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Conserved domains on  [gi|599044318|ref|NP_001265439|]
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zinc finger protein 229 isoform 2 [Homo sapiens]

Protein Classification

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

KRAB (Kruppel-associated box) domain-containing zinc finger protein (KRAB-ZFP) plays important roles in cell differentiation and organ development and in regulating viral replication and transcription

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 33-74 2.30e-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: 2.30e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 599044318   33 PLSFKDVAVVFTEEELELLDSTQRQLYQDVMQENFRNLLSVG 74
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
369-781 2.95e-14

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 75.89  E-value: 2.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044318 369 RPYKCEECGKAFGRSSNLLVHQRVHTGEKPYKCSECGKGFSYSSV--LQVHQRLHTGEKPYTCSECGKGfcAKSALHKHQ 446
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPleLSRHLRTHHNNPSDLNSKSLPL--SNSKASSSS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044318 447 HIHPGEKPYscgecgKGFSCSSHLSSHQKTHTGERPY--------QCDKCGKGFSHNSYLQAHQRVHMGQHlykcNVCGK 518
Cdd:COG5048  110 LSSSSSNSN------DNNLLSSHSLPPSSRDPQLPDLlsisnlrnNPLPGNNSSSVNTPQSNSLHPPLPAN----SLSKD 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044318 519 SFSYSSGLLMHQRLHTGEKPYKCECGKSFGRSSDLHIHQRVHTGEKPYKCSECGKGF------RRNSDLHSHQRVHTGER 592
Cdd:COG5048  180 PSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpksllsQSPSSLSSSDSSSSASE 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044318 593 PYVCDVCGKGFIYSSDLLIHQRVHTG-EKPYKCAECGKGFSYSSGLLIHQR--VHTGE--KPYRC--QECGKGFRCTSSL 665
Cdd:COG5048  260 SPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDAL 339

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044318 666 HKHQRVHTGKKPYTC--DQCGKGFSYGSNLRTHQRLH---------TGEKPYTCCEcgKGFRYGSGLLSHKRVHTGEKPY 734
Cdd:COG5048  340 KRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQqykdlkndkKSETLSNSCI--RNFKRDSNLSLHIITHLSFRPY 417

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 599044318 735 RCH--VCGKGYSQSSHLQGHQRVHTGEKPYKCEECGKGFGRNSCLHVHQ 781
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 2.30e-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: 2.30e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 599044318   33 PLSFKDVAVVFTEEELELLDSTQRQLYQDVMQENFRNLLSVG 74
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
34-76 4.91e-19

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 81.48  E-value: 4.91e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 599044318    34 LSFKDVAVVFTEEELELLDSTQRQLYQDVMQENFRNLLSVGDK 76
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQ 43
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 34-72 1.50e-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: 1.50e-14
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 599044318  34 LSFKDVAVVFTEEELELLDSTQRQLYQDVMQENFRNLLS 72
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
369-781 2.95e-14

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 75.89  E-value: 2.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044318 369 RPYKCEECGKAFGRSSNLLVHQRVHTGEKPYKCSECGKGFSYSSV--LQVHQRLHTGEKPYTCSECGKGfcAKSALHKHQ 446
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPleLSRHLRTHHNNPSDLNSKSLPL--SNSKASSSS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044318 447 HIHPGEKPYscgecgKGFSCSSHLSSHQKTHTGERPY--------QCDKCGKGFSHNSYLQAHQRVHMGQHlykcNVCGK 518
Cdd:COG5048  110 LSSSSSNSN------DNNLLSSHSLPPSSRDPQLPDLlsisnlrnNPLPGNNSSSVNTPQSNSLHPPLPAN----SLSKD 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044318 519 SFSYSSGLLMHQRLHTGEKPYKCECGKSFGRSSDLHIHQRVHTGEKPYKCSECGKGF------RRNSDLHSHQRVHTGER 592
Cdd:COG5048  180 PSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpksllsQSPSSLSSSDSSSSASE 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044318 593 PYVCDVCGKGFIYSSDLLIHQRVHTG-EKPYKCAECGKGFSYSSGLLIHQR--VHTGE--KPYRC--QECGKGFRCTSSL 665
Cdd:COG5048  260 SPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDAL 339

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044318 666 HKHQRVHTGKKPYTC--DQCGKGFSYGSNLRTHQRLH---------TGEKPYTCCEcgKGFRYGSGLLSHKRVHTGEKPY 734
Cdd:COG5048  340 KRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQqykdlkndkKSETLSNSCI--RNFKRDSNLSLHIITHLSFRPY 417

