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Conserved domains on  [gi|203097452|ref|NP_001075954|]
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zinc finger protein 561 [Mus musculus]

Protein Classification

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

KRAB (Kruppel-associated box) domain-containing zinc finger protein (KRAB-ZFP) plays important roles in cell differentiation and organ development and in regulating viral replication and transcription; similar to Homo sapiens zinc finger protein 2 that may be involved in transcriptional regulation

Gene Ontology:  GO:0003677|GO:0008270|GO:0003700
PubMed:  8183940|14519192|22803940

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
41-97 4.85e-26

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 100.74  E-value: 4.85e-26
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 203097452    41 VTFDDVAVEFTPDEWTLLDLTQKNLYREVMLENYENLTSVGCQLFIPSLTPWLKQEE 97
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGE 57
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
397-588 2.64e-08

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 56.63  E-value: 2.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203097452 397 KSYKCMECGKAFLRWSGLTEHIR--VHTGE--KPYECKE--CGKTFSRSTQLTEHIRTHTGIKPYECKEcgkaftqysgl 470
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKL----------- 356

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203097452 471 athvRIHSGEKPFACKECGKAFTRTSGLIHHVRTHTGEKPFECVHCGKTFITSSHRTKHLKihSGEKPFVCNICGKAFIY 550
Cdd:COG5048  357 ----LNSSSKFSPLLNNEPPQSLQQYKDLKNDKKSETLSNSCIRNFKRDSNLSLHIITHLS--FRPYNCKNPPCSKSFNR 430

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 203097452 551 STSLNIHMRTHTgEKPYICKQCGKAFAVYSRLRKHSRV 588
Cdd:COG5048  431 HYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLSNHGKD 467
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 371-393 6.66e-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: 6.66e-03
                          10        20
                  ....*....|....*....|...
gi 203097452  371 FVCKECGKAFKNMSYLNDHVRIH 393
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
41-97 4.85e-26

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 100.74  E-value: 4.85e-26
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 203097452    41 VTFDDVAVEFTPDEWTLLDLTQKNLYREVMLENYENLTSVGCQLFIPSLTPWLKQEE 97
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGE 57
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 40-81 4.96e-23

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: 91.76  E-value: 4.96e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 203097452   40 SVTFDDVAVEFTPDEWTLLDLTQKNLYREVMLENYENLTSVG 81
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 41-79 3.89e-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: 77.97  E-value: 3.89e-18
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 203097452  41 VTFDDVAVEFTPDEWTLLDLTQKNLYREVMLENYENLTS 79
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
397-588 2.64e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 56.63  E-value: 2.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203097452 397 KSYKCMECGKAFLRWSGLTEHIR--VHTGE--KPYECKE--CGKTFSRSTQLTEHIRTHTGIKPYECKEcgkaftqysgl 470
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKL----------- 356

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203097452 471 athvRIHSGEKPFACKECGKAFTRTSGLIHHVRTHTGEKPFECVHCGKTFITSSHRTKHLKihSGEKPFVCNICGKAFIY 550
Cdd:COG5048  357 ----LNSSSKFSPLLNNEPPQSLQQYKDLKNDKKSETLSNSCIRNFKRDSNLSLHIITHLS--FRPYNCKNPPCSKSFNR 430

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 203097452 551 STSLNIHMRTHTgEKPYICKQCGKAFAVYSRLRKHSRV 588
Cdd:COG5048  431 HYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLSNHGKD 467
zf-H2C2_2 pfam13465
Zinc-finger double domain;
442-466 4.62e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 4.62e-05
                          10        20
                  ....*....|....*....|....*
gi 203097452  442 LTEHIRTHTGIKPYECKECGKAFTQ 466
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
PHA00733 PHA00733
hypothetical protein
 452-502 2.83e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 38.32  E-value: 2.83e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 203097452 452 IKPYECKECGKAFTQYSGLATHVRIHSGEKpfACKECGKAFTRTSGLIHHV 502
Cdd:PHA00733  71 VSPYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDHV 119
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 371-393 6.66e-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: 6.66e-03
                          10        20
                  ....*....|....*....|...
gi 203097452  371 FVCKECGKAFKNMSYLNDHVRIH 393
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
41-97 4.85e-26

