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Conserved domains on  [gi|194239638|ref|NP_689908|]
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zinc finger protein 449 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCAN super family cl42860
leucine rich region;
27-134 4.40e-51

leucine rich region;


The actual alignment was detected with superfamily member smart00431:

Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 169.79  E-value: 4.40e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194239638    27 EVFRQRFRQFQYREAAGPHEAFNKLWELCCQWLKPKMRSKEQILELLVLEQFLTILPTEIETWVREHCPENRERVVSLIE 106
Cdd:smart00431   2 EIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLE 81

                           90       100       110
                   ....*....|....*....|....*....|..
gi 194239638   107 DLQRELEIPEQQVDMH----DMLLEELAPVGT 134
Cdd:smart00431  82 DLERELDEPGQQVSAHvhgqEVLLEKMVPLGA 113
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
321-483 2.36e-15

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 78.20  E-value: 2.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194239638 321 KPHRCPQCGKCFARKSQLTGHQR--IHSGE--EPHKCPE--CGKRFLRSSDLYRHQRLHTGERPYEC--TVCKKRFTRRS 392
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194239638 393 HLIGHQRT--HSEEETYKCLECGKSFCHG-----SSLKRHLKTHTGEKPHRCHN--CGKSFSRLTALTLHQRTHTEERPF 463
Cdd:COG5048  368 NNEPPQSLqqYKDLKNDKKSETLSNSCIRnfkrdSNLSLHIITHLSFRPYNCKNppCSKSFNRHYNLIPHKKIHTNHAPL 447

                        170       180
                 ....*....|....*....|
gi 194239638 464 KCNYCgKSFRQRPSLVIHLR 483
Cdd:COG5048  448 LCSIL-KSFRRDLDLSNHGK 466
zf-H2C2_2 pfam13465
Zinc-finger double domain;
477-502 3.27e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 3.27e-05
                          10        20
                  ....*....|....*....|....*.
gi 194239638  477 SLVIHLRIHTGEKPYKCTHCSKSFRQ 502
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 super family cl25788
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 235-402 2.10e-04

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


The actual alignment was detected with superfamily member COG5189:

Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 43.94  E-value: 2.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194239638 235 DTSKQKKMETMYPFIVTLEGN-ALQGPILQKDYVQLENQwetpPEDLQTDLAKLVdQQNPTLGETPeNSNLeeplnpkph 313
Cdd:COG5189  278 ELFEESSLGFDYEFIHKSVGNkEIRGGISTGEMIDVRKL----PCTNSSSNGKLA-HGGERNIDTP-SRML--------- 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194239638 314 kkKSPGEKPHRCP--QCGKCFARKSQLTGHqRIHSGEEPHKCPecgkrflrSSDLYRHQRLHTGERPYECTVCKKRFTRR 391
Cdd:COG5189  343 --KVKDGKPYKCPveGCNKKYKNQNGLKYH-MLHGHQNQKLHE--------NPSPEKMNIFSAKDKPYRCEVCDKRYKNL 411

                        170
                 ....*....|.
gi 194239638 392 SHLIGHqRTHS 402
Cdd:COG5189  412 NGLKYH-RKHS 421
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
27-134 4.40e-51

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 169.79  E-value: 4.40e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194239638    27 EVFRQRFRQFQYREAAGPHEAFNKLWELCCQWLKPKMRSKEQILELLVLEQFLTILPTEIETWVREHCPENRERVVSLIE 106
Cdd:smart00431   2 EIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLE 81

                           90       100       110
                   ....*....|....*....|....*....|..
gi 194239638   107 DLQRELEIPEQQVDMH----DMLLEELAPVGT 134
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 ...
 27-113 1.43e-47

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: 159.58  E-value: 1.43e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194239638   27 EVFRQRFRQFQYREAAGPHEAFNKLWELCCQWLKPKMRSKEQILELLVLEQFLTILPTEIETWVREHCPENRERVVSLIE 106
Cdd:pfam02023   2 EASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALAE 81


                  ....*..
gi 194239638  107 DLQRELE 113
Cdd:pfam02023  82 DLLLERG 88
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 26-110 1.68e-36

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: 130.07  E-value: 1.68e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194239638  26 CEVFRQRFRQFQYREAAGPHEAFNKLWELCCQWLKPKMRSKEQILELLVLEQFLTILPTEIETWVREHCPENRERVVSLI 105
Cdd:cd07936    1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80


