N-terminal domain of Kruppel-like factor 4; Kruppel-like factor 4 (KLF4; also known as Krueppel-like factor 4 or gut-enriched Kruppel-like factor/GKLF) is a protein that, in humans, is encoded by the KLF4 gene. Evidence also suggests that KLF4 is a tumor suppressor in certain cancers, including colorectal cancer, gastric cancer, esophageal squamous cell carcinoma, intestinal cancer, prostate cancer, bladder cancer and lung cancer. It may act as a tumor promoter where increased KLF4 expression has been reported, such as in oral squamous cell carcinoma and in primary breast ductal carcinoma. KLF4 is one of four key factors that are essential for inducing pluripotent stem cells. KLF4 is highly expressed in non-dividing cells and its overexpression induces cell cycle arrest. KLF proteins KLF1, KLF2, KLF4, KLF5, KLF6, and KLF7 are transcriptional activators. KLF4 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 KLF4, which is related to the N-terminal domains of KLF1 and KLF2.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916941934   7 DFDMALSGTLLPSISTFASGTPVKGKSTGLGMASSRWKEELSNLKRPCVPTGGGCPDHDLLAGIAKKEPDDADLLDYDFI 86
Cdd:cd21582     1 EFDMALSGTLLPSISTFASGPAVKEKALGQGSANNRWREELSHLKRPCPPLGGRCYDQDPPLGMRRKEEEFNDLLDYDFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916941934  87 LSNTMLQQQQQQQDAMAGSSRNLPPSPGSYSYQLPSPQDSAGDILYTIP-----DINDVSPSGGFVAELMRPELDPAYLQ 161
Cdd:cd21582    81 LSNSLLQQQQQQQQAASTSSSTSSSSSSPYSYQLPSPQGTATSFLYPIPranlaDINDVSPSGGFVAELMRPDLDPAYLQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916941934 162 PTSLQGKFVVKTTMDMADYSQGINVSKN------STVLESSLPFVCQRIKQENPSTCTITRPMDVHLGINSRPGSSQRPL 235
Cdd:cd21582   161 PTSLHGKFVVKTTMDMGDYSQSINVSKSapmtksSVAPSSSLPFMCPRIKQENPSTCTISRPMDGHLGGNSQHGFSQRAP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916941934 236 LNPHGYPSGRPGAASRPSASlspgDVLNRDHHPSSQVLSHPPLPLPQGYHTSAGYAPYSQPPSLQYQGQsylsvfeepvh 315
Cdd:cd21582   241 LPSRTTPSGGPGGGNSSTAE----SLMSRDHHPSSQVLSHPPLPLPQGYHPSPGYPPFPPPPSQPQQYQ----------- 305

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1916941934 316 ippllpeamltppssplELMSPVDCLPEEPKPKRGRRSWPRKRIATH 362
Cdd:cd21582   306 -----------------ELMSPGSCLPEEPKPKRGRRSWPRKRTATH 335

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.

                          10        20
                  ....*....|....*....|....*
gi 1916941934 362 HTCDYagCGKTYTKSSHLKAHHRTH 386
Cdd:pfam00096   1 YKCPD--CGKSFSRKSNLKRHLRTH 23

N-terminal domain of Kruppel-like factor 4; Kruppel-like factor 4 (KLF4; also known as Krueppel-like factor 4 or gut-enriched Kruppel-like factor/GKLF) is a protein that, in humans, is encoded by the KLF4 gene. Evidence also suggests that KLF4 is a tumor suppressor in certain cancers, including colorectal cancer, gastric cancer, esophageal squamous cell carcinoma, intestinal cancer, prostate cancer, bladder cancer and lung cancer. It may act as a tumor promoter where increased KLF4 expression has been reported, such as in oral squamous cell carcinoma and in primary breast ductal carcinoma. KLF4 is one of four key factors that are essential for inducing pluripotent stem cells. KLF4 is highly expressed in non-dividing cells and its overexpression induces cell cycle arrest. KLF proteins KLF1, KLF2, KLF4, KLF5, KLF6, and KLF7 are transcriptional activators. KLF4 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 KLF4, which is related to the N-terminal domains of KLF1 and KLF2.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916941934   7 DFDMALSGTLLPSISTFASGTPVKGKSTGLGMASSRWKEELSNLKRPCVPTGGGCPDHDLLAGIAKKEPDDADLLDYDFI 86
Cdd:cd21582     1 EFDMALSGTLLPSISTFASGPAVKEKALGQGSANNRWREELSHLKRPCPPLGGRCYDQDPPLGMRRKEEEFNDLLDYDFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916941934  87 LSNTMLQQQQQQQDAMAGSSRNLPPSPGSYSYQLPSPQDSAGDILYTIP-----DINDVSPSGGFVAELMRPELDPAYLQ 161
Cdd:cd21582    81 LSNSLLQQQQQQQQAASTSSSTSSSSSSPYSYQLPSPQGTATSFLYPIPranlaDINDVSPSGGFVAELMRPDLDPAYLQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916941934 162 PTSLQGKFVVKTTMDMADYSQGINVSKN------STVLESSLPFVCQRIKQENPSTCTITRPMDVHLGINSRPGSSQRPL 235
Cdd:cd21582   161 PTSLHGKFVVKTTMDMGDYSQSINVSKSapmtksSVAPSSSLPFMCPRIKQENPSTCTISRPMDGHLGGNSQHGFSQRAP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916941934 236 LNPHGYPSGRPGAASRPSASlspgDVLNRDHHPSSQVLSHPPLPLPQGYHTSAGYAPYSQPPSLQYQGQsylsvfeepvh 315
Cdd:cd21582   241 LPSRTTPSGGPGGGNSSTAE----SLMSRDHHPSSQVLSHPPLPLPQGYHPSPGYPPFPPPPSQPQQYQ----------- 305

