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Conserved domains on  [gi|2217327843|ref|XP_047300220|]
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transcription factor Sp5 isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SP5_N cd22541
N-terminal domain of transcription factor Specificity Protein (SP) 5; Specificity Proteins ...
 30-221 6.11e-22

N-terminal domain of transcription factor Specificity Protein (SP) 5; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in the chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. All of them contain clade SP5, which plays a potential role in human cancers and was found in several human tumors including hepatocellular carcinoma, gastric cancer, and colon cancer. Leukemia inhibitor factor/Stat3 and Wnt/beta-catenin signaling pathways converge on SP5 to promote mouse embryonic stem cell self-renewal. SP5 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. This model represents the N-terminal domain of SP5.


:

Pssm-ID: 412096 [Multi-domain]  Cd Length: 143  Bit Score: 89.93  E-value: 6.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327843  30 GAAHELPLTPPADPS------YPYEFSPVKMLPSSMAALPASCAPAYVPYAAQaalppgysnllpppppppppPTCRQLS 103
Cdd:cd22541     1 MAPHELPLTPPAEPSfhqslaYSFELSPVKMLPTPAPAPAASAPPHPSPVSSP--------------------TQQPQQL 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327843 104 PNPAPDDLPWWSIPQAGAGPGASGVPGsglsgacagaphaprfpasaaaaaaaaaalqrglvLGPSDFAQYQSQIAALLQ 183
Cdd:cd22541    61 PPNPADDIPWWSIQQSNPAHPPSTSTP-----------------------------------LGHPTFAGYQPQIAALLQ 105

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2217327843 184 TKAPLA--ATARRCRRCRCPNCQAAGGapEAEPGKKKQHV 221
Cdd:cd22541   106 TKSPAAslSTTRRCRRCRCPNCQNPST--SSEPGKKKQHI 143
zf-H2C2_2 pfam13465
Zinc-finger double domain;
266-289 1.76e-07

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 46.60  E-value: 1.76e-07
                          10        20
                  ....*....|....*....|....
gi 2217327843 266 ELQRHLRTHTGEKRFACPECGKRF 289
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
235-308 1.73e-06

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 49.31  E-value: 1.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327843 235 SHLKAHLRW--HTGE--RPFVCNWLFCGKSFTRSDELQRHLRTHTGEKRFACP--ECGKRFMRSDHLAKHVKTHQNKKLK 308
Cdd:COG5048   303 SPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQYKDLK 382
 
Name Accession Description Interval E-value
SP5_N cd22541
N-terminal domain of transcription factor Specificity Protein (SP) 5; Specificity Proteins ...
 30-221 6.11e-22

N-terminal domain of transcription factor Specificity Protein (SP) 5; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in the chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. All of them contain clade SP5, which plays a potential role in human cancers and was found in several human tumors including hepatocellular carcinoma, gastric cancer, and colon cancer. Leukemia inhibitor factor/Stat3 and Wnt/beta-catenin signaling pathways converge on SP5 to promote mouse embryonic stem cell self-renewal. SP5 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. This model represents the N-terminal domain of SP5.


Pssm-ID: 412096 [Multi-domain]  Cd Length: 143  Bit Score: 89.93  E-value: 6.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327843  30 GAAHELPLTPPADPS------YPYEFSPVKMLPSSMAALPASCAPAYVPYAAQaalppgysnllpppppppppPTCRQLS 103
Cdd:cd22541     1 MAPHELPLTPPAEPSfhqslaYSFELSPVKMLPTPAPAPAASAPPHPSPVSSP--------------------TQQPQQL 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327843 104 PNPAPDDLPWWSIPQAGAGPGASGVPGsglsgacagaphaprfpasaaaaaaaaaalqrglvLGPSDFAQYQSQIAALLQ 183
Cdd:cd22541    61 PPNPADDIPWWSIQQSNPAHPPSTSTP-----------------------------------LGHPTFAGYQPQIAALLQ 105

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2217327843 184 TKAPLA--ATARRCRRCRCPNCQAAGGapEAEPGKKKQHV 221
Cdd:cd22541   106 TKSPAAslSTTRRCRRCRCPNCQNPST--SSEPGKKKQHI 143
zf-H2C2_2 pfam13465
Zinc-finger double domain;
266-289 1.76e-07

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 46.60  E-value: 1.76e-07
                          10        20
                  ....*....|....*....|....
gi 2217327843 266 ELQRHLRTHTGEKRFACPECGKRF 289
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
235-308 1.73e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 49.31  E-value: 1.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327843 235 SHLKAHLRW--HTGE--RPFVCNWLFCGKSFTRSDELQRHLRTHTGEKRFACP--ECGKRFMRSDHLAKHVKTHQNKKLK 308
Cdd:COG5048   303 SPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQYKDLK 382
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 280-302 6.44e-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: 6.44e-05
                          10        20
                  ....*....|....*....|...
gi 2217327843 280 FACPECGKRFMRSDHLAKHVKTH 302
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA03247 PHA03247
large tegument protein UL36; Provisional
 2-147 9.09e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 9.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327843    2 PAHSPGALPPPHPSLGLTPQKTHLQPSFGAAHELPLTP--PADPSYPyefspvkMLPSSMAALPASCAPAYVPYAAQAAL 79
Cdd:PHA03247  2702 PPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPapPAVPAGP-------ATPGGPARPARPPTTAGPPAPAPPAA 2774

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217327843   80 PPGYSNLLPPPPPPPPPPTCRQLSPNPAPDDLPWWSIPQAGAGPGASGVPGSGLSGACAGAPHAPRFP 147
Cdd:PHA03247  2775 PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPP 2842
ZnF_C2H2 smart00355
zinc finger;
280-302 2.14e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.13  E-value: 2.14e-03
                           10        20
                   ....*....|....*....|...
gi 2217327843  280 FACPECGKRFMRSDHLAKHVKTH 302
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
PHA00733 PHA00733
hypothetical protein
 249-302 2.83e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.16  E-value: 2.83e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217327843 249 PFVCNwlFCGKSFTRSDELQRHLRTHTGEKrfACPECGKRFMRSDHLAKHV-KTH 302
Cdd:PHA00733   73 PYVCP--LCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDHVcKKH 123
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 248-308 3.12e-03

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 36.00  E-value: 3.12e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217327843 248 RPFvCnwLFCGKSFtrSDE--LQRHLRthtgEKRFACPECGKRFMRSDHLAKHVKTHQNKKLK 308
Cdd:cd20908     1 KPW-C--YYCDREF--DDEkiLIQHQK----AKHFKCHICHKKLYTAGGLAVHCLQVHKETLT 54
 
Name Accession Description Interval E-value
SP5_N cd22541
N-terminal domain of transcription factor Specificity Protein (SP) 5; Specificity Proteins ...
 30-221 6.11e-22

N-terminal domain of transcription factor Specificity Protein (SP) 5; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in the chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. All of them contain clade SP5, which plays a potential role in human cancers and was found in several human tumors including hepatocellular carcinoma, gastric cancer, and colon cancer. Leukemia inhibitor factor/Stat3 and Wnt/beta-catenin signaling pathways converge on SP5 to promote mouse embryonic stem cell self-renewal. SP5 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. This model represents the N-terminal domain of SP5.


Pssm-ID: 412096 [Multi-domain]  Cd Length: 143  Bit Score: 89.93  E-value: 6.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327843  30 GAAHELPLTPPADPS------YPYEFSPVKMLPSSMAALPASCAPAYVPYAAQaalppgysnllpppppppppPTCRQLS 103
Cdd:cd22541     1 MAPHELPLTPPAEPSfhqslaYSFELSPVKMLPTPAPAPAASAPPHPSPVSSP--------------------TQQPQQL 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327843 104 PNPAPDDLPWWSIPQAGAGPGASGVPGsglsgacagaphaprfpasaaaaaaaaaalqrglvLGPSDFAQYQSQIAALLQ 183
Cdd:cd22541    61 PPNPADDIPWWSIQQSNPAHPPSTSTP-----------------------------------LGHPTFAGYQPQIAALLQ 105

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2217327843 184 TKAPLA--ATARRCRRCRCPNCQAAGGapEAEPGKKKQHV 221
Cdd:cd22541   106 TKSPAAslSTTRRCRRCRCPNCQNPST--SSEPGKKKQHI 143
zf-H2C2_2 pfam13465
Zinc-finger double domain;
266-289 1.76e-07

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 46.60  E-value: 1.76e-07
                          10        20
                  ....*....|....*....|....
gi 2217327843 266 ELQRHLRTHTGEKRFACPECGKRF 289
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
235-308 1.73e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 49.31  E-value: 1.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327843 235 SHLKAHLRW--HTGE--RPFVCNWLFCGKSFTRSDELQRHLRTHTGEKRFACP--ECGKRFMRSDHLAKHVKTHQNKKLK 308
Cdd:COG5048   303 SPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQYKDLK 382
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
252-306 5.64e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.69  E-value: 5.64e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217327843 252 CNWLFCGKSFTRSDELQRHLRT--HTGE--KRFACPE--CGKRFMRSDHLAKHVKTHQNKK 306
Cdd:COG5048   290 IKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSIS 350
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 280-302 6.44e-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: 6.44e-05
                          10        20
                  ....*....|....*....|...
gi 2217327843 280 FACPECGKRFMRSDHLAKHVKTH 302
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
236-263 6.61e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 6.61e-05
                          10        20
                  ....*....|....*....|....*...
gi 2217327843 236 HLKAHLRWHTGERPFVCNwlFCGKSFTR 263
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCP--ECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 250-274 1.05e-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: 38.82  E-value: 1.05e-04
                          10        20
                  ....*....|....*....|....*
gi 2217327843 250 FVCNwlFCGKSFTRSDELQRHLRTH 274
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
248-307 1.74e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.15  E-value: 1.74e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217327843 248 RPFVCNwlFCGKSFTRSDELQRHLRTHTGEKRFAC--PECGKRFMRSDHLAKHVKTHQNKKL 307
Cdd:COG5048    32 RPDSCP--NCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPS 91
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
216-298 3.85e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.99  E-value: 3.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327843 216 KKKQHVCHVPGCGKVYGKTSHLKAHLRWHTGERPFVCNWLFCGKSFTRSDELQRHLRTHTgEKRFACPECGKRFMRSDHL 295
Cdd:COG5048   383 NDKKSETLSNSCIRNFKRDSNLSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLDL 461


                  ...
gi 2217327843 296 AKH 298
Cdd:COG5048   462 SNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
212-280 6.66e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.22  E-value: 6.66e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217327843 212 AEPGKKKQHVChvPGCGKVYGKTSHLKAHLRWHTGERPFVCNWLFCGKSFTRSDELQRHLRTHTGEKRF 280
Cdd:COG5048    26 SLSNAPRPDSC--PNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSD 92
PHA03247 PHA03247
large tegument protein UL36; Provisional
 2-147 9.09e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 9.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327843    2 PAHSPGALPPPHPSLGLTPQKTHLQPSFGAAHELPLTP--PADPSYPyefspvkMLPSSMAALPASCAPAYVPYAAQAAL 79
Cdd:PHA03247  2702 PPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPapPAVPAGP-------ATPGGPARPARPPTTAGPPAPAPPAA 2774

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217327843   80 PPGYSNLLPPPPPPPPPPTCRQLSPNPAPDDLPWWSIPQAGAGPGASGVPGSGLSGACAGAPHAPRFP 147
Cdd:PHA03247  2775 PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPP 2842
ZnF_C2H2 smart00355
zinc finger;
280-302 2.14e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.13  E-value: 2.14e-03
                           10        20
                   ....*....|....*....|...
gi 2217327843  280 FACPECGKRFMRSDHLAKHVKTH 302
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
PHA00733 PHA00733
hypothetical protein
 249-302 2.83e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.16  E-value: 2.83e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217327843 249 PFVCNwlFCGKSFTRSDELQRHLRTHTGEKrfACPECGKRFMRSDHLAKHV-KTH 302
Cdd:PHA00733   73 PYVCP--LCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDHVcKKH 123
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 248-308 3.12e-03

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 36.00  E-value: 3.12e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217327843 248 RPFvCnwLFCGKSFtrSDE--LQRHLRthtgEKRFACPECGKRFMRSDHLAKHVKTHQNKKLK 308
Cdd:cd20908     1 KPW-C--YYCDREF--DDEkiLIQHQK----AKHFKCHICHKKLYTAGGLAVHCLQVHKETLT 54
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 280-302 4.43e-03

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


Pssm-ID: 464025  Cd Length: 24  Bit Score: 34.16  E-value: 4.43e-03
                          10        20
                  ....*....|....*....|...
gi 2217327843 280 FACPECGKRFMRSDHLAKHVKTH 302
Cdd:pfam13894   1 FKCPICGKSFSSKKSLKRHLKTH 23
ZnF_C2H2 smart00355
zinc finger;
250-274 7.50e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 33.59  E-value: 7.50e-03
                           10        20
                   ....*....|....*....|....*
gi 2217327843  250 FVCNWlfCGKSFTRSDELQRHLRTH 274
Cdd:smart00355   1 YRCPE--CGKVFKSKSALREHMRTH 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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