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Conserved domains on  [gi|1609542404|ref|NP_001356383|]
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zinc finger protein 445 isoform 2 [Homo sapiens]

Protein Classification

SCAN and KRAB_A-box domain-containing protein( domain architecture ID 12210991)

protein containing domains SCAN, KRAB_A-box, and COG5048

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
51-155 1.65e-53

leucine rich region;


:

Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 181.73  E-value: 1.65e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404    51 QELFRQLFRQLRYHESSGPLETLSRLRELCRWWLRPDVLSKAQILELLVLEQFLSILPGELRVWVQLHNPESGEEAVALL 130
Cdd:smart00431    1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                            90       100
                    ....*....|....*....|....*
gi 1609542404   131 EELQRDLDGTSWRDPGPAQSPDVHW 155
Cdd:smart00431   81 EDLERELDEPGQQVSAHVHGQEVLL 105
KRAB smart00349
krueppel associated box;
222-280 2.87e-30

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 113.84  E-value: 2.87e-30
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404   222 MTFKDVEVTFSQDEWGWLDSAQRNLYRDVMLENYRNMASLVGPFTKPALISWLEAR-EPW 280
Cdd:smart00349    1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGeEPW 60
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
583-1019 2.96e-12

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 70.11  E-value: 2.96e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404  583 KLFDCSQCRKSFHCKSYVLEHQRIHTQEKPYKCTK--CRKTFRWRSNFTRHMRLHeeeKFYKQDECREGFRQSP--DCSQ 658
Cdd:COG5048     32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTH---HNNPSDLNSKSLPLSNskASSS 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404  659 PQGAPAVE--KTFLCQQCGKTFTRKKTLVDHQRIHTGEKPYQCSDCGKDFayrSAFIVHKKKHAMKRKPEGGPSFSQDTV 736
Cdd:COG5048    109 SLSSSSSNsnDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSS---VNTPQSNSLHPPLPANSLSKDPSSNLS 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404  737 FQVPQSSHSKEEPYKCSQCGKAFRNHSFLLIHQRVHTGEKPYKCRECGKAFRWSSNLYRHQRIHS------LQKQY---D 807
Cdd:COG5048    186 LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSsdssssASESPrssL 265

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404  808 CHESEKTPNVEPKILTGEKRFW----CQECGKTFTRKRTLLDHK--GIHSGE--KRYKC--NLCGKSYDRNYRLVNHQRI 877
Cdd:COG5048    266 PTASSQSSSPNESDSSSEKGFSlpikSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCpySLCGKLFSRNDALKRHILL 345

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404  878 HSTERPFKCQWcgkefigRHTLSSHQRKhtraaqaerSPPARSSSQDTKLRLQKLKPSEEMPLEDCKEACSQSSRLTGLQ 957
Cdd:COG5048    346 HTSISPAKEKL-------LNSSSKFSPL---------LNNEPPQSLQQYKDLKNDKKSETLSNSCIRNFKRDSNLSLHII 409

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1609542404  958 DISIGKKCH-KCSICGKTFNKSSQLISHKRFHTRERPFKCSKCGKTFRwssnlARHMKNHIRD 1019
Cdd:COG5048    410 THLSFRPYNcKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRR-----DLDLSNHGKD 467
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
445-631 1.94e-07

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 54.70  E-value: 1.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404  445 NKKDVCGKDFSLSSHHQRGQSLHTVGV------SFKCSDCGRTFSHSSHLAYHQR--LHTQE--KAFKCRV--CGKAFRW 512
Cdd:COG5048    256 SASESPRSSLPTASSQSSSPNESDSSSekgfslPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSR 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404  513 SSNCARHEKIHTGVKPYKCDL--CEKAFRRLSAYRLHRETHAKKKFLELNQYRAAL-----------TYSSGFDHHLGDQ 579
Cdd:COG5048    336 NDALKRHILLHTSISPAKEKLlnSSSKFSPLLNNEPPQSLQQYKDLKNDKKSETLSnscirnfkrdsNLSLHIITHLSFR 415

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1609542404  580 SGE-KLFDCSQCRKSFHCKSyvlEHQRIHTQEKPYkCTKCRKTFRWRSNFTRH 631
Cdd:COG5048    416 PYNcKNPPCSKSFNRHYNLI---PHKKIHTNHAPL-LCSILKSFRRDLDLSNH 464
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
51-155 1.65e-53

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 181.73  E-value: 1.65e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404    51 QELFRQLFRQLRYHESSGPLETLSRLRELCRWWLRPDVLSKAQILELLVLEQFLSILPGELRVWVQLHNPESGEEAVALL 130
Cdd:smart00431    1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                            90       100
                    ....*....|....*....|....*
gi 1609542404   131 EELQRDLDGTSWRDPGPAQSPDVHW 155
Cdd:smart00431   81 EDLERELDEPGQQVSAHVHGQEVLL 105
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 51-139 1.42e-43

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: 152.64  E-value: 1.42e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404   51 QELFRQLFRQLRYHESSGPLETLSRLRELCRWWLRPDVLSKAQILELLVLEQFLSILPGELRVWVQLHNPESGEEAVALL 130
Cdd:pfam02023    1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALA 80


                   ....*....
gi 1609542404  131 EELQRDLDG 139
Cdd:pfam02023   81 EDLLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 52-135 6.72e-35

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: 127.76  E-value: 6.72e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404   52 ELFRQLFRQLRYHESSGPLETLSRLRELCRWWLRPDVLSKAQILELLVLEQFLSILPGELRVWVQLHNPESGEEAVALLE 131
Cdd:cd07936      2 ETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLAE 81


                   ....
gi 1609542404  132 ELQR 135
Cdd:cd07936     82 DLLA 85
KRAB smart00349
krueppel associated box;
222-280 2.87e-30

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 113.84  E-value: 2.87e-30
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404   222 MTFKDVEVTFSQDEWGWLDSAQRNLYRDVMLENYRNMASLVGPFTKPALISWLEAR-EPW 280
Cdd:smart00349    1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGeEPW 60
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 222-261 5.27e-21

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: 86.76  E-value: 5.27e-21
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1609542404  222 MTFKDVEVTFSQDEWGWLDSAQRNLYRDVMLENYRNMASL 261
Cdd:pfam01352    2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 222-261 2.26e-19

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: 81.83  E-value: 2.26e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1609542404  222 MTFKDVEVTFSQDEWGWLDSAQRNLYRDVMLENYRNMASL 261
Cdd:cd07765      1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
583-1019 2.96e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 70.11  E-value: 2.96e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404  583 KLFDCSQCRKSFHCKSYVLEHQRIHTQEKPYKCTK--CRKTFRWRSNFTRHMRLHeeeKFYKQDECREGFRQSP--DCSQ 658
Cdd:COG5048     32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTH---HNNPSDLNSKSLPLSNskASSS 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404  659 PQGAPAVE--KTFLCQQCGKTFTRKKTLVDHQRIHTGEKPYQCSDCGKDFayrSAFIVHKKKHAMKRKPEGGPSFSQDTV 736
Cdd:COG5048    109 SLSSSSSNsnDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSS---VNTPQSNSLHPPLPANSLSKDPSSNLS 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404  737 FQVPQSSHSKEEPYKCSQCGKAFRNHSFLLIHQRVHTGEKPYKCRECGKAFRWSSNLYRHQRIHS------LQKQY---D 807
Cdd:COG5048    186 LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSsdssssASESPrssL 265

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404  808 CHESEKTPNVEPKILTGEKRFW----CQECGKTFTRKRTLLDHK--GIHSGE--KRYKC--NLCGKSYDRNYRLVNHQRI 877
Cdd:COG5048    266 PTASSQSSSPNESDSSSEKGFSlpikSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCpySLCGKLFSRNDALKRHILL 345

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404  878 HSTERPFKCQWcgkefigRHTLSSHQRKhtraaqaerSPPARSSSQDTKLRLQKLKPSEEMPLEDCKEACSQSSRLTGLQ 957
Cdd:COG5048    346 HTSISPAKEKL-------LNSSSKFSPL---------LNNEPPQSLQQYKDLKNDKKSETLSNSCIRNFKRDSNLSLHII 409

