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Conserved domains on  [gi|1034575314|ref|XP_016873757|]
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zinc finger protein 202 isoform X1 [Homo sapiens]

Protein Classification

SCAN and KRAB_A-box domain-containing protein( domain architecture ID 12210991)

protein containing domains SCAN, KRAB_A-box, and COG5048

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
43-153 1.48e-61

leucine rich region;


:

Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 200.22  E-value: 1.48e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575314   43 ETSHQNFRRFRYQEAASPREALIRLRELCHQWLRPERRTKEQILELLVLEQFLTVLPGELQSWVRGQRPESGEEAVTLVE 122
Cdd:smart00431   2 EIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLE 81

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1034575314  123 GLQKQPRRPRRWVTVHVHGQEVLSEETVHLG 153
Cdd:smart00431  82 DLERELDEPGQQVSAHVHGQEVLLEKMVPLG 112
KRAB smart00349
krueppel associated box;
237-297 5.37e-23

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 92.27  E-value: 5.37e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034575314  237 VTFKDVAVCFSQDQWSDLDPTQKEFYGEYVLeEDCGIVVSLSFPIPRPDEISQV-REEEPWV 297
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVML-ENYSNLVSLGFQVPKPDLISQLeQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
397-644 1.04e-08

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.17  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575314 397 HDCSVCGKSFTCNSHLVRHLRTHTGEKPYKCM--ECGKSYTRSSHLARHQKVHKMN----------------APYKYPL- 457
Cdd:COG5048    34 DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNpsdlnskslplsnskaSSSSLSSs 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575314 458 ----NRKNLEETSPVTQAERTPSVEKPYRCDD-------------------------------CGKHFRWTSDLVrHQRT 502
Cdd:COG5048   114 ssnsNDNNLLSSHSLPPSSRDPQLPDLLSISNlrnnplpgnnsssvntpqsnslhpplpanslSKDPSSNLSLLI-SSNV 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575314 503 HTGEKPFFCTICGKSFSQKSVLTTHQRIHLGGKPYLCGECGedFSEHRRYLAHRKTHAAEElYLCSECGRCFTHSAAFAK 582
Cdd:COG5048   193 STSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNS--QLSPKSLLSQSPSSLSSS-DSSSSASESPRSSLPTAS 269

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034575314 583 HLRGH----------ASVRPCRCNECGKSFSRRDHLVRHQRT--HTGE--KPFTCP--TCGKSFSRGYHLIRHQRTHS 644
Cdd:COG5048   270 SQSSSpnesdsssekGFSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPysLCGKLFSRNDALKRHILLHT 347
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
43-153 1.48e-61

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 200.22  E-value: 1.48e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575314   43 ETSHQNFRRFRYQEAASPREALIRLRELCHQWLRPERRTKEQILELLVLEQFLTVLPGELQSWVRGQRPESGEEAVTLVE 122
Cdd:smart00431   2 EIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLE 81

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1034575314  123 GLQKQPRRPRRWVTVHVHGQEVLSEETVHLG 153
Cdd:smart00431  82 DLERELDEPGQQVSAHVHGQEVLLEKMVPLG 112
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 42-130 2.55e-48

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: 163.81  E-value: 2.55e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575314  42 LETSHQNFRRFRYQEAASPREALIRLRELCHQWLRPERRTKEQILELLVLEQFLTVLPGELQSWVRGQRPESGEEAVTLV 121
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALA 80


                  ....*....
gi 1034575314 122 EGLQKQPRR 130
Cdd:pfam02023  81 EDLLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 42-125 1.39e-38

SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several vertebrate proteins that contain C2H2 zinc finger motifs, many of which may be transcription factors playing roles in cell survival and differentiation. This protein-interaction domain is able to mediate homo- and hetero-oligomerization of SCAN-containing proteins. Some SCAN-containing proteins, including those of lower vertebrates, do not contain zinc finger motifs. It has been noted that the SCAN domain resembles a domain-swapped version of the C-terminal domain of the HIV capsid protein. This domain model features elements common to the three general groups of SCAN domains (SCAN-A1, SCAN-A2, and SCAN-B). The SCAND1 protein is truncated at the C-terminus with respect to this model, the SCAND2 protein appears to have a truncated central helix.


Pssm-ID: 153421  Cd Length: 85  Bit Score: 137.01  E-value: 1.39e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575314  42 LETSHQNFRRFRYQEAASPREALIRLRELCHQWLRPERRTKEQILELLVLEQFLTVLPGELQSWVRGQRPESGEEAVTLV 121
Cdd:cd07936     1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80


                  ....
gi 1034575314 122 EGLQ 125
Cdd:cd07936    81 EDLL 84
KRAB smart00349
krueppel associated box;
237-297 5.37e-23

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 92.27  E-value: 5.37e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034575314  237 VTFKDVAVCFSQDQWSDLDPTQKEFYGEYVLeEDCGIVVSLSFPIPRPDEISQV-REEEPWV 297
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVML-ENYSNLVSLGFQVPKPDLISQLeQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 236-277 5.10e-12

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: 60.56  E-value: 5.10e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1034575314 236 LVTFKDVAVCFSQDQWSDLDPTQKEFYGEyVLEEDCGIVVSL 277
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRD-VMLENYRNLVSL 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 237-277 1.13e-11

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: 59.49  E-value: 1.13e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1034575314 237 VTFKDVAVCFSQDQWSDLDPTQKEFYGEYVLEEdCGIVVSL 277
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLEN-YENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
397-644 1.04e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.17  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575314 397 HDCSVCGKSFTCNSHLVRHLRTHTGEKPYKCM--ECGKSYTRSSHLARHQKVHKMN----------------APYKYPL- 457
Cdd:COG5048    34 DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNpsdlnskslplsnskaSSSSLSSs 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575314 458 ----NRKNLEETSPVTQAERTPSVEKPYRCDD-------------------------------CGKHFRWTSDLVrHQRT 502
Cdd:COG5048   114 ssnsNDNNLLSSHSLPPSSRDPQLPDLLSISNlrnnplpgnnsssvntpqsnslhpplpanslSKDPSSNLSLLI-SSNV 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575314 503 HTGEKPFFCTICGKSFSQKSVLTTHQRIHLGGKPYLCGECGedFSEHRRYLAHRKTHAAEElYLCSECGRCFTHSAAFAK 582
Cdd:COG5048   193 STSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNS--QLSPKSLLSQSPSSLSSS-DSSSSASESPRSSLPTAS 269

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034575314 583 HLRGH----------ASVRPCRCNECGKSFSRRDHLVRHQRT--HTGE--KPFTCP--TCGKSFSRGYHLIRHQRTHS 644
Cdd:COG5048   270 SQSSSpnesdsssekGFSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPysLCGKLFSRNDALKRHILLHT 347
zf-H2C2_2 pfam13465
Zinc-finger double domain;
607-632 1.07e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 45.05  E-value: 1.07e-06
                          10        20
                  ....*....|....*....|....*.
gi 1034575314 607 HLVRHQRTHTGEKPFTCPTCGKSFSR 632
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
43-153 1.48e-61

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 200.22  E-value: 1.48e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575314   43 ETSHQNFRRFRYQEAASPREALIRLRELCHQWLRPERRTKEQILELLVLEQFLTVLPGELQSWVRGQRPESGEEAVTLVE 122
Cdd:smart00431   2 EIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLE 81

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1034575314  123 GLQKQPRRPRRWVTVHVHGQEVLSEETVHLG 153
Cdd:smart00431  82 DLERELDEPGQQVSAHVHGQEVLLEKMVPLG 112
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 42-130 2.55e-48

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: 163.81  E-value: 2.55e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575314  42 LETSHQNFRRFRYQEAASPREALIRLRELCHQWLRPERRTKEQILELLVLEQFLTVLPGELQSWVRGQRPESGEEAVTLV 121
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALA 80


                  ....*....
gi 1034575314 122 EGLQKQPRR 130
Cdd:pfam02023  81 EDLLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 42-125 1.39e-38

SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several vertebrate proteins that contain C2H2 zinc finger motifs, many of which may be transcription factors playing roles in cell survival and differentiation. This protein-interaction domain is able to mediate homo- and hetero-oligomerization of SCAN-containing proteins. Some SCAN-containing proteins, including those of lower vertebrates, do not contain zinc finger motifs. It has been noted that the SCAN domain resembles a domain-swapped version of the C-terminal domain of the HIV capsid protein. This domain model features elements common to the three general groups of SCAN domains (SCAN-A1, SCAN-A2, and SCAN-B). The SCAND1 protein is truncated at the C-terminus with respect to this model, the SCAND2 protein appears to have a truncated central helix.


Pssm-ID: 153421  Cd Length: 85  Bit Score: 137.01  E-value: 1.39e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575314  42 LETSHQNFRRFRYQEAASPREALIRLRELCHQWLRPERRTKEQILELLVLEQFLTVLPGELQSWVRGQRPESGEEAVTLV 121
Cdd:cd07936     1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80


                  ....
gi 1034575314 122 EGLQ 125
Cdd:cd07936    81 EDLL 84
KRAB smart00349
krueppel associated box;
237-297 5.37e-23

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 92.27  E-value: 5.37e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034575314  237 VTFKDVAVCFSQDQWSDLDPTQKEFYGEYVLeEDCGIVVSLSFPIPRPDEISQV-REEEPWV 297
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVML-ENYSNLVSLGFQVPKPDLISQLeQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 236-277 5.10e-12

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: 60.56  E-value: 5.10e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1034575314 236 LVTFKDVAVCFSQDQWSDLDPTQKEFYGEyVLEEDCGIVVSL 277
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRD-VMLENYRNLVSL 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 237-277 1.13e-11

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: 59.49  E-value: 1.13e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1034575314 237 VTFKDVAVCFSQDQWSDLDPTQKEFYGEYVLEEdCGIVVSL 277
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLEN-YENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
397-644 1.04e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.17  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575314 397 HDCSVCGKSFTCNSHLVRHLRTHTGEKPYKCM--ECGKSYTRSSHLARHQKVHKMN----------------APYKYPL- 457
Cdd:COG5048    34 DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNpsdlnskslplsnskaSSSSLSSs 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575314 458 ----NRKNLEETSPVTQAERTPSVEKPYRCDD-------------------------------CGKHFRWTSDLVrHQRT 502
Cdd:COG5048   114 ssnsNDNNLLSSHSLPPSSRDPQLPDLLSISNlrnnplpgnnsssvntpqsnslhpplpanslSKDPSSNLSLLI-SSNV 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575314 503 HTGEKPFFCTICGKSFSQKSVLTTHQRIHLGGKPYLCGECGedFSEHRRYLAHRKTHAAEElYLCSECGRCFTHSAAFAK 582
Cdd:COG5048   193 STSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNS--QLSPKSLLSQSPSSLSSS-DSSSSASESPRSSLPTAS 269

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034575314 583 HLRGH----------ASVRPCRCNECGKSFSRRDHLVRHQRT--HTGE--KPFTCP--TCGKSFSRGYHLIRHQRTHS 644
Cdd:COG5048   270 SQSSSpnesdsssekGFSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPysLCGKLFSRNDALKRHILLHT 347
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
591-648 1.30e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 57.78  E-value: 1.30e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575314 591 RPCRCNECGKSFSRRDHLVRHQRTHTGEKPFTC--PTCGKSFSRGYHLIRHQRTHSEKTS 648
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPS 91
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
301-639 1.99e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 57.01  E-value: 1.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575314 301 QEPQETQEPEILSFTYTGDRSKDEEECLEQEDLSLEDIHrpVLGEPEIHQTPDWEIVFEDNPGRLNERRFGTNISQVNSF 380
Cdd:COG5048    88 NNPSDLNSKSLPLSNSKASSSSLSSSSSNSNDNNLLSSH--SLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSN 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575314 381 vNLRETTPVHPLLGRHHDCSVC---------GKSFTCNSHLVR---------HLRTHTGEKPYKCMECG----KSYTRSS 438
Cdd:COG5048   166 -SLHPPLPANSLSKDPSSNLSLlissnvstsIPSSSENSPLSSsysipssssDQNLENSSSSLPLTTNSqlspKSLLSQS 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575314 439 HLARHQKVHKMNAPYKYPLNRKNLEETSPvTQAERTPSVEK----PYRCDDCGKHFRWTSDLVRHQRT--HTGE--KPFF 510
Cdd:COG5048   245 PSSLSSSDSSSSASESPRSSLPTASSQSS-SPNESDSSSEKgfslPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFS 323

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575314 511 CTI--CGKSFSQKSVLTTHQRIHLGGKPYLC--GECGEDFS-----EHRRYLAHRKTHAAEELYLC--SECGRCFTHSAA 579
Cdd:COG5048   324 CPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSpllnnEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSN 403

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034575314 580 FAKHLRGHASVRP--CRCNECGKSFSRRDHLVRHQRTHTGEKPFTCPTCGKSFSRGyHLIRH 639
Cdd:COG5048   404 LSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDL-DLSNH 464
zf-H2C2_2 pfam13465
Zinc-finger double domain;
607-632 1.07e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 45.05  E-value: 1.07e-06
                          10        20
                  ....*....|....*....|....*.
gi 1034575314 607 HLVRHQRTHTGEKPFTCPTCGKSFSR 632
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
411-436 1.65e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 44.67  E-value: 1.65e-06
                          10        20
                  ....*....|....*....|....*.
gi 1034575314 411 HLVRHLRTHTGEKPYKCMECGKSYTR 436
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
495-520 1.60e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.97  E-value: 1.60e-05
                          10        20
                  ....*....|....*....|....*.
gi 1034575314 495 DLVRHQRTHTGEKPFFCTICGKSFSQ 520
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 593-615 3.79e-05

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: 40.75  E-value: 3.79e-05
                          10        20
                  ....*....|....*....|...
gi 1034575314 593 CRCNECGKSFSRRDHLVRHQRTH 615
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 621-643 6.83e-05

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 39.98  E-value: 6.83e-05
                          10        20
                  ....*....|....*....|...
gi 1034575314 621 FTCPTCGKSFSRGYHLIRHQRTH 643
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
479-539 8.42e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.46  E-value: 8.42e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034575314 479 KPYRCDDCGKHFRWTSDLVRHQRTHTGEKPFFCT--ICGKSFSQKSVLTTHQRIHLGGKPYLC 539
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLN 94
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 425-447 1.16e-04

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 39.59  E-value: 1.16e-04
                          10        20
                  ....*....|....*....|...
gi 1034575314 425 YKCMECGKSYTRSSHLARHQKVH 447
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 421-504 4.70e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 43.17  E-value: 4.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575314 421 GEKPYKC--MECGKSYTRSSHLarhqKVHKMNAPYKYPLNRKNLEETSPVTQAErtpsvEKPYRCDDCGKHFRWTSDLVR 498
Cdd:COG5189   346 DGKPYKCpvEGCNKKYKNQNGL----KYHMLHGHQNQKLHENPSPEKMNIFSAK-----DKPYRCEVCDKRYKNLNGLKY 416


                  ....*.
gi 1034575314 499 HqRTHT 504
Cdd:COG5189   417 H-RKHS 421
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 509-531 5.67e-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: 37.28  E-value: 5.67e-04
                          10        20
                  ....*....|....*....|...
gi 1034575314 509 FFCTICGKSFSQKSVLTTHQRIH 531
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 481-503 6.59e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.58  E-value: 6.59e-03
                          10        20
                  ....*....|....*....|...
gi 1034575314 481 YRCDDCGKHFRWTSDLVRHQRTH 503
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 397-419 6.79e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.58  E-value: 6.79e-03
                          10        20
                  ....*....|....*....|...
gi 1034575314 397 HDCSVCGKSFTCNSHLVRHLRTH 419
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
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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