NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|38569447|ref|NP_942152|]
View 

zinc finger protein 211 isoform 2 [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 ...
 32-73 1.22e-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: 1.22e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 38569447    32 SVTFEDVAVYFSWEEWDLLDEAQKHLYFDVMLENFALTSSLG 73
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
179-550 1.17e-08

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 57.40  E-value: 1.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569447 179 HVSEKPFTCREIRKDFLANMR-FLHQDATQTGEKPNNSN-KCAVAFYSGKSHHNWGKCSKAFSHIDTLVQD---QRILTR 253
Cdd:COG5048  56 HTGEKPSQCSYSGCDKSFSRPlELSRHLRTHHNNPSDLNsKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHslpPSSRDP 135

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569447 254 EGLFECSKC--GKACTRRCNLIQHQKVHSEERPYEC--NECGKFFTYYSSFIIHQRVHTGERPYACPECGKSFSQIYSLN 329
Cdd:COG5048 136 QLPDLLSISnlRNNPLPGNNSSSVNTPQSNSLHPPLpaNSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSS 215

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569447 330 SHRKVHTGERPYECGECGKSFSQRSNLMQHRRVHTGERPYECSECGKSFSQNFSLIYHQRVHTGERPHE-------CNEC 402
Cdd:COG5048 216 SDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKgfslpikSKQC 295

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569447 403 GKSFSRSSSLIHHRRLhtgerpyecskcgksfkqsssfsshrKVHTGE--RPYVCGE--CGKSFSHSSNLKNHQRVHTGE 478
Cdd:COG5048 296 NISFSRSSPLTRHLRS--------------------------VNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSI 349

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569447 479 RPVEC-------------------------------------SECSKSFSCKSNLIKHLRVHTGERPYEC--SECGKSFS 519
Cdd:COG5048 350 SPAKEkllnssskfspllnneppqslqqykdlkndkksetlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFN 429

                       410       420       430
                ....*....|....*....|....*....|.
gi 38569447 520 QSSSLIQHRRVHTGKRPYQCSQCGKSFGCKS 550
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 ...
 32-73 1.22e-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: 1.22e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 38569447    32 SVTFEDVAVYFSWEEWDLLDEAQKHLYFDVMLENFALTSSLG 73
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
33-74 1.32e-18

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 79.56  E-value: 1.32e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 38569447     33 VTFEDVAVYFSWEEWDLLDEAQKHLYFDVMLENFALTSSLGC 74
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGF 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 33-72 2.68e-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: 2.68e-17
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 38569447  33 VTFEDVAVYFSWEEWDLLDEAQKHLYFDVMLENFALTSSL 72
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
179-550 1.17e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 57.40  E-value: 1.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569447 179 HVSEKPFTCREIRKDFLANMR-FLHQDATQTGEKPNNSN-KCAVAFYSGKSHHNWGKCSKAFSHIDTLVQD---QRILTR 253
Cdd:COG5048  56 HTGEKPSQCSYSGCDKSFSRPlELSRHLRTHHNNPSDLNsKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHslpPSSRDP 135

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569447 254 EGLFECSKC--GKACTRRCNLIQHQKVHSEERPYEC--NECGKFFTYYSSFIIHQRVHTGERPYACPECGKSFSQIYSLN 329
Cdd:COG5048 136 QLPDLLSISnlRNNPLPGNNSSSVNTPQSNSLHPPLpaNSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSS 215

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569447 330 SHRKVHTGERPYECGECGKSFSQRSNLMQHRRVHTGERPYECSECGKSFSQNFSLIYHQRVHTGERPHE-------CNEC 402
Cdd:COG5048 216 SDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKgfslpikSKQC 295

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569447 403 GKSFSRSSSLIHHRRLhtgerpyecskcgksfkqsssfsshrKVHTGE--RPYVCGE--CGKSFSHSSNLKNHQRVHTGE 478
Cdd:COG5048 296 NISFSRSSPLTRHLRS--------------------------VNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSI 349

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569447 479 RPVEC-------------------------------------SECSKSFSCKSNLIKHLRVHTGERPYEC--SECGKSFS 519
Cdd:COG5048 350 SPAKEkllnssskfspllnneppqslqqykdlkndkksetlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFN 429

                       410       420       430
                ....*....|....*....|....*....|.
gi 38569447 520 QSSSLIQHRRVHTGKRPYQCSQCGKSFGCKS 550
Cdd:COG5048 430 RHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
zf-H2C2_2 pfam13465
Zinc-finger double domain;
355-380 1.10e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.10e-04
                          10        20
                  ....*....|....*....|....*.
gi 38569447   355 NLMQHRRVHTGERPYECSECGKSFSQ 380
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 ...
 32-73 1.22e-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: 1.22e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 38569447    32 SVTFEDVAVYFSWEEWDLLDEAQKHLYFDVMLENFALTSSLG 73
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
33-74 1.32e-18

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 79.56  E-value: 1.32e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 38569447     33 VTFEDVAVYFSWEEWDLLDEAQKHLYFDVMLENFALTSSLGC 74
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGF 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 33-72 2.68e-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: 2.68e-17
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 38569447  33 VTFEDVAVYFSWEEWDLLDEAQKHLYFDVMLENFALTSSL 72
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
179-550 1.17e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 57.40  E-value: 1.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569447 179 HVSEKPFTCREIRKDFLANMR-FLHQDATQTGEKPNNSN-KCAVAFYSGKSHHNWGKCSKAFSHIDTLVQD---QRILTR 253
Cdd:COG5048  56 HTGEKPSQCSYSGCDKSFSRPlELSRHLRTHHNNPSDLNsKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHslpPSSRDP 135

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569447 254 EGLFECSKC--GKACTRRCNLIQHQKVHSEERPYEC--NECGKFFTYYSSFIIHQRVHTGERPYACPECGKSFSQIYSLN 329
Cdd:COG5048 136 QLPDLLSISnlRNNPLPGNNSSSVNTPQSNSLHPPLpaNSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSS 215

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569447 330 SHRKVHTGERPYECGECGKSFSQRSNLMQHRRVHTGERPYECSECGKSFSQNFSLIYHQRVHTGERPHE-------CNEC 402
Cdd:COG5048 216 SDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKgfslpikSKQC 295

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569447 403 GKSFSRSSSLIHHRRLhtgerpyecskcgksfkqsssfsshrKVHTGE--RPYVCGE--CGKSFSHSSNLKNHQRVHTGE 478
Cdd:COG5048 296 NISFSRSSPLTRHLRS--------------------------VNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSI 349

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569447 479 RPVEC-------------------------------------SECSKSFSCKSNLIKHLRVHTGERPYEC--SECGKSFS 519
Cdd:COG5048 350 SPAKEkllnssskfspllnneppqslqqykdlkndkksetlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFN 429

                       410       420       430
                ....*....|....*....|....*....|.
gi 38569447 520 QSSSLIQHRRVHTGKRPYQCSQCGKSFGCKS 550
Cdd:COG5048 430 RHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
233-547 1.18e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 54.32  E-value: 1.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569447 233 KCSKAFSHIDTLVQDQRILTREGLFECSK--CGKACTRRCNLIQHQKVHSEERPYECNECGKFFTYYSSFIIHQRVHTGE 310
Cdd:COG5048  38 NCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLSSSSSNS 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569447 311 -RPYACPECGKSFSQIYSLNSHRKVHTGERPYECGECGKSFSQRSN----LMQHRRVHTGERPYEcsecgksfsqNFSLI 385
Cdd:COG5048 118 nDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQsnslHPPLPANSLSKDPSS----------NLSLL 187

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569447 386 YHQRVHTGERPHECNECGKSFSRSSSLIHHRRLHTGERPYECSKCGKSFKQSSSFSSHRKVHTGERPYVCGECGKSFSHS 465
Cdd:COG5048 188 ISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPT 267

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569447 466 SNLKNHQRVHTGERPVE-------CSECSKSFSCKSNLIKHLR--VHTGE--RPYECSE--CGKSFSQSSSLIQHRRVHT 532
Cdd:COG5048 268 ASSQSSSPNESDSSSEKgfslpikSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHT 347

                       330
                ....*....|....*..
gi 38569447 533 GKRPYQC--SQCGKSFG 547
Cdd:COG5048 348 SISPAKEklLNSSSKFS 364
zf-H2C2_2 pfam13465
Zinc-finger double domain;
355-380 1.10e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.10e-04
                          10        20
                  ....*....|....*....|....*.
gi 38569447   355 NLMQHRRVHTGERPYECSECGKSFSQ 380
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
367-431 1.60e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.30  E-value: 1.60e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38569447 367 RPYECSECGKSFSQNFSLIYHQRVHTGERPHECN--ECGKSFSRSSSLIHHRRLHTGERPYECSKCG 431
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSL 98
zf-H2C2_2 pfam13465
Zinc-finger double domain;
495-520 3.10e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.10e-04
                          10        20
                  ....*....|....*....|....*.
gi 38569447   495 NLIKHLRVHTGERPYECSECGKSFSQ 520
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
479-545 5.11e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.76  E-value: 5.11e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38569447 479 RPVECSECSKSFSCKSNLIKHLRVHTGERPYECS--ECGKSFSQSSSLIQHRRVHTGKRPYQCSQCGKS 545
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPL 100
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 309-392 6.42e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 42.40  E-value: 6.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569447 309 GERPYACP--ECGKSFSQIYSLNSHRKvHtgerpyecGECGKSFSQRSNLMQHRRVHTGERPYECSECGKSFSQNFSLIY 386
Cdd:COG5189 346 DGKPYKCPveGCNKKYKNQNGLKYHML-H--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                ....*.
gi 38569447 387 HqRVHT 392
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 ...
 453-475 9.84e-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: 36.51  E-value: 9.84e-04
                          10        20
                  ....*....|....*....|...
gi 38569447   453 YVCGECGKSFSHSSNLKNHQRVH 475
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
467-492 1.03e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.03e-03
                          10        20
                  ....*....|....*....|....*.
gi 38569447   467 NLKNHQRVHTGERPVECSECSKSFSC 492
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
383-408 1.51e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.51e-03
                          10        20
                  ....*....|....*....|....*.
gi 38569447   383 SLIYHQRVHTGERPHECNECGKSFSR 408
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
303-324 1.55e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.55e-03
                          10        20
                  ....*....|....*....|..
gi 38569447   303 HQRVHTGERPYACPECGKSFSQ 324
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
327-352 2.08e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.08e-03
                          10        20
                  ....*....|....*....|....*.
gi 38569447   327 SLNSHRKVHTGERPYECGECGKSFSQ 352
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 341-363 2.87e-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: 2.87e-03
                          10        20
                  ....*....|....*....|...
gi 38569447   341 YECGECGKSFSQRSNLMQHRRVH 363
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 509-531 3.52e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 3.52e-03
                          10        20
                  ....*....|....*....|...
gi 38569447   509 YECSECGKSFSQSSSLIQHRRVH 531
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 397-419 3.70e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 3.70e-03
                          10        20
                  ....*....|....*....|...
gi 38569447   397 HECNECGKSFSRSSSLIHHRRLH 419
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
523-546 4.70e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 4.70e-03
                          10        20
                  ....*....|....*....|....
gi 38569447   523 SLIQHRRVHTGKRPYQCSQCGKSF 546
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