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1609542404  958 DISIGKKCH-KCSICGKTFNKSSQLISHKRFHTRERPFKCSKCGKTFRwssnlARHMKNHIRD 1019
Cdd:COG5048    410 THLSFRPYNcKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRR-----DLDLSNHGKD 467
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
445-631 1.94e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 54.70  E-value: 1.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404  445 NKKDVCGKDFSLSSHHQRGQSLHTVGV------SFKCSDCGRTFSHSSHLAYHQR--LHTQE--KAFKCRV--CGKAFRW 512
Cdd:COG5048    256 SASESPRSSLPTASSQSSSPNESDSSSekgfslPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSR 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404  513 SSNCARHEKIHTGVKPYKCDL--CEKAFRRLSAYRLHRETHAKKKFLELNQYRAAL-----------TYSSGFDHHLGDQ 579
Cdd:COG5048    336 NDALKRHILLHTSISPAKEKLlnSSSKFSPLLNNEPPQSLQQYKDLKNDKKSETLSnscirnfkrdsNLSLHIITHLSFR 415

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1609542404  580 SGE-KLFDCSQCRKSFHCKSyvlEHQRIHTQEKPYkCTKCRKTFRWRSNFTRH 631
Cdd:COG5048    416 PYNcKNPPCSKSFNRHYNLI---PHKKIHTNHAPL-LCSILKSFRRDLDLSNH 464
zf-H2C2_2 pfam13465
Zinc-finger double domain;
684-708 3.50e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 3.50e-04
                           10        20
                   ....*....|....*....|....*
gi 1609542404  684 LVDHQRIHTGEKPYQCSDCGKDFAY 708
Cdd:pfam13465    2 LKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 966-1015 4.11e-04

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: 39.85  E-value: 4.11e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1609542404  966 HKCSICGKTFNKSSQLISHKRFHTrerpFKCSKCGKTFRWSSNLARHMKN 1015
Cdd:cd20908      2 PWCYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHCLQ 47
zf-H2C2_2 pfam13465
Zinc-finger double domain;
515-540 4.43e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 4.43e-04
                           10        20
                   ....*....|....*....|....*.
gi 1609542404  515 NCARHEKIHTGVKPYKCDLCEKAFRR 540
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
51-155 1.65e-53

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 181.73  E-value: 1.65e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404    51 QELFRQLFRQLRYHESSGPLETLSRLRELCRWWLRPDVLSKAQILELLVLEQFLSILPGELRVWVQLHNPESGEEAVALL 130
Cdd:smart00431    1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                            90       100
                    ....*....|....*....|....*
gi 1609542404   131 EELQRDLDGTSWRDPGPAQSPDVHW 155
Cdd:smart00431   81 EDLERELDEPGQQVSAHVHGQEVLL 105
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 51-139 1.42e-43

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: 152.64  E-value: 1.42e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404   51 QELFRQLFRQLRYHESSGPLETLSRLRELCRWWLRPDVLSKAQILELLVLEQFLSILPGELRVWVQLHNPESGEEAVALL 130
Cdd:pfam02023    1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALA 80


                   ....*....
gi 1609542404  131 EELQRDLDG 139
Cdd:pfam02023   81 EDLLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 52-135 6.72e-35

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: 127.76  E-value: 6.72e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404   52 ELFRQLFRQLRYHESSGPLETLSRLRELCRWWLRPDVLSKAQILELLVLEQFLSILPGELRVWVQLHNPESGEEAVALLE 131
Cdd:cd07936      2 ETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLAE 81


                   ....
gi 1609542404  132 ELQR 135
Cdd:cd07936     82 DLLA 85
KRAB smart00349
krueppel associated box;
222-280 2.87e-30

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 113.84  E-value: 2.87e-30
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404   222 MTFKDVEVTFSQDEWGWLDSAQRNLYRDVMLENYRNMASLVGPFTKPALISWLEAR-EPW 280
Cdd:smart00349    1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGeEPW 60
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 222-261 5.27e-21

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: 86.76  E-value: 5.27e-21
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1609542404  222 MTFKDVEVTFSQDEWGWLDSAQRNLYRDVMLENYRNMASL 261
Cdd:pfam01352    2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 222-261 2.26e-19

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: 81.83  E-value: 2.26e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1609542404  222 MTFKDVEVTFSQDEWGWLDSAQRNLYRDVMLENYRNMASL 261
Cdd:cd07765      1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
583-1019 2.96e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 70.11  E-value: 2.96e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404  583 KLFDCSQCRKSFHCKSYVLEHQRIHTQEKPYKCTK--CRKTFRWRSNFTRHMRLHeeeKFYKQDECREGFRQSP--DCSQ 658
Cdd:COG5048     32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTH---HNNPSDLNSKSLPLSNskASSS 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404  659 PQGAPAVE--KTFLCQQCGKTFTRKKTLVDHQRIHTGEKPYQCSDCGKDFayrSAFIVHKKKHAMKRKPEGGPSFSQDTV 736
Cdd:COG5048    109 SLSSSSSNsnDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSS---VNTPQSNSLHPPLPANSLSKDPSSNLS 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404  737 FQVPQSSHSKEEPYKCSQCGKAFRNHSFLLIHQRVHTGEKPYKCRECGKAFRWSSNLYRHQRIHS------LQKQY---D 807
Cdd:COG5048    186 LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSsdssssASESPrssL 265

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404  808 CHESEKTPNVEPKILTGEKRFW----CQECGKTFTRKRTLLDHK--GIHSGE--KRYKC--NLCGKSYDRNYRLVNHQRI 877
Cdd:COG5048    266 PTASSQSSSPNESDSSSEKGFSlpikSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCpySLCGKLFSRNDALKRHILL 345

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404  878 HSTERPFKCQWcgkefigRHTLSSHQRKhtraaqaerSPPARSSSQDTKLRLQKLKPSEEMPLEDCKEACSQSSRLTGLQ 957
Cdd:COG5048    346 HTSISPAKEKL-------LNSSSKFSPL---------LNNEPPQSLQQYKDLKNDKKSETLSNSCIRNFKRDSNLSLHII 409

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1609542404  958 DISIGKKCH-KCSICGKTFNKSSQLISHKRFHTRERPFKCSKCGKTFRwssnlARHMKNHIRD 1019
Cdd:COG5048    410 THLSFRPYNcKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRR-----DLDLSNHGKD 467
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
472-902 7.74e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 65.49  E-value: 7.74e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404  472 SFKCSDCGRTFSHSSHLAYHQRLHTQEKAFKCRVCGkafrwssncarhekihtgvkpykcdlCEKAF-RRLSAYRLHRET 550
Cdd:COG5048     33 PDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSG--------------------------CDKSFsRPLELSRHLRTH 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404  551 HAKKKFLELNQYRAALTYSSGFDHHLGDQSGEKLFDCSQCRKSFHCKSYVLEHQRIHTQEKPYKCTKCRKTFRWRSNFT- 629
Cdd:COG5048     87 HNNPSDLNSKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNs 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404  630 -----RHMRLHEEEKFYKQDECREGFRQSPDCSQpqgapavektflCQQCGKTFTRKKTLVDHQRIHTGEKPYQCS---- 700
Cdd:COG5048    167 lhpplPANSLSKDPSSNLSLLISSNVSTSIPSSS------------ENSPLSSSYSIPSSSSDQNLENSSSSLPLTtnsq 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404  701 -------DCGKDFAYRSAFIVHKKKHAMKRKPEggPSFSQDTVFQVPQSSHS-KEEPYKCSQCGKAFRNHSFLLIHQR-- 770
Cdd:COG5048    235 lspksllSQSPSSLSSSDSSSSASESPRSSLPT--ASSQSSSPNESDSSSEKgFSLPIKSKQCNISFSRSSPLTRHLRsv 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404  771 VHTGE--KPYKCRE--CGKAFRWSSNLYRHQRIHSLQKQYDCHE----SEKTPNVEPK---------ILTGEKRFWC--Q 831
Cdd:COG5048    313 NHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLlnssSKFSPLLNNEppqslqqykDLKNDKKSETlsN 392

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1609542404  832 ECGKTFTRKRTLLDHKGIH--SGEKRYKCNLCGKSYDRNYRLVNHQRIHSTERPFKCQWCGKeFIGRHTLSSH 902
Cdd:COG5048    393 SCIRNFKRDSNLSLHIITHlsFRPYNCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
729-1017 1.13e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 65.10  E-value: 1.13e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404  729 PSFSQDTVFQVPQSSHSKEE-----PYKCSQCGKAFRNHSFLLIHQRVHTGEKPYKCR--ECGKAFRWSSNLYRHQRIHS 801
Cdd:COG5048      8 SSSSNNSVLSSTPKSTLKSLsnaprPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHH 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404  802 LQKQYD--------------------CHESEKTPNVEPKILTGEKRFWCQECGKTFTRKRTLLDHKGIHSGEKRYKCNL- 860
Cdd:COG5048     88 NNPSDLnskslplsnskasssslsssSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSl 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404  861 --------CGKSYDRNYRLVNHQRIHSTERPFKCQWCGKEFIGRHTLSSHQRKH--------TRAAQAERSPPARSSSQD 924
Cdd:COG5048    168 hpplpansLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLEnsssslplTTNSQLSPKSLLSQSPSS 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404  925 TKLRLQKLKPSEEMPLEDCKEACSQSS-RLTGLQDISIGKKCHKCSICGKTFNKSSQLISHKR--FHTRE--RPFKC--S 997
Cdd:COG5048    248 LSSSDSSSSASESPRSSLPTASSQSSSpNESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpyS 327

                          330       340
                   ....*....|....*....|
gi 1609542404  998 KCGKTFRWSSNLARHMKNHI 1017
Cdd:COG5048    328 LCGKLFSRNDALKRHILLHT 347
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
445-631 1.94e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 54.70  E-value: 1.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404  445 NKKDVCGKDFSLSSHHQRGQSLHTVGV------SFKCSDCGRTFSHSSHLAYHQR--LHTQE--KAFKCRV--CGKAFRW 512
Cdd:COG5048    256 SASESPRSSLPTASSQSSSPNESDSSSekgfslPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSR 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609542404  513 SSNCARHEKIHTGVKPYKCDL--CEKAFRRLSAYRLHRETHAKKKFLELNQYRAAL-----------TYSSGFDHHLGDQ 579
Cdd:COG5048    336 NDALKRHILLHTSISPAKEKLlnSSSKFSPLLNNEPPQSLQQYKDLKNDKKSETLSnscirnfkrdsNLSLHIITHLSFR 415

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1609542404  580 SGE-KLFDCSQCRKSFHCKSyvlEHQRIHTQEKPYkCTKCRKTFRWRSNFTRH 631
Cdd:COG5048    416 PYNcKNPPCSKSFNRHYNLI---PHKKIHTNHAPL-LCSILKSFRRDLDLSNH 464
zf-H2C2_2 pfam13465
Zinc-finger double domain;
684-708 3.50e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 3.50e-04
                           10        20
                   ....*....|....*....|....*
gi 1609542404  684 LVDHQRIHTGEKPYQCSDCGKDFAY 708
Cdd:pfam13465    2 LKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 966-1015 4.11e-04

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: 39.85  E-value: 4.11e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1609542404  966 HKCSICGKTFNKSSQLISHKRFHTrerpFKCSKCGKTFRWSSNLARHMKN 1015
Cdd:cd20908      2 PWCYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHCLQ 47
zf-H2C2_2 pfam13465
Zinc-finger double domain;
515-540 4.43e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 4.43e-04
                           10        20
                   ....*....|....*....|....*.
gi 1609542404  515 NCARHEKIHTGVKPYKCDLCEKAFRR 540
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
765-787 9.80e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 9.80e-04
                           10        20
                   ....*....|....*....|...
gi 1609542404  765 LLIHQRVHTGEKPYKCRECGKAF 787
Cdd:pfam13465    2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 473-495 1.32e-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: 36.89  E-value: 1.32e-03
                           10        20
                   ....*....|....*....|...
gi 1609542404  473 FKCSDCGRTFSHSSHLAYHQRLH 495
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
602-622 3.48e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 3.48e-03
                           10        20
                   ....*....|....*....|.
gi 1609542404  602 EHQRIHTQEKPYKCTKCRKTF 622
Cdd:pfam13465    4 RHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
487-510 4.45e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 4.45e-03
                           10        20
                   ....*....|....*....|....
gi 1609542404  487 HLAYHQRLHTQEKAFKCRVCGKAF 510
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
981-1003 6.09e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 6.09e-03
                           10        20
                   ....*....|....*....|...
gi 1609542404  981 LISHKRFHTRERPFKCSKCGKTF 1003
Cdd:pfam13465    2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 750-772 8.05e-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: 8.05e-03
                           10        20
                   ....*....|....*....|...
gi 1609542404  750 YKCSQCGKAFRNHSFLLIHQRVH 772
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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