NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|142383655|ref|NP_001001180|]
View 

uncharacterized protein LOC407812 [Mus musculus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
3-43 4.90e-21

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: 86.37  E-value: 4.90e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 142383655    3 PMTFDDVAIIFSPEEWECLDSAQRDLYRDVMVENCRNLLSV 43
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
322-642 3.02e-07

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.55  E-value: 3.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142383655 322 SHQSLKDLQSSHLQDEAYKCEGCVLTFRQKSDLLEHQKTHGRAKSYKCG--ECGKAFSSCSDLNVHQRSHDGENPHEC-K 398
Cdd:COG5048   17 SSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNsK 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142383655 399 ECGRAFASGRALARHQHTHTGKKSYICEECGKNFKKGSNLNQHLRIHTGEKPFKCEDC-GLAFNQSSHLAKHQRIYAGEC 477
Cdd:COG5048   97 SLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnSSSVNTPQSNSLHPPLPANSL 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142383655 478 GRSFVKCSTSRRCHSIRPGAKPHKCKQCGKTFVDISKLTQHQNVHTGEKPFKCNECGKAFNSGLSLKQHQVVHTGEKPYK 557
Cdd:COG5048  177 SKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSS 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142383655 558 CKECEKAFTQIAKLTEHQRVHTGE-------KPYECKECGKAFRNFSAFNYHHRT--HTGE--KPYECKE--CGKAFTKS 624
Cdd:COG5048  257 ASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRN 336
                        330
                 ....*....|....*...
gi 142383655 625 SDLKRHHRIHSGEKPYKC 642
Cdd:COG5048  337 DALKRHILLHTSISPAKE 354
 
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 ...
3-43 4.90e-21

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: 86.37  E-value: 4.90e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 142383655    3 PMTFDDVAIIFSPEEWECLDSAQRDLYRDVMVENCRNLLSV 43
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB smart00349
krueppel associated box;
4-44 6.91e-21

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 86.49  E-value: 6.91e-21
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 142383655     4 MTFDDVAIIFSPEEWECLDSAQRDLYRDVMVENCRNLLSVE 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 3.84e-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: 3.84e-18
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 142383655   4 MTFDDVAIIFSPEEWECLDSAQRDLYRDVMVENCRNLLS 42
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
322-642 3.02e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.55  E-value: 3.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142383655 322 SHQSLKDLQSSHLQDEAYKCEGCVLTFRQKSDLLEHQKTHGRAKSYKCG--ECGKAFSSCSDLNVHQRSHDGENPHEC-K 398
Cdd:COG5048   17 SSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNsK 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142383655 399 ECGRAFASGRALARHQHTHTGKKSYICEECGKNFKKGSNLNQHLRIHTGEKPFKCEDC-GLAFNQSSHLAKHQRIYAGEC 477
Cdd:COG5048   97 SLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnSSSVNTPQSNSLHPPLPANSL 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142383655 478 GRSFVKCSTSRRCHSIRPGAKPHKCKQCGKTFVDISKLTQHQNVHTGEKPFKCNECGKAFNSGLSLKQHQVVHTGEKPYK 557
Cdd:COG5048  177 SKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSS 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142383655 558 CKECEKAFTQIAKLTEHQRVHTGE-------KPYECKECGKAFRNFSAFNYHHRT--HTGE--KPYECKE--CGKAFTKS 624
Cdd:COG5048  257 ASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRN 336
                        330
                 ....*....|....*...
gi 142383655 625 SDLKRHHRIHSGEKPYKC 642
Cdd:COG5048  337 DALKRHILLHTSISPAKE 354
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
500-550 3.27e-05

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 42.54  E-value: 3.27e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 142383655 500 HKCKQCGKTFVDISKLTQHQNvhtgEKPFKCNECGKAFNSGLSLKQH-QVVH 550
Cdd:cd20908    2 PWCYYCDREFDDEKILIQHQK----AKHFKCHICHKKLYTAGGLAVHcLQVH 49
zf-H2C2_2 pfam13465
Zinc-finger double domain;
626-650 1.39e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.39e-04
                          10        20
                  ....*....|....*....|....*
gi 142383655  626 DLKRHHRIHSGEKPYKCNECGKAFA 650
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
 
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 ...
3-43 4.90e-21

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: 86.37  E-value: 4.90e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 142383655    3 PMTFDDVAIIFSPEEWECLDSAQRDLYRDVMVENCRNLLSV 43
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB smart00349
krueppel associated box;
4-44 6.91e-21

