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Conserved domains on  [gi|599044121|ref|NP_055333|]
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zinc finger protein 229 isoform 1 [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 ...
33-74 2.32e-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: 2.32e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 599044121   33 PLSFKDVAVVFTEEELELLDSTQRQLYQDVMQENFRNLLSVG 74
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
375-787 3.01e-14

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 75.89  E-value: 3.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044121 375 RPYKCEECGKAFGRSSNLLVHQRVHTGEKPYKCSECGKGFSYSSV--LQVHQRLHTGEKPYTCSECGKGfcAKSALHKHQ 452
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPleLSRHLRTHHNNPSDLNSKSLPL--SNSKASSSS 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044121 453 HIHPGEKPYscgecgKGFSCSSHLSSHQKTHTGERPY--------QCDKCGKGFSHNSYLQAHQRVHMGQHlykcNVCGK 524
Cdd:COG5048  110 LSSSSSNSN------DNNLLSSHSLPPSSRDPQLPDLlsisnlrnNPLPGNNSSSVNTPQSNSLHPPLPAN----SLSKD 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044121 525 SFSYSSGLLMHQRLHTGEKPYKCECGKSFGRSSDLHIHQRVHTGEKPYKCSECGKGF------RRNSDLHSHQRVHTGER 598
Cdd:COG5048  180 PSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpksllsQSPSSLSSSDSSSSASE 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044121 599 PYVCDVCGKGFIYSSDLLIHQRVHTG-EKPYKCAECGKGFSYSSGLLIHQR--VHTGE--KPYRC--QECGKGFRCTSSL 671
Cdd:COG5048  260 SPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDAL 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044121 672 HKHQRVHTGKKPYTC--DQCGKGFSYGSNLRTHQRLH---------TGEKPYTCCEcgKGFRYGSGLLSHKRVHTGEKPY 740
Cdd:COG5048  340 KRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQqykdlkndkKSETLSNSCI--RNFKRDSNLSLHIITHLSFRPY 417
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 599044121 741 RCH--VCGKGYSQSSHLQGHQRVHTGEKPYKCEECGKGFGRNSCLHVHQ 787
Cdd:COG5048  418 NCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHGK 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 ...
33-74 2.32e-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: 2.32e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 599044121   33 PLSFKDVAVVFTEEELELLDSTQRQLYQDVMQENFRNLLSVG 74
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
34-74 5.40e-19

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 81.48  E-value: 5.40e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 599044121    34 LSFKDVAVVFTEEELELLDSTQRQLYQDVMQENFRNLLSVG 74
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLG 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
34-72 1.51e-14

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: 67.96  E-value: 1.51e-14
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 599044121  34 LSFKDVAVVFTEEELELLDSTQRQLYQDVMQENFRNLLS 72
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
375-787 3.01e-14

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 75.89  E-value: 3.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044121 375 RPYKCEECGKAFGRSSNLLVHQRVHTGEKPYKCSECGKGFSYSSV--LQVHQRLHTGEKPYTCSECGKGfcAKSALHKHQ 452
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPleLSRHLRTHHNNPSDLNSKSLPL--SNSKASSSS 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044121 453 HIHPGEKPYscgecgKGFSCSSHLSSHQKTHTGERPY--------QCDKCGKGFSHNSYLQAHQRVHMGQHlykcNVCGK 524
Cdd:COG5048  110 LSSSSSNSN------DNNLLSSHSLPPSSRDPQLPDLlsisnlrnNPLPGNNSSSVNTPQSNSLHPPLPAN----SLSKD 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044121 525 SFSYSSGLLMHQRLHTGEKPYKCECGKSFGRSSDLHIHQRVHTGEKPYKCSECGKGF------RRNSDLHSHQRVHTGER 598
Cdd:COG5048  180 PSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpksllsQSPSSLSSSDSSSSASE 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044121 599 PYVCDVCGKGFIYSSDLLIHQRVHTG-EKPYKCAECGKGFSYSSGLLIHQR--VHTGE--KPYRC--QECGKGFRCTSSL 671
Cdd:COG5048  260 SPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDAL 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044121 672 HKHQRVHTGKKPYTC--DQCGKGFSYGSNLRTHQRLH---------TGEKPYTCCEcgKGFRYGSGLLSHKRVHTGEKPY 740
Cdd:COG5048  340 KRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQqykdlkndkKSETLSNSCI--RNFKRDSNLSLHIITHLSFRPY 417
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 599044121 741 RCH--VCGKGYSQSSHLQGHQRVHTGEKPYKCEECGKGFGRNSCLHVHQ 787
Cdd:COG5048  418 NCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHGK 466
zf-H2C2_2 pfam13465
Zinc-finger double domain;
475-500 6.80e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 6.80e-04
                          10        20
                  ....*....|....*....|....*.
gi 599044121  475 HLSSHQKTHTGERPYQCDKCGKGFSH 500
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 ...
33-74 2.32e-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: 2.32e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 599044121   33 PLSFKDVAVVFTEEELELLDSTQRQLYQDVMQENFRNLLSVG 74
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
34-74 5.40e-19

