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Conserved domains on  [gi|1953082141|ref|XP_038397640|]
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zinc finger protein 316-like isoform X2 [Canis lupus familiaris]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
38-149 2.89e-66

leucine rich region;


:

Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 217.17  E-value: 2.89e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141   38 EVFRQRFRQFGYHDTPGPREALSQLRVLCCEWLRPEIHTKEQILELLVLEQFLTILPQELQAWVQEHCPESAEEAVTLLE 117
Cdd:smart00431   2 EIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLE 81

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1953082141  118 DLEQELDEPGQQVSSPPSEQQQMWEKKSSSGT 149
Cdd:smart00431  82 DLERELDEPGQQVSAHVHGQEVLLEKMVPLGA 113
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 566-607 5.05e-22

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: 89.45  E-value: 5.05e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1953082141 566 LVTFEDVAVYFIRKEWKRLEPAQRDLYRDVMLENYGNVFSLD 607
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
394-869 2.24e-13

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 73.58  E-value: 2.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 394 SQHAGLSSHQRLHTGE----KPYKCKECGKAFNHSSNFNKHHRIHTGEKPYWCN--NCGKTFCSKSNLSKHQRVHTGEGE 467
Cdd:COG5048    12 NNSVLSSTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 468 VLSAGDpgrsgkvRSPSPSKTRPRPPAAPAVGSgsaartRDPELLALPmetqaDCKTQEPQALLESALPSSKVPAFSDKD 547
Cdd:COG5048    92 DLNSKS-------LPLSNSKASSSSLSSSSSNS------NDNNLLSSH-----SLPPSSRDPQLPDLLSISNLRNNPLPG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 548 SLGDEmlaaallKAKSQELVTFEDVAVYFIRKEWkrlepaqrdlyrdvmleNYGNVFSLDGETRTEHDQdISEDTgsrgv 627
Cdd:COG5048   154 NNSSS-------VNTPQSNSLHPPLPANSLSKDP-----------------SSNLSLLISSNVSTSIPS-SSENS----- 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 628 lLGRFQKDISQGLKFEEAYEQDVSLKRQLGNSSGERLDRKIQDFGQMTDEEKLTPGGERSekySDFGNSLTVSSNLISHQ 707
Cdd:COG5048   204 -PLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPR---SSLPTASSQSSSPNESD 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 708 RLPVGDR--PHKCDECSKSFNRTSDLIQHQR--IHTGE--KPYECSE--CGKAFSQSSHLIQHQRIHTGEKPYEC--NDC 777
Cdd:COG5048   280 SSSEKGFslPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNS 359

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 778 GKTFS-----CSSALILHRRIHTGEKPYEC--NECGKTFSWSSTLTHHQRIHTGEKPYACN--ECGKAFSRSSTLIHHQR 848
Cdd:COG5048   360 SSKFSpllnnEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKK 439

                         490       500
                  ....*....|....*....|.
gi 1953082141 849 IHTGEKPYECNECGKAFSQSS 869
Cdd:COG5048   440 IHTNHAPLLCSILKSFRRDLD 460
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
272-449 7.26e-10

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 62.41  E-value: 7.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 272 RYICAECGKAFSNSSNLTKHRRT--HTGE--KPYVCTK--CGKAFSHSSNLTLHYRTHLVDRPYDCK---CGKAFGQSSD 342
Cdd:COG5048   289 PIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllnSSSKFSPLLN 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 343 LLKHQRMHteeapyqckdcgkafsgkgslirHYRIHTGEKPYQC--NECGKSFSQHAGLSSHQRLHTGEKPY--KCKECG 418
Cdd:COG5048   369 NEPPQSLQ-----------------------QYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYncKNPPCS 425

