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Conserved domains on  [gi|1958726021|ref|XP_038952093|]
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zinc finger protein 184 isoform X3 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
28-81 1.23e-21

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 88.80  E-value: 1.23e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958726021   28 VTFKDVVVNFTQEEWKHLDPTQRDLFRDVTLENYTHLVSIDWKIRPENSVSPLE 81
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLE 54
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
252-660 3.28e-12

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 69.34  E-value: 3.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958726021 252 KPYKCDECGKAFSQRTHLVQHQRIHTGEKPYTCN--ECGKSFSQRGHFMEHQKIHTGEKPFKCEECEKTFTRST-HLTQH 328
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKAsSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958726021 329 QKIHTGEKTYKCNECGKAFNGPSTFIRHHMIHT---GEKPYECNECGKAFSQhSNLTQHQKTHTgekpydcAECGKAFSY 405
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISnlrNNPLPGNNSSSVNTPQ-SNSLHPPLPAN-------SLSKDPSSN 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958726021 406 WSSLAQHLKIHTGEKPYKCSDCGKAFSYcSSLTQHRRIHTREKPFECSECGKAFSYLSNLNQHQKTHTQEKAYECKECG- 484
Cdd:COG5048   184 LSLLISSNVSTSIPSSSENSPLSSSYSI-PSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPr 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958726021 485 -----KAFIRSSSLAKHERIHTG-EKPYQCLECGKTFSYGSSLIQHK--KIHTGE--RPYKCNE--CERAFNQKIHLTQH 552
Cdd:COG5048   263 sslptASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPYslCGKLFSRNDALKRH 342

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958726021 553 KRIHTGVKPYACP--KCGKTFRHCS------SLAQHQKTHTEGKHYQC-NKCEKTFSQKSHLTQHQQVHMGEKP--YKCN 621
Cdd:COG5048   343 ILLHTSISPAKEKllNSSSKFSPLLnneppqSLQQYKDLKNDKKSETLsNSCIRNFKRDSNLSLHIITHLSFRPynCKNP 422

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1958726021 622 DCDRCFTQSTHLTEHQSIHTGEKPYSSNVCPQTFNQNTY 660
Cdd:COG5048   423 PCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDL 461
SFP1 super family cl25788
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 122-272 4.62e-04

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


The actual alignment was detected with superfamily member COG5189:

Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 43.17  E-value: 4.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958726021 122 TEKTMRPSYE---KDLGVSA---GLLTQTDIAVDQTSTNtraKQSSRPgqkeKLCKCNEcgkafTYCSALIRHQRThTGE 195
Cdd:COG5189   281 EESSLGFDYEfihKSVGNKEirgGISTGEMIDVRKLPCT---NSSSNG----KLAHGGE-----RNIDTPSRMLKV-KDG 347

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958726021 196 KPYKCN--DCNKAFsRNENLINHQRIHtgdkpykcDQCGKGFIEGPSLTQHQRIHTGEKPYKCDECGKAFSQRTHLVQH 272
Cdd:COG5189   348 KPYKCPveGCNKKY-KNQNGLKYHMLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKYH 417
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
28-81 1.23e-21

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 88.80  E-value: 1.23e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958726021   28 VTFKDVVVNFTQEEWKHLDPTQRDLFRDVTLENYTHLVSIDWKIRPENSVSPLE 81
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLE 54
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 27-68 4.91e-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: 86.37  E-value: 4.91e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958726021  27 SVTFKDVVVNFTQEEWKHLDPTQRDLFRDVTLENYTHLVSID 68
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 28-67 2.53e-18

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: 78.75  E-value: 2.53e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1958726021  28 VTFKDVVVNFTQEEWKHLDPTQRDLFRDVTLENYTHLVSI 67
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
252-660 3.28e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 69.34  E-value: 3.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958726021 252 KPYKCDECGKAFSQRTHLVQHQRIHTGEKPYTCN--ECGKSFSQRGHFMEHQKIHTGEKPFKCEECEKTFTRST-HLTQH 328
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKAsSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958726021 329 QKIHTGEKTYKCNECGKAFNGPSTFIRHHMIHT---GEKPYECNECGKAFSQhSNLTQHQKTHTgekpydcAECGKAFSY 405
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISnlrNNPLPGNNSSSVNTPQ-SNSLHPPLPAN-------SLSKDPSSN 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958726021 406 WSSLAQHLKIHTGEKPYKCSDCGKAFSYcSSLTQHRRIHTREKPFECSECGKAFSYLSNLNQHQKTHTQEKAYECKECG- 484
Cdd:COG5048   184 LSLLISSNVSTSIPSSSENSPLSSSYSI-PSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPr 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958726021 485 -----KAFIRSSSLAKHERIHTG-EKPYQCLECGKTFSYGSSLIQHK--KIHTGE--RPYKCNE--CERAFNQKIHLTQH 552
Cdd:COG5048   263 sslptASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPYslCGKLFSRNDALKRH 342

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958726021 553 KRIHTGVKPYACP--KCGKTFRHCS------SLAQHQKTHTEGKHYQC-NKCEKTFSQKSHLTQHQQVHMGEKP--YKCN 621
Cdd:COG5048   343 ILLHTSISPAKEKllNSSSKFSPLLnneppqSLQQYKDLKNDKKSETLsNSCIRNFKRDSNLSLHIITHLSFRPynCKNP 422

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1958726021 622 DCDRCFTQSTHLTEHQSIHTGEKPYSSNVCPQTFNQNTY 660
Cdd:COG5048   423 PCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDL 461
zf-H2C2_2 pfam13465
Zinc-finger double domain;
240-265 1.35e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.35e-04
                          10        20
                  ....*....|....*....|....*.
gi 1958726021 240 SLTQHQRIHTGEKPYKCDECGKAFSQ 265
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 560-612 3.77e-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: 3.77e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958726021 560 KPYaCPKCGKTFRHCSSLAQHQKThtegKHYQCNKCEKTFSQKSHLTQH-QQVH 612
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKA----KHFKCHICHKKLYTAGGLAVHcLQVH 49
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 122-272 4.62e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 43.17  E-value: 4.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958726021 122 TEKTMRPSYE---KDLGVSA---GLLTQTDIAVDQTSTNtraKQSSRPgqkeKLCKCNEcgkafTYCSALIRHQRThTGE 195
Cdd:COG5189   281 EESSLGFDYEfihKSVGNKEirgGISTGEMIDVRKLPCT---NSSSNG----KLAHGGE-----RNIDTPSRMLKV-KDG 347

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958726021 196 KPYKCN--DCNKAFsRNENLINHQRIHtgdkpykcDQCGKGFIEGPSLTQHQRIHTGEKPYKCDECGKAFSQRTHLVQH 272
Cdd:COG5189   348 KPYKCPveGCNKKY-KNQNGLKYHMLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKYH 417
zf-H2C2_2 pfam13465
Zinc-finger double domain;
184-209 7.11e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 7.11e-04
                          10        20
                  ....*....|....*....|....*.
gi 1958726021 184 ALIRHQRTHTGEKPYKCNDCNKAFSR 209
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
28-81 1.23e-21

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 88.80  E-value: 1.23e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958726021   28 VTFKDVVVNFTQEEWKHLDPTQRDLFRDVTLENYTHLVSIDWKIRPENSVSPLE 81
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLE 54
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 27-68 4.91e-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: 86.37  E-value: 4.91e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958726021  27 SVTFKDVVVNFTQEEWKHLDPTQRDLFRDVTLENYTHLVSID 68
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 28-67 2.53e-18

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: 78.75  E-value: 2.53e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1958726021  28 VTFKDVVVNFTQEEWKHLDPTQRDLFRDVTLENYTHLVSI 67
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
252-660 3.28e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 69.34  E-value: 3.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958726021 252 KPYKCDECGKAFSQRTHLVQHQRIHTGEKPYTCN--ECGKSFSQRGHFMEHQKIHTGEKPFKCEECEKTFTRST-HLTQH 328
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKAsSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958726021 329 QKIHTGEKTYKCNECGKAFNGPSTFIRHHMIHT---GEKPYECNECGKAFSQhSNLTQHQKTHTgekpydcAECGKAFSY 405
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISnlrNNPLPGNNSSSVNTPQ-SNSLHPPLPAN-------SLSKDPSSN 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958726021 406 WSSLAQHLKIHTGEKPYKCSDCGKAFSYcSSLTQHRRIHTREKPFECSECGKAFSYLSNLNQHQKTHTQEKAYECKECG- 484
Cdd:COG5048   184 LSLLISSNVSTSIPSSSENSPLSSSYSI-PSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPr 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958726021 485 -----KAFIRSSSLAKHERIHTG-EKPYQCLECGKTFSYGSSLIQHK--KIHTGE--RPYKCNE--CERAFNQKIHLTQH 552
Cdd:COG5048   263 sslptASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPYslCGKLFSRNDALKRH 342

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958726021 553 KRIHTGVKPYACP--KCGKTFRHCS------SLAQHQKTHTEGKHYQC-NKCEKTFSQKSHLTQHQQVHMGEKP--YKCN 621
Cdd:COG5048   343 ILLHTSISPAKEKllNSSSKFSPLLnneppqSLQQYKDLKNDKKSETLsNSCIRNFKRDSNLSLHIITHLSFRPynCKNP 422

