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Conserved domains on  [gi|119605809|gb|EAW85403|]
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zinc finger protein 206 [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;
2-71 1.31e-25

leucine rich region;


The actual alignment was detected with superfamily member smart00431:

Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 102.00  E-value: 1.31e-25
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605809     2 GPRASLSRLRELCGHWLRPALHTKKQILELLVLEQFLSVLPPHLLGRLQGQPLRDGEEVVLLLEGIHREP 71
Cdd:smart00431  18 GPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLEDLEREL 87
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
345-719 2.09e-15

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 79.35  E-value: 2.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605809 345 DERPHACHLCGHRFRQSSHLSKHLLTHSSEPAFLCAECGRG--FQRRASLVQHLLAHAQ-------DQKPPC---APESK 412
Cdd:COG5048   30 APRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHHNnpsdlnsKSLPLSnskASSSS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605809 413 AEAPPLTDV---LCSHCGQSFQRRSSLKRHLR--IHARDKD----RRSSEGSGSRRRDSDRRPFVCSDCGKAFRRSEHLv 483
Cdd:COG5048  110 LSSSSSNSNdnnLLSSHSLPPSSRDPQLPDLLsiSNLRNNPlpgnNSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLI- 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605809 484 aHRRVHTGERPFSCQACGRSFTQSSQLVSHQRVHTGEKPYACPQCGKRFVRRASLARHLLTHGGPRPHHCTQCGKSFGQT 563
Cdd:COG5048  189 -SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPT 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605809 564 QDLARHQRSHTGE-------KPCRCSECGEGFSQSAHLARHQR--IHTGE--KPHACD--TCGHRFRNSSNLARHRRSHT 630
Cdd:COG5048  268 ASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPysLCGKLFSRNDALKRHILLHT 347

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605809 631 GERPYSCQTCGRSFRRN------AHLRRHLATHAEPGQEQAEPPQECVecgKSFSRSCNLLRHLLVHTGARPYSC--TQC 702
Cdd:COG5048  348 SISPAKEKLLNSSSKFSpllnnePPQSLQQYKDLKNDKKSETLSNSCI---RNFKRDSNLSLHIITHLSFRPYNCknPPC 424

                        410
                 ....*....|....*..
gi 119605809 703 GRSFSRNSHLLRHLRTH 719
Cdd:COG5048  425 SKSFNRHYNLIPHKKIH 441
PHA03418 super family cl25519
hypothetical E4 protein; Provisional
 101-259 1.41e-04

hypothetical E4 protein; Provisional


The actual alignment was detected with superfamily member PHA03418:

Pssm-ID: 177646 [Multi-domain]  Cd Length: 230  Bit Score: 43.96  E-value: 1.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605809 101 SQVPSHSPKKELPAEEPSvlGPSDEPPRPQPraaqPAEPGQWRLPPSSKQPLSPGPQKTFQAlqessPQGP----SPWPE 176
Cdd:PHA03418  36 LPAPHHPNPQEDPDKNPS--PPPDPPLTPRP----PAQPNGHNKPPVTKQPGGEGTEEDHQA-----PLAAdaddDPRPG 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605809 177 ESSRDQElaavlecltfedvpenkawPAHPLGFGSRTPDKEEFKQEEPKGAAWPTPILAESQADSPGVPGEPCAQSLGRG 256
Cdd:PHA03418 105 KRSKADE-------------------HGPAPGRAALAPFKLDLDQDPLHGDPDPPPGATGGQGEEPPEGGEESQPPLGEG 165


                 ...
gi 119605809 257 AAA 259
Cdd:PHA03418 166 EGA 168
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
2-71 1.31e-25

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 102.00  E-value: 1.31e-25
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605809     2 GPRASLSRLRELCGHWLRPALHTKKQILELLVLEQFLSVLPPHLLGRLQGQPLRDGEEVVLLLEGIHREP 71
Cdd:smart00431  18 GPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLEDLEREL 87
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 1-69 8.52e-24

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: 95.79  E-value: 8.52e-24
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119605809   1 MGPRASLSRLRELCGHWLRPALHTKKQILELLVLEQFLSVLPPHLLGRLQGQPLRDGEEVVLLLEGIHR 69
Cdd:cd07936   17 SGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLAEDLLA 85
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 2-71 9.49e-24

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: 95.63  E-value: 9.49e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605809    2 GPRASLSRLRELCGHWLRPALHTKKQILELLVLEQFLSVLPPHLLGRLQGQPLRDGEEVVLLLEGIHREP 71
Cdd:pfam02023  18 GPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALAEDLLLER 87
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
345-719 2.09e-15

