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Conserved domains on  [gi|538920587|ref|NP_001269345|]
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zinc finger and SCAN domain-containing protein 10 isoform 3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
263-637 5.00e-17

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 84.36  E-value: 5.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538920587 263 DERPHACHLCGHRFRQSSHLSKHLLTHSSEPAFLCAECGRG--FQRRASLVQHLLAHAQ-------DQKPPC---APESK 330
Cdd:COG5048   30 APRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHHNnpsdlnsKSLPLSnskASSSS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538920587 331 AEAPPLTDV---LCSHCGQSFQRRSSLKRHLR--IHARDKD----RRSSEGSGSRRRDSDRRPFVCSDCGKAFRRSEHLv 401
Cdd:COG5048  110 LSSSSSNSNdnnLLSSHSLPPSSRDPQLPDLLsiSNLRNNPlpgnNSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLI- 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538920587 402 aHRRVHTGERPFSCQACGRSFTQSSQLVSHQRVHTGEKPYACPQCGKRFVRRASLARHLLTHGGPRPHHCTQCGKSFGQT 481
Cdd:COG5048  189 -SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPT 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538920587 482 QDLARHQRSHTGE-------KPCRCSECGEGFSQSAHLARHQR--IHTGE--KPHACD--TCGHRFRNSSNLARHRRSHT 548
Cdd:COG5048  268 ASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPysLCGKLFSRNDALKRHILLHT 347

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538920587 549 GERPYSCQTCGRSFRRN------AHLRRHLATHAEPGQEQAEPPQECVecgKSFSRSCNLLRHLLVHTGARPYSC--TQC 620
Cdd:COG5048  348 SISPAKEKLLNSSSKFSpllnnePPQSLQQYKDLKNDKKSETLSNSCI---RNFKRDSNLSLHIITHLSFRPYNCknPPC 424

                        410
                 ....*....|....*..
gi 538920587 621 GRSFSRNSHLLRHLRTH 637
Cdd:COG5048  425 SKSFNRHYNLIPHKKIH 441
PRK12323 super family cl46901
DNA polymerase III subunit gamma/tau;
13-180 4.78e-04

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK12323:

Pssm-ID: 481241 [Multi-domain]  Cd Length: 700  Bit Score: 43.33  E-value: 4.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538920587  13 VPEPAPGALRPLAAAGSAHQETDPGAAGAGAVPECAASAPPGPPAGAAAQGWGGGGAAARGHPPGAQPRGAAGPQGPSPW 92
Cdd:PRK12323 396 APAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAA 475

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538920587  93 PEESSRDQELAAVlECLTFEDVPenkAWPAHPLGFGSRTPDKEEFKQEEPKGAAWPTPILAESQADSPGVPGEPCAQSLG 172
Cdd:PRK12323 476 AAAAPARAAPAAA-PAPADDDPP---PWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAP 551


                 ....*...
gi 538920587 173 RGAAASGP 180
Cdd:PRK12323 552 RAAAATEP 559
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
263-637 5.00e-17

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 84.36  E-value: 5.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538920587 263 DERPHACHLCGHRFRQSSHLSKHLLTHSSEPAFLCAECGRG--FQRRASLVQHLLAHAQ-------DQKPPC---APESK 330
Cdd:COG5048   30 APRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHHNnpsdlnsKSLPLSnskASSSS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538920587 331 AEAPPLTDV---LCSHCGQSFQRRSSLKRHLR--IHARDKD----RRSSEGSGSRRRDSDRRPFVCSDCGKAFRRSEHLv 401
Cdd:COG5048  110 LSSSSSNSNdnnLLSSHSLPPSSRDPQLPDLLsiSNLRNNPlpgnNSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLI- 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538920587 402 aHRRVHTGERPFSCQACGRSFTQSSQLVSHQRVHTGEKPYACPQCGKRFVRRASLARHLLTHGGPRPHHCTQCGKSFGQT 481
Cdd:COG5048  189 -SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPT 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538920587 482 QDLARHQRSHTGE-------KPCRCSECGEGFSQSAHLARHQR--IHTGE--KPHACD--TCGHRFRNSSNLARHRRSHT 548
Cdd:COG5048  268 ASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPysLCGKLFSRNDALKRHILLHT 347

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538920587 549 GERPYSCQTCGRSFRRN------AHLRRHLATHAEPGQEQAEPPQECVecgKSFSRSCNLLRHLLVHTGARPYSC--TQC 620
Cdd:COG5048  348 SISPAKEKLLNSSSKFSpllnnePPQSLQQYKDLKNDKKSETLSNSCI---RNFKRDSNLSLHIITHLSFRPYNCknPPC 424

                        410
                 ....*....|....*..
gi 538920587 621 GRSFSRNSHLLRHLRTH 637
Cdd:COG5048  425 SKSFNRHYNLIPHKKIH 441
zf-H2C2_2 pfam13465
Zinc-finger double domain;
428-452 9.47e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 9.47e-05
                          10        20
                  ....*....|....*....|....*
gi 538920587  428 LVSHQRVHTGEKPYACPQCGKRFVR 452
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
13-180 4.78e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 43.33  E-value: 4.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538920587  13 VPEPAPGALRPLAAAGSAHQETDPGAAGAGAVPECAASAPPGPPAGAAAQGWGGGGAAARGHPPGAQPRGAAGPQGPSPW 92
Cdd:PRK12323 396 APAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAA 475

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538920587  93 PEESSRDQELAAVlECLTFEDVPenkAWPAHPLGFGSRTPDKEEFKQEEPKGAAWPTPILAESQADSPGVPGEPCAQSLG 172
Cdd:PRK12323 476 AAAAPARAAPAAA-PAPADDDPP---PWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAP 551


                 ....*...
gi 538920587 173 RGAAASGP 180
Cdd:PRK12323 552 RAAAATEP 559
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 411-462 1.07e-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: 38.31  E-value: 1.07e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 538920587 411 RPFsCQACGRSFTQSSQLVSHQRvhtgEKPYACPQCGKRFVRRASLARHLLT 462
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQK----AKHFKCHICHKKLYTAGGLAVHCLQ 47
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
263-637 5.00e-17

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 84.36  E-value: 5.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538920587 263 DERPHACHLCGHRFRQSSHLSKHLLTHSSEPAFLCAECGRG--FQRRASLVQHLLAHAQ-------DQKPPC---APESK 330
Cdd:COG5048   30 APRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHHNnpsdlnsKSLPLSnskASSSS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538920587 331 AEAPPLTDV---LCSHCGQSFQRRSSLKRHLR--IHARDKD----RRSSEGSGSRRRDSDRRPFVCSDCGKAFRRSEHLv 401
Cdd:COG5048  110 LSSSSSNSNdnnLLSSHSLPPSSRDPQLPDLLsiSNLRNNPlpgnNSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLI- 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538920587 402 aHRRVHTGERPFSCQACGRSFTQSSQLVSHQRVHTGEKPYACPQCGKRFVRRASLARHLLTHGGPRPHHCTQCGKSFGQT 481
Cdd:COG5048  189 -SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPT 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538920587 482 QDLARHQRSHTGE-------KPCRCSECGEGFSQSAHLARHQR--IHTGE--KPHACD--TCGHRFRNSSNLARHRRSHT 548
Cdd:COG5048  268 ASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPysLCGKLFSRNDALKRHILLHT 347

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538920587 549 GERPYSCQTCGRSFRRN------AHLRRHLATHAEPGQEQAEPPQECVecgKSFSRSCNLLRHLLVHTGARPYSC--TQC 620
Cdd:COG5048  348 SISPAKEKLLNSSSKFSpllnnePPQSLQQYKDLKNDKKSETLSNSCI---RNFKRDSNLSLHIITHLSFRPYNCknPPC 424

                        410
                 ....*....|....*..
gi 538920587 621 GRSFSRNSHLLRHLRTH 637
Cdd:COG5048  425 SKSFNRHYNLIPHKKIH 441
zf-H2C2_2 pfam13465
Zinc-finger double domain;
428-452 9.47e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 9.47e-05
                          10        20
                  ....*....|....*....|....*
gi 538920587  428 LVSHQRVHTGEKPYACPQCGKRFVR 452
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 615-637 2.57e-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: 38.44  E-value: 2.57e-04
                          10        20
                  ....*....|....*....|...
gi 538920587  615 YSCTQCGRSFSRNSHLLRHLRTH 637
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
13-180 4.78e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 43.33  E-value: 4.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538920587  13 VPEPAPGALRPLAAAGSAHQETDPGAAGAGAVPECAASAPPGPPAGAAAQGWGGGGAAARGHPPGAQPRGAAGPQGPSPW 92
Cdd:PRK12323 396 APAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAA 475

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538920587  93 PEESSRDQELAAVlECLTFEDVPenkAWPAHPLGFGSRTPDKEEFKQEEPKGAAWPTPILAESQADSPGVPGEPCAQSLG 172
Cdd:PRK12323 476 AAAAPARAAPAAA-PAPADDDPP---PWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAP 551


                 ....*...
gi 538920587 173 RGAAASGP 180
Cdd:PRK12323 552 RAAAATEP 559
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 411-462 1.07e-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: 38.31  E-value: 1.07e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 538920587 411 RPFsCQACGRSFTQSSQLVSHQRvhtgEKPYACPQCGKRFVRRASLARHLLT 462
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQK----AKHFKCHICHKKLYTAGGLAVHCLQ 47
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 385-407 1.88e-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: 36.12  E-value: 1.88e-03
                          10        20
                  ....*....|....*....|...
gi 538920587  385 FVCSDCGKAFRRSEHLVAHRRVH 407
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
254-278 1.93e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.93e-03
                          10        20
                  ....*....|....*....|....*
gi 538920587  254 LKLHMRTHTDERPHACHLCGHRFRQ 278
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
574-637 2.45e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.83  E-value: 2.45e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 538920587 574 THAEPGQEQAEPPQECVECGKSFSRSCNLLRHLLVHTGARPYSCTQCGR--SFSRNSHLLRHLRTH 637
Cdd:COG5048   21 KSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCdkSFSRPLELSRHLRTH 86
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 553-575 2.50e-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: 35.74  E-value: 2.50e-03
                          10        20
                  ....*....|....*....|...
gi 538920587  553 YSCQTCGRSFRRNAHLRRHLATH 575
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
455-478 4.19e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.19e-03
                          10        20
                  ....*....|....*....|....
gi 538920587  455 SLARHLLTHGGPRPHHCTQCGKSF 478
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 441-463 9.32e-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: 34.20  E-value: 9.32e-03
                          10        20
                  ....*....|....*....|...
gi 538920587  441 YACPQCGKRFVRRASLARHLLTH 463
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 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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