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 81.48  E-value: 5.40e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 599044121    34 LSFKDVAVVFTEEELELLDSTQRQLYQDVMQENFRNLLSVG 74
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLG 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
34-72 1.51e-14

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: 67.96  E-value: 1.51e-14
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 599044121  34 LSFKDVAVVFTEEELELLDSTQRQLYQDVMQENFRNLLS 72
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
375-787 3.01e-14

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 75.89  E-value: 3.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044121 375 RPYKCEECGKAFGRSSNLLVHQRVHTGEKPYKCSECGKGFSYSSV--LQVHQRLHTGEKPYTCSECGKGfcAKSALHKHQ 452
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPleLSRHLRTHHNNPSDLNSKSLPL--SNSKASSSS 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044121 453 HIHPGEKPYscgecgKGFSCSSHLSSHQKTHTGERPY--------QCDKCGKGFSHNSYLQAHQRVHMGQHlykcNVCGK 524
Cdd:COG5048  110 LSSSSSNSN------DNNLLSSHSLPPSSRDPQLPDLlsisnlrnNPLPGNNSSSVNTPQSNSLHPPLPAN----SLSKD 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044121 525 SFSYSSGLLMHQRLHTGEKPYKCECGKSFGRSSDLHIHQRVHTGEKPYKCSECGKGF------RRNSDLHSHQRVHTGER 598
Cdd:COG5048  180 PSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpksllsQSPSSLSSSDSSSSASE 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044121 599 PYVCDVCGKGFIYSSDLLIHQRVHTG-EKPYKCAECGKGFSYSSGLLIHQR--VHTGE--KPYRC--QECGKGFRCTSSL 671
Cdd:COG5048  260 SPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDAL 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044121 672 HKHQRVHTGKKPYTC--DQCGKGFSYGSNLRTHQRLH---------TGEKPYTCCEcgKGFRYGSGLLSHKRVHTGEKPY 740
Cdd:COG5048  340 KRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQqykdlkndkKSETLSNSCI--RNFKRDSNLSLHIITHLSFRPY 417
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 599044121 741 RCH--VCGKGYSQSSHLQGHQRVHTGEKPYKCEECGKGFGRNSCLHVHQ 787
Cdd:COG5048  418 NCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHGK 466
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
403-824 7.32e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 68.57  E-value: 7.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044121 403 KPYKCSECGKGFSYSSVLQVHQRLHTGEKPYTCS--ECGKGFCAKSALHKHQHIHPGEKPY-SCGECGKGFSCSSHLSSH 479
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDlNSKSLPLSNSKASSSSLS 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044121 480 QKTHTGERPYQCDKCGKGFSHNSYLQ--AHQRVHMG-QHLYKCNVCGKSFSYSSGLLM-HQRLHTGEKPYKCecgksfgr 555
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLpdLLSISNLRnNPLPGNNSSSVNTPQSNSLHPpLPANSLSKDPSSN-------- 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044121 556 sSDLHIHQRVHTGEKPYKCSECGKGFRRNSDLHSHQRVHTgerpyvcdvcgkgfiYSSDLLIHQRVHTGEKPYKCAecgk 635
Cdd:COG5048  184 -LSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLEN---------------SSSSLPLTTNSQLSPKSLLSQ---- 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044121 636 gfSYSSGLLIHQRVHTGEkPYRCQECGKGFRCTSSLHKHQRVHTGK-KPYTCDQCGKGFSYGSNLRTHQR--LHTGE--K 710
Cdd:COG5048  244 --SPSSLSSSDSSSSASE-SPRSSLPTASSQSSSPNESDSSSEKGFsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044121 711 PYTCCE--CGKGFRYGSGLLSHKRVHTGEKPYRCH--VCGKGYSQSSHLQGHQRV--HTGEKPYKCEE-----CGKGFGR 779
Cdd:COG5048  321 PFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLqqYKDLKNDKKSEtlsnsCIRNFKR 400
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 599044121 780 NSCLHVHQRVHTGEKP--YTCGVCGKGFSYTSGLRNHQRVHLGENPY 824
Cdd:COG5048  401 DSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPL 447
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
736-818 4.48e-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: 4.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044121 736 GEKPYRCHV--CGKGYSQSSHLQ-----GHQRVHTGEKPykCEECGKGFGrnsclhvhqrvhTGEKPYTCGVCGKGFSYT 808
Cdd:COG5189  346 DGKPYKCPVegCNKKYKNQNGLKyhmlhGHQNQKLHENP--SPEKMNIFS------------AKDKPYRCEVCDKRYKNL 411
                         90
                 ....*....|
gi 599044121 809 SGLRNHqRVH 818
Cdd:COG5189  412 NGLKYH-RKH 420
zf-H2C2_2 pfam13465
Zinc-finger double domain;
475-500 6.80e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 6.80e-04