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 86.49  E-value: 6.91e-21
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 142383655     4 MTFDDVAIIFSPEEWECLDSAQRDLYRDVMVENCRNLLSVE 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 3.84e-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: 3.84e-18
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 142383655   4 MTFDDVAIIFSPEEWECLDSAQRDLYRDVMVENCRNLLS 42
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
322-642 3.02e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.55  E-value: 3.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142383655 322 SHQSLKDLQSSHLQDEAYKCEGCVLTFRQKSDLLEHQKTHGRAKSYKCG--ECGKAFSSCSDLNVHQRSHDGENPHEC-K 398
Cdd:COG5048   17 SSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNsK 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142383655 399 ECGRAFASGRALARHQHTHTGKKSYICEECGKNFKKGSNLNQHLRIHTGEKPFKCEDC-GLAFNQSSHLAKHQRIYAGEC 477
Cdd:COG5048   97 SLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnSSSVNTPQSNSLHPPLPANSL 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142383655 478 GRSFVKCSTSRRCHSIRPGAKPHKCKQCGKTFVDISKLTQHQNVHTGEKPFKCNECGKAFNSGLSLKQHQVVHTGEKPYK 557
Cdd:COG5048  177 SKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSS 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142383655 558 CKECEKAFTQIAKLTEHQRVHTGE-------KPYECKECGKAFRNFSAFNYHHRT--HTGE--KPYECKE--CGKAFTKS 624
Cdd:COG5048  257 ASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRN 336
                        330
                 ....*....|....*...
gi 142383655 625 SDLKRHHRIHSGEKPYKC 642
Cdd:COG5048  337 DALKRHILLHTSISPAKE 354
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
377-652 1.12e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.54  E-value: 1.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142383655 377 SSCSDLNVHQRSHDGENPHECKECGRAFASGRALARHQHTHTGKKSYICEECGKNFKKGSNLNQHLRIHTGEKPFKCEDC 456
Cdd:COG5048  181 SSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASES 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142383655 457 GLAFNQSSHLAKHQRIYagecgrsfvKCSTSRRCHSirpgaKPHKCKQCGKTFVDISKLTQHQN--VHTGE--KPFKCNE 532
Cdd:COG5048  261 PRSSLPTASSQSSSPNE---------SDSSSEKGFS-----LPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPY 326
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142383655 533 --CGKAFNSGLSLKQHQVVHTGEKPYKCK--ECEKAFTQIAKLTEHQRVH-----TGEKPYEC--KECGKAFRNFSAFNY 601
Cdd:COG5048  327 slCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQqykdlKNDKKSETlsNSCIRNFKRDSNLSL 406
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 142383655 602 HHRTHTGEKPYECK--ECGKAFTKSSDLKRHHRIHSGEKPYKCNECGKAFAMN 652
Cdd:COG5048  407 HIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDL 459
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
500-550 3.27e-05

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 42.54  E-value: 3.27e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 142383655 500 HKCKQCGKTFVDISKLTQHQNvhtgEKPFKCNECGKAFNSGLSLKQH-QVVH 550
Cdd:cd20908    2 PWCYYCDREFDDEKILIQHQK----AKHFKCHICHKKLYTAGGLAVHcLQVH 49
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
524-607 5.07e-05

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 46.25  E-value: 5.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142383655 524 GEKPFKCN--ECGKAFNSGLSLKQHQvvhtgekpyKCKECEKAFTQIAKLTEHQRVHTGEKPYECKECGKAFRNFSAFNY 601
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLKYHM---------LHGHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416

                 ....*.
gi 142383655 602 hHRTHT 607
Cdd:COG5189  417 -HRKHS 421
zf-H2C2_2 pfam13465
Zinc-finger double domain;
626-650 1.39e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.39e-04
                          10        20
                  ....*....|....*....|....*
gi 142383655  626 DLKRHHRIHSGEKPYKCNECGKAFA 650
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
372-602 2.11e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.30  E-value: 2.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142383655 372 CGKAFSSCSDLNVHQRSHDgeNPHECKECGRAFASGRALARHQHTHTG-------KKSYICEECGKNFKKGSNLNQHLR- 443
Cdd:COG5048  234 QLSPKSLLSQSPSSLSSSD--SSSSASESPRSSLPTASSQSSSPNESDsssekgfSLPIKSKQCNISFSRSSPLTRHLRs 311
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142383655 444 -IHTGE--KPFKC--EDCGLAFNQSSHLAKHQRIYAGecgRSFVKCSTSRRCHSIRPgAKPHKCKQCGKTFVDISKLTQH 518
Cdd:COG5048  312 vNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTS---ISPAKEKLLNSSSKFSP-LLNNEPPQSLQQYKDLKNDKKS 387
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142383655 519 QNVHtgekpfkcNECGKAFNSGLSLKQHQVVHTGEKP--YKCKECEKAFTQIAKLTEHQRVHTGEKPYECKECGKAFRNF 596
Cdd:COG5048  388 ETLS--------NSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDL 459

                 ....*.
gi 142383655 597 SAFNYH 602
Cdd:COG5048  460 DLSNHG 465
zf-H2C2_2 pfam13465
Zinc-finger double domain;
437-462 2.76e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.76e-04
                          10        20
                  ....*....|....*....|....*.
gi 142383655  437 NLNQHLRIHTGEKPFKCEDCGLAFNQ 462
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
542-567 5.18e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 5.18e-04
                          10        20
                  ....*....|....*....|....*.
gi 142383655  542 SLKQHQVVHTGEKPYKCKECEKAFTQ 567
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
571-595 8.14e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 8.14e-04
                          10        20
                  ....*....|....*....|....*
gi 142383655  571 LTEHQRVHTGEKPYECKECGKAFRN 595
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
580-663 1.16e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 42.01  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142383655 580 GEKPYECK--ECGKAFRNFSAFNYHhRTHtgekpyecKECGKAFTKSSDLKRHHRIHSGEKPYKCNECGKAFAMNVSLRE 657
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416

                 ....*.
gi 142383655 658 HqRVHS 663
Cdd:COG5189  417 H-RKHS 421
zf-H2C2_2 pfam13465
Zinc-finger double domain;
598-623 1.38e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.38e-03
                          10        20
                  ....*....|....*....|....*.
gi 142383655  598 AFNYHHRTHTGEKPYECKECGKAFTK 623
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
612-634 1.83e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.12  E-value: 1.83e-03
                          10        20
                  ....*....|....*....|...
gi 142383655  612 YECKECGKAFTKSSDLKRHHRIH 634
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
515-539 2.11e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.11e-03
                          10        20
                  ....*....|....*....|....*
gi 142383655  515 LTQHQNVHTGEKPFKCNECGKAFNS 539
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
367-389 7.90e-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: 7.90e-03
                          10        20
                  ....*....|....*....|...
gi 142383655  367 YKCGECGKAFSSCSDLNVHQRSH 389
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH