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Conserved domains on  [gi|1985358432|ref|XP_039387879|]
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Krueppel-like factor 11 isoform X1 [Mauremys reevesii]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KLF11_N cd21584
N-terminal domain of Kruppel-like factor 11; Kruppel-like factor 11 (KLF11; also known as ...
37-405 2.26e-118

N-terminal domain of Kruppel-like factor 11; Kruppel-like factor 11 (KLF11; also known as Krueppel-like factor 11; Fetal Kruppel-like factor-1/FKLF-1; maturity-onset diabetes of the young 7/MODY7; TGFbeta Inducible Early Growth Response 2/TIEG2) is a protein that in humans is encoded by the KLF11 gene. KLF11 is involved in cell growth, apoptosis, cellular inflammation and differentiation, endometriosis, and cholesterol, prostaglandin, neurotransmitter, fat, and sugar metabolism. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved a-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF11 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. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF11.


:

Pssm-ID: 409242 [Multi-domain]  Cd Length: 217  Bit Score: 347.75  E-value: 2.26e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985358432  37 LEQNDIEAVQALVCMSSWGQRSQKGDLLKIRPLTPISDSGDFTMHAEAASELPKDYHFLSTLCMTPPHSPDFVEPSTTml 116
Cdd:cd21584     1 LEQNDLEAVEALVCMSSWGQRSQKGDLLKIRPLTPASDSCDSLTLHPAAPELPKDFHSLSSLCMTPPHSPSFAEPSTT-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985358432 117 lssqvtyskprtvmantsvcvvtstncasaiakpsvlnmerqsswksvisepPAPQPCRAMATSVIRHTGDSSAythipa 196
Cdd:cd21584    79 ----------------------------------------------------APPPPCRAMATSVIRHTADSSP------ 100
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985358432 197 vqvktkvtsgncststdwceaqdrrhsrvsedmdtadglisdtspvhqpylhnsscnttnkgqqpirpvspwtclpkncd 276
Cdd:cd21584       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985358432 277 nypqkkatqllPTPVSTPQVICQMIPFNRQRGMISAFIKPPTQTvATTVQPILPQTAPVSQPVLMGSSVPQGTVMLVLPQ 356
Cdd:cd21584   101 -----------PVPVPSPPVLCQMIPVSGQSGMISAFLQPPALS-AGTVKPILPQTAPASQPLLVGSPVPQGTVMLVLPQ 168
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1985358432 357 TAVAQTPQCQQTVMTVGNTKLLPLAPAPVFIASGQSCAPQMDFSRRRNY 405
Cdd:cd21584   169 ASVPQPPQCPQTVMTLGNTKLLPLAPAPVFIPSGQSCAPQVDFSRRRNY 217
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
404-460 9.94e-05

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.07  E-value: 9.94e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1985358432 404 NYVCNFPGCRKTYFKSSHLKAHLRTHTGEKPFSCNWEGCDKKFARSDELSRHRRTHT 460
Cdd:COG5048    31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHH 87
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
465-487 4.09e-04

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


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 37.66  E-value: 4.09e-04
                          10        20
                  ....*....|....*....|...
gi 1985358432 465 FACPVCDRRFMRSDHLTKHARRH 487
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KLF11_N cd21584
N-terminal domain of Kruppel-like factor 11; Kruppel-like factor 11 (KLF11; also known as ...
37-405 2.26e-118

N-terminal domain of Kruppel-like factor 11; Kruppel-like factor 11 (KLF11; also known as Krueppel-like factor 11; Fetal Kruppel-like factor-1/FKLF-1; maturity-onset diabetes of the young 7/MODY7; TGFbeta Inducible Early Growth Response 2/TIEG2) is a protein that in humans is encoded by the KLF11 gene. KLF11 is involved in cell growth, apoptosis, cellular inflammation and differentiation, endometriosis, and cholesterol, prostaglandin, neurotransmitter, fat, and sugar metabolism. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved a-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF11 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. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF11.


