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Conserved domains on  [gi|392354387|ref|XP_003751758|]
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zinc finger protein 184 isoform X1 [Rattus norvegicus]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204268)

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

CATH:  3.30.160.60
Gene Ontology:  GO:0003700|GO:0046872
PubMed:  22803940
SCOP:  4003583

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
28-88 6.83e-33

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 120.78  E-value: 6.83e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392354387    28 VTFKDVVVNFTQEEWKHLDPTQRDLFRDVTLENYTHLVSIGLQVSKPDMISHLEQGTEPWI 88
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
203-635 1.46e-12

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 70.49  E-value: 1.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392354387 203 KCNECGKAFTYCSALIRHQRTHTGEKPYKCND--CNKAFSRNENLINHQRIHTGDKPYKCDQCGKGFIEGPSLTQHQRIH 280
Cdd:COG5048   35 SCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLSSSS 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392354387 281 TGEkPYKCDECGKAFSQRTHLVQHQRIHTGEKpYTCNECGKSFSQRGHFMEHQKIHtGEKPFKCEECEKTFTRSTHLtqH 360
Cdd:COG5048  115 SNS-NDNNLLSSHSLPPSSRDPQLPDLLSISN-LRNNPLPGNNSSSVNTPQSNSLH-PPLPANSLSKDPSSNLSLLI--S 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392354387 361 QKIHTGEKTYKCNECGKAFNGPSTFIRHHMIHTGEKPYECNECGKAFSQHSNLTQHQKTHTGEKPYDCAEC-----GKAF 435
Cdd:COG5048  190 SNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESprsslPTAS 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392354387 436 SYWSSLAQHL--KIHTGEKPYKCSDCGKAFSYCSSLTQHRR--IHTRE--KPFECSE--CGKAFSYLSNLNQHQKTHTQE 507
Cdd:COG5048  270 SQSSSPNESDssSEKGFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSI 349

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392354387 508 KAYECKecgkaFIRSSSLAKherihtgekpyqclecGKTFSYGSSLIQHKKIHTGERPYKC--NECERAFNQKIHLTQHK 585
Cdd:COG5048  350 SPAKEK-----LLNSSSKFS----------------PLLNNEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHI 408

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 392354387 586 RIHTGVKPYAC--PKCGKTFRHCSSLAQHQKTHTEGKHYQCNKCEKTFSQKS 635
Cdd:COG5048  409 ITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
28-88 6.83e-33

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 120.78  E-value: 6.83e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392354387    28 VTFKDVVVNFTQEEWKHLDPTQRDLFRDVTLENYTHLVSIGLQVSKPDMISHLEQGTEPWI 88
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 27-68 1.05e-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: 88.30  E-value: 1.05e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 392354387   27 SVTFKDVVVNFTQEEWKHLDPTQRDLFRDVTLENYTHLVSIG 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 2.64e-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: 2.64e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 392354387  28 VTFKDVVVNFTQEEWKHLDPTQRDLFRDVTLENYTHLVSI 67
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
203-635 1.46e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 70.49  E-value: 1.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392354387 203 KCNECGKAFTYCSALIRHQRTHTGEKPYKCND--CNKAFSRNENLINHQRIHTGDKPYKCDQCGKGFIEGPSLTQHQRIH 280
Cdd:COG5048   35 SCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLSSSS 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392354387 281 TGEkPYKCDECGKAFSQRTHLVQHQRIHTGEKpYTCNECGKSFSQRGHFMEHQKIHtGEKPFKCEECEKTFTRSTHLtqH 360
Cdd:COG5048  115 SNS-NDNNLLSSHSLPPSSRDPQLPDLLSISN-LRNNPLPGNNSSSVNTPQSNSLH-PPLPANSLSKDPSSNLSLLI--S 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392354387 361 QKIHTGEKTYKCNECGKAFNGPSTFIRHHMIHTGEKPYECNECGKAFSQHSNLTQHQKTHTGEKPYDCAEC-----GKAF 435
Cdd:COG5048  190 SNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESprsslPTAS 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392354387 436 SYWSSLAQHL--KIHTGEKPYKCSDCGKAFSYCSSLTQHRR--IHTRE--KPFECSE--CGKAFSYLSNLNQHQKTHTQE 507
Cdd:COG5048  270 SQSSSPNESDssSEKGFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSI 349

