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Conserved domains on  [gi|568982550|ref|XP_006517011|]
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zinc finger protein 169 isoform X2 [Mus musculus]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204268)

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

CATH:  3.30.160.60|1.10.287.1360
Gene Ontology:  GO:0003677|GO:0008270|GO:0005515|GO:0001217|GO:0003700
PubMed:  8183940|22803940|2023909|8183939|8183940|10748030|27867147|28765213|11361095|30718982|10940247
SCOP:  4003583|4002243

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-73 1.50e-31

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 116.92  E-value: 1.50e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982550    14 MAFHDVAVAFSQMEWELLSPAQRILYRDVMLENYSHLVSLGIAFSKPKLITQLEQGAEPW 73
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPW 60
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
255-726 1.70e-15

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 79.74  E-value: 1.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982550 255 KPYSCSECGHQFAQKASLTVHQRKHSGEKPHVCEECGRGFMYVSSLNSHKKIIHSGESPLVCPEcgrgfrQKIDLLLHQR 334
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSDLNS------KSLPLSNSKA 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982550 335 THLDKkpfvcPECGRGFCRKASLLQHSWSHSGDNPFICSVcgrgfrllsrlltHQVTHSGEKPHvcPDCgqrFGQKGTLM 414
Cdd:COG5048  106 SSSSL-----SSSSSNSNDNNLLSSHSLPPSSRDPQLPDL-------------LSISNLRNNPL--PGN---NSSSVNTP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982550 415 RHQKTHtGEKPFVCRQCGWSFTQKVNLirHQRIHTEVKPFLCPECGRAFEFKSLLTRHRKTHMGEKPYVCPQCGRGFSQK 494
Cdd:COG5048  163 QSNSLH-PPLPANSLSKDPSSNLSLLI--SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982550 495 FNLIGHQRIHTGELPFLCPECGRAFVKQSMLIRHQ------RTHAGWEKPYQCPECGRTFEFKSLLTRHQ--KIHTGE-- 564
Cdd:COG5048  240 LLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSpnesdsSSEKGFSLPIKSKQCNISFSRSSPLTRHLrsVNHSGEsl 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982550 565 KPYVCP--QCGRGFSQKFNLIGHQKTHTGEKPYACPqcgqrfrqkfnLARHQRIHTGEKPflcaecgrafGKKVSLIRHQ 642
Cdd:COG5048  320 KPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEK-----------LLNSSSKFSPLLN----------NEPPQSLQQY 378

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982550 643 RTHGEEKPYQCT--ECGRAFEFKSLFIRHQKTHTGEKPYVC--PECGKAFSQKFNLIGHQRSHTGEKPYLCPQCGRAFAF 718
Cdd:COG5048  379 KDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRD 458


                 ....*...
gi 568982550 719 KSLLTRHQ 726
Cdd:COG5048  459 LDLSNHGK 466
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-73 1.50e-31

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 116.92  E-value: 1.50e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982550    14 MAFHDVAVAFSQMEWELLSPAQRILYRDVMLENYSHLVSLGIAFSKPKLITQLEQGAEPW 73
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPW 60
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 13-54 3.44e-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: 86.76  E-value: 3.44e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568982550   13 LMAFHDVAVAFSQMEWELLSPAQRILYRDVMLENYSHLVSLG 54
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 14-53 5.65e-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: 77.59  E-value: 5.65e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 568982550  14 MAFHDVAVAFSQMEWELLSPAQRILYRDVMLENYSHLVSL 53
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
255-726 1.70e-15

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 79.74  E-value: 1.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982550 255 KPYSCSECGHQFAQKASLTVHQRKHSGEKPHVCEECGRGFMYVSSLNSHKKIIHSGESPLVCPEcgrgfrQKIDLLLHQR 334
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSDLNS------KSLPLSNSKA 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982550 335 THLDKkpfvcPECGRGFCRKASLLQHSWSHSGDNPFICSVcgrgfrllsrlltHQVTHSGEKPHvcPDCgqrFGQKGTLM 414
Cdd:COG5048  106 SSSSL-----SSSSSNSNDNNLLSSHSLPPSSRDPQLPDL-------------LSISNLRNNPL--PGN---NSSSVNTP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982550 415 RHQKTHtGEKPFVCRQCGWSFTQKVNLirHQRIHTEVKPFLCPECGRAFEFKSLLTRHRKTHMGEKPYVCPQCGRGFSQK 494
Cdd:COG5048  163 QSNSLH-PPLPANSLSKDPSSNLSLLI--SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982550 495 FNLIGHQRIHTGELPFLCPECGRAFVKQSMLIRHQ------RTHAGWEKPYQCPECGRTFEFKSLLTRHQ--KIHTGE-- 564
Cdd:COG5048  240 LLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSpnesdsSSEKGFSLPIKSKQCNISFSRSSPLTRHLrsVNHSGEsl 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982550 565 KPYVCP--QCGRGFSQKFNLIGHQKTHTGEKPYACPqcgqrfrqkfnLARHQRIHTGEKPflcaecgrafGKKVSLIRHQ 642
Cdd:COG5048  320 KPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEK-----------LLNSSSKFSPLLN----------NEPPQSLQQY 378

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982550 643 RTHGEEKPYQCT--ECGRAFEFKSLFIRHQKTHTGEKPYVC--PECGKAFSQKFNLIGHQRSHTGEKPYLCPQCGRAFAF 718
Cdd:COG5048  379 KDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRD 458


                 ....*...
gi 568982550 719 KSLLTRHQ 726
Cdd:COG5048  459 LDLSNHGK 466
zf-H2C2_2 pfam13465
Zinc-finger double domain;
668-690 4.31e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 4.31e-05
                          10        20
                  ....*....|....*....|...
gi 568982550  668 RHQKTHTGEKPYVCPECGKAFSQ 690
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFKS 26
PHA00733 PHA00733
hypothetical protein
 481-528 7.18e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.16  E-value: 7.18e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 568982550 481 PYVCPQCGRGFSQKFNLIGHqrIHTGELPFLCPECGRAFVKQSMLIRH 528
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQH--IRYTEHSKVCPVCGKEFRNTDSTLDH 118
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-73 1.50e-31

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 116.92  E-value: 1.50e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982550    14 MAFHDVAVAFSQMEWELLSPAQRILYRDVMLENYSHLVSLGIAFSKPKLITQLEQGAEPW 73
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPW 60
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 13-54 3.44e-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: 86.76  E-value: 3.44e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568982550   13 LMAFHDVAVAFSQMEWELLSPAQRILYRDVMLENYSHLVSLG 54
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 14-53 5.65e-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: 77.59  E-value: 5.65e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 568982550  14 MAFHDVAVAFSQMEWELLSPAQRILYRDVMLENYSHLVSL 53
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
255-726 1.70e-15

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 79.74  E-value: 1.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982550 255 KPYSCSECGHQFAQKASLTVHQRKHSGEKPHVCEECGRGFMYVSSLNSHKKIIHSGESPLVCPEcgrgfrQKIDLLLHQR 334
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSDLNS------KSLPLSNSKA 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982550 335 THLDKkpfvcPECGRGFCRKASLLQHSWSHSGDNPFICSVcgrgfrllsrlltHQVTHSGEKPHvcPDCgqrFGQKGTLM 414
Cdd:COG5048  106 SSSSL-----SSSSSNSNDNNLLSSHSLPPSSRDPQLPDL-------------LSISNLRNNPL--PGN---NSSSVNTP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982550 415 RHQKTHtGEKPFVCRQCGWSFTQKVNLirHQRIHTEVKPFLCPECGRAFEFKSLLTRHRKTHMGEKPYVCPQCGRGFSQK 494
Cdd:COG5048  163 QSNSLH-PPLPANSLSKDPSSNLSLLI--SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982550 495 FNLIGHQRIHTGELPFLCPECGRAFVKQSMLIRHQ------RTHAGWEKPYQCPECGRTFEFKSLLTRHQ--KIHTGE-- 564
Cdd:COG5048  240 LLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSpnesdsSSEKGFSLPIKSKQCNISFSRSSPLTRHLrsVNHSGEsl 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982550 565 KPYVCP--QCGRGFSQKFNLIGHQKTHTGEKPYACPqcgqrfrqkfnLARHQRIHTGEKPflcaecgrafGKKVSLIRHQ 642
Cdd:COG5048  320 KPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEK-----------LLNSSSKFSPLLN----------NEPPQSLQQY 378

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982550 643 RTHGEEKPYQCT--ECGRAFEFKSLFIRHQKTHTGEKPYVC--PECGKAFSQKFNLIGHQRSHTGEKPYLCPQCGRAFAF 718
Cdd:COG5048  379 KDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRD 458


