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Conserved domains on  [gi|1720432748|ref|XP_030100466|]
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uncharacterized protein LOC71640 isoform X1 [Mus musculus]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-68 1.09e-28

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 108.45  E-value: 1.09e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720432748    8 VSFEDVTVKFTWEEWQNLNDAQKMLYRSVMLETYNSLLSLGQCIPKPELIFKLEQGEEPWT 68
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
246-594 3.39e-09

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 59.32  E-value: 3.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432748 246 KATFSKKYNLTKHQATNSGRKSCKCLES--KKTFPSELDIIEHQRTHNQKKDHVCIQCEKPFSTK--------------- 308
Cdd:COG5048    40 TDSFSRLEHLTRHIRSHTGEKPSQCSYSgcDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKasssslsssssnsnd 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432748 309 ----SSLTIHQRIHTGEKPYGCSECNKTFRQKSA--------------------------------LIVHERTHTGVKPF 352
Cdd:COG5048   120 nnllSSHSLPPSSRDPQLPDLLSISNLRNNPLPGnnsssvntpqsnslhpplpanslskdpssnlsLLISSNVSTSIPSS 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432748 353 ECCECGKAFQHKWYLKTHQRTHTGEKPYACIECGKAFLKKSYLKMHQGTHKSDKPYECEKCGKTFHNRSYFNMHHRTHTG 432
Cdd:COG5048   200 SENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESD 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432748 433 E-------KPYACSECGKAFYQKSDLRRHQR--IHNSEKL--HECKE--CGKAFQNKSYLKTHQKVHTGEKPYECK--EC 497
Cdd:COG5048   280 SssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGESLkpFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNS 359
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432748 498 GKAFQNKSYLNKHQIIH-----TGEKPYEC--NKCGKTFQWKLVLSKHHRTHTGEKPYEC--IQCGKMFGYKSSLIVHEL 568
Cdd:COG5048   360 SSKFSPLLNNEPPQSLQqykdlKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKK 439
                         410       420
                  ....*....|....*....|....*.
gi 1720432748 569 IHSGEKPYECNvCRKTFSQKSNLSRH 594
Cdd:COG5048   440 IHTNHAPLLCS-ILKSFRRDLDLSNH 464
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-68 1.09e-28

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 108.45  E-value: 1.09e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720432748    8 VSFEDVTVKFTWEEWQNLNDAQKMLYRSVMLETYNSLLSLGQCIPKPELIFKLEQGEEPWT 68
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
7-48 1.03e-18

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: 79.44  E-value: 1.03e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1720432748   7 LVSFEDVTVKFTWEEWQNLNDAQKMLYRSVMLETYNSLLSLG 48
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
8-47 2.35e-14

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: 67.19  E-value: 2.35e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1720432748   8 VSFEDVTVKFTWEEWQNLNDAQKMLYRSVMLETYNSLLSL 47
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
246-594 3.39e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 59.32  E-value: 3.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432748 246 KATFSKKYNLTKHQATNSGRKSCKCLES--KKTFPSELDIIEHQRTHNQKKDHVCIQCEKPFSTK--------------- 308
Cdd:COG5048    40 TDSFSRLEHLTRHIRSHTGEKPSQCSYSgcDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKasssslsssssnsnd 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432748 309 ----SSLTIHQRIHTGEKPYGCSECNKTFRQKSA--------------------------------LIVHERTHTGVKPF 352
Cdd:COG5048   120 nnllSSHSLPPSSRDPQLPDLLSISNLRNNPLPGnnsssvntpqsnslhpplpanslskdpssnlsLLISSNVSTSIPSS 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432748 353 ECCECGKAFQHKWYLKTHQRTHTGEKPYACIECGKAFLKKSYLKMHQGTHKSDKPYECEKCGKTFHNRSYFNMHHRTHTG 432
Cdd:COG5048   200 SENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESD 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432748 433 E-------KPYACSECGKAFYQKSDLRRHQR--IHNSEKL--HECKE--CGKAFQNKSYLKTHQKVHTGEKPYECK--EC 497
Cdd:COG5048   280 SssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGESLkpFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNS 359
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432748 498 GKAFQNKSYLNKHQIIH-----TGEKPYEC--NKCGKTFQWKLVLSKHHRTHTGEKPYEC--IQCGKMFGYKSSLIVHEL 568
Cdd:COG5048   360 SSKFSPLLNNEPPQSLQqykdlKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKK 439
                         410       420
                  ....*....|....*....|....*.
gi 1720432748 569 IHSGEKPYECNvCRKTFSQKSNLSRH 594
Cdd:COG5048   440 IHTNHAPLLCS-ILKSFRRDLDLSNH 464
zf-H2C2_2 pfam13465
Zinc-finger double domain;
366-389 2.56e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.56e-04
                          10        20
                  ....*....|....*....|....
gi 1720432748 366 YLKTHQRTHTGEKPYACIECGKAF 389
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-68 1.09e-28

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 108.45  E-value: 1.09e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720432748    8 VSFEDVTVKFTWEEWQNLNDAQKMLYRSVMLETYNSLLSLGQCIPKPELIFKLEQGEEPWT 68
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
7-48 1.03e-18

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: 79.44  E-value: 1.03e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1720432748   7 LVSFEDVTVKFTWEEWQNLNDAQKMLYRSVMLETYNSLLSLG 48
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
8-47 2.35e-14

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: 67.19  E-value: 2.35e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1720432748   8 VSFEDVTVKFTWEEWQNLNDAQKMLYRSVMLETYNSLLSL 47
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
246-594 3.39e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 59.32  E-value: 3.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432748 246 KATFSKKYNLTKHQATNSGRKSCKCLES--KKTFPSELDIIEHQRTHNQKKDHVCIQCEKPFSTK--------------- 308
Cdd:COG5048    40 TDSFSRLEHLTRHIRSHTGEKPSQCSYSgcDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKasssslsssssnsnd 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432748 309 ----SSLTIHQRIHTGEKPYGCSECNKTFRQKSA--------------------------------LIVHERTHTGVKPF 352
Cdd:COG5048   120 nnllSSHSLPPSSRDPQLPDLLSISNLRNNPLPGnnsssvntpqsnslhpplpanslskdpssnlsLLISSNVSTSIPSS 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432748 353 ECCECGKAFQHKWYLKTHQRTHTGEKPYACIECGKAFLKKSYLKMHQGTHKSDKPYECEKCGKTFHNRSYFNMHHRTHTG 432
Cdd:COG5048   200 SENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESD 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432748 433 E-------KPYACSECGKAFYQKSDLRRHQR--IHNSEKL--HECKE--CGKAFQNKSYLKTHQKVHTGEKPYECK--EC 497
Cdd:COG5048   280 SssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGESLkpFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNS 359
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432748 498 GKAFQNKSYLNKHQIIH-----TGEKPYEC--NKCGKTFQWKLVLSKHHRTHTGEKPYEC--IQCGKMFGYKSSLIVHEL 568
Cdd:COG5048   360 SSKFSPLLNNEPPQSLQqykdlKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKK 439
                         410       420
                  ....*....|....*....|....*.
gi 1720432748 569 IHSGEKPYECNvCRKTFSQKSNLSRH 594
Cdd:COG5048   440 IHTNHAPLLCS-ILKSFRRDLDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
254-599 2.44e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 56.63  E-value: 2.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432748 254 NLTKHQATNSGRKSCKCLESKKTFPSELDIIEHQRTHNQKKDHVC--IQCEKPFSTKSSLTIHQRIHTGEKPYGCSECNK 331
Cdd:COG5048    20 PKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLP 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432748 332 TFRQKSALIVHER-THTGVKPFECCECGKAFQHKWYLK--THQRTHTGEKP-YACIECGKAFLKKSYLKM---------- 397
Cdd:COG5048   100 LSNSKASSSSLSSsSSNSNDNNLLSSHSLPPSSRDPQLpdLLSISNLRNNPlPGNNSSSVNTPQSNSLHPplpanslskd 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432748 398 ----------HQGTHKSDKPYECEKCGKTFHNRSYFNMHHRTHTgEKPYACSECGKAFYQKSDLRRHQRIHNSEKLHECK 467
Cdd:COG5048   180 pssnlsllisSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENS-SSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSAS 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432748 468 ECGKAFQNKSYLKTHQKVHTGE-------KPYECKECGKAFQNKSYLNKHQ--IIHTGE--KPYEC--NKCGKTFQWKLV 534
Cdd:COG5048   259 ESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCpySLCGKLFSRNDA 338
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720432748 535 LSKHHRTHTGEKPYECIQCGKMFGYKSSL-------IVHELIHSGEKPYECNV--CRKTFSQKSNLSRHQRTHR 599
Cdd:COG5048   339 LKRHILLHTSISPAKEKLLNSSSKFSPLLnneppqsLQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHL 412
zf-H2C2_2 pfam13465
Zinc-finger double domain;
366-389 2.56e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.56e-04
                          10        20
                  ....*....|....*....|....
gi 1720432748 366 YLKTHQRTHTGEKPYACIECGKAF 389
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
270-511 3.89e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.15  E-value: 3.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432748 270 CLESKKTFPSELDIIEHQRTHNQKKD----------HVCIQCEKPFSTKSSLTIHQR--IHTGE--KPYGCSE--CNKTF 333
Cdd:COG5048   254 SSSASESPRSSLPTASSQSSSPNESDsssekgfslpIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLF 333
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432748 334 RQKSALIVHERTHTGVKPFeccecgkafqhKWYLKTHQRTHTGEKPYaciecgkafLKKSYLKMHQGTHKsDKPYECE-- 411
Cdd:COG5048   334 SRNDALKRHILLHTSISPA-----------KEKLLNSSSKFSPLLNN---------EPPQSLQQYKDLKN-DKKSETLsn 392
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432748 412 KCGKTFHNRSYFNMHHRTHTGEKPYACSecgkafyqksdlrrhqrihnseklheCKECGKAFQNKSYLKTHQKVHTGEKP 491
Cdd:COG5048   393 SCIRNFKRDSNLSLHIITHLSFRPYNCK--------------------------NPPCSKSFNRHYNLIPHKKIHTNHAP 446
                         250       260
                  ....*....|....*....|
gi 1720432748 492 YECKECGKAFQNKSYLNKHQ 511
Cdd:COG5048   447 LLCSILKSFRRDLDLSNHGK 466
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
376-431 4.55e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 42.78  E-value: 4.55e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720432748 376 GEKPYAC--IECGKAFLKKSYLKMH-------------------QGTHKSDKPYECEKCGKTFHNRSYFNmHHRTHT 431
Cdd:COG5189   346 DGKPYKCpvEGCNKKYKNQNGLKYHmlhghqnqklhenpspekmNIFSAKDKPYRCEVCDKRYKNLNGLK-YHRKHS 421
zf-H2C2_2 pfam13465
Zinc-finger double domain;
478-501 4.76e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.76e-04
                          10        20
                  ....*....|....*....|....
gi 1720432748 478 YLKTHQKVHTGEKPYECKECGKAF 501
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
516-600 1.35e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 41.63  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432748 516 GEKPYECN--KCGKTFQWKLVLsKHHRTHTgekpyeciQCGKMFGYKSSLIVHELIHSGEKPYECNVCRKTFSQKSNLSR 593
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGL-KYHMLHG--------HQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416

                  ....*..
gi 1720432748 594 HqRTHRH 600
Cdd:COG5189   417 H-RKHSH 422
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
432-510 1.46e-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: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432748 432 GEKPYACS--ECGKAFYQKSDLRRHQRI-HNSEKLHECKECGKafqnksylktHQKVHTGEKPYECKECGKAFQNKSYLN 508
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLKYHMLHgHQNQKLHENPSPEK----------MNIFSAKDKPYRCEVCDKRYKNLNGLK 415

                  ..
gi 1720432748 509 KH 510
Cdd:COG5189   416 YH 417
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
576-598 1.52e-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: 1.52e-03
                          10        20
                  ....*....|....*....|...
gi 1720432748 576 YECNVCRKTFSQKSNLSRHQRTH 598
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
535-557 1.59e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.59e-03
                          10        20
                  ....*....|....*....|...
gi 1720432748 535 LSKHHRTHTGEKPYECIQCGKMF 557
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
506-529 2.76e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 2.76e-03
                          10        20
                  ....*....|....*....|....
gi 1720432748 506 YLNKHQIIHTGEKPYECNKCGKTF 529
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
422-447 3.93e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 3.93e-03
                          10        20
                  ....*....|....*....|....*.
gi 1720432748 422 YFNMHHRTHTGEKPYACSECGKAFYQ 447
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
436-458 4.19e-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: 34.97  E-value: 4.19e-03
                          10        20
                  ....*....|....*....|...
gi 1720432748 436 YACSECGKAFYQKSDLRRHQRIH 458
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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