NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|325651958|ref|NP_001191765|]
View 

zinc finger protein 568 isoform 3 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
184-570 4.28e-19

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 90.14  E-value: 4.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325651958 184 KPYECKECGKAFSRKENLITHQKIHTGEKPYKCN--ECGKAFIQMSNLIRHHRIHTGEKPYACKDC------WKAFSQKS 255
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSlplsnsKASSSSLS 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325651958 256 NLIEHERIHTGEKPYECKecGKSFSQKQNLIEHEKIHTGEKPYACNECGRAF-------------------SRMSSVTLH 316
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLP--PSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTpqsnslhpplpanslskdpSSNLSLLIS 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325651958 317 MRSHTGEKPYKCNKCGKAFSQCSVFIIHMRSHTGEKPYVCSECGKAFSQSSSLTVHMRNHTAEKPYECKECGKAFSRKEN 396
Cdd:COG5048  190 SNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTAS 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325651958 397 LITHQKIHTGE-------KPYECSECGKAFIQMSNLIRHQR--IHTGE--KPYACTV--CGKAFSQKSNLTEHEKIHTGE 463
Cdd:COG5048  270 SQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSI 349
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325651958 464 KPYHC--NQCGKAFSQ------RQNLLEHEKIHTgEKPFKC--NECGKAFSRISSLTLHVRSHTGEKPYECN--KCGKAF 531
Cdd:COG5048  350 SPAKEklLNSSSKFSPllnnepPQSLQQYKDLKN-DKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSF 428
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 325651958 532 SQCSLLIIHMRSHTGEKPFECNECGKaFSQRASLSIHKR 570
Cdd:COG5048  429 NRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNHGK 466
KRAB smart00349
krueppel associated box;
1-38 7.46e-19

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 80.33  E-value: 7.46e-19
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 325651958     1 MKPAQRNLYRDVMLENYSNLVTVGCQVTKPDVIFKLEQ 38
Cdd:smart00349  18 LDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQ 55
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
184-570 4.28e-19

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 90.14  E-value: 4.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325651958 184 KPYECKECGKAFSRKENLITHQKIHTGEKPYKCN--ECGKAFIQMSNLIRHHRIHTGEKPYACKDC------WKAFSQKS 255
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSlplsnsKASSSSLS 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325651958 256 NLIEHERIHTGEKPYECKecGKSFSQKQNLIEHEKIHTGEKPYACNECGRAF-------------------SRMSSVTLH 316
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLP--PSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTpqsnslhpplpanslskdpSSNLSLLIS 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325651958 317 MRSHTGEKPYKCNKCGKAFSQCSVFIIHMRSHTGEKPYVCSECGKAFSQSSSLTVHMRNHTAEKPYECKECGKAFSRKEN 396
Cdd:COG5048  190 SNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTAS 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325651958 397 LITHQKIHTGE-------KPYECSECGKAFIQMSNLIRHQR--IHTGE--KPYACTV--CGKAFSQKSNLTEHEKIHTGE 463
Cdd:COG5048  270 SQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSI 349
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325651958 464 KPYHC--NQCGKAFSQ------RQNLLEHEKIHTgEKPFKC--NECGKAFSRISSLTLHVRSHTGEKPYECN--KCGKAF 531
Cdd:COG5048  350 SPAKEklLNSSSKFSPllnnepPQSLQQYKDLKN-DKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSF 428
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 325651958 532 SQCSLLIIHMRSHTGEKPFECNECGKaFSQRASLSIHKR 570
Cdd:COG5048  429 NRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNHGK 466
KRAB smart00349
krueppel associated box;
1-38 7.46e-19

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 80.33  E-value: 7.46e-19
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 325651958     1 MKPAQRNLYRDVMLENYSNLVTVGCQVTKPDVIFKLEQ 38
Cdd:smart00349  18 LDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQ 55
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
1-24 7.97e-10

