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Conserved domains on  [gi|2462612914|ref|XP_054213497|]
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zinc finger and SCAN domain-containing protein 25 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 38-123 6.27e-46

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: 155.72  E-value: 6.27e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462612914  38 PETFRLRFRQFRYQEAAGPQEALRELQELCRRWLRPELHTKEQILELLVLEQFLTILPREFYAWIREHGPESGKALAAMV 117
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALA 80


                  ....*.
gi 2462612914 118 EDLTER 123
Cdd:pfam02023  81 EDLLLE 86
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
324-532 7.85e-12

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 67.41  E-value: 7.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462612914 324 LPPPQHG-AIPLPDEVKTHSSFWKPFQCPECGKGFSRSSNLVRHQRT-----HEEKSYGCVE--CGKGFTLREYLMKHQR 395
Cdd:COG5048   265 LPTASSQsSSPNESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRSvnhsgESLKPFSCPYslCGKLFSRNDALKRHIL 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462612914 396 THLGKRPYVC--SECWKTFSQ----RHHLEVHQRSHTGEKPYKCGD---CWKSFSRRQHLQVHRRTHTGEKPYTCECGKs 466
Cdd:COG5048   345 LHTSISPAKEklLNSSSKFSPllnnEPPQSLQQYKDLKNDKKSETLsnsCIRNFKRDSNLSLHIITHLSFRPYNCKNPP- 423

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462612914 467 fsrnanlavhrrahtgekpygcqvCGKRFSKGERLVRHQRIHTgEKPYHCPACGRSFNQRSILNRH 532
Cdd:COG5048   424 ------------------------CSKSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLSNH 464
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 231-259 5.19e-06

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: 43.31  E-value: 5.19e-06
                          10        20
                  ....*....|....*....|....*....
gi 2462612914 231 PFKDMALAFPEEEWRHVTPAQIDCFGEYV 259
Cdd:cd07765     2 TFEDVAVYFSQEEWELLDPAQRDLYRDVM 30
 
Name Accession Description Interval E-value
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 38-123 6.27e-46

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: 155.72  E-value: 6.27e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462612914  38 PETFRLRFRQFRYQEAAGPQEALRELQELCRRWLRPELHTKEQILELLVLEQFLTILPREFYAWIREHGPESGKALAAMV 117
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALA 80


                  ....*.
gi 2462612914 118 EDLTER 123
Cdd:pfam02023  81 EDLLLE 86
SCAN smart00431
leucine rich region;
38-136 6.46e-45

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 154.00  E-value: 6.46e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462612914   38 PETFRLRFRQFRYQEAAGPQEALRELQELCRRWLRPELHTKEQILELLVLEQFLTILPREFYAWIREHGPESGKALAAMV 117
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                           90       100
                   ....*....|....*....|.
gi 2462612914  118 EDLtERALE--AKAVPCHRQG 136
Cdd:smart00431  81 EDL-ERELDepGQQVSAHVHG 100
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 38-121 1.38e-37

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: 133.15  E-value: 1.38e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462612914  38 PETFRLRFRQFRYQEAAGPQEALRELQELCRRWLRPELHTKEQILELLVLEQFLTILPREFYAWIREHGPESGKALAAMV 117
Cdd:cd07936     1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80


                  ....
gi 2462612914 118 EDLT 121
Cdd:cd07936    81 EDLL 84
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
324-532 7.85e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 67.41  E-value: 7.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462612914 324 LPPPQHG-AIPLPDEVKTHSSFWKPFQCPECGKGFSRSSNLVRHQRT-----HEEKSYGCVE--CGKGFTLREYLMKHQR 395
Cdd:COG5048   265 LPTASSQsSSPNESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRSvnhsgESLKPFSCPYslCGKLFSRNDALKRHIL 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462612914 396 THLGKRPYVC--SECWKTFSQ----RHHLEVHQRSHTGEKPYKCGD---CWKSFSRRQHLQVHRRTHTGEKPYTCECGKs 466
Cdd:COG5048   345 LHTSISPAKEklLNSSSKFSPllnnEPPQSLQQYKDLKNDKKSETLsnsCIRNFKRDSNLSLHIITHLSFRPYNCKNPP- 423

