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Conserved domains on  [gi|564347826|ref|XP_006236946|]
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Krueppel-like factor 15 isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KLF15_N cd21580
N-terminal domain of Kruppel-like factor 15; Kruppel-like factor 15 (KLF15; also known as ...
 3-320 3.61e-85

N-terminal domain of Kruppel-like factor 15; Kruppel-like factor 15 (KLF15; also known as Krueppel-like factor 15 or kidney-enriched Kruppel-like factor/KKLF) is a protein that in humans is encoded by the KLF15 gene. KLF15 plays a role in gluconeogenesis, adipogenesis, and may be a potential therapeutic target to reduce hepatitis B virus gene expression and viral replication, heart failure and aortic aneurysm formation, and endometrial, breast cancer, and other diseases related to estrogen. It 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 KLF15.


:

Pssm-ID: 410206  Cd Length: 213  Bit Score: 258.85  E-value: 3.61e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347826   3 DHLLPVDETFSSPKCPVGYLGDRLASRQPYHMLPSPISED-DSDVSSPCSCASPDSQAFCSCYsagpgpeaqgsildfll 81
Cdd:cd21580    1 DHLLPVEETFLPYTCSVGYLSDMVSDRRSYQMLPSPLSEDlDSDSSSPRSCSSPDSQVLSSSL----------------- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347826  82 sratlgsggasggvgdgsgpvtwgswrrasvpvKEEHLCFPEFLSGDPDDVSRPFQPTLEEIEEFLEENMEAEVKEApes 161
Cdd:cd21580   64 ---------------------------------KEECFEFPVFLDDMEDPAAGPFQPTLEEIEEFLEENMEVVLKKG--- 107

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347826 162 ssrdleacsqlsagshrshlhpesggrecrtpppggtsgggtqgagegsahdgpMPVLLQIQPVAVKQEAGAGPASPGQA 241
Cdd:cd21580  108 ------------------------------------------------------VPVILQIQPVQVKQEPGTSPVSPPQA 133

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347826 242 PESVKVAQLLVNIQGQTFALLPQVVPSSNLNLSSKFVRIAPVPIAAKPIGSGSLGPGPAGLLV-GQKFPKNPAAELLKMH 320
Cdd:cd21580  134 PSDIKIAQLLVNIQGQTFALVPQVVQSANLSLSSKFVRIAPVPIAAKPVGLGEGGGGQSGGLVgGQKFQKSPVADLIKMH 213
zf-H2C2_2 pfam13465
Zinc-finger double domain;
366-391 2.69e-06

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.51  E-value: 2.69e-06
                          10        20
                  ....*....|....*....|....*.
gi 564347826  366 ELSRHRRSHSGVKPYQCPVCEKKFAR 391
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 super family cl25788
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 318-400 7.85e-06

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


The actual alignment was detected with superfamily member COG5189:

Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 47.79  E-value: 7.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347826 318 KMHKCTFPGCSKMYTKSSHLKAH-LRRHTGEKPFACTWPGCGWRFSRSDelsrhrrshsgvKPYQCPVCEKKFARSDHLS 396
Cdd:COG5189  348 KPYKCPVEGCNKKYKNQNGLKYHmLHGHQNQKLHENPSPEKMNIFSAKD------------KPYRCEVCDKRYKNLNGLK 415


                 ....
gi 564347826 397 KHIK 400
Cdd:COG5189  416 YHRK 419
 
Name Accession Description Interval E-value
KLF15_N cd21580
N-terminal domain of Kruppel-like factor 15; Kruppel-like factor 15 (KLF15; also known as ...
 3-320 3.61e-85

N-terminal domain of Kruppel-like factor 15; Kruppel-like factor 15 (KLF15; also known as Krueppel-like factor 15 or kidney-enriched Kruppel-like factor/KKLF) is a protein that in humans is encoded by the KLF15 gene. KLF15 plays a role in gluconeogenesis, adipogenesis, and may be a potential therapeutic target to reduce hepatitis B virus gene expression and viral replication, heart failure and aortic aneurysm formation, and endometrial, breast cancer, and other diseases related to estrogen. It 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 KLF15.