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1916941934 316 ippllpeamltppssplELMSPVDCLPEEPKPKRGRRSWPRKRIATH 362
Cdd:cd21582   306 -----------------ELMSPGSCLPEEPKPKRGRRSWPRKRTATH 335

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.

                          10        20
                  ....*....|....*....|....*
gi 1916941934 362 HTCDYagCGKTYTKSSHLKAHHRTH 386
Cdd:pfam00096   1 YKCPD--CGKSFSRKSNLKRHLRTH 23

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916941934 279 PLPQGYHTSAGYAPYSQPPSLQYQGQSYLSvfeepvHIPPLLPEAMLTPPSSPLELMSPVDCLPEEPKPKRGRRSwPRKR 358
Cdd:COG5048   308 HLRSVNHSGESLKPFSCPYSLCGKLFSRND------ALKRHILLHTSISPAKEKLLNSSSKFSPLLNNEPPQSLQ-QYKD 380

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916941934 359 I---ATHTCDYAGCGKTYTKSSHLKAHHRTHTGEKPYHCDWEGCGWKFARSDELTRHYRKHTGHRPFQCQKCdRAFSRSD 435
Cdd:COG5048   381 LkndKKSETLSNSCIRNFKRDSNLSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSIL-KSFRRDL 459

                  ....*
gi 1916941934 436 HLALH 440
Cdd:COG5048   460 DLSNH 464

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*...
gi 1916941934 378 HLKAHHRTHTGEKPYHCDweGCGWKFAR 405
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCP--ECGKSFKS 26

N-terminal domain of Kruppel-like factor 4; Kruppel-like factor 4 (KLF4; also known as Krueppel-like factor 4 or gut-enriched Kruppel-like factor/GKLF) is a protein that, in humans, is encoded by the KLF4 gene. Evidence also suggests that KLF4 is a tumor suppressor in certain cancers, including colorectal cancer, gastric cancer, esophageal squamous cell carcinoma, intestinal cancer, prostate cancer, bladder cancer and lung cancer. It may act as a tumor promoter where increased KLF4 expression has been reported, such as in oral squamous cell carcinoma and in primary breast ductal carcinoma. KLF4 is one of four key factors that are essential for inducing pluripotent stem cells. KLF4 is highly expressed in non-dividing cells and its overexpression induces cell cycle arrest. KLF proteins KLF1, KLF2, KLF4, KLF5, KLF6, and KLF7 are transcriptional activators. KLF4 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 KLF4, which is related to the N-terminal domains of KLF1 and KLF2.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916941934   7 DFDMALSGTLLPSISTFASGTPVKGKSTGLGMASSRWKEELSNLKRPCVPTGGGCPDHDLLAGIAKKEPDDADLLDYDFI 86
Cdd:cd21582     1 EFDMALSGTLLPSISTFASGPAVKEKALGQGSANNRWREELSHLKRPCPPLGGRCYDQDPPLGMRRKEEEFNDLLDYDFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916941934  87 LSNTMLQQQQQQQDAMAGSSRNLPPSPGSYSYQLPSPQDSAGDILYTIP-----DINDVSPSGGFVAELMRPELDPAYLQ 161
Cdd:cd21582    81 LSNSLLQQQQQQQQAASTSSSTSSSSSSPYSYQLPSPQGTATSFLYPIPranlaDINDVSPSGGFVAELMRPDLDPAYLQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916941934 162 PTSLQGKFVVKTTMDMADYSQGINVSKN------STVLESSLPFVCQRIKQENPSTCTITRPMDVHLGINSRPGSSQRPL 235
Cdd:cd21582   161 PTSLHGKFVVKTTMDMGDYSQSINVSKSapmtksSVAPSSSLPFMCPRIKQENPSTCTISRPMDGHLGGNSQHGFSQRAP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916941934 236 LNPHGYPSGRPGAASRPSASlspgDVLNRDHHPSSQVLSHPPLPLPQGYHTSAGYAPYSQPPSLQYQGQsylsvfeepvh 315
Cdd:cd21582   241 LPSRTTPSGGPGGGNSSTAE----SLMSRDHHPSSQVLSHPPLPLPQGYHPSPGYPPFPPPPSQPQQYQ----------- 305