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1953082141 419 KAFNHSSNFNKHHRIHTGEKPYWCNNCGKTF 449
Cdd:COG5048   426 KSFNRHYNLIPHKKIHTNHAPLLCSILKSFR 456
zf-H2C2_2 pfam13465
Zinc-finger double domain;
870-895 3.40e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 3.40e-05
                          10        20
                  ....*....|....*....|....*.
gi 1953082141 870 HLYQHQRIHTGEKPYECMECGGKFTY 895
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
899-923 1.73e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.73e-04
                          10        20
                  ....*....|....*....|....*
gi 1953082141 899 LIQHQRIHTGENPYECSECGKAFRY 923
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
38-149 2.89e-66

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 217.17  E-value: 2.89e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141   38 EVFRQRFRQFGYHDTPGPREALSQLRVLCCEWLRPEIHTKEQILELLVLEQFLTILPQELQAWVQEHCPESAEEAVTLLE 117
Cdd:smart00431   2 EIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLE 81

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1953082141  118 DLEQELDEPGQQVSSPPSEQQQMWEKKSSSGT 149
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 ...
 37-125 3.80e-52

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: 176.91  E-value: 3.80e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141  37 LEVFRQRFRQFGYHDTPGPREALSQLRVLCCEWLRPEIHTKEQILELLVLEQFLTILPQELQAWVQEHCPESAEEAVTLL 116
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALA 80


                  ....*....
gi 1953082141 117 EDLEQELDE 125
Cdd:pfam02023  81 EDLLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 37-121 1.16e-43

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: 152.80  E-value: 1.16e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141  37 LEVFRQRFRQFGYHDTPGPREALSQLRVLCCEWLRPEIHTKEQILELLVLEQFLTILPQELQAWVQEHCPESAEEAVTLL 116
Cdd:cd07936     1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80


                  ....*
gi 1953082141 117 EDLEQ 121
Cdd:cd07936    81 EDLLA 85
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 566-607 5.05e-22

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: 89.45  E-value: 5.05e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1953082141 566 LVTFEDVAVYFIRKEWKRLEPAQRDLYRDVMLENYGNVFSLD 607
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
567-612 1.19e-21

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 89.19  E-value: 1.19e-21
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1953082141  567 VTFEDVAVYFIRKEWKRLEPAQRDLYRDVMLENYGNVFSLDGETRT 612
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPK 46
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 567-606 2.45e-21

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: 87.60  E-value: 2.45e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1953082141 567 VTFEDVAVYFIRKEWKRLEPAQRDLYRDVMLENYGNVFSL 606
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
394-869 2.24e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 73.58  E-value: 2.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 394 SQHAGLSSHQRLHTGE----KPYKCKECGKAFNHSSNFNKHHRIHTGEKPYWCN--NCGKTFCSKSNLSKHQRVHTGEGE 467
Cdd:COG5048    12 NNSVLSSTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 468 VLSAGDpgrsgkvRSPSPSKTRPRPPAAPAVGSgsaartRDPELLALPmetqaDCKTQEPQALLESALPSSKVPAFSDKD 547
Cdd:COG5048    92 DLNSKS-------LPLSNSKASSSSLSSSSSNS------NDNNLLSSH-----SLPPSSRDPQLPDLLSISNLRNNPLPG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 548 SLGDEmlaaallKAKSQELVTFEDVAVYFIRKEWkrlepaqrdlyrdvmleNYGNVFSLDGETRTEHDQdISEDTgsrgv 627
Cdd:COG5048   154 NNSSS-------VNTPQSNSLHPPLPANSLSKDP-----------------SSNLSLLISSNVSTSIPS-SSENS----- 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 628 lLGRFQKDISQGLKFEEAYEQDVSLKRQLGNSSGERLDRKIQDFGQMTDEEKLTPGGERSekySDFGNSLTVSSNLISHQ 707
Cdd:COG5048   204 -PLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPR---SSLPTASSQSSSPNESD 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 708 RLPVGDR--PHKCDECSKSFNRTSDLIQHQR--IHTGE--KPYECSE--CGKAFSQSSHLIQHQRIHTGEKPYEC--NDC 777
Cdd:COG5048   280 SSSEKGFslPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNS 359

