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Conserved domains on  [gi|820971932|ref|XP_004634807|]
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transcription factor Sp3 [Octodon degus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SP3_N cd22537
N-terminal domain of transcription factor Specificity Protein (SP) 3; Specificity Proteins ...
 275-803 0e+00

N-terminal domain of transcription factor Specificity Protein (SP) 3; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP1 and SP3 can interact with and recruit a large number of proteins including the transcription initiation complex, histone modifying enzymes, and chromatin remodeling complexes, which strongly suggest that SP1 and SP3 are important transcription factors in remodeling chromatin and the regulation of gene expression. SP3 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP3.


:

Pssm-ID: 411774 [Multi-domain]  Cd Length: 574  Bit Score: 806.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 275 TGDLASAQLGGAPNRWEVLSATPTTIKDEAGNLVQIPSAA--TSSGQYVLPLQNLQNQQIFSVAPGSDSSNGTVSNVQYQ 352
Cdd:cd22537   43 TGDLASAQLTGAPNRWEVLTPTPTTIKDEAGNLVQIPGGGtvTSSGQYVLPLQSLQNQQIFSVAPGSDASNGTVPNVQYQ 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 353 VIPQIQSTDGQQVQIGFTGSSDNGGLNQESSQIQIIPGSNQTLLASGTPPANIQNLMPQTGQVQVQGVAIGGSSFPGQTQ 432
Cdd:cd22537  123 VIPQIQTTDGQQVQLGFATSSDNTGLQQEGGQIQIIPGSNQTIIASGTPSAVQQLLSQSGHVVQIQGVSIGGSSFPGQTQ 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 433 VVANVPLGLPGNITFVPINSVDLDSLGLSGSSQTMTAGINADGHLINTGQAMDSSDNSERTGeRVSPDINETNTDTDLFV 512
Cdd:cd22537  203 VVANVPLGLPGNITFVPINSVDLDSLGLSGTSQTMTTGITADGQLINTGQAVQSSDNSGESG-KVSPDINETNTNADLFV 281

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 513 PTSSSSQLPVTIDSTGILQQNTNSLTTSSGQVHSSDLQGNYIQSPVSEETQAQNIQVSTAQPVVQHLQLQESQQPTSQAQ 592
Cdd:cd22537  282 PTSSSSQLPVTIDSTGILQQNASSLTTVSGQVHTSDLQGNYIQAPVSDETQAQNIQVSTAQPSVQQIQLHESQQPTSQAQ 361

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 593 IVQGITPQTIHGVQA-SGQNISQQALQNLQLQ-LNPGTFLIQAQTVTPSGQITWQTFQVQGVQNLQNLQIQNTAAQQITL 670
Cdd:cd22537  362 IVQGITQQAIQGVQAlGAQAIPQQALQNLQLQlLNPGTFLIQAQTVTPSGQITWQTFQVQGVQNLQNLQIQNAPAQQITL 441

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 671 TPVQTLTLGQVAAGGTLTSTPVSLSTGQLPNLQTVTVNSIDSTGIQLHPGENADSPADIRIKEEEPDPEEWQLSGDSTLN 750
Cdd:cd22537  442 TPVQTLTLGQVGAGGAITSTPVSLSTGQLPNLQTVTVNSIDSAGIQLQQSENADSPADIQIKEEEPDSEEWQLSGDSTLN 521

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|...
gi 820971932 751 TNDLTHLRVQVVDEEGDQQHQEGKRLRRVACTCPNCKEGGGRGTNLGKKKQHI 803
Cdd:cd22537  522 TNDLTHLRVQLVEEEGDQPHQEGKRLRRVACTCPNCKEGGGRGSNLGKKKQHI 574
zf-H2C2_2 pfam13465
Zinc-finger double domain;
848-871 2.45e-08

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 50.45  E-value: 2.45e-08
                          10        20
                  ....*....|....*....|....
gi 820971932  848 ELQRHRRTHTGEKKFVCPECSKRF 871
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 862-884 9.77e-06

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: 43.06  E-value: 9.77e-06
                          10        20
                  ....*....|....*....|...
gi 820971932  862 FVCPECSKRFMRSDHLAKHIKTH 884
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 832-856 5.93e-05