                 ....*
gi 194239638 106 EDLQR 110
Cdd:cd07936   81 EDLLA 85
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
321-483 2.36e-15

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 78.20  E-value: 2.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194239638 321 KPHRCPQCGKCFARKSQLTGHQR--IHSGE--EPHKCPE--CGKRFLRSSDLYRHQRLHTGERPYEC--TVCKKRFTRRS 392
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194239638 393 HLIGHQRT--HSEEETYKCLECGKSFCHG-----SSLKRHLKTHTGEKPHRCHN--CGKSFSRLTALTLHQRTHTEERPF 463
Cdd:COG5048  368 NNEPPQSLqqYKDLKNDKKSETLSNSCIRnfkrdSNLSLHIITHLSFRPYNCKNppCSKSFNRHYNLIPHKKIHTNHAPL 447

                        170       180
                 ....*....|....*....|
gi 194239638 464 KCNYCgKSFRQRPSLVIHLR 483
Cdd:COG5048  448 LCSIL-KSFRRDLDLSNHGK 466
zf-H2C2_2 pfam13465
Zinc-finger double domain;
421-446 1.38e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 44.67  E-value: 1.38e-06
                          10        20
                  ....*....|....*....|....*.
gi 194239638  421 SLKRHLKTHTGEKPHRCHNCGKSFSR 446
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
477-502 3.27e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 3.27e-05
                          10        20
                  ....*....|....*....|....*.
gi 194239638  477 SLVIHLRIHTGEKPYKCTHCSKSFRQ 502
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 235-402 2.10e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 43.94  E-value: 2.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194239638 235 DTSKQKKMETMYPFIVTLEGN-ALQGPILQKDYVQLENQwetpPEDLQTDLAKLVdQQNPTLGETPeNSNLeeplnpkph 313
Cdd:COG5189  278 ELFEESSLGFDYEFIHKSVGNkEIRGGISTGEMIDVRKL----PCTNSSSNGKLA-HGGERNIDTP-SRML--------- 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194239638 314 kkKSPGEKPHRCP--QCGKCFARKSQLTGHqRIHSGEEPHKCPecgkrflrSSDLYRHQRLHTGERPYECTVCKKRFTRR 391
Cdd:COG5189  343 --KVKDGKPYKCPveGCNKKYKNQNGLKYH-MLHGHQNQKLHE--------NPSPEKMNIFSAKDKPYRCEVCDKRYKNL 411

                        170
                 ....*....|.
gi 194239638 392 SHLIGHqRTHS 402
Cdd:COG5189  412 NGLKYH-RKHS 421
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 437-485 2.28e-04

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 39.85  E-value: 2.28e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 194239638 437 CHNCGKSFSRLTALTLHQRTHTeerpFKCNYCGKSFRQRPSLVIH-LRIH 485
Cdd:cd20908    4 CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
27-134 4.40e-51

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 169.79  E-value: 4.40e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194239638    27 EVFRQRFRQFQYREAAGPHEAFNKLWELCCQWLKPKMRSKEQILELLVLEQFLTILPTEIETWVREHCPENRERVVSLIE 106
Cdd:smart00431   2 EIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLE 81

                           90       100       110
                   ....*....|....*....|....*....|..
gi 194239638   107 DLQRELEIPEQQVDMH----DMLLEELAPVGT 134
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 ...
 27-113 1.43e-47

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: 159.58  E-value: 1.43e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194239638   27 EVFRQRFRQFQYREAAGPHEAFNKLWELCCQWLKPKMRSKEQILELLVLEQFLTILPTEIETWVREHCPENRERVVSLIE 106
Cdd:pfam02023   2 EASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALAE 81


                  ....*..
gi 194239638  107 DLQRELE 113
Cdd:pfam02023  82 DLLLERG 88
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 26-110 1.68e-36

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: 130.07  E-value: 1.68e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194239638  26 CEVFRQRFRQFQYREAAGPHEAFNKLWELCCQWLKPKMRSKEQILELLVLEQFLTILPTEIETWVREHCPENRERVVSLI 105
Cdd:cd07936    1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80


                 ....*
gi 194239638 106 EDLQR 110
Cdd:cd07936   81 EDLLA 85
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
321-483 2.36e-15

