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Conserved domains on  [gi|1388876046|ref|NP_001350154|]
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transcription factor Sp2 isoform 3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
 4-520 0e+00

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: 577.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046   4 AATAAVSPSDYLQPAAATTQDSQPSPLALLAATCSKIGPPAVEAAVTPPAPPQPTPRKLVPIKPAPLPLSPCKNSFSILS 83
Cdd:cd22540     1 AATAAVSPSEYLQPAASTTQDSQPSPLALLAATCSKIGPPAVEAAVTPPAPPQPTPRKLVPIKPAPLPLGPGKNSIGFLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046  84 SKGNILQIQGSQLSTSYPGGQFVFAIQNPTLINKGS--RSNASIQYQ-VPQIQgnssqtIQVQPSLTNQIQVIPGTNQAI 160
Cdd:cd22540    81 AKGNIIQLQGSQLSSSAPGGQQVFAIQNPTMIIKGSqtRSSTNQQYQiSPQIQ------AAGQINNSGQIQIIPGTNQAI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 161 TTP------STSGHKPVPIKPAPVQKSSTTTTPVQSGANVVKLTGGGsNMTLTLPLNNLVNTSDIGGPAQLltespPTPL 234
Cdd:cd22540   155 ITPvqvlqqPQQAHKPVPIKPAPLQTSNTNSASLQVPGNVIKLQSGG-NVALTLPVNNLVGTQDGATQLQL-----AAAP 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 235 SKTNKKARKKSLPVSQPSVAVAEQVETVLIETTADNIIQAGNNLLIVQSPGGGQPAVVQQVQVVPPKAEQQQVVQIPQqA 314
Cdd:cd22540   229 SKPSKKIRKKSAQAAQPAVTVAEQVETVLIETTADNIIQAGNNLLIVQSPGTGQPAVLQQVQVLQPKQEQQVVQIPQQ-A 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 315 LRVVQAASATLPTVPQKPSQNFQIQTTEPTPTQVYIRTPSGEVQTVLVQDSPPATAATTSTVTCNSPAlrAPHLSGTSKK 394
Cdd:cd22540   308 LRVVQAASATLPTVPQKPLQNIQIQNSEPTPTQVYIKTPSGEVQTVLLQEAPAATATPSSSTSTVQQQ--VTANNGTGTS 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 395 HSAAILRKERPLPKIAPAGSIISLNAAQLAAAAQAMQTININGVQVQGVPVTITNTGGQQQLTVQNVSGNNLTISGLSPT 474
Cdd:cd22540   386 KPNYNVRKERTLPKIAPAGGIISLNAAQLAAAAQAIQTININGVQVQGVPVTITNAGGQQQLTVQTVSSNNLTISGLSPT 465

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 1388876046 475 QIQLQMEQALAGEAQPGEKRRRMACTCPNCKDGEKRSGEQGKKKHV 520
Cdd:cd22540   466 QIQLQMEQALEIETQPGEKRRRMACTCPNCKDGEKRSGEQGKKKHI 511
zf-H2C2_2 pfam13465
Zinc-finger double domain;
565-588 7.96e-07

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 45.44  E-value: 7.96e-07
                          10        20
                  ....*....|....*....|....
gi 1388876046 565 ELQRHARTHTGDKRFECAQCQKRF 588
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
536-562 1.79e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 1.79e-05
                          10        20
                  ....*....|....*....|....*..
gi 1388876046 536 LRAHVRLHTGERPFVCNwfFCGKRFTR 562
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCP--ECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 579-601 5.42e-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: 40.36  E-value: 5.42e-05
                          10        20
                  ....*....|....*....|...
gi 1388876046 579 FECAQCQKRFMRSDHLTKHYKTH 601
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
 4-520 0e+00

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: 577.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046   4 AATAAVSPSDYLQPAAATTQDSQPSPLALLAATCSKIGPPAVEAAVTPPAPPQPTPRKLVPIKPAPLPLSPCKNSFSILS 83
Cdd:cd22540     1 AATAAVSPSEYLQPAASTTQDSQPSPLALLAATCSKIGPPAVEAAVTPPAPPQPTPRKLVPIKPAPLPLGPGKNSIGFLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046  84 SKGNILQIQGSQLSTSYPGGQFVFAIQNPTLINKGS--RSNASIQYQ-VPQIQgnssqtIQVQPSLTNQIQVIPGTNQAI 160
Cdd:cd22540    81 AKGNIIQLQGSQLSSSAPGGQQVFAIQNPTMIIKGSqtRSSTNQQYQiSPQIQ------AAGQINNSGQIQIIPGTNQAI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 161 TTP------STSGHKPVPIKPAPVQKSSTTTTPVQSGANVVKLTGGGsNMTLTLPLNNLVNTSDIGGPAQLltespPTPL 234
Cdd:cd22540   155 ITPvqvlqqPQQAHKPVPIKPAPLQTSNTNSASLQVPGNVIKLQSGG-NVALTLPVNNLVGTQDGATQLQL-----AAAP 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 235 SKTNKKARKKSLPVSQPSVAVAEQVETVLIETTADNIIQAGNNLLIVQSPGGGQPAVVQQVQVVPPKAEQQQVVQIPQqA 314
Cdd:cd22540   229 SKPSKKIRKKSAQAAQPAVTVAEQVETVLIETTADNIIQAGNNLLIVQSPGTGQPAVLQQVQVLQPKQEQQVVQIPQQ-A 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 315 LRVVQAASATLPTVPQKPSQNFQIQTTEPTPTQVYIRTPSGEVQTVLVQDSPPATAATTSTVTCNSPAlrAPHLSGTSKK 394
Cdd:cd22540   308 LRVVQAASATLPTVPQKPLQNIQIQNSEPTPTQVYIKTPSGEVQTVLLQEAPAATATPSSSTSTVQQQ--VTANNGTGTS 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 395 HSAAILRKERPLPKIAPAGSIISLNAAQLAAAAQAMQTININGVQVQGVPVTITNTGGQQQLTVQNVSGNNLTISGLSPT 474
Cdd:cd22540   386 KPNYNVRKERTLPKIAPAGGIISLNAAQLAAAAQAIQTININGVQVQGVPVTITNAGGQQQLTVQTVSSNNLTISGLSPT 465

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 1388876046 475 QIQLQMEQALAGEAQPGEKRRRMACTCPNCKDGEKRSGEQGKKKHV 520
Cdd:cd22540   466 QIQLQMEQALEIETQPGEKRRRMACTCPNCKDGEKRSGEQGKKKHI 511
zf-H2C2_2 pfam13465
Zinc-finger double domain;
565-588 7.96e-07

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 45.44  E-value: 7.96e-07
                          10        20
                  ....*....|....*....|....
gi 1388876046 565 ELQRHARTHTGDKRFECAQCQKRF 588
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
536-562 1.79e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 1.79e-05
                          10        20
                  ....*....|....*....|....*..
gi 1388876046 536 LRAHVRLHTGERPFVCNwfFCGKRFTR 562
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCP--ECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 579-601 5.42e-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: 40.36  E-value: 5.42e-05
                          10        20
                  ....*....|....*....|...
gi 1388876046 579 FECAQCQKRFMRSDHLTKHYKTH 601
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
ZnF_C2H2 smart00355
zinc finger;
579-601 2.44e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.52  E-value: 2.44e-03
                           10        20
                   ....*....|....*....|...
gi 1388876046  579 FECAQCQKRFMRSDHLTKHYKTH 601
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
ZnF_C2H2 smart00355
zinc finger;
549-573 2.56e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.52  E-value: 2.56e-03
                           10        20
                   ....*....|....*....|....*
gi 1388876046  549 FVCNWffCGKRFTRSDELQRHARTH 573
Cdd:smart00355   1 YRCPE--CGKVFKSKSALREHMRTH 23
NEAT COG5386
Heme-binding NEAT domain [Inorganic ion transport and metabolism];
107-279 3.61e-03

Heme-binding NEAT domain [Inorganic ion transport and metabolism];


Pssm-ID: 444149 [Multi-domain]  Cd Length: 302  Bit Score: 39.89  E-value: 3.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 107 FAIQNPTlinkgSRSNASIQYQVPQIQGNSSQTIQVQPSlTNQIQVIPGTNQAITTPSTSGHKPVPIKPAPVQKSSTTTT 186
Cdd:COG5386   117 FEVPDLS-----KPLNAKVHVVIPAINYDHKYDVRLVFD-TNSIKPVGPVKEEPAPPPENTTDPEKLEDGTYTIDFKVLK 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 187 PVQSGANVVKLTGG-------GSNMTLTLPLNNLVNTSDIGGPAQLLTESPPTPLSKTNKKARKKSLPVSQPSVAvaeqv 259
Cdd:COG5386   191 DGTKEISMMDQTRTvefknpkPSDNVTSTAANSGSLQAKEGIKSQPTKSDSTSKPATTTKPKKKVVPIAVNSLKL----- 265

                         170       180
                  ....*....|....*....|
gi 1388876046 260 etVLIETTADNIIQAGNNLL 279
Cdd:COG5386   266 --GLKFSNTVNKKQILNKLT 283
zf-C2H2_8 pfam15909
C2H2-type zinc ribbon; This family carries three zinc-fingers in tandem.
 521-597 8.00e-03

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


Pssm-ID: 464935 [Multi-domain]  Cd Length: 98  Bit Score: 36.24  E-value: 8.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 521 CHIPDCGKTFRKTSLLRAHVRLHTGE------RPFVCNWFFCGKRFTRSDELQRHARTHTGDKR-FECAQCQKRFMRSDH 593
Cdd:pfam15909   2 CSSPGCCLSFPSVRDLAQHLRTHCPPtqslegKLFRCSALSCTETFPSMQELVAHSKLHYKPNRyFKCENCLLRFRTHRS 81


                  ....
gi 1388876046 594 LTKH 597
Cdd:pfam15909  82 LFKH 85
 
Name Accession Description Interval E-value
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
 4-520 0e+00

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: 577.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046   4 AATAAVSPSDYLQPAAATTQDSQPSPLALLAATCSKIGPPAVEAAVTPPAPPQPTPRKLVPIKPAPLPLSPCKNSFSILS 83
Cdd:cd22540     1 AATAAVSPSEYLQPAASTTQDSQPSPLALLAATCSKIGPPAVEAAVTPPAPPQPTPRKLVPIKPAPLPLGPGKNSIGFLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046  84 SKGNILQIQGSQLSTSYPGGQFVFAIQNPTLINKGS--RSNASIQYQ-VPQIQgnssqtIQVQPSLTNQIQVIPGTNQAI 160
Cdd:cd22540    81 AKGNIIQLQGSQLSSSAPGGQQVFAIQNPTMIIKGSqtRSSTNQQYQiSPQIQ------AAGQINNSGQIQIIPGTNQAI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 161 TTP------STSGHKPVPIKPAPVQKSSTTTTPVQSGANVVKLTGGGsNMTLTLPLNNLVNTSDIGGPAQLltespPTPL 234
Cdd:cd22540   155 ITPvqvlqqPQQAHKPVPIKPAPLQTSNTNSASLQVPGNVIKLQSGG-NVALTLPVNNLVGTQDGATQLQL-----AAAP 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 235 SKTNKKARKKSLPVSQPSVAVAEQVETVLIETTADNIIQAGNNLLIVQSPGGGQPAVVQQVQVVPPKAEQQQVVQIPQqA 314
Cdd:cd22540   229 SKPSKKIRKKSAQAAQPAVTVAEQVETVLIETTADNIIQAGNNLLIVQSPGTGQPAVLQQVQVLQPKQEQQVVQIPQQ-A 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 315 LRVVQAASATLPTVPQKPSQNFQIQTTEPTPTQVYIRTPSGEVQTVLVQDSPPATAATTSTVTCNSPAlrAPHLSGTSKK 394
Cdd:cd22540   308 LRVVQAASATLPTVPQKPLQNIQIQNSEPTPTQVYIKTPSGEVQTVLLQEAPAATATPSSSTSTVQQQ--VTANNGTGTS 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 395 HSAAILRKERPLPKIAPAGSIISLNAAQLAAAAQAMQTININGVQVQGVPVTITNTGGQQQLTVQNVSGNNLTISGLSPT 474
Cdd:cd22540   386 KPNYNVRKERTLPKIAPAGGIISLNAAQLAAAAQAIQTININGVQVQGVPVTITNAGGQQQLTVQTVSSNNLTISGLSPT 465