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: 40.75  E-value: 5.93e-05
                          10        20
                  ....*....|....*....|....*
gi 820971932  832 FICNwmFCGKRFTRSDELQRHRRTH 856
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
SP3_N cd22537
N-terminal domain of transcription factor Specificity Protein (SP) 3; Specificity Proteins ...
 275-803 0e+00

N-terminal domain of transcription factor Specificity Protein (SP) 3; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP1 and SP3 can interact with and recruit a large number of proteins including the transcription initiation complex, histone modifying enzymes, and chromatin remodeling complexes, which strongly suggest that SP1 and SP3 are important transcription factors in remodeling chromatin and the regulation of gene expression. SP3 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP3.


Pssm-ID: 411774 [Multi-domain]  Cd Length: 574  Bit Score: 806.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 275 TGDLASAQLGGAPNRWEVLSATPTTIKDEAGNLVQIPSAA--TSSGQYVLPLQNLQNQQIFSVAPGSDSSNGTVSNVQYQ 352
Cdd:cd22537   43 TGDLASAQLTGAPNRWEVLTPTPTTIKDEAGNLVQIPGGGtvTSSGQYVLPLQSLQNQQIFSVAPGSDASNGTVPNVQYQ 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 353 VIPQIQSTDGQQVQIGFTGSSDNGGLNQESSQIQIIPGSNQTLLASGTPPANIQNLMPQTGQVQVQGVAIGGSSFPGQTQ 432
Cdd:cd22537  123 VIPQIQTTDGQQVQLGFATSSDNTGLQQEGGQIQIIPGSNQTIIASGTPSAVQQLLSQSGHVVQIQGVSIGGSSFPGQTQ 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 433 VVANVPLGLPGNITFVPINSVDLDSLGLSGSSQTMTAGINADGHLINTGQAMDSSDNSERTGeRVSPDINETNTDTDLFV 512
Cdd:cd22537  203 VVANVPLGLPGNITFVPINSVDLDSLGLSGTSQTMTTGITADGQLINTGQAVQSSDNSGESG-KVSPDINETNTNADLFV 281

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 513 PTSSSSQLPVTIDSTGILQQNTNSLTTSSGQVHSSDLQGNYIQSPVSEETQAQNIQVSTAQPVVQHLQLQESQQPTSQAQ 592
Cdd:cd22537  282 PTSSSSQLPVTIDSTGILQQNASSLTTVSGQVHTSDLQGNYIQAPVSDETQAQNIQVSTAQPSVQQIQLHESQQPTSQAQ 361

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 593 IVQGITPQTIHGVQA-SGQNISQQALQNLQLQ-LNPGTFLIQAQTVTPSGQITWQTFQVQGVQNLQNLQIQNTAAQQITL 670
Cdd:cd22537  362 IVQGITQQAIQGVQAlGAQAIPQQALQNLQLQlLNPGTFLIQAQTVTPSGQITWQTFQVQGVQNLQNLQIQNAPAQQITL 441

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 671 TPVQTLTLGQVAAGGTLTSTPVSLSTGQLPNLQTVTVNSIDSTGIQLHPGENADSPADIRIKEEEPDPEEWQLSGDSTLN 750
Cdd:cd22537  442 TPVQTLTLGQVGAGGAITSTPVSLSTGQLPNLQTVTVNSIDSAGIQLQQSENADSPADIQIKEEEPDSEEWQLSGDSTLN 521

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|...
gi 820971932 751 TNDLTHLRVQVVDEEGDQQHQEGKRLRRVACTCPNCKEGGGRGTNLGKKKQHI 803
Cdd:cd22537  522 TNDLTHLRVQLVEEEGDQPHQEGKRLRRVACTCPNCKEGGGRGSNLGKKKQHI 574
zf-H2C2_2 pfam13465
Zinc-finger double domain;
848-871 2.45e-08

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 50.45  E-value: 2.45e-08
                          10        20
                  ....*....|....*....|....
gi 820971932  848 ELQRHRRTHTGEKKFVCPECSKRF 871
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 862-884 9.77e-06

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: 43.06  E-value: 9.77e-06
                          10        20
                  ....*....|....*....|...
gi 820971932  862 FVCPECSKRFMRSDHLAKHIKTH 884
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 832-856 5.93e-05

