NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1785412681|ref|XP_031748864|]
View 

oocyte zinc finger protein XlCOF7.1-like [Xenopus tropicalis]

Protein Classification

KRAB_A-box and COG5048 domain-containing protein( domain architecture ID 11640445)

protein containing domains KRAB_A-box, SFP1, and COG5048

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
316-678 3.25e-09

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 59.71  E-value: 3.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412681 316 KPLSCSECGKCFSHRSNFARHLRTHTGEKPYSCS--ECGKCFSHPFNFARHRKTHTG--------------EKTFPCSVC 379
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNnpsdlnskslplsnSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412681 380 GKIFATPSELTLHQQEI-HMEEKPFPCLKCGKSFASSSDLTAHRRQIHTEEKPFS------CTECGKCFSVEAFLVRHQR 452
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLpPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSlhpplpANSLSKDPSSNLSLLISSN 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412681 453 THTKEKPFSCPECGKCFSHPSNLTRHRRIhrgEKPFSCSECDKCYATPSELTVHHRRTHTGeKPFSCSECGKCFATSSIL 532
Cdd:COG5048   192 VSTSIPSSSENSPLSSSYSIPSSSSDQNL---ENSSSSLPLTTNSQLSPKSLLSQSPSSLS-SSDSSSSASESPRSSLPT 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412681 533 IVHYRTH----------TGEKPFSCSECGKCFATSSALTVHHRRT-HTGE--KPFPCSE--CGKCFSTSSLLTVHYRTHT 597
Cdd:COG5048   268 ASSQSSSpnesdsssekGFSLPIKSKQCNISFSRSSPLTRHLRSVnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHT 347

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412681 598 GERPYPC--SECGKCFTTK-----AELIAHRRRMHAEKLFTCL--KCGKSFATAPLLATHQRTHV----KPFSCTECGKC 664
Cdd:COG5048   348 SISPAKEklLNSSSKFSPLlnnepPQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLsfrpYNCKNPPCSKS 427

                         410
                  ....*....|....
gi 1785412681 665 FSRRIYLTHHQRTH 678
Cdd:COG5048   428 FNRHYNLIPHKKIH 441
KRAB_A-box super family cl02581
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 88-117 3.47e-05

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.


The actual alignment was detected with superfamily member cd07765:

Pssm-ID: 470626  Cd Length: 40  Bit Score: 41.38  E-value: 3.47e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1785412681  88 IRCEDVSIYFSLEEWEYIK-GNKALYREGIK 117
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDpAQRDLYRDVML 31
SFP1 super family cl25788
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 125-426 2.83e-03

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: 40.86  E-value: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412681 125 QLHPLACEYkdGSDVTAHTEATLCCNNDGNLTNPDVSPVEQPPPANGIKEASNKGGNQSDCSINPQIQGTDTPTpIMGCS 204
Cdd:COG5189   142 QVHTSGAVP--TPSVMGSATASSTTANPSITGAPGLLVDAVDVPHNKQINSNNNSTSHNSNMGSKNAKMNDSSK-LKKLS 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412681 205 LNISLSanyiaNDIKEEAASREGGSQSDCSINPLTEQIQGTDTPTPIMGYSTISSLF---KMKGNKNHEDAHwSPDKSDI 281
Cdd:COG5189   219 LIEEKK-----FPERVRSRYIDIGHMMDTHQFYLEDVDLMDDDILGPSNEEMLYKYIspsQGSAELFEESSL-GFDYEFI 292

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412681 282 TENAVSGKYSCNechihFSSKRDFDKhlrthkREKPLSCSECGKCFSHRSNF-----ARHLRThTGEKPYSCS--ECGKC 354
Cdd:COG5189   293 HKSVGNKEIRGG-----ISTGEMIDV------RKLPCTNSSSNGKLAHGGERnidtpSRMLKV-KDGKPYKCPveGCNKK 360

