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Conserved domains on  [gi|21687264|ref|NP_653294|]
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zinc finger protein 558 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|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;
43-100 6.24e-33

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 117.69  E-value: 6.24e-33
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 21687264     43 VTFEDVAVEFTQEEWALLDPAQRTLYRDVMLENCRNLASLGCRVNKPSLISQLEQDKK 100
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEE 58
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
162-398 1.76e-07

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.16  E-value: 1.76e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687264 162 STKSNLTQHKRIHTGEKPYDCSQCGKSFSSRSYLTIHKRIHNGEKPYECNHCGKAFSDPSSLRLHLRIHTGEKPYECNQC 241
Cdd:COG5048 181 SSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASES 260

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687264 242 FHVFRTSCNLKSHKRIHTGE-------NHHECNQCGKAFSTRSSLTGHN--SIHTGE--KPYEC--HDCGKTFRKSSYLT 308
Cdd:COG5048 261 PRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCpySLCGKLFSRNDALK 340

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687264 309 QHVRTHTGEKPYECNEC-------GKSFSSSFSLTVHKRIHTGEKPYECSD--CGKAFNNLSAVKKHLRTHTGEKPYECN 379
Cdd:COG5048 341 RHILLHTSISPAKEKLLnssskfsPLLNNEPPQSLQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPYNCK 420

                       250       260
                ....*....|....*....|.
gi 21687264 380 --HCGKSFTSNSYLSVHKRIH 398
Cdd:COG5048 421 npPCSKSFNRHYNLIPHKKIH 441
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
43-100 6.24e-33

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 117.69  E-value: 6.24e-33
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 21687264     43 VTFEDVAVEFTQEEWALLDPAQRTLYRDVMLENCRNLASLGCRVNKPSLISQLEQDKK 100
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEE 58
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 42-83 2.91e-27

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: 102.16  E-value: 2.91e-27
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 21687264    42 LVTFEDVAVEFTQEEWALLDPAQRTLYRDVMLENCRNLASLG 83
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 43-82 3.47e-23

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: 91.07  E-value: 3.47e-23
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 21687264  43 VTFEDVAVEFTQEEWALLDPAQRTLYRDVMLENCRNLASL 82
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
162-398 1.76e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.16  E-value: 1.76e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687264 162 STKSNLTQHKRIHTGEKPYDCSQCGKSFSSRSYLTIHKRIHNGEKPYECNHCGKAFSDPSSLRLHLRIHTGEKPYECNQC 241
Cdd:COG5048 181 SSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASES 260

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687264 242 FHVFRTSCNLKSHKRIHTGE-------NHHECNQCGKAFSTRSSLTGHN--SIHTGE--KPYEC--HDCGKTFRKSSYLT 308
Cdd:COG5048 261 PRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCpySLCGKLFSRNDALK 340

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687264 309 QHVRTHTGEKPYECNEC-------GKSFSSSFSLTVHKRIHTGEKPYECSD--CGKAFNNLSAVKKHLRTHTGEKPYECN 379
Cdd:COG5048 341 RHILLHTSISPAKEKLLnssskfsPLLNNEPPQSLQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPYNCK 420

                       250       260
                ....*....|....*....|.
gi 21687264 380 --HCGKSFTSNSYLSVHKRIH 398
Cdd:COG5048 421 npPCSKSFNRHYNLIPHKKIH 441
zf-H2C2_2 pfam13465
Zinc-finger double domain;
306-331 3.11e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 3.11e-05
                          10        20
                  ....*....|....*....|....*.
gi 21687264   306 YLTQHVRTHTGEKPYECNECGKSFSS 331
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
43-100 6.24e-33

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 117.69  E-value: 6.24e-33
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 21687264     43 VTFEDVAVEFTQEEWALLDPAQRTLYRDVMLENCRNLASLGCRVNKPSLISQLEQDKK 100
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEE 58
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 42-83 2.91e-27

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: 102.16  E-value: 2.91e-27
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 21687264    42 LVTFEDVAVEFTQEEWALLDPAQRTLYRDVMLENCRNLASLG 83
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 43-82 3.47e-23