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392354387 508 KAYECKecgkaFIRSSSLAKherihtgekpyqclecGKTFSYGSSLIQHKKIHTGERPYKC--NECERAFNQKIHLTQHK 585
Cdd:COG5048  350 SPAKEK-----LLNSSSKFS----------------PLLNNEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHI 408

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 392354387 586 RIHTGVKPYAC--PKCGKTFRHCSSLAQHQKTHTEGKHYQCNKCEKTFSQKS 635
Cdd:COG5048  409 ITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
zf-H2C2_2 pfam13465
Zinc-finger double domain;
272-297 9.65e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 9.65e-05
                          10        20
                  ....*....|....*....|....*.
gi 392354387  272 SLTQHQRIHTGEKPYKCDECGKAFSQ 297
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 592-644 3.48e-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: 3.48e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 392354387 592 KPYaCPKCGKTFRHCSSLAQHQKThtegKHYQCNKCEKTFSQKSHLTQH-QQVH 644
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKA----KHFKCHICHKKLYTAGGLAVHcLQVH 49
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
28-88 6.83e-33

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 120.78  E-value: 6.83e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392354387    28 VTFKDVVVNFTQEEWKHLDPTQRDLFRDVTLENYTHLVSIGLQVSKPDMISHLEQGTEPWI 88
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 27-68 1.05e-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: 88.30  E-value: 1.05e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 392354387   27 SVTFKDVVVNFTQEEWKHLDPTQRDLFRDVTLENYTHLVSIG 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 2.64e-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: 2.64e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 392354387  28 VTFKDVVVNFTQEEWKHLDPTQRDLFRDVTLENYTHLVSI 67
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
203-635 1.46e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 70.49  E-value: 1.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392354387 203 KCNECGKAFTYCSALIRHQRTHTGEKPYKCND--CNKAFSRNENLINHQRIHTGDKPYKCDQCGKGFIEGPSLTQHQRIH 280
Cdd:COG5048   35 SCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLSSSS 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392354387 281 TGEkPYKCDECGKAFSQRTHLVQHQRIHTGEKpYTCNECGKSFSQRGHFMEHQKIHtGEKPFKCEECEKTFTRSTHLtqH 360
Cdd:COG5048  115 SNS-NDNNLLSSHSLPPSSRDPQLPDLLSISN-LRNNPLPGNNSSSVNTPQSNSLH-PPLPANSLSKDPSSNLSLLI--S 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392354387 361 QKIHTGEKTYKCNECGKAFNGPSTFIRHHMIHTGEKPYECNECGKAFSQHSNLTQHQKTHTGEKPYDCAEC-----GKAF 435
Cdd:COG5048  190 SNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESprsslPTAS 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392354387 436 SYWSSLAQHL--KIHTGEKPYKCSDCGKAFSYCSSLTQHRR--IHTRE--KPFECSE--CGKAFSYLSNLNQHQKTHTQE 507
Cdd:COG5048  270 SQSSSPNESDssSEKGFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSI 349

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392354387 508 KAYECKecgkaFIRSSSLAKherihtgekpyqclecGKTFSYGSSLIQHKKIHTGERPYKC--NECERAFNQKIHLTQHK 585
Cdd:COG5048  350 SPAKEK-----LLNSSSKFS----------------PLLNNEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHI 408

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 392354387 586 RIHTGVKPYAC--PKCGKTFRHCSSLAQHQKTHTEGKHYQCNKCEKTFSQKS 635
Cdd:COG5048  409 ITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
284-692 1.51e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 70.49  E-value: 1.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392354387 284 KPYKCDECGKAFSQRTHLVQHQRIHTGEKPYTCN--ECGKSFSQRGHFMEHQKIHTGEKPFKCEECEKTFTRST-HLTQH 360
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKAsSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392354387 361 QKIHTGEKTYKCNECGKAFNGPSTFIRHHMIHT---GEKPYECNECGKAFSQhSNLTQHQKTHTgekpydcAECGKAFSY 437
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISnlrNNPLPGNNSSSVNTPQ-SNSLHPPLPAN-------SLSKDPSSN 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392354387 438 WSSLAQHLKIHTGEKPYKCSDCGKAFSYcSSLTQHRRIHTREKPFECSECGKAFSYLSNLNQHQKTHTQEKAYECKECG- 516
Cdd:COG5048  184 LSLLISSNVSTSIPSSSENSPLSSSYSI-PSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPr 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392354387 517 -----KAFIRSSSLAKHERIHTG-EKPYQCLECGKTFSYGSSLIQHK--KIHTGE--RPYKCNE--CERAFNQKIHLTQH 584
Cdd:COG5048  263 sslptASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPYslCGKLFSRNDALKRH 342

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392354387 585 KRIHTGVKPYACP--KCGKTFRHCS------SLAQHQKTHTEGKHYQC-NKCEKTFSQKSHLTQHQQVHMGEKP--YKCN 653
Cdd:COG5048  343 ILLHTSISPAKEKllNSSSKFSPLLnneppqSLQQYKDLKNDKKSETLsNSCIRNFKRDSNLSLHIITHLSFRPynCKNP 422

                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 392354387 654 DCDRCFTQSTHLTEHQSIHTGEKPYSSNVCPQTFNQNTY 692
Cdd:COG5048  423 PCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDL 461
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
396-708 6.78e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 68.57  E-value: 6.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392354387 396 KPYECNECGKAFSQHSNLTQHQKTHTGEKPYDCA--ECGKAFSYWSSLAQHLKIHTGEKPYKCSD-CGKAFSYCSSLTQH 472
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKsLPLSNSKASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392354387 473 RRIHTREKPFECSECGKAFSYLSNLNQHQKTHTQEKAYECKEC-GKAFIRSSSLAKHERIHTGEKpyqcleCGKTFSYGS 551
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnSSSVNTPQSNSLHPPLPANSL------SKDPSSNLS 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392354387 552 SLIQHKKIHTGERPYKCNECERaFNQKIHLTQHKRIHTGVKPYACPKCGKTFRHCSSLAQHQKTHTEGKHYQCNKCEKTF 631
Cdd:COG5048  186 LLISSNVSTSIPSSSENSPLSS-SYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSS 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392354387 632 SQKSHLTQHQQVHMGE-------KPYKCNDCDRCFTQSTHLTEHQ--SIHTGE--KPYS--SNVCPQTFNQNTYLTQHQK 698
Cdd:COG5048  265 LPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFScpYSLCGKLFSRNDALKRHIL 344

                        330
                 ....*....|
gi 392354387 699 IHSGEKSFVC 708
Cdd:COG5048  345 LHTSISPAKE 354
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
192-389 1.42e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.15  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392354387 192 SSRPGQKEKLCKCNECGKAFTYCSALIRHQRT--HTGE--KPYKC--NDCNKAFSRNENLINHQRIHTGDKPYKCDQCGK 265
Cdd:COG5048  280 SSSEKGFSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKLLNS 359

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392354387 266 GFIEGPSLTQhqrihtgekpykcdecgkafSQRTHLVQHQRIHTGEKPYTC-NECGKSFSQRGHFMEHQKIHTGEKP--F 342
Cdd:COG5048  360 SSKFSPLLNN--------------------EPPQSLQQYKDLKNDKKSETLsNSCIRNFKRDSNLSLHIITHLSFRPynC 419

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 392354387 343 KCEECEKTFTRSTHLTQHQKIHTgEKTYKCNECGKAFNGPSTFIRHH 389
Cdd:COG5048  420 KNPPCSKSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLSNHG 465
zf-H2C2_2 pfam13465
Zinc-finger double domain;
272-297 9.65e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 9.65e-05
                          10        20
                  ....*....|....*....|....*.
gi 392354387  272 SLTQHQRIHTGEKPYKCDECGKAFSQ 297
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
300-325 1.84e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.84e-04
                          10        20
                  ....*....|....*....|....*.
gi 392354387  300 HLVQHQRIHTGEKPYTCNECGKSFSQ 325
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
440-465 3.19e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 3.19e-04
                          10        20
                  ....*....|....*....|....*.
gi 392354387  440 SLAQHLKIHTGEKPYKCSDCGKAFSY 465
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 592-644 3.48e-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: 3.48e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 392354387 592 KPYaCPKCGKTFRHCSSLAQHQKThtegKHYQCNKCEKTFSQKSHLTQH-QQVH 644
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKA----KHFKCHICHKKLYTAGGLAVHcLQVH 49
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 154-304 3.77e-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: 3.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392354387 154 TEKTMRPSYE---KDLGVSA---GLLTQTDIAVDQTSTNtraKQSSRPgqkeKLCKCNEcgkafTYCSALIRHQRThTGE 227
Cdd:COG5189  281 EESSLGFDYEfihKSVGNKEirgGISTGEMIDVRKLPCT---NSSSNG----KLAHGGE-----RNIDTPSRMLKV-KDG 347

