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Conserved domains on  [gi|1317049025|ref|NP_001346116|]
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zinc finger protein with KRAB and SCAN domains 5 isoform 3 [Mus musculus]

Protein Classification

C2H2-type zinc finger protein; zinc finger and BTB domain-containing protein( domain architecture ID 12210844)

Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation| zinc finger and BTB (BR-C, ttk and bab)/POZ (Pox virus and Zinc finger) domain-containing protein may be involved in transcriptional regulation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
47-155 8.05e-57

leucine rich region;


:

Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 189.82  E-value: 8.05e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317049025   47 ETFYQRFKHFQYHEAAGPRDALSQLRVLCCEWLRPELHTKEQILELLVLEQFLTILPEEFQAWVREHHPESGEEAVAVIE 126
Cdd:smart00431   2 EIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLE 81

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1317049025  127 SIQRELEERRQQIATSP---EVLPQKMVPPGA 155
Cdd:smart00431  82 DLERELDEPGQQVSAHVhgqEVLLEKMVPLGA 113
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
308-729 1.57e-07

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 54.70  E-value: 1.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317049025 308 LRSGPDVNRKQKSNGERGHRCGDCGKFFLQASNFIQHRRIHTGEKPFKCG--ECGKSYNQRVHLTQHQRVHTGEKPYKC- 384
Cdd:COG5048    16 LSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNs 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317049025 385 -QVCGKAFRVSSHLVQHHSVHSgerPYGCNECGKSFGRHSHLIEHLKRHFREKSQRCSDRRSKNTKLNIKQIpglseADL 463
Cdd:COG5048    96 kSLPLSNSKASSSSLSSSSSNS---NDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQS-----NSL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317049025 464 ELSGEVQRNACQAEGHSEGCEHQDGQQGVVMKE--TLGQSSSKRTDCNEFSYVHKKSSPGERPHQcnecgkSFIQSAHLI 541
Cdd:COG5048   168 HPPLPANSLSKDPSSNLSLLISSNVSTSIPSSSenSPLSSSYSIPSSSSDQNLENSSSSLPLTTN------SQLSPKSLL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317049025 542 QHRRIHTGEK--PFRCEECGKSYNQRVHLTQHHRVHTGE-------KPYACHLCGKAFRVRSHLVQHQ--SVHSRE--RP 608
Cdd:COG5048   242 SQSPSSLSSSdsSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKP 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317049025 609 FKCNE--CGKGFGRRSHLAGHLRLHSRDKSHQCHECGEIFFQYVSLLE--------HQVLHVGQKSEKNGICEEAYSW-N 677
Cdd:COG5048   322 FSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNNeppqslqqYKDLKNDKKSETLSNSCIRNFKrD 401

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1317049025 678 LTVIKDKKLELQEQPYQCDS--CGKAFSYSSDLIQHYRTHSAEKPQKCDACRDS 729
Cdd:COG5048   402 SNLSLHIITHLSFRPYNCKNppCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSF 455
KRAB_A-box super family cl02581
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 220-257 1.70e-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: 42.54  E-value: 1.70e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1317049025 220 DVAVSFILEEWAHLDQSQKSLdYepKEGNLEFTVQQVS 257
Cdd:cd07765     5 DVAVYFSQEEWELLDPAQRDL-Y--RDVMLENYENLVS 39
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
47-155 8.05e-57

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 189.82  E-value: 8.05e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317049025   47 ETFYQRFKHFQYHEAAGPRDALSQLRVLCCEWLRPELHTKEQILELLVLEQFLTILPEEFQAWVREHHPESGEEAVAVIE 126
Cdd:smart00431   2 EIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLE 81

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1317049025  127 SIQRELEERRQQIATSP---EVLPQKMVPPGA 155
Cdd:smart00431  82 DLERELDEPGQQVSAHVhgqEVLLEKMVPLGA 113
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 46-134 1.01e-45

SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several pfam00096 proteins. The domain has been shown to be able to mediate homo- and hetero-oligomerization.


