NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|388240790|ref|NP_001252526|]
View 

zinc finger protein 211 isoform 3 [Homo sapiens]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 45-86 1.38e-21

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: 87.91  E-value: 1.38e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 388240790   45 SVTFEDVAVYFSWEEWDLLDEAQKHLYFDVMLENFALTSSLG 86
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
244-615 7.86e-10

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 61.64  E-value: 7.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240790 244 HVSEKPFTCREIRKDFLANMR-FLHQDATQTGEKPNNSN-KCAVAFYSGKSHHNWGKCSKAFSHIDTLVQD---QRILTR 318
Cdd:COG5048   56 HTGEKPSQCSYSGCDKSFSRPlELSRHLRTHHNNPSDLNsKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHslpPSSRDP 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240790 319 EGLFECSKC--GKACTRRCNLIQHQKVHSEERPYEC--NECGKFFTYYSSFIIHQRVHTGERPYACPECGKSFSQIYSLN 394
Cdd:COG5048  136 QLPDLLSISnlRNNPLPGNNSSSVNTPQSNSLHPPLpaNSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSS 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240790 395 SHRKVHTGERPYECGECGKSFSQRSNLMQHRRVHTGERPYECSECGKSFSQNFSLIYHQRVHTGERPHE-------CNEC 467
Cdd:COG5048  216 SDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKgfslpikSKQC 295

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240790 468 GKSFSRSSSLIHHRRLhtgerpyecskcgksfkqsssfsshrKVHTGE--RPYVCGE--CGKSFSHSSNLKNHQRVHTGE 543
Cdd:COG5048  296 NISFSRSSPLTRHLRS--------------------------VNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSI 349

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240790 544 RPVEC-------------------------------------SECSKSFSCKSNLIKHLRVHTGERPYEC--SECGKSFS 584
Cdd:COG5048  350 SPAKEkllnssskfspllnneppqslqqykdlkndkksetlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFN 429

                        410       420       430
                 ....*....|....*....|....*....|.
gi 388240790 585 QSSSLIQHRRVHTGKRPYQCSQCGKSFGCKS 615
Cdd:COG5048  430 RHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
 
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 ...
 45-86 1.38e-21

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: 87.91  E-value: 1.38e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 388240790   45 SVTFEDVAVYFSWEEWDLLDEAQKHLYFDVMLENFALTSSLG 86
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
46-106 1.72e-19

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 82.26  E-value: 1.72e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 388240790    46 VTFEDVAVYFSWEEWDLLDEAQKHLYFDVMLENFALTSSLGLISSWSHVVAQLGLGEVPSV 106
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 46-85 2.98e-17

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: 75.28  E-value: 2.98e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 388240790  46 VTFEDVAVYFSWEEWDLLDEAQKHLYFDVMLENFALTSSL 85
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
244-615 7.86e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 61.64  E-value: 7.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240790 244 HVSEKPFTCREIRKDFLANMR-FLHQDATQTGEKPNNSN-KCAVAFYSGKSHHNWGKCSKAFSHIDTLVQD---QRILTR 318
Cdd:COG5048   56 HTGEKPSQCSYSGCDKSFSRPlELSRHLRTHHNNPSDLNsKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHslpPSSRDP 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240790 319 EGLFECSKC--GKACTRRCNLIQHQKVHSEERPYEC--NECGKFFTYYSSFIIHQRVHTGERPYACPECGKSFSQIYSLN 394
Cdd:COG5048  136 QLPDLLSISnlRNNPLPGNNSSSVNTPQSNSLHPPLpaNSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSS 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240790 395 SHRKVHTGERPYECGECGKSFSQRSNLMQHRRVHTGERPYECSECGKSFSQNFSLIYHQRVHTGERPHE-------CNEC 467
Cdd:COG5048  216 SDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKgfslpikSKQC 295

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240790 468 GKSFSRSSSLIHHRRLhtgerpyecskcgksfkqsssfsshrKVHTGE--RPYVCGE--CGKSFSHSSNLKNHQRVHTGE 543
Cdd:COG5048  296 NISFSRSSPLTRHLRS--------------------------VNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSI 349