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: 91.07  E-value: 3.47e-23
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 21687264  43 VTFEDVAVEFTQEEWALLDPAQRTLYRDVMLENCRNLASL 82
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
162-398 1.76e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.16  E-value: 1.76e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687264 162 STKSNLTQHKRIHTGEKPYDCSQCGKSFSSRSYLTIHKRIHNGEKPYECNHCGKAFSDPSSLRLHLRIHTGEKPYECNQC 241
Cdd:COG5048 181 SSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASES 260

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687264 242 FHVFRTSCNLKSHKRIHTGE-------NHHECNQCGKAFSTRSSLTGHN--SIHTGE--KPYEC--HDCGKTFRKSSYLT 308
Cdd:COG5048 261 PRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCpySLCGKLFSRNDALK 340

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687264 309 QHVRTHTGEKPYECNEC-------GKSFSSSFSLTVHKRIHTGEKPYECSD--CGKAFNNLSAVKKHLRTHTGEKPYECN 379
Cdd:COG5048 341 RHILLHTSISPAKEKLLnssskfsPLLNNEPPQSLQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPYNCK 420

                       250       260
                ....*....|....*....|.
gi 21687264 380 --HCGKSFTSNSYLSVHKRIH 398
Cdd:COG5048 421 npPCSKSFNRHYNLIPHKKIH 441
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
164-395 9.72e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.85  E-value: 9.72e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687264 164 KSNLTQHKRIHTGEKPYDCSQCG----KSFSSRSYLTIHKRIHNGEKPYECNHCG--KAFSDPSSLRLHLRIHTG-EKPY 236
Cdd:COG5048 211 IPSSSSDQNLENSSSSLPLTTNSqlspKSLLSQSPSSLSSSDSSSSASESPRSSLptASSQSSSPNESDSSSEKGfSLPI 290

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687264 237 ECNQCFHVFRTSCNLKSHKR--IHTGENH--HEC--NQCGKAFSTRSSLTGHNSIHTGEKPYECH--DCGKTFRKSSY-- 306
Cdd:COG5048 291 KSKQCNISFSRSSPLTRHLRsvNHSGESLkpFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNne 370

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687264 307 ---LTQHVRTHTGEKPYEC--NECGKSFSSSFSLTVHKRIHTGEKPYEC--SDCGKAFNNLSAVKKHLRTHTGEKPYECN 379
Cdd:COG5048 371 ppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHTNHAPLLCS 450

                       250
                ....*....|....*.
gi 21687264 380 HCGKSFTSNSYLSVHK 395
Cdd:COG5048 451 ILKSFRRDLDLSNHGK 466
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
150-398 5.12e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.54  E-value: 5.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687264 150 KLNECNQCFKVFSTKSNLTQHKRIHTGEKPYDCSQ--CGKSFSSRSYLTIHKRIHNGEKPYECNHCG------KAFSDPS 221
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLplsnskASSSSLS 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687264 222 SLRLHLRIHTGEKPYECNQ-------CFHVFRT--------SCNLKSHKRIHTGENHHECNQ---CGKAFSTRSSLTGHN 283
Cdd:COG5048 112 SSSSNSNDNNLLSSHSLPPssrdpqlPDLLSISnlrnnplpGNNSSSVNTPQSNSLHPPLPAnslSKDPSSNLSLLISSN 191

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687264 284 SIHTGEKPYECHDCGKT------------FRKSSYLTQHVRTHTGEK------------PYECNECGKSFSSSFSLTVHK 339
Cdd:COG5048 192 VSTSIPSSSENSPLSSSysipssssdqnlENSSSSLPLTTNSQLSPKsllsqspsslssSDSSSSASESPRSSLPTASSQ 271

