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Conserved domains on  [gi|37693525|ref|NP_003443|]
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zinc finger protein 189 isoform 1 [Homo sapiens]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12016931)

KRAB (Kruppel-associated box) domain-containing zinc finger protein (KRAB-ZFP) plays important roles in cell differentiation and organ development and in regulating viral replication and transcription

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 13-54 4.30e-24

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: 94.84  E-value: 4.30e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 37693525    13 LLTFEDVAVFFTQEEWDYLDPAQRSLYKDVMMENYGNLVSLD 54
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
138-524 1.57e-17

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 85.52  E-value: 1.57e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37693525 138 RKRPNSEEKCHKCEECGKGFVRKAHFIQHQRVHTGEKPFQCN--ECGKSFSRSSFVIEHQRIHTGERPYECNYCG----- 210
Cdd:COG5048  24 LKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLplsns 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37693525 211 ---------------KTFSVSSTLIRHQRIHTGERP------YQCNQCKQSFSQR------------------------- 244
Cdd:COG5048 104 kasssslsssssnsnDNNLLSSHSLPPSSRDPQLPDllsisnLRNNPLPGNNSSSvntpqsnslhpplpanslskdpssn 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37693525 245 RSLVKHQRIHTGEKPHKCSDCGKAFSWKSHLIEHQRTHTGEKPYHCTKCKKSFSRNSLLVEHQRIHTGERPHKCGECGKA 324
Cdd:COG5048 184 LSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRS 263

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37693525 325 FRLSTYLIQHQKIHTGE-------KPFLCIECGKSFSRSSFLIEHQR--IHTGE--RPYQCKE--CGKSFSQLCNLTRHQ 391
Cdd:COG5048 264 SLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHI 343

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37693525 392 RIHTGDKPHKC--EECGKAFSRSSGLIQHQRIHtrektyPYNETKESfDPNCSLVIQQEVYPKEKSYkcdecgktfsVSA 469
Cdd:COG5048 344 LLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQ------QYKDLKND-KKSETLSNSCIRNFKRDSN----------LSL 406

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*
gi 37693525 470 HLVQHQRIHTGEKPylCTVCGKSFSRSSFLIEHQRIHTGERPYLCRQCGKSFSQL 524
Cdd:COG5048 407 HIITHLSFRPYNCK--NPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDL 459
zf-H2C2_2 pfam13465
Zinc-finger double domain;
555-579 2.23e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.23e-04
                          10        20
                  ....*....|....*....|....*
gi 37693525   555 LIQHQRIHTGEKPYKCEKCDKSFSQ 579
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
526-551 2.54e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.54e-03
                          10        20
                  ....*....|....*....|....*.
gi 37693525   526 NLIRHQGVHTGNKPHKCDECGKAFSR 551
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 13-54 4.30e-24

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: 94.84  E-value: 4.30e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 37693525    13 LLTFEDVAVFFTQEEWDYLDPAQRSLYKDVMMENYGNLVSLD 54
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
14-68 3.43e-23

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 93.04  E-value: 3.43e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 37693525     14 LTFEDVAVFFTQEEWDYLDPAQRSLYKDVMMENYGNLVSLDVLNRDKDEEPTVKQ 68
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQ 55
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 14-53 9.81e-22

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: 87.99  E-value: 9.81e-22
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 37693525  14 LTFEDVAVFFTQEEWDYLDPAQRSLYKDVMMENYGNLVSL 53
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
138-524 1.57e-17

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 85.52  E-value: 1.57e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37693525 138 RKRPNSEEKCHKCEECGKGFVRKAHFIQHQRVHTGEKPFQCN--ECGKSFSRSSFVIEHQRIHTGERPYECNYCG----- 210
Cdd:COG5048  24 LKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLplsns 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37693525 211 ---------------KTFSVSSTLIRHQRIHTGERP------YQCNQCKQSFSQR------------------------- 244
Cdd:COG5048 104 kasssslsssssnsnDNNLLSSHSLPPSSRDPQLPDllsisnLRNNPLPGNNSSSvntpqsnslhpplpanslskdpssn 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37693525 245 RSLVKHQRIHTGEKPHKCSDCGKAFSWKSHLIEHQRTHTGEKPYHCTKCKKSFSRNSLLVEHQRIHTGERPHKCGECGKA 324
Cdd:COG5048 184 LSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRS 263

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37693525 325 FRLSTYLIQHQKIHTGE-------KPFLCIECGKSFSRSSFLIEHQR--IHTGE--RPYQCKE--CGKSFSQLCNLTRHQ 391
Cdd:COG5048 264 SLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHI 343

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37693525 392 RIHTGDKPHKC--EECGKAFSRSSGLIQHQRIHtrektyPYNETKESfDPNCSLVIQQEVYPKEKSYkcdecgktfsVSA 469
Cdd:COG5048 344 LLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQ------QYKDLKND-KKSETLSNSCIRNFKRDSN----------LSL 406

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*
gi 37693525 470 HLVQHQRIHTGEKPylCTVCGKSFSRSSFLIEHQRIHTGERPYLCRQCGKSFSQL 524
Cdd:COG5048 407 HIITHLSFRPYNCK--NPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDL 459
zf-H2C2_2 pfam13465
Zinc-finger double domain;
386-411 5.65e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 5.65e-05
                          10        20
                  ....*....|....*....|....*.
gi 37693525   386 NLTRHQRIHTGDKPHKCEECGKAFSR 411
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
555-579 2.23e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.23e-04
                          10        20
                  ....*....|....*....|....*
gi 37693525   555 LIQHQRIHTGEKPYKCEKCDKSFSQ 579
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
526-551 2.54e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.54e-03
                          10        20
                  ....*....|....*....|....*.
gi 37693525   526 NLIRHQGVHTGNKPHKCDECGKAFSR 551
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 202-254 7.94e-03

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 35.61  E-value: 7.94e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 37693525 202 RPYeCNYCGKTFSVSSTLIRHQRIHTgerpYQCNQCKQSFSQRRSLVKH-QRIH 254
Cdd:cd20908   1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
 
Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 13-54 4.30e-24

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: 94.84  E-value: 4.30e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 37693525    13 LLTFEDVAVFFTQEEWDYLDPAQRSLYKDVMMENYGNLVSLD 54
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
14-68 3.43e-23

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 93.04  E-value: 3.43e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 37693525     14 LTFEDVAVFFTQEEWDYLDPAQRSLYKDVMMENYGNLVSLDVLNRDKDEEPTVKQ 68
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQ 55
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 14-53 9.81e-22

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: 87.99  E-value: 9.81e-22
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 37693525  14 LTFEDVAVFFTQEEWDYLDPAQRSLYKDVMMENYGNLVSL 53
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
138-524 1.57e-17

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 85.52  E-value: 1.57e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37693525 138 RKRPNSEEKCHKCEECGKGFVRKAHFIQHQRVHTGEKPFQCN--ECGKSFSRSSFVIEHQRIHTGERPYECNYCG----- 210
Cdd:COG5048  24 LKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLplsns 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37693525 211 ---------------KTFSVSSTLIRHQRIHTGERP------YQCNQCKQSFSQR------------------------- 244
Cdd:COG5048 104 kasssslsssssnsnDNNLLSSHSLPPSSRDPQLPDllsisnLRNNPLPGNNSSSvntpqsnslhpplpanslskdpssn 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37693525 245 RSLVKHQRIHTGEKPHKCSDCGKAFSWKSHLIEHQRTHTGEKPYHCTKCKKSFSRNSLLVEHQRIHTGERPHKCGECGKA 324
Cdd:COG5048 184 LSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRS 263

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37693525 325 FRLSTYLIQHQKIHTGE-------KPFLCIECGKSFSRSSFLIEHQR--IHTGE--RPYQCKE--CGKSFSQLCNLTRHQ 391
Cdd:COG5048 264 SLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHI 343

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37693525 392 RIHTGDKPHKC--EECGKAFSRSSGLIQHQRIHtrektyPYNETKESfDPNCSLVIQQEVYPKEKSYkcdecgktfsVSA 469
Cdd:COG5048 344 LLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQ------QYKDLKND-KKSETLSNSCIRNFKRDSN----------LSL 406

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*
gi 37693525 470 HLVQHQRIHTGEKPylCTVCGKSFSRSSFLIEHQRIHTGERPYLCRQCGKSFSQL 524
Cdd:COG5048 407 HIITHLSFRPYNCK--NPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDL 459
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
230-622 4.13e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 72.04  E-value: 4.13e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37693525 230 RPYQCNQCKQSFSQRRSLVKHQRIHTGEKPHKCSD--CGKAFSWKSHLIEHQRTHTGEKPYhcTKCKKSFSRNSLLVEHQ 307
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSD--LNSKSLPLSNSKASSSS 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37693525 308 RIHtgerphkcgeCGKAFRLSTYLIQHQKIHTGEKPFLCIECGKSFSRSSFLIEHQRIHTGERPYQCK-------ECGKS 380
Cdd:COG5048 110 LSS----------SSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLhpplpanSLSKD 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37693525 381 FSQLCNLTRHQRIHTGDKPHKCEECGKAFSRSSGLIQHQRIHTREKTYPYNETKESFDPNCSLVIQQEVYPKEKSYKCDE 460
Cdd:COG5048 180 PSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASE 259

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37693525 461 CGKTFSVSAHLVQHQRIHTGE-------KPYLCTVCGKSFSRSSFLIEHQR--IHTGE--RPYLCR--QCGKSFSQLCNL 527
Cdd:COG5048 260 SPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPysLCGKLFSRNDAL 339

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37693525 528 IRHQGVHTGNKPHKC--DECGKAFSRNS-----GLIQHQRIHTGEKPYKCE--KCDKSFSQQRSLVNHQKIHAEVKTQET 598
Cdd:COG5048 340 KRHILLHTSISPAKEklLNSSSKFSPLLnneppQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNC 419

                       410       420
                ....*....|....*....|....
gi 37693525 599 HeCDACGEAFNCRISLIQHQKLHT 622
Cdd:COG5048 420 K-NPPCSKSFNRHYNLIPHKKIHT 442
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
121-358 3.10e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 59.71  E-value: 3.10e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37693525 121 ESLTQEQRMFRENTNIIRKRPNSE---EKCHKCEECGKGFVRKAHFIQHQRVHTGE-------KPFQCNECGKSFSRSSF 190
Cdd:COG5048 225 SSLPLTTNSQLSPKSLLSQSPSSLsssDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSP 304

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37693525 191 VIEHQR--IHTGE--RPYEC--NYCGKTFSVSSTLIRHQRIHTGERPYQCNQCKQSFSQRRSLvkhqrihtGEKPHKCSD 264
Cdd:COG5048 305 LTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLL--------NNEPPQSLQ 376

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37693525 265 cgkafswKSHLIEHQRTHTGEKPyhctKCKKSFSRNSLLVEHQRIHTGERPH--KCGECGKAFRLSTYLIQHQKIHTGEK 342
Cdd:COG5048 377 -------QYKDLKNDKKSETLSN----SCIRNFKRDSNLSLHIITHLSFRPYncKNPPCSKSFNRHYNLIPHKKIHTNHA 445

