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Conserved domains on  [gi|33438598|ref|NP_872415|]
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zinc finger protein 677 isoform a [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;
9-59 1.69e-25

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 99.20  E-value: 1.69e-25
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 33438598      9 TFKDVAIEFSQEEWECLDPAQRALYRDVMLENYRNLLSLdEDNIPPEDDIS 59
Cdd:smart00349   2 TFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSL-GFQVPKPDLIS 51
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
194-540 1.03e-05

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.15  E-value: 1.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33438598 194 SLQAQLAELQRFQTGEKMYECNPVEKSINSSSVSPLPPCVKNICNKYRKILKYPLLHTQYGRTH--IREKSYKCNDCGKA 271
Cdd:COG5048  44 SRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSssLSSSSSNSNDNNLL 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33438598 272 FSKSSNLTNHQRIHS---------GQRPYKCNECGKAFNQCSNL-------------------TRHQRVHTGEKPYQCNI 323
Cdd:COG5048 124 SSHSLPPSSRDPQLPdllsisnlrNNPLPGNNSSSVNTPQSNSLhpplpanslskdpssnlslLISSNVSTSIPSSSENS 203

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33438598 324 CGKVCSQNSNLASHQRMHTGEKPYKCNECGKAF------IQRSHLWGHERIHTGEKPYKCNECDKAFAERSSLTQHKRIH 397
Cdd:COG5048 204 PLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpksllsQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSE 283

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33438598 398 TG-EKPYICNECGKAFKQCSHLTRHQN--IHPGE--KPHKCNV--CGRAFIQSSSLVEHQRIHTGEKPYKC--NKCDKAF 468
Cdd:COG5048 284 KGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKF 363

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33438598 469 IKRSHLWGHQRT--HTGEKPYKCTE-----CGKAFTERSNLTQHKKIHTGEKPY--KCTECGKAFTQFANLTRHQKIHIE 539
Cdd:COG5048 364 SPLLNNEPPQSLqqYKDLKNDKKSEtlsnsCIRNFKRDSNLSLHIITHLSFRPYncKNPPCSKSFNRHYNLIPHKKIHTN 443


                .
gi 33438598 540 K 540
Cdd:COG5048 444 H 444
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
9-59 1.69e-25

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 99.20  E-value: 1.69e-25
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 33438598      9 TFKDVAIEFSQEEWECLDPAQRALYRDVMLENYRNLLSLdEDNIPPEDDIS 59
Cdd:smart00349   2 TFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSL-GFQVPKPDLIS 51
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 9-48 1.25e-24

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: 96.39  E-value: 1.25e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 33438598     9 TFKDVAIEFSQEEWECLDPAQRALYRDVMLENYRNLLSLD 48
Cdd:pfam01352   3 TFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 9-47 2.93e-22

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: 89.53  E-value: 2.93e-22
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 33438598   9 TFKDVAIEFSQEEWECLDPAQRALYRDVMLENYRNLLSL 47
Cdd:cd07765   2 TFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
194-540 1.03e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.15  E-value: 1.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33438598 194 SLQAQLAELQRFQTGEKMYECNPVEKSINSSSVSPLPPCVKNICNKYRKILKYPLLHTQYGRTH--IREKSYKCNDCGKA 271
Cdd:COG5048  44 SRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSssLSSSSSNSNDNNLL 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33438598 272 FSKSSNLTNHQRIHS---------GQRPYKCNECGKAFNQCSNL-------------------TRHQRVHTGEKPYQCNI 323
Cdd:COG5048 124 SSHSLPPSSRDPQLPdllsisnlrNNPLPGNNSSSVNTPQSNSLhpplpanslskdpssnlslLISSNVSTSIPSSSENS 203

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33438598 324 CGKVCSQNSNLASHQRMHTGEKPYKCNECGKAF------IQRSHLWGHERIHTGEKPYKCNECDKAFAERSSLTQHKRIH 397
Cdd:COG5048 204 PLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpksllsQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSE 283

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33438598 398 TG-EKPYICNECGKAFKQCSHLTRHQN--IHPGE--KPHKCNV--CGRAFIQSSSLVEHQRIHTGEKPYKC--NKCDKAF 468
Cdd:COG5048 284 KGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKF 363

