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Conserved domains on  [gi|289547686|ref|NP_001026891|]
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zinc finger protein 613 isoform 1 [Homo sapiens]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204268)

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
Gene Ontology:  GO:0003700|GO:0046872
PubMed:  22803940
SCOP:  4003583

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-67 7.01e-33

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 120.39  E-value: 7.01e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 289547686     8 LTLEDVAVEFTWEEWQLLGPAQKDLYRDVMLENYSNLVSVGYQASKPDALFKLEQG-EPWT 67
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGeEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
176-531 4.49e-08

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.86  E-value: 4.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547686 176 MNFPEGGNSVNTNSQFI-----KHQRTQNIDKPHVCTECGKAFLKKSRLIYHQRVHTGEKPHGCS--ICGKAFSRKSGLT 248
Cdd:COG5048    1 ATLTSSQSSSSNNSVLSstpksTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547686 249 EHQRNHTGEKPYECT-ECDKAFRWKSQLNAHQKIHTGEKSYICSDCGKGFIKKSRLIN---------------------- 305
Cdd:COG5048   81 RHLRTHHNNPSDLNSkSLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPdllsisnlrnnplpgnnsssvn 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547686 306 ----------------------------HQRVHTGEKPHGCSLCGKAFSKRSRLTEHQRTHTGEKPYECTECDKAF---- 353
Cdd:COG5048  161 tpqsnslhpplpanslskdpssnlslliSSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpksl 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547686 354 --RWKSQLNAHQKAHTGEKSYICRDCGKGFIQKGNLIVHQRIHTG-EKPYICNECGKGFIQKGNLLIHRRT--HTGE--K 426
Cdd:COG5048  241 lsQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547686 427 PYVCNE--CGKGFSQKTCLISHQRFHTGKTPFVCTECGKSCSHKSGLIN-------HQRIHTGEKPYTCSD--CGKAFRD 495
Cdd:COG5048  321 PFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNNeppqslqQYKDLKNDKKSETLSnsCIRNFKR 400

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 289547686 496 KSCLNRHRRTHTGERPYGC--SDCGKAFSHLSCLVYHK 531
Cdd:COG5048  401 DSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHK 438
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-67 7.01e-33

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 120.39  E-value: 7.01e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 289547686     8 LTLEDVAVEFTWEEWQLLGPAQKDLYRDVMLENYSNLVSVGYQASKPDALFKLEQG-EPWT 67
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGeEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 7-48 9.58e-24

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 93.69  E-value: 9.58e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 289547686    7 SLTLEDVAVEFTWEEWQLLGPAQKDLYRDVMLENYSNLVSVG 48
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 8-46 1.60e-20

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: 84.52  E-value: 1.60e-20
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 289547686   8 LTLEDVAVEFTWEEWQLLGPAQKDLYRDVMLENYSNLVS 46
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
176-531 4.49e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.86  E-value: 4.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547686 176 MNFPEGGNSVNTNSQFI-----KHQRTQNIDKPHVCTECGKAFLKKSRLIYHQRVHTGEKPHGCS--ICGKAFSRKSGLT 248
Cdd:COG5048    1 ATLTSSQSSSSNNSVLSstpksTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547686 249 EHQRNHTGEKPYECT-ECDKAFRWKSQLNAHQKIHTGEKSYICSDCGKGFIKKSRLIN---------------------- 305
Cdd:COG5048   81 RHLRTHHNNPSDLNSkSLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPdllsisnlrnnplpgnnsssvn 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547686 306 ----------------------------HQRVHTGEKPHGCSLCGKAFSKRSRLTEHQRTHTGEKPYECTECDKAF---- 353
Cdd:COG5048  161 tpqsnslhpplpanslskdpssnlslliSSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpksl 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547686 354 --RWKSQLNAHQKAHTGEKSYICRDCGKGFIQKGNLIVHQRIHTG-EKPYICNECGKGFIQKGNLLIHRRT--HTGE--K 426
Cdd:COG5048  241 lsQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547686 427 PYVCNE--CGKGFSQKTCLISHQRFHTGKTPFVCTECGKSCSHKSGLIN-------HQRIHTGEKPYTCSD--CGKAFRD 495
Cdd:COG5048  321 PFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNNeppqslqQYKDLKNDKKSETLSnsCIRNFKR 400

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 289547686 496 KSCLNRHRRTHTGERPYGC--SDCGKAFSHLSCLVYHK 531
Cdd:COG5048  401 DSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHK 438
zf-H2C2_2 pfam13465
Zinc-finger double domain;
330-353 3.07e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.07e-04
                          10        20
                  ....*....|....*....|....
gi 289547686  330 RLTEHQRTHTGEKPYECTECDKAF 353
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-67 7.01e-33

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 120.39  E-value: 7.01e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 289547686     8 LTLEDVAVEFTWEEWQLLGPAQKDLYRDVMLENYSNLVSVGYQASKPDALFKLEQG-EPWT 67
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGeEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 7-48 9.58e-24

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 93.69  E-value: 9.58e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 289547686    7 SLTLEDVAVEFTWEEWQLLGPAQKDLYRDVMLENYSNLVSVG 48
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 8-46 1.60e-20

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: 84.52  E-value: 1.60e-20
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 289547686   8 LTLEDVAVEFTWEEWQLLGPAQKDLYRDVMLENYSNLVS 46
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
176-531 4.49e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.86  E-value: 4.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547686 176 MNFPEGGNSVNTNSQFI-----KHQRTQNIDKPHVCTECGKAFLKKSRLIYHQRVHTGEKPHGCS--ICGKAFSRKSGLT 248
Cdd:COG5048    1 ATLTSSQSSSSNNSVLSstpksTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547686 249 EHQRNHTGEKPYECT-ECDKAFRWKSQLNAHQKIHTGEKSYICSDCGKGFIKKSRLIN---------------------- 305
Cdd:COG5048   81 RHLRTHHNNPSDLNSkSLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPdllsisnlrnnplpgnnsssvn 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547686 306 ----------------------------HQRVHTGEKPHGCSLCGKAFSKRSRLTEHQRTHTGEKPYECTECDKAF---- 353
Cdd:COG5048  161 tpqsnslhpplpanslskdpssnlslliSSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpksl 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547686 354 --RWKSQLNAHQKAHTGEKSYICRDCGKGFIQKGNLIVHQRIHTG-EKPYICNECGKGFIQKGNLLIHRRT--HTGE--K 426
Cdd:COG5048  241 lsQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547686 427 PYVCNE--CGKGFSQKTCLISHQRFHTGKTPFVCTECGKSCSHKSGLIN-------HQRIHTGEKPYTCSD--CGKAFRD 495
Cdd:COG5048  321 PFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNNeppqslqQYKDLKNDKKSETLSnsCIRNFKR 400

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 289547686 496 KSCLNRHRRTHTGERPYGC--SDCGKAFSHLSCLVYHK 531
Cdd:COG5048  401 DSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHK 438
zf-H2C2_2 pfam13465
Zinc-finger double domain;
330-353 3.07e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.07e-04
                          10        20
                  ....*....|....*....|....
gi 289547686  330 RLTEHQRTHTGEKPYECTECDKAF 353
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
102-503 3.98e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.15  E-value: 3.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547686 102 QCHKHNAFGNIIHQRKSDFPLRQNHDTFDLHGKILKSNLSLVNQNKRYEIKNSVGVNGDGKSFLHAKHEQFHNeMNFPEG 181
Cdd:COG5048   81 RHLRTHHNNPSDLNSKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPG-NNSSSV 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547686 182 GNSVNTNSQFIKHQRTQNIDKPhvctecgkaflKKSRLIYHQRVHTGEKPHGCSICGKAFSRKSGLTEHQRNHTGEKPYE 261
Cdd:COG5048  160 NTPQSNSLHPPLPANSLSKDPS-----------SNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLP 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547686 262 CTECDKAFRWKSQLNAHQKIHTGEKSYICSDCGKGFIKKSRLINHQRVHTGEKPHG-------CSLCGKAFSKRSRLTEH 334
Cdd:COG5048  229 LTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKgfslpikSKQCNISFSRSSPLTRH 308

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547686 335 QRT--HTGE--KPYECTE--CDKAFRWKSQLNAHQKAHTGEKSYIC--RDCGKGFIQKGN-----LIVHQRIHTGEKPYI 401
Cdd:COG5048  309 LRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSE 388

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547686 402 C--NECGKGFIQKGNLLIHRRTHTGEKPYVCNecgkgfsqktclishqrfhtgktpfvCTECGKSCSHKSGLINHQRIHT 479
Cdd:COG5048  389 TlsNSCIRNFKRDSNLSLHIITHLSFRPYNCK--------------------------NPPCSKSFNRHYNLIPHKKIHT 442

                        410       420
                 ....*....|....*....|....
gi 289547686 480 GEKPYTCSDCGKAFRDKSCLNRHR 503
Cdd:COG5048  443 NHAPLLCSILKSFRRDLDLSNHGK 466
zf-H2C2_2 pfam13465
Zinc-finger double domain;
247-269 5.47e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 5.47e-04
                          10        20
                  ....*....|....*....|...
gi 289547686  247 LTEHQRNHTGEKPYECTECDKAF 269
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
414-439 1.18e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.18e-03
                          10        20
                  ....*....|....*....|....*.
gi 289547686  414 NLLIHRRTHTGEKPYVCNECGKGFSQ 439
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 484-506 1.31e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.51  E-value: 1.31e-03
                          10        20
                  ....*....|....*....|...
gi 289547686  484 YTCSDCGKAFRDKSCLNRHRRTH 506
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
471-493 2.51e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.51e-03
                          10        20
                  ....*....|....*....|...
gi 289547686  471 LINHQRIHTGEKPYTCSDCGKAF 493
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
499-523 3.27e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.27e-03
                          10        20
                  ....*....|....*....|....*
gi 289547686  499 LNRHRRTHTGERPYGCSDCGKAFSH 523
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
 
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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