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: 40.75  E-value: 5.93e-05
                          10        20
                  ....*....|....*....|....*
gi 820971932  832 FICNwmFCGKRFTRSDELQRHRRTH 856
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
ZnF_C2H2 smart00355
zinc finger;
862-884 2.10e-04

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 39.37  E-value: 2.10e-04
                           10        20
                   ....*....|....*....|...
gi 820971932   862 FVCPECSKRFMRSDHLAKHIKTH 884
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
817-899 1.34e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.38  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 817 SHLRAHLRW--HSGE--RPFICNWMFCGKRFTRSDELQRHRRTHTGEKKFVCP--ECSKRFMRSDHLAKHIKTHQNKKVI 890
Cdd:COG5048  303 SPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQYKDLK 382


                 ....*....
gi 820971932 891 HSSSAVLAS 899
Cdd:COG5048  383 NDKKSETLS 391
ZnF_C2H2 smart00355
zinc finger;
832-856 2.44e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 36.29  E-value: 2.44e-03
                           10        20
                   ....*....|....*....|....*
gi 820971932   832 FICNWmfCGKRFTRSDELQRHRRTH 856
Cdd:smart00355   1 YRCPE--CGKVFKSKSALREHMRTH 23
zf-C2H2_8 pfam15909
C2H2-type zinc ribbon; This family carries three zinc-fingers in tandem.
 804-881 3.40e-03

C2H2-type zinc ribbon; This family carries three zinc-fingers in tandem.


Pssm-ID: 464935 [Multi-domain]  Cd Length: 98  Bit Score: 37.78  E-value: 3.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932  804 CHIPGCGKVYGKTSHLRAHLRWHSGE------RPFICNWMFCGKRFTRSDELQRHRRTHTGEKK-FVCPECSKRFMRSDH 876
Cdd:pfam15909   2 CSSPGCCLSFPSVRDLAQHLRTHCPPtqslegKLFRCSALSCTETFPSMQELVAHSKLHYKPNRyFKCENCLLRFRTHRS 81


                  ....*
gi 820971932  877 LAKHI 881
Cdd:pfam15909  82 LFKHL 86
 
Name Accession Description Interval E-value
SP3_N cd22537
N-terminal domain of transcription factor Specificity Protein (SP) 3; Specificity Proteins ...
 275-803 0e+00

N-terminal domain of transcription factor Specificity Protein (SP) 3; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP1 and SP3 can interact with and recruit a large number of proteins including the transcription initiation complex, histone modifying enzymes, and chromatin remodeling complexes, which strongly suggest that SP1 and SP3 are important transcription factors in remodeling chromatin and the regulation of gene expression. SP3 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP3.


Pssm-ID: 411774 [Multi-domain]  Cd Length: 574  Bit Score: 806.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 275 TGDLASAQLGGAPNRWEVLSATPTTIKDEAGNLVQIPSAA--TSSGQYVLPLQNLQNQQIFSVAPGSDSSNGTVSNVQYQ 352
Cdd:cd22537   43 TGDLASAQLTGAPNRWEVLTPTPTTIKDEAGNLVQIPGGGtvTSSGQYVLPLQSLQNQQIFSVAPGSDASNGTVPNVQYQ 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 353 VIPQIQSTDGQQVQIGFTGSSDNGGLNQESSQIQIIPGSNQTLLASGTPPANIQNLMPQTGQVQVQGVAIGGSSFPGQTQ 432
Cdd:cd22537  123 VIPQIQTTDGQQVQLGFATSSDNTGLQQEGGQIQIIPGSNQTIIASGTPSAVQQLLSQSGHVVQIQGVSIGGSSFPGQTQ 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 433 VVANVPLGLPGNITFVPINSVDLDSLGLSGSSQTMTAGINADGHLINTGQAMDSSDNSERTGeRVSPDINETNTDTDLFV 512
Cdd:cd22537  203 VVANVPLGLPGNITFVPINSVDLDSLGLSGTSQTMTTGITADGQLINTGQAVQSSDNSGESG-KVSPDINETNTNADLFV 281

