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Conserved domains on  [gi|918612218|ref|XP_005393250|]
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PREDICTED: transcription factor Sp3 [Chinchilla lanigera]

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 ...
 316-844 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: 813.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  316 TGDLASAQLGGAPNRWEVLSATPTTIKDEAGNLVQIPSAA--TSSGQYVLPLQNLQNQQIFSVAPGSDSSNGTVSNVQYQ 393
Cdd:cd22537    43 TGDLASAQLTGAPNRWEVLTPTPTTIKDEAGNLVQIPGGGtvTSSGQYVLPLQSLQNQQIFSVAPGSDASNGTVPNVQYQ 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  394 VIPQIQSTDGQQVQIGFTGSSDNGGLNQESSQIQIIPGSNQTLLASGTPPANIQNLMPQTGQVQVQGVAIGGSSFPGQTQ 473
Cdd:cd22537   123 VIPQIQTTDGQQVQLGFATSSDNTGLQQEGGQIQIIPGSNQTIIASGTPSAVQQLLSQSGHVVQIQGVSIGGSSFPGQTQ 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  474 VVANVPLGLPGNITFVPINSVDLDSLGLSGSSQTMTAGINADGHLINTGQAMDSSDNSERTGeRVSPDINETNTDSDLFV 553
Cdd:cd22537   203 VVANVPLGLPGNITFVPINSVDLDSLGLSGTSQTMTTGITADGQLINTGQAVQSSDNSGESG-KVSPDINETNTNADLFV 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  554 PTSSSSQLPVTIDSTGILQQNTNSLTTSSGQVHSSDLQGNYIQSPVSEETQAQNIQVSTAQPVVQHLQLQESQQPTSQAQ 633
Cdd:cd22537   282 PTSSSSQLPVTIDSTGILQQNASSLTTVSGQVHTSDLQGNYIQAPVSDETQAQNIQVSTAQPSVQQIQLHESQQPTSQAQ 361

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  634 IVQGITPQTIHGVQA-SGQNISQQALQNLQLQ-LNPGTFLIQAQTVTPSGQITWQTFQVQGVQNLQNLQIQNTAAQQITL 711
Cdd:cd22537   362 IVQGITQQAIQGVQAlGAQAIPQQALQNLQLQlLNPGTFLIQAQTVTPSGQITWQTFQVQGVQNLQNLQIQNAPAQQITL 441

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  712 TPVQTLTLGQVAAGGTLTSTPVSLSTGQLPNLQTVTVNSIDSTGIQLHPGENADSPADIRIKEEEPDPEEWQLSGDSTLN 791
Cdd:cd22537   442 TPVQTLTLGQVGAGGAITSTPVSLSTGQLPNLQTVTVNSIDSAGIQLQQSENADSPADIQIKEEEPDSEEWQLSGDSTLN 521

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 918612218  792 TNDLTHLRVQVVDEEGDQQHQEGKRLRRVACTCPNCKEGGGRGTNLGKKKQHI 844
Cdd:cd22537   522 TNDLTHLRVQLVEEEGDQPHQEGKRLRRVACTCPNCKEGGGRGSNLGKKKQHI 574
zf-H2C2_2 pfam13465
Zinc-finger double domain;
889-912 2.55e-08