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240790 544 RPVEC-------------------------------------SECSKSFSCKSNLIKHLRVHTGERPYEC--SECGKSFS 584
Cdd:COG5048  350 SPAKEkllnssskfspllnneppqslqqykdlkndkksetlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFN 429

                        410       420       430
                 ....*....|....*....|....*....|.
gi 388240790 585 QSSSLIQHRRVHTGKRPYQCSQCGKSFGCKS 615
Cdd:COG5048  430 RHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
zf-H2C2_2 pfam13465
Zinc-finger double domain;
420-445 6.14e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 6.14e-05
                          10        20
                  ....*....|....*....|....*.
gi 388240790  420 NLMQHRRVHTGERPYECSECGKSFSQ 445
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
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 ...
 45-86 1.38e-21

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: 87.91  E-value: 1.38e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 388240790   45 SVTFEDVAVYFSWEEWDLLDEAQKHLYFDVMLENFALTSSLG 86
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
46-106 1.72e-19

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 82.26  E-value: 1.72e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 388240790    46 VTFEDVAVYFSWEEWDLLDEAQKHLYFDVMLENFALTSSLGLISSWSHVVAQLGLGEVPSV 106
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 46-85 2.98e-17

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: 75.28  E-value: 2.98e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 388240790  46 VTFEDVAVYFSWEEWDLLDEAQKHLYFDVMLENFALTSSL 85
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
244-615 7.86e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 61.64  E-value: 7.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240790 244 HVSEKPFTCREIRKDFLANMR-FLHQDATQTGEKPNNSN-KCAVAFYSGKSHHNWGKCSKAFSHIDTLVQD---QRILTR 318
Cdd:COG5048   56 HTGEKPSQCSYSGCDKSFSRPlELSRHLRTHHNNPSDLNsKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHslpPSSRDP 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240790 319 EGLFECSKC--GKACTRRCNLIQHQKVHSEERPYEC--NECGKFFTYYSSFIIHQRVHTGERPYACPECGKSFSQIYSLN 394
Cdd:COG5048  136 QLPDLLSISnlRNNPLPGNNSSSVNTPQSNSLHPPLpaNSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSS 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240790 395 SHRKVHTGERPYECGECGKSFSQRSNLMQHRRVHTGERPYECSECGKSFSQNFSLIYHQRVHTGERPHE-------CNEC 467
Cdd:COG5048  216 SDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKgfslpikSKQC 295

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240790 468 GKSFSRSSSLIHHRRLhtgerpyecskcgksfkqsssfsshrKVHTGE--RPYVCGE--CGKSFSHSSNLKNHQRVHTGE 543
Cdd:COG5048  296 NISFSRSSPLTRHLRS--------------------------VNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSI 349

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240790 544 RPVEC-------------------------------------SECSKSFSCKSNLIKHLRVHTGERPYEC--SECGKSFS 584
Cdd:COG5048  350 SPAKEkllnssskfspllnneppqslqqykdlkndkksetlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFN 429

                        410       420       430
                 ....*....|....*....|....*....|.
gi 388240790 585 QSSSLIQHRRVHTGKRPYQCSQCGKSFGCKS 615
Cdd:COG5048  430 RHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
298-612 1.71e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 57.40  E-value: 1.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240790 298 KCSKAFSHIDTLVQDQRILTREGLFECSK--CGKACTRRCNLIQHQKVHSEERPYECNECGKFFTYYSSFIIHQRVHTGE 375
Cdd:COG5048   38 NCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLSSSSSNS 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240790 376 -RPYACPECGKSFSQIYSLNSHRKVHTGERPYECGECGKSFSQRSN----LMQHRRVHTGERPYEcsecgksfsqNFSLI 450
Cdd:COG5048  118 nDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQsnslHPPLPANSLSKDPSS----------NLSLL 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240790 451 YHQRVHTGERPHECNECGKSFSRSSSLIHHRRLHTGERPYECSKCGKSFKQSSSFSSHRKVHTGERPYVCGECGKSFSHS 530
Cdd:COG5048  188 ISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPT 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240790 531 SNLKNHQRVHTGERPVE-------CSECSKSFSCKSNLIKHLR--VHTGE--RPYECSE--CGKSFSQSSSLIQHRRVHT 597
Cdd:COG5048  268 ASSQSSSPNESDSSSEKgfslpikSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHT 347