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785412681 355 FSHPFNFARHRKT-HTGEKTFPcsvcgkifaTPSELTLhqQEIHMEEKPFPCLKCGKSFASSSDLTAHRRQIH 426
Cdd:COG5189   361 YKNQNGLKYHMLHgHQNQKLHE---------NPSPEKM--NIFSAKDKPYRCEVCDKRYKNLNGLKYHRKHSH 422
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
316-678 3.25e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 59.71  E-value: 3.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412681 316 KPLSCSECGKCFSHRSNFARHLRTHTGEKPYSCS--ECGKCFSHPFNFARHRKTHTG--------------EKTFPCSVC 379
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNnpsdlnskslplsnSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412681 380 GKIFATPSELTLHQQEI-HMEEKPFPCLKCGKSFASSSDLTAHRRQIHTEEKPFS------CTECGKCFSVEAFLVRHQR 452
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLpPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSlhpplpANSLSKDPSSNLSLLISSN 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412681 453 THTKEKPFSCPECGKCFSHPSNLTRHRRIhrgEKPFSCSECDKCYATPSELTVHHRRTHTGeKPFSCSECGKCFATSSIL 532
Cdd:COG5048   192 VSTSIPSSSENSPLSSSYSIPSSSSDQNL---ENSSSSLPLTTNSQLSPKSLLSQSPSSLS-SSDSSSSASESPRSSLPT 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412681 533 IVHYRTH----------TGEKPFSCSECGKCFATSSALTVHHRRT-HTGE--KPFPCSE--CGKCFSTSSLLTVHYRTHT 597
Cdd:COG5048   268 ASSQSSSpnesdsssekGFSLPIKSKQCNISFSRSSPLTRHLRSVnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHT 347

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412681 598 GERPYPC--SECGKCFTTK-----AELIAHRRRMHAEKLFTCL--KCGKSFATAPLLATHQRTHV----KPFSCTECGKC 664
Cdd:COG5048   348 SISPAKEklLNSSSKFSPLlnnepPQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLsfrpYNCKNPPCSKS 427

                         410
                  ....*....|....
gi 1785412681 665 FSRRIYLTHHQRTH 678
Cdd:COG5048   428 FNRHYNLIPHKKIH 441
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 88-117 3.47e-05

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: 41.38  E-value: 3.47e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1785412681  88 IRCEDVSIYFSLEEWEYIK-GNKALYREGIK 117
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDpAQRDLYRDVML 31
zf-H2C2_2 pfam13465
Zinc-finger double domain;
447-471 1.43e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.43e-04
                          10        20
                  ....*....|....*....|....*
gi 1785412681 447 LVRHQRTHTKEKPFSCPECGKCFSH 471
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 515-567 1.31e-03

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 38.31  E-value: 1.31e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1785412681 515 KPFsCSECGKCFATSSILIVHYRTHTgekpFSCSECGKCFATSSALTVH----HRRT 567
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHclqvHKET 52
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 125-426 2.83e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.86  E-value: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412681 125 QLHPLACEYkdGSDVTAHTEATLCCNNDGNLTNPDVSPVEQPPPANGIKEASNKGGNQSDCSINPQIQGTDTPTpIMGCS 204
Cdd:COG5189   142 QVHTSGAVP--TPSVMGSATASSTTANPSITGAPGLLVDAVDVPHNKQINSNNNSTSHNSNMGSKNAKMNDSSK-LKKLS 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412681 205 LNISLSanyiaNDIKEEAASREGGSQSDCSINPLTEQIQGTDTPTPIMGYSTISSLF---KMKGNKNHEDAHwSPDKSDI 281
Cdd:COG5189   219 LIEEKK-----FPERVRSRYIDIGHMMDTHQFYLEDVDLMDDDILGPSNEEMLYKYIspsQGSAELFEESSL-GFDYEFI 292

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412681 282 TENAVSGKYSCNechihFSSKRDFDKhlrthkREKPLSCSECGKCFSHRSNF-----ARHLRThTGEKPYSCS--ECGKC 354
Cdd:COG5189   293 HKSVGNKEIRGG-----ISTGEMIDV------RKLPCTNSSSNGKLAHGGERnidtpSRMLKV-KDGKPYKCPveGCNKK 360

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785412681 355 FSHPFNFARHRKT-HTGEKTFPcsvcgkifaTPSELTLhqQEIHMEEKPFPCLKCGKSFASSSDLTAHRRQIH 426
Cdd:COG5189   361 YKNQNGLKYHMLHgHQNQKLHE---------NPSPEKM--NIFSAKDKPYRCEVCDKRYKNLNGLKYHRKHSH 422
KRAB smart00349
krueppel associated box;
91-117 3.04e-03

