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Conserved domains on  [gi|1913184172|ref|NP_001374342|]
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zinc finger protein 544 isoform 12 [Homo sapiens]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204794)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
68-127 1.10e-27

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 106.14  E-value: 1.10e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184172   68 VCFEDVAMAFTQEEWEQLDLAQRTLYREVTLETWEHIVSLGLFLSKSDVISQLEQEEDLC 127
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPW 60
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
460-753 9.68e-18

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 86.67  E-value: 9.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184172 460 KPYECDLCGKSFTQRSKLITHQRIHTGEKPYQC--IECRKSFRWNSNLIVHQRIHTGEKPYECTHCGKS--FSQSYELVT 535
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLsnSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184172 536 HKRTHTgEKPFKCTQCGKSFSQKYDLV--VHQRTHTGEKPYE-CNLCGKSFSQSSKLI-------------------THQ 593
Cdd:COG5048   112 SSSSNS-NDNNLLSSHSLPPSSRDPQLpdLLSISNLRNNPLPgNNSSSVNTPQSNSLHpplpanslskdpssnlsllISS 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184172 594 RIHTGEKPYQCIECGKSFRWNSNLVIHQRIHTGEKPYDCTHCGKSFSQSYQLVAHKRTHTGEKPYECNECGKAFNRSTQL 673
Cdd:COG5048   191 NVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASS 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184172 674 IRHLQIHTGE-------KPYKCNQCNKAFARSSYLVMHQRT--HTGE--KPFEC--SQCGKAFSGSSNLLSHHRIHSGEK 740
Cdd:COG5048   271 QSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSIS 350

                         330
                  ....*....|....*
gi 1913184172 741 PYEC--SDCGKSFRQ 753
Cdd:COG5048   351 PAKEklLNSSSKFSP 365
zf-H2C2_2 pfam13465
Zinc-finger double domain;
424-445 3.13e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 3.13e-04
                          10        20
                  ....*....|....*....|..
gi 1913184172 424 HQRTHTGEKPFECTQCGKSFSQ 445
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
68-127 1.10e-27

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 106.14  E-value: 1.10e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184172   68 VCFEDVAMAFTQEEWEQLDLAQRTLYREVTLETWEHIVSLGLFLSKSDVISQLEQEEDLC 127
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPW 60
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 67-108 5.61e-19

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: 80.59  E-value: 5.61e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1913184172  67 SVCFEDVAMAFTQEEWEQLDLAQRTLYREVTLETWEHIVSLG 108
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
460-753 9.68e-18

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 86.67  E-value: 9.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184172 460 KPYECDLCGKSFTQRSKLITHQRIHTGEKPYQC--IECRKSFRWNSNLIVHQRIHTGEKPYECTHCGKS--FSQSYELVT 535
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLsnSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184172 536 HKRTHTgEKPFKCTQCGKSFSQKYDLV--VHQRTHTGEKPYE-CNLCGKSFSQSSKLI-------------------THQ 593
Cdd:COG5048   112 SSSSNS-NDNNLLSSHSLPPSSRDPQLpdLLSISNLRNNPLPgNNSSSVNTPQSNSLHpplpanslskdpssnlsllISS 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184172 594 RIHTGEKPYQCIECGKSFRWNSNLVIHQRIHTGEKPYDCTHCGKSFSQSYQLVAHKRTHTGEKPYECNECGKAFNRSTQL 673
Cdd:COG5048   191 NVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASS 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184172 674 IRHLQIHTGE-------KPYKCNQCNKAFARSSYLVMHQRT--HTGE--KPFEC--SQCGKAFSGSSNLLSHHRIHSGEK 740
Cdd:COG5048   271 QSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSIS 350

                         330
                  ....*....|....*
gi 1913184172 741 PYEC--SDCGKSFRQ 753
Cdd:COG5048   351 PAKEklLNSSSKFSP 365
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 68-107 1.05e-17

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: 76.82  E-value: 1.05e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1913184172  68 VCFEDVAMAFTQEEWEQLDLAQRTLYREVTLETWEHIVSL 107
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
zf-H2C2_2 pfam13465
Zinc-finger double domain;
532-557 3.99e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 3.99e-05
                          10        20
                  ....*....|....*....|....*.
gi 1913184172 532 ELVTHKRTHTGEKPFKCTQCGKSFSQ 557
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
424-445 3.13e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 3.13e-04
                          10        20
                  ....*....|....*....|..
gi 1913184172 424 HQRTHTGEKPFECTQCGKSFSQ 445
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
68-127 1.10e-27