Pssm-ID: 410206  Cd Length: 213  Bit Score: 258.85  E-value: 3.61e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347826   3 DHLLPVDETFSSPKCPVGYLGDRLASRQPYHMLPSPISED-DSDVSSPCSCASPDSQAFCSCYsagpgpeaqgsildfll 81
Cdd:cd21580    1 DHLLPVEETFLPYTCSVGYLSDMVSDRRSYQMLPSPLSEDlDSDSSSPRSCSSPDSQVLSSSL----------------- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347826  82 sratlgsggasggvgdgsgpvtwgswrrasvpvKEEHLCFPEFLSGDPDDVSRPFQPTLEEIEEFLEENMEAEVKEApes 161
Cdd:cd21580   64 ---------------------------------KEECFEFPVFLDDMEDPAAGPFQPTLEEIEEFLEENMEVVLKKG--- 107

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347826 162 ssrdleacsqlsagshrshlhpesggrecrtpppggtsgggtqgagegsahdgpMPVLLQIQPVAVKQEAGAGPASPGQA 241
Cdd:cd21580  108 ------------------------------------------------------VPVILQIQPVQVKQEPGTSPVSPPQA 133

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347826 242 PESVKVAQLLVNIQGQTFALLPQVVPSSNLNLSSKFVRIAPVPIAAKPIGSGSLGPGPAGLLV-GQKFPKNPAAELLKMH 320
Cdd:cd21580  134 PSDIKIAQLLVNIQGQTFALVPQVVQSANLSLSSKFVRIAPVPIAAKPVGLGEGGGGQSGGLVgGQKFQKSPVADLIKMH 213
zf-H2C2_2 pfam13465
Zinc-finger double domain;
366-391 2.69e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.51  E-value: 2.69e-06
                          10        20
                  ....*....|....*....|....*.
gi 564347826  366 ELSRHRRSHSGVKPYQCPVCEKKFAR 391
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 318-400 7.85e-06

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 47.79  E-value: 7.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347826 318 KMHKCTFPGCSKMYTKSSHLKAH-LRRHTGEKPFACTWPGCGWRFSRSDelsrhrrshsgvKPYQCPVCEKKFARSDHLS 396
Cdd:COG5189  348 KPYKCPVEGCNKKYKNQNGLKYHmLHGHQNQKLHENPSPEKMNIFSAKD------------KPYRCEVCDKRYKNLNGLK 415


                 ....
gi 564347826 397 KHIK 400
Cdd:COG5189  416 YHRK 419
ZnF_C2H2 smart00355
zinc finger;
380-402 1.59e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.52  E-value: 1.59e-03
                           10        20
                   ....*....|....*....|...
gi 564347826   380 YQCPVCEKKFARSDHLSKHIKVH 402
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
336-363 2.95e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 2.95e-03
                          10        20
                  ....*....|....*....|....*...
gi 564347826  336 HLKAHLRRHTGEKPFACtwPGCGWRFSR 363
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKC--PECGKSFKS 26
 
Name Accession Description Interval E-value
KLF15_N cd21580
N-terminal domain of Kruppel-like factor 15; Kruppel-like factor 15 (KLF15; also known as ...
 3-320 3.61e-85

N-terminal domain of Kruppel-like factor 15; Kruppel-like factor 15 (KLF15; also known as Krueppel-like factor 15 or kidney-enriched Kruppel-like factor/KKLF) is a protein that in humans is encoded by the KLF15 gene. KLF15 plays a role in gluconeogenesis, adipogenesis, and may be a potential therapeutic target to reduce hepatitis B virus gene expression and viral replication, heart failure and aortic aneurysm formation, and endometrial, breast cancer, and other diseases related to estrogen. It 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 KLF15.


