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Conserved domains on  [gi|1958774545|ref|XP_038965147|]
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zinc finger protein 483 isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 45-133 1.28e-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: 149.18  E-value: 1.28e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774545  45 LESFRQKFRWFCYSQEEGPRKTLNQLWELCKQWLRPDIHTKEQILELLVFEQFLRVLPGEMRIWVNSQHPESSVEVVTLV 124
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALA 80


                  ....*....
gi 1958774545 125 EDLNQTLEE 133
Cdd:pfam02023  81 EDLLLERGE 89
KRAB smart00349
krueppel associated box;
176-229 1.40e-18

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 79.94  E-value: 1.40e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958774545  176 VTFEDVSVDFTRGEWKLLEPSQRELYKEVLLENLGSLEVLGSPVSKFDLISHLK 229
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLE 54
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
487-730 6.30e-10

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 62.02  E-value: 6.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774545 487 SYKCDECGKRFAEENDFSQHQRTHTREKPYVCKHCGRAFSDNSSFCQHQRIHTGE-------KPYTCKECGKSFTHSSSL 559
Cdd:COG5048   226 SLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPL 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774545 560 SKHQR--IHTGE--KPYKCKE--CGKAFRQNSCLTRHQKIHTGEKPFLCKECGLSFrlfssimyhqrlHKGEKPYKCPHc 633
Cdd:COG5048   306 TRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSS------------KFSPLLNNEPP- 372

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774545 634 ekGFPSHSRLSRHLRIHTGAKPykckECGKTFRQSSSLNLHIRTHTGEKP--YKCNYCGAAFTRSTILVEHVKTHTRVKY 711
Cdd:COG5048   373 --QSLQQYKDLKNDKKSETLSN----SCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAP 446

                         250
                  ....*....|....*....
gi 1958774545 712 DCkKCGKSFKSRSANLRHH 730
Cdd:COG5048   447 LL-CSILKSFRRDLDLSNH 464
 
Name Accession Description Interval E-value
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 45-133 1.28e-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: 149.18  E-value: 1.28e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774545  45 LESFRQKFRWFCYSQEEGPRKTLNQLWELCKQWLRPDIHTKEQILELLVFEQFLRVLPGEMRIWVNSQHPESSVEVVTLV 124
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALA 80


                  ....*....
gi 1958774545 125 EDLNQTLEE 133
Cdd:pfam02023  81 EDLLLERGE 89
SCAN smart00431
leucine rich region;
46-133 1.72e-40

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 143.98  E-value: 1.72e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774545   46 ESFRQKFRWFCYSQEEGPRKTLNQLWELCKQWLRPDIHTKEQILELLVFEQFLRVLPGEMRIWVNSQHPESSVEVVTLVE 125
Cdd:smart00431   2 EIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLE 81


                   ....*...
gi 1958774545  126 DLNQTLEE 133
Cdd:smart00431  82 DLERELDE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 45-127 7.75e-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: 132.77  E-value: 7.75e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774545  45 LESFRQKFRWFCYSQEEGPRKTLNQLWELCKQWLRPDIHTKEQILELLVFEQFLRVLPGEMRIWVNSQHPESSVEVVTLV 124
Cdd:cd07936     1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80


                  ...
gi 1958774545 125 EDL 127
Cdd:cd07936    81 EDL 83
KRAB smart00349
krueppel associated box;
176-229 1.40e-18

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 79.94  E-value: 1.40e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958774545  176 VTFEDVSVDFTRGEWKLLEPSQRELYKEVLLENLGSLEVLGSPVSKFDLISHLK 229
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLE 54
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 176-216 2.72e-17

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: 75.58  E-value: 2.72e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958774545 176 VTFEDVSVDFTRGEWKLLEPSQRELYKEVLLENLGSLEVLG 216
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 176-215 3.71e-15

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: 69.50  E-value: 3.71e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1958774545 176 VTFEDVSVDFTRGEWKLLEPSQRELYKEVLLENLGSLEVL 215
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
487-730 6.30e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 62.02  E-value: 6.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774545 487 SYKCDECGKRFAEENDFSQHQRTHTREKPYVCKHCGRAFSDNSSFCQHQRIHTGE-------KPYTCKECGKSFTHSSSL 559
Cdd:COG5048   226 SLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPL 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774545 560 SKHQR--IHTGE--KPYKCKE--CGKAFRQNSCLTRHQKIHTGEKPFLCKECGLSFrlfssimyhqrlHKGEKPYKCPHc 633
Cdd:COG5048   306 TRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSS------------KFSPLLNNEPP- 372

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774545 634 ekGFPSHSRLSRHLRIHTGAKPykckECGKTFRQSSSLNLHIRTHTGEKP--YKCNYCGAAFTRSTILVEHVKTHTRVKY 711
Cdd:COG5048   373 --QSLQQYKDLKNDKKSETLSN----SCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAP 446

                         250
                  ....*....|....*....
gi 1958774545 712 DCkKCGKSFKSRSANLRHH 730
Cdd:COG5048   447 LL-CSILKSFRRDLDLSNH 464
zf-H2C2_2 pfam13465
Zinc-finger double domain;
558-583 2.31e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 2.31e-05
                          10        20
                  ....*....|....*....|....*.
gi 1958774545 558 SLSKHQRIHTGEKPYKCKECGKAFRQ 583
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 514-566 3.81e-05

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: 42.54  E-value: 3.81e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958774545 514 KPYvCKHCGRAFSDNSSFCQHQRIHTgekpYTCKECGKSFTHSSSLSKH-QRIH 566
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
PHA00733 PHA00733
hypothetical protein
 613-675 1.27e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 39.47  E-value: 1.27e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958774545 613 SSIMYHQRLHKGEKPYKCPHCEKGFPSHSRLSRHLRIHTGAKpyKCKECGKTFRQSSSLNLHI 675
Cdd:PHA00733   59 SSYLYKLLTSKAVSPYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDHV 119
 
Name Accession Description Interval E-value
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 45-133 1.28e-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: 149.18  E-value: 1.28e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774545  45 LESFRQKFRWFCYSQEEGPRKTLNQLWELCKQWLRPDIHTKEQILELLVFEQFLRVLPGEMRIWVNSQHPESSVEVVTLV 124
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALA 80


                  ....*....
gi 1958774545 125 EDLNQTLEE 133
Cdd:pfam02023  81 EDLLLERGE 89
SCAN smart00431
leucine rich region;
46-133 1.72e-40

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 143.98  E-value: 1.72e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774545   46 ESFRQKFRWFCYSQEEGPRKTLNQLWELCKQWLRPDIHTKEQILELLVFEQFLRVLPGEMRIWVNSQHPESSVEVVTLVE 125
Cdd:smart00431   2 EIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLE 81


                   ....*...
gi 1958774545  126 DLNQTLEE 133
Cdd:smart00431  82 DLERELDE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 45-127 7.75e-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: 132.77  E-value: 7.75e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774545  45 LESFRQKFRWFCYSQEEGPRKTLNQLWELCKQWLRPDIHTKEQILELLVFEQFLRVLPGEMRIWVNSQHPESSVEVVTLV 124
Cdd:cd07936     1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80


                  ...
gi 1958774545 125 EDL 127
Cdd:cd07936    81 EDL 83
KRAB smart00349
krueppel associated box;
176-229 1.40e-18

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 79.94  E-value: 1.40e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958774545  176 VTFEDVSVDFTRGEWKLLEPSQRELYKEVLLENLGSLEVLGSPVSKFDLISHLK 229
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLE 54
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 176-216 2.72e-17

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: 75.58  E-value: 2.72e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958774545 176 VTFEDVSVDFTRGEWKLLEPSQRELYKEVLLENLGSLEVLG 216
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 176-215 3.71e-15

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: 69.50  E-value: 3.71e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1958774545 176 VTFEDVSVDFTRGEWKLLEPSQRELYKEVLLENLGSLEVL 215
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
487-730 6.30e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 62.02  E-value: 6.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774545 487 SYKCDECGKRFAEENDFSQHQRTHTREKPYVCKHCGRAFSDNSSFCQHQRIHTGE-------KPYTCKECGKSFTHSSSL 559
Cdd:COG5048   226 SLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPL 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774545 560 SKHQR--IHTGE--KPYKCKE--CGKAFRQNSCLTRHQKIHTGEKPFLCKECGLSFrlfssimyhqrlHKGEKPYKCPHc 633
Cdd:COG5048   306 TRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSS------------KFSPLLNNEPP- 372

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774545 634 ekGFPSHSRLSRHLRIHTGAKPykckECGKTFRQSSSLNLHIRTHTGEKP--YKCNYCGAAFTRSTILVEHVKTHTRVKY 711
Cdd:COG5048   373 --QSLQQYKDLKNDKKSETLSN----SCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAP 446

                         250
                  ....*....|....*....
gi 1958774545 712 DCkKCGKSFKSRSANLRHH 730
Cdd:COG5048   447 LL-CSILKSFRRDLDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
493-730 2.65e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.93  E-value: 2.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774545 493 CGKRFAEENDFSQHQRTHTREKPYVCKHCGRAFSDNSSFcQHQRIHTGEKPYTCKECGKSFTHSSSLSKHQRIHTGEKPY 572
Cdd:COG5048   177 SKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSS-SDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSS 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774545 573 KCKECGKAFRQNSCLTRHQKIHTGE-------KPFLCKECGLSFRLFSSIMYHQR--LHKGE--KPYKCPH--CEKGFPS 639
Cdd:COG5048   256 SASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSR 335

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774545 640 HSRLSRHLRIHTGAKPYKCKECGKTFRQSSSLN----LHIRTHTGEKPYK---CNY--CGAAFTRSTILVEHVKTHTRVK 710
Cdd:COG5048   336 NDALKRHILLHTSISPAKEKLLNSSSKFSPLLNneppQSLQQYKDLKNDKkseTLSnsCIRNFKRDSNLSLHIITHLSFR 415

                         250       260
                  ....*....|....*....|..
gi 1958774545 711 YDCKKCGKSFK--SRSANLRHH 730
Cdd:COG5048   416 PYNCKNPPCSKsfNRHYNLIPH 437
zf-H2C2_2 pfam13465
Zinc-finger double domain;
558-583 2.31e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 2.31e-05
                          10        20
                  ....*....|....*....|....*.
gi 1958774545 558 SLSKHQRIHTGEKPYKCKECGKAFRQ 583
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 514-566 3.81e-05

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: 42.54  E-value: 3.81e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958774545 514 KPYvCKHCGRAFSDNSSFCQHQRIHTgekpYTCKECGKSFTHSSSLSKH-QRIH 566
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
471-613 3.82e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.00  E-value: 3.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774545 471 ASPSLKPQGKTDRRKKSYKCDECGKRFAEENDFSQHQRT--HTRE--KPYVCKH--CGRAFSDNSSFCQHQRIHTGEKPY 544
Cdd:COG5048   273 SSPNESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPA 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774545 545 TCK--ECGKSFTHSSSLSKHQRIHT-------------------------------------GEKPYKCKECGKAFRQNS 585
Cdd:COG5048   353 KEKllNSSSKFSPLLNNEPPQSLQQykdlkndkksetlsnscirnfkrdsnlslhiithlsfRPYNCKNPPCSKSFNRHY 432

                         170       180
                  ....*....|....*....|....*...
gi 1958774545 586 CLTRHQKIHTGEKPFLCKECGLSFRLFS 613
Cdd:COG5048   433 NLIPHKKIHTNHAPLLCSILKSFRRDLD 460
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
542-678 6.53e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 46.23  E-value: 6.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774545 542 KPYTCKECGKSFTHSSSLSKHQRIHTGEKPYKC--KECGKAFRQNSCLTRHQKIHTGEKPFLC-KECGLSFRLFSSIMYH 618
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNsKSLPLSNSKASSSSLS 111

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958774545 619 QRLHKGEKPYKCPHCEKGFPSHSRLSRHLRIHTGAKPYKCKEC-GKTFRQSSSLNLHIRTH 678
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnSSSVNTPQSNSLHPPLP 172
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 656-678 8.25e-05

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: 39.98  E-value: 8.25e-05
                          10        20
                  ....*....|....*....|...
gi 1958774545 656 YKCKECGKTFRQSSSLNLHIRTH 678
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
670-695 1.16e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 1.16e-04
                          10        20
                  ....*....|....*....|....*.
gi 1958774545 670 SLNLHIRTHTGEKPYKCNYCGAAFTR 695
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
626-733 1.17e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.46  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774545 626 KPYKCPHCEKGFPSHSRLSRHLRIHTGAKPYKCKECGKTFRQSSSLNL--HIRTHTGEKPYKCNYCG--AAFTRSTILVE 701
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELsrHLRTHHNNPSDLNSKSLplSNSKASSSSLS 111

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958774545 702 HVKTHTRVKYDCKKCGKSFKSRSANLRHHCTL 733
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSI 143
zf-H2C2_2 pfam13465
Zinc-finger double domain;
533-555 1.18e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 1.18e-04
                          10        20
                  ....*....|....*....|...
gi 1958774545 533 QHQRIHTGEKPYTCKECGKSFTH 555
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
642-667 1.32e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.32e-04
                          10        20
                  ....*....|....*....|....*.
gi 1958774545 642 RLSRHLRIHTGAKPYKCKECGKTFRQ 667
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 544-566 1.36e-04

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 39.21  E-value: 1.36e-04
                          10        20
                  ....*....|....*....|...
gi 1958774545 544 YTCKECGKSFTHSSSLSKHQRIH 566
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 572-594 3.22e-04

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 38.44  E-value: 3.22e-04
                          10        20
                  ....*....|....*....|...
gi 1958774545 572 YKCKECGKAFRQNSCLTRHQKIH 594
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
485-730 6.01e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.15  E-value: 6.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774545 485 KKSYKCDECGKRFAEENDFSQHQRTHTREKPYVCKHCGRA--FSDNSSFCQHQRIHTGEKP------------------- 543
Cdd:COG5048    31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHHNNPSdlnskslplsnskassssl 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774545 544 --------YTCKECGKSFTHSSSLSKH----QRIHTGEKPYK-CKECGKAFRQNSCL-------------------TRHQ 591
Cdd:COG5048   111 sssssnsnDNNLLSSHSLPPSSRDPQLpdllSISNLRNNPLPgNNSSSVNTPQSNSLhpplpanslskdpssnlslLISS 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774545 592 KIHTGEKPFLCKECGLSFRLFSSIMYHQRLHKGEKPYKCPHCEKGFPSHSRLSRHLRIHTGAKPYKCKECG------KTF 665
Cdd:COG5048   191 NVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPrsslptASS 270

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958774545 666 RQSSSLNLHIRTHTG-EKPYKCNYCGAAFTRSTILVEHVKT--HTRVKY-----DCKKCGKSFKSRSANLRHH 730
Cdd:COG5048   271 QSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGESLkpfscPYSLCGKLFSRNDALKRHI 343
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 623-679 7.08e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 42.78  E-value: 7.08e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958774545 623 KGEKPYKCP--HCEKGFPSHSRLSRHlRIH--------------------TGAKPYKCKECGKTFRQSSSLNLHiRTHT 679
Cdd:COG5189   345 KDGKPYKCPveGCNKKYKNQNGLKYH-MLHghqnqklhenpspekmnifsAKDKPYRCEVCDKRYKNLNGLKYH-RKHS 421
PHA00733 PHA00733
hypothetical protein
 613-675 1.27e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 39.47  E-value: 1.27e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958774545 613 SSIMYHQRLHKGEKPYKCPHCEKGFPSHSRLSRHLRIHTGAKpyKCKECGKTFRQSSSLNLHI 675
Cdd:PHA00733   59 SSYLYKLLTSKAVSPYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDHV 119
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 516-538 1.69e-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: 36.12  E-value: 1.69e-03
                          10        20
                  ....*....|....*....|...
gi 1958774545 516 YVCKHCGRAFSDNSSFCQHQRIH 538
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
502-526 5.97e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 5.97e-03
                          10        20
                  ....*....|....*....|....*
gi 1958774545 502 DFSQHQRTHTREKPYVCKHCGRAFS 526
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
616-637 5.97e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 5.97e-03
                          10        20
                  ....*....|....*....|..
gi 1958774545 616 MYHQRLHKGEKPYKCPHCEKGF 637
Cdd:pfam13465   3 KRHMRTHTGEKPYKCPECGKSF 24
 
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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