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Conserved domains on  [gi|1996192364|ref|NP_001380612|]
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zinc finger protein 382 isoform 1 [Rattus norvegicus]

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;
12-72 2.52e-35

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 126.55  E-value: 2.52e-35
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1996192364   12 VSFKDVTVDFTQEEWQRLDPAQKALYRDVMLENYCHFISVGFHITKPDMIRKLEQGEELWT 72
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
293-532 1.17e-07

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 54.32  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996192364 293 RPFQCPYCGNSFRRKSYLIEHQRIHTGEKPYICSQCGKAFRQKTALTLHEKTHTDGKPYLCVDCGKSFRQKATLTRHHKT 372
Cdd:COG5048   197 PSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPN 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996192364 373 HTGE-------KAYECTQCGSAFGKKSYLIDHQRT--HTGE--KPYQCAE--CGKAFIQKTTLTVHQRTHTGEKPYMC-- 437
Cdd:COG5048   277 ESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEkl 356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996192364 438 SECGKSFCQKTT-----LTLHQRIHTGEKPYVCSD--CGKSFRQKAILTVHYRIHTGEKS--NGCPQCGKAFSRKSNLIR 508
Cdd:COG5048   357 LNSSSKFSPLLNneppqSLQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIP 436

                         250       260
                  ....*....|....*....|....
gi 1996192364 509 HQKTHTGEKPYECHECGKFFSCKS 532
Cdd:COG5048   437 HKKIHTNHAPLLCSILKSFRRDLD 460
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
12-72 2.52e-35

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 126.55  E-value: 2.52e-35
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1996192364   12 VSFKDVTVDFTQEEWQRLDPAQKALYRDVMLENYCHFISVGFHITKPDMIRKLEQGEELWT 72
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 11-52 3.76e-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: 92.15  E-value: 3.76e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1996192364  11 PVSFKDVTVDFTQEEWQRLDPAQKALYRDVMLENYCHFISVG 52
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 12-50 3.69e-19

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: 80.67  E-value: 3.69e-19
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1996192364  12 VSFKDVTVDFTQEEWQRLDPAQKALYRDVMLENYCHFIS 50
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
293-532 1.17e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 54.32  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996192364 293 RPFQCPYCGNSFRRKSYLIEHQRIHTGEKPYICSQCGKAFRQKTALTLHEKTHTDGKPYLCVDCGKSFRQKATLTRHHKT 372
Cdd:COG5048   197 PSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPN 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996192364 373 HTGE-------KAYECTQCGSAFGKKSYLIDHQRT--HTGE--KPYQCAE--CGKAFIQKTTLTVHQRTHTGEKPYMC-- 437
Cdd:COG5048   277 ESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEkl 356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996192364 438 SECGKSFCQKTT-----LTLHQRIHTGEKPYVCSD--CGKSFRQKAILTVHYRIHTGEKS--NGCPQCGKAFSRKSNLIR 508
Cdd:COG5048   357 LNSSSKFSPLLNneppqSLQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIP 436

                         250       260
                  ....*....|....*....|....
gi 1996192364 509 HQKTHTGEKPYECHECGKFFSCKS 532
Cdd:COG5048   437 HKKIHTNHAPLLCSILKSFRRDLD 460
zf-H2C2_2 pfam13465
Zinc-finger double domain;
505-530 4.43e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 4.43e-05
                          10        20
                  ....*....|....*....|....*.
gi 1996192364 505 NLIRHQKTHTGEKPYECHECGKFFSC 530
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
12-72 2.52e-35

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 126.55  E-value: 2.52e-35
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1996192364   12 VSFKDVTVDFTQEEWQRLDPAQKALYRDVMLENYCHFISVGFHITKPDMIRKLEQGEELWT 72
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 11-52 3.76e-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: 92.15  E-value: 3.76e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1996192364  11 PVSFKDVTVDFTQEEWQRLDPAQKALYRDVMLENYCHFISVG 52
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 12-50 3.69e-19

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: 80.67  E-value: 3.69e-19
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1996192364  12 VSFKDVTVDFTQEEWQRLDPAQKALYRDVMLENYCHFIS 50
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
293-532 1.17e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 54.32  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996192364 293 RPFQCPYCGNSFRRKSYLIEHQRIHTGEKPYICSQCGKAFRQKTALTLHEKTHTDGKPYLCVDCGKSFRQKATLTRHHKT 372
Cdd:COG5048   197 PSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPN 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996192364 373 HTGE-------KAYECTQCGSAFGKKSYLIDHQRT--HTGE--KPYQCAE--CGKAFIQKTTLTVHQRTHTGEKPYMC-- 437
Cdd:COG5048   277 ESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEkl 356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996192364 438 SECGKSFCQKTT-----LTLHQRIHTGEKPYVCSD--CGKSFRQKAILTVHYRIHTGEKS--NGCPQCGKAFSRKSNLIR 508
Cdd:COG5048   357 LNSSSKFSPLLNneppqSLQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIP 436