Pssm-ID: 409242 [Multi-domain]  Cd Length: 217  Bit Score: 347.75  E-value: 2.26e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985358432  37 LEQNDIEAVQALVCMSSWGQRSQKGDLLKIRPLTPISDSGDFTMHAEAASELPKDYHFLSTLCMTPPHSPDFVEPSTTml 116
Cdd:cd21584     1 LEQNDLEAVEALVCMSSWGQRSQKGDLLKIRPLTPASDSCDSLTLHPAAPELPKDFHSLSSLCMTPPHSPSFAEPSTT-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985358432 117 lssqvtyskprtvmantsvcvvtstncasaiakpsvlnmerqsswksvisepPAPQPCRAMATSVIRHTGDSSAythipa 196
Cdd:cd21584    79 ----------------------------------------------------APPPPCRAMATSVIRHTADSSP------ 100
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985358432 197 vqvktkvtsgncststdwceaqdrrhsrvsedmdtadglisdtspvhqpylhnsscnttnkgqqpirpvspwtclpkncd 276
Cdd:cd21584       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985358432 277 nypqkkatqllPTPVSTPQVICQMIPFNRQRGMISAFIKPPTQTvATTVQPILPQTAPVSQPVLMGSSVPQGTVMLVLPQ 356
Cdd:cd21584   101 -----------PVPVPSPPVLCQMIPVSGQSGMISAFLQPPALS-AGTVKPILPQTAPASQPLLVGSPVPQGTVMLVLPQ 168
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1985358432 357 TAVAQTPQCQQTVMTVGNTKLLPLAPAPVFIASGQSCAPQMDFSRRRNY 405
Cdd:cd21584   169 ASVPQPPQCPQTVMTLGNTKLLPLAPAPVFIPSGQSCAPQVDFSRRRNY 217
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
404-460 9.94e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.07  E-value: 9.94e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1985358432 404 NYVCNFPGCRKTYFKSSHLKAHLRTHTGEKPFSCNWEGCDKKFARSDELSRHRRTHT 460
Cdd:COG5048    31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHH 87
zf-H2C2_2 pfam13465
Zinc-finger double domain;
421-448 1.46e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.46e-04
                          10        20
                  ....*....|....*....|....*...
gi 1985358432 421 HLKAHLRTHTGEKPFSCnwEGCDKKFAR 448
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKC--PECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
465-487 4.09e-04

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 37.66  E-value: 4.09e-04
                          10        20
                  ....*....|....*....|...
gi 1985358432 465 FACPVCDRRFMRSDHLTKHARRH 487
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KLF11_N cd21584
N-terminal domain of Kruppel-like factor 11; Kruppel-like factor 11 (KLF11; also known as ...
37-405 2.26e-118

N-terminal domain of Kruppel-like factor 11; Kruppel-like factor 11 (KLF11; also known as Krueppel-like factor 11; Fetal Kruppel-like factor-1/FKLF-1; maturity-onset diabetes of the young 7/MODY7; TGFbeta Inducible Early Growth Response 2/TIEG2) is a protein that in humans is encoded by the KLF11 gene. KLF11 is involved in cell growth, apoptosis, cellular inflammation and differentiation, endometriosis, and cholesterol, prostaglandin, neurotransmitter, fat, and sugar metabolism. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved a-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF11 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. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF11.