                       250
                ....*....|....*.
gi 37693525 343 PFLCIECGKSFSRSSF 358
Cdd:COG5048 446 PLLCSILKSFRRDLDL 461
zf-H2C2_2 pfam13465
Zinc-finger double domain;
386-411 5.65e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 5.65e-05
                          10        20
                  ....*....|....*....|....*.
gi 37693525   386 NLTRHQRIHTGDKPHKCEECGKAFSR 411
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
555-579 2.23e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.23e-04
                          10        20
                  ....*....|....*....|....*
gi 37693525   555 LIQHQRIHTGEKPYKCEKCDKSFSQ 579
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
470-495 3.30e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.30e-04
                          10        20
                  ....*....|....*....|....*.
gi 37693525   470 HLVQHQRIHTGEKPYLCTVCGKSFSR 495
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 480-558 3.56e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 43.55  E-value: 3.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37693525 480 GEKPYLCTV--CGKSFsRSSFLIEHQRIHTgerpylcrQCGKSFSQLCNLIRHQGVHTGNKPHKCDECGKAFSRNSGLIQ 557
Cdd:COG5189 346 DGKPYKCPVegCNKKY-KNQNGLKYHMLHG--------HQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                .
gi 37693525 558 H 558
Cdd:COG5189 417 H 417
zf-H2C2_2 pfam13465
Zinc-finger double domain;
359-383 5.34e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 5.34e-04
                          10        20
                  ....*....|....*....|....*
gi 37693525   359 LIEHQRIHTGERPYQCKECGKSFSQ 383
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
246-270 7.24e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 7.24e-04
                          10        20
                  ....*....|....*....|....*
gi 37693525   246 SLVKHQRIHTGEKPHKCSDCGKAFS 270
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
274-299 7.91e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 7.91e-04
                          10        20
                  ....*....|....*....|....*.
gi 37693525   274 HLIEHQRTHTGEKPYHCTKCKKSFSR 299
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
330-355 9.25e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 9.25e-04
                          10        20
                  ....*....|....*....|....*.
gi 37693525   330 YLIQHQKIHTGEKPFLCIECGKSFSR 355
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
162-187 1.21e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.21e-03
                          10        20
                  ....*....|....*....|....*.
gi 37693525   162 HFIQHQRVHTGEKPFQCNECGKSFSR 187
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 372-394 1.96e-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: 1.96e-03
                          10        20
                  ....*....|....*....|...
gi 37693525   372 YQCKECGKSFSQLCNLTRHQRIH 394
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
526-551 2.54e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.54e-03
                          10        20
                  ....*....|....*....|....*.
gi 37693525   526 NLIRHQGVHTGNKPHKCDECGKAFSR 551
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
499-523 2.54e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.54e-03
                          10        20
                  ....*....|....*....|....*
gi 37693525   499 LIEHQRIHTGERPYLCRQCGKSFSQ 523
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
303-325 3.38e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.38e-03
                          10        20
                  ....*....|....*....|...
gi 37693525   303 LVEHQRIHTGERPHKCGECGKAF 325
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 204-226 3.47e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.35  E-value: 3.47e-03
                          10        20
                  ....*....|....*....|...
gi 37693525   204 YECNYCGKTFSVSSTLIRHQRIH 226
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
219-243 4.41e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.41e-03
                          10        20
                  ....*....|....*....|....*
gi 37693525   219 LIRHQRIHTGERPYQCNQCKQSFSQ 243
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
193-214 4.72e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.72e-03
                          10        20
                  ....*....|....*....|..
gi 37693525   193 EHQRIHTGERPYECNYCGKTFS 214
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 400-422 7.60e-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: 7.60e-03
                          10        20
                  ....*....|....*....|...
gi 37693525   400 HKCEECGKAFSRSSGLIQHQRIH 422
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 202-254 7.94e-03

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 35.61  E-value: 7.94e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 37693525 202 RPYeCNYCGKTFSVSSTLIRHQRIHTgerpYQCNQCKQSFSQRRSLVKH-QRIH 254
Cdd:cd20908   1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 540-562 8.39e-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: 8.39e-03
                          10        20
                  ....*....|....*....|...
gi 37693525   540 HKCDECGKAFSRNSGLIQHQRIH 562
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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