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 106.14  E-value: 1.10e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184172   68 VCFEDVAMAFTQEEWEQLDLAQRTLYREVTLETWEHIVSLGLFLSKSDVISQLEQEEDLC 127
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPW 60
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 67-108 5.61e-19

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: 80.59  E-value: 5.61e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1913184172  67 SVCFEDVAMAFTQEEWEQLDLAQRTLYREVTLETWEHIVSLG 108
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
460-753 9.68e-18

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 86.67  E-value: 9.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184172 460 KPYECDLCGKSFTQRSKLITHQRIHTGEKPYQC--IECRKSFRWNSNLIVHQRIHTGEKPYECTHCGKS--FSQSYELVT 535
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLsnSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184172 536 HKRTHTgEKPFKCTQCGKSFSQKYDLV--VHQRTHTGEKPYE-CNLCGKSFSQSSKLI-------------------THQ 593
Cdd:COG5048   112 SSSSNS-NDNNLLSSHSLPPSSRDPQLpdLLSISNLRNNPLPgNNSSSVNTPQSNSLHpplpanslskdpssnlsllISS 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184172 594 RIHTGEKPYQCIECGKSFRWNSNLVIHQRIHTGEKPYDCTHCGKSFSQSYQLVAHKRTHTGEKPYECNECGKAFNRSTQL 673
Cdd:COG5048   191 NVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASS 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184172 674 IRHLQIHTGE-------KPYKCNQCNKAFARSSYLVMHQRT--HTGE--KPFEC--SQCGKAFSGSSNLLSHHRIHSGEK 740
Cdd:COG5048   271 QSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSIS 350

                         330
                  ....*....|....*
gi 1913184172 741 PYEC--SDCGKSFRQ 753
Cdd:COG5048   351 PAKEklLNSSSKFSP 365
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 68-107 1.05e-17

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: 76.82  E-value: 1.05e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1913184172  68 VCFEDVAMAFTQEEWEQLDLAQRTLYREVTLETWEHIVSL 107
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
401-755 1.72e-14

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 76.66  E-value: 1.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184172 401 IQTTEKPSVCNQCGKSFSCC--KLIHQRTHTGEKPFECTQ--CGKSFSQSYDLVIHQRTHTGEKPYECDLCGKSFTQ--- 473
Cdd:COG5048    27 LSNAPRPDSCPNCTDSFSRLehLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSkas 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184172 474 -----------------RSKLITHQRIHTGEKP------YQCIECRKSFRWNSNLIVHQRIHtgeKPYECTHCGKSFSQS 530
Cdd:COG5048   107 ssslsssssnsndnnllSSHSLPPSSRDPQLPDllsisnLRNNPLPGNNSSSVNTPQSNSLH---PPLPANSLSKDPSSN 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184172 531 YELVTHKRTHTGEKPFKCTQCGKSFSQKYDLVVHQRTHTGEKPYECNLCGKSFSQSSKLITHQRIHTGEKPYQCIECGKS 610
Cdd:COG5048   184 LSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRS 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184172 611 FRWNSNLVIHQRIHTGE-------KPYDCTHCGKSFSQSYQLVAHKRT--HTGE--KPYECNE--CGKAFNRSTQLIRHL 677
Cdd:COG5048   264 SLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHI 343

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184172 678 QIHTGEKPYKC-------------------------------------NQCNKAFARSSYLVMHQRTHTGEKP--FECSQ 718
Cdd:COG5048   344 LLHTSISPAKEkllnssskfspllnneppqslqqykdlkndkksetlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPP 423

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1913184172 719 CGKAFSGSSNLLSHHRIHSGEKPYECSDCGKSFRQQS 755
Cdd:COG5048   424 CSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
405-700 4.56e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 65.87  E-value: 4.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184172 405 EKPSVCNQCGKSFSCCKLIHQRTHTGEKPFECTQCGKSFSQSYDLVIHQRTHTGEKPYECDLCGKSFTQRSKLITHQRIH 484
Cdd:COG5048   170 PLPANSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLS 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184172 485 TGEKPYQCIECRKSFRWNSNLIVHQrihtgekpyecthcgksfSQSYELVTHKRTHTgekPFKCTQCGKSFSQKYDLVVH 564
Cdd:COG5048   250 SSDSSSSASESPRSSLPTASSQSSS------------------PNESDSSSEKGFSL---PIKSKQCNISFSRSSPLTRH 308

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184172 565 QRT--HTGE--KPYEC--NLCGKSFSQSSKLITHQRIHTGEKPYQCIEC-------GKSFRWNSNLVIHQRIHTGEKPYD 631
Cdd:COG5048   309 LRSvnHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKLLnssskfsPLLNNEPPQSLQQYKDLKNDKKSE 388