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 1388876046 475 QIQLQMEQALAGEAQPGEKRRRMACTCPNCKDGEKRSGEQGKKKHV 520
Cdd:cd22540   466 QIQLQMEQALEIETQPGEKRRRMACTCPNCKDGEKRSGEQGKKKHI 511
SP4_N cd22536
N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins ...
 14-518 1.17e-33

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: 136.20  E-value: 1.17e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046  14 YLQPAAATTQDSQPSPLALLAATCSKIG-PPAVEAAVTPPAPPQPTPRKLVPIK--PAPLPLSPCK---NSFSIL----- 82
Cdd:cd22536     1 NKKGKTSGSQDSQPSPLALLAATCSKIGtPGENQGAGQQQQIIIDPSQGLVQLQnqPQQLELVTTQlagNAWQIVaaapp 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046  83 SSKGNILQIQGSQLSTSYPG------------------------GQF----VFAIQNPTlinkgsrsnASIQYQV-PQIQ 133
Cdd:cd22536    81 TSKENNVAQQGVSAATSSAApsssnngstsptkvkagnsnasapGQFqviqVQNMQNPS---------GSVQYQViPQIQ 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 134 GNSSQTIQVQPS-------LTNQIQVIP-GTNQAI-TTPSTSGHK------------PVPIKPA---PVQKSSTTTTPVQ 189
Cdd:cd22536   152 TVEGQQIQISPAnatalqdLQGQIQLIPaGNNQAIlTTPNRTASGniiaqnlanqtvPVQIRPGvsiPLQLQTIPGAQAQ 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 190 SGANVVKLTGGgsnMTLTLPLNNLVNTSdiGGPAQLLT--------------------------ESPPTPLSKTNKKArk 243
Cdd:cd22536   232 VVTTLPINIGG---VTLALPVINNVAAG--GGSGQLVQpsdggvsngnqlvstpittasvstmpESPSSSTTCTTTAS-- 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 244 KSLPVSQ----------------PSVAVAEQVETVLIETTADNIIQAGNNLLIVQSPGGGQPAVVQQVQVVPPK----AE 303
Cdd:cd22536   305 TSLTSSDtlvssaetgqyastaaSSERTEEEPQTSAAESEAQSSSQLQSNGLQNVQDQSNSLQQVQIVGQPILQqiqiQQ 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 304 QQQVVQIPQQALRVVQAASATLPTVPQKPSQNFQIQTTEpTPTQVYIR----TPSGEV--QTVLVQDSPPATAATTSTvt 377
Cdd:cd22536   385 PQQQIIQAIQPQSFQLQSGQTIQTIQQQPLQNVQLQAVQ-SPTQVLIRaptlTPSGQIswQTVQVQNIQSLSNLQVQN-- 461

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 378 cnspALRAPHLSGTSKKHSAAilrkERPLPKIAP---AGSIISLNAAQLAAAAQAMqTININ-----GVQVQGVPVTITN 449
Cdd:cd22536   462 ----AGLPQQLTLTPVSSSAG----GTTIAQIAPvavAGTPITLNAAQLASVPNLQ-TVNVAnlgaaGVQVQGVPVTITS 532

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 450 TGGQQQ----------------LTVQNVSgnNLTISGLSP---TQIQLQM-EQALAGEAQPGEKRRRMACTCPNCKDGEK 509
Cdd:cd22536   533 VAGQQQgqdgvkvqqatiapvtVAVGNIA--NATIGAVSPdqiTQVQLQQaQQASDQEVQPGKRLRRVACSCPNCREGEG 610

                         650
                  ....*....|
gi 1388876046 510 R-SGEQGKKK 518
Cdd:cd22536   611 RgSSEPGKKK 620
SP1_N cd22539
N-terminal domain of transcription factor Specificity Protein (SP) 1; Specificity Proteins ...
 23-518 4.06e-22