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 513 PTSSSSQLPVTIDSTGILQQNTNSLTTSSGQVHSSDLQGNYIQSPVSEETQAQNIQVSTAQPVVQHLQLQESQQPTSQAQ 592
Cdd:cd22537  282 PTSSSSQLPVTIDSTGILQQNASSLTTVSGQVHTSDLQGNYIQAPVSDETQAQNIQVSTAQPSVQQIQLHESQQPTSQAQ 361

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 593 IVQGITPQTIHGVQA-SGQNISQQALQNLQLQ-LNPGTFLIQAQTVTPSGQITWQTFQVQGVQNLQNLQIQNTAAQQITL 670
Cdd:cd22537  362 IVQGITQQAIQGVQAlGAQAIPQQALQNLQLQlLNPGTFLIQAQTVTPSGQITWQTFQVQGVQNLQNLQIQNAPAQQITL 441

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 671 TPVQTLTLGQVAAGGTLTSTPVSLSTGQLPNLQTVTVNSIDSTGIQLHPGENADSPADIRIKEEEPDPEEWQLSGDSTLN 750
Cdd:cd22537  442 TPVQTLTLGQVGAGGAITSTPVSLSTGQLPNLQTVTVNSIDSAGIQLQQSENADSPADIQIKEEEPDSEEWQLSGDSTLN 521

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|...
gi 820971932 751 TNDLTHLRVQVVDEEGDQQHQEGKRLRRVACTCPNCKEGGGRGTNLGKKKQHI 803
Cdd:cd22537  522 TNDLTHLRVQLVEEEGDQPHQEGKRLRRVACTCPNCKEGGGRGSNLGKKKQHI 574
SP4_N cd22536
N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins ...
 277-803 5.29e-58

N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. Human SP4 is a risk gene of multiple psychiatric disorders including schizophrenia, bipolar disorder, and major depression. SP4 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP4.


Pssm-ID: 411773 [Multi-domain]  Cd Length: 623  Bit Score: 210.93  E-value: 5.29e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 277 DLASAQLGGapNRWEVLSATPTTIKDeaGNLVQIPSAATSSGQYVLPLQN--------------LQNQQIFSVAPGSDSS 342
Cdd:cd22536   61 ELVTTQLAG--NAWQIVAAAPPTSKE--NNVAQQGVSAATSSAAPSSSNNgstsptkvkagnsnASAPGQFQVIQVQNMQ 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 343 NGTvSNVQYQVIPQIQSTDGQQVQIGFTGSSDNGGLNQessQIQIIP-GSNQTLLASG--TPPANI--QNLMPQTGQVQV 417
Cdd:cd22536  137 NPS-GSVQYQVIPQIQTVEGQQIQISPANATALQDLQG---QIQLIPaGNNQAILTTPnrTASGNIiaQNLANQTVPVQI 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 418 QgvaiGGSSFP--------GQTQVVANVPLGLPGNITFVPINSVDLDSLGLSGSSQTMTAGINADGHLINTGQAMDSSDN 489
Cdd:cd22536  213 R----PGVSIPlqlqtipgAQAQVVTTLPINIGGVTLALPVINNVAAGGGSGQLVQPSDGGVSNGNQLVSTPITTASVST 288

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 490 ---SERTGERVSPDINETNTDTDLFVPTSSSSQLPVTIDSTGILQQNTNSLTTSSGQVHSSDLQGNYIQsPVSEETQAQN 566
Cdd:cd22536  289 mpeSPSSSTTCTTTASTSLTSSDTLVSSAETGQYASTAASSERTEEEPQTSAAESEAQSSSQLQSNGLQ-NVQDQSNSLQ 367

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 567 IQVSTAQPVVQHLQLQESQQPTSQAQIVQ------GITPQTIHgvQASGQNIsqqalqNLQLQLNPGTFLIQAQTVTPSG 640
Cdd:cd22536  368 QVQIVGQPILQQIQIQQPQQQIIQAIQPQsfqlqsGQTIQTIQ--QQPLQNV------QLQAVQSPTQVLIRAPTLTPSG 439

