NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|238859629|ref|NP_001005788|]
View 

zinc finger protein 69 isoform 1 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
131-192 3.55e-29

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 109.60  E-value: 3.55e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 238859629   131 LTFKDIAVDLSQEEWGQLAPAYQDLYREVMLENYRNLVSVaGYQLSKPTVISQLEKGEGPCM 192
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSL-GFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
279-510 1.07e-11

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 67.41  E-value: 1.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859629 279 NKLENPESSNVILEQKHRKHKPARKRNKYKLDSIDHPVSCmrARRYPCNVCEKMFKQPIHLVEHMRTHTG-EKPFRCKEC 357
Cdd:COG5048  218 QNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSA--SESPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQC 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859629 358 GRAFSQSASLNTHQR--IHTGE--KPFACEE--CGKAFRHRSSLNQHHRTHTGEKPFTC--DKCQKAFSQ--NISLVQHL 427
Cdd:COG5048  296 NISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPllNNEPPQSL 375

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859629 428 RTHSG---EKPFSC--SECGKPFRQIRHLSEHVRIHTGEKP--YKCTSCCKTFSHRAYLTHHQRIHTGERPYKCkECGKA 500
Cdd:COG5048  376 QQYKDlknDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLC-SILKS 454

                        250
                 ....*....|
gi 238859629 501 FRQRIHLSNH 510
Cdd:COG5048  455 FRRDLDLSNH 464
CTD smart01104
Spt5 C-terminal nonapeptide repeat binding Spt4; The C-terminal domain of the transcription ...
 52-128 3.31e-06

Spt5 C-terminal nonapeptide repeat binding Spt4; The C-terminal domain of the transcription elongation factor protein Spt5 is necessary for binding to Spt4 to form the functional complex that regulates early transcription elongation by RNA polymerase II. The complex may be involved in pre-mRNA processing through its association with mRNA capping enzymes. This CTD domain carries a regular nonapeptide repeat that can be present in up to 18 copies, as in S. pombe. The repeat has a characteristic TPA motif.


:

Pssm-ID: 215026 [Multi-domain]  Cd Length: 121  Bit Score: 46.36  E-value: 3.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859629    52 GTTPG-------TPAAGSHDGATPGTTATGSHDEATPGTPAAGSHDGETpgiPAAGSHDGETPGTPT--AGSHDGVTPGT 122
Cdd:smart01104   2 GRTPAwgasgskTPAWGSRTPGTAAGGAPTARGGSGSRTPAWGGAGSRT---PAWGGAGPTGSRTPAwgGASAWGNKSSE 78


                   ....*.
gi 238859629   123 TAAGSQ 128
Cdd:smart01104  79 GSASSW 84
zf-H2C2_2 pfam13465
Zinc-finger double domain;
534-559 5.68e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 5.68e-05
                          10        20
                  ....*....|....*....|....*.
gi 238859629  534 SFKKHQRHHTGEKPYECTECGKSFSY 559
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
131-192 3.55e-29

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 109.60  E-value: 3.55e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 238859629   131 LTFKDIAVDLSQEEWGQLAPAYQDLYREVMLENYRNLVSVaGYQLSKPTVISQLEKGEGPCM 192
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSL-GFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 130-170 7.40e-19

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: 79.82  E-value: 7.40e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 238859629  130 SLTFKDIAVDLSQEEWGQLAPAYQDLYREVMLENYRNLVSV 170
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 131-169 5.74e-18

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: 77.20  E-value: 5.74e-18
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 238859629 131 LTFKDIAVDLSQEEWGQLAPAYQDLYREVMLENYRNLVS 169
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
279-510 1.07e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 67.41  E-value: 1.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859629 279 NKLENPESSNVILEQKHRKHKPARKRNKYKLDSIDHPVSCmrARRYPCNVCEKMFKQPIHLVEHMRTHTG-EKPFRCKEC 357
Cdd:COG5048  218 QNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSA--SESPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQC 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859629 358 GRAFSQSASLNTHQR--IHTGE--KPFACEE--CGKAFRHRSSLNQHHRTHTGEKPFTC--DKCQKAFSQ--NISLVQHL 427
Cdd:COG5048  296 NISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPllNNEPPQSL 375

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859629 428 RTHSG---EKPFSC--SECGKPFRQIRHLSEHVRIHTGEKP--YKCTSCCKTFSHRAYLTHHQRIHTGERPYKCkECGKA 500
Cdd:COG5048  376 QQYKDlknDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLC-SILKS 454

                        250
                 ....*....|
gi 238859629 501 FRQRIHLSNH 510
Cdd:COG5048  455 FRRDLDLSNH 464
CTD smart01104
Spt5 C-terminal nonapeptide repeat binding Spt4; The C-terminal domain of the transcription ...
 52-128 3.31e-06

Spt5 C-terminal nonapeptide repeat binding Spt4; The C-terminal domain of the transcription elongation factor protein Spt5 is necessary for binding to Spt4 to form the functional complex that regulates early transcription elongation by RNA polymerase II. The complex may be involved in pre-mRNA processing through its association with mRNA capping enzymes. This CTD domain carries a regular nonapeptide repeat that can be present in up to 18 copies, as in S. pombe. The repeat has a characteristic TPA motif.


Pssm-ID: 215026 [Multi-domain]  Cd Length: 121  Bit Score: 46.36  E-value: 3.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859629    52 GTTPG-------TPAAGSHDGATPGTTATGSHDEATPGTPAAGSHDGETpgiPAAGSHDGETPGTPT--AGSHDGVTPGT 122
Cdd:smart01104   2 GRTPAwgasgskTPAWGSRTPGTAAGGAPTARGGSGSRTPAWGGAGSRT---PAWGGAGPTGSRTPAwgGASAWGNKSSE 78


                   ....*.
gi 238859629   123 TAAGSQ 128
Cdd:smart01104  79 GSASSW 84
zf-H2C2_2 pfam13465
Zinc-finger double domain;
338-363 9.64e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 9.64e-06
                          10        20
                  ....*....|....*....|....*.
gi 238859629  338 HLVEHMRTHTGEKPFRCKECGRAFSQ 363
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
534-559 5.68e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 5.68e-05
                          10        20
                  ....*....|....*....|....*.
gi 238859629  534 SFKKHQRHHTGEKPYECTECGKSFSY 559
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PHA00733 PHA00733
hypothetical protein
 407-455 5.85e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.16  E-value: 5.85e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 238859629 407 PFTCDKCQKAFSQNISLVQHLRTHSGEKpfSCSECGKPFRQIRHLSEHV 455
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDHV 119
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 488-568 8.32e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 38.93  E-value: 8.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859629 488 GERPYKCK--ECGKAFRQRIHLSNHRtVHtgvkayecNRCGKAYRHDSSFKKHQRHHTGEKPYECTECGKSFSYNSSLSR 565
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLKYHM-LH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                 ...
gi 238859629 566 HQK 568
Cdd:COG5189  417 HRK 419
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
131-192 3.55e-29

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 109.60  E-value: 3.55e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 238859629   131 LTFKDIAVDLSQEEWGQLAPAYQDLYREVMLENYRNLVSVaGYQLSKPTVISQLEKGEGPCM 192
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSL-GFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 130-170 7.40e-19

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: 79.82  E-value: 7.40e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 238859629  130 SLTFKDIAVDLSQEEWGQLAPAYQDLYREVMLENYRNLVSV 170
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 131-169 5.74e-18

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: 77.20  E-value: 5.74e-18
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 238859629 131 LTFKDIAVDLSQEEWGQLAPAYQDLYREVMLENYRNLVS 169
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
279-510 1.07e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 67.41  E-value: 1.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859629 279 NKLENPESSNVILEQKHRKHKPARKRNKYKLDSIDHPVSCmrARRYPCNVCEKMFKQPIHLVEHMRTHTG-EKPFRCKEC 357
Cdd:COG5048  218 QNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSA--SESPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQC 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859629 358 GRAFSQSASLNTHQR--IHTGE--KPFACEE--CGKAFRHRSSLNQHHRTHTGEKPFTC--DKCQKAFSQ--NISLVQHL 427
Cdd:COG5048  296 NISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPllNNEPPQSL 375

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859629 428 RTHSG---EKPFSC--SECGKPFRQIRHLSEHVRIHTGEKP--YKCTSCCKTFSHRAYLTHHQRIHTGERPYKCkECGKA 500
Cdd:COG5048  376 QQYKDlknDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLC-SILKS 454

                        250
                 ....*....|
gi 238859629 501 FRQRIHLSNH 510
Cdd:COG5048  455 FRRDLDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
362-566 7.72e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.17  E-value: 7.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859629 362 SQSASLNTHQRIHTGEKPFACEecGKAFRHRSSLNQHH-RTHTG-EKPFTCDKCQKAFSQNISLVQHLRT--HSGE--KP 435
Cdd:COG5048  244 SPSSLSSSDSSSSASESPRSSL--PTASSQSSSPNESDsSSEKGfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKP 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859629 436 FSCSE--CGKPFRQIRHLSEHVRIHTGEKPYKC--TSCCKTFS------HRAYLTHHQRIHTgERPYKC--KECGKAFRQ 503
Cdd:COG5048  322 FSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSpllnnePPQSLQQYKDLKN-DKKSETlsNSCIRNFKR 400

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 238859629 504 RIHLSNHRTVHTGVKAYECN--RCGKAYRHDSSFKKHQRHHTgEKPYECTECGKSFSYNSSLSRH 566
Cdd:COG5048  401 DSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLSNH 464
CTD smart01104
Spt5 C-terminal nonapeptide repeat binding Spt4; The C-terminal domain of the transcription ...
 52-128 3.31e-06

Spt5 C-terminal nonapeptide repeat binding Spt4; The C-terminal domain of the transcription elongation factor protein Spt5 is necessary for binding to Spt4 to form the functional complex that regulates early transcription elongation by RNA polymerase II. The complex may be involved in pre-mRNA processing through its association with mRNA capping enzymes. This CTD domain carries a regular nonapeptide repeat that can be present in up to 18 copies, as in S. pombe. The repeat has a characteristic TPA motif.


Pssm-ID: 215026 [Multi-domain]  Cd Length: 121  Bit Score: 46.36  E-value: 3.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859629    52 GTTPG-------TPAAGSHDGATPGTTATGSHDEATPGTPAAGSHDGETpgiPAAGSHDGETPGTPT--AGSHDGVTPGT 122
Cdd:smart01104   2 GRTPAwgasgskTPAWGSRTPGTAAGGAPTARGGSGSRTPAWGGAGSRT---PAWGGAGPTGSRTPAwgGASAWGNKSSE 78


                   ....*.
gi 238859629   123 TAAGSQ 128
Cdd:smart01104  79 GSASSW 84
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
195-570 7.06e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.92  E-value: 7.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859629 195 SQGPEDPILDVKNKLETKESTAEDDISVK----LDHGITRGRLI--EDDIVCSPLKKASSYSDTLESHRatcgkgtrrai 268
Cdd:COG5048   13 NSVLSSTPKSTLKSLSNAPRPDSCPNCTDsfsrLEHLTRHIRSHtgEKPSQCSYSGCDKSFSRPLELSR----------- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859629 269 wtHKKKRQEgNKLENPESSNVILEQKHRKHKPARKRNKYKLDSIDHPVSCMRARRYP--CNVCEKMFKQPIHLVEHMRTH 346
Cdd:COG5048   82 --HLRTHHN-NPSDLNSKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPqlPDLLSISNLRNNPLPGNNSSS 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859629 347 TGEK-------PFRCKECGRAFSQSASLNTHQRIHTGEKPFACEECGKAFRHRSSLNQHHRTHTGEKPFTCDKCQKAFSQ 419
Cdd:COG5048  159 VNTPqsnslhpPLPANSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPK 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859629 420 NISLVQHLRTHSGEKPFSCSECGKPFRQIRHLSEHVRIHTGE-------KPYKCTSCCKTFSHRAYLTHHQR--IHTGE- 489
Cdd:COG5048  239 SLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEs 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859629 490 -RPYKCKE--CGKAFRQRIHLSNHRTVHTGVKAYEC-------------NRCGKAYRH---------------------- 531
Cdd:COG5048  319 lKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEkllnssskfspllNNEPPQSLQqykdlkndkksetlsnscirnf 398

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 238859629 532 --DSSFKKHQRHHTGEKPYEC--TECGKSFSYNSSLSRHQKIH 570
Cdd:COG5048  399 krDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIH 441
zf-H2C2_2 pfam13465
Zinc-finger double domain;
338-363 9.64e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 9.64e-06
                          10        20
                  ....*....|....*....|....*.
gi 238859629  338 HLVEHMRTHTGEKPFRCKECGRAFSQ 363
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
450-475 3.80e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 3.80e-05
                          10        20
                  ....*....|....*....|....*.
gi 238859629  450 HLSEHVRIHTGEKPYKCTSCCKTFSH 475
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
534-559 5.68e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 5.68e-05
                          10        20
                  ....*....|....*....|....*.
gi 238859629  534 SFKKHQRHHTGEKPYECTECGKSFSY 559
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
366-391 8.08e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 8.08e-05
                          10        20
                  ....*....|....*....|....*.
gi 238859629  366 SLNTHQRIHTGEKPFACEECGKAFRH 391
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
394-419 1.97e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 1.97e-04
                          10        20
                  ....*....|....*....|....*.
gi 238859629  394 SLNQHHRTHTGEKPFTCDKCQKAFSQ 419
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
482-503 2.07e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.07e-04
                          10        20
                  ....*....|....*....|..
gi 238859629  482 HQRIHTGERPYKCKECGKAFRQ 503
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
CTD smart01104
Spt5 C-terminal nonapeptide repeat binding Spt4; The C-terminal domain of the transcription ...
 65-132 7.20e-04

Spt5 C-terminal nonapeptide repeat binding Spt4; The C-terminal domain of the transcription elongation factor protein Spt5 is necessary for binding to Spt4 to form the functional complex that regulates early transcription elongation by RNA polymerase II. The complex may be involved in pre-mRNA processing through its association with mRNA capping enzymes. This CTD domain carries a regular nonapeptide repeat that can be present in up to 18 copies, as in S. pombe. The repeat has a characteristic TPA motif.


Pssm-ID: 215026 [Multi-domain]  Cd Length: 121  Bit Score: 39.81  E-value: 7.20e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 238859629    65 GATPGTTATGSHdeatpgTPAAGSHDGETPGIPAAGSHDGETPGTPTAGSHDGVTPGTTAAGSQESLT 132
Cdd:smart01104   2 GRTPAWGASGSK------TPAWGSRTPGTAAGGAPTARGGSGSRTPAWGGAGSRTPAWGGAGPTGSRT 63
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 548-570 8.01e-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: 36.89  E-value: 8.01e-04
                          10        20
                  ....*....|....*....|...
gi 238859629  548 YECTECGKSFSYNSSLSRHQKIH 570
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 380-402 1.58e-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: 1.58e-03
                          10        20
                  ....*....|....*....|...
gi 238859629  380 FACEECGKAFRHRSSLNQHHRTH 402
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 352-374 2.14e-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: 2.14e-03
                          10        20
                  ....*....|....*....|...
gi 238859629  352 FRCKECGRAFSQSASLNTHQRIH 374
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
422-447 4.48e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.48e-03
                          10        20
                  ....*....|....*....|....*.
gi 238859629  422 SLVQHLRTHSGEKPFSCSECGKPFRQ 447
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PHA00733 PHA00733
hypothetical protein
 407-455 5.85e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.16  E-value: 5.85e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 238859629 407 PFTCDKCQKAFSQNISLVQHLRTHSGEKpfSCSECGKPFRQIRHLSEHV 455
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDHV 119
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 324-346 6.60e-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: 6.60e-03
                          10        20
                  ....*....|....*....|...
gi 238859629  324 YPCNVCEKMFKQPIHLVEHMRTH 346
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 488-568 8.32e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 38.93  E-value: 8.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859629 488 GERPYKCK--ECGKAFRQRIHLSNHRtVHtgvkayecNRCGKAYRHDSSFKKHQRHHTGEKPYECTECGKSFSYNSSLSR 565
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLKYHM-LH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                 ...
gi 238859629 566 HQK 568
Cdd:COG5189  417 HRK 419
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH