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Conserved domains on  [gi|1622935047|ref|XP_028703588|]
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zinc finger protein with KRAB and SCAN domains 4 isoform X2 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SCAN super family cl42860
leucine rich region;
49-131 1.02e-40

leucine rich region;


The actual alignment was detected with superfamily member smart00431:

Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 142.44  E-value: 1.02e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935047   49 PERSRQRFRGFRYPEAAGPREALSRLRELCRQWLQPEMHSKEQILELLVLEQFLTILPGNLQSWV--------------- 113
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVrehhpesgeeavtll 80
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1622935047  114 --------------PVGDQGQEMLCCKMALLT 131
Cdd:smart00431  81 edlereldepgqqvSAHVHGQEVLLEKMVPLG 112
KRAB super family cl42959
krueppel associated box;
192-254 2.06e-13

krueppel associated box;


The actual alignment was detected with superfamily member smart00349:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 64.92  E-value: 2.06e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622935047  192 LKMEDVALTLSPG-WTQLDSSQVNIYRDEKQENHSSLVSLGGEKQTesrdlPPVkkLSKKEHGK 254
Cdd:smart00349   1 VTFEDVAVYFTQEeWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPK-----PDL--ISQLEQGE 57
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
345-509 5.54e-10

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 61.64  E-value: 5.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935047 345 KPYECEECGKVFSHSSNLIKHQRT--HTGE--KPYECD--DCGKTFSQSCSLLEHHKIHTGEKPYQCNM--CGKTFRRNS 416
Cdd:COG5048   288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEKLlnSSSKFSPLL 367
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935047 417 HLLRHQRIHgdkNVQNPEHGESWERQGrtesqwenieapmsykcNECERSFTRNRSLIEHQKIHTGEKPYQCD--TCGKG 494
Cdd:COG5048   368 NNEPPQSLQ---QYKDLKNDKKSETLS-----------------NSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKS 427
                         170
                  ....*....|....*
gi 1622935047 495 FTRTSYLVQHQRSHV 509
Cdd:COG5048   428 FNRHYNLIPHKKIHT 442
zf-H2C2_2 pfam13465
Zinc-finger double domain;
306-328 1.15e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.15e-04
                          10        20
                  ....*....|....*....|...
gi 1622935047 306 LTKHRRIHTGEKPYECEDCGKTF 328
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
291-313 3.38e-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: 3.38e-04
                          10        20
                  ....*....|....*....|...
gi 1622935047 291 HYCHECGKSFAQSSGLTKHRRIH 313
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
319-341 3.23e-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: 3.23e-03
                          10        20
                  ....*....|....*....|...
gi 1622935047 319 YECEDCGKTFIGSSALVIHQRVH 341
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
49-131 1.02e-40

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 142.44  E-value: 1.02e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935047   49 PERSRQRFRGFRYPEAAGPREALSRLRELCRQWLQPEMHSKEQILELLVLEQFLTILPGNLQSWV--------------- 113
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVrehhpesgeeavtll 80
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1622935047  114 --------------PVGDQGQEMLCCKMALLT 131
Cdd:smart00431  81 edlereldepgqqvSAHVHGQEVLLEKMVPLG 112
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
49-113 9.71e-40

SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several pfam00096 proteins. The domain has been shown to be able to mediate homo- and hetero-oligomerization.


Pssm-ID: 460417 [Multi-domain]  Cd Length: 89  Bit Score: 138.78  E-value: 9.71e-40
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622935047  49 PERSRQRFRGFRYPEAAGPREALSRLRELCRQWLQPEMHSKEQILELLVLEQFLTILPGNLQSWV 113
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWV 65
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
49-113 6.89e-33

SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several vertebrate proteins that contain C2H2 zinc finger motifs, many of which may be transcription factors playing roles in cell survival and differentiation. This protein-interaction domain is able to mediate homo- and hetero-oligomerization of SCAN-containing proteins. Some SCAN-containing proteins, including those of lower vertebrates, do not contain zinc finger motifs. It has been noted that the SCAN domain resembles a domain-swapped version of the C-terminal domain of the HIV capsid protein. This domain model features elements common to the three general groups of SCAN domains (SCAN-A1, SCAN-A2, and SCAN-B). The SCAND1 protein is truncated at the C-terminus with respect to this model, the SCAND2 protein appears to have a truncated central helix.