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 641 QITWQTFQVQGVQNLQNLQIQNTA-AQQITLTPVQT----LTLGQVAAgGTLTSTPVSLSTGQL---PNLQTVTVNSIDS 712
Cdd:cd22536  440 QISWQTVQVQNIQSLSNLQVQNAGlPQQLTLTPVSSsaggTTIAQIAP-VAVAGTPITLNAAQLasvPNLQTVNVANLGA 518

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 713 TGIQLHPGENADSPADIRIKEEEPDPEEWQLSGDST-------------LNTNDLTHLRVQVVDEEGDQQHQEGKRLRRV 779
Cdd:cd22536  519 AGVQVQGVPVTITSVAGQQQGQDGVKVQQATIAPVTvavgnianatigaVSPDQITQVQLQQAQQASDQEVQPGKRLRRV 598

                        570       580
                 ....*....|....*....|....*
gi 820971932 780 ACTCPNCKEGGGRGTN-LGKKKQHI 803
Cdd:cd22536  599 ACSCPNCREGEGRGSSePGKKKQHI 623
SP1_N cd22539
N-terminal domain of transcription factor Specificity Protein (SP) 1; Specificity Proteins ...
 277-803 2.21e-41

N-terminal domain of transcription factor Specificity Protein (SP) 1; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP1 has been shown to interact with a variety of proteins including myogenin, SMAD3, SUMO1, SF1, TAL1, and UBC. Some 12,000 SP1 binding sites are found in the human genome. SP1 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLF bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP1.


Pssm-ID: 411775  Cd Length: 433  Bit Score: 157.75  E-value: 2.21e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 277 DLASAQLGGAPNRWEVLSA---TPTTIKDEAGNLVQIPS----AATSSGQYVLPLQNLQNQQIFSVAPGsdssngTVSNV 349
Cdd:cd22539   45 DLTQAQIAQSANGWQIIPTgsqAPTPSKEQSGDSSTADSskksRVATAGYVVVAAPNLQNQQVLTSLPG------VMPNI 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 350 QYQVIPQIQSTDGQQVQIGFTGSSDNGglnQESSQIQIIPGSNQTLLASGTPPANIQNLMPQTGQ--VQVQGVAIGGSSF 427
Cdd:cd22539  119 QYQVIPQFQTVDGQQLQFATTQAQVQQ---DASGQLQIIPGTNQQIITTNRSGSGNIITMPNLLQqaVPIQGLGLANNVL 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 428 PGQTQVVANVPLGLPGNITFVPINSVdldslglsgssqtmtaginadghlintgqamdssdnsertgervsPDINETNTd 507
Cdd:cd22539  196 PGQTQFVANVPVALNGNITLLPVSSV---------------------------------------------TASFFTNA- 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 508 tdlfvptssssqlpvtidstgilqqNTNSLTTSSGQVhssdlqgnyiqspvseetqaqniqvstaqpvvqhlqLQESQQP 587
Cdd:cd22539  230 -------------------------NSYSTTTTTSNM------------------------------------GQQQQQI 248

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 588 TSQAQIVQGI-TPQTIHGVQASG-----QNISQQALQNLQLQLNPGTFLIQAQT-VTPSGQITWQTFQvqgvqnLQNLQi 660
Cdd:cd22539  249 LIQPQLVQGGqTIQALQAASLPGqtfttQTISQEALQNLQIQTVPNSGPIIIRTpVGPNGQVSWQTIQ------LQNLQ- 321

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 661 qntaaqqitltpvqtltlgqvaaggtlTSTPVSLSTGQLPNLQTVTVNSIDSTGIQLHPGENAdsPADIrikEEEPDPEE 740
Cdd:cd22539  322 ---------------------------TVTVNAAQLSSMPGLQTINLNALGASGIQVHQLQGL--PLTI---ANATGEHG 369

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 820971932 741 WQLSGDSTLNTNDLTHLRVQVVDEEGDQQHQEGKRLRRVACTCPNCKEGGGRG-TNLGKKKQHI 803
Cdd:cd22539  370 AQLGLHGAGGDGLHDDSAAEEGETEPDPQPQPGRRTRREACTCPYCKDGEGRDsGDPGKKKQHI 433
SP1-4_N cd22545
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ...
 760-803 1.41e-17

N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. SPs belong to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP1-4.


