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Conserved domains on  [gi|2462536166|ref|XP_054230064|]
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Krueppel-like factor 12 isoform X6 [Homo sapiens]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 15347866)

Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KLF12_N cd21441
N-terminal domain of Kruppel-like factor 12; Kruppel-like factor 12 (also known as ...
 8-205 1.38e-98

N-terminal domain of Kruppel-like factor 12; Kruppel-like factor 12 (also known as Krueppel-like transcription factor 12, KLF12) regulates, by transcriptionally repressing Nur77 expression, endometrial decidualization, which is a prerequisite for successful implantation and the establishment of pregnancy. It is involved in the maturation processes of kidney collecting ducts after birth, and is able to increase the promoter activity of the UT-A1 urea transporter promoter by binding to the CACCC motif. KLF12 has also been found to promote colorectal cancer growth is also involved in the invasion and apoptosis of basal-like breast carcinoma. KLF12 belongs to a family of proteins called the Specificity Protein (SP)/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. Although these factors bind to similar elements in vitro, they have distinct activities in vivo depending on their expression profile and the sequence of the N-terminal activation/repression domain, which differ between members. KLF12 contains an N-terminal domain that is related to the N-terminal repression domain of KLF8.


:

Pssm-ID: 410608 [Multi-domain]  Cd Length: 197  Bit Score: 291.14  E-value: 1.38e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536166   8 PAVRVKTELLESEQGSPNVHNYPDMEAVPLLLNNVKGEPPEDSLSVDHFQTQTEPVDLSINKARTSPTAVSSSPVSMTAS 87
Cdd:cd21441     1 PAVRVKTELLESEQGSPNVHNYPDMEAVPLLLNNVKAEPPEDSLSTDHFQTQTEPVDLSINKARTSPTAVSSSPVSMTAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536166  88 ASSPSSTSTSSSSSSRLASsPTVITSVSSASSSSTVLTPGPLVASASGVGGQQFLHIIHPVPPSSPMNLQSNKLSHVHRI 167
Cdd:cd21441    81 ASPSSSSSSSSSSSRPASS-PTVITSVSSASSVPTVLTPGPLVASASGVGGQQFLHIIHPVPPSSPMNLQSNKLSHVHRI 159

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462536166 168 PVVVQSVPVVYTAVRSPGNVNNTIVVPLLEDGRGHGKA 205
Cdd:cd21441   160 PVVVQSVPVVYTAVRSPGNVNNTIVVPLLEDGRSHGKA 197
zf-H2C2_2 pfam13465
Zinc-finger double domain;
344-369 7.97e-06

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.97  E-value: 7.97e-06
                          10        20
                  ....*....|....*....|....*.
gi 2462536166 344 ELTRHYRKHTGVKPFKCADCDRSFSR 369
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
209-382 7.89e-05

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.69  E-value: 7.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536166 209 PRGLSPRQSKSDSDDDDLPNVTLDSVNETGSTALSIARAVQEVHPSPVSRVRGNRMNNQkfpCSISPFSIESTRRQRRSE 288
Cdd:COG5048   236 SPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGFSLPIKSKQ---CNISFSRSSPLTRHLRSV 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536166 289 SPDSRKRRIHRCDFEGCNKVYTKSSHLKAHRRTHTGEKPYKCTWEGCTWKF-----ARSDELTRHYRKHTGVKPFKCAD- 362
Cdd:COG5048   313 NHSGESLKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFspllnNEPPQSLQQYKDLKNDKKSETLSn 392

                         170       180
                  ....*....|....*....|.
gi 2462536166 363 -CDRSFSRSDHLALHRRRHML 382
Cdd:COG5048   393 sCIRNFKRDSNLSLHIITHLS 413
 
Name Accession Description Interval E-value
KLF12_N cd21441
N-terminal domain of Kruppel-like factor 12; Kruppel-like factor 12 (also known as ...
 8-205 1.38e-98

N-terminal domain of Kruppel-like factor 12; Kruppel-like factor 12 (also known as Krueppel-like transcription factor 12, KLF12) regulates, by transcriptionally repressing Nur77 expression, endometrial decidualization, which is a prerequisite for successful implantation and the establishment of pregnancy. It is involved in the maturation processes of kidney collecting ducts after birth, and is able to increase the promoter activity of the UT-A1 urea transporter promoter by binding to the CACCC motif. KLF12 has also been found to promote colorectal cancer growth is also involved in the invasion and apoptosis of basal-like breast carcinoma. KLF12 belongs to a family of proteins called the Specificity Protein (SP)/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. Although these factors bind to similar elements in vitro, they have distinct activities in vivo depending on their expression profile and the sequence of the N-terminal activation/repression domain, which differ between members. KLF12 contains an N-terminal domain that is related to the N-terminal repression domain of KLF8.


Pssm-ID: 410608 [Multi-domain]  Cd Length: 197  Bit Score: 291.14  E-value: 1.38e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536166   8 PAVRVKTELLESEQGSPNVHNYPDMEAVPLLLNNVKGEPPEDSLSVDHFQTQTEPVDLSINKARTSPTAVSSSPVSMTAS 87
Cdd:cd21441     1 PAVRVKTELLESEQGSPNVHNYPDMEAVPLLLNNVKAEPPEDSLSTDHFQTQTEPVDLSINKARTSPTAVSSSPVSMTAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536166  88 ASSPSSTSTSSSSSSRLASsPTVITSVSSASSSSTVLTPGPLVASASGVGGQQFLHIIHPVPPSSPMNLQSNKLSHVHRI 167
Cdd:cd21441    81 ASPSSSSSSSSSSSRPASS-PTVITSVSSASSVPTVLTPGPLVASASGVGGQQFLHIIHPVPPSSPMNLQSNKLSHVHRI 159

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462536166 168 PVVVQSVPVVYTAVRSPGNVNNTIVVPLLEDGRGHGKA 205
Cdd:cd21441   160 PVVVQSVPVVYTAVRSPGNVNNTIVVPLLEDGRSHGKA 197
zf-H2C2_2 pfam13465
Zinc-finger double domain;
344-369 7.97e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.97  E-value: 7.97e-06
                          10        20
                  ....*....|....*....|....*.
gi 2462536166 344 ELTRHYRKHTGVKPFKCADCDRSFSR 369
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
209-382 7.89e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.69  E-value: 7.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536166 209 PRGLSPRQSKSDSDDDDLPNVTLDSVNETGSTALSIARAVQEVHPSPVSRVRGNRMNNQkfpCSISPFSIESTRRQRRSE 288
Cdd:COG5048   236 SPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGFSLPIKSKQ---CNISFSRSSPLTRHLRSV 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536166 289 SPDSRKRRIHRCDFEGCNKVYTKSSHLKAHRRTHTGEKPYKCTWEGCTWKF-----ARSDELTRHYRKHTGVKPFKCAD- 362
Cdd:COG5048   313 NHSGESLKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFspllnNEPPQSLQQYKDLKNDKKSETLSn 392

                         170       180
                  ....*....|....*....|.
gi 2462536166 363 -CDRSFSRSDHLALHRRRHML 382
Cdd:COG5048   393 sCIRNFKRDSNLSLHIITHLS 413
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 298-322 5.15e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.20  E-value: 5.15e-03
                          10        20
                  ....*....|....*....|....*
gi 2462536166 298 HRCdfEGCNKVYTKSSHLKAHRRTH 322
Cdd:pfam00096   1 YKC--PDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KLF12_N cd21441
N-terminal domain of Kruppel-like factor 12; Kruppel-like factor 12 (also known as ...
 8-205 1.38e-98

N-terminal domain of Kruppel-like factor 12; Kruppel-like factor 12 (also known as Krueppel-like transcription factor 12, KLF12) regulates, by transcriptionally repressing Nur77 expression, endometrial decidualization, which is a prerequisite for successful implantation and the establishment of pregnancy. It is involved in the maturation processes of kidney collecting ducts after birth, and is able to increase the promoter activity of the UT-A1 urea transporter promoter by binding to the CACCC motif. KLF12 has also been found to promote colorectal cancer growth is also involved in the invasion and apoptosis of basal-like breast carcinoma. KLF12 belongs to a family of proteins called the Specificity Protein (SP)/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. Although these factors bind to similar elements in vitro, they have distinct activities in vivo depending on their expression profile and the sequence of the N-terminal activation/repression domain, which differ between members. KLF12 contains an N-terminal domain that is related to the N-terminal repression domain of KLF8.


