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Conserved domains on  [gi|1331383514|ref|NP_001346863|]
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zinc finger protein 445 isoform 2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
48-160 9.25e-52

leucine rich region;


:

Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 176.73  E-value: 9.25e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514   48 QELFRQLFRQLRYHESSGPLETLSRLQELCRWWMRPDVLSKAQMLELLVLEQFLSILPGELRTWVQLHCPESGAEVVALL 127
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1331383514  128 EELQRDLDGTPLKDPCLTQNPDVHWIGTSALQP 160
Cdd:smart00431  81 EDLERELDEPGQQVSAHVHGQEVLLEKMVPLGA 113
KRAB smart00349
krueppel associated box;
231-289 1.53e-26

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 103.06  E-value: 1.53e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514  231 LTFQDVEVTFSQEEWGCLNSAQRNLYRDVILENYGNVVSVVGSSPKPALISWLEARK-PW 289
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEePW 60
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
566-995 5.15e-10

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 63.18  E-value: 5.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514 566 HCNQCGKNFSCKSYAIEHQRIHTQEKPYKCTR--CRKTFRWKSNFSRHMKLHHKEVY----KQEKRQEDFKQSYRQSQVI 639
Cdd:COG5048    35 SCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSdlnsKSLPLSNSKASSSSLSSSS 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514 640 STVEKTFPCQNCGKTFTQKKSLIEHQRIHTGEKPYQCSGCGETF--TYRSSYIIHMKRTQHAIKIKPEHGCLTFSQGAVF 717
Cdd:COG5048   115 SNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSvnTPQSNSLHPPLPANSLSKDPSSNLSLLISSNVST 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514 718 PIPRGSHNTEGS-----NKCKYCGKAFHNRSFLLIHERVHTREKPYQCreCEKAFRWSSNLYRHQRKHFLHKRYKYRESK 792
Cdd:COG5048   195 SIPSSSENSPLSssysiPSSSSDQNLENSSSSLPLTTNSQLSPKSLLS--QSPSSLSSSDSSSSASESPRSSLPTASSQS 272

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514 793 ETSN--LQSKILIDQKPFWCQECGKTFTRKRSLLDHK--GIHSGE--RRFKC--NLCEKSFDRNYRLVNHQRIHT-TEQP 863
Cdd:COG5048   273 SSPNesDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTsISPA 352

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514 864 QWRDKDFVGIHARSVDQRKHSNTlQSEYGLHSDKPglSYCQDVRLNIQELSGKlrkecdNPSDESSKSIAFQNVptkkka 943
Cdd:COG5048   353 KEKLLNSSSKFSPLLNNEPPQSL-QQYKDLKNDKK--SETLSNSCIRNFKRDS------NLSLHIITHLSFRPY------ 417

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1331383514 944 CHKCSTCGKTFKKHSHLISHKRCHTKERPFKCIVCGKTFRwssnlTRHMKNH 995
Cdd:COG5048   418 NCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRR-----DLDLSNH 464
zf-H2C2_2 pfam13465
Zinc-finger double domain;
499-519 3.15e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 3.15e-03
                          10        20
                  ....*....|....*....|.
gi 1331383514 499 RHEKIHTGVKPYQCSLCEKAF 519
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSF 24
COG5048 super family cl34881
FOG: Zn-finger [General function prediction only];
461-611 5.24e-03

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


The actual alignment was detected with superfamily member COG5048:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.45  E-value: 5.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514 461 SRKSWHAHPEhRQPSYSEEGL--FQCRV--CGKAFKWRSNRIRHEKIHTGVKPYQCSL--CEKAFQRLSSYRLHQKTHsk 534
Cdd:COG5048   300 SRSSPLTRHL-RSVNHSGESLkpFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLlnSSSKFSPLLNNEPPQSLQ-- 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514 535 QKRGSSKYKNALT----C----------SLDVSHHLTDRDerKHLHCNQCGKNFSCKSYAIEHQRIHTQEKPYkCTRCRK 600
Cdd:COG5048   377 QYKDLKNDKKSETlsnsCirnfkrdsnlSLHIITHLSFRP--YNCKNPPCSKSFNRHYNLIPHKKIHTNHAPL-LCSILK 453