                         250       260
                  ....*....|....*....|....
gi 1996192364 509 HQKTHTGEKPYECHECGKFFSCKS 532
Cdd:COG5048   437 HKKIHTNHAPLLCSILKSFRRDLD 460
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
294-482 1.92e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.46  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996192364 294 PFQCPYCGNSFRRKSYLIEHQR--IHTGE--KPYIC--SQCGKAFRQKTALTLHEKTHTDGKPYlcvdcgksfrqKATLT 367
Cdd:COG5048   289 PIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPA-----------KEKLL 357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996192364 368 RHHKTHTGEKAYECTQCgsafgkksylIDHQRTHTGEKPYQCA--ECGKAFIQKTTLTVHQRTHTGEKPYMC--SECGKS 443
Cdd:COG5048   358 NSSSKFSPLLNNEPPQS----------LQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKS 427

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1996192364 444 FCQKTTLTLHQRIHTGEKPYVCSDCGKSFRQKAILTVHY 482
Cdd:COG5048   428 FNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHGK 466
zf-H2C2_2 pfam13465
Zinc-finger double domain;
505-530 4.43e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 4.43e-05
                          10        20
                  ....*....|....*....|....*.
gi 1996192364 505 NLIRHQKTHTGEKPYECHECGKFFSC 530
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
291-541 1.38e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.69  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996192364 291 DERPFQCPYCGNSFRRKSYLIEHQRIHTGEKPYICSQCGKAFRQKTALTLH----------------------------- 341
Cdd:COG5048    30 APRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSrhlrthhnnpsdlnskslplsnskassss 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996192364 342 --EKTHTDGKPYLCVDCGKSFRQKATLTRHHKTHTGEKAYECTQCGSAFGK-----------------------KSYLID 396
Cdd:COG5048   110 lsSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNtpqsnslhpplpanslskdpssnLSLLIS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996192364 397 HQRTHTGEKPYQCAECGKAFIQKTTLTVHQRTHTgEKPYMCSECGKSFCQKTTLTLHQRIHTGEKPYVCSDCGKSFRQKA 476
Cdd:COG5048   190 SNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENS-SSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTA 268

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1996192364 477 --ILTVHYRIHTGEKSNG-----CPQCGKAFSRKSNLIRHQKT--HTGE--KPYECHE--CGKFFSCKSNLVAHQKTH 541
Cdd:COG5048   269 ssQSSSPNESDSSSEKGFslpikSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLH 346
zf-H2C2_2 pfam13465
Zinc-finger double domain;
393-418 2.23e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.23e-04
                          10        20
                  ....*....|....*....|....*.
gi 1996192364 393 YLIDHQRTHTGEKPYQCAECGKAFIQ 418
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 493-513 8.29e-04

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: 36.89  E-value: 8.29e-04
                          10        20
                  ....*....|....*....|.
gi 1996192364 493 CPQCGKAFSRKSNLIRHQKTH 513
Cdd:pfam00096   3 CPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
450-474 8.99e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 8.99e-04
                          10        20
                  ....*....|....*....|....*
gi 1996192364 450 LTLHQRIHTGEKPYVCSDCGKSFRQ 474
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
422-444 1.05e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.05e-03
                          10        20
                  ....*....|....*....|...
gi 1996192364 422 LTVHQRTHTGEKPYMCSECGKSF 444
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 295-317 2.74e-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: 2.74e-03
                          10        20
                  ....*....|....*....|...
gi 1996192364 295 FQCPYCGNSFRRKSYLIEHQRIH 317
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
309-334 3.49e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 3.49e-03
                          10        20
                  ....*....|....*....|....*.
gi 1996192364 309 YLIEHQRIHTGEKPYICSQCGKAFRQ 334
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 435-457 5.73e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.58  E-value: 5.73e-03
                          10        20
                  ....*....|....*....|...
gi 1996192364 435 YMCSECGKSFCQKTTLTLHQRIH 457
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 407-429 5.90e-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: 5.90e-03
                          10        20
                  ....*....|....*....|...
gi 1996192364 407 YQCAECGKAFIQKTTLTVHQRTH 429
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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