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 50.45  E-value: 2.55e-08
                           10        20
                   ....*....|....*....|....
gi 918612218   889 ELQRHRRTHTGEKKFVCPECSKRF 912
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 903-925 1.02e-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: 43.06  E-value: 1.02e-05
                           10        20
                   ....*....|....*....|...
gi 918612218   903 FVCPECSKRFMRSDHLAKHIKTH 925
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 873-897 6.17e-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: 6.17e-05
                           10        20
                   ....*....|....*....|....*
gi 918612218   873 FICNwmFCGKRFTRSDELQRHRRTH 897
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 ...
 316-844 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: 813.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  316 TGDLASAQLGGAPNRWEVLSATPTTIKDEAGNLVQIPSAA--TSSGQYVLPLQNLQNQQIFSVAPGSDSSNGTVSNVQYQ 393
Cdd:cd22537    43 TGDLASAQLTGAPNRWEVLTPTPTTIKDEAGNLVQIPGGGtvTSSGQYVLPLQSLQNQQIFSVAPGSDASNGTVPNVQYQ 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  394 VIPQIQSTDGQQVQIGFTGSSDNGGLNQESSQIQIIPGSNQTLLASGTPPANIQNLMPQTGQVQVQGVAIGGSSFPGQTQ 473
Cdd:cd22537   123 VIPQIQTTDGQQVQLGFATSSDNTGLQQEGGQIQIIPGSNQTIIASGTPSAVQQLLSQSGHVVQIQGVSIGGSSFPGQTQ 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  474 VVANVPLGLPGNITFVPINSVDLDSLGLSGSSQTMTAGINADGHLINTGQAMDSSDNSERTGeRVSPDINETNTDSDLFV 553
Cdd:cd22537   203 VVANVPLGLPGNITFVPINSVDLDSLGLSGTSQTMTTGITADGQLINTGQAVQSSDNSGESG-KVSPDINETNTNADLFV 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  554 PTSSSSQLPVTIDSTGILQQNTNSLTTSSGQVHSSDLQGNYIQSPVSEETQAQNIQVSTAQPVVQHLQLQESQQPTSQAQ 633
Cdd:cd22537   282 PTSSSSQLPVTIDSTGILQQNASSLTTVSGQVHTSDLQGNYIQAPVSDETQAQNIQVSTAQPSVQQIQLHESQQPTSQAQ 361

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  634 IVQGITPQTIHGVQA-SGQNISQQALQNLQLQ-LNPGTFLIQAQTVTPSGQITWQTFQVQGVQNLQNLQIQNTAAQQITL 711
Cdd:cd22537   362 IVQGITQQAIQGVQAlGAQAIPQQALQNLQLQlLNPGTFLIQAQTVTPSGQITWQTFQVQGVQNLQNLQIQNAPAQQITL 441

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  712 TPVQTLTLGQVAAGGTLTSTPVSLSTGQLPNLQTVTVNSIDSTGIQLHPGENADSPADIRIKEEEPDPEEWQLSGDSTLN 791
Cdd:cd22537   442 TPVQTLTLGQVGAGGAITSTPVSLSTGQLPNLQTVTVNSIDSAGIQLQQSENADSPADIQIKEEEPDSEEWQLSGDSTLN 521

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 918612218  792 TNDLTHLRVQVVDEEGDQQHQEGKRLRRVACTCPNCKEGGGRGTNLGKKKQHI 844
Cdd:cd22537   522 TNDLTHLRVQLVEEEGDQPHQEGKRLRRVACTCPNCKEGGGRGSNLGKKKQHI 574
zf-H2C2_2 pfam13465
Zinc-finger double domain;
889-912 2.55e-08

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 50.45  E-value: 2.55e-08
                           10        20
                   ....*....|....*....|....
gi 918612218   889 ELQRHRRTHTGEKKFVCPECSKRF 912
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 903-925 1.02e-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: 43.06  E-value: 1.02e-05
                           10        20
                   ....*....|....*....|...
gi 918612218   903 FVCPECSKRFMRSDHLAKHIKTH 925
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 873-897 6.17e-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: 6.17e-05
                           10        20
                   ....*....|....*....|....*
gi 918612218   873 FICNwmFCGKRFTRSDELQRHRRTH 897
Cdd:pfam00096    1 YKCP--DCGKSFSRKSNLKRHLRTH 23
ZnF_C2H2 smart00355
zinc finger;
903-925 2.19e-04

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 39.37  E-value: 2.19e-04
                            10        20
                    ....*....|....*....|...
gi 918612218    903 FVCPECSKRFMRSDHLAKHIKTH 925
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
858-940 8.23e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.15  E-value: 8.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  858 SHLRAHLRW--HSGE--RPFICNWMFCGKRFTRSDELQRHRRTHTGEKKFVCP--ECSKRFMRSDHLAKHIKTHQNKKVI 931
Cdd:COG5048   303 SPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQYKDLK 382


                  ....*....
gi 918612218  932 HSSSAVLAS 940
Cdd:COG5048   383 NDKKSETLS 391
ZnF_C2H2 smart00355
zinc finger;
873-897 2.54e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 36.29  E-value: 2.54e-03
                            10        20
                    ....*....|....*....|....*
gi 918612218    873 FICNWmfCGKRFTRSDELQRHRRTH 897
Cdd:smart00355    1 YRCPE--CGKVFKSKSALREHMRTH 23
zf-C2H2_8 pfam15909
C2H2-type zinc ribbon; This family carries three zinc-fingers in tandem.
 845-922 3.55e-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: 3.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218   845 CHIPGCGKVYGKTSHLRAHLRWHSGE------RPFICNWMFCGKRFTRSDELQRHRRTHTGEKK-FVCPECSKRFMRSDH 917
Cdd:pfam15909    2 CSSPGCCLSFPSVRDLAQHLRTHCPPtqslegKLFRCSALSCTETFPSMQELVAHSKLHYKPNRyFKCENCLLRFRTHRS 81


                   ....*
gi 918612218   918 LAKHI 922
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 ...
 316-844 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: 813.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  316 TGDLASAQLGGAPNRWEVLSATPTTIKDEAGNLVQIPSAA--TSSGQYVLPLQNLQNQQIFSVAPGSDSSNGTVSNVQYQ 393
Cdd:cd22537    43 TGDLASAQLTGAPNRWEVLTPTPTTIKDEAGNLVQIPGGGtvTSSGQYVLPLQSLQNQQIFSVAPGSDASNGTVPNVQYQ 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  394 VIPQIQSTDGQQVQIGFTGSSDNGGLNQESSQIQIIPGSNQTLLASGTPPANIQNLMPQTGQVQVQGVAIGGSSFPGQTQ 473
Cdd:cd22537   123 VIPQIQTTDGQQVQLGFATSSDNTGLQQEGGQIQIIPGSNQTIIASGTPSAVQQLLSQSGHVVQIQGVSIGGSSFPGQTQ 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  474 VVANVPLGLPGNITFVPINSVDLDSLGLSGSSQTMTAGINADGHLINTGQAMDSSDNSERTGeRVSPDINETNTDSDLFV 553
Cdd:cd22537   203 VVANVPLGLPGNITFVPINSVDLDSLGLSGTSQTMTTGITADGQLINTGQAVQSSDNSGESG-KVSPDINETNTNADLFV 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  554 PTSSSSQLPVTIDSTGILQQNTNSLTTSSGQVHSSDLQGNYIQSPVSEETQAQNIQVSTAQPVVQHLQLQESQQPTSQAQ 633
Cdd:cd22537   282 PTSSSSQLPVTIDSTGILQQNASSLTTVSGQVHTSDLQGNYIQAPVSDETQAQNIQVSTAQPSVQQIQLHESQQPTSQAQ 361

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  634 IVQGITPQTIHGVQA-SGQNISQQALQNLQLQ-LNPGTFLIQAQTVTPSGQITWQTFQVQGVQNLQNLQIQNTAAQQITL 711
Cdd:cd22537   362 IVQGITQQAIQGVQAlGAQAIPQQALQNLQLQlLNPGTFLIQAQTVTPSGQITWQTFQVQGVQNLQNLQIQNAPAQQITL 441

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  712 TPVQTLTLGQVAAGGTLTSTPVSLSTGQLPNLQTVTVNSIDSTGIQLHPGENADSPADIRIKEEEPDPEEWQLSGDSTLN 791
Cdd:cd22537   442 TPVQTLTLGQVGAGGAITSTPVSLSTGQLPNLQTVTVNSIDSAGIQLQQSENADSPADIQIKEEEPDSEEWQLSGDSTLN 521

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 918612218  792 TNDLTHLRVQVVDEEGDQQHQEGKRLRRVACTCPNCKEGGGRGTNLGKKKQHI 844
Cdd:cd22537   522 TNDLTHLRVQLVEEEGDQPHQEGKRLRRVACTCPNCKEGGGRGSNLGKKKQHI 574
SP4_N cd22536
N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins ...
 318-844 2.36e-60

