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Conserved domains on  [gi|662236799|ref|NP_001284548|]
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zinc finger protein 14 homolog isoform 1 [Homo sapiens]

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;
6-68 4.81e-30

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 111.92  E-value: 4.81e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 662236799     6 VTFRDVAIDFSQEEWEFLDPAQRDLYRDVMWENYSNFISLaGPSISKPDVITLLdEERKEPGM 68
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSL-GFQVPKPDLISQL-EQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
199-534 2.01e-11

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 66.26  E-value: 2.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236799 199 KPYKCKECGQAFRQRAHLIRHHKLHTGEKPYEC--KECGKAFTVLQELTQHQRLHTGEKPYECkeCGKAFRVHQQLARHQ 276
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLN--SKSLPLSNSKASSSS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236799 277 RIHTGEKPYECKDCgkTFRQCTHLTRHQRLHTAEKLY-----ECKECGKAFVCGPdlrVHQKIHFgekPYECKECGKAFR 351
Cdd:COG5048  110 LSSSSSNSNDNNLL--SSHSLPPSSRDPQLPDLLSISnlrnnPLPGNNSSSVNTP---QSNSLHP---PLPANSLSKDPS 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236799 352 ICQQLTVHQSIHTGEKPYECKECGKTFRLRQQLVRHQRIHTREKPYECMECWKTFSSYSQLISHQSIHIGERPYECEECG 431
Cdd:COG5048  182 SNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESP 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236799 432 KAFRLLSQLTQHQSIHTGE-------KPYECKECRKPFRLLSQLTQHQ--SIHTGE--KPYECKE--CGKAFRLYSFLTQ 498
Cdd:COG5048  262 RSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPYslCGKLFSRNDALKR 341

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 662236799 499 HQRIHTGEKPYKCK--ECKKAFRQ------HSHLTQHQKIHNGI 534
Cdd:COG5048  342 HILLHTSISPAKEKllNSSSKFSPllnnepPQSLQQYKDLKNDK 385
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
6-68 4.81e-30

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 111.92  E-value: 4.81e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 662236799     6 VTFRDVAIDFSQEEWEFLDPAQRDLYRDVMWENYSNFISLaGPSISKPDVITLLdEERKEPGM 68
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSL-GFQVPKPDLISQL-EQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 5-45 8.13e-24

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: 93.69  E-value: 8.13e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 662236799    5 SVTFRDVAIDFSQEEWEFLDPAQRDLYRDVMWENYSNFISL 45
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 6-45 1.64e-19

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: 81.44  E-value: 1.64e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 662236799   6 VTFRDVAIDFSQEEWEFLDPAQRDLYRDVMWENYSNFISL 45
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
199-534 2.01e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 66.26  E-value: 2.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236799 199 KPYKCKECGQAFRQRAHLIRHHKLHTGEKPYEC--KECGKAFTVLQELTQHQRLHTGEKPYECkeCGKAFRVHQQLARHQ 276
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLN--SKSLPLSNSKASSSS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236799 277 RIHTGEKPYECKDCgkTFRQCTHLTRHQRLHTAEKLY-----ECKECGKAFVCGPdlrVHQKIHFgekPYECKECGKAFR 351
Cdd:COG5048  110 LSSSSSNSNDNNLL--SSHSLPPSSRDPQLPDLLSISnlrnnPLPGNNSSSVNTP---QSNSLHP---PLPANSLSKDPS 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236799 352 ICQQLTVHQSIHTGEKPYECKECGKTFRLRQQLVRHQRIHTREKPYECMECWKTFSSYSQLISHQSIHIGERPYECEECG 431
Cdd:COG5048  182 SNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESP 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236799 432 KAFRLLSQLTQHQSIHTGE-------KPYECKECRKPFRLLSQLTQHQ--SIHTGE--KPYECKE--CGKAFRLYSFLTQ 498
Cdd:COG5048  262 RSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPYslCGKLFSRNDALKR 341

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 662236799 499 HQRIHTGEKPYKCK--ECKKAFRQ------HSHLTQHQKIHNGI 534
Cdd:COG5048  342 HILLHTSISPAKEKllNSSSKFSPllnnepPQSLQQYKDLKNDK 385
zf-H2C2_2 pfam13465
Zinc-finger double domain;
272-296 2.46e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 2.46e-04
                          10        20
                  ....*....|....*....|....*
gi 662236799  272 LARHQRIHTGEKPYECKDCGKTFRQ 296
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
6-68 4.81e-30

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 111.92  E-value: 4.81e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 662236799     6 VTFRDVAIDFSQEEWEFLDPAQRDLYRDVMWENYSNFISLaGPSISKPDVITLLdEERKEPGM 68
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSL-GFQVPKPDLISQL-EQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 5-45 8.13e-24

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: 93.69  E-value: 8.13e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 662236799    5 SVTFRDVAIDFSQEEWEFLDPAQRDLYRDVMWENYSNFISL 45
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 6-45 1.64e-19

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: 81.44  E-value: 1.64e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 662236799   6 VTFRDVAIDFSQEEWEFLDPAQRDLYRDVMWENYSNFISL 45
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
199-534 2.01e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 66.26  E-value: 2.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236799 199 KPYKCKECGQAFRQRAHLIRHHKLHTGEKPYEC--KECGKAFTVLQELTQHQRLHTGEKPYECkeCGKAFRVHQQLARHQ 276
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLN--SKSLPLSNSKASSSS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236799 277 RIHTGEKPYECKDCgkTFRQCTHLTRHQRLHTAEKLY-----ECKECGKAFVCGPdlrVHQKIHFgekPYECKECGKAFR 351
Cdd:COG5048  110 LSSSSSNSNDNNLL--SSHSLPPSSRDPQLPDLLSISnlrnnPLPGNNSSSVNTP---QSNSLHP---PLPANSLSKDPS 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236799 352 ICQQLTVHQSIHTGEKPYECKECGKTFRLRQQLVRHQRIHTREKPYECMECWKTFSSYSQLISHQSIHIGERPYECEECG 431
Cdd:COG5048  182 SNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESP 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236799 432 KAFRLLSQLTQHQSIHTGE-------KPYECKECRKPFRLLSQLTQHQ--SIHTGE--KPYECKE--CGKAFRLYSFLTQ 498
Cdd:COG5048  262 RSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPYslCGKLFSRNDALKR 341

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 662236799 499 HQRIHTGEKPYKCK--ECKKAFRQ------HSHLTQHQKIHNGI 534
Cdd:COG5048  342 HILLHTSISPAKEKllNSSSKFSPllnnepPQSLQQYKDLKNDK 385
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
156-524 9.37e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 51.24  E-value: 9.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236799 156 RHNFLTEYQIVHNGEKVYEC--KECRKTFIRRSTLSQHLRIHTGEKPYKC-KECGQAFRQRAHLIRHHKLHTGEKPYECK 232
Cdd:COG5048   45 RLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNsKSLPLSNSKASSSSLSSSSSNSNDNNLLS 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236799 233 ECGKAFTVLQELTQHQRLHTGEKPYECKECGKAFRVHQQ----------------------LARHQRIHTGEKPYECKDC 290
Cdd:COG5048  125 SHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQsnslhpplpanslskdpssnlsLLISSNVSTSIPSSSENSP 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236799 291 GKTFRQCTHLTRHQRLHTAEKLYECKECGKAFVCGPDLRVHQKIHFGEKPYECKECGKAFRICQQLTVHQSIHTGE---- 366
Cdd:COG5048  205 LSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssek 284

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236799 367 ---KPYECKECGKTFRLRQQLVRHQR--IHTRE--KPYECME--CWKTFSSYSQLISHQSIHIGERPYEC--EECGKAFR 435
Cdd:COG5048  285 gfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFS 364

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236799 436 LLS-----QLTQHQSIHTGEKPYEC--KECRKPFRLLSQLTQHQSIHTGEKPYECK--ECGKAFRLYSFLTQHQRIHTGE 506
Cdd:COG5048  365 PLLnneppQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNH 444

                        410
                 ....*....|....*...
gi 662236799 507 KPYKCkECKKAFRQHSHL 524
Cdd:COG5048  445 APLLC-SILKSFRRDLDL 461
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
407-483 5.83e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.92  E-value: 5.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236799 407 SSYSQLISHQSIHIGE----RPYECEECGKAFRLLSQLTQHQSIHTGEKPYEC--KECRKPFRLLSQLTQHQSIHTGEKP 480
Cdd:COG5048   12 NNSVLSSTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPS 91


                 ...
gi 662236799 481 YEC 483
Cdd:COG5048   92 DLN 94
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
171-303 1.03e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.69  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236799 171 KVYECKECRKTFIRRSTLSQHLR--IHTGE--KPYKCKE--CGQAFRQRAHLIRHHKLHTGEKPYECK--ECGKAFTVL- 241
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLl 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236799 242 -QELTQHQRLHTGEKP-----------------------------------YECKECGKAFRVHQQLARHQRIHTGEKPY 285
Cdd:COG5048  368 nNEPPQSLQQYKDLKNdkksetlsnscirnfkrdsnlslhiithlsfrpynCKNPPCSKSFNRHYNLIPHKKIHTNHAPL 447

                        170
                 ....*....|....*...
gi 662236799 286 ECKDCGKtFRQCTHLTRH 303
Cdd:COG5048  448 LCSILKS-FRRDLDLSNH 464
zf-H2C2_2 pfam13465
Zinc-finger double domain;
272-296 2.46e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 2.46e-04
                          10        20
                  ....*....|....*....|....*
gi 662236799  272 LARHQRIHTGEKPYECKDCGKTFRQ 296
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
496-520 5.56e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 5.56e-04
                          10        20
                  ....*....|....*....|....*
gi 662236799  496 LTQHQRIHTGEKPYKCKECKKAFRQ 520
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
188-212 5.96e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 5.96e-04
                          10        20
                  ....*....|....*....|....*
gi 662236799  188 LSQHLRIHTGEKPYKCKECGQAFRQ 212
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
243-266 1.00e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.00e-03
                          10        20
                  ....*....|....*....|....
gi 662236799  243 ELTQHQRLHTGEKPYECKECGKAF 266
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 365-443 1.01e-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: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236799 365 GEKPYECK--ECGKTFRlRQQLVRHQRIHTREKPyecmecwKTFSSYSQlISHQSIHIGERPYECEECGKAFRLLSQLTQ 442
Cdd:COG5189  346 DGKPYKCPveGCNKKYK-NQNGLKYHMLHGHQNQ-------KLHENPSP-EKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                 .
gi 662236799 443 H 443
Cdd:COG5189  417 H 417
zf-H2C2_2 pfam13465
Zinc-finger double domain;
215-239 1.26e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.26e-03
                          10        20
                  ....*....|....*....|....*
gi 662236799  215 HLIRHHKLHTGEKPYECKECGKAFT 239
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
327-350 2.07e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.07e-03
                          10        20
                  ....*....|....*....|....
gi 662236799  327 DLRVHQKIHFGEKPYECKECGKAF 350
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 285-307 2.32e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.35  E-value: 2.32e-03
                          10        20
                  ....*....|....*....|...
gi 662236799  285 YECKDCGKTFRQCTHLTRHQRLH 307
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
468-490 5.07e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 5.07e-03
                          10        20
                  ....*....|....*....|...
gi 662236799  468 LTQHQSIHTGEKPYECKECGKAF 490
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 509-531 5.96e-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: 5.96e-03
                          10        20
                  ....*....|....*....|...
gi 662236799  509 YKCKECKKAFRQHSHLTQHQKIH 531
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
299-324 9.41e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.88  E-value: 9.41e-03
                          10        20
                  ....*....|....*....|....*.
gi 662236799  299 HLTRHQRLHTAEKLYECKECGKAFVC 324
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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