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1958726021 622 DCDRCFTQSTHLTEHQSIHTGEKPYSSNVCPQTFNQNTY 660
Cdd:COG5048   423 PCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDL 461
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
171-603 3.49e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 69.34  E-value: 3.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958726021 171 KCNECGKAFTYCSALIRHQRTHTGEKPYKCND--CNKAFSRNENLINHQRIHTGDKPYKCDQCGKGFIEGPSLTQHQRIH 248
Cdd:COG5048    35 SCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLSSSS 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958726021 249 TGEkPYKCDECGKAFSQRTHLVQHQRIHTGEKpYTCNECGKSFSQRGHFMEHQKIHtGEKPFKCEECEKTFTRSTHLtqH 328
Cdd:COG5048   115 SNS-NDNNLLSSHSLPPSSRDPQLPDLLSISN-LRNNPLPGNNSSSVNTPQSNSLH-PPLPANSLSKDPSSNLSLLI--S 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958726021 329 QKIHTGEKTYKCNECGKAFNGPSTFIRHHMIHTGEKPYECNECGKAFSQHSNLTQHQKTHTGEKPYDCAEC-----GKAF 403
Cdd:COG5048   190 SNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESprsslPTAS 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958726021 404 SYWSSLAQHL--KIHTGEKPYKCSDCGKAFSYCSSLTQHRR--IHTRE--KPFECSE--CGKAFSYLSNLNQHQKTHTQE 475
Cdd:COG5048   270 SQSSSPNESDssSEKGFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSI 349

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958726021 476 KAYECKecgkaFIRSSSLAKherihtgekpyqclecGKTFSYGSSLIQHKKIHTGERPYKC--NECERAFNQKIHLTQHK 553
Cdd:COG5048   350 SPAKEK-----LLNSSSKFS----------------PLLNNEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHI 408

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958726021 554 RIHTGVKPYAC--PKCGKTFRHCSSLAQHQKTHTEGKHYQCNKCEKTFSQKS 603
Cdd:COG5048   409 ITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
364-676 1.30e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 67.41  E-value: 1.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958726021 364 KPYECNECGKAFSQHSNLTQHQKTHTGEKPYDCA--ECGKAFSYWSSLAQHLKIHTGEKPYKCSD-CGKAFSYCSSLTQH 440
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKsLPLSNSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958726021 441 RRIHTREKPFECSECGKAFSYLSNLNQHQKTHTQEKAYECKEC-GKAFIRSSSLAKHERIHTGEKpyqcleCGKTFSYGS 519
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnSSSVNTPQSNSLHPPLPANSL------SKDPSSNLS 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958726021 520 SLIQHKKIHTGERPYKCNECERaFNQKIHLTQHKRIHTGVKPYACPKCGKTFRHCSSLAQHQKTHTEGKHYQCNKCEKTF 599
Cdd:COG5048   186 LLISSNVSTSIPSSSENSPLSS-SYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSS 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958726021 600 SQKSHLTQHQQVHMGE-------KPYKCNDCDRCFTQSTHLTEHQ--SIHTGE--KPYS--SNVCPQTFNQNTYLTQHQK 666
Cdd:COG5048   265 LPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFScpYSLCGKLFSRNDALKRHIL 344

                         330
                  ....*....|
gi 1958726021 667 IHSGEKSFVC 676
Cdd:COG5048   345 LHTSISPAKE 354
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
160-357 2.29e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.38  E-value: 2.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958726021 160 SSRPGQKEKLCKCNECGKAFTYCSALIRHQRT--HTGE--KPYKC--NDCNKAFSRNENLINHQRIHTGDKPYKCDQCGK 233
Cdd:COG5048   280 SSSEKGFSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKLLNS 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958726021 234 GFIEGPSLTQhqrihtgekpykcdecgkafSQRTHLVQHQRIHTGEKPYTC-NECGKSFSQRGHFMEHQKIHTGEKP--F 310
Cdd:COG5048   360 SSKFSPLLNN--------------------EPPQSLQQYKDLKNDKKSETLsNSCIRNFKRDSNLSLHIITHLSFRPynC 419