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 778 GKTFS-----CSSALILHRRIHTGEKPYEC--NECGKTFSWSSTLTHHQRIHTGEKPYACN--ECGKAFSRSSTLIHHQR 848
Cdd:COG5048   360 SSKFSpllnnEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKK 439

                         490       500
                  ....*....|....*....|.
gi 1953082141 849 IHTGEKPYECNECGKAFSQSS 869
Cdd:COG5048   440 IHTNHAPLLCSILKSFRRDLD 460
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
272-449 7.26e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 62.41  E-value: 7.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 272 RYICAECGKAFSNSSNLTKHRRT--HTGE--KPYVCTK--CGKAFSHSSNLTLHYRTHLVDRPYDCK---CGKAFGQSSD 342
Cdd:COG5048   289 PIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllnSSSKFSPLLN 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 343 LLKHQRMHteeapyqckdcgkafsgkgslirHYRIHTGEKPYQC--NECGKSFSQHAGLSSHQRLHTGEKPY--KCKECG 418
Cdd:COG5048   369 NEPPQSLQ-----------------------QYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYncKNPPCS 425

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1953082141 419 KAFNHSSNFNKHHRIHTGEKPYWCNNCGKTF 449
Cdd:COG5048   426 KSFNRHYNLIPHKKIHTNHAPLLCSILKSFR 456
zf-H2C2_2 pfam13465
Zinc-finger double domain;
370-395 1.12e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 1.12e-05
                          10        20
                  ....*....|....*....|....*.
gi 1953082141 370 SLIRHYRIHTGEKPYQCNECGKSFSQ 395
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
730-755 1.71e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 1.71e-05
                          10        20
                  ....*....|....*....|....*.
gi 1953082141 730 DLIQHQRIHTGEKPYECSECGKAFSQ 755
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
870-895 3.40e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 3.40e-05
                          10        20
                  ....*....|....*....|....*.
gi 1953082141 870 HLYQHQRIHTGEKPYECMECGGKFTY 895
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
899-923 1.73e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.73e-04
                          10        20
                  ....*....|....*....|....*
gi 1953082141 899 LIQHQRIHTGENPYECSECGKAFRY 923
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 742-790 1.31e-03

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 38.69  E-value: 1.31e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1953082141 742 KPYeCSECGKAFSQSSHLIQHQRIHTgekpYECNDCGKTFSCSSALILH 790
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
882-939 3.91e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.83  E-value: 3.91e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 882 KPYECMECGGKFTYSSGLIQHQRIHTGENPYECSECGKAFRYS--SALVRHQRIHTGEKP 939
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSrpLELSRHLRTHHNNPS 91
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
38-149 2.89e-66

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 217.17  E-value: 2.89e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141   38 EVFRQRFRQFGYHDTPGPREALSQLRVLCCEWLRPEIHTKEQILELLVLEQFLTILPQELQAWVQEHCPESAEEAVTLLE 117
Cdd:smart00431   2 EIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLE 81

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1953082141  118 DLEQELDEPGQQVSSPPSEQQQMWEKKSSSGT 149
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 ...
 37-125 3.80e-52

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: 176.91  E-value: 3.80e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141  37 LEVFRQRFRQFGYHDTPGPREALSQLRVLCCEWLRPEIHTKEQILELLVLEQFLTILPQELQAWVQEHCPESAEEAVTLL 116
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALA 80


                  ....*....
gi 1953082141 117 EDLEQELDE 125
Cdd:pfam02023  81 EDLLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 37-121 1.16e-43

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: 152.80  E-value: 1.16e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141  37 LEVFRQRFRQFGYHDTPGPREALSQLRVLCCEWLRPEIHTKEQILELLVLEQFLTILPQELQAWVQEHCPESAEEAVTLL 116
Cdd:cd07936     1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80


                  ....*
gi 1953082141 117 EDLEQ 121
Cdd:cd07936    81 EDLLA 85
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 566-607 5.05e-22

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: 89.45  E-value: 5.05e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1953082141 566 LVTFEDVAVYFIRKEWKRLEPAQRDLYRDVMLENYGNVFSLD 607
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
567-612 1.19e-21