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 36.42  E-value: 3.04e-03
                           10        20
                   ....*....|....*....|....*...
gi 1785412681   91 EDVSIYFSLEEWEYIK-GNKALYREGIK 117
Cdd:smart00349   4 EDVAVYFTQEEWEQLDpAQKNLYRDVML 31
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
316-678 3.25e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 59.71  E-value: 3.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412681 316 KPLSCSECGKCFSHRSNFARHLRTHTGEKPYSCS--ECGKCFSHPFNFARHRKTHTG--------------EKTFPCSVC 379
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNnpsdlnskslplsnSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412681 380 GKIFATPSELTLHQQEI-HMEEKPFPCLKCGKSFASSSDLTAHRRQIHTEEKPFS------CTECGKCFSVEAFLVRHQR 452
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLpPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSlhpplpANSLSKDPSSNLSLLISSN 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412681 453 THTKEKPFSCPECGKCFSHPSNLTRHRRIhrgEKPFSCSECDKCYATPSELTVHHRRTHTGeKPFSCSECGKCFATSSIL 532
Cdd:COG5048   192 VSTSIPSSSENSPLSSSYSIPSSSSDQNL---ENSSSSLPLTTNSQLSPKSLLSQSPSSLS-SSDSSSSASESPRSSLPT 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412681 533 IVHYRTH----------TGEKPFSCSECGKCFATSSALTVHHRRT-HTGE--KPFPCSE--CGKCFSTSSLLTVHYRTHT 597
Cdd:COG5048   268 ASSQSSSpnesdsssekGFSLPIKSKQCNISFSRSSPLTRHLRSVnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHT 347

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412681 598 GERPYPC--SECGKCFTTK-----AELIAHRRRMHAEKLFTCL--KCGKSFATAPLLATHQRTHV----KPFSCTECGKC 664
Cdd:COG5048   348 SISPAKEklLNSSSKFSPLlnnepPQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLsfrpYNCKNPPCSKS 427

                         410
                  ....*....|....
gi 1785412681 665 FSRRIYLTHHQRTH 678
Cdd:COG5048   428 FNRHYNLIPHKKIH 441
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 88-117 3.47e-05

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: 41.38  E-value: 3.47e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1785412681  88 IRCEDVSIYFSLEEWEYIK-GNKALYREGIK 117
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDpAQRDLYRDVML 31
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
456-513 6.99e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.84  E-value: 6.99e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412681 456 KEKPFSCPECGKCFSHPSNLTRHRRIHRGEKPFSCS--ECDKCYATPSELTVHHRRTHTG 513
Cdd:COG5048    30 APRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNN 89
zf-H2C2_2 pfam13465
Zinc-finger double domain;
447-471 1.43e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.43e-04
                          10        20
                  ....*....|....*....|....*
gi 1785412681 447 LVRHQRTHTKEKPFSCPECGKCFSH 471
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
332-357 1.60e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.60e-04
                          10        20
                  ....*....|....*....|....*.
gi 1785412681 332 NFARHLRTHTGEKPYSCSECGKCFSH 357
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
411-491 1.86e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.69  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412681 411 SFASSSDLTAHRRQIHTEEKPFSCTECGKCFSVEAFLVRHQRTHTKEKPFSC--PECGKCFSHPSNLTRHRRIHRGEKPF 488
Cdd:COG5048    13 NSVLSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSD 92


                  ...
gi 1785412681 489 SCS 491
Cdd:COG5048    93 LNS 95
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 460-482 2.93e-04

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 38.44  E-value: 2.93e-04
                          10        20
                  ....*....|....*....|...
gi 1785412681 460 FSCPECGKCFSHPSNLTRHRRIH 482
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
344-684 8.13e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.38  E-value: 8.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412681 344 KPYSCSECGKCFSHPFNFARHRKTHTGEKTFPCSV--CGKIFATPSELTLHQQeIHMEEKPFPCLKCGKSFASSSDLTAH 421
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLR-THHNNPSDLNSKSLPLSNSKASSSSL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412681 422 RRQIHTEEKPFSCTECGKCFSVEAFLVRHQRTHTKEKPFSCPECGKcfSHPSNLTRHRRIHRGEKPFSCSECDKCYATPS 501
Cdd:COG5048   111 SSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNS--SSVNTPQSNSLHPPLPANSLSKDPSSNLSLLI 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412681 502 ELTVHHrrthtgekPFSCSECGKCFATSSILIVHYRTHTGEKPFSCSECGKCFATSSALTVHHRRTHTGeKPFPCSECGK 581
Cdd:COG5048   189 SSNVST--------SIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLS-SSDSSSSASE 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412681 582 CFSTSSLLTVHYRTH----------TGERPYPCSECGKCFTTKAELIAHRRRMHaeklftclkcgksfatapllatHQRT 651
Cdd:COG5048   260 SPRSSLPTASSQSSSpnesdsssekGFSLPIKSKQCNISFSRSSPLTRHLRSVN----------------------HSGE 317

