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Conserved domains on  [gi|578832927|ref|XP_006722683|]
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zinc finger protein 266 isoform X1 [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;
39-95 1.21e-30

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 113.84  E-value: 1.21e-30
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 578832927    39 VTFDDLAVDFTPEEWTLLDPTQRNLYRDVMLENYKNLATVGYQLFKPSLISWLEQEE 95
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGE 57
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
277-616 3.42e-09

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 59.32  E-value: 3.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832927 277 KPYKCKECGKGFRYSAYLNIHMGTHTGDNPYEC--KECGKAFTRSCQLTQHRKTHTGEKPYKCKDCGRAFTVSSCLSQ-H 353
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSlS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832927 354 MKIHVGEKPYECKECGIAFTRSSQLTEHLKTHTAKDPFECKICGKSFRNS-SCLSDHFRIHTGIKpykckdCGKAFTQNS 432
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTpQSNSLHPPLPANSL------SKDPSSNLS 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832927 433 DLTKHARTHSGERPYECKECGKAFARSSRLSEHTRTHTgEKPFECVKCGKAFAISSNLSGHLRIHTGEKPFECLEC---- 508
Cdd:COG5048  186 LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENS-SSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESprss 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832927 509 -GKAFTHSSSLNNH-MRTHSAK-KPFTCMECGKAFKFPTCVNLHMR--IHTGE--KPYKC--KQCGKSFSYSNSFQLHER 579
Cdd:COG5048  265 lPTASSQSSSPNESdSSSEKGFsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHIL 344

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 578832927 580 THTGEKPYECK--ECGKAFSSSSSFRNHERRHADERLSA 616
Cdd:COG5048  345 LHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQYKDLKN 383
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
39-95 1.21e-30

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 113.84  E-value: 1.21e-30
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 578832927    39 VTFDDLAVDFTPEEWTLLDPTQRNLYRDVMLENYKNLATVGYQLFKPSLISWLEQEE 95
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGE 57
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 38-79 5.54e-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: 94.46  E-value: 5.54e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 578832927   38 SVTFDDLAVDFTPEEWTLLDPTQRNLYRDVMLENYKNLATVG 79
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 39-76 1.60e-18

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: 79.13  E-value: 1.60e-18
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 578832927  39 VTFDDLAVDFTPEEWTLLDPTQRNLYRDVMLENYKNLA 76
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLV 38
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
277-616 3.42e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 59.32  E-value: 3.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832927 277 KPYKCKECGKGFRYSAYLNIHMGTHTGDNPYEC--KECGKAFTRSCQLTQHRKTHTGEKPYKCKDCGRAFTVSSCLSQ-H 353
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSlS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832927 354 MKIHVGEKPYECKECGIAFTRSSQLTEHLKTHTAKDPFECKICGKSFRNS-SCLSDHFRIHTGIKpykckdCGKAFTQNS 432
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTpQSNSLHPPLPANSL------SKDPSSNLS 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832927 433 DLTKHARTHSGERPYECKECGKAFARSSRLSEHTRTHTgEKPFECVKCGKAFAISSNLSGHLRIHTGEKPFECLEC---- 508
Cdd:COG5048  186 LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENS-SSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESprss 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832927 509 -GKAFTHSSSLNNH-MRTHSAK-KPFTCMECGKAFKFPTCVNLHMR--IHTGE--KPYKC--KQCGKSFSYSNSFQLHER 579
Cdd:COG5048  265 lPTASSQSSSPNESdSSSEKGFsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHIL 344

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 578832927 580 THTGEKPYECK--ECGKAFSSSSSFRNHERRHADERLSA 616
Cdd:COG5048  345 LHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQYKDLKN 383
zf-H2C2_2 pfam13465
Zinc-finger double domain;
549-570 6.01e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 6.01e-05
                          10        20
                  ....*....|....*....|..
gi 578832927  549 HMRIHTGEKPYKCKQCGKSFSY 570
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
PHA00733 PHA00733
hypothetical protein
 362-409 7.19e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.16  E-value: 7.19e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 578832927 362 PYECKECGIAFTRSSQLTEHLK--THTAKdpfeCKICGKSFRNSSCLSDH 409
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRytEHSKV----CPVCGKEFRNTDSTLDH 118
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
39-95 1.21e-30