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 89.19  E-value: 1.19e-21
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1953082141  567 VTFEDVAVYFIRKEWKRLEPAQRDLYRDVMLENYGNVFSLDGETRT 612
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPK 46
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 567-606 2.45e-21

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: 87.60  E-value: 2.45e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1953082141 567 VTFEDVAVYFIRKEWKRLEPAQRDLYRDVMLENYGNVFSL 606
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
394-869 2.24e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 73.58  E-value: 2.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 394 SQHAGLSSHQRLHTGE----KPYKCKECGKAFNHSSNFNKHHRIHTGEKPYWCN--NCGKTFCSKSNLSKHQRVHTGEGE 467
Cdd:COG5048    12 NNSVLSSTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 468 VLSAGDpgrsgkvRSPSPSKTRPRPPAAPAVGSgsaartRDPELLALPmetqaDCKTQEPQALLESALPSSKVPAFSDKD 547
Cdd:COG5048    92 DLNSKS-------LPLSNSKASSSSLSSSSSNS------NDNNLLSSH-----SLPPSSRDPQLPDLLSISNLRNNPLPG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 548 SLGDEmlaaallKAKSQELVTFEDVAVYFIRKEWkrlepaqrdlyrdvmleNYGNVFSLDGETRTEHDQdISEDTgsrgv 627
Cdd:COG5048   154 NNSSS-------VNTPQSNSLHPPLPANSLSKDP-----------------SSNLSLLISSNVSTSIPS-SSENS----- 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 628 lLGRFQKDISQGLKFEEAYEQDVSLKRQLGNSSGERLDRKIQDFGQMTDEEKLTPGGERSekySDFGNSLTVSSNLISHQ 707
Cdd:COG5048   204 -PLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPR---SSLPTASSQSSSPNESD 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 708 RLPVGDR--PHKCDECSKSFNRTSDLIQHQR--IHTGE--KPYECSE--CGKAFSQSSHLIQHQRIHTGEKPYEC--NDC 777
Cdd:COG5048   280 SSSEKGFslPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNS 359

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 778 GKTFS-----CSSALILHRRIHTGEKPYEC--NECGKTFSWSSTLTHHQRIHTGEKPYACN--ECGKAFSRSSTLIHHQR 848
Cdd:COG5048   360 SSKFSpllnnEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKK 439

                         490       500
                  ....*....|....*....|.
gi 1953082141 849 IHTGEKPYECNECGKAFSQSS 869
Cdd:COG5048   440 IHTNHAPLLCSILKSFRRDLD 460
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
684-930 4.14e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 66.26  E-value: 4.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 684 GERSEKYSDFGNSLTVSSNLISHQRLPVGDRPHKCDECSKSFNRTSDLIQHQRIHTGEKPYECSECGKAFSQSSHLIQHQ 763
Cdd:COG5048   195 SIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSS 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 764 RIHTGE-------KPYECNDCGKTFSCSSALILHRR--IHTGE--KPYECNE--CGKTFSWSSTLTHHQRIHTGEKPYAC 830
Cdd:COG5048   275 PNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKE 354

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 831 --NECGKAFSRSST-----LIHHQRIHTGEKPYEC--NECGKAFSQSSHLYQHQRIHTGEKPYECM--ECGGKFTYSSGL 899
Cdd:COG5048   355 klLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNL 434

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1953082141 900 IQHQRIHTGENPYECSECGKaFRYSSALVRH 930
Cdd:COG5048   435 IPHKKIHTNHAPLLCSILKS-FRRDLDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
272-449 7.26e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 62.41  E-value: 7.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 272 RYICAECGKAFSNSSNLTKHRRT--HTGE--KPYVCTK--CGKAFSHSSNLTLHYRTHLVDRPYDCK---CGKAFGQSSD 342
Cdd:COG5048   289 PIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllnSSSKFSPLLN 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 343 LLKHQRMHteeapyqckdcgkafsgkgslirHYRIHTGEKPYQC--NECGKSFSQHAGLSSHQRLHTGEKPY--KCKECG 418
Cdd:COG5048   369 NEPPQSLQ-----------------------QYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYncKNPPCS 425