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 78.20  E-value: 2.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194239638 321 KPHRCPQCGKCFARKSQLTGHQR--IHSGE--EPHKCPE--CGKRFLRSSDLYRHQRLHTGERPYEC--TVCKKRFTRRS 392
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194239638 393 HLIGHQRT--HSEEETYKCLECGKSFCHG-----SSLKRHLKTHTGEKPHRCHN--CGKSFSRLTALTLHQRTHTEERPF 463
Cdd:COG5048  368 NNEPPQSLqqYKDLKNDKKSETLSNSCIRnfkrdSNLSLHIITHLSFRPYNCKNppCSKSFNRHYNLIPHKKIHTNHAPL 447

                        170       180
                 ....*....|....*....|
gi 194239638 464 KCNYCgKSFRQRPSLVIHLR 483
Cdd:COG5048  448 LCSIL-KSFRRDLDLSNHGK 466
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
301-503 1.03e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 60.86  E-value: 1.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194239638 301 NSNLEEPLNPKpHKKKSPGEKPHRCPQCGKCFARKSQLTGHQRIHSGEEPHKC--PECGKRFLRSSDLYRHQRLHTGERP 378
Cdd:COG5048   13 NSVLSSTPKST-LKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPS 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194239638 379 YEC--TVCKKRFTRRSHLIGHQRTHSeeeTYKCLECGKSFCH--GSSLKRHLKTHTGEKPHRCHNCGKSF---------- 444
Cdd:COG5048   92 DLNskSLPLSNSKASSSSLSSSSSNS---NDNNLLSSHSLPPssRDPQLPDLLSISNLRNNPLPGNNSSSvntpqsnslh 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194239638 445 ------------SRLTALTLHQRTHTEERPFKCNYCGKSFRQRPSLVIHLRIHTGEKPYKCTHCSKSFRQR 503
Cdd:COG5048  169 pplpanslskdpSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKS 239
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
263-502 2.68e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.16  E-value: 2.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194239638 263 QKDYVQLENQWETPPEDLQTDLAKLVDQQNPT-LGETPENSNLEEPLNPKPHKKKSPGEKPHRCpqcgkcfarksqltgH 341
Cdd:COG5048  125 SHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSsSVNTPQSNSLHPPLPANSLSKDPSSNLSLLI---------------S 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194239638 342 QRIHSGEEPHKCPECGKRFLRSSDLYRHQRLHTGERPYECT----VCKKRFTRRSHLIGHQRTHSEEETYKCLEC-GKSF 416
Cdd:COG5048  190 SNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTtnsqLSPKSLLSQSPSSLSSSDSSSSASESPRSSlPTAS 269

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194239638 417 CHGSSLKRHL-KTHTG-EKPHRCHNCGKSFSRLTALTLHQRT--HTEE--RPFKC--NYCGKSFRQRPSLVIHLRIHTGE 488
Cdd:COG5048  270 SQSSSPNESDsSSEKGfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSI 349

                        250
                 ....*....|....*.
gi 194239638 489 KPYKC--THCSKSFRQ 502
Cdd:COG5048  350 SPAKEklLNSSSKFSP 365
zf-H2C2_2 pfam13465
Zinc-finger double domain;
421-446 1.38e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 44.67  E-value: 1.38e-06
                          10        20
                  ....*....|....*....|....*.
gi 194239638  421 SLKRHLKTHTGEKPHRCHNCGKSFSR 446
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
477-502 3.27e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 3.27e-05
                          10        20
                  ....*....|....*....|....*.
gi 194239638  477 SLVIHLRIHTGEKPYKCTHCSKSFRQ 502
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
365-390 4.69e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 4.69e-05
                          10        20
                  ....*....|....*....|....*.
gi 194239638  365 DLYRHQRLHTGERPYECTVCKKRFTR 390
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
449-474 1.33e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.33e-04
                          10        20
                  ....*....|....*....|....*.
gi 194239638  449 ALTLHQRTHTEERPFKCNYCGKSFRQ 474
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 235-402 2.10e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 43.94  E-value: 2.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194239638 235 DTSKQKKMETMYPFIVTLEGN-ALQGPILQKDYVQLENQwetpPEDLQTDLAKLVdQQNPTLGETPeNSNLeeplnpkph 313
Cdd:COG5189  278 ELFEESSLGFDYEFIHKSVGNkEIRGGISTGEMIDVRKL----PCTNSSSNGKLA-HGGERNIDTP-SRML--------- 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194239638 314 kkKSPGEKPHRCP--QCGKCFARKSQLTGHqRIHSGEEPHKCPecgkrflrSSDLYRHQRLHTGERPYECTVCKKRFTRR 391
Cdd:COG5189  343 --KVKDGKPYKCPveGCNKKYKNQNGLKYH-MLHGHQNQKLHE--------NPSPEKMNIFSAKDKPYRCEVCDKRYKNL 411