Pssm-ID: 410608 [Multi-domain]  Cd Length: 197  Bit Score: 291.14  E-value: 1.38e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536166   8 PAVRVKTELLESEQGSPNVHNYPDMEAVPLLLNNVKGEPPEDSLSVDHFQTQTEPVDLSINKARTSPTAVSSSPVSMTAS 87
Cdd:cd21441     1 PAVRVKTELLESEQGSPNVHNYPDMEAVPLLLNNVKAEPPEDSLSTDHFQTQTEPVDLSINKARTSPTAVSSSPVSMTAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536166  88 ASSPSSTSTSSSSSSRLASsPTVITSVSSASSSSTVLTPGPLVASASGVGGQQFLHIIHPVPPSSPMNLQSNKLSHVHRI 167
Cdd:cd21441    81 ASPSSSSSSSSSSSRPASS-PTVITSVSSASSVPTVLTPGPLVASASGVGGQQFLHIIHPVPPSSPMNLQSNKLSHVHRI 159

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462536166 168 PVVVQSVPVVYTAVRSPGNVNNTIVVPLLEDGRGHGKA 205
Cdd:cd21441   160 PVVVQSVPVVYTAVRSPGNVNNTIVVPLLEDGRSHGKA 197
KLF8_12_N cd21093
N-terminal domain of Kruppel-like factor (KLF) 8, KLF12, and similar proteins; Kruppel-like ...
 23-205 2.85e-65

N-terminal domain of Kruppel-like factor (KLF) 8, KLF12, and similar proteins; Kruppel-like transcription factors (also known as Krueppel-like transcription factors, KLFs) belong to a family of proteins called the Specificity Protein (SP)/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. Although these factors bind to similar elements in vitro, they have distinct activities in vivo depending on their expression profile and the sequence of the N-terminal activation/repression domain, which differ between members. This model represents the related N-terminal activation/repression domains of KLF8 and KLF12.


Pssm-ID: 410606 [Multi-domain]  Cd Length: 172  Bit Score: 205.40  E-value: 2.85e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536166  23 SPNVHNYPDMEaVPLLLNNVKGEPPEDSLSVDHFQTQTEPVDLSINKARTSPTAVSSSPVsmtasaSSPSSTSTSSSSSS 102
Cdd:cd21093     1 SPNLLNYPDME-VPLLLNNIKTEPPEELLSSDHSQPQTEPVDLSINKARTSPTAVSSSPV------SMSSSISSSSSSSP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536166 103 RLASSPTVITSVSSASSSSTVLTPGPLVASASGVGGQQFLHIIHPVPPSSpmnlQSNKLSHVHRIPVVVQSVPVVYTAVR 182
Cdd:cd21093    74 RPASSPTVITSVSSASAIPTVLSPGSILASAQGVGGQQILHVIHTVPSVS----LPNKMSHLHTIPVVVQSLPVVYTAVR 149

                         170       180
                  ....*....|....*....|....
gi 2462536166 183 SPGNVnNTIVVPLLE-DGRGHGKA 205
Cdd:cd21093   150 SDGNT-ATITVPLIGgDGKSHGKV 172
KLF8_N cd21440
N-terminal domain of Kruppel-like factor 8; Kruppel-like factor 8 (also known as Krueppel-like ...
 36-203 3.07e-20

N-terminal domain of Kruppel-like factor 8; Kruppel-like factor 8 (also known as Krueppel-like transcription factor 8, KLF8) is a CACCC-box binding protein that associates with C-terminal Binding Protein (CtBP) and represses transcription. It plays an essential role in the regulation of the cell cycle, apoptosis, and differentiation. It has been identified as a key component of the transcription factor network that controls terminal differentiation during adipogenesis. It also plays an important role in the formation of several human tumors, including the promotion of tumorigenesis, invasion, and metastasis of colorectal cancer cells, and the progression of pancreatic cancer. KLF8 belongs to a family of proteins called the Specificity Protein (SP)/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. Although these factors bind to similar elements in vitro, they have distinct activities in vivo depending on their expression profile and the sequence of the N-terminal activation/repression domain, which differ between members. KLF8 contains an N-terminal repression domain that is related to that of KLF12.


Pssm-ID: 410607 [Multi-domain]  Cd Length: 169  Bit Score: 86.82  E-value: 3.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536166  36 PLLLNNVKGEPPEDSLSVDHFQTQTEPVDLSINKARTSPTAVSSSPVSMTASASSPSSTSTSSSSSSRLASSPTVItsvs 115
Cdd:cd21440    13 PALLSDIKTEPPEELLASDCSQPQAEPVDLSLHKPKAPLQPPSVLSPSPMILSVSPSAPQSLVSSTGTGMGTTSAI---- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536166 116 sasssSTVLTPGPLVASASGVGGQQFLHIIHPVPpssPMNLQSnKLSHVHRIPVVVQSVPVVYTAVRSPGnVNNTIVVPL 195
Cdd:cd21440    89 -----PAVLSPGSILASSQGSGGQQILHVIHTIP---SVNLPS-KMGNLQTIPVVVQSLPVVYTTLPTDG-VTAAITVPL 158


                  ....*....
gi 2462536166 196 L-EDGRGHG 203
Cdd:cd21440   159 IgGDGKNAG 167
zf-H2C2_2 pfam13465
Zinc-finger double domain;
344-369 7.97e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.97  E-value: 7.97e-06
                          10        20
                  ....*....|....*....|....*.
gi 2462536166 344 ELTRHYRKHTGVKPFKCADCDRSFSR 369
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
209-382 7.89e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.69  E-value: 7.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536166 209 PRGLSPRQSKSDSDDDDLPNVTLDSVNETGSTALSIARAVQEVHPSPVSRVRGNRMNNQkfpCSISPFSIESTRRQRRSE 288
Cdd:COG5048   236 SPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGFSLPIKSKQ---CNISFSRSSPLTRHLRSV 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536166 289 SPDSRKRRIHRCDFEGCNKVYTKSSHLKAHRRTHTGEKPYKCTWEGCTWKF-----ARSDELTRHYRKHTGVKPFKCAD- 362
Cdd:COG5048   313 NHSGESLKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFspllnNEPPQSLQQYKDLKNDKKSETLSn 392

                         170       180
                  ....*....|....*....|.
gi 2462536166 363 -CDRSFSRSDHLALHRRRHML 382
Cdd:COG5048   393 sCIRNFKRDSNLSLHIITHLS 413
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 358-380 8.38e-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: 39.21  E-value: 8.38e-05
                          10        20
                  ....*....|....*....|...
gi 2462536166 358 FKCADCDRSFSRSDHLALHRRRH 380
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 239-377 1.57e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.47  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536166 239 STALSIARAVQEVHPSPVSR------VRGNRMNNQKFPCSISPFSIESTR-RQRRSESPDSRKR----RIHRCDFEGCNK 307
Cdd:COG5189   280 FEESSLGFDYEFIHKSVGNKeirggiSTGEMIDVRKLPCTNSSSNGKLAHgGERNIDTPSRMLKvkdgKPYKCPVEGCNK 359

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462536166 308 VYTKSSHLKAHRRT-HTGEKPYKCTWEGCTWKFARSDeltrhyrkhtgvKPFKCADCDRSFSRSDHLALHR 377
Cdd:COG5189   360 KYKNQNGLKYHMLHgHQNQKLHENPSPEKMNIFSAKD------------KPYRCEVCDKRYKNLNGLKYHR 418
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 298-322 5.15e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.20  E-value: 5.15e-03
                          10        20
                  ....*....|....*....|....*
gi 2462536166 298 HRCdfEGCNKVYTKSSHLKAHRRTH 322
Cdd:pfam00096   1 YKC--PDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
314-331 8.53e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.50  E-value: 8.53e-03
                          10
                  ....*....|....*...
gi 2462536166 314 HLKAHRRTHTGEKPYKCT 331
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCP 18
 
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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