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 599044318 735 RCH--VCGKGYSQSSHLQGHQRVHTGEKPYKCEECGKGFGRNSCLHVHQ 781
Cdd:COG5048  418 NCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHGK 466
zf-H2C2_2 pfam13465
Zinc-finger double domain;
385-410 7.30e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 7.30e-04
                          10        20
                  ....*....|....*....|....*.
gi 599044318  385 NLLVHQRVHTGEKPYKCSECGKGFSY 410
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 2.30e-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: 2.30e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 599044318   33 PLSFKDVAVVFTEEELELLDSTQRQLYQDVMQENFRNLLSVG 74
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
34-76 4.91e-19

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 81.48  E-value: 4.91e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 599044318    34 LSFKDVAVVFTEEELELLDSTQRQLYQDVMQENFRNLLSVGDK 76
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQ 43
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 34-72 1.50e-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: 1.50e-14
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 599044318  34 LSFKDVAVVFTEEELELLDSTQRQLYQDVMQENFRNLLS 72
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
369-781 2.95e-14

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 75.89  E-value: 2.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044318 369 RPYKCEECGKAFGRSSNLLVHQRVHTGEKPYKCSECGKGFSYSSV--LQVHQRLHTGEKPYTCSECGKGfcAKSALHKHQ 446
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPleLSRHLRTHHNNPSDLNSKSLPL--SNSKASSSS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044318 447 HIHPGEKPYscgecgKGFSCSSHLSSHQKTHTGERPY--------QCDKCGKGFSHNSYLQAHQRVHMGQHlykcNVCGK 518
Cdd:COG5048  110 LSSSSSNSN------DNNLLSSHSLPPSSRDPQLPDLlsisnlrnNPLPGNNSSSVNTPQSNSLHPPLPAN----SLSKD 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044318 519 SFSYSSGLLMHQRLHTGEKPYKCECGKSFGRSSDLHIHQRVHTGEKPYKCSECGKGF------RRNSDLHSHQRVHTGER 592
Cdd:COG5048  180 PSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpksllsQSPSSLSSSDSSSSASE 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044318 593 PYVCDVCGKGFIYSSDLLIHQRVHTG-EKPYKCAECGKGFSYSSGLLIHQR--VHTGE--KPYRC--QECGKGFRCTSSL 665
Cdd:COG5048  260 SPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDAL 339

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044318 666 HKHQRVHTGKKPYTC--DQCGKGFSYGSNLRTHQRLH---------TGEKPYTCCEcgKGFRYGSGLLSHKRVHTGEKPY 734
Cdd:COG5048  340 KRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQqykdlkndkKSETLSNSCI--RNFKRDSNLSLHIITHLSFRPY 417

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 599044318 735 RCH--VCGKGYSQSSHLQGHQRVHTGEKPYKCEECGKGFGRNSCLHVHQ 781
Cdd:COG5048  418 NCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHGK 466
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
397-818 6.99e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 68.57  E-value: 6.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044318 397 KPYKCSECGKGFSYSSVLQVHQRLHTGEKPYTCS--ECGKGFCAKSALHKHQHIHPGEKPY-SCGECGKGFSCSSHLSSH 473
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDlNSKSLPLSNSKASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044318 474 QKTHTGERPYQCDKCGKGFSHNSYLQ--AHQRVHMG-QHLYKCNVCGKSFSYSSGLLM-HQRLHTGEKPYKCecgksfgr 549
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLpdLLSISNLRnNPLPGNNSSSVNTPQSNSLHPpLPANSLSKDPSSN-------- 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044318 550 sSDLHIHQRVHTGEKPYKCSECGKGFRRNSDLHSHQRVHTgerpyvcdvcgkgfiYSSDLLIHQRVHTGEKPYKCAecgk 629
Cdd:COG5048  184 -LSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLEN---------------SSSSLPLTTNSQLSPKSLLSQ---- 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044318 630 gfSYSSGLLIHQRVHTGEkPYRCQECGKGFRCTSSLHKHQRVHTGK-KPYTCDQCGKGFSYGSNLRTHQR--LHTGE--K 704
Cdd:COG5048  244 --SPSSLSSSDSSSSASE-SPRSSLPTASSQSSSPNESDSSSEKGFsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044318 705 PYTCCE--CGKGFRYGSGLLSHKRVHTGEKPYRCH--VCGKGYSQSSHLQGHQRV--HTGEKPYKCEE-----CGKGFGR 773
Cdd:COG5048  321 PFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLqqYKDLKNDKKSEtlsnsCIRNFKR 400

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 599044318 774 NSCLHVHQRVHTGEKPY--TCGVCGKGFSYTSGLRNHQRVHLGENPY 818
Cdd:COG5048  401 DSNLSLHIITHLSFRPYncKNPPCSKSFNRHYNLIPHKKIHTNHAPL 447
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 730-812 4.40e-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: 4.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044318 730 GEKPYRCHV--CGKGYSQSSHLQ-----GHQRVHTGEKPykCEECGKGFGrnsclhvhqrvhTGEKPYTCGVCGKGFSYT 802
Cdd:COG5189  346 DGKPYKCPVegCNKKYKNQNGLKyhmlhGHQNQKLHENP--SPEKMNIFS------------AKDKPYRCEVCDKRYKNL 411

                         90
                 ....*....|
gi 599044318 803 SGLRNHqRVH 812
Cdd:COG5189  412 NGLKYH-RKH 420
zf-H2C2_2 pfam13465
Zinc-finger double domain;
385-410 7.30e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 7.30e-04
                          10        20
                  ....*....|....*....|....*.
gi 599044318  385 NLLVHQRVHTGEKPYKCSECGKGFSY 410
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
469-494 7.38e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 7.38e-04
                          10        20
                  ....*....|....*....|....*.
gi 599044318  469 HLSSHQKTHTGERPYQCDKCGKGFSH 494
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 492-589 9.25e-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: 9.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044318 492 FSHNSYLQ----AHQRVHMGQHLYKCNV--CGKSFSYSSGLLMHqRLHTgekpykcECGKSFGRSSDLHIHQRVHTGEKP 565
Cdd:COG5189  327 LAHGGERNidtpSRMLKVKDGKPYKCPVegCNKKYKNQNGLKYH-MLHG-------HQNQKLHENPSPEKMNIFSAKDKP 398

                         90       100
                 ....*....|....*....|....
gi 599044318 566 YKCSECGKGFRRNSDLHSHqRVHT 589
Cdd:COG5189  399 YRCEVCDKRYKNLNGLKYH-RKHS 421
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 535-601 1.53e-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: 1.53e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044318 535 GEKPYKCE---CGKSFGRSSDLHIHqRVHtgekpykcSECGKGFRRNSDLHSHQRVHTGERPYVCDVCGK 601
Cdd:COG5189  346 DGKPYKCPvegCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDK 406
zf-H2C2_2 pfam13465
Zinc-finger double domain;
748-771 1.57e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.57e-03
                          10        20
                  ....*....|....*....|....
gi 599044318  748 HLQGHQRVHTGEKPYKCEECGKGF 771
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
608-633 3.52e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.52e-03
                          10        20
                  ....*....|....*....|....*.
gi 599044318  608 DLLIHQRVHTGEKPYKCAECGKGFSY 633
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 483-505 3.93e-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: 3.93e-03
                          10        20
                  ....*....|....*....|...
gi 599044318  483 YQCDKCGKGFSHNSYLQAHQRVH 505
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
414-436 4.86e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.86e-03
                          10        20
                  ....*....|....*....|...
gi 599044318  414 LQVHQRLHTGEKPYTCSECGKGF 436
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 566-588 5.03e-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: 5.03e-03
                          10        20
                  ....*....|....*....|...
gi 599044318  566 YKCSECGKGFRRNSDLHSHQRVH 588
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
556-577 5.21e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 5.21e-03
                          10        20
                  ....*....|....*....|..
gi 599044318  556 HQRVHTGEKPYKCSECGKGFRR 577
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
721-745 5.26e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 5.26e-03
                          10        20
                  ....*....|....*....|....*
gi 599044318  721 LLSHKRVHTGEKPYRCHVCGKGYSQ 745
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 371-393 6.30e-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: 6.30e-03
                          10        20
                  ....*....|....*....|...
gi 599044318  371 YKCEECGKAFGRSSNLLVHQRVH 393
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
637-661 6.40e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 6.40e-03
                          10        20
                  ....*....|....*....|....*
gi 599044318  637 LLIHQRVHTGEKPYRCQECGKGFRC 661
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
667-689 8.77e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 8.77e-03
                          10        20
                  ....*....|....*....|...
gi 599044318  667 KHQRVHTGKKPYTCDQCGKGFSY 689
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFKS 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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