                        330
                 ....*....|....*..
gi 388240790 598 GKRPYQC--SQCGKSFG 612
Cdd:COG5048  348 SISPAKEklLNSSSKFS 364
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
432-610 4.98e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 46.23  E-value: 4.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240790 432 RPYECSECGKSFSQNFSLIYHQRVHTGERPHECN--ECGKSFSRSSSLIHHRRLHTGERPYECSKCGKSFKQSSSFSSHR 509
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240790 510 KVHTgERPYVCGECGKSFSHSSNLKNHQ--RVHTGERPVECSECSKSFSC--KSNLIKH-LRVHtgerpyecSECGKSFS 584
Cdd:COG5048  112 SSSS-NSNDNNLLSSHSLPPSSRDPQLPdlLSISNLRNNPLPGNNSSSVNtpQSNSLHPpLPAN--------SLSKDPSS 182

                        170       180
                 ....*....|....*....|....*.
gi 388240790 585 QSSSLIQHRRVHTGKRPYQCSQCGKS 610
Cdd:COG5048  183 NLSLLISSNVSTSIPSSSENSPLSSS 208
zf-H2C2_2 pfam13465
Zinc-finger double domain;
420-445 6.14e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 6.14e-05
                          10        20
                  ....*....|....*....|....*.
gi 388240790  420 NLMQHRRVHTGERPYECSECGKSFSQ 445
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
560-585 1.79e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.79e-04
                          10        20
                  ....*....|....*....|....*.
gi 388240790  560 NLIKHLRVHTGERPYECSECGKSFSQ 585
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 374-457 5.34e-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: 5.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240790 374 GERPYACP--ECGKSFSQIYSLNSHRKvHtgerpyecGECGKSFSQRSNLMQHRRVHTGERPYECSECGKSFSQNFSLIY 451
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLKYHML-H--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                 ....*.
gi 388240790 452 HqRVHT 457
Cdd:COG5189  417 H-RKHS 421
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 518-540 5.62e-04

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 37.28  E-value: 5.62e-04
                          10        20
                  ....*....|....*....|...
gi 388240790  518 YVCGECGKSFSHSSNLKNHQRVH 540
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
532-557 5.98e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 5.98e-04
                          10        20
                  ....*....|....*....|....*.
gi 388240790  532 NLKNHQRVHTGERPVECSECSKSFSC 557
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
448-473 9.11e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 9.11e-04
                          10        20
                  ....*....|....*....|....*.
gi 388240790  448 SLIYHQRVHTGERPHECNECGKSFSR 473
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
368-389 9.39e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 9.39e-04
                          10        20
                  ....*....|....*....|..
gi 388240790  368 HQRVHTGERPYACPECGKSFSQ 389
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
392-417 1.25e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.25e-03
                          10        20
                  ....*....|....*....|....*.
gi 388240790  392 SLNSHRKVHTGERPYECGECGKSFSQ 417
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 406-428 1.69e-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: 36.12  E-value: 1.69e-03
                          10        20
                  ....*....|....*....|...
gi 388240790  406 YECGECGKSFSQRSNLMQHRRVH 428
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 574-596 2.07e-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: 35.74  E-value: 2.07e-03
                          10        20
                  ....*....|....*....|...
gi 388240790  574 YECSECGKSFSQSSSLIQHRRVH 596
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 462-484 2.20e-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: 35.74  E-value: 2.20e-03
                          10        20
                  ....*....|....*....|...
gi 388240790  462 HECNECGKSFSRSSSLIHHRRLH 484
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
588-611 2.90e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 2.90e-03
                          10        20
                  ....*....|....*....|....
gi 388240790  588 SLIQHRRVHTGKRPYQCSQCGKSF 611
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
336-361 7.39e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 7.39e-03
                          10        20
                  ....*....|....*....|....*.
gi 388240790  336 NLIQHQKVHSEERPYECNECGKFFTY 361
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 434-456 9.58e-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: 33.81  E-value: 9.58e-03
                          10        20
                  ....*....|....*....|...
gi 388240790  434 YECSECGKSFSQNFSLIYHQRVH 456
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH