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Conserved domains on  [gi|2166948758|ref|XP_045329267|]
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zinc finger protein 674 isoform X2 [Leopardus geoffroyi]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204699)

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; similar to Homo sapiens zinc finger protein 2 that may be involved in transcriptional regulation

Gene Ontology:  GO:0003677|GO:0008270|GO:0003700
PubMed:  8183940|14519192|22803940

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
50-107 1.00e-30

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 114.23  E-value: 1.00e-30
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2166948758   50 LTFRDVFVDFTLEEWRCLDLAQKNLYRDVMLENYSHLVSVGQLVPKPDVVIRLGQGEE 107
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEE 58
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
287-612 3.52e-12

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 68.95  E-value: 3.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948758 287 KPYECSECTRAFSQKSTLIAHQRTHTGEKPYECS--ECGKTFIQKSTLMKHTRTHTAEKPFvcgECAKAFKSSYHLTRHE 364
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSD---LNSKSLPLSNSKASSS 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948758 365 K----THIRQAFYEGVHCGKSGLTYPRTHMGEKPNCNKHGKPSDEKPNPIKHQRSP---IKEKAYECSKCGKSFRGKSHL 437
Cdd:COG5048   109 SlsssSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSnslHPPLPANSLSKDPSSNLSLLI 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948758 438 svHQRTHTGEKPYECSICGKTFSGKSHLSVHQRTHTGEKPYECRRCGKAF------GEKSTLVVHHRTHTGEKPYKCGEC 511
Cdd:COG5048   189 --SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpksllsQSPSSLSSSDSSSSASESPRSSLP 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948758 512 GKAFSEKSPLIKHERIHTGER-PYECSNCGKAFSRKSTLIKHQR--IHTGE--KPYECSE--CGKAFSVKSTLIVHHRTH 584
Cdd:COG5048   267 TASSQSSSPNESDSSSEKGFSlPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLH 346

                         330       340       350
                  ....*....|....*....|....*....|
gi 2166948758 585 TGEKPYEC--RDCGKAFSGKSTLIKHQRSH 612
Cdd:COG5048   347 TSISPAKEklLNSSSKFSPLLNNEPPQSLQ 376
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 261-283 3.13e-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: 3.13e-03
                          10        20
                  ....*....|....*....|...
gi 2166948758 261 FECSECGKVFIQKANLVVHQRTH 283
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
50-107 1.00e-30

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 114.23  E-value: 1.00e-30
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2166948758   50 LTFRDVFVDFTLEEWRCLDLAQKNLYRDVMLENYSHLVSVGQLVPKPDVVIRLGQGEE 107
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEE 58
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 49-90 1.69e-23

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: 93.30  E-value: 1.69e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2166948758  49 SLTFRDVFVDFTLEEWRCLDLAQKNLYRDVMLENYSHLVSVG 90
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 50-88 1.34e-18

KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta , KRAB-A interacting protein , and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation.


Pssm-ID: 143639  Cd Length: 40  Bit Score: 79.13  E-value: 1.34e-18
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2166948758  50 LTFRDVFVDFTLEEWRCLDLAQKNLYRDVMLENYSHLVS 88
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
287-612 3.52e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 68.95  E-value: 3.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948758 287 KPYECSECTRAFSQKSTLIAHQRTHTGEKPYECS--ECGKTFIQKSTLMKHTRTHTAEKPFvcgECAKAFKSSYHLTRHE 364
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSD---LNSKSLPLSNSKASSS 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948758 365 K----THIRQAFYEGVHCGKSGLTYPRTHMGEKPNCNKHGKPSDEKPNPIKHQRSP---IKEKAYECSKCGKSFRGKSHL 437
Cdd:COG5048   109 SlsssSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSnslHPPLPANSLSKDPSSNLSLLI 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948758 438 svHQRTHTGEKPYECSICGKTFSGKSHLSVHQRTHTGEKPYECRRCGKAF------GEKSTLVVHHRTHTGEKPYKCGEC 511
Cdd:COG5048   189 --SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpksllsQSPSSLSSSDSSSSASESPRSSLP 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948758 512 GKAFSEKSPLIKHERIHTGER-PYECSNCGKAFSRKSTLIKHQR--IHTGE--KPYECSE--CGKAFSVKSTLIVHHRTH 584
Cdd:COG5048   267 TASSQSSSPNESDSSSEKGFSlPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLH 346

                         330       340       350
                  ....*....|....*....|....*....|
gi 2166948758 585 TGEKPYEC--RDCGKAFSGKSTLIKHQRSH 612
Cdd:COG5048   347 TSISPAKEklLNSSSKFSPLLNNEPPQSLQ 376
zf-H2C2_2 pfam13465
Zinc-finger double domain;
549-572 4.33e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.33e-04
                          10        20
                  ....*....|....*....|....
gi 2166948758 549 LIKHQRIHTGEKPYECSECGKAFS 572
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 261-283 3.13e-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: 3.13e-03
                          10        20
                  ....*....|....*....|...
gi 2166948758 261 FECSECGKVFIQKANLVVHQRTH 283
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
50-107 1.00e-30

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 114.23  E-value: 1.00e-30
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2166948758   50 LTFRDVFVDFTLEEWRCLDLAQKNLYRDVMLENYSHLVSVGQLVPKPDVVIRLGQGEE 107
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEE 58
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 49-90 1.69e-23

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: 93.30  E-value: 1.69e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2166948758  49 SLTFRDVFVDFTLEEWRCLDLAQKNLYRDVMLENYSHLVSVG 90
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 50-88 1.34e-18

KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta , KRAB-A interacting protein , and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation.


Pssm-ID: 143639  Cd Length: 40  Bit Score: 79.13  E-value: 1.34e-18
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2166948758  50 LTFRDVFVDFTLEEWRCLDLAQKNLYRDVMLENYSHLVS 88
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
287-612 3.52e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 68.95  E-value: 3.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948758 287 KPYECSECTRAFSQKSTLIAHQRTHTGEKPYECS--ECGKTFIQKSTLMKHTRTHTAEKPFvcgECAKAFKSSYHLTRHE 364
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSD---LNSKSLPLSNSKASSS 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948758 365 K----THIRQAFYEGVHCGKSGLTYPRTHMGEKPNCNKHGKPSDEKPNPIKHQRSP---IKEKAYECSKCGKSFRGKSHL 437
Cdd:COG5048   109 SlsssSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSnslHPPLPANSLSKDPSSNLSLLI 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948758 438 svHQRTHTGEKPYECSICGKTFSGKSHLSVHQRTHTGEKPYECRRCGKAF------GEKSTLVVHHRTHTGEKPYKCGEC 511
Cdd:COG5048   189 --SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpksllsQSPSSLSSSDSSSSASESPRSSLP 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948758 512 GKAFSEKSPLIKHERIHTGER-PYECSNCGKAFSRKSTLIKHQR--IHTGE--KPYECSE--CGKAFSVKSTLIVHHRTH 584
Cdd:COG5048   267 TASSQSSSPNESDSSSEKGFSlPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLH 346

                         330       340       350
                  ....*....|....*....|....*....|
gi 2166948758 585 TGEKPYEC--RDCGKAFSGKSTLIKHQRSH 612
Cdd:COG5048   347 TSISPAKEklLNSSSKFSPLLNNEPPQSLQ 376
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
259-618 4.70e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 68.57  E-value: 4.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948758 259 KLFECSECGKVFIQKANLVVHQRTHTGEKPYECSECTRAFSQKST--LIAHQRTHTGEKPYECSECGKTFIQKSTLMKHT 336
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPleLSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948758 337 RTHTA----EKPFVCGECAKAFKSSYHLTRHEKTHIRQAFYEGVHCGKSGLTYPRTHMGEKPNCNKHGKPSDEKPNPikH 412
Cdd:COG5048   112 SSSSNsndnNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLI--S 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948758 413 QRSPIKEKAYECSKCGKSFRGKSHLSVHQRTHTGEKPYECSICG----KTFSGKSHLSVHQRTHTGEKPYECRRCGKAFG 488
Cdd:COG5048   190 SNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSqlspKSLLSQSPSSLSSSDSSSSASESPRSSLPTAS 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948758 489 EKSTLVVHH--RTHTG-EKPYKCGECGKAFSEKSPLIKHER--IHTGE--RPYEC--SNCGKAFSRKSTLIKHQRIHTGE 559
Cdd:COG5048   270 SQSSSPNESdsSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSI 349

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2166948758 560 KPYEC--SECGKAFSVKST-----LIVHHRTHTGEKPYEC--RDCGKAFSGKSTLIKHQRSHTGDKTY 618
Cdd:COG5048   350 SPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPY 417
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
384-572 1.15e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 54.70  E-value: 1.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948758 384 TYPRTHMGEKPNCNKHGKPSDEK--PNPIKHQRSPIKEKA--YECSKCGKSFRGKSHLSVHQRT--HTGE--KPYEC--S 453
Cdd:COG5048   248 LSSSDSSSSASESPRSSLPTASSqsSSPNESDSSSEKGFSlpIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCpyS 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948758 454 ICGKTFSGKSHLSVHQRTHTGEKPYEC--RRCGKAFGEKST-----LVVHHRTHTGEKPYKC--GECGKAFSEKSPLIKH 524
Cdd:COG5048   328 LCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLH 407

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2166948758 525 ERIHTGERPYECSN--CGKAFSRKSTLIKHQRIHTGEKPYECSECGKAFS 572
Cdd:COG5048   408 IITHLSFRPYNCKNppCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRR 457
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
287-460 6.70e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.84  E-value: 6.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948758 287 KPYECSECTRAFSQKSTLIAHQRT--HTGE--KPYECSE--CGKTFIQKSTLMKHTRTHTAekpfvcgecakaFKSSYHL 360
Cdd:COG5048   288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTS------------ISPAKEK 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948758 361 TRHEKTHIRQAFYE---GVHCGKSGLTYPRTHMGEKPNCNKhgkPSDEKPNPIKH--QRSPIKEKAYECSKCGKSFRGKS 435
Cdd:COG5048   356 LLNSSSKFSPLLNNeppQSLQQYKDLKNDKKSETLSNSCIR---NFKRDSNLSLHiiTHLSFRPYNCKNPPCSKSFNRHY 432

                         170       180
                  ....*....|....*....|....*
gi 2166948758 436 HLSVHQRTHTGEKPYECSICGKTFS 460
Cdd:COG5048   433 NLIPHKKIHTNHAPLLCSILKSFRR 457
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
405-480 4.16e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.15  E-value: 4.16e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2166948758 405 EKPNPIKHQRSPIKEKAYECSKCGKSFRGKSHLSVHQRTHTGEKPYECS--ICGKTFSGKSHLSVHQRTHTGEKPYEC 480
Cdd:COG5048    17 SSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLN 94
zf-H2C2_2 pfam13465
Zinc-finger double domain;
549-572 4.33e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.33e-04
                          10        20
                  ....*....|....*....|....
gi 2166948758 549 LIKHQRIHTGEKPYECSECGKAFS 572
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
436-460 4.92e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.92e-04
                          10        20
                  ....*....|....*....|....*
gi 2166948758 436 HLSVHQRTHTGEKPYECSICGKTFS 460
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
275-300 4.97e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.97e-04
                          10        20
                  ....*....|....*....|....*.
gi 2166948758 275 NLVVHQRTHTGEKPYECSECTRAFSQ 300
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
521-545 6.94e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 6.94e-04
                          10        20
                  ....*....|....*....|....*
gi 2166948758 521 LIKHERIHTGERPYECSNCGKAFSR 545
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
307-328 1.01e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.01e-03
                          10        20
                  ....*....|....*....|..
gi 2166948758 307 HQRTHTGEKPYECSECGKTFIQ 328
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 534-556 1.02e-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: 36.51  E-value: 1.02e-03
                          10        20
                  ....*....|....*....|...
gi 2166948758 534 YECSNCGKAFSRKSTLIKHQRIH 556
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
464-487 1.38e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.38e-03
                          10        20
                  ....*....|....*....|....
gi 2166948758 464 HLSVHQRTHTGEKPYECRRCGKAF 487
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 317-339 1.46e-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: 1.46e-03
                          10        20
                  ....*....|....*....|...
gi 2166948758 317 YECSECGKTFIQKSTLMKHTRTH 339
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 450-472 1.47e-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: 1.47e-03
                          10        20
                  ....*....|....*....|...
gi 2166948758 450 YECSICGKTFSGKSHLSVHQRTH 472
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 342-445 1.62e-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: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948758 342 EKPFVCG--ECAKAFKSSYHLTRHEKthirqafyEGvHCGksgltyPRTHmgekpncnkhgkpsdEKPNPIKHQRSPIKE 419
Cdd:COG5189   347 GKPYKCPveGCNKKYKNQNGLKYHML--------HG-HQN------QKLH---------------ENPSPEKMNIFSAKD 396

                          90       100
                  ....*....|....*....|....*.
gi 2166948758 420 KAYECSKCGKSFRGKSHLSVHqRTHT 445
Cdd:COG5189   397 KPYRCEVCDKRYKNLNGLKYH-RKHS 421
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 422-444 1.83e-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: 1.83e-03
                          10        20
                  ....*....|....*....|...
gi 2166948758 422 YECSKCGKSFRGKSHLSVHQRTH 444
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
493-516 1.93e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 1.93e-03
                          10        20
                  ....*....|....*....|....
gi 2166948758 493 LVVHHRTHTGEKPYKCGECGKAFS 516
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
577-600 3.06e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.06e-03
                          10        20
                  ....*....|....*....|....
gi 2166948758 577 LIVHHRTHTGEKPYECRDCGKAFS 600
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 261-283 3.13e-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: 3.13e-03
                          10        20
                  ....*....|....*....|...
gi 2166948758 261 FECSECGKVFIQKANLVVHQRTH 283
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 502-585 3.61e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.09  E-value: 3.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948758 502 GEKPYKCG--ECGKAFSEKSPLiKHERIHtgerpyecSNCGKAFSRKSTLIKHQRIHTGEKPYECSECGKAFSVKSTLiV 579
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGL-KYHMLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGL-K 415


                  ....*.
gi 2166948758 580 HHRTHT 585
Cdd:COG5189   416 YHRKHS 421
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 590-612 6.48e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.58  E-value: 6.48e-03
                          10        20
                  ....*....|....*....|...
gi 2166948758 590 YECRDCGKAFSGKSTLIKHQRSH 612
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 289-311 7.58e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.20  E-value: 7.58e-03
                          10        20
                  ....*....|....*....|...
gi 2166948758 289 YECSECTRAFSQKSTLIAHQRTH 311
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 562-584 7.81e-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: 7.81e-03
                          10        20
                  ....*....|....*....|...
gi 2166948758 562 YECSECGKAFSVKSTLIVHHRTH 584
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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