Pssm-ID: 409242 [Multi-domain]  Cd Length: 217  Bit Score: 347.75  E-value: 2.26e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985358432  37 LEQNDIEAVQALVCMSSWGQRSQKGDLLKIRPLTPISDSGDFTMHAEAASELPKDYHFLSTLCMTPPHSPDFVEPSTTml 116
Cdd:cd21584     1 LEQNDLEAVEALVCMSSWGQRSQKGDLLKIRPLTPASDSCDSLTLHPAAPELPKDFHSLSSLCMTPPHSPSFAEPSTT-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985358432 117 lssqvtyskprtvmantsvcvvtstncasaiakpsvlnmerqsswksvisepPAPQPCRAMATSVIRHTGDSSAythipa 196
Cdd:cd21584    79 ----------------------------------------------------APPPPCRAMATSVIRHTADSSP------ 100
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985358432 197 vqvktkvtsgncststdwceaqdrrhsrvsedmdtadglisdtspvhqpylhnsscnttnkgqqpirpvspwtclpkncd 276
Cdd:cd21584       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985358432 277 nypqkkatqllPTPVSTPQVICQMIPFNRQRGMISAFIKPPTQTvATTVQPILPQTAPVSQPVLMGSSVPQGTVMLVLPQ 356
Cdd:cd21584   101 -----------PVPVPSPPVLCQMIPVSGQSGMISAFLQPPALS-AGTVKPILPQTAPASQPLLVGSPVPQGTVMLVLPQ 168
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1985358432 357 TAVAQTPQCQQTVMTVGNTKLLPLAPAPVFIASGQSCAPQMDFSRRRNY 405
Cdd:cd21584   169 ASVPQPPQCPQTVMTLGNTKLLPLAPAPVFIPSGQSCAPQVDFSRRRNY 217
KLF10_11_N cd21974
N-terminal domain of Kruppel-like factor (KLF) 10, KLF11, and similar proteins; This subfamily ...
38-405 9.09e-89

N-terminal domain of Kruppel-like factor (KLF) 10, KLF11, and similar proteins; This subfamily is composed of Kruppel-like factor or Krueppel-like factor (KLF) 10, KLF11, and similar proteins. KLF10 was first identified in human osteoblasts and plays a role in mediating estrogen (E2) signaling in bone and skeletal homeostasis and a regulatory role in tumor formation and metastasis. KLF11 is involved in cell growth, apoptosis, cellular inflammation and differentiation, endometriosis, and cholesterol, prostaglandin, neurotransmitter, fat, and sugar metabolism. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved a-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF10/11 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. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF10, KLF11, and similar proteins.


Pssm-ID: 409243 [Multi-domain]  Cd Length: 229  Bit Score: 272.19  E-value: 9.09e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985358432  38 EQNDIEAVQALVCMSSWGQRSQKgDLLKIRPLTPISDSGDftmhAEAASELPKDYHFLSTLCMTPPHSPDFVEPSTTMLL 117
Cdd:cd21974     1 EQGDLEAVEALVSMSSWWKRRQK-RLRKPRPLTPSSDSSD----EDDAPESPKDFHSLSSLCMTPPYSPPFFEASHSPSV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985358432 118 SSQVTYSKPRTvmantsvcvvtstncasaiakpsvlnmerQSSWKSVISEPPAPQPCRAMATSVIRHTGDssaythipav 197
Cdd:cd21974    76 ASLHPPSAASS-----------------------------QPPPEPESSEPPAASPQRAQATSVIRHTAD---------- 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985358432 198 qvktkvtsgncststdwceaqdrrhsrvsedmdtadglisdtspvhqpylhnsscnttnkgqqpirpvspwtclpkncdn 277
Cdd:cd21974       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985358432 278 ypqkkatqllPTPVSTPQVICQMIPFNRQRGMISAFIKPPTQTVATTVQPILPQTapvsQPVLMGSSVPQGTVMLVLPQT 357
Cdd:cd21974   117 ----------PVPVSPPPVLCQMLPVSSSSGVIVAFLKAPQQPSPQPQKPALPQP----QVVLVGGQVPQGPVMLVVPQP 182
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1985358432 358 AVAQTPQcQQTVMTVGNTKLLPLAPAPVFIASGQSCAPQMDFSRRRNY 405
Cdd:cd21974   183 AVPQPYV-QPTVVTPGGTKLLPIAPAPGFIPSGQSSAPQPDFSRRRNH 229
KLF10_N cd21572
N-terminal domain of Kruppel-like factor 10; Kruppel-like factor 10 (KLF10; also known as ...
37-404 6.53e-27

N-terminal domain of Kruppel-like factor 10; Kruppel-like factor 10 (KLF10; also known as Krueppel-like factor 10; early growth response(EGR)-alpha/EGRA; TGFbeta inducible early gene-1/TIEG1) is a protein that in humans is encoded by the KLF10 gene. KLF10 was first identified in human osteoblasts and plays a role in mediating estrogen (E2) signaling in bone and skeletal homeostasis and a regulatory role in tumor formation and metastasis. It may also play a role in adipocyte differentiation and adipose tissue function. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved a-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF10 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. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF10.


Pssm-ID: 409241 [Multi-domain]  Cd Length: 245  Bit Score: 108.92  E-value: 6.53e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985358432  37 LEQNDIEAVQALVCMSS-WGQRSQKgdLLKIRPLTPISDSGDftmhaEAASELPKDYHFLSTLCMTPPHSPDFVEPS--T 113
Cdd:cd21572     1 MGAGDMEAVEALMSMTKhWKTRSFR--LRHFRPLTPSSDSSE-----DDDLPSPADFHDSPPFCMTPPYSPPHFEAThpP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985358432 114 TMLLSSQVTYSKPRTvmantsvcvvtstncasaiakpsvlnmerqsswKSVISEPPAPQPcRAMATSVIRHTGDSsayth 193
Cdd:cd21572    74 SAATLHPPAAQPPEE---------------------------------QHLSAETAASQQ-RFQCTSVIRHTADA----- 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985358432 194 ipavqvktkvtsgncststdwceaqdrrhsrvsedmdtadglisdtspvhqpylHNSSCNTTNKGQQPIRPVSPwtclpk 273
Cdd:cd21572   115 ------------------------------------------------------QPCSCSSCPSSPSVVPSVPA------ 134
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985358432 274 ncdnypqkkatqlLPTPVSTPQVICQMIPFnrqrgmisAFIKPPTQTVATTVQPILPQTAPVSQPVLMGSSVPQGTVMLV 353
Cdd:cd21572   135 -------------GVAGVSPVPVYCQILPV--------SSSSTTVVAAQAPLPQPQQQAASPAQVFLMGGQVPKGPVMFL 193
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1985358432 354 LPQTAVaQTPQCQQTVMTVGNTKLLPLAPAPVFIASGQ-SCAPQMDFSRRRN 404
Cdd:cd21572   194 VPQPVV-PTLYVQPTLVTPGGTKLAAIAPAPGHTPSEQrKSPPQPEVSRVRS 244
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
404-460 9.94e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.07  E-value: 9.94e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1985358432 404 NYVCNFPGCRKTYFKSSHLKAHLRTHTGEKPFSCNWEGCDKKFARSDELSRHRRTHT 460
Cdd:COG5048    31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHH 87
zf-H2C2_2 pfam13465
Zinc-finger double domain;
421-448 1.46e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.46e-04
                          10        20
                  ....*....|....*....|....*...
gi 1985358432 421 HLKAHLRTHTGEKPFSCnwEGCDKKFAR 448
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKC--PECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
465-487 4.09e-04

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 37.66  E-value: 4.09e-04
                          10        20
                  ....*....|....*....|...
gi 1985358432 465 FACPVCDRRFMRSDHLTKHARRH 487
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
431-489 1.01e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 41.63  E-value: 1.01e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1985358432 431 GEKPFSCNWEGCDKKFARSDELSRHR-------RTH------------TGEKKFACPVCDRRFMRSDHLTKHaRRHMT 489
Cdd:COG5189   346 DGKPYKCPVEGCNKKYKNQNGLKYHMlhghqnqKLHenpspekmnifsAKDKPYRCEVCDKRYKNLNGLKYH-RKHSH 422
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
435-459 3.54e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 3.54e-03
                          10        20
                  ....*....|....*....|....*
gi 1985358432 435 FSCNweGCDKKFARSDELSRHRRTH 459
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
zf-C2H2_8 pfam15909
C2H2-type zinc ribbon; This family carries three zinc-fingers in tandem.
407-483 6.00e-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: 6.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985358432 407 CNFPGCRKTYFKSSHLKAHLRTHTGE------KPFSCNWEGCDKKFARSDELSRHRRTHTGEKK-FACPVCDRRFMRSDH 479
Cdd:pfam15909   2 CSSPGCCLSFPSVRDLAQHLRTHCPPtqslegKLFRCSALSCTETFPSMQELVAHSKLHYKPNRyFKCENCLLRFRTHRS 81

                  ....
gi 1985358432 480 LTKH 483
Cdd:pfam15909  82 LFKH 85
 
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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