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958726021 311 KCEECEKTFTRSTHLTQHQKIHTgEKTYKCNECGKAFNGPSTFIRHH 357
Cdd:COG5048   420 KNPPCSKSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLSNHG 465
zf-H2C2_2 pfam13465
Zinc-finger double domain;
240-265 1.35e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.35e-04
                          10        20
                  ....*....|....*....|....*.
gi 1958726021 240 SLTQHQRIHTGEKPYKCDECGKAFSQ 265
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
268-293 2.56e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.56e-04
                          10        20
                  ....*....|....*....|....*.
gi 1958726021 268 HLVQHQRIHTGEKPYTCNECGKSFSQ 293
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 560-612 3.77e-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: 3.77e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958726021 560 KPYaCPKCGKTFRHCSSLAQHQKThtegKHYQCNKCEKTFSQKSHLTQH-QQVH 612
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKA----KHFKCHICHKKLYTAGGLAVHcLQVH 49
zf-H2C2_2 pfam13465
Zinc-finger double domain;
408-433 4.40e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 4.40e-04
                          10        20
                  ....*....|....*....|....*.
gi 1958726021 408 SLAQHLKIHTGEKPYKCSDCGKAFSY 433
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 122-272 4.62e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 43.17  E-value: 4.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958726021 122 TEKTMRPSYE---KDLGVSA---GLLTQTDIAVDQTSTNtraKQSSRPgqkeKLCKCNEcgkafTYCSALIRHQRThTGE 195
Cdd:COG5189   281 EESSLGFDYEfihKSVGNKEirgGISTGEMIDVRKLPCT---NSSSNG----KLAHGGE-----RNIDTPSRMLKV-KDG 347

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958726021 196 KPYKCN--DCNKAFsRNENLINHQRIHtgdkpykcDQCGKGFIEGPSLTQHQRIHTGEKPYKCDECGKAFSQRTHLVQH 272
Cdd:COG5189   348 KPYKCPveGCNKKY-KNQNGLKYHMLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKYH 417
zf-H2C2_2 pfam13465
Zinc-finger double domain;
184-209 7.11e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 7.11e-04
                          10        20
                  ....*....|....*....|....*.
gi 1958726021 184 ALIRHQRTHTGEKPYKCNDCNKAFSR 209
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
548-573 7.47e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 7.47e-04
                          10        20
                  ....*....|....*....|....*.
gi 1958726021 548 HLTQHKRIHTGVKPYACPKCGKTFRH 573
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
296-321 8.24e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 8.24e-04
                          10        20
                  ....*....|....*....|....*.
gi 1958726021 296 HFMEHQKIHTGEKPFKCEECEKTFTR 321
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
380-405 9.09e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 9.09e-04
                          10        20
                  ....*....|....*....|....*.
gi 1958726021 380 NLTQHQKTHTGEKPYDCAECGKAFSY 405
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
492-517 9.93e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 9.93e-04
                          10        20
                  ....*....|....*....|....*.
gi 1958726021 492 SLAKHERIHTGEKPYQCLECGKTFSY 517
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
464-489 1.70e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.70e-03
                          10        20
                  ....*....|....*....|....*.
gi 1958726021 464 NLNQHQKTHTQEKAYECKECGKAFIR 489
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 306-389 2.02e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 41.24  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958726021 306 GEKPFKCE--ECEKTFTRSTHLTQHQKI-HTGEKTYKcnecgkafnGPSTfIRHHMIHTGEKPYECNECGKAFSQHSNLT 382
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLKYHMLHgHQNQKLHE---------NPSP-EKMNIFSAKDKPYRCEVCDKRYKNLNGLK 415


                  ....*..
gi 1958726021 383 QHQKTHT 389
Cdd:COG5189   416 YHRKHSH 422
zf-H2C2_2 pfam13465
Zinc-finger double domain;
324-348 2.14e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.14e-03
                          10        20
                  ....*....|....*....|....*
gi 1958726021 324 HLTQHQKIHTGEKTYKCNECGKAFN 348
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
212-235 2.22e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.22e-03
                          10        20
                  ....*....|....*....|....
gi 1958726021 212 NLINHQRIHTGDKPYKCDQCGKGF 235
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
436-461 2.68e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.68e-03
                          10        20
                  ....*....|....*....|....*.
gi 1958726021 436 SLTQHRRIHTREKPFECSECGKAFSY 461
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
520-545 2.81e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.81e-03
                          10        20
                  ....*....|....*....|....*.
gi 1958726021 520 SLIQHKKIHTGERPYKCNECERAFNQ 545
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 308-348 2.89e-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: 37.15  E-value: 2.89e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958726021 308 KPFkCEECEKTFTRSTHLTQHQKihtgEKTYKCNECGKAFN 348
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQK----AKHFKCHICHKKLY 36
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 366-388 4.62e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 4.62e-03
                          10        20
                  ....*....|....*....|...
gi 1958726021 366 YECNECGKAFSQHSNLTQHQKTH 388
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 198-220 4.99e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 4.99e-03
                          10        20
                  ....*....|....*....|...
gi 1958726021 198 YKCNDCNKAFSRNENLINHQRIH 220
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
355-377 6.11e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 6.11e-03
                          10        20
                  ....*....|....*....|...
gi 1958726021 355 RHHMIHTGEKPYECNECGKAFSQ 377
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 590-612 8.91e-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: 8.91e-03
                          10        20
                  ....*....|....*....|...
gi 1958726021 590 YQCNKCEKTFSQKSHLTQHQQVH 612
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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