                         170
                  ....*....|.
gi 1331383514 601 TFRWKSNFSRH 611
Cdd:COG5048   454 SFRRDLDLSNH 464
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
48-160 9.25e-52

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 176.73  E-value: 9.25e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514   48 QELFRQLFRQLRYHESSGPLETLSRLQELCRWWMRPDVLSKAQMLELLVLEQFLSILPGELRTWVQLHCPESGAEVVALL 127
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1331383514  128 EELQRDLDGTPLKDPCLTQNPDVHWIGTSALQP 160
Cdd:smart00431  81 EDLERELDEPGQQVSAHVHGQEVLLEKMVPLGA 113
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 48-136 3.38e-42

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: 148.79  E-value: 3.38e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514  48 QELFRQLFRQLRYHESSGPLETLSRLQELCRWWMRPDVLSKAQMLELLVLEQFLSILPGELRTWVQLHCPESGAEVVALL 127
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALA 80


                  ....*....
gi 1331383514 128 EELQRDLDG 136
Cdd:pfam02023  81 EDLLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 49-132 1.34e-33

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: 123.91  E-value: 1.34e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514  49 ELFRQLFRQLRYHESSGPLETLSRLQELCRWWMRPDVLSKAQMLELLVLEQFLSILPGELRTWVQLHCPESGAEVVALLE 128
Cdd:cd07936     2 ETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLAE 81


                  ....
gi 1331383514 129 ELQR 132
Cdd:cd07936    82 DLLA 85
KRAB smart00349
krueppel associated box;
231-289 1.53e-26

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 103.06  E-value: 1.53e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514  231 LTFQDVEVTFSQEEWGCLNSAQRNLYRDVILENYGNVVSVVGSSPKPALISWLEARK-PW 289
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEePW 60
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 231-270 3.28e-20

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: 84.44  E-value: 3.28e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1331383514 231 LTFQDVEVTFSQEEWGCLNSAQRNLYRDVILENYGNVVSV 270
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 231-269 1.28e-17

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: 76.82  E-value: 1.28e-17
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1331383514 231 LTFQDVEVTFSQEEWGCLNSAQRNLYRDVILENYGNVVS 269
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
566-995 5.15e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 63.18  E-value: 5.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514 566 HCNQCGKNFSCKSYAIEHQRIHTQEKPYKCTR--CRKTFRWKSNFSRHMKLHHKEVY----KQEKRQEDFKQSYRQSQVI 639
Cdd:COG5048    35 SCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSdlnsKSLPLSNSKASSSSLSSSS 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514 640 STVEKTFPCQNCGKTFTQKKSLIEHQRIHTGEKPYQCSGCGETF--TYRSSYIIHMKRTQHAIKIKPEHGCLTFSQGAVF 717
Cdd:COG5048   115 SNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSvnTPQSNSLHPPLPANSLSKDPSSNLSLLISSNVST 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514 718 PIPRGSHNTEGS-----NKCKYCGKAFHNRSFLLIHERVHTREKPYQCreCEKAFRWSSNLYRHQRKHFLHKRYKYRESK 792
Cdd:COG5048   195 SIPSSSENSPLSssysiPSSSSDQNLENSSSSLPLTTNSQLSPKSLLS--QSPSSLSSSDSSSSASESPRSSLPTASSQS 272

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514 793 ETSN--LQSKILIDQKPFWCQECGKTFTRKRSLLDHK--GIHSGE--RRFKC--NLCEKSFDRNYRLVNHQRIHT-TEQP 863
Cdd:COG5048   273 SSPNesDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTsISPA 352

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514 864 QWRDKDFVGIHARSVDQRKHSNTlQSEYGLHSDKPglSYCQDVRLNIQELSGKlrkecdNPSDESSKSIAFQNVptkkka 943
Cdd:COG5048   353 KEKLLNSSSKFSPLLNNEPPQSL-QQYKDLKNDKK--SETLSNSCIRNFKRDS------NLSLHIITHLSFRPY------ 417

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1331383514 944 CHKCSTCGKTFKKHSHLISHKRCHTKERPFKCIVCGKTFRwssnlTRHMKNH 995
Cdd:COG5048   418 NCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRR-----DLDLSNH 464
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 945-994 1.78e-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: 41.00  E-value: 1.78e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1331383514 945 HKCSTCGKTFKKHSHLISHKRCHTkerpFKCIVCGKTFRWSSNLTRHMKN 994
Cdd:cd20908     2 PWCYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHCLQ 47
zf-H2C2_2 pfam13465
Zinc-finger double domain;
959-982 9.32e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 9.32e-04
                          10        20
                  ....*....|....*....|....
gi 1331383514 959 HLISHKRCHTKERPFKCIVCGKTF 982
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
499-519 3.15e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 3.15e-03
                          10        20
                  ....*....|....*....|.
gi 1331383514 499 RHEKIHTGVKPYQCSLCEKAF 519
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSF 24
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
461-611 5.24e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.45  E-value: 5.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514 461 SRKSWHAHPEhRQPSYSEEGL--FQCRV--CGKAFKWRSNRIRHEKIHTGVKPYQCSL--CEKAFQRLSSYRLHQKTHsk 534
Cdd:COG5048   300 SRSSPLTRHL-RSVNHSGESLkpFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLlnSSSKFSPLLNNEPPQSLQ-- 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514 535 QKRGSSKYKNALT----C----------SLDVSHHLTDRDerKHLHCNQCGKNFSCKSYAIEHQRIHTQEKPYkCTRCRK 600
Cdd:COG5048   377 QYKDLKNDKKSETlsnsCirnfkrdsnlSLHIITHLSFRP--YNCKNPPCSKSFNRHYNLIPHKKIHTNHAPL-LCSILK 453

                         170
                  ....*....|.
gi 1331383514 601 TFRWKSNFSRH 611
Cdd:COG5048   454 SFRRDLDLSNH 464
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
48-160 9.25e-52

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 176.73  E-value: 9.25e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514   48 QELFRQLFRQLRYHESSGPLETLSRLQELCRWWMRPDVLSKAQMLELLVLEQFLSILPGELRTWVQLHCPESGAEVVALL 127
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1331383514  128 EELQRDLDGTPLKDPCLTQNPDVHWIGTSALQP 160
Cdd:smart00431  81 EDLERELDEPGQQVSAHVHGQEVLLEKMVPLGA 113
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 48-136 3.38e-42

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: 148.79  E-value: 3.38e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514  48 QELFRQLFRQLRYHESSGPLETLSRLQELCRWWMRPDVLSKAQMLELLVLEQFLSILPGELRTWVQLHCPESGAEVVALL 127
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALA 80


                  ....*....
gi 1331383514 128 EELQRDLDG 136
Cdd:pfam02023  81 EDLLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 49-132 1.34e-33

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: 123.91  E-value: 1.34e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514  49 ELFRQLFRQLRYHESSGPLETLSRLQELCRWWMRPDVLSKAQMLELLVLEQFLSILPGELRTWVQLHCPESGAEVVALLE 128
Cdd:cd07936     2 ETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLAE 81


                  ....
gi 1331383514 129 ELQR 132
Cdd:cd07936    82 DLLA 85
KRAB smart00349
krueppel associated box;
231-289 1.53e-26

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 103.06  E-value: 1.53e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514  231 LTFQDVEVTFSQEEWGCLNSAQRNLYRDVILENYGNVVSVVGSSPKPALISWLEARK-PW 289
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEePW 60
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 231-270 3.28e-20

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: 84.44  E-value: 3.28e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1331383514 231 LTFQDVEVTFSQEEWGCLNSAQRNLYRDVILENYGNVVSV 270
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 231-269 1.28e-17