Pssm-ID: 410206  Cd Length: 213  Bit Score: 258.85  E-value: 3.61e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347826   3 DHLLPVDETFSSPKCPVGYLGDRLASRQPYHMLPSPISED-DSDVSSPCSCASPDSQAFCSCYsagpgpeaqgsildfll 81
Cdd:cd21580    1 DHLLPVEETFLPYTCSVGYLSDMVSDRRSYQMLPSPLSEDlDSDSSSPRSCSSPDSQVLSSSL----------------- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347826  82 sratlgsggasggvgdgsgpvtwgswrrasvpvKEEHLCFPEFLSGDPDDVSRPFQPTLEEIEEFLEENMEAEVKEApes 161
Cdd:cd21580   64 ---------------------------------KEECFEFPVFLDDMEDPAAGPFQPTLEEIEEFLEENMEVVLKKG--- 107

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347826 162 ssrdleacsqlsagshrshlhpesggrecrtpppggtsgggtqgagegsahdgpMPVLLQIQPVAVKQEAGAGPASPGQA 241
Cdd:cd21580  108 ------------------------------------------------------VPVILQIQPVQVKQEPGTSPVSPPQA 133

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347826 242 PESVKVAQLLVNIQGQTFALLPQVVPSSNLNLSSKFVRIAPVPIAAKPIGSGSLGPGPAGLLV-GQKFPKNPAAELLKMH 320
Cdd:cd21580  134 PSDIKIAQLLVNIQGQTFALVPQVVQSANLSLSSKFVRIAPVPIAAKPVGLGEGGGGQSGGLVgGQKFQKSPVADLIKMH 213
zf-H2C2_2 pfam13465
Zinc-finger double domain;
366-391 2.69e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.51  E-value: 2.69e-06
                          10        20
                  ....*....|....*....|....*.
gi 564347826  366 ELSRHRRSHSGVKPYQCPVCEKKFAR 391
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 318-400 7.85e-06

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 47.79  E-value: 7.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347826 318 KMHKCTFPGCSKMYTKSSHLKAH-LRRHTGEKPFACTWPGCGWRFSRSDelsrhrrshsgvKPYQCPVCEKKFARSDHLS 396
Cdd:COG5189  348 KPYKCPVEGCNKKYKNQNGLKYHmLHGHQNQKLHENPSPEKMNIFSAKD------------KPYRCEVCDKRYKNLNGLK 415


                 ....
gi 564347826 397 KHIK 400
Cdd:COG5189  416 YHRK 419
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 380-402 4.22e-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: 4.22e-05
                          10        20
                  ....*....|....*....|...
gi 564347826  380 YQCPVCEKKFARSDHLSKHIKVH 402
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
325-375 2.20e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.15  E-value: 2.20e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564347826 325 PGCSKMYTKSSHLKAHLRRHTGEKPFACTWPGCGWRFSRSDELSRHRRSHS 375
Cdd:COG5048   37 PNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHH 87
ZnF_C2H2 smart00355
zinc finger;
380-402 1.59e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.52  E-value: 1.59e-03
                           10        20
                   ....*....|....*....|...
gi 564347826   380 YQCPVCEKKFARSDHLSKHIKVH 402
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
322-401 1.94e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.45  E-value: 1.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347826 322 CTFPGCSKMYTKSSHLKAHLRRHTGEKPFACTWPGCGWRFSRSDELSRHRRSHSgVKPYQCPVCEKKFARSDHLSKHIKV 401
Cdd:COG5048  389 TLSNSCIRNFKRDSNLSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLSNHGKD 467
zf-H2C2_2 pfam13465
Zinc-finger double domain;
336-363 2.95e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 2.95e-03
                          10        20
                  ....*....|....*....|....*...
gi 564347826  336 HLKAHLRRHTGEKPFACtwPGCGWRFSR 363
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 ...
 350-374 7.04e-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: 33.81  E-value: 7.04e-03
                          10        20
                  ....*....|....*....|....*
gi 564347826  350 FACtwPGCGWRFSRSDELSRHRRSH 374
Cdd:pfam00096   1 YKC--PDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
327-383 7.04e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 38.52  E-value: 7.04e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564347826 327 CSKMYTKSSHLKAHLR--RHTGE--KPFACTWPGCGWRFSRSDELSRHRRSHSGVKPYQCP 383
Cdd:COG5048  295 CNISFSRSSPLTRHLRsvNHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEK 355
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 380-402 8.56e-03

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


Pssm-ID: 464025  Cd Length: 24  Bit Score: 33.77  E-value: 8.56e-03
                          10        20
                  ....*....|....*....|...
gi 564347826  380 YQCPVCEKKFARSDHLSKHIKVH 402
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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