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33438598 469 IKRSHLWGHQRT--HTGEKPYKCTE-----CGKAFTERSNLTQHKKIHTGEKPY--KCTECGKAFTQFANLTRHQKIHIE 539
Cdd:COG5048 364 SPLLNNEPPQSLqqYKDLKNDKKSEtlsnsCIRNFKRDSNLSLHIITHLSFRPYncKNPPCSKSFNRHYNLIPHKKIHTN 443


                .
gi 33438598 540 K 540
Cdd:COG5048 444 H 444
zf-H2C2_2 pfam13465
Zinc-finger double domain;
501-526 3.39e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 3.39e-05
                          10        20
                  ....*....|....*....|....*.
gi 33438598   501 NLTQHKKIHTGEKPYKCTECGKAFTQ 526
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
9-59 1.69e-25

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 99.20  E-value: 1.69e-25
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 33438598      9 TFKDVAIEFSQEEWECLDPAQRALYRDVMLENYRNLLSLdEDNIPPEDDIS 59
Cdd:smart00349   2 TFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSL-GFQVPKPDLIS 51
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 9-48 1.25e-24

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: 96.39  E-value: 1.25e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 33438598     9 TFKDVAIEFSQEEWECLDPAQRALYRDVMLENYRNLLSLD 48
Cdd:pfam01352   3 TFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 9-47 2.93e-22

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: 89.53  E-value: 2.93e-22
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 33438598   9 TFKDVAIEFSQEEWECLDPAQRALYRDVMLENYRNLLSL 47
Cdd:cd07765   2 TFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
194-540 1.03e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.15  E-value: 1.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33438598 194 SLQAQLAELQRFQTGEKMYECNPVEKSINSSSVSPLPPCVKNICNKYRKILKYPLLHTQYGRTH--IREKSYKCNDCGKA 271
Cdd:COG5048  44 SRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSssLSSSSSNSNDNNLL 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33438598 272 FSKSSNLTNHQRIHS---------GQRPYKCNECGKAFNQCSNL-------------------TRHQRVHTGEKPYQCNI 323
Cdd:COG5048 124 SSHSLPPSSRDPQLPdllsisnlrNNPLPGNNSSSVNTPQSNSLhpplpanslskdpssnlslLISSNVSTSIPSSSENS 203

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33438598 324 CGKVCSQNSNLASHQRMHTGEKPYKCNECGKAF------IQRSHLWGHERIHTGEKPYKCNECDKAFAERSSLTQHKRIH 397
Cdd:COG5048 204 PLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpksllsQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSE 283

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33438598 398 TG-EKPYICNECGKAFKQCSHLTRHQN--IHPGE--KPHKCNV--CGRAFIQSSSLVEHQRIHTGEKPYKC--NKCDKAF 468
Cdd:COG5048 284 KGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKF 363

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33438598 469 IKRSHLWGHQRT--HTGEKPYKCTE-----CGKAFTERSNLTQHKKIHTGEKPY--KCTECGKAFTQFANLTRHQKIHIE 539
Cdd:COG5048 364 SPLLNNEPPQSLqqYKDLKNDKKSEtlsnsCIRNFKRDSNLSLHIITHLSFRPYncKNPPCSKSFNRHYNLIPHKKIHTN 443


                .
gi 33438598 540 K 540
Cdd:COG5048 444 H 444
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
255-583 1.71e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.38  E-value: 1.71e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33438598 255 RTHIREKSYKCND--CGKAFSKSSNLTNHQRIHSGQRPYKCNECGKAFNQ--CSNLTRHQRVHT--GEKPYQCNICGKVC 328
Cdd:COG5048  54 RSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSkaSSSSLSSSSSNSndNNLLSSHSLPPSSR 133

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33438598 329 SQNSNLASHQRMHTGEKPYKCNECGKAFIQRSHLWG-------------------HERIHTGEKPYKCNECDKAFAERSS 389
Cdd:COG5048 134 DPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPplpanslskdpssnlslliSSNVSTSIPSSSENSPLSSSYSIPS 213

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33438598 390 LTQHKRIHTGEKPYICNECGKAFKQCSHLTRHQNIHPGEKPHKCNVCGRAFIQSSSLVEHQRIHTGE-------KPYKCN 462
Cdd:COG5048 214 SSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSK 293

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33438598 463 KCDKAFIKRSHLWGHQRT--HTGE--KPYKCTE--CGKAFTERSNLTQHKKIHTGEKPYKC--TECGKAFTQFANLTRHQ 534
Cdd:COG5048 294 QCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQ 373