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: 217.86  E-value: 2.36e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  318 DLASAQLGGapNRWEVLSATPTTIKDeaGNLVQIPSAATSSGQYVLPLQN--------------LQNQQIFSVAPGSDSS 383
Cdd:cd22536    61 ELVTTQLAG--NAWQIVAAAPPTSKE--NNVAQQGVSAATSSAAPSSSNNgstsptkvkagnsnASAPGQFQVIQVQNMQ 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  384 NGTvSNVQYQVIPQIQSTDGQQVQIGFTGSSDNGGLNQessQIQIIP-GSNQTLLASG--TPPANI--QNLMPQTGQVQV 458
Cdd:cd22536   137 NPS-GSVQYQVIPQIQTVEGQQIQISPANATALQDLQG---QIQLIPaGNNQAILTTPnrTASGNIiaQNLANQTVPVQI 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  459 QgvaiGGSSFP--------GQTQVVANVPLGLPGNITFVPINSVDLDSLGLSGSSQTMTAGINADGHLINTGQAMDSSDN 530
Cdd:cd22536   213 R----PGVSIPlqlqtipgAQAQVVTTLPINIGGVTLALPVINNVAAGGGSGQLVQPSDGGVSNGNQLVSTPITTASVST 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  531 ---SERTGERVSPDINETNTDSDLFVPTSSSSQLPVTIDSTGILQQNTNSLTTSSGQVHSSDLQGNYIQsPVSEETQAQN 607
Cdd:cd22536   289 mpeSPSSSTTCTTTASTSLTSSDTLVSSAETGQYASTAASSERTEEEPQTSAAESEAQSSSQLQSNGLQ-NVQDQSNSLQ 367

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  608 IQVSTAQPVVQHLQLQESQQPTSQAQIVQ------GITPQTIHgvQASGQNIsqqalqNLQLQLNPGTFLIQAQTVTPSG 681
Cdd:cd22536   368 QVQIVGQPILQQIQIQQPQQQIIQAIQPQsfqlqsGQTIQTIQ--QQPLQNV------QLQAVQSPTQVLIRAPTLTPSG 439

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  682 QITWQTFQVQGVQNLQNLQIQNTA-AQQITLTPVQT----LTLGQVAAgGTLTSTPVSLSTGQL---PNLQTVTVNSIDS 753
Cdd:cd22536   440 QISWQTVQVQNIQSLSNLQVQNAGlPQQLTLTPVSSsaggTTIAQIAP-VAVAGTPITLNAAQLasvPNLQTVNVANLGA 518

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  754 TGIQLHPGENADSPADIRIKEEEPDPEEWQLSGDST-------------LNTNDLTHLRVQVVDEEGDQQHQEGKRLRRV 820
Cdd:cd22536   519 AGVQVQGVPVTITSVAGQQQGQDGVKVQQATIAPVTvavgnianatigaVSPDQITQVQLQQAQQASDQEVQPGKRLRRV 598

                         570       580
                  ....*....|....*....|....*
gi 918612218  821 ACTCPNCKEGGGRGTN-LGKKKQHI 844
Cdd:cd22536   599 ACSCPNCREGEGRGSSePGKKKQHI 623
SP1_N cd22539
N-terminal domain of transcription factor Specificity Protein (SP) 1; Specificity Proteins ...
 318-844 6.73e-43

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: 162.38  E-value: 6.73e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  318 DLASAQLGGAPNRWEVLSA---TPTTIKDEAGNLVQIPS----AATSSGQYVLPLQNLQNQQIFSVAPGsdssngTVSNV 390
Cdd:cd22539    45 DLTQAQIAQSANGWQIIPTgsqAPTPSKEQSGDSSTADSskksRVATAGYVVVAAPNLQNQQVLTSLPG------VMPNI 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  391 QYQVIPQIQSTDGQQVQIGFTGSSDNGglnQESSQIQIIPGSNQTLLASGTPPANIQNLMPQTGQ--VQVQGVAIGGSSF 468
Cdd:cd22539   119 QYQVIPQFQTVDGQQLQFATTQAQVQQ---DASGQLQIIPGTNQQIITTNRSGSGNIITMPNLLQqaVPIQGLGLANNVL 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  469 PGQTQVVANVPLGLPGNITFVPINSVdldslglsgssqtmtaginadghlintgqamdssdnsertgervsPDINETNTd 548
Cdd:cd22539   196 PGQTQFVANVPVALNGNITLLPVSSV---------------------------------------------TASFFTNA- 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  549 sdlfvptssssqlpvtidstgilqqNTNSLTTSSGQVhssdlqgnyiqspvseetqaqniqvstaqpvvqhlqLQESQQP 628
Cdd:cd22539   230 -------------------------NSYSTTTTTSNM------------------------------------GQQQQQI 248