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: 99.20  E-value: 4.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046  23 QDSQPSPLALLAATCSKIGPPAVEAAVTPPAPPQPTPRKLvpiKPAPLPLSPCKNSFSILSS-----------KGNILQI 91
Cdd:cd22539     5 QESQPSPLALLAATCSRIESPNENSNSSQQQQQQQGELEL---DLTQAQIAQSANGWQIIPTgsqaptpskeqSGDSSTA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046  92 QGSQLSTSYPGGQFVFA---IQNPTLINKGSRSNASIQYQV-PQIQGNSSQTIQ-------VQPSLTNQIQVIPGTNQAI 160
Cdd:cd22539    82 DSSKKSRVATAGYVVVAapnLQNQQVLTSLPGVMPNIQYQViPQFQTVDGQQLQfattqaqVQQDASGQLQIIPGTNQQI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 161 TTPSTSGHKPVPIKPAPVQKSsttttpvqsganvvkltgggsnmtltLPLNNLVNTSDI-GGPAQLLTESPptplskTNK 239
Cdd:cd22539   162 ITTNRSGSGNIITMPNLLQQA--------------------------VPIQGLGLANNVlPGQTQFVANVP------VAL 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 240 KARKKSLPVSQPSVAVAEQVETVLIETTADNIIQAGNNLLIVQspgggqpavvqqvqvvppkaeqqqVVQIPQQALRVVQ 319
Cdd:cd22539   210 NGNITLLPVSSVTASFFTNANSYSTTTTTSNMGQQQQQILIQP------------------------QLVQGGQTIQALQ 265

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 320 AASA-----TLPTVPQKPSQNFQIQTTePTPTQVYIRT---PSGEV--QTVLVQDsppataatTSTVTCNSPALRAphls 389
Cdd:cd22539   266 AASLpgqtfTTQTISQEALQNLQIQTV-PNSGPIIIRTpvgPNGQVswQTIQLQN--------LQTVTVNAAQLSS---- 332

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 390 gtskkhsaailrkerplpkiAPAGSIISLNaaqlaaaaqamqTININGVQV---QGVPVTITNTGGQQ--QLTVQNVSGn 464
Cdd:cd22539   333 --------------------MPGLQTINLN------------ALGASGIQVhqlQGLPLTIANATGEHgaQLGLHGAGG- 379

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1388876046 465 nltiSGLSPTQIQLQMEQALAGEAQPGEKRRRMACTCPNCKDGEKR-SGEQGKKK 518
Cdd:cd22539   380 ----DGLHDDSAAEEGETEPDPQPQPGRRTRREACTCPYCKDGEGRdSGDPGKKK 430
SP3_N cd22537
N-terminal domain of transcription factor Specificity Protein (SP) 3; Specificity Proteins ...
 19-518 4.73e-21

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: 97.33  E-value: 4.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046  19 AATTQDSQPSPLALLAATCSKIGPPAVEAAVTPPAPPQPTPrklVPIKPAPLPLSPCKNSFSILSS--------KGNILQ 90
Cdd:cd22537     1 GAAEQDTQPSPLALLAATCSKIGSPSPGDDAAAAGNAASAG---QTGDLASAQLTGAPNRWEVLTPtpttikdeAGNLVQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046  91 IQGSQLSTSypGGQFVFAIQ------NPTLINKGSRSNA---SIQYQV-PQIQGNSSQTIQVQPS----------LTNQI 150
Cdd:cd22537    78 IPGGGTVTS--SGQYVLPLQslqnqqIFSVAPGSDASNGtvpNVQYQViPQIQTTDGQQVQLGFAtssdntglqqEGGQI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 151 QVIPGTNQAITTPST----------SGHKPVPIKPA------PVQKSSTTTTPVQSGANV------------VKLTGGGS 202
Cdd:cd22537   156 QIIPGSNQTIIASGTpsavqqllsqSGHVVQIQGVSiggssfPGQTQVVANVPLGLPGNItfvpinsvdldsLGLSGTSQ 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 203 NMTLTLP-------LNNLVNTSDIGGPAQLLTESPPTPLSKTN---KKARKKSLPVSQPSVAVAEQvETVLIETTADNII 272
Cdd:cd22537   236 TMTTGITadgqlinTGQAVQSSDNSGESGKVSPDINETNTNADlfvPTSSSSQLPVTIDSTGILQQ-NASSLTTVSGQVH 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 273 QAGNNLLIVQSPGGGQPAVVQQVQVVPPKAEQQQVVQI--------------PQQALRVVQAASATlpTVPQKPSQNFQI 338
Cdd:cd22537   315 TSDLQGNYIQAPVSDETQAQNIQVSTAQPSVQQIQLHEsqqptsqaqivqgiTQQAIQGVQALGAQ--AIPQQALQNLQL 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 339 QTTEPTP--TQVYIRTPSGEV--QTVLVQdsppataattstvtcNSPALRAPHLSGTSKKHSAAILRKERPLPKIAPAGS 414
Cdd:cd22537   393 QLLNPGTflIQAQTVTPSGQItwQTFQVQ---------------GVQNLQNLQIQNAPAQQITLTPVQTLTLGQVGAGGA 457