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 113.84  E-value: 1.21e-30
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 578832927    39 VTFDDLAVDFTPEEWTLLDPTQRNLYRDVMLENYKNLATVGYQLFKPSLISWLEQEE 95
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGE 57
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 38-79 5.54e-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: 94.46  E-value: 5.54e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 578832927   38 SVTFDDLAVDFTPEEWTLLDPTQRNLYRDVMLENYKNLATVG 79
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 39-76 1.60e-18

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: 79.13  E-value: 1.60e-18
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 578832927  39 VTFDDLAVDFTPEEWTLLDPTQRNLYRDVMLENYKNLA 76
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLV 38
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
277-616 3.42e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 59.32  E-value: 3.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832927 277 KPYKCKECGKGFRYSAYLNIHMGTHTGDNPYEC--KECGKAFTRSCQLTQHRKTHTGEKPYKCKDCGRAFTVSSCLSQ-H 353
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSlS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832927 354 MKIHVGEKPYECKECGIAFTRSSQLTEHLKTHTAKDPFECKICGKSFRNS-SCLSDHFRIHTGIKpykckdCGKAFTQNS 432
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTpQSNSLHPPLPANSL------SKDPSSNLS 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832927 433 DLTKHARTHSGERPYECKECGKAFARSSRLSEHTRTHTgEKPFECVKCGKAFAISSNLSGHLRIHTGEKPFECLEC---- 508
Cdd:COG5048  186 LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENS-SSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESprss 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832927 509 -GKAFTHSSSLNNH-MRTHSAK-KPFTCMECGKAFKFPTCVNLHMR--IHTGE--KPYKC--KQCGKSFSYSNSFQLHER 579
Cdd:COG5048  265 lPTASSQSSSPNESdSSSEKGFsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHIL 344

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 578832927 580 THTGEKPYECK--ECGKAFSSSSSFRNHERRHADERLSA 616
Cdd:COG5048  345 LHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQYKDLKN 383
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
231-426 2.82e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 56.63  E-value: 2.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832927 231 SFINHSHLQGHLRTHNGESlHEWKECGRGFIHSTDLAVRIQTH----------RSEKPYKCKECGKGFRYSAYLNIHMGT 300
Cdd:COG5048  233 SQLSPKSLLSQSPSSLSSS-DSSSSASESPRSSLPTASSQSSSpnesdsssekGFSLPIKSKQCNISFSRSSPLTRHLRS 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832927 301 --HTGDN--PYECKE--CGKAFTRSCQLTQHRKTHTGEKPYKCKDCGRAFTVSSCL-------SQHMKIHVGEKPYEC-- 365
Cdd:COG5048  312 vnHSGESlkPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLnneppqsLQQYKDLKNDKKSETls 391

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578832927 366 KECGIAFTRSSQLTEHLKTHTAKDP--FECKICGKSFRNSSCLSDHFRIHTGIKPYKCKDCGK 426
Cdd:COG5048  392 NSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS 454
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
361-547 4.64e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.86  E-value: 4.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832927 361 KPYECKECGIAFTRSSQLTEHLKT--HTAKD--PFECKI--CGKSFRNSSCLSDHFRIHTGIKPYKCK--DCGKAFTQNS 432
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGESlkPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832927 433 DLTKHARTH-----SGERPYEC--KECGKAFARSSRLSEHTRTHTGEKPfecvkcgkafaissnlsghlrihtgeKPFEC 505
Cdd:COG5048  368 NNEPPQSLQqykdlKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRP--------------------------YNCKN 421

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 578832927 506 LECGKAFTHSSSLNNHMRTHSAKKPFTCMECGKAFKFPTCVN 547
Cdd:COG5048  422 PPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLSN 463
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
402-605 1.89e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.85  E-value: 1.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832927 402 NSSCLSDHFRIhtgIKPYKCKDCGKAFTQNSDLTKHART--HSGE--RPYECKE--CGKAFARSSRLSEHTRTHTGEKPF 475
Cdd:COG5048  276 NESDSSSEKGF---SLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPA 352

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832927 476 ECV--KCGKAFAISSNLSGHLRIH-----TGEKPFECLecgkaftHSSSLNNHMRTHSAKKPFTCmecgkafkfptcvNL 548
Cdd:COG5048  353 KEKllNSSSKFSPLLNNEPPQSLQqykdlKNDKKSETL-------SNSCIRNFKRDSNLSLHIIT-------------HL 412

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 578832927 549 HMRIHtgekPYKCKQCGKSFSYSNSFQLHERTHTGEKPYECkECGKAFSSSSSFRNH 605
Cdd:COG5048  413 SFRPY----NCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLC-SILKSFRRDLDLSNH 464
zf-H2C2_2 pfam13465
Zinc-finger double domain;
549-570 6.01e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 6.01e-05
                          10        20
                  ....*....|....*....|..
gi 578832927  549 HMRIHTGEKPYKCKQCGKSFSY 570
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
573-598 2.26e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.26e-04
                          10        20
                  ....*....|....*....|....*.
gi 578832927  573 SFQLHERTHTGEKPYECKECGKAFSS 598
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
489-514 4.72e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.72e-04
                          10        20
                  ....*....|....*....|....*.
gi 578832927  489 NLSGHLRIHTGEKPFECLECGKAFTH 514
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
406-430 6.78e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 6.78e-04
                          10        20
                  ....*....|....*....|....*
gi 578832927  406 LSDHFRIHTGIKPYKCKDCGKAFTQ 430
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 419-441 7.68e-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: 7.68e-04
                          10        20
                  ....*....|....*....|...
gi 578832927  419 YKCKDCGKAFTQNSDLTKHARTH 441
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
433-458 8.26e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 8.26e-04
                          10        20
                  ....*....|....*....|....*.
gi 578832927  433 DLTKHARTHSGERPYECKECGKAFAR 458
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
517-541 8.76e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 8.76e-04
                          10        20
                  ....*....|....*....|....*
gi 578832927  517 SLNNHMRTHSAKKPFTCMECGKAFK 541
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
322-345 1.27e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.27e-03
                          10        20
                  ....*....|....*....|....
gi 578832927  322 LTQHRKTHTGEKPYKCKDCGRAFT 345
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 503-525 1.62e-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: 36.12  E-value: 1.62e-03
                          10        20
                  ....*....|....*....|...
gi 578832927  503 FECLECGKAFTHSSSLNNHMRTH 525
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
350-374 1.72e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.72e-03
                          10        20
                  ....*....|....*....|....*
gi 578832927  350 LSQHMKIHVGEKPYECKECGIAFTR 374
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
293-318 1.98e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 1.98e-03
                          10        20
                  ....*....|....*....|....*.
gi 578832927  293 YLNIHMGTHTGDNPYECKECGKAFTR 318
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 499-582 2.33e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.86  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832927 499 GEKPFEC--LECGKAFTHSSSLNNHMRtHSAKKPFTcmecgkafkFPTCVNLHMRIHTGE-KPYKCKQCGKSFSYSNSFQ 575
Cdd:COG5189  346 DGKPYKCpvEGCNKKYKNQNGLKYHML-HGHQNQKL---------HENPSPEKMNIFSAKdKPYRCEVCDKRYKNLNGLK 415


                 ....*..
gi 578832927 576 LHeRTHT 582
Cdd:COG5189  416 YH-RKHS 421
zf-H2C2_2 pfam13465
Zinc-finger double domain;
461-485 7.17e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 7.17e-03
                          10        20
                  ....*....|....*....|....*
gi 578832927  461 RLSEHTRTHTGEKPFECVKCGKAFA 485
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
PHA00733 PHA00733
hypothetical protein
 362-409 7.19e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.16  E-value: 7.19e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 578832927 362 PYECKECGIAFTRSSQLTEHLK--THTAKdpfeCKICGKSFRNSSCLSDH 409
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRytEHSKV----CPVCGKEFRNTDSTLDH 118
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 307-329 7.63e-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: 7.63e-03
                          10        20
                  ....*....|....*....|...
gi 578832927  307 YECKECGKAFTRSCQLTQHRKTH 329
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 363-385 8.34e-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: 8.34e-03
                          10        20
                  ....*....|....*....|...
gi 578832927  363 YECKECGIAFTRSSQLTEHLKTH 385
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 587-609 9.29e-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: 9.29e-03
                          10        20
                  ....*....|....*....|...
gi 578832927  587 YECKECGKAFSSSSSFRNHERRH 609
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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