                        170
                 ....*....|.
gi 194239638 392 SHLIGHqRTHS 402
Cdd:COG5189  412 NGLKYH-RKHS 421
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 437-485 2.28e-04

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 39.85  E-value: 2.28e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 194239638 437 CHNCGKSFSRLTALTLHQRTHTeerpFKCNYCGKSFRQRPSLVIH-LRIH 485
Cdd:cd20908    4 CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 323-345 3.30e-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: 38.05  E-value: 3.30e-04
                          10        20
                  ....*....|....*....|...
gi 194239638  323 HRCPQCGKCFARKSQLTGHQRIH 345
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 379-401 4.05e-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: 37.66  E-value: 4.05e-04
                          10        20
                  ....*....|....*....|...
gi 194239638  379 YECTVCKKRFTRRSHLIGHQRTH 401
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 435-457 4.22e-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: 37.66  E-value: 4.22e-04
                          10        20
                  ....*....|....*....|...
gi 194239638  435 HRCHNCGKSFSRLTALTLHQRTH 457
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
341-362 4.48e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 4.48e-04
                          10        20
                  ....*....|....*....|..
gi 194239638  341 HQRIHSGEEPHKCPECGKRFLR 362
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 463-485 5.60e-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: 37.28  E-value: 5.60e-04
                          10        20
                  ....*....|....*....|...
gi 194239638  463 FKCNYCGKSFRQRPSLVIHLRIH 485
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 407-429 5.83e-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: 37.28  E-value: 5.83e-04
                          10        20
                  ....*....|....*....|...
gi 194239638  407 YKCLECGKSFCHGSSLKRHLKTH 429
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
ROS_MUCR pfam05443
ROS/MUCR transcriptional regulator protein; This family consists of several ROS/MUCR ...
 409-429 6.08e-04

ROS/MUCR transcriptional regulator protein; This family consists of several ROS/MUCR transcriptional regulator proteins. The ros chromosomal gene is present in octopine and nopaline strains of Agrobacterium tumefaciens as well as in Rhizobium meliloti. This gene encodes a 15.5-kDa protein that specifically represses the virC and virD operons in the virulence region of the Ti plasmid and is necessary for succinoglycan production. Sinorhizobium meliloti can produce two types of acidic exopolysaccharides, succinoglycan and galactoglucan, that are interchangeable for infection of alfalfa nodules. MucR from Sinorhizobium meliloti acts as a transcriptional repressor that blocks the expression of the exp genes responsible for galactoglucan production therefore allowing the exclusive production of succinoglycan.


Pssm-ID: 428475  Cd Length: 122  Bit Score: 39.75  E-value: 6.08e-04
                          10        20
                  ....*....|....*....|.
gi 194239638  409 CLECGKSFchgSSLKRHLKTH 429
Cdd:pfam05443  67 CLEDGKPF---KTLKRHLTAH 84
COG4957 COG4957
Predicted transcriptional regulator [Transcription];
409-434 1.11e-03

Predicted transcriptional regulator [Transcription];


Pssm-ID: 443984  Cd Length: 141  Bit Score: 39.42  E-value: 1.11e-03
                         10        20
                 ....*....|....*....|....*.
gi 194239638 409 CLECGKSFchgSSLKRHLKTHTGEKP 434
Cdd:COG4957   74 CLEDGKKF---KMLKRHLRTTHGLTP 96
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 351-373 1.52e-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: 1.52e-03
                          10        20
                  ....*....|....*....|...
gi 194239638  351 HKCPECGKRFLRSSDLYRHQRLH 373
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 491-513 8.24e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 33.81  E-value: 8.24e-03
                          10        20
                  ....*....|....*....|...
gi 194239638  491 YKCTHCSKSFRQRAGLIMHQVTH 513
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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