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Conserved domains on  [gi|568938550|ref|XP_006504688|]
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zinc finger protein 157 isoform X1 [Mus musculus]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204268)

KRAB (Kruppel-associated box) domain-containing zinc finger protein (KRAB-ZFP) plays important roles in cell differentiation and organ development, and in regulating viral replication and transcription

CATH:  3.30.160.60
Gene Ontology:  GO:0003700|GO:0046872
PubMed:  22803940
SCOP:  4003583

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
19-79 4.17e-32

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 117.69  E-value: 4.17e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568938550    19 VSFEDVAVDFTWQEWQELDAAQRTLYRDVMLENYSSLVSLGHCVTKPELILRLEHGFQPWS 79
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
196-550 4.18e-08

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.86  E-value: 4.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938550 196 KIYQCTECKKAFSSKSELTVHHRIHTGEKPHAC--EECGKAFYRKSTLTVHQKTHRGEKPYEC-KECWKAFYYKSTLTEH 272
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNsKSLPLSNSKASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938550 273 QRIHTGEKPYVCKDCGKAFFYKSNLTRHHRTHTREKPYECKEC-RKGFSSKSELTSHHRTHTGEKPYQCEECGKAFYCKS 351
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLISSN 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938550 352 ---TLRVHQKIHSGEKPYE---CKECQKSFYYKSTLTEHQRTHTGEKPY---------------ECKDCGKAFFYKSQLT 410
Cdd:COG5048  192 vstSIPSSSENSPLSSSYSipsSSSDQNLENSSSSLPLTTNSQLSPKSLlsqspsslsssdsssSASESPRSSLPTASSQ 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938550 411 RHHRIHTGE-------KPYECEECRKAFSSKSELTAHHRT--HTGE--RPYEC--KDCGKCFYRKSHLTLHHRIHTGEKP 477
Cdd:COG5048  272 SSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISP 351

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568938550 478 YECKdcrkaffcksgLARHLGTHTHGTNTKNREKHFPaTHSSVNIRNDIQVRNPVALNNEKKLSTINHSSVHM 550
Cdd:COG5048  352 AKEK-----------LLNSSSKFSPLLNNEPPQSLQQ-YKDLKNDKKSETLSNSCIRNFKRDSNLSLHIITHL 412
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
19-79 4.17e-32

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 117.69  E-value: 4.17e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568938550    19 VSFEDVAVDFTWQEWQELDAAQRTLYRDVMLENYSSLVSLGHCVTKPELILRLEHGFQPWS 79
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 18-59 6.22e-23

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: 91.38  E-value: 6.22e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568938550   18 LVSFEDVAVDFTWQEWQELDAAQRTLYRDVMLENYSSLVSLG 59
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 19-58 6.18e-20

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: 82.98  E-value: 6.18e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 568938550  19 VSFEDVAVDFTWQEWQELDAAQRTLYRDVMLENYSSLVSL 58
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
196-550 4.18e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.86  E-value: 4.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938550 196 KIYQCTECKKAFSSKSELTVHHRIHTGEKPHAC--EECGKAFYRKSTLTVHQKTHRGEKPYEC-KECWKAFYYKSTLTEH 272
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNsKSLPLSNSKASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938550 273 QRIHTGEKPYVCKDCGKAFFYKSNLTRHHRTHTREKPYECKEC-RKGFSSKSELTSHHRTHTGEKPYQCEECGKAFYCKS 351
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLISSN 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938550 352 ---TLRVHQKIHSGEKPYE---CKECQKSFYYKSTLTEHQRTHTGEKPY---------------ECKDCGKAFFYKSQLT 410
Cdd:COG5048  192 vstSIPSSSENSPLSSSYSipsSSSDQNLENSSSSLPLTTNSQLSPKSLlsqspsslsssdsssSASESPRSSLPTASSQ 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938550 411 RHHRIHTGE-------KPYECEECRKAFSSKSELTAHHRT--HTGE--RPYEC--KDCGKCFYRKSHLTLHHRIHTGEKP 477
Cdd:COG5048  272 SSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISP 351

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568938550 478 YECKdcrkaffcksgLARHLGTHTHGTNTKNREKHFPaTHSSVNIRNDIQVRNPVALNNEKKLSTINHSSVHM 550
Cdd:COG5048  352 AKEK-----------LLNSSSKFSPLLNNEPPQSLQQ-YKDLKNDKKSETLSNSCIRNFKRDSNLSLHIITHL 412
zf-H2C2_2 pfam13465
Zinc-finger double domain;
409-433 6.87e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 6.87e-04
                          10        20
                  ....*....|....*....|....*
gi 568938550  409 LTRHHRIHTGEKPYECEECRKAFSS 433
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
19-79 4.17e-32

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 117.69  E-value: 4.17e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568938550    19 VSFEDVAVDFTWQEWQELDAAQRTLYRDVMLENYSSLVSLGHCVTKPELILRLEHGFQPWS 79
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 18-59 6.22e-23

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: 91.38  E-value: 6.22e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568938550   18 LVSFEDVAVDFTWQEWQELDAAQRTLYRDVMLENYSSLVSLG 59
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 19-58 6.18e-20

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: 82.98  E-value: 6.18e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 568938550  19 VSFEDVAVDFTWQEWQELDAAQRTLYRDVMLENYSSLVSL 58
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
196-550 4.18e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.86  E-value: 4.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938550 196 KIYQCTECKKAFSSKSELTVHHRIHTGEKPHAC--EECGKAFYRKSTLTVHQKTHRGEKPYEC-KECWKAFYYKSTLTEH 272
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNsKSLPLSNSKASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938550 273 QRIHTGEKPYVCKDCGKAFFYKSNLTRHHRTHTREKPYECKEC-RKGFSSKSELTSHHRTHTGEKPYQCEECGKAFYCKS 351
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLISSN 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938550 352 ---TLRVHQKIHSGEKPYE---CKECQKSFYYKSTLTEHQRTHTGEKPY---------------ECKDCGKAFFYKSQLT 410
Cdd:COG5048  192 vstSIPSSSENSPLSSSYSipsSSSDQNLENSSSSLPLTTNSQLSPKSLlsqspsslsssdsssSASESPRSSLPTASSQ 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938550 411 RHHRIHTGE-------KPYECEECRKAFSSKSELTAHHRT--HTGE--RPYEC--KDCGKCFYRKSHLTLHHRIHTGEKP 477
Cdd:COG5048  272 SSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISP 351

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568938550 478 YECKdcrkaffcksgLARHLGTHTHGTNTKNREKHFPaTHSSVNIRNDIQVRNPVALNNEKKLSTINHSSVHM 550
Cdd:COG5048  352 AKEK-----------LLNSSSKFSPLLNNEPPQSLQQ-YKDLKNDKKSETLSNSCIRNFKRDSNLSLHIITHL 412
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
280-436 2.21e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.55  E-value: 2.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938550 280 KPYVCKDCGKAFFYKSNLTRHHRT--HTRE--KPYECKE--CRKGFSSKSELTSHHRTHTGEKPYQCEEC-------GKA 346
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLnssskfsPLL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938550 347 FYCKSTLRVHQKIHSGEKPYEC--KECQKSFYYKSTLTEHQRTHTGEKPYECKD--CGKAFFYKSQLTRHHRIHTGEKPY 422
Cdd:COG5048  368 NNEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKNppCSKSFNRHYNLIPHKKIHTNHAPL 447

                        170
                 ....*....|....
gi 568938550 423 ECEECRKAFSSKSE 436
Cdd:COG5048  448 LCSILKSFRRDLDL 461
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
252-414 4.04e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 49.69  E-value: 4.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938550 252 KPYECKECWKAFYYKSTLTEHQR--IHTGE--KPYVC--KDCGKAFFYKSNLTRHHRTHTREKPYECKECRKGFSSKSEL 325
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938550 326 TS-------HHRTHTGEKPYQCEECGKAFYCK--STLRVHQKIHSGEKPYECK--ECQKSFYYKSTLTEHQRTHTGEKPY 394
Cdd:COG5048  368 NNeppqslqQYKDLKNDKKSETLSNSCIRNFKrdSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPL 447

