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Conserved domains on  [gi|530363191|ref|XP_005271193|]
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zinc finger protein 69 homolog B isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
74-134 6.77e-33

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 119.62  E-value: 6.77e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530363191    74 LTFKDVSVDFTQEEWGQLAPAHRNLYREVMLENYGNLVSVaGCQLSKPGVISQLEKGEEPW 134
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSL-GFQVPKPDLISQLEQGEEPW 60
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
194-430 1.32e-07

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.93  E-value: 1.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363191 194 NKLESQQENQRMGKGQIPLMCkkTFTQERGQESNRFEKRINVKSEVMPGPIGLPRKRDRKYDTPGKRSRYNIDLVNHSRS 273
Cdd:COG5048  209 YSIPSSSSDQNLENSSSSLPL--TTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGF 286

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363191 274 YTKmktFECNICEKIFKQLIHLTEHMR--IHTGE--KPFRCKE--CGKAFSQSSSLIPHQRIHTGEKPYECK--ECGKTF 345
Cdd:COG5048  287 SLP---IKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKF 363

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363191 346 ------RHPSSLTQHVRIHTgEKPYECRV--CEKAFSQSIGLIQHLRTHVREKP--FTCKDCGKAF----FQIRHLRQHE 411
Cdd:COG5048  364 spllnnEPPQSLQQYKDLKN-DKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFnrhyNLIPHKKIHT 442

                        250
                 ....*....|....*....
gi 530363191 412 IihtgvKPYICNVCSKTFS 430
Cdd:COG5048  443 N-----HAPLLCSILKSFR 456
zf-H2C2_2 pfam13465
Zinc-finger double domain;
434-459 1.63e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 1.63e-05
                          10        20
                  ....*....|....*....|....*.
gi 530363191  434 YLTQHQRTHTGERPYKCKECGKAFSQ 459
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
490-515 3.51e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 3.51e-04
                          10        20
                  ....*....|....*....|....*.
gi 530363191  490 SFAKHQRIHTGEKPYDCNECGKAFSC 515
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SCAN super family cl47715
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 2-40 4.94e-04

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.


The actual alignment was detected with superfamily member pfam02023:

Pssm-ID: 460417 [Multi-domain]  Cd Length: 89  Bit Score: 39.01  E-value: 4.94e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 530363191    2 LQQLLITLPTEASTWVKLRHPKAATERVALWEDVTKMFK 40
Cdd:pfam02023  50 LEQFLTILPEEIQSWVREHHPESGEEAVALAEDLLLERG 88
zf-H2C2_2 pfam13465
Zinc-finger double domain;
462-487 6.85e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 6.85e-04
                          10        20
                  ....*....|....*....|....*.
gi 530363191  462 HLSIHQRVHTGVKPYECSHCGKAFRH 487
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
74-134 6.77e-33

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 119.62  E-value: 6.77e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530363191    74 LTFKDVSVDFTQEEWGQLAPAHRNLYREVMLENYGNLVSVaGCQLSKPGVISQLEKGEEPW 134
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSL-GFQVPKPDLISQLEQGEEPW 60
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 73-113 5.41e-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: 88.68  E-value: 5.41e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 530363191   73 LLTFKDVSVDFTQEEWGQLAPAHRNLYREVMLENYGNLVSV 113
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 74-112 5.78e-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: 5.78e-20
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 530363191  74 LTFKDVSVDFTQEEWGQLAPAHRNLYREVMLENYGNLVS 112
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
194-430 1.32e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.93  E-value: 1.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363191 194 NKLESQQENQRMGKGQIPLMCkkTFTQERGQESNRFEKRINVKSEVMPGPIGLPRKRDRKYDTPGKRSRYNIDLVNHSRS 273
Cdd:COG5048  209 YSIPSSSSDQNLENSSSSLPL--TTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGF 286

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363191 274 YTKmktFECNICEKIFKQLIHLTEHMR--IHTGE--KPFRCKE--CGKAFSQSSSLIPHQRIHTGEKPYECK--ECGKTF 345
Cdd:COG5048  287 SLP---IKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKF 363

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363191 346 ------RHPSSLTQHVRIHTgEKPYECRV--CEKAFSQSIGLIQHLRTHVREKP--FTCKDCGKAF----FQIRHLRQHE 411
Cdd:COG5048  364 spllnnEPPQSLQQYKDLKN-DKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFnrhyNLIPHKKIHT 442

                        250
                 ....*....|....*....
gi 530363191 412 IihtgvKPYICNVCSKTFS 430
Cdd:COG5048  443 N-----HAPLLCSILKSFR 456
zf-H2C2_2 pfam13465
Zinc-finger double domain;
294-319 3.44e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.51  E-value: 3.44e-06
                          10        20
                  ....*....|....*....|....*.
gi 530363191  294 HLTEHMRIHTGEKPFRCKECGKAFSQ 319
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
434-459 1.63e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 1.63e-05
                          10        20
                  ....*....|....*....|....*.
gi 530363191  434 YLTQHQRTHTGERPYKCKECGKAFSQ 459
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
490-515 3.51e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 3.51e-04
                          10        20
                  ....*....|....*....|....*.
gi 530363191  490 SFAKHQRIHTGEKPYDCNECGKAFSC 515
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 2-40 4.94e-04

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: 39.01  E-value: 4.94e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 530363191    2 LQQLLITLPTEASTWVKLRHPKAATERVALWEDVTKMFK 40
Cdd:pfam02023  50 LEQFLTILPEEIQSWVREHHPESGEEAVALAEDLLLERG 88
zf-H2C2_2 pfam13465
Zinc-finger double domain;
462-487 6.85e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 6.85e-04
                          10        20
                  ....*....|....*....|....*.
gi 530363191  462 HLSIHQRVHTGVKPYECSHCGKAFRH 487
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
474-529 2.60e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.45  E-value: 2.60e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530363191 474 KPYECSHCGKAFRHDSSFAKHQRIHTGEKPYDCNECGKAFSCS--SSLIRHCKTHLRN 529
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSrpLELSRHLRTHHNN 89
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
74-134 6.77e-33

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 119.62  E-value: 6.77e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530363191    74 LTFKDVSVDFTQEEWGQLAPAHRNLYREVMLENYGNLVSVaGCQLSKPGVISQLEKGEEPW 134
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSL-GFQVPKPDLISQLEQGEEPW 60
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 73-113 5.41e-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: 88.68  E-value: 5.41e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 530363191   73 LLTFKDVSVDFTQEEWGQLAPAHRNLYREVMLENYGNLVSV 113
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 74-112 5.78e-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: 5.78e-20
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 530363191  74 LTFKDVSVDFTQEEWGQLAPAHRNLYREVMLENYGNLVS 112
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
194-430 1.32e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.93  E-value: 1.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363191 194 NKLESQQENQRMGKGQIPLMCkkTFTQERGQESNRFEKRINVKSEVMPGPIGLPRKRDRKYDTPGKRSRYNIDLVNHSRS 273
Cdd:COG5048  209 YSIPSSSSDQNLENSSSSLPL--TTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGF 286

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363191 274 YTKmktFECNICEKIFKQLIHLTEHMR--IHTGE--KPFRCKE--CGKAFSQSSSLIPHQRIHTGEKPYECK--ECGKTF 345
Cdd:COG5048  287 SLP---IKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKF 363

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363191 346 ------RHPSSLTQHVRIHTgEKPYECRV--CEKAFSQSIGLIQHLRTHVREKP--FTCKDCGKAF----FQIRHLRQHE 411
Cdd:COG5048  364 spllnnEPPQSLQQYKDLKN-DKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFnrhyNLIPHKKIHT 442

                        250
                 ....*....|....*....
gi 530363191 412 IihtgvKPYICNVCSKTFS 430
Cdd:COG5048  443 N-----HAPLLCSILKSFR 456
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
273-522 2.77e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.16  E-value: 2.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363191 273 SYTKMKTFECNICEKIFKQLIHLTEHMRIHTGEKPFRC--KECGKAFSQSSSLIPHQRIHTGEKPYECKECGKTFRHPSS 350
Cdd:COG5048   27 LSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKAS 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363191 351 LTQHvRIHTGEKPYECRVCEKAFSQSIGLIQH----LRTHVREKPftCKDCGKAFFQ------------------IRHLR 408
Cdd:COG5048  107 SSSL-SSSSSNSNDNNLLSSHSLPPSSRDPQLpdllSISNLRNNP--LPGNNSSSVNtpqsnslhpplpanslskDPSSN 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363191 409 QHEIIHTGVKPYICNVCSKTFSHSTYLTQHQRTHTGER----PYKCKECGKAFSQRihlSIHQRVHTGVKPYECSHCGKA 484
Cdd:COG5048  184 LSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLEnsssSLPLTTNSQLSPKS---LLSQSPSSLSSSDSSSSASES 260

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 530363191 485 FRHDSSFAKHQRIH----------TGEKPYDCNECGKAFSCSSSLIRH 522
Cdd:COG5048  261 PRSSLPTASSQSSSpnesdsssekGFSLPIKSKQCNISFSRSSPLTRH 308
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
306-495 3.54e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.78  E-value: 3.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363191 306 KPFRCKECGKAFSQSSSLIPHQR--IHTGE--KPYECKE--CGKTFRHPSSLTQHVRIHTGEKPYECRVCEKAFSQSIGL 379
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363191 380 IQHLRTHVrekpftckdcgkaffqirhlrQHEIIHTGVKPYICNV--CSKTFSHSTYLTQHQRTHTGERP--YKCKECGK 455
Cdd:COG5048  368 NNEPPQSL---------------------QQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSK 426

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 530363191 456 AFSQRIHLSIHQRVHTGVKPYECSHCGKAFRHDSSFAKHQ 495
Cdd:COG5048  427 SFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHGK 466
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
321-533 2.06e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.46  E-value: 2.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363191 321 SSLIPHQRIHTGEKPYECKECGKTFRHPSSLTQHVRIHTGEKPYECRVCEKAFSQSIGLIQHLRTHVREKPFTCKDCGKA 400
Cdd:COG5048  184 LSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRS 263

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363191 401 FFQIRHLRQHEIIHTGV-------KPYICNVCSKTFSHSTYLTQHQRT--HTGE--RPYKCKE--CGKAFSQRIHLSIHQ 467
Cdd:COG5048  264 SLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHI 343

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363191 468 RVHTGVKPYEC--SHCGKAFRHDSSFAKHQRIHT-------------------------------------GEKPYDCNE 508
Cdd:COG5048  344 LLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQQykdlkndkksetlsnscirnfkrdsnlslhiithlsfRPYNCKNPP 423

                        250       260
                 ....*....|....*....|....*
gi 530363191 509 CGKAFSCSSSLIRHCKTHLRNTFSN 533
Cdd:COG5048  424 CSKSFNRHYNLIPHKKIHTNHAPLL 448
zf-H2C2_2 pfam13465
Zinc-finger double domain;
294-319 3.44e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.51  E-value: 3.44e-06
                          10        20
                  ....*....|....*....|....*.
gi 530363191  294 HLTEHMRIHTGEKPFRCKECGKAFSQ 319
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
434-459 1.63e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 1.63e-05
                          10        20
                  ....*....|....*....|....*.
gi 530363191  434 YLTQHQRTHTGERPYKCKECGKAFSQ 459
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 360-443 3.28e-05

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 46.25  E-value: 3.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363191 360 GEKPYECRV--CEKAFSQSIGLIQHlRTHVREKPFTCKDCGKAffqirhlrQHEIIHTGVKPYICNVCSKTFSHSTYLTQ 437
Cdd:COG5189  346 DGKPYKCPVegCNKKYKNQNGLKYH-MLHGHQNQKLHENPSPE--------KMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                 ....*.
gi 530363191 438 HqRTHT 443
Cdd:COG5189  417 H-RKHS 421
zf-H2C2_2 pfam13465
Zinc-finger double domain;
350-375 4.52e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 4.52e-05
                          10        20
                  ....*....|....*....|....*.
gi 530363191  350 SLTQHVRIHTGEKPYECRVCEKAFSQ 375
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
318-517 5.06e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.84  E-value: 5.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363191 318 SQSSSLIPHQRIHTGE----KPYECKECGKTFRHPSSLTQHVRIHTGEKPYECRV--CEKAFSQSIGLIQHLRTHVREKP 391
Cdd:COG5048   12 NNSVLSSTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPS 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363191 392 FTC-KDCGKAFFQIRHLRQHEIIHTGVKPYICNVCSKTFSHSTYLTQHQRTHTGERPYKCKECGKAFSQRI--------- 461
Cdd:COG5048   92 DLNsKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPqsnslhppl 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530363191 462 -------------HLSIHQRVHTGVKPYECSHCGKAFRHDSSFAKHQRIHTGEKPYDCNECGKAFSCSS 517
Cdd:COG5048  172 panslskdpssnlSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSL 240
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 418-470 1.17e-04

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 40.62  E-value: 1.17e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530363191 418 KPYiCNVCSKTFSHSTYLTQHQRTHTgerpYKCKECGKAFSQRIHLSIH-QRVH 470
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
zf-H2C2_2 pfam13465
Zinc-finger double domain;
326-347 2.24e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.24e-04
                          10        20
                  ....*....|....*....|..
gi 530363191  326 HQRIHTGEKPYECKECGKTFRH 347
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
490-515 3.51e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 3.51e-04
                          10        20
                  ....*....|....*....|....*.
gi 530363191  490 SFAKHQRIHTGEKPYDCNECGKAFSC 515
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 336-358 4.66e-04

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 37.66  E-value: 4.66e-04
                          10        20
                  ....*....|....*....|...
gi 530363191  336 YECKECGKTFRHPSSLTQHVRIH 358
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 2-40 4.94e-04

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: 39.01  E-value: 4.94e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 530363191    2 LQQLLITLPTEASTWVKLRHPKAATERVALWEDVTKMFK 40
Cdd:pfam02023  50 LEQFLTILPEEIQSWVREHHPESGEEAVALAEDLLLERG 88
zf-H2C2_2 pfam13465
Zinc-finger double domain;
462-487 6.85e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 6.85e-04
                          10        20
                  ....*....|....*....|....*.
gi 530363191  462 HLSIHQRVHTGVKPYECSHCGKAFRH 487
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 448-470 1.44e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.12  E-value: 1.44e-03
                          10        20
                  ....*....|....*....|...
gi 530363191  448 YKCKECGKAFSQRIHLSIHQRVH 470
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
474-529 2.60e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.45  E-value: 2.60e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530363191 474 KPYECSHCGKAFRHDSSFAKHQRIHTGEKPYDCNECGKAFSCS--SSLIRHCKTHLRN 529
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSrpLELSRHLRTHHNN 89
zf-H2C2_2 pfam13465
Zinc-finger double domain;
406-431 3.29e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 3.29e-03
                          10        20
                  ....*....|....*....|....*.
gi 530363191  406 HLRQHEIIHTGVKPYICNVCSKTFSH 431
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 420-442 4.36e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.58  E-value: 4.36e-03
                          10        20
                  ....*....|....*....|...
gi 530363191  420 YICNVCSKTFSHSTYLTQHQRTH 442
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 476-498 5.05e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.58  E-value: 5.05e-03
                          10        20
                  ....*....|....*....|...
gi 530363191  476 YECSHCGKAFRHDSSFAKHQRIH 498
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 280-302 7.41e-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: 34.20  E-value: 7.41e-03
                          10        20
                  ....*....|....*....|...
gi 530363191  280 FECNICEKIFKQLIHLTEHMRIH 302
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
379-403 8.30e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.88  E-value: 8.30e-03
                          10        20
                  ....*....|....*....|....*
gi 530363191  379 LIQHLRTHVREKPFTCKDCGKAFFQ 403
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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