NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|38569445|ref|NP_006376|]
View 

zinc finger protein 211 isoform 1 [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 1.26e-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: 1.26e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 38569445    45 SVTFEDVAVYFSWEEWDLLDEAQKHLYFDVMLENFALTSSLG 86
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
192-563 4.90e-09

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.94  E-value: 4.90e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569445 192 HVSEKPFTCREIRKDFLANMR-FLHQDATQTGEKPNN-SNKCAVAFYSGKSHHNWGKCSKAFSHIDTLVQD---QRILTR 266
Cdd:COG5048  56 HTGEKPSQCSYSGCDKSFSRPlELSRHLRTHHNNPSDlNSKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHslpPSSRDP 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569445 267 EGLFECSKC--GKACTRRCNLIQHQKVHSEERPYEC--NECGKFFTYYSSFIIHQRVHTGERPYACPECGKSFSQIYSLN 342
Cdd:COG5048 136 QLPDLLSISnlRNNPLPGNNSSSVNTPQSNSLHPPLpaNSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSS 215
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569445 343 SHRKVHTGERPYECGECGKSFSQRSNLMQHRRVHTGERPYECSECGKSFSQNFSLIYHQRVHTGERPHE-------CNEC 415
Cdd:COG5048 216 SDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKgfslpikSKQC 295
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569445 416 GKSFSRSSSLIHHRRLhtgerpyecskcgksfkqsssfsshrKVHTGE--RPYVCGE--CGKSFSHSSNLKNHQRVHTGE 491
Cdd:COG5048 296 NISFSRSSPLTRHLRS--------------------------VNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSI 349
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569445 492 RPVEC-------------------------------------SECSKSFSCKSNLIKHLRVHTGERPYEC--SECGKSFS 532
Cdd:COG5048 350 SPAKEkllnssskfspllnneppqslqqykdlkndkksetlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFN 429
                       410       420       430
                ....*....|....*....|....*....|.
gi 38569445 533 QSSSLIQHRRVHTGKRPYQCSQCGKSFGCKS 563
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 1.26e-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: 1.26e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 38569445    45 SVTFEDVAVYFSWEEWDLLDEAQKHLYFDVMLENFALTSSLG 86
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
46-87 1.36e-18

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 79.56  E-value: 1.36e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 38569445     46 VTFEDVAVYFSWEEWDLLDEAQKHLYFDVMLENFALTSSLGC 87
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGF 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
46-85 2.74e-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: 2.74e-17
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 38569445  46 VTFEDVAVYFSWEEWDLLDEAQKHLYFDVMLENFALTSSL 85
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
192-563 4.90e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.94  E-value: 4.90e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569445 192 HVSEKPFTCREIRKDFLANMR-FLHQDATQTGEKPNN-SNKCAVAFYSGKSHHNWGKCSKAFSHIDTLVQD---QRILTR 266
Cdd:COG5048  56 HTGEKPSQCSYSGCDKSFSRPlELSRHLRTHHNNPSDlNSKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHslpPSSRDP 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569445 267 EGLFECSKC--GKACTRRCNLIQHQKVHSEERPYEC--NECGKFFTYYSSFIIHQRVHTGERPYACPECGKSFSQIYSLN 342
Cdd:COG5048 136 QLPDLLSISnlRNNPLPGNNSSSVNTPQSNSLHPPLpaNSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSS 215
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569445 343 SHRKVHTGERPYECGECGKSFSQRSNLMQHRRVHTGERPYECSECGKSFSQNFSLIYHQRVHTGERPHE-------CNEC 415
Cdd:COG5048 216 SDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKgfslpikSKQC 295
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569445 416 GKSFSRSSSLIHHRRLhtgerpyecskcgksfkqsssfsshrKVHTGE--RPYVCGE--CGKSFSHSSNLKNHQRVHTGE 491
Cdd:COG5048 296 NISFSRSSPLTRHLRS--------------------------VNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSI 349
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569445 492 RPVEC-------------------------------------SECSKSFSCKSNLIKHLRVHTGERPYEC--SECGKSFS 532
Cdd:COG5048 350 SPAKEkllnssskfspllnneppqslqqykdlkndkksetlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFN 429
                       410       420       430
                ....*....|....*....|....*....|.
gi 38569445 533 QSSSLIQHRRVHTGKRPYQCSQCGKSFGCKS 563
Cdd:COG5048 430 RHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
zf-H2C2_2 pfam13465
Zinc-finger double domain;
368-393 9.21e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 9.21e-05
                          10        20
                  ....*....|....*....|....*.
gi 38569445   368 NLMQHRRVHTGERPYECSECGKSFSQ 393
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 1.26e-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: 1.26e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 38569445    45 SVTFEDVAVYFSWEEWDLLDEAQKHLYFDVMLENFALTSSLG 86
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
46-87 1.36e-18

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 79.56  E-value: 1.36e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 38569445     46 VTFEDVAVYFSWEEWDLLDEAQKHLYFDVMLENFALTSSLGC 87
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGF 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
46-85 2.74e-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: 2.74e-17
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 38569445  46 VTFEDVAVYFSWEEWDLLDEAQKHLYFDVMLENFALTSSL 85
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
192-563 4.90e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.94  E-value: 4.90e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569445 192 HVSEKPFTCREIRKDFLANMR-FLHQDATQTGEKPNN-SNKCAVAFYSGKSHHNWGKCSKAFSHIDTLVQD---QRILTR 266
Cdd:COG5048  56 HTGEKPSQCSYSGCDKSFSRPlELSRHLRTHHNNPSDlNSKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHslpPSSRDP 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569445 267 EGLFECSKC--GKACTRRCNLIQHQKVHSEERPYEC--NECGKFFTYYSSFIIHQRVHTGERPYACPECGKSFSQIYSLN 342
Cdd:COG5048 136 QLPDLLSISnlRNNPLPGNNSSSVNTPQSNSLHPPLpaNSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSS 215
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569445 343 SHRKVHTGERPYECGECGKSFSQRSNLMQHRRVHTGERPYECSECGKSFSQNFSLIYHQRVHTGERPHE-------CNEC 415
Cdd:COG5048 216 SDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKgfslpikSKQC 295
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569445 416 GKSFSRSSSLIHHRRLhtgerpyecskcgksfkqsssfsshrKVHTGE--RPYVCGE--CGKSFSHSSNLKNHQRVHTGE 491
Cdd:COG5048 296 NISFSRSSPLTRHLRS--------------------------VNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSI 349
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569445 492 RPVEC-------------------------------------SECSKSFSCKSNLIKHLRVHTGERPYEC--SECGKSFS 532
Cdd:COG5048 350 SPAKEkllnssskfspllnneppqslqqykdlkndkksetlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFN 429
                       410       420       430
                ....*....|....*....|....*....|.
gi 38569445 533 QSSSLIQHRRVHTGKRPYQCSQCGKSFGCKS 563
Cdd:COG5048 430 RHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
246-560 6.26e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.09  E-value: 6.26e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569445 246 KCSKAFSHIDTLVQDQRILTREGLFECSK--CGKACTRRCNLIQHQKVHSEERPYECNECGKFFTYYSSFIIHQRVHTGE 323
Cdd:COG5048  38 NCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLSSSSSNS 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569445 324 -RPYACPECGKSFSQIYSLNSHRKVHTGERPYECGECGKSFSQRSN----LMQHRRVHTGERPYEcsecgksfsqNFSLI 398
Cdd:COG5048 118 nDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQsnslHPPLPANSLSKDPSS----------NLSLL 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569445 399 YHQRVHTGERPHECNECGKSFSRSSSLIHHRRLHTGERPYECSKCGKSFKQSSSFSSHRKVHTGERPYVCGECGKSFSHS 478
Cdd:COG5048 188 ISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPT 267
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569445 479 SNLKNHQRVHTGERPVE-------CSECSKSFSCKSNLIKHLR--VHTGE--RPYECSE--CGKSFSQSSSLIQHRRVHT 545
Cdd:COG5048 268 ASSQSSSPNESDSSSEKgfslpikSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHT 347
                       330
                ....*....|....*..
gi 38569445 546 GKRPYQC--SQCGKSFG 560
Cdd:COG5048 348 SISPAKEklLNSSSKFS 364
zf-H2C2_2 pfam13465
Zinc-finger double domain;
368-393 9.21e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 9.21e-05
                          10        20
                  ....*....|....*....|....*.
gi 38569445   368 NLMQHRRVHTGERPYECSECGKSFSQ 393
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
380-558 1.11e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.07  E-value: 1.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569445 380 RPYECSECGKSFSQNFSLIYHQRVHTGERPHECN--ECGKSFSRSSSLIHHRRLHTGERPYECSKCGKSFKQSSSFSSHR 457
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLS 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569445 458 KVHTgERPYVCGECGKSFSHSSNLKNHQ--RVHTGERPVECSECSKSFSC--KSNLIKH-LRVHtgerpyecSECGKSFS 532
Cdd:COG5048 112 SSSS-NSNDNNLLSSHSLPPSSRDPQLPdlLSISNLRNNPLPGNNSSSVNtpQSNSLHPpLPAN--------SLSKDPSS 182
                       170       180
                ....*....|....*....|....*.
gi 38569445 533 QSSSLIQHRRVHTGKRPYQCSQCGKS 558
Cdd:COG5048 183 NLSLLISSNVSTSIPSSSENSPLSSS 208
zf-H2C2_2 pfam13465
Zinc-finger double domain;
508-533 2.63e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.63e-04
                          10        20
                  ....*....|....*....|....*.
gi 38569445   508 NLIKHLRVHTGERPYECSECGKSFSQ 533
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
322-405 5.47e-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: 5.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569445 322 GERPYACP--ECGKSFSQIYSLNSHRKvHtgerpyecGECGKSFSQRSNLMQHRRVHTGERPYECSECGKSFSQNFSLIY 399
Cdd:COG5189 346 DGKPYKCPveGCNKKYKNQNGLKYHML-H--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416

                ....*.
gi 38569445 400 HqRVHT 405
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 ...
466-488 8.27e-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: 36.89  E-value: 8.27e-04
                          10        20
                  ....*....|....*....|...
gi 38569445   466 YVCGECGKSFSHSSNLKNHQRVH 488
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
480-505 8.63e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 8.63e-04
                          10        20
                  ....*....|....*....|....*.
gi 38569445   480 NLKNHQRVHTGERPVECSECSKSFSC 505
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
396-421 1.30e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.30e-03
                          10        20
                  ....*....|....*....|....*.
gi 38569445   396 SLIYHQRVHTGERPHECNECGKSFSR 421
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
316-337 1.34e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.34e-03
                          10        20
                  ....*....|....*....|..
gi 38569445   316 HQRVHTGERPYACPECGKSFSQ 337
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
340-365 1.80e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 1.80e-03
                          10        20
                  ....*....|....*....|....*.
gi 38569445   340 SLNSHRKVHTGERPYECGECGKSFSQ 365
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
354-376 2.48e-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: 35.35  E-value: 2.48e-03
                          10        20
                  ....*....|....*....|...
gi 38569445   354 YECGECGKSFSQRSNLMQHRRVH 376
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
522-544 3.05e-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: 3.05e-03
                          10        20
                  ....*....|....*....|...
gi 38569445   522 YECSECGKSFSQSSSLIQHRRVH 544
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
410-432 3.20e-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: 35.35  E-value: 3.20e-03
                          10        20
                  ....*....|....*....|...
gi 38569445   410 HECNECGKSFSRSSSLIHHRRLH 432
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
536-559 4.11e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.11e-03
                          10        20
                  ....*....|....*....|....
gi 38569445   536 SLIQHRRVHTGKRPYQCSQCGKSF 559
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
 
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