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1953082141 419 KAFNHSSNFNKHHRIHTGEKPYWCNNCGKTF 449
Cdd:COG5048   426 KSFNRHYNLIPHKKIHTNHAPLLCSILKSFR 456
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
693-941 1.44e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 61.64  E-value: 1.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 693 FGNSLTVSSNLISHQRLPVGDRPHKCDECSKSFNRTSDLIQHQRIHTGEKPYECSECGKAFSQSSHLIQHQRIHTGEKPY 772
Cdd:COG5048   176 LSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSS 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 773 ECNDCGKTFSCSSALILHRRIHTGE-------KPYECNECGKTFSWSSTLTHHQR--IHTGE--KPYACNE--CGKAFSR 839
Cdd:COG5048   256 SASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSR 335

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 840 SSTLIHHQRIHTGEKPYEC--NECGKAFSQSSHLYQHQRIH-----TGEKPYECME------CGGKFTYSSGLIQH--QR 904
Cdd:COG5048   336 NDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQqykdlKNDKKSETLSnscirnFKRDSNLSLHIITHlsFR 415

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1953082141 905 IHtgenPYECSECGKAFRYSSALVRHQRIHTGEKPLN 941
Cdd:COG5048   416 PY----NCKNPPCSKSFNRHYNLIPHKKIHTNHAPLL 448
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
690-937 3.69e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.93  E-value: 3.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 690 YSDFGNSLTVSSNLISHQRLPVGD-RPHKCDECSKSFNRTSDLIQHQRIHTGEKPYECS--ECGKAFSQSSHLIQHQRIH 766
Cdd:COG5048     7 QSSSSNNSVLSSTPKSTLKSLSNApRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTH 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 767 TGEKPYECNDCG-----KTFSCS-SALILHRRIHTGEKPYECNE------------------------------------ 804
Cdd:COG5048    87 HNNPSDLNSKSLplsnsKASSSSlSSSSSNSNDNNLLSSHSLPPssrdpqlpdllsisnlrnnplpgnnsssvntpqsns 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 805 ----------CGKTFSWSSTLTHHqRIHTGEKPYACNECGKAFSRSSTLIHHQRIHTGEKPYECNECGKAFSQSSHLYQH 874
Cdd:COG5048   167 lhpplpanslSKDPSSNLSLLISS-NVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSP 245