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21687264 340 RIH----------TGEKPYECSDCGKAFNNLSAVKKHLRT--HTGE--KPYECNH--CGKSFTSNSYLSVHKRIH 398
Cdd:COG5048 272 SSSpnesdsssekGFSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLH 346
zf-H2C2_2 pfam13465
Zinc-finger double domain;
306-331 3.11e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 3.11e-05
                          10        20
                  ....*....|....*....|....*.
gi 21687264   306 YLTQHVRTHTGEKPYECNECGKSFSS 331
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
166-191 6.35e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 6.35e-05
                          10        20
                  ....*....|....*....|....*.
gi 21687264   166 NLTQHKRIHTGEKPYDCSQCGKSFSS 191
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
362-387 7.01e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 7.01e-05
                          10        20
                  ....*....|....*....|....*.
gi 21687264   362 AVKKHLRTHTGEKPYECNHCGKSFTS 387
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
250-275 1.94e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 1.94e-04
                          10        20
                  ....*....|....*....|....*.
gi 21687264   250 NLKSHKRIHTGENHHECNQCGKAFST 275
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
334-359 2.02e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 2.02e-04
                          10        20
                  ....*....|....*....|....*.
gi 21687264   334 SLTVHKRIHTGEKPYECSDCGKAFNN 359
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 212-315 3.68e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 42.40  E-value: 3.68e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687264 212 HCGKAFSDPSSLRLHLRihtGEKPYECN--QCFHVFRTSCNLKSHKRihtgenHHECNQcgkAFSTRSSLTGHNSIHTGE 289
Cdd:COG5189 329 HGGERNIDTPSRMLKVK---DGKPYKCPveGCNKKYKNQNGLKYHML------HGHQNQ---KLHENPSPEKMNIFSAKD 396

                        90       100
                ....*....|....*....|....*.
gi 21687264 290 KPYECHDCGKTFRKSSYLTQHvRTHT 315
Cdd:COG5189 397 KPYRCEVCDKRYKNLNGLKYH-RKHS 421
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 316-371 4.02e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 42.40  E-value: 4.02e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21687264 316 GEKPYECN--ECGKSFSSSFSLTVHKR-------------------IHTGEKPYECSDCGKAFNNLSAVKKHlRTHT 371
Cdd:COG5189 346 DGKPYKCPveGCNKKYKNQNGLKYHMLhghqnqklhenpspekmniFSAKDKPYRCEVCDKRYKNLNGLKYH-RKHS 421
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 292-314 9.05e-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: 36.51  E-value: 9.05e-04
                          10        20
                  ....*....|....*....|...
gi 21687264   292 YECHDCGKTFRKSSYLTQHVRTH 314
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 208-230 1.28e-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: 1.28e-03
                          10        20
                  ....*....|....*....|...
gi 21687264   208 YECNHCGKAFSDPSSLRLHLRIH 230
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
194-218 2.35e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 2.35e-03
                          10        20
                  ....*....|....*....|....*
gi 21687264   194 YLTIHKRIHNGEKPYECNHCGKAFS 218
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 376-398 3.24e-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: 3.24e-03
                          10        20
                  ....*....|....*....|...
gi 21687264   376 YECNHCGKSFTSNSYLSVHKRIH 398
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
155-277 4.19e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 39.29  E-value: 4.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687264 155 NQCFKVFSTKSNLTQHKRIHTGEKPYDC--SQCGKSFS------SRSYLTIHKRIHNgEKPYECNH--CGKAFSDPSSLR 224
Cdd:COG5048 327 SLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSpllnnePPQSLQQYKDLKN-DKKSETLSnsCIRNFKRDSNLS 405

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21687264 225 LHLRIHTGEKPYECN--QCFHVFRTSCNLKSHKRIHTGENHHECNQCGKAFSTRS 277
Cdd:COG5048 406 LHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 320-342 6.76e-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: 6.76e-03
                          10        20
                  ....*....|....*....|...
gi 21687264   320 YECNECGKSFSSSFSLTVHKRIH 342
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
222-241 9.86e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.50  E-value: 9.86e-03
                          10        20
                  ....*....|....*....|
gi 21687264   222 SLRLHLRIHTGEKPYECNQC 241
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPEC 20
 
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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