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Conserved domains on  [gi|1953269493|ref|XP_038511621|]
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zinc finger protein 28 homolog isoform X5 [Canis lupus familiaris]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12016853)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 13-54 8.67e-26

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: 99.47  E-value: 8.67e-26
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1953269493  13 SVTFRDVTVDFTQEEWQQLEPAQKDLYRDVMLENYRNLVSLD 54
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
163-520 7.86e-13

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 70.49  E-value: 7.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953269493 163 KKSYDCSACGKAFSRSSSLMKHQRIHTGEKPYECDV--CGKHFIERSSLTIHQRVHTG------------EKPYACGD-- 226
Cdd:COG5048    31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNnpsdlnskslplSNSKASSSsl 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953269493 227 --CGKAFS---------------QRMNLIVHQRTHTGEKPY-----VCDVCRKAFRKTSSLAQ---------------HE 269
Cdd:COG5048   111 ssSSSNSNdnnllsshslppssrDPQLPDLLSISNLRNNPLpgnnsSSVNTPQSNSLHPPLPAnslskdpssnlslliSS 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953269493 270 RVHTGEKPYACGDCGKAFSQNMHLIVHQRTHTGEKPYVCDVCGRAFSQnmHLTEHQRTHTGEKPYA--CKECGKAFNKSS 347
Cdd:COG5048   191 NVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPK--SLLSQSPSSLSSSDSSssASESPRSSLPTA 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953269493 348 SLTLHHRNHTGE-------KPYACGECGKAFSQSSYLIQHQR--FHIG--VKPFECNA--CGKAFSKNSSLTQHQRIHTG 414
Cdd:COG5048   269 SSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGesLKPFSCPYslCGKLFSRNDALKRHILLHTS 348

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953269493 415 EKPYECYI--CKKHFTGRSSLLVHQM-----GHTGEKPYAC--GECGKAFSQSAYLIEHQRIHTGEKP--YKCGQCGKAF 483
Cdd:COG5048   349 ISPAKEKLlnSSSKFSPLLNNEPPQSlqqykDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSF 428

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1953269493 484 IKNSSLTVHQRIHTGEKPYKCgeCGKTFSRNTNLTRH 520
Cdd:COG5048   429 NRHYNLIPHKKIHTNHAPLLC--SILKSFRRDLDLSN 463
 
Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 13-54 8.67e-26

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: 99.47  E-value: 8.67e-26
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1953269493  13 SVTFRDVTVDFTQEEWQQLEPAQKDLYRDVMLENYRNLVSLD 54
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
14-57 6.88e-25

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 97.28  E-value: 6.88e-25
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1953269493   14 VTFRDVTVDFTQEEWQQLEPAQKDLYRDVMLENYRNLVSLDLET 57
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQV 44
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 14-53 1.00e-22

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: 90.69  E-value: 1.00e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1953269493  14 VTFRDVTVDFTQEEWQQLEPAQKDLYRDVMLENYRNLVSL 53
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
163-520 7.86e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 70.49  E-value: 7.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953269493 163 KKSYDCSACGKAFSRSSSLMKHQRIHTGEKPYECDV--CGKHFIERSSLTIHQRVHTG------------EKPYACGD-- 226
Cdd:COG5048    31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNnpsdlnskslplSNSKASSSsl 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953269493 227 --CGKAFS---------------QRMNLIVHQRTHTGEKPY-----VCDVCRKAFRKTSSLAQ---------------HE 269
Cdd:COG5048   111 ssSSSNSNdnnllsshslppssrDPQLPDLLSISNLRNNPLpgnnsSSVNTPQSNSLHPPLPAnslskdpssnlslliSS 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953269493 270 RVHTGEKPYACGDCGKAFSQNMHLIVHQRTHTGEKPYVCDVCGRAFSQnmHLTEHQRTHTGEKPYA--CKECGKAFNKSS 347
Cdd:COG5048   191 NVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPK--SLLSQSPSSLSSSDSSssASESPRSSLPTA 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953269493 348 SLTLHHRNHTGE-------KPYACGECGKAFSQSSYLIQHQR--FHIG--VKPFECNA--CGKAFSKNSSLTQHQRIHTG 414
Cdd:COG5048   269 SSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGesLKPFSCPYslCGKLFSRNDALKRHILLHTS 348

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953269493 415 EKPYECYI--CKKHFTGRSSLLVHQM-----GHTGEKPYAC--GECGKAFSQSAYLIEHQRIHTGEKP--YKCGQCGKAF 483
Cdd:COG5048   349 ISPAKEKLlnSSSKFSPLLNNEPPQSlqqykDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSF 428

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1953269493 484 IKNSSLTVHQRIHTGEKPYKCgeCGKTFSRNTNLTRH 520
Cdd:COG5048   429 NRHYNLIPHKKIHTNHAPLLC--SILKSFRRDLDLSN 463
zf-H2C2_2 pfam13465
Zinc-finger double domain;
320-345 8.32e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 8.32e-05
                          10        20
                  ....*....|....*....|....*.
gi 1953269493 320 HLTEHQRTHTGEKPYACKECGKAFNK 345
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PHA00733 PHA00733
hypothetical protein
 361-426 1.68e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 38.70  E-value: 1.68e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953269493 361 PYACGECGKAFSQSSYLIQHQRFHIGVKpfECNACGKAFSKNSSLTQHqrihtgekpyecyICKKH 426
Cdd:PHA00733   73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH-------------VCKKH 123
 
Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 13-54 8.67e-26

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: 99.47  E-value: 8.67e-26
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1953269493  13 SVTFRDVTVDFTQEEWQQLEPAQKDLYRDVMLENYRNLVSLD 54
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
14-57 6.88e-25

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 97.28  E-value: 6.88e-25
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1953269493   14 VTFRDVTVDFTQEEWQQLEPAQKDLYRDVMLENYRNLVSLDLET 57
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQV 44
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 14-53 1.00e-22

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: 90.69  E-value: 1.00e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1953269493  14 VTFRDVTVDFTQEEWQQLEPAQKDLYRDVMLENYRNLVSL 53
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
163-520 7.86e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 70.49  E-value: 7.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953269493 163 KKSYDCSACGKAFSRSSSLMKHQRIHTGEKPYECDV--CGKHFIERSSLTIHQRVHTG------------EKPYACGD-- 226
Cdd:COG5048    31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNnpsdlnskslplSNSKASSSsl 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953269493 227 --CGKAFS---------------QRMNLIVHQRTHTGEKPY-----VCDVCRKAFRKTSSLAQ---------------HE 269
Cdd:COG5048   111 ssSSSNSNdnnllsshslppssrDPQLPDLLSISNLRNNPLpgnnsSSVNTPQSNSLHPPLPAnslskdpssnlslliSS 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953269493 270 RVHTGEKPYACGDCGKAFSQNMHLIVHQRTHTGEKPYVCDVCGRAFSQnmHLTEHQRTHTGEKPYA--CKECGKAFNKSS 347
Cdd:COG5048   191 NVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPK--SLLSQSPSSLSSSDSSssASESPRSSLPTA 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953269493 348 SLTLHHRNHTGE-------KPYACGECGKAFSQSSYLIQHQR--FHIG--VKPFECNA--CGKAFSKNSSLTQHQRIHTG 414
Cdd:COG5048   269 SSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGesLKPFSCPYslCGKLFSRNDALKRHILLHTS 348

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953269493 415 EKPYECYI--CKKHFTGRSSLLVHQM-----GHTGEKPYAC--GECGKAFSQSAYLIEHQRIHTGEKP--YKCGQCGKAF 483
Cdd:COG5048   349 ISPAKEKLlnSSSKFSPLLNNEPPQSlqqykDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSF 428

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1953269493 484 IKNSSLTVHQRIHTGEKPYKCgeCGKTFSRNTNLTRH 520
Cdd:COG5048   429 NRHYNLIPHKKIHTNHAPLLC--SILKSFRRDLDLSN 463
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
178-524 2.59e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 68.95  E-value: 2.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953269493 178 SSSLMKHQRIHTGE----KPYECDVCGKHFIERSSLTIHQRVHTGEKPYACGD--CGKAFSQRMNLIVHQRTHTGEKPYV 251
Cdd:COG5048    14 SVLSSTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953269493 252 CDVCRKAFRKTSSLAQHERVHTGE-KPYACGDCGKAFSQN--MHLIVHQRTHTGEKPYvcDVCGRAFSQNMHLTEHQRTH 328
Cdd:COG5048    94 NSKSLPLSNSKASSSSLSSSSSNSnDNNLLSSHSLPPSSRdpQLPDLLSISNLRNNPL--PGNNSSSVNTPQSNSLHPPL 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953269493 329 TGEkpyackECGKAFNKSSSLTLHHRNHTGEKPYACGECGKAFSQSSYLIQHQRFHIGVKPFECNACGKAFSK------N 402
Cdd:COG5048   172 PAN------SLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKsllsqsP 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953269493 403 SSLTQHQRIHTGEKPYECYICKKHFTGRSSLLVHQMGHTG-EKPYACGECGKAFSQSAYLIEHQR--IHTGE--KPYKCG 477
Cdd:COG5048   246 SSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCP 325

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1953269493 478 --QCGKAFIKNSSLTVHQRIHTGEKPYKC--GECGKTFSRNTNLTRHLRIH 524
Cdd:COG5048   326 ysLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQ 376
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
276-525 3.95e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 62.02  E-value: 3.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953269493 276 KPYACGDCGKAFSQNMHLIVHQRTHTGEKPYVCDVCGRA--FSQNMHLTEHQRTHTGEKPYACK---------------- 337
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHHNNPSDLNSkslplsnskassssls 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953269493 338 ECGKAFNKSSSL----------------TLHHRNHTGEKPYACGECGKAFSQSSYLIQ-------------------HQR 382
Cdd:COG5048   112 SSSSNSNDNNLLsshslppssrdpqlpdLLSISNLRNNPLPGNNSSSVNTPQSNSLHPplpanslskdpssnlslliSSN 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953269493 383 FHIGVKPFECNACGKAFSKNSSLTQHQRIHTGEKPYECY----ICKKHFTGRSSLLVHQMGHTGEKPYACGEC-GKAFSQ 457
Cdd:COG5048   192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTtnsqLSPKSLLSQSPSSLSSSDSSSSASESPRSSlPTASSQ 271

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953269493 458 SAYLIEH-QRIHTG-EKPYKCGQCGKAFIKNSSLTVHQR--IHTGE--KPYKCGE--CGKTFSRNTNLTRHLRIHT 525
Cdd:COG5048   272 SSSPNESdSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHT 347
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 246-329 1.37e-05

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 47.41  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953269493 246 GEKPYVCDV--CRKAFRKTSSLAQHeRVHtgekpyacGDCGKAFSQNMHLIVHQRTHTGEKPYVCDVCGRAFSQNMHLTE 323
Cdd:COG5189   346 DGKPYKCPVegCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                  ....*.
gi 1953269493 324 HqRTHT 329
Cdd:COG5189   417 H-RKHS 421
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 330-413 4.07e-05

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 45.86  E-value: 4.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953269493 330 GEKPYACK--ECGKAFNKSSSLTlHHRNHtgekpyacGECGKAFSQSSYLIQHQRFHIGVKPFECNACGKAFSKNSSLTQ 407
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLK-YHMLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                  ....*.
gi 1953269493 408 HqRIHT 413
Cdd:COG5189   417 H-RKHS 421
zf-H2C2_2 pfam13465
Zinc-finger double domain;
320-345 8.32e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 8.32e-05
                          10        20
                  ....*....|....*....|....*.
gi 1953269493 320 HLTEHQRTHTGEKPYACKECGKAFNK 345
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
180-203 1.54e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.54e-04
                          10        20
                  ....*....|....*....|....
gi 1953269493 180 SLMKHQRIHTGEKPYECDVCGKHF 203
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 502-524 2.33e-04

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 38.44  E-value: 2.33e-04
                          10        20
                  ....*....|....*....|...
gi 1953269493 502 YKCGECGKTFSRNTNLTRHLRIH 524
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
488-513 2.70e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 2.70e-04
                          10        20
                  ....*....|....*....|....*.
gi 1953269493 488 SLTVHQRIHTGEKPYKCGECGKTFSR 513
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
292-317 4.11e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.11e-04
                          10        20
                  ....*....|....*....|....*.
gi 1953269493 292 HLIVHQRTHTGEKPYVCDVCGRAFSQ 317
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
460-483 4.28e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.28e-04
                          10        20
                  ....*....|....*....|....
gi 1953269493 460 YLIEHQRIHTGEKPYKCGQCGKAF 483
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
236-259 5.36e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 5.36e-04
                          10        20
                  ....*....|....*....|....
gi 1953269493 236 NLIVHQRTHTGEKPYVCDVCRKAF 259
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 190-273 6.51e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 42.40  E-value: 6.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953269493 190 GEKPYECDV--CGKHFIERSSLTIHqRVHtgekpyacGDCGKAFSQRMNLIVHQRTHTGEKPYVCDVCRKAFRKTSSLAQ 267
Cdd:COG5189   346 DGKPYKCPVegCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                  ....*.
gi 1953269493 268 HeRVHT 273
Cdd:COG5189   417 H-RKHS 421
zf-H2C2_2 pfam13465
Zinc-finger double domain;
264-289 6.53e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 6.53e-04
                          10        20
                  ....*....|....*....|....*.
gi 1953269493 264 SLAQHERVHTGEKPYACGDCGKAFSQ 289
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 442-525 1.21e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 41.24  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953269493 442 GEKPYACG--ECGKAFSQSAYLIEHqRIHtgekpykcGQCGKAFIKNSSLTVHQRIHTGEKPYKCGECGKTFSRNTNLTR 519
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                  ....*.
gi 1953269493 520 HlRIHT 525
Cdd:COG5189   417 H-RKHS 421
PHA00733 PHA00733
hypothetical protein
 361-426 1.68e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 38.70  E-value: 1.68e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953269493 361 PYACGECGKAFSQSSYLIQHQRFHIGVKpfECNACGKAFSKNSSLTQHqrihtgekpyecyICKKH 426
Cdd:PHA00733   73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH-------------VCKKH 123
zf-H2C2_2 pfam13465
Zinc-finger double domain;
404-428 1.96e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 1.96e-03
                          10        20
                  ....*....|....*....|....*
gi 1953269493 404 SLTQHQRIHTGEKPYECYICKKHFT 428
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
348-373 2.87e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 2.87e-03
                          10        20
                  ....*....|....*....|....*.
gi 1953269493 348 SLTLHHRNHTGEKPYACGECGKAFSQ 373
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
208-233 3.40e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 3.40e-03
                          10        20
                  ....*....|....*....|....*.
gi 1953269493 208 SLTIHQRVHTGEKPYACGDCGKAFSQ 233
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 306-328 4.91e-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: 4.91e-03
                          10        20
                  ....*....|....*....|...
gi 1953269493 306 YVCDVCGRAFSQNMHLTEHQRTH 328
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
376-401 5.08e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 5.08e-03
                          10        20
                  ....*....|....*....|....*.
gi 1953269493 376 YLIQHQRFHIGVKPFECNACGKAFSK 401
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 222-244 5.42e-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: 5.42e-03
                          10        20
                  ....*....|....*....|...
gi 1953269493 222 YACGDCGKAFSQRMNLIVHQRTH 244
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 278-300 5.69e-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: 5.69e-03
                          10        20
                  ....*....|....*....|...
gi 1953269493 278 YACGDCGKAFSQNMHLIVHQRTH 300
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 166-188 5.86e-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: 5.86e-03
                          10        20
                  ....*....|....*....|...
gi 1953269493 166 YDCSACGKAFSRSSSLMKHQRIH 188
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA00733 PHA00733
hypothetical protein
 372-436 5.95e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.16  E-value: 5.95e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953269493 372 SQSSYLIQHQRFHiGVKPFECNACGKAFSKNSSLTQHQRIHTGEKpyECYICKKHFTGRSSLLVH 436
Cdd:PHA00733   57 DESSYLYKLLTSK-AVSPYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH 118
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 474-496 7.49e-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: 7.49e-03
                          10        20
                  ....*....|....*....|...
gi 1953269493 474 YKCGQCGKAFIKNSSLTVHQRIH 496
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA00733 PHA00733
hypothetical protein
 221-268 8.65e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 36.78  E-value: 8.65e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1953269493 221 PYACGDCGKAFSQRMNLIVHQRTHTGEKpyVCDVCRKAFRKTSSLAQH 268
Cdd:PHA00733   73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH 118
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 390-412 9.30e-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: 33.81  E-value: 9.30e-03
                          10        20
                  ....*....|....*....|...
gi 1953269493 390 FECNACGKAFSKNSSLTQHQRIH 412
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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