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 100.74  E-value: 4.85e-26
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 203097452    41 VTFDDVAVEFTPDEWTLLDLTQKNLYREVMLENYENLTSVGCQLFIPSLTPWLKQEE 97
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGE 57
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 40-81 4.96e-23

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: 91.76  E-value: 4.96e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 203097452   40 SVTFDDVAVEFTPDEWTLLDLTQKNLYREVMLENYENLTSVG 81
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 41-79 3.89e-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: 77.97  E-value: 3.89e-18
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 203097452  41 VTFDDVAVEFTPDEWTLLDLTQKNLYREVMLENYENLTS 79
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
397-588 2.64e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 56.63  E-value: 2.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203097452 397 KSYKCMECGKAFLRWSGLTEHIR--VHTGE--KPYECKE--CGKTFSRSTQLTEHIRTHTGIKPYECKEcgkaftqysgl 470
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKL----------- 356

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203097452 471 athvRIHSGEKPFACKECGKAFTRTSGLIHHVRTHTGEKPFECVHCGKTFITSSHRTKHLKihSGEKPFVCNICGKAFIY 550
Cdd:COG5048  357 ----LNSSSKFSPLLNNEPPQSLQQYKDLKNDKKSETLSNSCIRNFKRDSNLSLHIITHLS--FRPYNCKNPPCSKSFNR 430

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 203097452 551 STSLNIHMRTHTgEKPYICKQCGKAFAVYSRLRKHSRV 588
Cdd:COG5048  431 HYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLSNHGKD 467
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
341-524 9.80e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 51.62  E-value: 9.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203097452 341 KSKVCKICGKSFANYSRLSAHVKTHNEE----KPFVCKE--CGKAFKNMSYLNDHVRIHTGIKSYKCMecgkaflrwsgL 414
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRSVNHSgeslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEK-----------L 356

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203097452 415 TEHIRVHTGEKPyeckecgktfSRSTQLTEHIRTHTGIKPYEC--KECGKAFTQYSGLATHVRIHSGEKP--FACKECGK 490
Cdd:COG5048  357 LNSSSKFSPLLN----------NEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSK 426

                        170       180       190
                 ....*....|....*....|....*....|....
gi 203097452 491 AFTRTSGLIHHVRTHTGEKPFECVHCGKTFITSS 524
Cdd:COG5048  427 SFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
zf-H2C2_2 pfam13465
Zinc-finger double domain;
442-466 4.62e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 4.62e-05
                          10        20
                  ....*....|....*....|....*
gi 203097452  442 LTEHIRTHTGIKPYECKECGKAFTQ 466
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
414-438 4.75e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 4.75e-05
                          10        20
                  ....*....|....*....|....*
gi 203097452  414 LTEHIRVHTGEKPYECKECGKTFSR 438
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
434-599 5.41e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.84  E-value: 5.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203097452 434 KTFSRSTQLTEHIRTHTGI-KPYECKECGKAFTQYSGLATHVR--IHSGE--KPFACKE--CGKAFTRTSGLIHHVRTHT 506
Cdd:COG5048  268 ASSQSSSPNESDSSSEKGFsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHT 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203097452 507 GEKPFECV--HCGKTFITSSHRTKHLKIH-----SGEKPFVC--NICGKAFI--YSTSLNIHMRTHTGEKPYICKQCGKA 575
Cdd:COG5048  348 SISPAKEKllNSSSKFSPLLNNEPPQSLQqykdlKNDKKSETlsNSCIRNFKrdSNLSLHIITHLSFRPYNCKNPPCSKS 427