                          10        20
                  ....*....|....*....|....*.
gi 599044121  475 HLSSHQKTHTGERPYQCDKCGKGFSH 500
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
391-416 6.87e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 6.87e-04
                          10        20
                  ....*....|....*....|....*.
gi 599044121  391 NLLVHQRVHTGEKPYKCSECGKGFSY 416
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
498-595 9.34e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 42.40  E-value: 9.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044121 498 FSHNSYLQ----AHQRVHMGQHLYKCNV--CGKSFSYSSGLLMHqRLHTgekpykcECGKSFGRSSDLHIHQRVHTGEKP 571
Cdd:COG5189  327 LAHGGERNidtpSRMLKVKDGKPYKCPVegCNKKYKNQNGLKYH-MLHG-------HQNQKLHENPSPEKMNIFSAKDKP 398
                         90       100
                 ....*....|....*....|....
gi 599044121 572 YKCSECGKGFRRNSDLHSHqRVHT 595
Cdd:COG5189  399 YRCEVCDKRYKNLNGLKYH-RKHS 421
zf-H2C2_2 pfam13465
Zinc-finger double domain;
754-777 1.46e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.46e-03
                          10        20
                  ....*....|....*....|....
gi 599044121  754 HLQGHQRVHTGEKPYKCEECGKGF 777
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
541-607 1.54e-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: 1.54e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044121 541 GEKPYKCE---CGKSFGRSSDLHIHqRVHtgekpykcSECGKGFRRNSDLHSHQRVHTGERPYVCDVCGK 607
Cdd:COG5189  346 DGKPYKCPvegCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDK 406
zf-H2C2_2 pfam13465
Zinc-finger double domain;
614-639 3.31e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 3.31e-03
                          10        20
                  ....*....|....*....|....*.
gi 599044121  614 DLLIHQRVHTGEKPYKCAECGKGFSY 639
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
489-511 3.70e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.35  E-value: 3.70e-03
                          10        20
                  ....*....|....*....|...
gi 599044121  489 YQCDKCGKGFSHNSYLQAHQRVH 511
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
420-442 4.53e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 4.53e-03
                          10        20
                  ....*....|....*....|...
gi 599044121  420 LQVHQRLHTGEKPYTCSECGKGF 442
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
572-594 4.73e-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: 4.73e-03
                          10        20
                  ....*....|....*....|...
gi 599044121  572 YKCSECGKGFRRNSDLHSHQRVH 594
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
562-583 4.85e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.85e-03
                          10        20
                  ....*....|....*....|..
gi 599044121  562 HQRVHTGEKPYKCSECGKGFRR 583
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
727-751 4.94e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.94e-03
                          10        20
                  ....*....|....*....|....*
gi 599044121  727 LLSHKRVHTGEKPYRCHVCGKGYSQ 751
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
377-399 5.98e-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: 5.98e-03
                          10        20
                  ....*....|....*....|...
gi 599044121  377 YKCEECGKAFGRSSNLLVHQRVH 399
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
643-667 6.02e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 6.02e-03
                          10        20
                  ....*....|....*....|....*
gi 599044121  643 LLIHQRVHTGEKPYRCQECGKGFRC 667
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
673-695 8.08e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 8.08e-03
                          10        20
                  ....*....|....*....|...
gi 599044121  673 KHQRVHTGKKPYTCDQCGKGFSY 695
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
698-723 9.65e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 9.65e-03
                          10        20
                  ....*....|....*....|....*.
gi 599044121  698 NLRTHQRLHTGEKPYTCCECGKGFRY 723
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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