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  629 TSQAQIVQGI-TPQTIHGVQASG-----QNISQQALQNLQLQLNPGTFLIQAQT-VTPSGQITWQTFQvqgvqnLQNLQi 701
Cdd:cd22539   249 LIQPQLVQGGqTIQALQAASLPGqtfttQTISQEALQNLQIQTVPNSGPIIIRTpVGPNGQVSWQTIQ------LQNLQ- 321

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  702 qntaaqqitltpvqtltlgqvaaggtlTSTPVSLSTGQLPNLQTVTVNSIDSTGIQLHPGENAdsPADIrikEEEPDPEE 781
Cdd:cd22539   322 ---------------------------TVTVNAAQLSSMPGLQTINLNALGASGIQVHQLQGL--PLTI---ANATGEHG 369

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 918612218  782 WQLSGDSTLNTNDLTHLRVQVVDEEGDQQHQEGKRLRRVACTCPNCKEGGGRG-TNLGKKKQHI 844
Cdd:cd22539   370 AQLGLHGAGGDGLHDDSAAEEGETEPDPQPQPGRRTRREACTCPYCKDGEGRDsGDPGKKKQHI 433
SP1-4_N cd22545
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ...
 801-844 5.78e-18

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: 79.41  E-value: 5.78e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 918612218  801 QVVDEEGDQQHQEGKRLRRVACTCPNCKEGGGRGTNLGKKKQHI 844
Cdd:cd22545    39 QVIPQFQDQEPQPGKRLRRVACTCPNCKDGEGRGSEDGKKKQHI 82
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
 346-844 1.31e-17

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: 87.29  E-value: 1.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  346 GNLVQIP----SAATSSGQYVLPLQNlqnqqifSVAPGSDSSNGTVSNVQYQVIPQIQstdgqqvqigftgssdNGGLNQ 421
Cdd:cd22540    83 GNIIQLQgsqlSSSAPGGQQVFAIQN-------PTMIIKGSQTRSSTNQQYQISPQIQ----------------AAGQIN 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  422 ESSQIQIIPGSNQTLLASgTPPANIQNLMPQTGQVQVQGVAIGGSSfPGQTQVVAN-VPLGLPGNITFV-PINSVDLDSl 499
Cdd:cd22540   140 NSGQIQIIPGTNQAIITP-VQVLQQPQQAHKPVPIKPAPLQTSNTN-SASLQVPGNvIKLQSGGNVALTlPVNNLVGTQ- 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  500 glSGSSQTMTAGINADGHLINTGQAMDSSDNSERTGERVSPDINETNTDSdlfvptssssqlpvtidstgILQQNTNSLt 579
Cdd:cd22540   217 --DGATQLQLAAAPSKPSKKIRKKSAQAAQPAVTVAEQVETVLIETTADN--------------------IIQAGNNLL- 273

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  580 tssgqvhssdlqgnYIQSPvseetqaqniqvSTAQPVVqhLQLQESQQPTSQAQIVQgITPQTIHGVQASGQN-ISQQAL 658
Cdd:cd22540   274 --------------IVQSP------------GTGQPAV--LQQVQVLQPKQEQQVVQ-IPQQALRVVQAASATlPTVPQK 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  659 QNLQLQLNPGTFL-IQAQTVTPSGQITWQTFQVQGVQnlqnlqiqnTAAQQITLTPVQtltLGQVAAGGTLTSTP----- 732
Cdd:cd22540   325 PLQNIQIQNSEPTpTQVYIKTPSGEVQTVLLQEAPAA---------TATPSSSTSTVQ---QQVTANNGTGTSKPnynvr 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  733 --------------VSLSTGQLP----NLQTVTVN---------SIDSTGIQLHPGENADSPADIRIKEeePDPEEWQLS 785
Cdd:cd22540   393 kertlpkiapaggiISLNAAQLAaaaqAIQTININgvqvqgvpvTITNAGGQQQLTVQTVSSNNLTISG--LSPTQIQLQ 470

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 918612218  786 GDSTLNTndlthlrvqvvdeegdqQHQEGKRLRRVACTCPNCKEGGGRGTNLGKKKqHI 844
Cdd:cd22540   471 MEQALEI-----------------ETQPGEKRRRMACTCPNCKDGEKRSGEQGKKK-HI 511
SP1-4_arthropods_N cd22553
N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; ...
 592-844 9.27e-14