                        170       180
                 ....*....|....*....|
gi 568938550 395 ECKDCGKaFFYKSQLTRHHR 414
Cdd:COG5048  448 LCSILKS-FRRDLDLSNHGK 466
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
136-329 6.11e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.84  E-value: 6.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938550 136 PRGTKPYECKPCMKMVSLPSQCSKQHAYYPSVK------PYEWKECQKAFCYKSALTQHQRART----RLKIYQCTE--C 203
Cdd:COG5048  250 SSDSSSSASESPRSSLPTASSQSSSPNESDSSSekgfslPIKSKQCNISFSRSSPLTRHLRSVNhsgeSLKPFSCPYslC 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938550 204 KKAFSSKSELTVHHRIHTGEKPHAC--EECGKAFYRKST-----LTVHQKTHRGEKPYEC--KECWKAFYYKSTLTEHQR 274
Cdd:COG5048  330 GKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHII 409

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568938550 275 IHTGEKPYVCKD--CGKAFFYKSNLTRHHRTHTREKPYECkeCRKGFSSKSELTSHH 329
Cdd:COG5048  410 THLSFRPYNCKNppCSKSFNRHYNLIPHKKIHTNHAPLLC--SILKSFRRDLDLSNH 464
zf-H2C2_2 pfam13465
Zinc-finger double domain;
409-433 6.87e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 6.87e-04
                          10        20
                  ....*....|....*....|....*
gi 568938550  409 LTRHHRIHTGEKPYECEECRKAFSS 433
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
324-349 1.20e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.20e-03
                          10        20
                  ....*....|....*....|....*.
gi 568938550  324 ELTSHHRTHTGEKPYQCEECGKAFYC 349
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
381-403 1.24e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.24e-03
                          10        20
                  ....*....|....*....|...
gi 568938550  381 LTEHQRTHTGEKPYECKDCGKAF 403
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
448-567 1.69e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.22  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938550 448 RPYECKDCGKCFYRKSHLTLHHRIHTGEKPYECKDCRKAFFCKSGLARHLGTHTHGTNTKNREKH--------------- 512
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSDLNSKslplsnskassssls 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568938550 513 ----------FPATHSSVNIRNDIQVRNPVALNN--EKKLSTINHSSVHMMDFLELRSPIDVHNAGK 567
Cdd:COG5048  112 ssssnsndnnLLSSHSLPPSSRDPQLPDLLSISNlrNNPLPGNNSSSVNTPQSNSLHPPLPANSLSK 178
zf-H2C2_2 pfam13465
Zinc-finger double domain;
296-321 2.00e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.00e-03
                          10        20
                  ....*....|....*....|....*.
gi 568938550  296 NLTRHHRTHTREKPYECKECRKGFSS 321
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 450-472 2.04e-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: 2.04e-03
                          10        20
                  ....*....|....*....|...
gi 568938550  450 YECKDCGKCFYRKSHLTLHHRIH 472
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 282-304 2.41e-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: 2.41e-03
                          10        20
                  ....*....|....*....|...
gi 568938550  282 YVCKDCGKAFFYKSNLTRHHRTH 304
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
269-291 2.66e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 2.66e-03
                          10        20
                  ....*....|....*....|...
gi 568938550  269 LTEHQRIHTGEKPYVCKDCGKAF 291
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 175-216 4.50e-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: 36.38  E-value: 4.50e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 568938550 175 CQKAFCYKSALTQHQRARTrlkiYQCTECKKAFSSKSELTVH 216
Cdd:cd20908    7 CDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
zf-H2C2_2 pfam13465
Zinc-finger double domain;
212-237 5.79e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 5.79e-03
                          10        20
                  ....*....|....*....|....*.
gi 568938550  212 ELTVHHRIHTGEKPHACEECGKAFYR 237
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 394-416 6.55e-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: 6.55e-03
                          10        20
                  ....*....|....*....|...
gi 568938550  394 YECKDCGKAFFYKSQLTRHHRIH 416
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
464-487 6.78e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 6.78e-03
                          10        20
                  ....*....|....*....|....
gi 568938550  464 HLTLHHRIHTGEKPYECKDCRKAF 487
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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