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953082141 875 QRIHTGEKPYECMECGGKFTYSSGLIQHQRIHTGE-------NPYECSECGKAFRYSSALVRHQR--IHTGE 937
Cdd:COG5048   246 SSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGE 317
zf-H2C2_2 pfam13465
Zinc-finger double domain;
370-395 1.12e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 1.12e-05
                          10        20
                  ....*....|....*....|....*.
gi 1953082141 370 SLIRHYRIHTGEKPYQCNECGKSFSQ 395
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
730-755 1.71e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 1.71e-05
                          10        20
                  ....*....|....*....|....*.
gi 1953082141 730 DLIQHQRIHTGEKPYECSECGKAFSQ 755
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
399-423 2.08e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.97  E-value: 2.08e-05
                          10        20
                  ....*....|....*....|....*
gi 1953082141 399 LSSHQRLHTGEKPYKCKECGKAFNH 423
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
758-783 2.48e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.97  E-value: 2.48e-05
                          10        20
                  ....*....|....*....|....*.
gi 1953082141 758 HLIQHQRIHTGEKPYECNDCGKTFSC 783
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
287-312 2.87e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 2.87e-05
                          10        20
                  ....*....|....*....|....*.
gi 1953082141 287 NLTKHRRTHTGEKPYVCTKCGKAFSH 312
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
870-895 3.40e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 3.40e-05
                          10        20
                  ....*....|....*....|....*.
gi 1953082141 870 HLYQHQRIHTGEKPYECMECGGKFTY 895
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
846-867 8.05e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 8.05e-05
                          10        20
                  ....*....|....*....|..
gi 1953082141 846 HQRIHTGEKPYECNECGKAFSQ 867
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 744-766 1.39e-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: 39.59  E-value: 1.39e-04
                          10        20
                  ....*....|....*....|...
gi 1953082141 744 YECSECGKAFSQSSHLIQHQRIH 766
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 412-434 1.49e-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: 39.59  E-value: 1.49e-04
                          10        20
                  ....*....|....*....|...
gi 1953082141 412 YKCKECGKAFNHSSNFNKHHRIH 434
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 273-295 1.55e-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: 39.59  E-value: 1.55e-04
                          10        20
                  ....*....|....*....|...
gi 1953082141 273 YICAECGKAFSNSSNLTKHRRTH 295
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 301-323 1.64e-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: 39.59  E-value: 1.64e-04
                          10        20
                  ....*....|....*....|...
gi 1953082141 301 YVCTKCGKAFSHSSNLTLHYRTH 323
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
818-839 1.65e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 1.65e-04
                          10        20
                  ....*....|....*....|..
gi 1953082141 818 HQRIHTGEKPYACNECGKAFSR 839
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
899-923 1.73e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.73e-04
                          10        20
                  ....*....|....*....|....*
gi 1953082141 899 LIQHQRIHTGENPYECSECGKAFRY 923
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 856-878 2.20e-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: 2.20e-04
                          10        20
                  ....*....|....*....|...
gi 1953082141 856 YECNECGKAFSQSSHLYQHQRIH 878
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
786-810 2.61e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 2.61e-04
                          10        20
                  ....*....|....*....|....*
gi 1953082141 786 ALILHRRIHTGEKPYECNECGKTFS 810
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
273-846 3.17e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.30  E-value: 3.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 273 YICAECGKAFSNSSNLTKHRRTHTGEKPYVCTKCGKAFSHSSNLTLHyrthlvdrpydckcgkafgqssdllKHQRMHTE 352
Cdd:COG5048    34 DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELS-------------------------RHLRTHHN 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 353 EAPY-QCKDCGKAFSGKGSLIRHYRIHTGEKPYQCNECGKSFSQHAGLSSHQRLHTGEKPYKCKECGKAFNHSSNFNKHH 431
Cdd:COG5048    89 NPSDlNSKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLH 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 432 rihtgeKPYWCNNCGKTFCSKSNLSKHQRVHTGEGEVLSAGDPGRSGKVRSPSPSKTRPRPPAapavgsgsaartrdpel 511
Cdd:COG5048   169 ------PPLPANSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSS----------------- 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 512 lalpmETQADCKTQEPQALLESALPSSKVPAFSDKdslgdemlaaallkaksqelvtfedvavyfirkewkrlepaqrdl 591
Cdd:COG5048   226 -----SLPLTTNSQLSPKSLLSQSPSSLSSSDSSS--------------------------------------------- 255

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 592 yrdVMLENYGNVFSLDGETRTEHDQDISEDTgsrgvllgrfqkdISQGLKFEEAYEQdvslkrqlgnssgerldrkiqdf 671
Cdd:COG5048   256 ---SASESPRSSLPTASSQSSSPNESDSSSE-------------KGFSLPIKSKQCN----------------------- 296

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 672 gqmtdeekltpggersekysdfgNSLTVSSNLISHQRLPV----GDRPHKCDE--CSKSFNRTSDLIQHQRIHTGEKPYE 745
Cdd:COG5048   297 -----------------------ISFSRSSPLTRHLRSVNhsgeSLKPFSCPYslCGKLFSRNDALKRHILLHTSISPAK 353

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 746 C--SECGKAFSQSSH-----LIQHQRIHTGEKPYEC--NDCGKTFSCSSALILHRRIHTGEKPYECN--ECGKTFSWSST 814
Cdd:COG5048   354 EklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYN 433

                         570       580       590
                  ....*....|....*....|....*....|..
gi 1953082141 815 LTHHQRIHTgEKPYACNECGKAFSRSSTLIHH 846
Cdd:COG5048   434 LIPHKKIHT-NHAPLLCSILKSFRRDLDLSNH 464
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 828-850 3.29e-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: 3.29e-04
                          10        20
                  ....*....|....*....|...
gi 1953082141 828 YACNECGKAFSRSSTLIHHQRIH 850
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 912-934 6.11e-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: 6.11e-04
                          10        20
                  ....*....|....*....|...
gi 1953082141 912 YECSECGKAFRYSSALVRHQRIH 934
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 670-791 6.75e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 43.17  E-value: 6.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 670 DFGQMTDEEKLTPGGERSEKYSDFGNSLTV---SSNLIShqrlpVGDRPHKCD--ECSKSFNRTSDLIQHqRIHtgekpy 744
Cdd:COG5189   306 STGEMIDVRKLPCTNSSSNGKLAHGGERNIdtpSRMLKV-----KDGKPYKCPveGCNKKYKNQNGLKYH-MLH------ 373

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1953082141 745 ecSECGKAFSQSSHLIQHQRIHTGEKPYECNDCGKTFSCSSALILHR 791
Cdd:COG5189   374 --GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKYHR 418
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 356-378 7.50e-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: 7.50e-04
                          10        20
                  ....*....|....*....|...
gi 1953082141 356 YQCKDCGKAFSGKGSLIRHYRIH 378
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 442-462 1.02e-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: 37.28  E-value: 1.02e-03
                          10        20
                  ....*....|....*....|.
gi 1953082141 442 CNNCGKTFCSKSNLSKHQRVH 462
Cdd:pfam00096   3 CPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 742-790 1.31e-03

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 38.69  E-value: 1.31e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1953082141 742 KPYeCSECGKAFSQSSHLIQHQRIHTgekpYECNDCGKTFSCSSALILH 790
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
zf-H2C2_2 pfam13465
Zinc-finger double domain;
342-366 1.75e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.75e-03
                          10        20
                  ....*....|....*....|....*
gi 1953082141 342 DLLKHQRMHTEEAPYQCKDCGKAFS 366
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 384-406 2.63e-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: 2.63e-03
                          10        20
                  ....*....|....*....|...
gi 1953082141 384 YQCNECGKSFSQHAGLSSHQRLH 406
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 716-738 3.14e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.74  E-value: 3.14e-03
                          10        20
                  ....*....|....*....|...
gi 1953082141 716 HKCDECSKSFNRTSDLIQHQRIH 738
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 309-402 3.66e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.86  E-value: 3.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 309 AFSHSSNLTLHY---RTHLVD-RPYDCK---CGKAFgQSSDLLKHQRMHTEeapyqckdCGKAFSGKGSLIRHYRIHTGE 381
Cdd:COG5189   326 KLAHGGERNIDTpsrMLKVKDgKPYKCPvegCNKKY-KNQNGLKYHMLHGH--------QNQKLHENPSPEKMNIFSAKD 396

                          90       100
                  ....*....|....*....|.
gi 1953082141 382 KPYQCNECGKSFSQHAGLSSH 402
Cdd:COG5189   397 KPYRCEVCDKRYKNLNGLKYH 417
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
882-939 3.91e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.83  E-value: 3.91e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953082141 882 KPYECMECGGKFTYSSGLIQHQRIHTGENPYECSECGKAFRYS--SALVRHQRIHTGEKP 939
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSrpLELSRHLRTHHNNPS 91
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 800-822 6.25e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 6.25e-03
                          10        20
                  ....*....|....*....|...
gi 1953082141 800 YECNECGKTFSWSSTLTHHQRIH 822
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
426-449 9.98e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 9.98e-03
                          10        20
                  ....*....|....*....|....
gi 1953082141 426 NFNKHHRIHTGEKPYWCNNCGKTF 449
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 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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