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392354387 228 KPYKCN--DCNKAFsRNENLINHQRIHtgdkpykcDQCGKGFIEGPSLTQHQRIHTGEKPYKCDECGKAFSQRTHLVQH 304
Cdd:COG5189  348 KPYKCPveGCNKKY-KNQNGLKYHMLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKYH 417
zf-H2C2_2 pfam13465
Zinc-finger double domain;
216-241 5.27e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 5.27e-04
                          10        20
                  ....*....|....*....|....*.
gi 392354387  216 ALIRHQRTHTGEKPYKCNDCNKAFSR 241
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
580-605 5.48e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 5.48e-04
                          10        20
                  ....*....|....*....|....*.
gi 392354387  580 HLTQHKRIHTGVKPYACPKCGKTFRH 605
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
328-353 5.93e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 5.93e-04
                          10        20
                  ....*....|....*....|....*.
gi 392354387  328 HFMEHQKIHTGEKPFKCEECEKTFTR 353
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
412-437 6.67e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 6.67e-04
                          10        20
                  ....*....|....*....|....*.
gi 392354387  412 NLTQHQKTHTGEKPYDCAECGKAFSY 437
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
524-549 7.21e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 7.21e-04
                          10        20
                  ....*....|....*....|....*.
gi 392354387  524 SLAKHERIHTGEKPYQCLECGKTFSY 549
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
496-521 1.24e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.24e-03
                          10        20
                  ....*....|....*....|....*.
gi 392354387  496 NLNQHQKTHTQEKAYECKECGKAFIR 521
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
356-380 1.57e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.57e-03
                          10        20
                  ....*....|....*....|....*
gi 392354387  356 HLTQHQKIHTGEKTYKCNECGKAFN 380
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
244-267 1.66e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.66e-03
                          10        20
                  ....*....|....*....|....
gi 392354387  244 NLINHQRIHTGDKPYKCDQCGKGF 267
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 338-421 1.82e-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: 1.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392354387 338 GEKPFKCE--ECEKTFTRSTHLTQHQKI-HTGEKTYKcnecgkafnGPSTfIRHHMIHTGEKPYECNECGKAFSQHSNLT 414
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLKYHMLHgHQNQKLHE---------NPSP-EKMNIFSAKDKPYRCEVCDKRYKNLNGLK 415


                 ....*..
gi 392354387 415 QHQKTHT 421
Cdd:COG5189  416 YHRKHSH 422
zf-H2C2_2 pfam13465
Zinc-finger double domain;
468-493 2.02e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 2.02e-03
                          10        20
                  ....*....|....*....|....*.
gi 392354387  468 SLTQHRRIHTREKPFECSECGKAFSY 493
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
552-577 2.08e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 2.08e-03
                          10        20
                  ....*....|....*....|....*.
gi 392354387  552 SLIQHKKIHTGERPYKCNECERAFNQ 577
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 340-380 2.62e-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: 37.54  E-value: 2.62e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 392354387 340 KPFkCEECEKTFTRSTHLTQHQKihtgEKTYKCNECGKAFN 380
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 ...
 398-420 3.45e-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: 3.45e-03
                          10        20
                  ....*....|....*....|...
gi 392354387  398 YECNECGKAFSQHSNLTQHQKTH 420
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 230-252 3.66e-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: 3.66e-03
                          10        20
                  ....*....|....*....|...
gi 392354387  230 YKCNDCNKAFSRNENLINHQRIH 252
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
387-409 4.61e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.61e-03
                          10        20
                  ....*....|....*....|...
gi 392354387  387 RHHMIHTGEKPYECNECGKAFSQ 409
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 622-644 6.47e-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: 34.58  E-value: 6.47e-03
                          10        20
                  ....*....|....*....|...
gi 392354387  622 YQCNKCEKTFSQKSHLTQHQQVH 644
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 286-308 9.21e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.20  E-value: 9.21e-03
                          10        20
                  ....*....|....*....|...
gi 392354387  286 YKCDECGKAFSQRTHLVQHQRIH 308
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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