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Conserved domains on  [gi|117956407|ref|NP_940941|]
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zinc finger protein 568 isoform 1 [Homo sapiens]

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
Gene Ontology:  GO:0003700|GO:0046872
PubMed:  22803940
SCOP:  4003583

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
48-102 3.15e-33

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 121.16  E-value: 3.15e-33
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 117956407    48 VTFKDVAVDLTQEEWEQMKPAQRNLYRDVMLENYSNLVTVGCQVTKPDVIFKLEQ 102
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQ 55
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
248-634 2.15e-19

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 91.68  E-value: 2.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117956407 248 KPYECKECGKAFSRKENLITHQKIHTGEKPYKCN--ECGKAFIQMSNLIRHHRIHTGEKPYACKDC------WKAFSQKS 319
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSlplsnsKASSSSLS 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117956407 320 NLIEHERIHTGEKPYECKecGKSFSQKQNLIEHEKIHTGEKPYACNECGRAF-------------------SRMSSVTLH 380
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLP--PSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTpqsnslhpplpanslskdpSSNLSLLIS 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117956407 381 MRSHTGEKPYKCNKCGKAFSQCSVFIIHMRSHTGEKPYVCSECGKAFSQSSSLTVHMRNHTAEKPYECKECGKAFSRKEN 460
Cdd:COG5048  190 SNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTAS 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117956407 461 LITHQKIHTGE-------KPYECSECGKAFIQMSNLIRHQR--IHTGE--KPYACTV--CGKAFSQKSNLTEHEKIHTGE 527
Cdd:COG5048  270 SQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSI 349
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117956407 528 KPYHC--NQCGKAFSQ------RQNLLEHEKIHTgEKPFKC--NECGKAFSRISSLTLHVRSHTGEKPYECN--KCGKAF 595
Cdd:COG5048  350 SPAKEklLNSSSKFSPllnnepPQSLQQYKDLKN-DKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSF 428
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 117956407 596 SQCSLLIIHMRSHTGEKPFECNECGKaFSQRASLSIHKR 634
Cdd:COG5048  429 NRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNHGK 466
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
48-102 3.15e-33

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 121.16  E-value: 3.15e-33
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 117956407    48 VTFKDVAVDLTQEEWEQMKPAQRNLYRDVMLENYSNLVTVGCQVTKPDVIFKLEQ 102
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQ 55
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
48-88 2.13e-23

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 92.92  E-value: 2.13e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 117956407   48 VTFKDVAVDLTQEEWEQMKPAQRNLYRDVMLENYSNLVTVG 88
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
48-85 1.80e-20

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: 84.52  E-value: 1.80e-20
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 117956407  48 VTFKDVAVDLTQEEWEQMKPAQRNLYRDVMLENYSNLV 85
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLV 38
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
248-634 2.15e-19

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 91.68  E-value: 2.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117956407 248 KPYECKECGKAFSRKENLITHQKIHTGEKPYKCN--ECGKAFIQMSNLIRHHRIHTGEKPYACKDC------WKAFSQKS 319
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSlplsnsKASSSSLS 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117956407 320 NLIEHERIHTGEKPYECKecGKSFSQKQNLIEHEKIHTGEKPYACNECGRAF-------------------SRMSSVTLH 380
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLP--PSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTpqsnslhpplpanslskdpSSNLSLLIS 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117956407 381 MRSHTGEKPYKCNKCGKAFSQCSVFIIHMRSHTGEKPYVCSECGKAFSQSSSLTVHMRNHTAEKPYECKECGKAFSRKEN 460
Cdd:COG5048  190 SNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTAS 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117956407 461 LITHQKIHTGE-------KPYECSECGKAFIQMSNLIRHQR--IHTGE--KPYACTV--CGKAFSQKSNLTEHEKIHTGE 527
Cdd:COG5048  270 SQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSI 349
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117956407 528 KPYHC--NQCGKAFSQ------RQNLLEHEKIHTgEKPFKC--NECGKAFSRISSLTLHVRSHTGEKPYECN--KCGKAF 595
Cdd:COG5048  350 SPAKEklLNSSSKFSPllnnepPQSLQQYKDLKN-DKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSF 428
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 117956407 596 SQCSLLIIHMRSHTGEKPFECNECGKaFSQRASLSIHKR 634
Cdd:COG5048  429 NRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNHGK 466
zf-H2C2_2 pfam13465
Zinc-finger double domain;
320-345 7.95e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 7.95e-05
                          10        20
                  ....*....|....*....|....*.
gi 117956407  320 NLIEHERIHTGEKPYECKECGKSFSQ 345
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
48-102 3.15e-33

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 121.16  E-value: 3.15e-33
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 117956407    48 VTFKDVAVDLTQEEWEQMKPAQRNLYRDVMLENYSNLVTVGCQVTKPDVIFKLEQ 102
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQ 55
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
48-88 2.13e-23

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 92.92  E-value: 2.13e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 117956407   48 VTFKDVAVDLTQEEWEQMKPAQRNLYRDVMLENYSNLVTVG 88
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
48-85 1.80e-20

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: 84.52  E-value: 1.80e-20
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 117956407  48 VTFKDVAVDLTQEEWEQMKPAQRNLYRDVMLENYSNLV 85
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLV 38
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
248-634 2.15e-19

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 91.68  E-value: 2.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117956407 248 KPYECKECGKAFSRKENLITHQKIHTGEKPYKCN--ECGKAFIQMSNLIRHHRIHTGEKPYACKDC------WKAFSQKS 319
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSlplsnsKASSSSLS 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117956407 320 NLIEHERIHTGEKPYECKecGKSFSQKQNLIEHEKIHTGEKPYACNECGRAF-------------------SRMSSVTLH 380
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLP--PSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTpqsnslhpplpanslskdpSSNLSLLIS 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117956407 381 MRSHTGEKPYKCNKCGKAFSQCSVFIIHMRSHTGEKPYVCSECGKAFSQSSSLTVHMRNHTAEKPYECKECGKAFSRKEN 460
Cdd:COG5048  190 SNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTAS 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117956407 461 LITHQKIHTGE-------KPYECSECGKAFIQMSNLIRHQR--IHTGE--KPYACTV--CGKAFSQKSNLTEHEKIHTGE 527
Cdd:COG5048  270 SQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSI 349
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117956407 528 KPYHC--NQCGKAFSQ------RQNLLEHEKIHTgEKPFKC--NECGKAFSRISSLTLHVRSHTGEKPYECN--KCGKAF 595
Cdd:COG5048  350 SPAKEklLNSSSKFSPllnnepPQSLQQYKDLKN-DKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSF 428
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 117956407 596 SQCSLLIIHMRSHTGEKPFECNECGKaFSQRASLSIHKR 634
Cdd:COG5048  429 NRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNHGK 466
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
428-553 8.21e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.01  E-value: 8.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117956407 428 SQSSSLTVHMRNHTAE----KPYECKECGKAFSRKENLITHQKIHTGEKPYECS--ECGKAFIQMSNLIRHQRIHTGEKP 501
Cdd:COG5048   12 NNSVLSSTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPS 91
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 117956407 502 YACTV-CGKAFSQKSNLTEHEKIHTGEKPYHCNQCGKAFSQRQNLLEHEKIHT 553
Cdd:COG5048   92 DLNSKsLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSIS 144
zf-H2C2_2 pfam13465
Zinc-finger double domain;
320-345 7.95e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 7.95e-05
                          10        20
                  ....*....|....*....|....*.
gi 117956407  320 NLIEHERIHTGEKPYECKECGKSFSQ 345
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
488-513 9.21e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 9.21e-05
                          10        20
                  ....*....|....*....|....*.
gi 117956407  488 NLIRHQRIHTGEKPYACTVCGKAFSQ 513
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
544-569 1.35e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.35e-04
                          10        20
                  ....*....|....*....|....*.
gi 117956407  544 NLLEHEKIHTGEKPFKCNECGKAFSR 569
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
516-541 1.71e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.71e-04
                          10        20
                  ....*....|....*....|....*.
gi 117956407  516 NLTEHEKIHTGEKPYHCNQCGKAFSQ 541
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
380-401 2.79e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.79e-04
                          10        20
                  ....*....|....*....|..
gi 117956407  380 HMRSHTGEKPYKCNKCGKAFSQ 401
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
264-289 2.93e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.93e-04
                          10        20
                  ....*....|....*....|....*.
gi 117956407  264 NLITHQKIHTGEKPYKCNECGKAFIQ 289
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
604-625 3.05e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.05e-04
                          10        20
                  ....*....|....*....|..
gi 117956407  604 HMRSHTGEKPFECNECGKAFSQ 625
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
432-457 4.42e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.42e-04
                          10        20
                  ....*....|....*....|....*.
gi 117956407  432 SLTVHMRNHTAEKPYECKECGKAFSR 457
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
460-485 4.65e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.65e-04
                          10        20
                  ....*....|....*....|....*.
gi 117956407  460 NLITHQKIHTGEKPYECSECGKAFIQ 485
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
408-429 5.23e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 5.23e-04
                          10        20
                  ....*....|....*....|..
gi 117956407  408 HMRSHTGEKPYVCSECGKAFSQ 429
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
236-261 5.60e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 5.60e-04
                          10        20
                  ....*....|....*....|....*.
gi 117956407  236 DLIRHERIHAGEKPYECKECGKAFSR 261
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
572-597 8.54e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 8.54e-04
                          10        20
                  ....*....|....*....|....*.
gi 117956407  572 SLTLHVRSHTGEKPYECNKCGKAFSQ 597
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
348-373 1.22e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.22e-03
                          10        20
                  ....*....|....*....|....*.
gi 117956407  348 NLIEHEKIHTGEKPYACNECGRAFSR 373
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
250-272 2.43e-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: 35.74  E-value: 2.43e-03
                          10        20
                  ....*....|....*....|...
gi 117956407  250 YECKECGKAFSRKENLITHQKIH 272
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
446-468 2.43e-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: 35.74  E-value: 2.43e-03
                          10        20
                  ....*....|....*....|...
gi 117956407  446 YECKECGKAFSRKENLITHQKIH 468
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
418-440 2.99e-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: 2.99e-03
                          10        20
                  ....*....|....*....|...
gi 117956407  418 YVCSECGKAFSQSSSLTVHMRNH 440
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
584-637 3.02e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.45  E-value: 3.02e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 117956407 584 KPYECNKCGKAFSQCSLLIIHMRSHTGEKPFECN--ECGKAFSQRASLSIHKRGHT 637
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHH 87
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
498-581 3.06e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.47  E-value: 3.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117956407 498 GEKPYACTV--CGKAFSQKSNLTEHeKIHTgekpyHCNQcgkAFSQRQNLLEHEKIHTGEKPFKCNECGKAFSRISSLTL 575
Cdd:COG5189  346 DGKPYKCPVegCNKKYKNQNGLKYH-MLHG-----HQNQ---KLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416

                 ....*.
gi 117956407 576 HvRSHT 581
Cdd:COG5189  417 H-RKHS 421
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
278-300 4.51e-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: 4.51e-03
                          10        20
                  ....*....|....*....|...
gi 117956407  278 YKCNECGKAFIQMSNLIRHHRIH 300
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
586-608 4.98e-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: 4.98e-03
                          10        20
                  ....*....|....*....|...
gi 117956407  586 YECNKCGKAFSQCSLLIIHMRSH 608
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
474-496 5.65e-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: 5.65e-03
                          10        20
                  ....*....|....*....|...
gi 117956407  474 YECSECGKAFIQMSNLIRHQRIH 496
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
292-317 8.76e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 8.76e-03
                          10        20
                  ....*....|....*....|....*.
gi 117956407  292 NLIRHHRIHTGEKPYACKDCWKAFSQ 317
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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