Pssm-ID: 411777 [Multi-domain]  Cd Length: 82  Bit Score: 78.25  E-value: 1.41e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 820971932 760 QVVDEEGDQQHQEGKRLRRVACTCPNCKEGGGRGTNLGKKKQHI 803
Cdd:cd22545   39 QVIPQFQDQEPQPGKRLRRVACTCPNCKDGEGRGSEDGKKKQHI 82
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
 305-803 4.05e-16

N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2.


Pssm-ID: 411776 [Multi-domain]  Cd Length: 511  Bit Score: 82.67  E-value: 4.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 305 GNLVQIP----SAATSSGQYVLPLQNlqnqqifSVAPGSDSSNGTVSNVQYQVIPQIQstdgqqvqigftgssdNGGLNQ 380
Cdd:cd22540   83 GNIIQLQgsqlSSSAPGGQQVFAIQN-------PTMIIKGSQTRSSTNQQYQISPQIQ----------------AAGQIN 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 381 ESSQIQIIPGSNQTLLASgTPPANIQNLMPQTGQVQVQGVAIGGSSfPGQTQVVAN-VPLGLPGNITFV-PINSVDLDSl 458
Cdd:cd22540  140 NSGQIQIIPGTNQAIITP-VQVLQQPQQAHKPVPIKPAPLQTSNTN-SASLQVPGNvIKLQSGGNVALTlPVNNLVGTQ- 216

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 459 glSGSSQTMTAGINADGHLINTGQAMDSSDNSERTGERVSPDINETNTDTdlfvptssssqlpvtidstgILQQNTNSLt 538
Cdd:cd22540  217 --DGATQLQLAAAPSKPSKKIRKKSAQAAQPAVTVAEQVETVLIETTADN--------------------IIQAGNNLL- 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 539 tssgqvhssdlqgnYIQSPvseetqaqniqvSTAQPVVqhLQLQESQQPTSQAQIVQgITPQTIHGVQASGQN-ISQQAL 617
Cdd:cd22540  274 --------------IVQSP------------GTGQPAV--LQQVQVLQPKQEQQVVQ-IPQQALRVVQAASATlPTVPQK 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 618 QNLQLQLNPGTFL-IQAQTVTPSGQITWQTFQVQGVQnlqnlqiqnTAAQQITLTPVQtltLGQVAAGGTLTSTP----- 691
Cdd:cd22540  325 PLQNIQIQNSEPTpTQVYIKTPSGEVQTVLLQEAPAA---------TATPSSSTSTVQ---QQVTANNGTGTSKPnynvr 392

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 692 --------------VSLSTGQLP----NLQTVTVN---------SIDSTGIQLHPGENADSPADIRIKEEEPDPEEWQLs 744
Cdd:cd22540  393 kertlpkiapaggiISLNAAQLAaaaqAIQTININgvqvqgvpvTITNAGGQQQLTVQTVSSNNLTISGLSPTQIQLQM- 471

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 820971932 745 gdstlntndlthlrvqvvDEEGDQQHQEGKRLRRVACTCPNCKEGGGRGTNLGKKKqHI 803
Cdd:cd22540  472 ------------------EQALEIETQPGEKRRRMACTCPNCKDGEKRSGEQGKKK-HI 511
SP1-4_arthropods_N cd22553
N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; ...
 551-803 5.44e-13

N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in the chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. One SP is clade SP1-4, which is expressed ubiquitously throughout development. SP1-4 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. This model represents the N-terminal domain of SP1-4 from arthropods.


Pssm-ID: 411778 [Multi-domain]  Cd Length: 384  Bit Score: 71.98  E-value: 5.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 551 GNYIQSPVSEETQAQNIQV----STAQPVVQHLQLQ-ESQQPTSQAQIVQGITPQTIHGVQASGQnisqqalqnlqlqln 625
Cdd:cd22553  144 GNAVQLPLNNMTQTIPVQVpvstANGQTVYQTIQVPiQAIQSGNAGGGNQALQAQVIPQLAQAAQ--------------- 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 626 pgtfLIQAQTVTPSGQITWQTF-QVQGVQNLQNLQIQNTAAQQIT---------------LTPVQTLTLGQVAA----GG 685
Cdd:cd22553  209 ----LQPQQLAQVSSQGYIQQIpANASQQQPQMVQQGPNQSGQIIgqvasassiqaaaipLTVYTGALAGQNGSnqqqVG 284