                        170       180
                 ....*....|....*....|....
gi 203097452 576 FAVYSRLRKHSRVHTEEKPYQCEG 599
Cdd:COG5048  428 FNRHYNLIPHKKIHTNHAPLLCSI 451
zf-H2C2_2 pfam13465
Zinc-finger double domain;
470-494 9.35e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 9.35e-05
                          10        20
                  ....*....|....*....|....*
gi 203097452  470 LATHVRIHSGEKPFACKECGKAFTR 494
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 427-449 1.57e-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: 38.82  E-value: 1.57e-04
                          10        20
                  ....*....|....*....|...
gi 203097452  427 YECKECGKTFSRSTQLTEHIRTH 449
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
397-450 2.07e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.30  E-value: 2.07e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 203097452 397 KSYKCMECGKAFLRWSGLTEHIRVHTGEKPYEC--KECGKTFSRSTQLTEHIRTHT 450
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHH 87
zf-H2C2_2 pfam13465
Zinc-finger double domain;
553-577 2.37e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.37e-04
                          10        20
                  ....*....|....*....|....*
gi 203097452  553 SLNIHMRTHTGEKPYICKQCGKAFA 577
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 479-562 2.75e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 43.55  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203097452 479 GEKPFACK--ECGKAFTRTSGLIHHvRTHTgekpfecvHCGKTFITSSHRTKHLKIHSGEKPFVCNICGKAFIYSTSLNI 556
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLKYH-MLHG--------HQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                 ....*.
gi 203097452 557 HmRTHT 562
Cdd:COG5189  417 H-RKHS 421
zf-H2C2_2 pfam13465
Zinc-finger double domain;
385-410 3.22e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.22e-04
                          10        20
                  ....*....|....*....|....*.
gi 203097452  385 YLNDHVRIHTGIKSYKCMECGKAFLR 410
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 539-561 1.28e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.51  E-value: 1.28e-03
                          10        20
                  ....*....|....*....|...
gi 203097452  539 FVCNICGKAFIYSTSLNIHMRTH 561
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
425-483 1.79e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.22  E-value: 1.79e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 203097452 425 KPYECKECGKTFSRSTQLTEHIRTHTGIKPYEC--KECGKAFTQYSGLATHVRIHSGEKPF 483
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSD 92
PHA00733 PHA00733
hypothetical protein
 452-502 2.83e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 38.32  E-value: 2.83e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 203097452 452 IKPYECKECGKAFTQYSGLATHVRIHSGEKpfACKECGKAFTRTSGLIHHV 502
Cdd:PHA00733  71 VSPYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDHV 119
zf-H2C2_2 pfam13465
Zinc-finger double domain;
501-522 3.90e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 3.90e-03
                          10        20
                  ....*....|....*....|..
gi 203097452  501 HVRTHTGEKPFECVHCGKTFIT 522
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 483-505 4.00e-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: 34.97  E-value: 4.00e-03
                          10        20
                  ....*....|....*....|...
gi 203097452  483 FACKECGKAFTRTSGLIHHVRTH 505
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 371-393 6.66e-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: 6.66e-03
                          10        20
                  ....*....|....*....|...
gi 203097452  371 FVCKECGKAFKNMSYLNDHVRIH 393
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 455-477 6.92e-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: 6.92e-03
                          10        20
                  ....*....|....*....|...
gi 203097452  455 YECKECGKAFTQYSGLATHVRIH 477
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA00733 PHA00733
hypothetical protein
 426-474 7.60e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.16  E-value: 7.60e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 203097452 426 PYECKECGKTFSRSTQLTEHIR--THTGIKPYeckeCGKAFTQYSGLATHV 474
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRytEHSKVCPV----CGKEFRNTDSTLDHV 119
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 511-533 8.02e-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: 8.02e-03
                          10        20
                  ....*....|....*....|...
gi 203097452  511 FECVHCGKTFITSSHRTKHLKIH 533
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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