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1916941934 316 ippllpeamltppssplELMSPVDCLPEEPKPKRGRRSWPRKRIATH 362
Cdd:cd21582   306 -----------------ELMSPGSCLPEEPKPKRGRRSWPRKRTATH 335

N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of Kruppel-like factor (KLF)1, KLF2, and KLF4; Kruppel/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. 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 specifity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domains of an unknown subfamily of KLFs, predominantly found in fish, related to the N-terminal domains of KLF1, KLF2, and KLF4.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916941934  16 LLPSISTFASGTPVKGKST----GLGMASSRWKEELSNLKRPCVPTgggcPDHDLLAGIAKKEPDDADLLDYDFILSNTM 91
Cdd:cd22056     2 MLPSISTFASLQPLEEKQPeilcRWSVDAASSEVEFSIVQSPIEVP----KDDDELGKFLDEEDILSNFLDLEFILSSSN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916941934  92 lqqqqqqqdamAGSSRNLPPSPGSYSyqLP-SPQ------DSAGDILYTIPDIN----DVSPSGGFVAELMRPELdpAYL 160
Cdd:cd22056    78 -----------GSSSGPSQQQQCAYP--LPeSPEscstgsDSDGSDAPQPYHGSagftSSSPVHSLMAELLTPEM--NYP 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916941934 161 QPTSLQGKFVVKTTmDMADYSQGINVSKNSTVLESSLPFVCQRIKQENPS-TCTITRPMDVHLGinsrPGSSQRPLLNPH 239
Cdd:cd22056   143 GESSPDSAGKARDG-REYTELRALPTAPPAHQPATSPPPLGYKIKTEPVEqSCMMAAGGGGFMG----QQKPKHQMHSVH 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916941934 240 GYPsgRPGAASRPSASLSPGDVLNRDHHPSSQVLSHPPLPLPQGYHT-SAGYAPYSQPPSL-QYQGQSylSVFEEPVHI- 316
Cdd:cd22056   218 PQA--FTHHQAAGPGALQGRGGRGGPDCHLLHSSHHHHHHHHLQYQYmNAPYPPHYAHQGApQFHGQY--SVFREPMRVh 293

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1916941934 317 PPLLPEAMLTPPSSP--LELMSPVDclPEEPKPKRGRRSWPRKRIATH 362
Cdd:cd22056   294 HQGHPGSMLTPPSSPplLEFYAQDE--PEDIKPKRGRRSWARKRTATH 339

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*.
gi 1916941934 408 ELTRHYRKHTGHRPFQCQKCDRAFSR 433
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

N-terminal domain of Kruppel-like Factor 1; Kruppel-like Factor 1 (KLF1, also known as Krueppel-like factor 1 or Erythroid Kruppel-like Factor/EKLF) was the first Kruppel-like factor discovered. It was found to be vitally important for embryonic erythropoiesis in promoting the switch from fetal hemoglobin (Hemoglobin F) to adult hemoglobin (Hemoglobin A) gene expression by binding to highly conserved CACCC domains. EKLF ablation in mouse embryos produces a lethal anemic phenotype, causing death by embryonic day 14, and natural mutations lead to beta+ thalassemia in humans. However, expression of embryonic hemoglobin and fetal hemoglobin genes is normal in EKLF-deficient mice, suggesting other factors may be involved. KLF1 functions as a transcriptional activator. 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 specifity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF1, which is related to the N-terminal domains of KLF2 and KLF4.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916941934 221 HLGINSRPGSSQRPLLNPHGYPSGRPGAASRPSASLSPgdVLNRDHHPSSQVLSHPPLPLPQGYH--TSAGYAPYSQPps 298
Cdd:cd21581   140 HGYPDAFVGPALFPAPANVDQFGFPQGGSVDRRGNLSK--SGSWDFGSYYPQQHPSVVAFPDSRFgpLSGPQALTPDP-- 215

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1916941934 299 lQYQG--QSY---LSVFEEPVHIP-----PLLPEAMLTPPSSPlelmspvdclPEEPKPKRGRRSWPRKRIATH 362
Cdd:cd21581   216 -QHYGyfQLFrhnAALFPDYAHSPgpghlPLGQQPLLPDPPLP----------PGGAEGKRGRRSWAKKRPAVH 278

zinc finger;

                           10        20
                   ....*....|....*....|...
gi 1916941934  422 FQCQKCDRAFSRSDHLALHMKRH 444
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23

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.

                          10        20
                  ....*....|....*....|....*
gi 1916941934 392 YHCdwEGCGWKFARSDELTRHYRKH 416
Cdd:pfam00096   1 YKC--PDCGKSFSRKSNLKRHLRTH 23