Pssm-ID: 460417 [Multi-domain]  Cd Length: 89  Bit Score: 158.04  E-value: 1.01e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317049025  46 LETFYQRFKHFQYHEAAGPRDALSQLRVLCCEWLRPELHTKEQILELLVLEQFLTILPEEFQAWVREHHPESGEEAVAVI 125
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALA 80


                  ....*....
gi 1317049025 126 ESIQRELEE 134
Cdd:pfam02023  81 EDLLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 46-130 1.27e-37

SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several vertebrate proteins that contain C2H2 zinc finger motifs, many of which may be transcription factors playing roles in cell survival and differentiation. This protein-interaction domain is able to mediate homo- and hetero-oligomerization of SCAN-containing proteins. Some SCAN-containing proteins, including those of lower vertebrates, do not contain zinc finger motifs. It has been noted that the SCAN domain resembles a domain-swapped version of the C-terminal domain of the HIV capsid protein. This domain model features elements common to the three general groups of SCAN domains (SCAN-A1, SCAN-A2, and SCAN-B). The SCAND1 protein is truncated at the C-terminus with respect to this model, the SCAND2 protein appears to have a truncated central helix.


Pssm-ID: 153421  Cd Length: 85  Bit Score: 135.08  E-value: 1.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317049025  46 LETFYQRFKHFQYHEAAGPRDALSQLRVLCCEWLRPELHTKEQILELLVLEQFLTILPEEFQAWVREHHPESGEEAVAVI 125
Cdd:cd07936     1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80


                  ....*
gi 1317049025 126 ESIQR 130
Cdd:cd07936    81 EDLLA 85
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
308-729 1.57e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 54.70  E-value: 1.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317049025 308 LRSGPDVNRKQKSNGERGHRCGDCGKFFLQASNFIQHRRIHTGEKPFKCG--ECGKSYNQRVHLTQHQRVHTGEKPYKC- 384
Cdd:COG5048    16 LSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNs 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317049025 385 -QVCGKAFRVSSHLVQHHSVHSgerPYGCNECGKSFGRHSHLIEHLKRHFREKSQRCSDRRSKNTKLNIKQIpglseADL 463
Cdd:COG5048    96 kSLPLSNSKASSSSLSSSSSNS---NDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQS-----NSL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317049025 464 ELSGEVQRNACQAEGHSEGCEHQDGQQGVVMKE--TLGQSSSKRTDCNEFSYVHKKSSPGERPHQcnecgkSFIQSAHLI 541
Cdd:COG5048   168 HPPLPANSLSKDPSSNLSLLISSNVSTSIPSSSenSPLSSSYSIPSSSSDQNLENSSSSLPLTTN------SQLSPKSLL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317049025 542 QHRRIHTGEK--PFRCEECGKSYNQRVHLTQHHRVHTGE-------KPYACHLCGKAFRVRSHLVQHQ--SVHSRE--RP 608
Cdd:COG5048   242 SQSPSSLSSSdsSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKP 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317049025 609 FKCNE--CGKGFGRRSHLAGHLRLHSRDKSHQCHECGEIFFQYVSLLE--------HQVLHVGQKSEKNGICEEAYSW-N 677
Cdd:COG5048   322 FSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNNeppqslqqYKDLKNDKKSETLSNSCIRNFKrD 401

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1317049025 678 LTVIKDKKLELQEQPYQCDS--CGKAFSYSSDLIQHYRTHSAEKPQKCDACRDS 729
Cdd:COG5048   402 SNLSLHIITHLSFRPYNCKNppCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSF 455
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 220-257 1.70e-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: 42.54  E-value: 1.70e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1317049025 220 DVAVSFILEEWAHLDQSQKSLdYepKEGNLEFTVQQVS 257
Cdd:cd07765     5 DVAVYFSQEEWELLDPAQRDL-Y--RDVMLENYENLVS 39
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 220-240 8.11e-05