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 33438598 535 KIHIEKKHCKHNIHGNALFQS--SNLGDHQKSYNREKHIKYNETKIKYSSC 583
Cdd:COG5048 374 SLQQYKDLKNDKKSETLSNSCirNFKRDSNLSLHIITHLSFRPYNCKNPPC 424
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
288-584 1.74e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.38  E-value: 1.74e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33438598 288 QRPYKCNECGKAFNQCSNLTRHQRVHTGEKPYQCN--ICGKVCSQNSNLASHQRMHTGEKPYKCN--ECGKAFIQRSHLW 363
Cdd:COG5048  31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSksLPLSNSKASSSSL 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33438598 364 GHErIHTGEKPYKCNECDKAFAERSSLTQHKRIHT---GEKPYICNECGKAFKQCSHL-------------------TRH 421
Cdd:COG5048 111 SSS-SSNSNDNNLLSSHSLPPSSRDPQLPDLLSISnlrNNPLPGNNSSSVNTPQSNSLhpplpanslskdpssnlslLIS 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33438598 422 QNIHPGEKPHKCNVCGRAFIQSSSLVEHQRIHTGEKPYKCNKCDKAFIKRSHLWGHQRTHTGEKPYKCTECGKAFTERSN 501
Cdd:COG5048 190 SNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTAS 269

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33438598 502 LTQHKKIHTGE-------KPYKCTECGKAFTQFANLTRHQ--KIHIEKKHCKHNIHGNALFQSSNLGDHQKSyNREKHIK 572
Cdd:COG5048 270 SQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLrsVNHSGESLKPFSCPYSLCGKLFSRNDALKR-HILLHTS 348

                       330
                ....*....|..
gi 33438598 573 YNETKIKYSSCT 584
Cdd:COG5048 349 ISPAKEKLLNSS 360
zf-H2C2_2 pfam13465
Zinc-finger double domain;
501-526 3.39e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 3.39e-05
                          10        20
                  ....*....|....*....|....*.
gi 33438598   501 NLTQHKKIHTGEKPYKCTECGKAFTQ 526
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
333-358 5.54e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 5.54e-05
                          10        20
                  ....*....|....*....|....*.
gi 33438598   333 NLASHQRMHTGEKPYKCNECGKAFIQ 358
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
473-497 2.39e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.39e-04
                          10        20
                  ....*....|....*....|....*
gi 33438598   473 HLWGHQRTHTGEKPYKCTECGKAFT 497
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
361-385 2.46e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.46e-04
                          10        20
                  ....*....|....*....|....*
gi 33438598   361 HLWGHERIHTGEKPYKCNECDKAFA 385
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
445-468 3.86e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 3.86e-04
                          10        20
                  ....*....|....*....|....
gi 33438598   445 SLVEHQRIHTGEKPYKCNKCDKAF 468
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
277-302 4.26e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.26e-04
                          10        20
                  ....*....|....*....|....*.
gi 33438598   277 NLTNHQRIHSGQRPYKCNECGKAFNQ 302
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 263-285 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 33438598   263 YKCNDCGKAFSKSSNLTNHQRIH 285
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
389-414 1.10e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.10e-03
                          10        20
                  ....*....|....*....|....*.
gi 33438598   389 SLTQHKRIHTGEKPYICNECGKAFKQ 414
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 291-313 1.12e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.51  E-value: 1.12e-03
                          10        20
                  ....*....|....*....|...
gi 33438598   291 YKCNECGKAFNQCSNLTRHQRVH 313
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
305-330 1.43e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.43e-03
                          10        20
                  ....*....|....*....|....*.
gi 33438598   305 NLTRHQRVHTGEKPYQCNICGKVCSQ 330
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 403-425 4.26e-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: 4.26e-03
                          10        20
                  ....*....|....*....|...
gi 33438598   403 YICNECGKAFKQCSHLTRHQNIH 425
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 515-537 4.61e-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: 4.61e-03
                          10        20
                  ....*....|....*....|...
gi 33438598   515 YKCTECGKAFTQFANLTRHQKIH 537
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 319-341 4.66e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.58  E-value: 4.66e-03
                          10        20
                  ....*....|....*....|...
gi 33438598   319 YQCNICGKVCSQNSNLASHQRMH 341
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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