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 686 TLTSTPVSLSTGQLPNLQTVTVNSIDS----TGIQLHPGENAdSPADIRIKEEEPDPEEWQLSGDSTLNTndlthlrvqv 761
Cdd:cd22553  285 QIVTSPIQGMTQGLTAPASSSIPTVVQqqaiQGNPLPPGTQI-IAAGQQLQQDPNDPTKWQVVADGTPGS---------- 353

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 820971932 762 vdeegdqqhqeGKRLRRVACTCPNCKEGGGRGTNLGKKKQHI 803
Cdd:cd22553  354 -----------KKRLRRVACTCPNCRDGDGTRNGENKKKQHI 384
zf-H2C2_2 pfam13465
Zinc-finger double domain;
848-871 2.45e-08

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 50.45  E-value: 2.45e-08
                          10        20
                  ....*....|....*....|....
gi 820971932  848 ELQRHRRTHTGEKKFVCPECSKRF 871
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 862-884 9.77e-06

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: 43.06  E-value: 9.77e-06
                          10        20
                  ....*....|....*....|...
gi 820971932  862 FVCPECSKRFMRSDHLAKHIKTH 884
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 832-856 5.93e-05

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: 40.75  E-value: 5.93e-05
                          10        20
                  ....*....|....*....|....*
gi 820971932  832 FICNwmFCGKRFTRSDELQRHRRTH 856
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
ZnF_C2H2 smart00355
zinc finger;
862-884 2.10e-04

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 39.37  E-value: 2.10e-04
                           10        20
                   ....*....|....*....|...
gi 820971932   862 FVCPECSKRFMRSDHLAKHIKTH 884
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 862-884 5.63e-04

C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.


Pssm-ID: 464025  Cd Length: 24  Bit Score: 38.01  E-value: 5.63e-04
                          10        20
                  ....*....|....*....|...
gi 820971932  862 FVCPECSKRFMRSDHLAKHIKTH 884
Cdd:pfam13894   1 FKCPICGKSFSSKKSLKRHLKTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
817-899 1.34e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.38  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932 817 SHLRAHLRW--HSGE--RPFICNWMFCGKRFTRSDELQRHRRTHTGEKKFVCP--ECSKRFMRSDHLAKHIKTHQNKKVI 890
Cdd:COG5048  303 SPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQYKDLK 382


                 ....*....
gi 820971932 891 HSSSAVLAS 899
Cdd:COG5048  383 NDKKSETLS 391
ZnF_C2H2 smart00355
zinc finger;
832-856 2.44e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 36.29  E-value: 2.44e-03
                           10        20
                   ....*....|....*....|....*
gi 820971932   832 FICNWmfCGKRFTRSDELQRHRRTH 856
Cdd:smart00355   1 YRCPE--CGKVFKSKSALREHMRTH 23
zf-C2H2_8 pfam15909
C2H2-type zinc ribbon; This family carries three zinc-fingers in tandem.
 804-881 3.40e-03

C2H2-type zinc ribbon; This family carries three zinc-fingers in tandem.


Pssm-ID: 464935 [Multi-domain]  Cd Length: 98  Bit Score: 37.78  E-value: 3.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820971932  804 CHIPGCGKVYGKTSHLRAHLRWHSGE------RPFICNWMFCGKRFTRSDELQRHRRTHTGEKK-FVCPECSKRFMRSDH 876
Cdd:pfam15909   2 CSSPGCCLSFPSVRDLAQHLRTHCPPtqslegKLFRCSALSCTETFPSMQELVAHSKLHYKPNRyFKCENCLLRFRTHRS 81


                  ....*
gi 820971932  877 LAKHI 881
Cdd:pfam15909  82 LFKHL 86
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 832-856 9.33e-03

C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.


Pssm-ID: 464025  Cd Length: 24  Bit Score: 34.54  E-value: 9.33e-03
                          10        20
                  ....*....|....*....|....*
gi 820971932  832 FICNwmFCGKRFTRSDELQRHRRTH 856
Cdd:pfam13894   1 FKCP--ICGKSFSSKKSLKRHLKTH 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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