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 415 IISLNAAQLAAAAQAMQTININGV---QVQGVPVTITNTGGQQQLTV--------QNVSGNNLTISGLSPTQIQLqMEQA 483
Cdd:cd22537   458 ITSTPVSLSTGQLPNLQTVTVNSIdsaGIQLQQSENADSPADIQIKEeepdseewQLSGDSTLNTNDLTHLRVQL-VEEE 536

                         570       580       590
                  ....*....|....*....|....*....|....*
gi 1388876046 484 LAGEAQPGEKRRRMACTCPNCKDGEKRSGEQGKKK 518
Cdd:cd22537   537 GDQPHQEGKRLRRVACTCPNCKEGGGRGSNLGKKK 571
SP1-4_N cd22545
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ...
 475-523 2.31e-13

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: 65.54  E-value: 2.31e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1388876046 475 QIQLQ-MEQALAGEAQPGEKRRRMACTCPNCKDGEKRSGEQGKKKHvcHI 523
Cdd:cd22545    35 NIQYQvIPQFQDQEPQPGKRLRRVACTCPNCKDGEGRGSEDGKKKQ--HI 82
SP1-4_N cd22545
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ...
 19-46 6.26e-10

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: 55.91  E-value: 6.26e-10
                          10        20
                  ....*....|....*....|....*...
gi 1388876046  19 AATTQDSQPSPLALLAATCSKIGPPAVE 46
Cdd:cd22545     1 TSSAQDSQPSPLALLAATCSKIGSPAEN 28
zf-H2C2_2 pfam13465
Zinc-finger double domain;
565-588 7.96e-07

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 45.44  E-value: 7.96e-07
                          10        20
                  ....*....|....*....|....
gi 1388876046 565 ELQRHARTHTGDKRFECAQCQKRF 588
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
536-562 1.79e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 1.79e-05
                          10        20
                  ....*....|....*....|....*..
gi 1388876046 536 LRAHVRLHTGERPFVCNwfFCGKRFTR 562
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCP--ECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 579-601 5.42e-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: 40.36  E-value: 5.42e-05
                          10        20
                  ....*....|....*....|...
gi 1388876046 579 FECAQCQKRFMRSDHLTKHYKTH 601
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 549-573 7.13e-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: 39.98  E-value: 7.13e-05
                          10        20
                  ....*....|....*....|....*
gi 1388876046 549 FVCNwfFCGKRFTRSDELQRHARTH 573
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
SP1-4_arthropods_N cd22553
N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; ...
 411-520 5.86e-04

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: 42.71  E-value: 5.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 411 PAGSIISLNAAQLAAAAQAMQTININGVQVQGVPVTITNTGGQQQLTvqnvSGNNLTISGLSPTQIQLQMEqalaGEAQP 490
Cdd:cd22553   282 QVGQIVTSPIQGMTQGLTAPASSSIPTVVQQQAIQGNPLPPGTQIIA----AGQQLQQDPNDPTKWQVVAD----GTPGS 353

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1388876046 491 GEKRRRMACTCPNCKDGE-KRSGEQGKKKHV 520
Cdd:cd22553   354 KKRLRRVACTCPNCRDGDgTRNGENKKKQHI 384
ZnF_C2H2 smart00355
zinc finger;
579-601 2.44e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.52  E-value: 2.44e-03
                           10        20
                   ....*....|....*....|...
gi 1388876046  579 FECAQCQKRFMRSDHLTKHYKTH 601
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
ZnF_C2H2 smart00355
zinc finger;
549-573 2.56e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.52  E-value: 2.56e-03
                           10        20
                   ....*....|....*....|....*
gi 1388876046  549 FVCNWffCGKRFTRSDELQRHARTH 573
Cdd:smart00355   1 YRCPE--CGKVFKSKSALREHMRTH 23
NEAT COG5386
Heme-binding NEAT domain [Inorganic ion transport and metabolism];
107-279 3.61e-03

Heme-binding NEAT domain [Inorganic ion transport and metabolism];


Pssm-ID: 444149 [Multi-domain]  Cd Length: 302  Bit Score: 39.89  E-value: 3.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 107 FAIQNPTlinkgSRSNASIQYQVPQIQGNSSQTIQVQPSlTNQIQVIPGTNQAITTPSTSGHKPVPIKPAPVQKSSTTTT 186
Cdd:COG5386   117 FEVPDLS-----KPLNAKVHVVIPAINYDHKYDVRLVFD-TNSIKPVGPVKEEPAPPPENTTDPEKLEDGTYTIDFKVLK 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 187 PVQSGANVVKLTGG-------GSNMTLTLPLNNLVNTSDIGGPAQLLTESPPTPLSKTNKKARKKSLPVSQPSVAvaeqv 259
Cdd:COG5386   191 DGTKEISMMDQTRTvefknpkPSDNVTSTAANSGSLQAKEGIKSQPTKSDSTSKPATTTKPKKKVVPIAVNSLKL----- 265

                         170       180
                  ....*....|....*....|
gi 1388876046 260 etVLIETTADNIIQAGNNLL 279
Cdd:COG5386   266 --GLKFSNTVNKKQILNKLT 283
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
443-581 4.16e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.06  E-value: 4.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 443 VPVTITNTGGQQQLTVQNVSGNNLTISgLSPTQIQLQMEQALAGEAQPGekrrrmactcPNCKDGEKRSGEQGKKKHvch 522
Cdd:COG5048   227 LPLTTNSQLSPKSLLSQSPSSLSSSDS-SSSASESPRSSLPTASSQSSS----------PNESDSSSEKGFSLPIKS--- 292

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388876046 523 iPDCGKTFRKTSLLRAHVR--LHTGE--RPFVCNWFFCGKRFTRSDELQRHARTHTGDKRFEC 581
Cdd:COG5048   293 -KQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKE 354
zf-C2H2_8 pfam15909
C2H2-type zinc ribbon; This family carries three zinc-fingers in tandem.
 521-597 8.00e-03

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


Pssm-ID: 464935 [Multi-domain]  Cd Length: 98  Bit Score: 36.24  E-value: 8.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876046 521 CHIPDCGKTFRKTSLLRAHVRLHTGE------RPFVCNWFFCGKRFTRSDELQRHARTHTGDKR-FECAQCQKRFMRSDH 593
Cdd:pfam15909   2 CSSPGCCLSFPSVRDLAQHLRTHCPPtqslegKLFRCSALSCTETFPSMQELVAHSKLHYKPNRyFKCENCLLRFRTHRS 81


                  ....
gi 1388876046 594 LTKH 597
Cdd:pfam15909  82 LFKH 85
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 549-573 8.29e-03

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


Pssm-ID: 464025  Cd Length: 24  Bit Score: 34.16  E-value: 8.29e-03
                          10        20
                  ....*....|....*....|....*
gi 1388876046 549 FVCNwfFCGKRFTRSDELQRHARTH 573
Cdd:pfam13894   1 FKCP--ICGKSFSSKKSLKRHLKTH 23
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 579-601 8.29e-03

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


Pssm-ID: 464025  Cd Length: 24  Bit Score: 34.16  E-value: 8.29e-03
                          10        20
                  ....*....|....*....|...
gi 1388876046 579 FECAQCQKRFMRSDHLTKHYKTH 601
Cdd:pfam13894   1 FKCPICGKSFSSKKSLKRHLKTH 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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