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: 40.53  E-value: 8.11e-05
                          10        20
                  ....*....|....*....|.
gi 1317049025 220 DVAVSFILEEWAHLDQSQKSL 240
Cdd:pfam01352   6 DVAVDFTQEEWALLDPAQRNL 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
368-391 1.35e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 1.35e-04
                          10        20
                  ....*....|....*....|....
gi 1317049025 368 HLTQHQRVHTGEKPYKCQVCGKAF 391
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
KRAB smart00349
krueppel associated box;
220-240 3.47e-04

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 39.11  E-value: 3.47e-04
                           10        20
                   ....*....|....*....|.
gi 1317049025  220 DVAVSFILEEWAHLDQSQKSL 240
Cdd:smart00349   5 DVAVYFTQEEWEQLDPAQKNL 25
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 579-631 1.80e-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: 37.92  E-value: 1.80e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1317049025 579 KPYaCHLCGKAFRVRSHLVQHQsvhsRERPFKCNECGKGFGRRSHLAGH-LRLH 631
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQ----KAKHFKCHICHKKLYTAGGLAVHcLQVH 49
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
47-155 8.05e-57

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 189.82  E-value: 8.05e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317049025   47 ETFYQRFKHFQYHEAAGPRDALSQLRVLCCEWLRPELHTKEQILELLVLEQFLTILPEEFQAWVREHHPESGEEAVAVIE 126
Cdd:smart00431   2 EIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLE 81

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1317049025  127 SIQRELEERRQQIATSP---EVLPQKMVPPGA 155
Cdd:smart00431  82 DLERELDEPGQQVSAHVhgqEVLLEKMVPLGA 113
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 46-134 1.01e-45

SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several pfam00096 proteins. The domain has been shown to be able to mediate homo- and hetero-oligomerization.


Pssm-ID: 460417 [Multi-domain]  Cd Length: 89  Bit Score: 158.04  E-value: 1.01e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317049025  46 LETFYQRFKHFQYHEAAGPRDALSQLRVLCCEWLRPELHTKEQILELLVLEQFLTILPEEFQAWVREHHPESGEEAVAVI 125
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALA 80


                  ....*....
gi 1317049025 126 ESIQRELEE 134
Cdd:pfam02023  81 EDLLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 46-130 1.27e-37

SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several vertebrate proteins that contain C2H2 zinc finger motifs, many of which may be transcription factors playing roles in cell survival and differentiation. This protein-interaction domain is able to mediate homo- and hetero-oligomerization of SCAN-containing proteins. Some SCAN-containing proteins, including those of lower vertebrates, do not contain zinc finger motifs. It has been noted that the SCAN domain resembles a domain-swapped version of the C-terminal domain of the HIV capsid protein. This domain model features elements common to the three general groups of SCAN domains (SCAN-A1, SCAN-A2, and SCAN-B). The SCAND1 protein is truncated at the C-terminus with respect to this model, the SCAND2 protein appears to have a truncated central helix.


Pssm-ID: 153421  Cd Length: 85  Bit Score: 135.08  E-value: 1.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317049025  46 LETFYQRFKHFQYHEAAGPRDALSQLRVLCCEWLRPELHTKEQILELLVLEQFLTILPEEFQAWVREHHPESGEEAVAVI 125
Cdd:cd07936     1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80


                  ....*
gi 1317049025 126 ESIQR 130
Cdd:cd07936    81 EDLLA 85
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
308-729 1.57e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 54.70  E-value: 1.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317049025 308 LRSGPDVNRKQKSNGERGHRCGDCGKFFLQASNFIQHRRIHTGEKPFKCG--ECGKSYNQRVHLTQHQRVHTGEKPYKC- 384
Cdd:COG5048    16 LSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNs 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317049025 385 -QVCGKAFRVSSHLVQHHSVHSgerPYGCNECGKSFGRHSHLIEHLKRHFREKSQRCSDRRSKNTKLNIKQIpglseADL 463
Cdd:COG5048    96 kSLPLSNSKASSSSLSSSSSNS---NDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQS-----NSL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317049025 464 ELSGEVQRNACQAEGHSEGCEHQDGQQGVVMKE--TLGQSSSKRTDCNEFSYVHKKSSPGERPHQcnecgkSFIQSAHLI 541
Cdd:COG5048   168 HPPLPANSLSKDPSSNLSLLISSNVSTSIPSSSenSPLSSSYSIPSSSSDQNLENSSSSLPLTTN------SQLSPKSLL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317049025 542 QHRRIHTGEK--PFRCEECGKSYNQRVHLTQHHRVHTGE-------KPYACHLCGKAFRVRSHLVQHQ--SVHSRE--RP 608
Cdd:COG5048   242 SQSPSSLSSSdsSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKP 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317049025 609 FKCNE--CGKGFGRRSHLAGHLRLHSRDKSHQCHECGEIFFQYVSLLE--------HQVLHVGQKSEKNGICEEAYSW-N 677
Cdd:COG5048   322 FSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNNeppqslqqYKDLKNDKKSETLSNSCIRNFKrD 401

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1317049025 678 LTVIKDKKLELQEQPYQCDS--CGKAFSYSSDLIQHYRTHSAEKPQKCDACRDS 729
Cdd:COG5048   402 SNLSLHIITHLSFRPYNCKNppCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSF 455
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
501-799 4.84e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.16  E-value: 4.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317049025 501 SSSKRTDCNEFsyvHKKSSPGERPHQCNECGKSFIQSAHLIQHRRIHTGEKPFRC--EECGKSYNQRVHLTQHHRVHTG- 577
Cdd:COG5048    13 NSVLSSTPKST---LKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNn 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317049025 578 -----------EKPYACH----LCGKAFRVRSHLVQHQSVHSRERP----------FKCNECGKGFGRRSHLAGHLRLHS 632
Cdd:COG5048    90 psdlnskslplSNSKASSsslsSSSSNSNDNNLLSSHSLPPSSRDPqlpdllsisnLRNNPLPGNNSSSVNTPQSNSLHP 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317049025 633 RdkSHQCHECGEIFFQYVSLLEHQVLHVGQKSEKNGICEEAYS-WNLtvIKDKKLELQEQPYQCDSCGKAFSYSSDLIQH 711
Cdd:COG5048   170 P--LPANSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSiPSS--SSDQNLENSSSSLPLTTNSQLSPKSLLSQSP 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317049025 712 YRT---HSAEKPQKCDACRDSTCQCPHIKQQQ----KSCPSGKSHQCNECGRGFSLKSHLSQHQR--IHTGE--KPLQCK 780
Cdd:COG5048   246 SSLsssDSSSSASESPRSSLPTASSQSSSPNEsdssSEKGFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCP 325