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 79.35  E-value: 2.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605809 345 DERPHACHLCGHRFRQSSHLSKHLLTHSSEPAFLCAECGRG--FQRRASLVQHLLAHAQ-------DQKPPC---APESK 412
Cdd:COG5048   30 APRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHHNnpsdlnsKSLPLSnskASSSS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605809 413 AEAPPLTDV---LCSHCGQSFQRRSSLKRHLR--IHARDKD----RRSSEGSGSRRRDSDRRPFVCSDCGKAFRRSEHLv 483
Cdd:COG5048  110 LSSSSSNSNdnnLLSSHSLPPSSRDPQLPDLLsiSNLRNNPlpgnNSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLI- 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605809 484 aHRRVHTGERPFSCQACGRSFTQSSQLVSHQRVHTGEKPYACPQCGKRFVRRASLARHLLTHGGPRPHHCTQCGKSFGQT 563
Cdd:COG5048  189 -SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPT 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605809 564 QDLARHQRSHTGE-------KPCRCSECGEGFSQSAHLARHQR--IHTGE--KPHACD--TCGHRFRNSSNLARHRRSHT 630
Cdd:COG5048  268 ASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPysLCGKLFSRNDALKRHILLHT 347

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605809 631 GERPYSCQTCGRSFRRN------AHLRRHLATHAEPGQEQAEPPQECVecgKSFSRSCNLLRHLLVHTGARPYSC--TQC 702
Cdd:COG5048  348 SISPAKEKLLNSSSKFSpllnnePPQSLQQYKDLKNDKKSETLSNSCI---RNFKRDSNLSLHIITHLSFRPYNCknPPC 424

                        410
                 ....*....|....*..
gi 119605809 703 GRSFSRNSHLLRHLRTH 719
Cdd:COG5048  425 SKSFNRHYNLIPHKKIH 441
zf-H2C2_2 pfam13465
Zinc-finger double domain;
510-534 6.52e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 6.52e-05
                          10        20
                  ....*....|....*....|....*
gi 119605809  510 LVSHQRVHTGEKPYACPQCGKRFVR 534
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
PHA03418 PHA03418
hypothetical E4 protein; Provisional
 101-259 1.41e-04

hypothetical E4 protein; Provisional


Pssm-ID: 177646 [Multi-domain]  Cd Length: 230  Bit Score: 43.96  E-value: 1.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605809 101 SQVPSHSPKKELPAEEPSvlGPSDEPPRPQPraaqPAEPGQWRLPPSSKQPLSPGPQKTFQAlqessPQGP----SPWPE 176
Cdd:PHA03418  36 LPAPHHPNPQEDPDKNPS--PPPDPPLTPRP----PAQPNGHNKPPVTKQPGGEGTEEDHQA-----PLAAdaddDPRPG 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605809 177 ESSRDQElaavlecltfedvpenkawPAHPLGFGSRTPDKEEFKQEEPKGAAWPTPILAESQADSPGVPGEPCAQSLGRG 256
Cdd:PHA03418 105 KRSKADE-------------------HGPAPGRAALAPFKLDLDQDPLHGDPDPPPGATGGQGEEPPEGGEESQPPLGEG 165


                 ...
gi 119605809 257 AAA 259
Cdd:PHA03418 166 EGA 168
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 493-544 9.17e-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: 38.69  E-value: 9.17e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 119605809 493 RPFsCQACGRSFTQSSQLVSHQRvhtgEKPYACPQCGKRFVRRASLARHLLT 544
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQK----AKHFKCHICHKKLYTAGGLAVHCLQ 47
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
2-71 1.31e-25

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 102.00  E-value: 1.31e-25
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605809     2 GPRASLSRLRELCGHWLRPALHTKKQILELLVLEQFLSVLPPHLLGRLQGQPLRDGEEVVLLLEGIHREP 71
Cdd:smart00431  18 GPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLEDLEREL 87
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 1-69 8.52e-24

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: 95.79  E-value: 8.52e-24
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119605809   1 MGPRASLSRLRELCGHWLRPALHTKKQILELLVLEQFLSVLPPHLLGRLQGQPLRDGEEVVLLLEGIHR 69
Cdd:cd07936   17 SGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLAEDLLA 85
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 2-71 9.49e-24

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: 95.63  E-value: 9.49e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605809    2 GPRASLSRLRELCGHWLRPALHTKKQILELLVLEQFLSVLPPHLLGRLQGQPLRDGEEVVLLLEGIHREP 71
Cdd:pfam02023  18 GPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALAEDLLLER 87
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
345-719 2.09e-15

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 79.35  E-value: 2.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605809 345 DERPHACHLCGHRFRQSSHLSKHLLTHSSEPAFLCAECGRG--FQRRASLVQHLLAHAQ-------DQKPPC---APESK 412
Cdd:COG5048   30 APRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHHNnpsdlnsKSLPLSnskASSSS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605809 413 AEAPPLTDV---LCSHCGQSFQRRSSLKRHLR--IHARDKD----RRSSEGSGSRRRDSDRRPFVCSDCGKAFRRSEHLv 483
Cdd:COG5048  110 LSSSSSNSNdnnLLSSHSLPPSSRDPQLPDLLsiSNLRNNPlpgnNSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLI- 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605809 484 aHRRVHTGERPFSCQACGRSFTQSSQLVSHQRVHTGEKPYACPQCGKRFVRRASLARHLLTHGGPRPHHCTQCGKSFGQT 563
Cdd:COG5048  189 -SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPT 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605809 564 QDLARHQRSHTGE-------KPCRCSECGEGFSQSAHLARHQR--IHTGE--KPHACD--TCGHRFRNSSNLARHRRSHT 630
Cdd:COG5048  268 ASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPysLCGKLFSRNDALKRHILLHT 347

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605809 631 GERPYSCQTCGRSFRRN------AHLRRHLATHAEPGQEQAEPPQECVecgKSFSRSCNLLRHLLVHTGARPYSC--TQC 702
Cdd:COG5048  348 SISPAKEKLLNSSSKFSpllnnePPQSLQQYKDLKNDKKSETLSNSCI---RNFKRDSNLSLHIITHLSFRPYNCknPPC 424

                        410
                 ....*....|....*..
gi 119605809 703 GRSFSRNSHLLRHLRTH 719
Cdd:COG5048  425 SKSFNRHYNLIPHKKIH 441
zf-H2C2_2 pfam13465
Zinc-finger double domain;
510-534 6.52e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 6.52e-05
                          10        20
                  ....*....|....*....|....*
gi 119605809  510 LVSHQRVHTGEKPYACPQCGKRFVR 534
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
PHA03418 PHA03418
hypothetical E4 protein; Provisional
 101-259 1.41e-04

hypothetical E4 protein; Provisional


Pssm-ID: 177646 [Multi-domain]  Cd Length: 230  Bit Score: 43.96  E-value: 1.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605809 101 SQVPSHSPKKELPAEEPSvlGPSDEPPRPQPraaqPAEPGQWRLPPSSKQPLSPGPQKTFQAlqessPQGP----SPWPE 176
Cdd:PHA03418  36 LPAPHHPNPQEDPDKNPS--PPPDPPLTPRP----PAQPNGHNKPPVTKQPGGEGTEEDHQA-----PLAAdaddDPRPG 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605809 177 ESSRDQElaavlecltfedvpenkawPAHPLGFGSRTPDKEEFKQEEPKGAAWPTPILAESQADSPGVPGEPCAQSLGRG 256
Cdd:PHA03418 105 KRSKADE-------------------HGPAPGRAALAPFKLDLDQDPLHGDPDPPPGATGGQGEEPPEGGEESQPPLGEG 165


                 ...
gi 119605809 257 AAA 259
Cdd:PHA03418 166 EGA 168
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 697-719 1.70e-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: 1.70e-04
                          10        20
                  ....*....|....*....|...
gi 119605809  697 YSCTQCGRSFSRNSHLLRHLRTH 719
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 102-287 5.35e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 43.54  E-value: 5.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605809  102 QVPSHSPKKELPAEEPSVLGPSDEP---PRPQPRAAQPAEPGQWRLPPsskQPLSPGPQKTFQ---ALQESSPQGPS--- 172
Cdd:PRK10263  404 QQPYYAPAAEQPAQQPYYAPAPEQPaqqPYYAPAPEQPVAGNAWQAEE---QQSTFAPQSTYQteqTYQQPAAQEPLyqq 480

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605809  173 PWPEESSRDQELAAVLE--------CLTFEDVPENKAWPAHPLGfGSRTPDKEEFKQEEPKGAAWPTPILAESQADSPGV 244
Cdd:PRK10263  481 PQPVEQQPVVEPEPVVEetkparppLYYFEEVEEKRAREREQLA-AWYQPIPEPVKEPEPIKSSLKAPSVAAVPPVEAAA 559

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 119605809  245 PGEPCAQSLGRGAAASGPGEDGSL----LGSSEILEVKVAEGV----PEPN 287
Cdd:PRK10263  560 AVSPLASGVKKATLATGAAATVAApvfsLANSGGPRPQVKEGIgpqlPRPK 610
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 493-544 9.17e-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: 38.69  E-value: 9.17e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 119605809 493 RPFsCQACGRSFTQSSQLVSHQRvhtgEKPYACPQCGKRFVRRASLARHLLT 544
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQK----AKHFKCHICHKKLYTAGGLAVHCLQ 47
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 467-489 1.28e-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: 36.51  E-value: 1.28e-03
                          10        20
                  ....*....|....*....|...
gi 119605809  467 FVCSDCGKAFRRSEHLVAHRRVH 489
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
336-360 1.39e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.39e-03
                          10        20
                  ....*....|....*....|....*
gi 119605809  336 LKLHMRTHTDERPHACHLCGHRFRQ 360
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 635-657 1.70e-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: 1.70e-03
                          10        20
                  ....*....|....*....|...
gi 119605809  635 YSCQTCGRSFRRNAHLRRHLATH 657
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA03247 PHA03247
large tegument protein UL36; Provisional
 104-262 2.53e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605809  104 PSHSPKKELPAEEPSVLGPSDEPPRPQPRAA--QPAEPGQWRLPPSSKQPLSPGPQKTF---QALQESSPQGPSPWPEES 178
Cdd:PHA03247 2604 DRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAanEPDPHPPPTVPPPERPRDDPAPGRVSrprRARRLGRAAQASSPPQRP 2683

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605809  179 SRDQELAAVLECLTFEDVPENKAWPA---HPLGFGSRTP-DKEEFKQEEPKGAAWPTPILAESQADSPGVPGEPCAQSLG 254
Cdd:PHA03247 2684 RRRAARPTVGSLTSLADPPPPPPTPEpapHALVSATPLPpGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTT 2763


                  ....*...
gi 119605809  255 RGAAASGP 262
Cdd:PHA03247 2764 AGPPAPAP 2771
PHA03247 PHA03247
large tegument protein UL36; Provisional
 104-289 2.85e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 2.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605809  104 PSHSPKKELPA------EEPSVLGPSDEPPRPQPRAAQPAEPGQWRLPPSSKQPLSPGPQKTFQALQESSPQGPSPWPEE 177
Cdd:PHA03247 2878 PARPPVRRLARpavsrsTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSG 2957

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605809  178 SSRDQELAAVLECLTfeDVPENKAWPAHPLGFGSRTPDKEEFKQEEPKGAAWPTPILAESQADSPGVpgePCAQSLGRGA 257
Cdd:PHA03247 2958 AVPQPWLGALVPGRV--AVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSWASSLALHEETDPPPV---SLKQTLWPPD 3032

                         170       180       190
                  ....*....|....*....|....*....|..
gi 119605809  258 AASGPGEDGSLLGSSEILEVKVAEgvPEPNPE 289
Cdd:PHA03247 3033 DTEDSDADSLFDSDSERSDLEALD--PLPPEP 3062
PHA03247 PHA03247
large tegument protein UL36; Provisional
 100-174 3.05e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 3.05e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119605809  100 ASQVPSHSPKKELPAEEPSVLGPSDEPPRPQPRAAQPAEPGQWRLPPSSKQPLSP-GPQKTFQALQESSPQGPSPW 174
Cdd:PHA03247 2888 RPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPlAPTTDPAGAGEPSGAVPQPW 2963
zf-H2C2_2 pfam13465
Zinc-finger double domain;
537-560 3.06e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.06e-03
                          10        20
                  ....*....|....*....|....
gi 119605809  537 SLARHLLTHGGPRPHHCTQCGKSF 560
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 523-545 6.54e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.58  E-value: 6.54e-03
                          10        20
                  ....*....|....*....|...
gi 119605809  523 YACPQCGKRFVRRASLARHLLTH 545
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
656-719 7.49e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 39.29  E-value: 7.49e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119605809 656 THAEPGQEQAEPPQECVECGKSFSRSCNLLRHLLVHTGARPYSCTQCGR--SFSRNSHLLRHLRTH 719
Cdd:COG5048   21 KSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCdkSFSRPLELSRHLRTH 86
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 423-443 7.80e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.20  E-value: 7.80e-03
                          10        20
                  ....*....|....*....|.
gi 119605809  423 CSHCGQSFQRRSSLKRHLRIH 443
Cdd:pfam00096   3 CPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
683-708 8.01e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 8.01e-03
                          10        20
                  ....*....|....*....|....*.
gi 119605809  683 NLLRHLLVHTGARPYSCTQCGRSFSR 708
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
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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