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Conserved domains on  [gi|215273921|sp|Q13398|]
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RecName: Full=Zinc finger protein 211; AltName: Full=Zinc finger protein C2H2-25

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

CATH:  3.30.160.60|1.10.287.1360
Gene Ontology:  GO:0003700|GO:0005515|GO:0008270|GO:0003677|GO:0006355|GO:0001217
PubMed:  22803940|8183940|2023909|8183939|10748030|27867147|28765213|11361095|30718982|10940247
SCOP:  4003583|4002243

Graphical summary

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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 215273921   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 215273921 179 HVSEKPFTCREIRKDFLANMR-FLHQDATQTGEKPNNSN-KCAVAFYSGKSHHNWGKCSKAFSHIDTLVQD---QRILTR 253
Cdd:COG5048   56 HTGEKPSQCSYSGCDKSFSRPlELSRHLRTHHNNPSDLNsKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHslpPSSRDP 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273921 254 EGLFECSKC--GKACTRRCNLIQHQKVHSEERPYEC--NECGKFFTYYSSFIIHQRVHTGERPYACPECGKSFSQIYSLN 329
Cdd:COG5048  136 QLPDLLSISnlRNNPLPGNNSSSVNTPQSNSLHPPLpaNSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSS 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273921 330 SHRKVHTGERPYECGECGKSFSQRSNLMQHRRVHTGERPYECSECGKSFSQNFSLIYHQRVHTGERPHE-------CNEC 402
Cdd:COG5048  216 SDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKgfslpikSKQC 295

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273921 403 GKSFSRSSSLIHHRRLhtgerpyecskcgksfkqsssfsshrKVHTGE--RPYVCGE--CGKSFSHSSNLKNHQRVHTGE 478
Cdd:COG5048  296 NISFSRSSPLTRHLRS--------------------------VNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSI 349

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273921 479 RPVEC-------------------------------------SECSKSFSCKSNLIKHLRVHTGERPYEC--SECGKSFS 519
Cdd:COG5048  350 SPAKEkllnssskfspllnneppqslqqykdlkndkksetlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFN 429

                        410       420       430
                 ....*....|....*....|....*....|.
gi 215273921 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 215273921   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 215273921    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 215273921  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 215273921 179 HVSEKPFTCREIRKDFLANMR-FLHQDATQTGEKPNNSN-KCAVAFYSGKSHHNWGKCSKAFSHIDTLVQD---QRILTR 253
Cdd:COG5048   56 HTGEKPSQCSYSGCDKSFSRPlELSRHLRTHHNNPSDLNsKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHslpPSSRDP 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273921 254 EGLFECSKC--GKACTRRCNLIQHQKVHSEERPYEC--NECGKFFTYYSSFIIHQRVHTGERPYACPECGKSFSQIYSLN 329
Cdd:COG5048  136 QLPDLLSISnlRNNPLPGNNSSSVNTPQSNSLHPPLpaNSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSS 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273921 330 SHRKVHTGERPYECGECGKSFSQRSNLMQHRRVHTGERPYECSECGKSFSQNFSLIYHQRVHTGERPHE-------CNEC 402
Cdd:COG5048  216 SDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKgfslpikSKQC 295

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273921 403 GKSFSRSSSLIHHRRLhtgerpyecskcgksfkqsssfsshrKVHTGE--RPYVCGE--CGKSFSHSSNLKNHQRVHTGE 478
Cdd:COG5048  296 NISFSRSSPLTRHLRS--------------------------VNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSI 349

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273921 479 RPVEC-------------------------------------SECSKSFSCKSNLIKHLRVHTGERPYEC--SECGKSFS 519
Cdd:COG5048  350 SPAKEkllnssskfspllnneppqslqqykdlkndkksetlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFN 429

                        410       420       430
                 ....*....|....*....|....*....|.
gi 215273921 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 215273921  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 215273921   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 215273921    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 215273921  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 215273921 179 HVSEKPFTCREIRKDFLANMR-FLHQDATQTGEKPNNSN-KCAVAFYSGKSHHNWGKCSKAFSHIDTLVQD---QRILTR 253
Cdd:COG5048   56 HTGEKPSQCSYSGCDKSFSRPlELSRHLRTHHNNPSDLNsKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHslpPSSRDP 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273921 254 EGLFECSKC--GKACTRRCNLIQHQKVHSEERPYEC--NECGKFFTYYSSFIIHQRVHTGERPYACPECGKSFSQIYSLN 329
Cdd:COG5048  136 QLPDLLSISnlRNNPLPGNNSSSVNTPQSNSLHPPLpaNSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSS 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273921 330 SHRKVHTGERPYECGECGKSFSQRSNLMQHRRVHTGERPYECSECGKSFSQNFSLIYHQRVHTGERPHE-------CNEC 402
Cdd:COG5048  216 SDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKgfslpikSKQC 295

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273921 403 GKSFSRSSSLIHHRRLhtgerpyecskcgksfkqsssfsshrKVHTGE--RPYVCGE--CGKSFSHSSNLKNHQRVHTGE 478
Cdd:COG5048  296 NISFSRSSPLTRHLRS--------------------------VNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSI 349

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273921 479 RPVEC-------------------------------------SECSKSFSCKSNLIKHLRVHTGERPYEC--SECGKSFS 519
Cdd:COG5048  350 SPAKEkllnssskfspllnneppqslqqykdlkndkksetlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFN 429

                        410       420       430
                 ....*....|....*....|....*....|.
gi 215273921 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 215273921 233 KCSKAFSHIDTLVQDQRILTREGLFECSK--CGKACTRRCNLIQHQKVHSEERPYECNECGKFFTYYSSFIIHQRVHTGE 310
Cdd:COG5048   38 NCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLSSSSSNS 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273921 311 -RPYACPECGKSFSQIYSLNSHRKVHTGERPYECGECGKSFSQRSN----LMQHRRVHTGERPYEcsecgksfsqNFSLI 385
Cdd:COG5048  118 nDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQsnslHPPLPANSLSKDPSS----------NLSLL 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273921 386 YHQRVHTGERPHECNECGKSFSRSSSLIHHRRLHTGERPYECSKCGKSFKQSSSFSSHRKVHTGERPYVCGECGKSFSHS 465
Cdd:COG5048  188 ISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPT 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273921 466 SNLKNHQRVHTGERPVE-------CSECSKSFSCKSNLIKHLR--VHTGE--RPYECSE--CGKSFSQSSSLIQHRRVHT 532
Cdd:COG5048  268 ASSQSSSPNESDSSSEKgfslpikSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHT 347

                        330
                 ....*....|....*..
gi 215273921 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 215273921  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 215273921 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 215273921  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 215273921 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 215273921 309 GERPYACP--ECGKSFSQIYSLNSHRKvHtgerpyecGECGKSFSQRSNLMQHRRVHTGERPYECSECGKSFSQNFSLIY 386
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLKYHML-H--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                 ....*.
gi 215273921 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 215273921  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 215273921  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 215273921  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 215273921  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 215273921  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 215273921  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 215273921  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 215273921  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 215273921  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.
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