                         330       340
                  ....*....|....*....|.
gi 1317049025 781 E--CGMSFSWSCSLFKHLRSH 799
Cdd:COG5048   326 YslCGKLFSRNDALKRHILLH 346
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 220-257 1.70e-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: 42.54  E-value: 1.70e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1317049025 220 DVAVSFILEEWAHLDQSQKSLdYepKEGNLEFTVQQVS 257
Cdd:cd07765     5 DVAVYFSQEEWELLDPAQRDL-Y--RDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
380-804 3.85e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.00  E-value: 3.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317049025 380 KPYKCQVCGKAFRVSSHLVQHHSVHSGERPYGCN--ECGKSFGRHSHLIEHLKRHFREKSQRCSDRRSKNTKLNIKQIPG 457
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317049025 458 LSeadlelsgevqrnacqaegHSEGCEHQDGQQGvvmkeTLGQSSSKRTDCNEfsyVHKKSSPGERPHQCNECGKSFIQS 537
Cdd:COG5048   112 SS-------------------SSNSNDNNLLSSH-----SLPPSSRDPQLPDL---LSISNLRNNPLPGNNSSSVNTPQS 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317049025 538 AHLI-QHRRIHTGEKPFRCEecgksynqrvHLTQHHRVHTGEKPYACHLCGKAFRVRSHLVQHQSVHSRERPFKCNECGK 616
Cdd:COG5048   165 NSLHpPLPANSLSKDPSSNL----------SLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQ 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317049025 617 GFGRRSHLAGHLRLHSRDKSHQCHECGEIFFQYVSLLEHQVLHVGQ----------KSEKNGICEEAYSWNLTVIKDKKL 686
Cdd:COG5048   235 LSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfslpiKSKQCNISFSRSSPLTRHLRSVNH 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317049025 687 ELQEQ-PYQCDS--CGKAFSYSSDLIQHYRTHSAEKPQKCDACRDS--------------TCQCPHIKQQQKSCPSGksh 749
Cdd:COG5048   315 SGESLkPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSskfspllnneppqsLQQYKDLKNDKKSETLS--- 391

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1317049025 750 qcNECGRGFSLKSHLSQHQRIHTGEKPLQCK--ECGMSFSWSCSLFKHLRSHERTDP 804
Cdd:COG5048   392 --NSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAP 446
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 220-240 8.11e-05

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: 40.53  E-value: 8.11e-05
                          10        20
                  ....*....|....*....|.
gi 1317049025 220 DVAVSFILEEWAHLDQSQKSL 240
Cdd:pfam01352   6 DVAVDFTQEEWALLDPAQRNL 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
368-391 1.35e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 1.35e-04
                          10        20
                  ....*....|....*....|....
gi 1317049025 368 HLTQHQRVHTGEKPYKCQVCGKAF 391
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
539-564 1.94e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.94e-04
                          10        20
                  ....*....|....*....|....*.
gi 1317049025 539 HLIQHRRIHTGEKPFRCEECGKSYNQ 564
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
KRAB smart00349
krueppel associated box;
220-240 3.47e-04

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 39.11  E-value: 3.47e-04
                           10        20
                   ....*....|....*....|.
gi 1317049025  220 DVAVSFILEEWAHLDQSQKSL 240
Cdd:smart00349   5 DVAVYFTQEEWEQLDPAQKNL 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
340-365 1.00e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 1.00e-03
                          10        20
                  ....*....|....*....|....*.
gi 1317049025 340 NFIQHRRIHTGEKPFKCGECGKSYNQ 365
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
567-590 1.38e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.38e-03
                          10        20
                  ....*....|....*....|....
gi 1317049025 567 HLTQHHRVHTGEKPYACHLCGKAF 590
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 579-631 1.80e-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: 37.92  E-value: 1.80e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1317049025 579 KPYaCHLCGKAFRVRSHLVQHQsvhsRERPFKCNECGKGFGRRSHLAGH-LRLH 631
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQ----KAKHFKCHICHKKLYTAGGLAVHcLQVH 49
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 525-547 3.05e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.74  E-value: 3.05e-03
                          10        20
                  ....*....|....*....|...
gi 1317049025 525 HQCNECGKSFIQSAHLIQHRRIH 547
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 354-376 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 1317049025 354 FKCGECGKSYNQRVHLTQHQRVH 376
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 693-715 7.83e-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: 7.83e-03
                          10        20
                  ....*....|....*....|...
gi 1317049025 693 YQCDSCGKAFSYSSDLIQHYRTH 715
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 553-575 9.35e-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: 9.35e-03
                          10        20
                  ....*....|....*....|...
gi 1317049025 553 FRCEECGKSYNQRVHLTQHHRVH 575
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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