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1785412681 652 HVKPFSCTE--CGKCFSRRIYLTHHQRTHRDEKPF 684
Cdd:COG5048   318 SLKPFSCPYslCGKLFSRNDALKRHILLHTSISPA 352
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 515-567 1.31e-03

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 38.31  E-value: 1.31e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1785412681 515 KPFsCSECGKCFATSSILIVHYRTHTgekpFSCSECGKCFATSSALTVH----HRRT 567
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHclqvHKET 52
zf-H2C2_2 pfam13465
Zinc-finger double domain;
474-499 1.43e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.43e-03
                          10        20
                  ....*....|....*....|....*.
gi 1785412681 474 NLTRHRRIHRGEKPFSCSECDKCYAT 499
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
589-613 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 1785412681 589 LTVHYRTHTGERPYPCSECGKCFTT 613
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
564-585 2.28e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.28e-03
                          10        20
                  ....*....|....*....|..
gi 1785412681 564 HRRTHTGEKPFPCSECGKCFST 585
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 125-426 2.83e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.86  E-value: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412681 125 QLHPLACEYkdGSDVTAHTEATLCCNNDGNLTNPDVSPVEQPPPANGIKEASNKGGNQSDCSINPQIQGTDTPTpIMGCS 204
Cdd:COG5189   142 QVHTSGAVP--TPSVMGSATASSTTANPSITGAPGLLVDAVDVPHNKQINSNNNSTSHNSNMGSKNAKMNDSSK-LKKLS 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412681 205 LNISLSanyiaNDIKEEAASREGGSQSDCSINPLTEQIQGTDTPTPIMGYSTISSLF---KMKGNKNHEDAHwSPDKSDI 281
Cdd:COG5189   219 LIEEKK-----FPERVRSRYIDIGHMMDTHQFYLEDVDLMDDDILGPSNEEMLYKYIspsQGSAELFEESSL-GFDYEFI 292

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412681 282 TENAVSGKYSCNechihFSSKRDFDKhlrthkREKPLSCSECGKCFSHRSNF-----ARHLRThTGEKPYSCS--ECGKC 354
Cdd:COG5189   293 HKSVGNKEIRGG-----ISTGEMIDV------RKLPCTNSSSNGKLAHGGERnidtpSRMLKV-KDGKPYKCPveGCNKK 360

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785412681 355 FSHPFNFARHRKT-HTGEKTFPcsvcgkifaTPSELTLhqQEIHMEEKPFPCLKCGKSFASSSDLTAHRRQIH 426
Cdd:COG5189   361 YKNQNGLKYHMLHgHQNQKLHE---------NPSPEKM--NIFSAKDKPYRCEVCDKRYKNLNGLKYHRKHSH 422
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 656-678 2.99e-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: 35.35  E-value: 2.99e-03
                          10        20
                  ....*....|....*....|...
gi 1785412681 656 FSCTECGKCFSRRIYLTHHQRTH 678
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
KRAB smart00349
krueppel associated box;
91-117 3.04e-03

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 36.42  E-value: 3.04e-03
                           10        20
                   ....*....|....*....|....*...
gi 1785412681   91 EDVSIYFSLEEWEYIK-GNKALYREGIK 117
Cdd:smart00349   4 EDVAVYFTQEEWEQLDpAQKNLYRDVML 31
zf-H2C2_2 pfam13465
Zinc-finger double domain;
532-556 3.19e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.19e-03
                          10        20
                  ....*....|....*....|....*
gi 1785412681 532 LIVHYRTHTGEKPFSCSECGKCFAT 556
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 574-596 3.37e-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: 3.37e-03
                          10        20
                  ....*....|....*....|...
gi 1785412681 574 FPCSECGKCFSTSSLLTVHYRTH 596
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
507-528 3.73e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.73e-03
                          10        20
                  ....*....|....*....|..
gi 1785412681 507 HRRTHTGEKPFSCSECGKCFAT 528
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 319-340 5.24e-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: 5.24e-03
                          10        20
                  ....*....|....*....|..
gi 1785412681 319 SCSECGKCFSHRSNFARHLRTH 340
Cdd:pfam00096   2 KCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
360-385 6.93e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 6.93e-03
                          10        20
                  ....*....|....*....|....*.
gi 1785412681 360 NFARHRKTHTGEKTFPCSVCGKIFAT 385
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 346-368 7.10e-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: 7.10e-03
                          10        20
                  ....*....|....*....|...
gi 1785412681 346 YSCSECGKCFSHPFNFARHRKTH 368
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH