI 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785715 560 SFNFPCELKVHYQNHTGEKPYKcrecwKLFSKMSQLKAHYRVhtgerPYKCSHCGKAFSTKEQVQEHERIHTGEKPFVCT 639
Cdd:COG5048 189 SSNVSTSIPSSSENSPLSSSYS-----IPSSSSDQNLENSSS-----SLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSAS 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785715 640 ECGKAFSSRSSFRKHQLIHT-------KEKPFVSQKCETGL-QEATLIPHQQ--LHIGE--KPYKCP--DCGKLFNYPSQ 705
Cdd:COG5048 259 ESPRSSLPTASSQSSSPNESdsssekgFSLPIKSKQCNISFsRSSPLTRHLRsvNHSGEslKPFSCPysLCGKLFSRNDA 338
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785715 706 LKSHYQIHTGEKPCKCP--DCGKSFS------KTSQLKAHSRIHTgERPYVCSV--CGKAFKQLSTLSRHEKIHMVEKP- 774
Cdd:COG5048 339 LKRHILLHTSISPAKEKllNSSSKFSpllnnePPQSLQQYKDLKN-DKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPy 417
                       410       420       430
                ....*....|....*....|....*....|....*....
gi 34785715 775 -YKCSFCGKSFCSPSELKVHLLIHTGERPYkCSSCWKAF 812
Cdd:COG5048 418 nCKNPPCSKSFNRHYNLIPHKKIHTNHAPL-LCSILKSF 455
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
354-766 6.26e-14

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 75.12  E-value: 6.26e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785715 354 DPYKCSSCEKSFCNAAALQQHEQIHTEEKLYVCTL--CGKAFSDGSAFYEHELIHKNHTPFICDICG---KAFLRKSELT 428
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLplsNSKASSSSLS 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785715 429 SHkqCHNGEKPYKCNDCEKSFKFPSQLKVHHQIHTGEKPYECRECGKSFSKTaklKVHQRIHtGEKPYVCSQCGKAFNQK 508
Cdd:COG5048 112 SS--SSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNT---PQSNSLH-PPLPANSLSKDPSSNLS 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785715 509 SILdrHEKLHPGEKPYKCNDCGKSFNYPSQLKVHCHSHTGEKPYKCHECgkSFNFPCELKVHYQNHTGEKPYKCRECWKL 588
Cdd:COG5048 186 LLI--SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTN--SQLSPKSLLSQSPSSLSSSDSSSSASESP 261
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785715 589 FS----KMSQLKAHYRVHTGER-----PYKCSHCGKAFSTKEQVQEHER--IHTGE--KPFVCTE--CGKAFSSRSSFRK 653
Cdd:COG5048 262 RSslptASSQSSSPNESDSSSEkgfslPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKR 341
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785715 654 HQLIHTKEKPF---------VSQKCETGLQEATLIPHQQLHIgEKPYKCPDCGKLFNYPSQ--LKSHYQIHTGEKP--CK 720
Cdd:COG5048 342 HILLHTSISPAkekllnsssKFSPLLNNEPPQSLQQYKDLKN-DKKSETLSNSCIRNFKRDsnLSLHIITHLSFRPynCK 420
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*.
gi 34785715 721 CPDCGKSFSKTSQLKAHSRIHTGERPYVCSVCGKAFKQLSTLSRHE 766
Cdd:COG5048 421 NPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHGK 466
zf-H2C2_2 pfam13465
Zinc-finger double domain;
483-507 1.26e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 1.26e-04
                          10        20
                  ....*....|....*....|....*
gi 34785715   483 LKVHQRIHTGEKPYVCSQCGKAFNQ 507
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
686-767 1.36e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 45.09  E-value: 1.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785715 686 IGEKPYKCP--DCGKLFNYPSQLKSH-YQIHTGEKPCKCPDCGKsfsktsqlkaHSRIHTGERPYVCSVCGKAFKQLSTL 762
Cdd:COG5189 345 KDGKPYKCPveGCNKKYKNQNGLKYHmLHGHQNQKLHENPSPEK----------MNIFSAKDKPYRCEVCDKRYKNLNGL 414

                ....*
gi 34785715 763 SRHEK 767
Cdd:COG5189 415 KYHRK 419
zf-H2C2_2 pfam13465
Zinc-finger double domain;
762-784 2.98e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.98e-04
                          10        20
                  ....*....|....*....|...
gi 34785715   762 LSRHEKIHMVEKPYKCSFCGKSF 784
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
734-758 4.12e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 4.12e-04
                          10        20
                  ....*....|....*....|....*
gi 34785715   734 LKAHSRIHTGERPYVCSVCGKAFKQ 758
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
624-647 4.20e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 4.20e-04
                          10        20
                  ....*....|....*....|....
gi 34785715   624 QEHERIHTGEKPFVCTECGKAFSS 647
Cdd:pfam13465   3 KRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
511-535 4.55e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 4.55e-04
                          10        20
                  ....*....|....*....|....*
gi 34785715   511 LDRHEKLHPGEKPYKCNDCGKSFNY 535
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
539-562 5.53e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 5.53e-04
                          10        20
                  ....*....|....*....|....
gi 34785715   539 LKVHCHSHTGEKPYKCHECGKSFN 562
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
595-619 8.69e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 8.69e-04
                          10        20
                  ....*....|....*....|....*
gi 34785715   595 LKAHYRVHTGERPYKCSHCGKAFST 619
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
455-479 1.09e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 1.09e-03
                          10        20
                  ....*....|....*....|....*
gi 34785715   455 LKVHHQIHTGEKPYECRECGKSFSK 479
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
632-709 2.44e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 41.24  E-value: 2.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785715 632 GEKPFVC--TECGKAFSSRSSFRKHQLiHTKEKPFVSQKCETglqeatlIPHQQLHIGEKPYKCPDCGKLFNYPSQLKSH 709
Cdd:COG5189 346 DGKPYKCpvEGCNKKYKNQNGLKYHML-HGHQNQKLHENPSP-------EKMNIFSAKDKPYRCEVCDKRYKNLNGLKYH 417
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
716-793 3.51e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.86  E-value: 3.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785715 716 EKPCKCPDCGKSFSKTSQLKAH---SRIHT-GERPYVCSV--CGKAFKQLSTLSRHEK-------------------IHM 770
Cdd:COG5189 315 KLPCTNSSSNGKLAHGGERNIDtpsRMLKVkDGKPYKCPVegCNKKYKNQNGLKYHMLhghqnqklhenpspekmniFSA 394
                        90       100
                ....*....|....*....|...
gi 34785715 771 VEKPYKCSFCGKSFCSPSELKVH 793
Cdd:COG5189 395 KDKPYRCEVCDKRYKNLNGLKYH 417
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
393-546 3.66e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.86  E-value: 3.66e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785715 393 FSDGSAFYEHELIHKNHTpfICDICGkAFLRKSELTSHKQCHNGEK--PYKCNDCEKSFKFPSQLkvhhQIHTGEKPYEC 470
Cdd:COG5189 280 FEESSLGFDYEFIHKSVG--NKEIRG-GISTGEMIDVRKLPCTNSSsnGKLAHGGERNIDTPSRM----LKVKDGKPYKC 352
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34785715 471 R--ECGKSFSKTAKLKVHqRIHtgekpyvcSQCGKAFNQKSILDRHEKLHPGEKPYKCNDCGKSFNYPSQLKVH-CHSH 546
Cdd:COG5189 353 PveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKYHrKHSH 422
zf-H2C2_2 pfam13465
Zinc-finger double domain;
818-838 6.64e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 6.64e-03
                          10        20
                  ....*....|....*....|.
gi 34785715   818 LQEHERIHTGERPYVCTHCGK 838
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGK 22
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
775-797 7.00e-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: 34.58  E-value: 7.00e-03
                          10        20
                  ....*....|....*....|...
gi 34785715   775 YKCSFCGKSFCSPSELKVHLLIH 797
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
636-658 7.50e-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: 7.50e-03
                          10        20
                  ....*....|....*....|...
gi 34785715   636 FVCTECGKAFSSRSSFRKHQLIH 658
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
706-730 9.01e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 9.01e-03
                          10        20
                  ....*....|....*....|....*
gi 34785715   706 LKSHYQIHTGEKPCKCPDCGKSFSK 730
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 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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