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: 54.40  E-value: 7.97e-10
                          10        20
                  ....*....|....*....|....
gi 325651958    1 MKPAQRNLYRDVMLENYSNLVTVG 24
Cdd:pfam01352  19 LDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
1-21 3.45e-07

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: 46.77  E-value: 3.45e-07
                         10        20
                 ....*....|....*....|.
gi 325651958   1 MKPAQRNLYRDVMLENYSNLV 21
Cdd:cd07765   18 LDPAQRDLYRDVMLENYENLV 38
zf-H2C2_2 pfam13465
Zinc-finger double domain;
256-281 1.28e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.28e-04
                          10        20
                  ....*....|....*....|....*.
gi 325651958  256 NLIEHERIHTGEKPYECKECGKSFSQ 281
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
184-570 4.28e-19

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 90.14  E-value: 4.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325651958 184 KPYECKECGKAFSRKENLITHQKIHTGEKPYKCN--ECGKAFIQMSNLIRHHRIHTGEKPYACKDC------WKAFSQKS 255
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSlplsnsKASSSSLS 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325651958 256 NLIEHERIHTGEKPYECKecGKSFSQKQNLIEHEKIHTGEKPYACNECGRAF-------------------SRMSSVTLH 316
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLP--PSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTpqsnslhpplpanslskdpSSNLSLLIS 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325651958 317 MRSHTGEKPYKCNKCGKAFSQCSVFIIHMRSHTGEKPYVCSECGKAFSQSSSLTVHMRNHTAEKPYECKECGKAFSRKEN 396
Cdd:COG5048  190 SNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTAS 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325651958 397 LITHQKIHTGE-------KPYECSECGKAFIQMSNLIRHQR--IHTGE--KPYACTV--CGKAFSQKSNLTEHEKIHTGE 463
Cdd:COG5048  270 SQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSI 349
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325651958 464 KPYHC--NQCGKAFSQ------RQNLLEHEKIHTgEKPFKC--NECGKAFSRISSLTLHVRSHTGEKPYECN--KCGKAF 531
Cdd:COG5048  350 SPAKEklLNSSSKFSPllnnepPQSLQQYKDLKN-DKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSF 428
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 325651958 532 SQCSLLIIHMRSHTGEKPFECNECGKaFSQRASLSIHKR 570
Cdd:COG5048  429 NRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNHGK 466
KRAB smart00349
krueppel associated box;
1-38 7.46e-19

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 80.33  E-value: 7.46e-19
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 325651958     1 MKPAQRNLYRDVMLENYSNLVTVGCQVTKPDVIFKLEQ 38
Cdd:smart00349  18 LDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQ 55
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
1-24 7.97e-10

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: 54.40  E-value: 7.97e-10
                          10        20
                  ....*....|....*....|....
gi 325651958    1 MKPAQRNLYRDVMLENYSNLVTVG 24
Cdd:pfam01352  19 LDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
1-21 3.45e-07

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: 46.77  E-value: 3.45e-07
                         10        20
                 ....*....|....*....|.
gi 325651958   1 MKPAQRNLYRDVMLENYSNLV 21
Cdd:cd07765   18 LDPAQRDLYRDVMLENYENLV 38
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
364-489 9.65e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 51.62  E-value: 9.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325651958 364 SQSSSLTVHMRNHTAE----KPYECKECGKAFSRKENLITHQKIHTGEKPYECS--ECGKAFIQMSNLIRHQRIHTGEKP 437
Cdd:COG5048   12 NNSVLSSTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPS 91
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 325651958 438 YACTV-CGKAFSQKSNLTEHEKIHTGEKPYHCNQCGKAFSQRQNLLEHEKIHT 489
Cdd:COG5048   92 DLNSKsLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSIS 144
zf-H2C2_2 pfam13465
Zinc-finger double domain;
256-281 1.28e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.28e-04
                          10        20
                  ....*....|....*....|....*.
gi 325651958  256 NLIEHERIHTGEKPYECKECGKSFSQ 281
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
424-449 1.50e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.50e-04
                          10        20
                  ....*....|....*....|....*.
gi 325651958  424 NLIRHQRIHTGEKPYACTVCGKAFSQ 449
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
480-505 2.11e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.11e-04
                          10        20
                  ....*....|....*....|....*.
gi 325651958  480 NLLEHEKIHTGEKPFKCNECGKAFSR 505
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
452-477 2.70e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 2.70e-04
                          10        20
                  ....*....|....*....|....*.
gi 325651958  452 NLTEHEKIHTGEKPYHCNQCGKAFSQ 477
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
316-337 4.40e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.40e-04
                          10        20
                  ....*....|....*....|..
gi 325651958  316 HMRSHTGEKPYKCNKCGKAFSQ 337
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
200-225 4.67e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.67e-04
                          10        20
                  ....*....|....*....|....*.
gi 325651958  200 NLITHQKIHTGEKPYKCNECGKAFIQ 225
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
540-561 4.76e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.76e-04
                          10        20
                  ....*....|....*....|..
gi 325651958  540 HMRSHTGEKPFECNECGKAFSQ 561
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
368-393 6.99e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 6.99e-04
                          10        20
                  ....*....|....*....|....*.
gi 325651958  368 SLTVHMRNHTAEKPYECKECGKAFSR 393
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
396-421 7.27e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 7.27e-04
                          10        20
                  ....*....|....*....|....*.
gi 325651958  396 NLITHQKIHTGEKPYECSECGKAFIQ 421
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
344-365 8.01e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 8.01e-04
                          10        20
                  ....*....|....*....|..
gi 325651958  344 HMRSHTGEKPYVCSECGKAFSQ 365
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
172-197 8.75e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 8.75e-04
                          10        20
                  ....*....|....*....|....*.
gi 325651958  172 DLIRHERIHAGEKPYECKECGKAFSR 197
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
508-533 1.32e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.32e-03
                          10        20
                  ....*....|....*....|....*.
gi 325651958  508 SLTLHVRSHTGEKPYECNKCGKAFSQ 533
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
284-309 1.85e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 1.85e-03
                          10        20
                  ....*....|....*....|....*.
gi 325651958  284 NLIEHEKIHTGEKPYACNECGRAFSR 309
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
434-517 2.84e-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: 2.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325651958 434 GEKPYACTV--CGKAFSQKSNLTEHeKIHTgekpyHCNQcgkAFSQRQNLLEHEKIHTGEKPFKCNECGKAFSRISSLTL 511
Cdd:COG5189  346 DGKPYKCPVegCNKKYKNQNGLKYH-MLHG-----HQNQ---KLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416

                 ....*.
gi 325651958 512 HvRSHT 517
Cdd:COG5189  417 H-RKHS 421
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
520-573 3.16e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.45  E-value: 3.16e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 325651958 520 KPYECNKCGKAFSQCSLLIIHMRSHTGEKPFECN--ECGKAFSQRASLSIHKRGHT 573
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHH 87
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
186-208 4.07e-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: 4.07e-03
                          10        20
                  ....*....|....*....|...
gi 325651958  186 YECKECGKAFSRKENLITHQKIH 208
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
382-404 4.07e-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: 4.07e-03
                          10        20
                  ....*....|....*....|...
gi 325651958  382 YECKECGKAFSRKENLITHQKIH 404
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
354-376 4.91e-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: 4.91e-03
                          10        20
                  ....*....|....*....|...
gi 325651958  354 YVCSECGKAFSQSSSLTVHMRNH 376
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
214-236 7.41e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.20  E-value: 7.41e-03
                          10        20
                  ....*....|....*....|...
gi 325651958  214 YKCNECGKAFIQMSNLIRHHRIH 236
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
522-544 8.02e-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: 8.02e-03
                          10        20
                  ....*....|....*....|...
gi 325651958  522 YECNKCGKAFSQCSLLIIHMRSH 544
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
410-432 9.20e-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: 33.81  E-value: 9.20e-03
                          10        20
                  ....*....|....*....|...
gi 325651958  410 YECSECGKAFIQMSNLIRHQRIH 432
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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