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462612914 467 fsrnanlavhrrahtgekpygcqvCGKRFSKGERLVRHQRIHTgEKPYHCPACGRSFNQRSILNRH 532
Cdd:COG5048   424 ------------------------CSKSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLSNH 464
zf-H2C2_2 pfam13465
Zinc-finger double domain;
500-525 1.31e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 44.67  E-value: 1.31e-06
                          10        20
                  ....*....|....*....|....*.
gi 2462612914 500 RLVRHQRIHTGEKPYHCPACGRSFNQ 525
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 231-259 5.19e-06

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: 43.31  E-value: 5.19e-06
                          10        20
                  ....*....|....*....|....*....
gi 2462612914 231 PFKDMALAFPEEEWRHVTPAQIDCFGEYV 259
Cdd:cd07765     2 TFEDVAVYFSQEEWELLDPAQRDLYRDVM 30
ZnF_C2H2 smart00355
zinc finger;
348-370 2.70e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.52  E-value: 2.70e-03
                           10        20
                   ....*....|....*....|...
gi 2462612914  348 FQCPECGKGFSRSSNLVRHQRTH 370
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 232-251 4.38e-03

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: 35.14  E-value: 4.38e-03
                          10        20
                  ....*....|....*....|
gi 2462612914 232 FKDMALAFPEEEWRHVTPAQ 251
Cdd:pfam01352   4 FEDVAVDFTQEEWALLDPAQ 23
 
Name Accession Description Interval E-value
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 38-123 6.27e-46

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: 155.72  E-value: 6.27e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462612914  38 PETFRLRFRQFRYQEAAGPQEALRELQELCRRWLRPELHTKEQILELLVLEQFLTILPREFYAWIREHGPESGKALAAMV 117
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALA 80


                  ....*.
gi 2462612914 118 EDLTER 123
Cdd:pfam02023  81 EDLLLE 86
SCAN smart00431
leucine rich region;
38-136 6.46e-45

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 154.00  E-value: 6.46e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462612914   38 PETFRLRFRQFRYQEAAGPQEALRELQELCRRWLRPELHTKEQILELLVLEQFLTILPREFYAWIREHGPESGKALAAMV 117
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                           90       100
                   ....*....|....*....|.
gi 2462612914  118 EDLtERALE--AKAVPCHRQG 136
Cdd:smart00431  81 EDL-ERELDepGQQVSAHVHG 100
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 38-121 1.38e-37

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: 133.15  E-value: 1.38e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462612914  38 PETFRLRFRQFRYQEAAGPQEALRELQELCRRWLRPELHTKEQILELLVLEQFLTILPREFYAWIREHGPESGKALAAMV 117
Cdd:cd07936     1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80


                  ....
gi 2462612914 118 EDLT 121
Cdd:cd07936    81 EDLL 84
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
324-532 7.85e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 67.41  E-value: 7.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462612914 324 LPPPQHG-AIPLPDEVKTHSSFWKPFQCPECGKGFSRSSNLVRHQRT-----HEEKSYGCVE--CGKGFTLREYLMKHQR 395
Cdd:COG5048   265 LPTASSQsSSPNESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRSvnhsgESLKPFSCPYslCGKLFSRNDALKRHIL 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462612914 396 THLGKRPYVC--SECWKTFSQ----RHHLEVHQRSHTGEKPYKCGD---CWKSFSRRQHLQVHRRTHTGEKPYTCECGKs 466
Cdd:COG5048   345 LHTSISPAKEklLNSSSKFSPllnnEPPQSLQQYKDLKNDKKSETLsnsCIRNFKRDSNLSLHIITHLSFRPYNCKNPP- 423

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462612914 467 fsrnanlavhrrahtgekpygcqvCGKRFSKGERLVRHQRIHTgEKPYHCPACGRSFNQRSILNRH 532
Cdd:COG5048   424 ------------------------CSKSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
438-542 5.81e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.01  E-value: 5.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462612914 438 KSFSRRQHLQVHRRTHTG-EKPYTC-ECGKSFSRNANLAVHRRA--HTGE--KPYGC--QVCGKRFSKGERLVRHQRIHT 509
Cdd:COG5048   268 ASSQSSSPNESDSSSEKGfSLPIKSkQCNISFSRSSPLTRHLRSvnHSGEslKPFSCpySLCGKLFSRNDALKRHILLHT 347

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462612914 510 GEKPYHCPACGRSFNQRSILN--RHQKTQHRQEPL 542
Cdd:COG5048   348 SISPAKEKLLNSSSKFSPLLNnePPQSLQQYKDLK 382
zf-H2C2_2 pfam13465
Zinc-finger double domain;
500-525 1.31e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 44.67  E-value: 1.31e-06
                          10        20
                  ....*....|....*....|....*.
gi 2462612914 500 RLVRHQRIHTGEKPYHCPACGRSFNQ 525
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 348-370 2.02e-06

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: 44.21  E-value: 2.02e-06
                          10        20
                  ....*....|....*....|...
gi 2462612914 348 FQCPECGKGFSRSSNLVRHQRTH 370
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 231-259 5.19e-06

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: 43.31  E-value: 5.19e-06
                          10        20
                  ....*....|....*....|....*....
gi 2462612914 231 PFKDMALAFPEEEWRHVTPAQIDCFGEYV 259
Cdd:cd07765     2 TFEDVAVYFSQEEWELLDPAQRDLYRDVM 30
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
429-485 6.32e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.92  E-value: 6.32e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462612914 429 KPYKCGDCWKSFSRRQHLQVHRRTHTGEKPYTC---ECGKSFSRNANLAVHRRAHTGEKP 485
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsysGCDKSFSRPLELSRHLRTHHNNPS 91
zf-H2C2_2 pfam13465
Zinc-finger double domain;
445-469 5.02e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 5.02e-05
                          10        20
                  ....*....|....*....|....*.
gi 2462612914 445 HLQVHRRTHTGEKPYTC-ECGKSFSR 469
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCpECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 431-453 6.54e-05

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 39.98  E-value: 6.54e-05
                          10        20
                  ....*....|....*....|...
gi 2462612914 431 YKCGDCWKSFSRRQHLQVHRRTH 453
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-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: 1.40e-04
                          10        20
                  ....*....|....*....|...
gi 2462612914 403 YVCSECWKTFSQRHHLEVHQRSH 425
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
484-540 1.89e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.92  E-value: 1.89e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462612914 484 KPYGCQVCGKRFSKGERLVRHQRIHTGEKPYHCPACGRSFNQRSILNRHQKTQHRQE 540
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHN 88
zf-H2C2_2 pfam13465
Zinc-finger double domain;
417-442 2.00e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.00e-04
                          10        20
                  ....*....|....*....|....*.
gi 2462612914 417 HLEVHQRSHTGEKPYKCGDCWKSFSR 442
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
389-414 1.59e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.59e-03
                          10        20
                  ....*....|....*....|....*.
gi 2462612914 389 YLMKHQRTHLGKRPYVCSECWKTFSQ 414
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
ZnF_C2H2 smart00355
zinc finger;
348-370 2.70e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.52  E-value: 2.70e-03
                           10        20
                   ....*....|....*....|...
gi 2462612914  348 FQCPECGKGFSRSSNLVRHQRTH 370
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
457-525 2.95e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.06  E-value: 2.95e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462612914 457 KPYTCE-CGKSFSRNANLAVHRRAHTGEKPYGCQV--CGKRFSKGERLVRHQRIHTGEKPYHCPACGRSFNQ 525
Cdd:COG5048    32 RPDSCPnCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNS 103
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 232-251 4.38e-03

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: 35.14  E-value: 4.38e-03
                          10        20
                  ....*....|....*....|
gi 2462612914 232 FKDMALAFPEEEWRHVTPAQ 251
Cdd:pfam01352   4 FEDVAVDFTQEEWALLDPAQ 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
472-497 4.96e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 4.96e-03
                          10        20
                  ....*....|....*....|....*.
gi 2462612914 472 NLAVHRRAHTGEKPYGCQVCGKRFSK 497
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 459-480 5.29e-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: 34.58  E-value: 5.29e-03
                          10        20
                  ....*....|....*....|...
gi 2462612914 459 YTC-ECGKSFSRNANLAVHRRAH 480
Cdd:pfam00096   1 YKCpDCGKSFSRKSNLKRHLRTH 23
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 348-370 9.61e-03

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


Pssm-ID: 464025  Cd Length: 24  Bit Score: 33.77  E-value: 9.61e-03
                          10        20
                  ....*....|....*....|...
gi 2462612914 348 FQCPECGKGFSRSSNLVRHQRTH 370
Cdd:pfam13894   1 FKCPICGKSFSSKKSLKRHLKTH 23
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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