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1913184172 632 CTH--CGKSFSQSYQLVAHKRTHTGEKPYECN--ECGKAFNRSTQLIRHLQIHTGEKPYKCNQCNKAFARSSY 700
Cdd:COG5048   389 TLSnsCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDL 461
zf-H2C2_2 pfam13465
Zinc-finger double domain;
532-557 3.99e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 3.99e-05
                          10        20
                  ....*....|....*....|....*.
gi 1913184172 532 ELVTHKRTHTGEKPFKCTQCGKSFSQ 557
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
504-529 8.75e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 8.75e-05
                          10        20
                  ....*....|....*....|....*.
gi 1913184172 504 NLIVHQRIHTGEKPYECTHCGKSFSQ 529
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
645-669 1.84e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.84e-04
                          10        20
                  ....*....|....*....|....*
gi 1913184172 645 LVAHKRTHTGEKPYECNECGKAFNR 669
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
448-473 1.88e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.88e-04
                          10        20
                  ....*....|....*....|....*.
gi 1913184172 448 DLVIHQRTHTGEKPYECDLCGKSFTQ 473
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
700-724 1.88e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.88e-04
                          10        20
                  ....*....|....*....|....*
gi 1913184172 700 YLVMHQRTHTGEKPFECSQCGKAFS 724
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
560-585 1.95e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.95e-04
                          10        20
                  ....*....|....*....|....*.
gi 1913184172 560 DLVVHQRTHTGEKPYECNLCGKSFSQ 585
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
424-445 3.13e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 3.13e-04
                          10        20
                  ....*....|....*....|..
gi 1913184172 424 HQRTHTGEKPFECTQCGKSFSQ 445
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
616-641 3.29e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 3.29e-04
                          10        20
                  ....*....|....*....|....*.
gi 1913184172 616 NLVIHQRIHTGEKPYDCTHCGKSFSQ 641
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
589-611 3.85e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.85e-04
                          10        20
                  ....*....|....*....|...
gi 1913184172 589 LITHQRIHTGEKPYQCIECGKSF 611
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
728-753 4.64e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 4.64e-04
                          10        20
                  ....*....|....*....|....*.
gi 1913184172 728 NLLSHHRIHSGEKPYECSDCGKSFRQ 753
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
673-697 4.68e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 4.68e-04
                          10        20
                  ....*....|....*....|....*
gi 1913184172 673 LIRHLQIHTGEKPYKCNQCNKAFAR 697
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
477-499 7.80e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 7.80e-04
                          10        20
                  ....*....|....*....|...
gi 1913184172 477 LITHQRIHTGEKPYQCIECRKSF 499
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 742-764 8.24e-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: 37.28  E-value: 8.24e-04
                          10        20
                  ....*....|....*....|...
gi 1913184172 742 YECSDCGKSFRQQSQLVVHRRTH 764
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 546-568 1.16e-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: 36.89  E-value: 1.16e-03
                          10        20
                  ....*....|....*....|...
gi 1913184172 546 FKCTQCGKSFSQKYDLVVHQRTH 568
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 574-596 2.07e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.12  E-value: 2.07e-03
                          10        20
                  ....*....|....*....|...
gi 1913184172 574 YECNLCGKSFSQSSKLITHQRIH 596
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 518-540 2.29e-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: 36.12  E-value: 2.29e-03
                          10        20
                  ....*....|....*....|...
gi 1913184172 518 YECTHCGKSFSQSYELVTHKRTH 540
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 462-484 2.81e-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: 2.81e-03
                          10        20
                  ....*....|....*....|...
gi 1913184172 462 YECDLCGKSFTQRSKLITHQRIH 484
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 434-456 2.95e-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: 2.95e-03
                          10        20
                  ....*....|....*....|...
gi 1913184172 434 FECTQCGKSFSQSYDLVIHQRTH 456
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 630-652 3.66e-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: 35.35  E-value: 3.66e-03
                          10        20
                  ....*....|....*....|...
gi 1913184172 630 YDCTHCGKSFSQSYQLVAHKRTH 652
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 658-680 4.96e-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: 4.96e-03
                          10        20
                  ....*....|....*....|...
gi 1913184172 658 YECNECGKAFNRSTQLIRHLQIH 680
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 686-708 7.28e-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: 34.58  E-value: 7.28e-03
                          10        20
                  ....*....|....*....|...
gi 1913184172 686 YKCNQCNKAFARSSYLVMHQRTH 708
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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