                 ....*...
gi 568982550 719 KSLLTRHQ 726
Cdd:COG5048  459 LDLSNHGK 466
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
480-731 8.94e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.09  E-value: 8.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982550 480 KPYVCPQCGRGFSQKFNLIGHQRIHTGELPFLCPECGRAFVKQSM--LIRHQRTH------------------------- 532
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPleLSRHLRTHhnnpsdlnskslplsnskassssls 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982550 533 -AGWEKPYQCPECGRTFefkSLLTRHQKIHTGEKPYV-----CPQCGRGF----------------------SQKFNLIG 584
Cdd:COG5048  112 sSSSNSNDNNLLSSHSL---PPSSRDPQLPDLLSISNlrnnpLPGNNSSSvntpqsnslhpplpanslskdpSSNLSLLI 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982550 585 HQKTHTGEKPYACPQCGQRFRQKFNLARHQRIHTGEKPFLCAECGRAFGKKVSLIRHQRTHGEEKPYQCTECGRAFEFKS 664
Cdd:COG5048  189 SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTA 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982550 665 LFIRHQKTHTGE-------KPYVCPECGKAFSQKFNLIGHQRS--HTGE--KPYLCP--QCGRAFAFKSLLTRHQRTHSK 731
Cdd:COG5048  269 SSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTS 348
zf-H2C2_2 pfam13465
Zinc-finger double domain;
668-690 4.31e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 4.31e-05
                          10        20
                  ....*....|....*....|...
gi 568982550  668 RHQKTHTGEKPYVCPECGKAFSQ 690
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
554-578 1.84e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.84e-04
                          10        20
                  ....*....|....*....|....*
gi 568982550  554 LTRHQKIHTGEKPYVCPQCGRGFSQ 578
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
469-493 4.77e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.77e-04
                          10        20
                  ....*....|....*....|....*
gi 568982550  469 LTRHRKTHMGEKPYVCPQCGRGFSQ 493
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
440-464 7.42e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 7.42e-04
                          10        20
                  ....*....|....*....|....*
gi 568982550  440 NLIRHQRIHTEVKPFLCPECGRAFE 464
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
413-437 7.42e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 7.42e-04
                          10        20
                  ....*....|....*....|....*
gi 568982550  413 LMRHQKTHTGEKPFVCRQCGWSFTQ 437
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
581-606 9.77e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 9.77e-04
                          10        20
                  ....*....|....*....|....*.
gi 568982550  581 NLIGHQKTHTGEKPYACPQCGQRFRQ 606
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
693-717 1.19e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.19e-03
                          10        20
                  ....*....|....*....|....*
gi 568982550  693 NLIGHQRSHTGEKPYLCPQCGRAFA 717
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 539-561 1.69e-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: 1.69e-03
                          10        20
                  ....*....|....*....|...
gi 568982550  539 YQCPECGRTFEFKSLLTRHQKIH 561
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
637-661 2.41e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.41e-03
                          10        20
                  ....*....|....*....|....*
gi 568982550  637 SLIRHQRTHGEEKPYQCTECGRAFE 661
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 679-701 2.98e-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: 35.74  E-value: 2.98e-03
                          10        20
                  ....*....|....*....|...
gi 568982550  679 YVCPECGKAFSQKFNLIGHQRSH 701
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG1655 COG1655
Uncharacterized conserved protein, DUF2225 family [Function unknown];
535-580 3.31e-03

Uncharacterized conserved protein, DUF2225 family [Function unknown];


Pssm-ID: 441261  Cd Length: 228  Bit Score: 39.89  E-value: 3.31e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568982550 535 WEKPYQCPECGRTFEFKSLLTRHQKIHT----------GEKPY-----VCPQCGRGFSQKF 580
Cdd:COG1655    9 YDKKVTCPVCKKEFKTKKVRSSKIRVGKrdsdfcphyeGVNPLlyevwVCPHCGYAAFEKD 69
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 426-448 3.66e-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: 35.35  E-value: 3.66e-03
                          10        20
                  ....*....|....*....|...
gi 568982550  426 FVCRQCGWSFTQKVNLIRHQRIH 448
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 595-617 5.06e-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: 5.06e-03
                          10        20
                  ....*....|....*....|...
gi 568982550  595 YACPQCGQRFRQKFNLARHQRIH 617
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 510-532 6.86e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.58  E-value: 6.86e-03
                          10        20
                  ....*....|....*....|...
gi 568982550  510 FLCPECGRAFVKQSMLIRHQRTH 532
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA00733 PHA00733
hypothetical protein
 481-528 7.18e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.16  E-value: 7.18e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 568982550 481 PYVCPQCGRGFSQKFNLIGHqrIHTGELPFLCPECGRAFVKQSMLIRH 528
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQH--IRYTEHSKVCPVCGKEFRNTDSTLDH 118
zf-H2C2_2 pfam13465
Zinc-finger double domain;
496-521 7.69e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 7.69e-03
                          10        20
                  ....*....|....*....|....*.
gi 568982550  496 NLIGHQRIHTGELPFLCPECGRAFVK 521
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 707-729 8.43e-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: 8.43e-03
                          10        20
                  ....*....|....*....|...
gi 568982550  707 YLCPQCGRAFAFKSLLTRHQRTH 729
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 651-673 8.60e-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: 8.60e-03
                          10        20
                  ....*....|....*....|...
gi 568982550  651 YQCTECGRAFEFKSLFIRHQKTH 673
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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