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: 76.82  E-value: 1.28e-17
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1331383514 231 LTFQDVEVTFSQEEWGCLNSAQRNLYRDVILENYGNVVS 269
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
566-995 5.15e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 63.18  E-value: 5.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514 566 HCNQCGKNFSCKSYAIEHQRIHTQEKPYKCTR--CRKTFRWKSNFSRHMKLHHKEVY----KQEKRQEDFKQSYRQSQVI 639
Cdd:COG5048    35 SCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSdlnsKSLPLSNSKASSSSLSSSS 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514 640 STVEKTFPCQNCGKTFTQKKSLIEHQRIHTGEKPYQCSGCGETF--TYRSSYIIHMKRTQHAIKIKPEHGCLTFSQGAVF 717
Cdd:COG5048   115 SNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSvnTPQSNSLHPPLPANSLSKDPSSNLSLLISSNVST 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514 718 PIPRGSHNTEGS-----NKCKYCGKAFHNRSFLLIHERVHTREKPYQCreCEKAFRWSSNLYRHQRKHFLHKRYKYRESK 792
Cdd:COG5048   195 SIPSSSENSPLSssysiPSSSSDQNLENSSSSLPLTTNSQLSPKSLLS--QSPSSLSSSDSSSSASESPRSSLPTASSQS 272

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514 793 ETSN--LQSKILIDQKPFWCQECGKTFTRKRSLLDHK--GIHSGE--RRFKC--NLCEKSFDRNYRLVNHQRIHT-TEQP 863
Cdd:COG5048   273 SSPNesDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTsISPA 352

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514 864 QWRDKDFVGIHARSVDQRKHSNTlQSEYGLHSDKPglSYCQDVRLNIQELSGKlrkecdNPSDESSKSIAFQNVptkkka 943
Cdd:COG5048   353 KEKLLNSSSKFSPLLNNEPPQSL-QQYKDLKNDKK--SETLSNSCIRNFKRDS------NLSLHIITHLSFRPY------ 417

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1331383514 944 CHKCSTCGKTFKKHSHLISHKRCHTKERPFKCIVCGKTFRwssnlTRHMKNH 995
Cdd:COG5048   418 NCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRR-----DLDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
466-865 1.08e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.94  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514 466 HAHPEHRQPSYSEEGLFQCRVCGKAFKWRSNRIRHEKIHTGVKPYQCSL--CEKAFQRLSSYRLHQKTHSKQKRGSSKYK 543
Cdd:COG5048    18 STPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKS 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514 544 NALT------CSLDVSHHLTDrderKHLHCNQCGKNFSCKSYAIEHQRIHTQEKPYKCTRC-RKTFRWKSNFSRHMKLHH 616
Cdd:COG5048    98 LPLSnskassSSLSSSSSNSN----DNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnSSSVNTPQSNSLHPPLPA 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514 617 KEVYKQEKRQEDFKQSYRqsqvISTVEKTFPCQNCGKTFTQKKSLIEHQRIHTGEKPYQCSGCGETFTYRSSYIIHMKRT 696
Cdd:COG5048   174 NSLSKDPSSNLSLLISSN----VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLS 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514 697 QHAIKIKPEHGCLTFSQGAVFPIPRGSHNTEGSNK-------CKYCGKAFHNRSFLLIHER--VHTRE--KPYQCRE--C 763
Cdd:COG5048   250 SSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKgfslpikSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslC 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514 764 EKAFRWSSNLYRHQRKHFLHKRYKY----RESKETSNL---------QSKILIDQKPFWC--QECGKTFTRKRSLLDHKG 828
Cdd:COG5048   330 GKLFSRNDALKRHILLHTSISPAKEkllnSSSKFSPLLnneppqslqQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHII 409

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1331383514 829 IH--SGERRFKCNLCEKSFDRNYRLVNHQRIHTTEQPQW 865
Cdd:COG5048   410 THlsFRPYNCKNPPCSKSFNRHYNLIPHKKIHTNHAPLL 448
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
644-995 1.29e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.47  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514 644 KTFPCQNCGKTFTQKKSLIEHQRIHTGEKPYQCS--GCGETFTYRSSYIIHMKRTQHAIKIKPEHG-CLTFSQGAVFPIP 720
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSlPLSNSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514 721 RGSHNTEGSNKCKYCGKAFHNRSFLLIHERVHTREKPYQCRECekaFRWSSNLYRHQRKHFlhkrykyresketsnlqsk 800
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGN---NSSSVNTPQSNSLHP------------------- 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514 801 ilidqkPFWCQECGKTFTRKRSLLDHKGIHSGERRFKCNLCEKSFDRNYRLVNHQRIHTTEQPQWRDKdFVGIHARSVDQ 880
Cdd:COG5048   170 ------PLPANSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTT-NSQLSPKSLLS 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514 881 RKHSNTlqseyglhSDKPGLSYCQDVRLNIQELSGKLRKecdNPSD-ESSKSIAFQNVptkkkacHKCSTCGKTFKKHSH 959
Cdd:COG5048   243 QSPSSL--------SSSDSSSSASESPRSSLPTASSQSS---SPNEsDSSSEKGFSLP-------IKSKQCNISFSRSSP 304

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1331383514 960 LISHKRC--HTKE--RPFKC--IVCGKTFRWSSNLTRHMKNH 995
Cdd:COG5048   305 LTRHLRSvnHSGEslKPFSCpySLCGKLFSRNDALKRHILLH 346
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 945-994 1.78e-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: 41.00  E-value: 1.78e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1331383514 945 HKCSTCGKTFKKHSHLISHKRCHTkerpFKCIVCGKTFRWSSNLTRHMKN 994
Cdd:cd20908     2 PWCYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHCLQ 47
zf-H2C2_2 pfam13465
Zinc-finger double domain;
959-982 9.32e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 9.32e-04
                          10        20
                  ....*....|....*....|....
gi 1331383514 959 HLISHKRCHTKERPFKCIVCGKTF 982
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
660-685 1.33e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 1.33e-03
                          10        20
                  ....*....|....*....|....*.
gi 1331383514 660 SLIEHQRIHTGEKPYQCSGCGETFTY 685
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
922-995 1.60e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.99  E-value: 1.60e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331383514 922 DNPSDESSKSIAFQNVPTKKKACHKCSTCGKTFKKHSHLISHKRCHTKERPFKCIV--CGKTFRWSSNLTRHMKNH 995
Cdd:COG5048    11 SNNSVLSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTH 86
zf-H2C2_2 pfam13465
Zinc-finger double domain;
499-519 3.15e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 3.15e-03
                          10        20
                  ....*....|....*....|.
gi 1331383514 499 RHEKIHTGVKPYQCSLCEKAF 519
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSF 24
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
461-611 5.24e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.45  E-value: 5.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514 461 SRKSWHAHPEhRQPSYSEEGL--FQCRV--CGKAFKWRSNRIRHEKIHTGVKPYQCSL--CEKAFQRLSSYRLHQKTHsk 534
Cdd:COG5048   300 SRSSPLTRHL-RSVNHSGESLkpFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLlnSSSKFSPLLNNEPPQSLQ-- 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383514 535 QKRGSSKYKNALT----C----------SLDVSHHLTDRDerKHLHCNQCGKNFSCKSYAIEHQRIHTQEKPYkCTRCRK 600
Cdd:COG5048   377 QYKDLKNDKKSETlsnsCirnfkrdsnlSLHIITHLSFRP--YNCKNPPCSKSFNRHYNLIPHKKIHTNHAPL-LCSILK 453

                         170
                  ....*....|.
gi 1331383514 601 TFRWKSNFSRH 611
Cdd:COG5048   454 SFRRDLDLSNH 464
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 646-668 6.05e-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: 34.97  E-value: 6.05e-03
                          10        20
                  ....*....|....*....|...
gi 1331383514 646 FPCQNCGKTFTQKKSLIEHQRIH 668
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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