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: 74.29  E-value: 9.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  592 GNYIQSPVSEETQAQNIQV----STAQPVVQHLQLQ-ESQQPTSQAQIVQGITPQTIHGVQASGQnisqqalqnlqlqln 666
Cdd:cd22553   144 GNAVQLPLNNMTQTIPVQVpvstANGQTVYQTIQVPiQAIQSGNAGGGNQALQAQVIPQLAQAAQ--------------- 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  667 pgtfLIQAQTVTPSGQITWQTF-QVQGVQNLQNLQIQNTAAQQIT---------------LTPVQTLTLGQVAA----GG 726
Cdd:cd22553   209 ----LQPQQLAQVSSQGYIQQIpANASQQQPQMVQQGPNQSGQIIgqvasassiqaaaipLTVYTGALAGQNGSnqqqVG 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  727 TLTSTPVSLSTGQLPNLQTVTVNSIDS----TGIQLHPGENAdSPADIRIKEEEPDPEEWQLSGDSTLNTndlthlrvqv 802
Cdd:cd22553   285 QIVTSPIQGMTQGLTAPASSSIPTVVQqqaiQGNPLPPGTQI-IAAGQQLQQDPNDPTKWQVVADGTPGS---------- 353

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 918612218  803 vdeegdqqhqeGKRLRRVACTCPNCKEGGGRGTNLGKKKQHI 844
Cdd:cd22553   354 -----------KKRLRRVACTCPNCRDGDGTRNGENKKKQHI 384
zf-H2C2_2 pfam13465
Zinc-finger double domain;
889-912 2.55e-08

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 50.45  E-value: 2.55e-08
                           10        20
                   ....*....|....*....|....
gi 918612218   889 ELQRHRRTHTGEKKFVCPECSKRF 912
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 903-925 1.02e-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: 43.06  E-value: 1.02e-05
                           10        20
                   ....*....|....*....|...
gi 918612218   903 FVCPECSKRFMRSDHLAKHIKTH 925
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 873-897 6.17e-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: 6.17e-05
                           10        20
                   ....*....|....*....|....*
gi 918612218   873 FICNwmFCGKRFTRSDELQRHRRTH 897
Cdd:pfam00096    1 YKCP--DCGKSFSRKSNLKRHLRTH 23
ZnF_C2H2 smart00355
zinc finger;
903-925 2.19e-04

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 39.37  E-value: 2.19e-04
                            10        20
                    ....*....|....*....|...
gi 918612218    903 FVCPECSKRFMRSDHLAKHIKTH 925
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 903-925 5.87e-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: 5.87e-04
                           10        20
                   ....*....|....*....|...
gi 918612218   903 FVCPECSKRFMRSDHLAKHIKTH 925
Cdd:pfam13894    1 FKCPICGKSFSSKKSLKRHLKTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
858-940 8.23e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.15  E-value: 8.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218  858 SHLRAHLRW--HSGE--RPFICNWMFCGKRFTRSDELQRHRRTHTGEKKFVCP--ECSKRFMRSDHLAKHIKTHQNKKVI 931
Cdd:COG5048   303 SPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQYKDLK 382


                  ....*....
gi 918612218  932 HSSSAVLAS 940
Cdd:COG5048   383 NDKKSETLS 391
ZnF_C2H2 smart00355
zinc finger;
873-897 2.54e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 36.29  E-value: 2.54e-03
                            10        20
                    ....*....|....*....|....*
gi 918612218    873 FICNWmfCGKRFTRSDELQRHRRTH 897
Cdd:smart00355    1 YRCPE--CGKVFKSKSALREHMRTH 23
zf-C2H2_8 pfam15909
C2H2-type zinc ribbon; This family carries three zinc-fingers in tandem.
 845-922 3.55e-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: 3.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918612218   845 CHIPGCGKVYGKTSHLRAHLRWHSGE------RPFICNWMFCGKRFTRSDELQRHRRTHTGEKK-FVCPECSKRFMRSDH 917
Cdd:pfam15909    2 CSSPGCCLSFPSVRDLAQHLRTHCPPtqslegKLFRCSALSCTETFPSMQELVAHSKLHYKPNRyFKCENCLLRFRTHRS 81


                   ....*
gi 918612218   918 LAKHI 922
Cdd:pfam15909   82 LFKHL 86
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 873-897 9.73e-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: 9.73e-03
                           10        20
                   ....*....|....*....|....*
gi 918612218   873 FICNwmFCGKRFTRSDELQRHRRTH 897
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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