Pssm-ID: 153421  Cd Length: 85  Bit Score: 120.06  E-value: 6.89e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622935047  49 PERSRQRFRGFRYPEAAGPREALSRLRELCRQWLQPEMHSKEQILELLVLEQFLTILPGNLQSWV 113
Cdd:cd07936     1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWV 65
KRAB smart00349
krueppel associated box;
192-254 2.06e-13

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 64.92  E-value: 2.06e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622935047  192 LKMEDVALTLSPG-WTQLDSSQVNIYRDEKQENHSSLVSLGGEKQTesrdlPPVkkLSKKEHGK 254
Cdd:smart00349   1 VTFEDVAVYFTQEeWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPK-----PDL--ISQLEQGE 57
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
345-509 5.54e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 61.64  E-value: 5.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935047 345 KPYECEECGKVFSHSSNLIKHQRT--HTGE--KPYECD--DCGKTFSQSCSLLEHHKIHTGEKPYQCNM--CGKTFRRNS 416
Cdd:COG5048   288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEKLlnSSSKFSPLL 367
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935047 417 HLLRHQRIHgdkNVQNPEHGESWERQGrtesqwenieapmsykcNECERSFTRNRSLIEHQKIHTGEKPYQCD--TCGKG 494
Cdd:COG5048   368 NNEPPQSLQ---QYKDLKNDKKSETLS-----------------NSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKS 427
                         170
                  ....*....|....*
gi 1622935047 495 FTRTSYLVQHQRSHV 509
Cdd:COG5048   428 FNRHYNLIPHKKIHT 442
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
192-230 2.18e-07

KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta , KRAB-A interacting protein , and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation.


Pssm-ID: 143639  Cd Length: 40  Bit Score: 47.16  E-value: 2.18e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622935047 192 LKMEDVALTLSP-GWTQLDSSQVNIYRDEKQENHSSLVSL 230
Cdd:cd07765     1 VTFEDVAVYFSQeEWELLDPAQRDLYRDVMLENYENLVSL 40
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
195-231 3.59e-07

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 46.70  E-value: 3.59e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1622935047 195 EDVALTLSPG-WTQLDSSQVNIYRDEKQENHSSLVSLG 231
Cdd:pfam01352   5 EDVAVDFTQEeWALLDPAQRNLYRDVMLENYRNLVSLG 42
zf-H2C2_2 pfam13465
Zinc-finger double domain;
361-386 6.85e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 6.85e-06
                          10        20
                  ....*....|....*....|....*.
gi 1622935047 361 NLIKHQRTHTGEKPYECDDCGKTFSQ 386
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
306-328 1.15e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.15e-04
                          10        20
                  ....*....|....*....|...
gi 1622935047 306 LTKHRRIHTGEKPYECEDCGKTF 328
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
291-313 3.38e-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: 3.38e-04
                          10        20
                  ....*....|....*....|...
gi 1622935047 291 HYCHECGKSFAQSSGLTKHRRIH 313
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
319-341 3.23e-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: 3.23e-03
                          10        20
                  ....*....|....*....|...
gi 1622935047 319 YECEDCGKTFIGSSALVIHQRVH 341
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA00733 PHA00733
hypothetical protein
374-421 7.49e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 36.78  E-value: 7.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1622935047 374 PYECDDCGKTFSQSCSLLEHhkIHTGEKPYQCNMCGKTFRRNSHLLRH 421
Cdd:PHA00733   73 PYVCPLCLMPFSSSVSLKQH--IRYTEHSKVCPVCGKEFRNTDSTLDH 118
ZnF_C2H2 smart00355
zinc finger;
347-369 8.40e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 33.98  E-value: 8.40e-03
                           10        20
                   ....*....|....*....|...
gi 1622935047  347 YECEECGKVFSHSSNLIKHQRTH 369
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
49-131 1.02e-40

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 142.44  E-value: 1.02e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935047   49 PERSRQRFRGFRYPEAAGPREALSRLRELCRQWLQPEMHSKEQILELLVLEQFLTILPGNLQSWV--------------- 113
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVrehhpesgeeavtll 80
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1622935047  114 --------------PVGDQGQEMLCCKMALLT 131
Cdd:smart00431  81 edlereldepgqqvSAHVHGQEVLLEKMVPLG 112
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
49-113 9.71e-40

SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several pfam00096 proteins. The domain has been shown to be able to mediate homo- and hetero-oligomerization.


Pssm-ID: 460417 [Multi-domain]  Cd Length: 89  Bit Score: 138.78  E-value: 9.71e-40
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622935047  49 PERSRQRFRGFRYPEAAGPREALSRLRELCRQWLQPEMHSKEQILELLVLEQFLTILPGNLQSWV 113
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWV 65
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
49-113 6.89e-33

SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several vertebrate proteins that contain C2H2 zinc finger motifs, many of which may be transcription factors playing roles in cell survival and differentiation. This protein-interaction domain is able to mediate homo- and hetero-oligomerization of SCAN-containing proteins. Some SCAN-containing proteins, including those of lower vertebrates, do not contain zinc finger motifs. It has been noted that the SCAN domain resembles a domain-swapped version of the C-terminal domain of the HIV capsid protein. This domain model features elements common to the three general groups of SCAN domains (SCAN-A1, SCAN-A2, and SCAN-B). The SCAND1 protein is truncated at the C-terminus with respect to this model, the SCAND2 protein appears to have a truncated central helix.


Pssm-ID: 153421  Cd Length: 85  Bit Score: 120.06  E-value: 6.89e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622935047  49 PERSRQRFRGFRYPEAAGPREALSRLRELCRQWLQPEMHSKEQILELLVLEQFLTILPGNLQSWV 113
Cdd:cd07936     1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWV 65
KRAB smart00349
krueppel associated box;
192-254 2.06e-13

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 64.92  E-value: 2.06e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622935047  192 LKMEDVALTLSPG-WTQLDSSQVNIYRDEKQENHSSLVSLGGEKQTesrdlPPVkkLSKKEHGK 254
Cdd:smart00349   1 VTFEDVAVYFTQEeWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPK-----PDL--ISQLEQGE 57
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
345-509 5.54e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 61.64  E-value: 5.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935047 345 KPYECEECGKVFSHSSNLIKHQRT--HTGE--KPYECD--DCGKTFSQSCSLLEHHKIHTGEKPYQCNM--CGKTFRRNS 416
Cdd:COG5048   288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEKLlnSSSKFSPLL 367
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935047 417 HLLRHQRIHgdkNVQNPEHGESWERQGrtesqwenieapmsykcNECERSFTRNRSLIEHQKIHTGEKPYQCD--TCGKG 494
Cdd:COG5048   368 NNEPPQSLQ---QYKDLKNDKKSETLS-----------------NSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKS 427
                         170
                  ....*....|....*
gi 1622935047 495 FTRTSYLVQHQRSHV 509
Cdd:COG5048   428 FNRHYNLIPHKKIHT 442
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
192-230 2.18e-07

KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta , KRAB-A interacting protein , and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation.


Pssm-ID: 143639  Cd Length: 40  Bit Score: 47.16  E-value: 2.18e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622935047 192 LKMEDVALTLSP-GWTQLDSSQVNIYRDEKQENHSSLVSL 230
Cdd:cd07765     1 VTFEDVAVYFSQeEWELLDPAQRDLYRDVMLENYENLVSL 40
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
195-231 3.59e-07

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 46.70  E-value: 3.59e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1622935047 195 EDVALTLSPG-WTQLDSSQVNIYRDEKQENHSSLVSLG 231
Cdd:pfam01352   5 EDVAVDFTQEeWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
282-435 1.62e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.46  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935047 282 QKNAVGSKRHYCHECGKSFAQSSGLTKHRR--IHTGE--KPYEC--EDCGKTFIGSSALVIHQRVHTGEKPYEC--EECG 353
Cdd:COG5048   281 SSEKGFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEklLNSS 360
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935047 354 KVFSHSSNLIKHQRTH-----TGEKPYECDD--CGKTFSQSCSLLEHHKIHTGEKPYQCN--MCGKTFRRNSHLLRHQRI 424
Cdd:COG5048   361 SKFSPLLNNEPPQSLQqykdlKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKI 440
                         170
                  ....*....|.
gi 1622935047 425 HGDKNVQNPEH 435
Cdd:COG5048   441 HTNHAPLLCSI 451
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
451-508 4.82e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.92  E-value: 4.82e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935047 451 NIEAPMSYKCNECERSFTRNRSLIEHQKIHTGEKPYQC--DTCGKGFTRTSYLVQHQRSH 508
Cdd:COG5048    27 LSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTH 86
zf-H2C2_2 pfam13465
Zinc-finger double domain;
361-386 6.85e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 6.85e-06
                          10        20
                  ....*....|....*....|....*.
gi 1622935047 361 NLIKHQRTHTGEKPYECDDCGKTFSQ 386
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
345-411 1.14e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.77  E-value: 1.14e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622935047 345 KPYECEECGKVFSHSSNLIKHQRTHTGEKPYEC--DDCGKTFSQSCSLLEHHKIHTGEKPYQCNMCGKT 411
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPL 100
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
347-369 1.26e-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: 41.90  E-value: 1.26e-05
                          10        20
                  ....*....|....*....|...
gi 1622935047 347 YECEECGKVFSHSSNLIKHQRTH 369
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
403-425 1.40e-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: 41.90  E-value: 1.40e-05
                          10        20
                  ....*....|....*....|...
gi 1622935047 403 YQCNMCGKTFRRNSHLLRHQRIH 425
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
278-481 2.06e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.00  E-value: 2.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935047 278 LQRKQKNAVGSKR-HYCHECGKSFAQSSGLTKHRRIHTGEKPYECEDCGktfigssalvihqrvhtgekpyeceeCGKVF 356
Cdd:COG5048    20 PKSTLKSLSNAPRpDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSG--------------------------CDKSF 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935047 357 SHSSNLIKHQRTHTGEKPYEC-DDCGKTFSQSCSLLEHHKIHTGEKPYQCNMCGKTF--RRNSHLLRHQRIHGDKNVQNP 433
Cdd:COG5048    74 SRPLELSRHLRTHHNNPSDLNsKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPssRDPQLPDLLSISNLRNNPLPG 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1622935047 434 EHGESWERQGRTESqWENIEAPMSYKCNECERSFTRNRSLIEHQKIHT 481
Cdd:COG5048   154 NNSSSVNTPQSNSL-HPPLPANSLSKDPSSNLSLLISSNVSTSIPSSS 200
zf-H2C2_2 pfam13465
Zinc-finger double domain;
472-497 9.20e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 9.20e-05
                          10        20
                  ....*....|....*....|....*.
gi 1622935047 472 SLIEHQKIHTGEKPYQCDTCGKGFTR 497
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
306-328 1.15e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.15e-04
                          10        20
                  ....*....|....*....|...
gi 1622935047 306 LTKHRRIHTGEKPYECEDCGKTF 328
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
333-358 1.21e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.21e-04
                          10        20
                  ....*....|....*....|....*.
gi 1622935047 333 ALVIHQRVHTGEKPYECEECGKVFSH 358
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
291-313 3.38e-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: 3.38e-04
                          10        20
                  ....*....|....*....|...
gi 1622935047 291 HYCHECGKSFAQSSGLTKHRRIH 313
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
389-414 3.56e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 3.56e-04
                          10        20
                  ....*....|....*....|....*.
gi 1622935047 389 SLLEHHKIHTGEKPYQCNMCGKTFRR 414
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
287-421 8.97e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.99  E-value: 8.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935047 287 GSKRHYCHE--CGKSFAQSSGLTKHRRIHTGEKPYEC--EDCGKTFIGSSALVIHQRVH-----TGEKPYECE--ECGKV 355
Cdd:COG5048   318 SLKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQqykdlKNDKKSETLsnSCIRN 397
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622935047 356 FSHSSNLIKHQRTHTGEKPYECDD--CGKTFSQSCSLLEHHKIHTGEKPYQCNMCGKtFRRNSHLLRH 421
Cdd:COG5048   398 FKRDSNLSLHIITHLSFRPYNCKNppCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNH 464
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
343-425 1.97e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.47  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935047 343 GEKPYECE--ECGKVFShSSNLIKHQRTHtgekpyecDDCGKTFSQSCSLLEHHKIHTGEKPYQCNMCGKTFrRNSHLLR 420
Cdd:COG5189   346 DGKPYKCPveGCNKKYK-NQNGLKYHMLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRY-KNLNGLK 415

                  ....*
gi 1622935047 421 HQRIH 425
Cdd:COG5189   416 YHRKH 420
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
458-480 2.20e-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: 35.35  E-value: 2.20e-03
                          10        20
                  ....*....|....*....|...
gi 1622935047 458 YKCNECERSFTRNRSLIEHQKIH 480
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
486-508 2.29e-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: 35.35  E-value: 2.29e-03
                          10        20
                  ....*....|....*....|...
gi 1622935047 486 YQCDTCGKGFTRTSYLVQHQRSH 508
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
319-341 3.23e-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: 3.23e-03
                          10        20
                  ....*....|....*....|...
gi 1622935047 319 YECEDCGKTFIGSSALVIHQRVH 341
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
375-397 4.47e-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: 34.58  E-value: 4.47e-03
                          10        20
                  ....*....|....*....|...
gi 1622935047 375 YECDDCGKTFSQSCSLLEHHKIH 397
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA00733 PHA00733
hypothetical protein
374-421 7.49e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 36.78  E-value: 7.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1622935047 374 PYECDDCGKTFSQSCSLLEHhkIHTGEKPYQCNMCGKTFRRNSHLLRH 421
Cdd:PHA00733   73 PYVCPLCLMPFSSSVSLKQH--IRYTEHSKVCPVCGKEFRNTDSTLDH 118
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
290-341 7.79e-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: 35.61  E-value: 7.79e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622935047 290 RHYCHECGKSFAQSSGLTKHRRIHTgekpYECEDCGKTFIGSSALVIH-QRVH 341
Cdd:cd20908     1 KPWCYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
ZnF_C2H2 smart00355
zinc finger;
347-369 8.40e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 33.98  E-value: 8.40e-03
                           10        20
                   ....*....|....*....|...
gi 1622935047  347 YECEECGKVFSHSSNLIKHQRTH 369
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 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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