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Conserved domains on  [gi|302318934|ref|NP_001180559|]
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zinc finger protein 705B [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
7-66 8.22e-32

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 112.69  E-value: 8.22e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 302318934     7 VTFEDVAIDFTQEEWDMMDTSKRKLYRDVMLENISHLVSLGYQISKSYIILQLEQGKELW 66
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPW 60
zf-H2C2_2 pfam13465
Zinc-finger double domain;
214-239 5.42e-06

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 5.42e-06
                          10        20
                  ....*....|....*....|....*.
gi 302318934  214 HLRRHEKTHTGERPYKCHQCGKAFIQ 239
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
186-211 5.99e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 5.99e-05
                          10        20
                  ....*....|....*....|....*.
gi 302318934  186 YLRRHKMTHTGERPYACHLCGKAFTQ 211
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 super family cl34881
FOG: Zn-finger [General function prediction only];
116-300 4.12e-04

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


The actual alignment was detected with superfamily member COG5048:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.61  E-value: 4.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302318934 116 FEYNDSGEDCTHSSTITQCLLT---HSGKKPCVSKQCGKSLRNLLSPKPRKQIHT-----------KGKSYQCNLCEKAY 181
Cdd:COG5048  220 LENSSSSLPLTTNSQLSPKSLLsqsPSSLSSSDSSSSASESPRSSLPTASSQSSSpnesdsssekgFSLPIKSKQCNISF 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302318934 182 TNCFYLRRHK--MTHTGE--RPYAC--HLCGKAFTQCSHLRRHEKTHTGERPYKCH--QCGKAFIQSFNLRRHERTH--- 250
Cdd:COG5048  300 SRSSPLTRHLrsVNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQqyk 379

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 302318934 251 --LGQKCYECDKSG--KAFSQSSGFRGNKIIHIGEKPPAC--LLCGKAFSLSSDLR 300
Cdd:COG5048  380 dlKNDKKSETLSNSciRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLI 435
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
7-66 8.22e-32

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 112.69  E-value: 8.22e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 302318934     7 VTFEDVAIDFTQEEWDMMDTSKRKLYRDVMLENISHLVSLGYQISKSYIILQLEQGKELW 66
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPW 60
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 7-47 9.09e-22

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: 85.60  E-value: 9.09e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 302318934    7 VTFEDVAIDFTQEEWDMMDTSKRKLYRDVMLENISHLVSLG 47
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 7-46 9.44e-18

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: 74.89  E-value: 9.44e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 302318934   7 VTFEDVAIDFTQEEWDMMDTSKRKLYRDVMLENISHLVSL 46
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
zf-H2C2_2 pfam13465
Zinc-finger double domain;
214-239 5.42e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 5.42e-06
                          10        20
                  ....*....|....*....|....*.
gi 302318934  214 HLRRHEKTHTGERPYKCHQCGKAFIQ 239
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
186-211 5.99e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 5.99e-05
                          10        20
                  ....*....|....*....|....*.
gi 302318934  186 YLRRHKMTHTGERPYACHLCGKAFTQ 211
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
116-300 4.12e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.61  E-value: 4.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302318934 116 FEYNDSGEDCTHSSTITQCLLT---HSGKKPCVSKQCGKSLRNLLSPKPRKQIHT-----------KGKSYQCNLCEKAY 181
Cdd:COG5048  220 LENSSSSLPLTTNSQLSPKSLLsqsPSSLSSSDSSSSASESPRSSLPTASSQSSSpnesdsssekgFSLPIKSKQCNISF 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302318934 182 TNCFYLRRHK--MTHTGE--RPYAC--HLCGKAFTQCSHLRRHEKTHTGERPYKCH--QCGKAFIQSFNLRRHERTH--- 250
Cdd:COG5048  300 SRSSPLTRHLrsVNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQqyk 379

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 302318934 251 --LGQKCYECDKSG--KAFSQSSGFRGNKIIHIGEKPPAC--LLCGKAFSLSSDLR 300
Cdd:COG5048  380 dlKNDKKSETLSNSciRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLI 435
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
7-66 8.22e-32

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 112.69  E-value: 8.22e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 302318934     7 VTFEDVAIDFTQEEWDMMDTSKRKLYRDVMLENISHLVSLGYQISKSYIILQLEQGKELW 66
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPW 60
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 7-47 9.09e-22

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: 85.60  E-value: 9.09e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 302318934    7 VTFEDVAIDFTQEEWDMMDTSKRKLYRDVMLENISHLVSLG 47
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 7-46 9.44e-18

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: 74.89  E-value: 9.44e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 302318934   7 VTFEDVAIDFTQEEWDMMDTSKRKLYRDVMLENISHLVSL 46
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
zf-H2C2_2 pfam13465
Zinc-finger double domain;
214-239 5.42e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 5.42e-06
                          10        20
                  ....*....|....*....|....*.
gi 302318934  214 HLRRHEKTHTGERPYKCHQCGKAFIQ 239
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
186-211 5.99e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 5.99e-05
                          10        20
                  ....*....|....*....|....*.
gi 302318934  186 YLRRHKMTHTGERPYACHLCGKAFTQ 211
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
116-300 4.12e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.61  E-value: 4.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302318934 116 FEYNDSGEDCTHSSTITQCLLT---HSGKKPCVSKQCGKSLRNLLSPKPRKQIHT-----------KGKSYQCNLCEKAY 181
Cdd:COG5048  220 LENSSSSLPLTTNSQLSPKSLLsqsPSSLSSSDSSSSASESPRSSLPTASSQSSSpnesdsssekgFSLPIKSKQCNISF 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302318934 182 TNCFYLRRHK--MTHTGE--RPYAC--HLCGKAFTQCSHLRRHEKTHTGERPYKCH--QCGKAFIQSFNLRRHERTH--- 250
Cdd:COG5048  300 SRSSPLTRHLrsVNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQqyk 379

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 302318934 251 --LGQKCYECDKSG--KAFSQSSGFRGNKIIHIGEKPPAC--LLCGKAFSLSSDLR 300
Cdd:COG5048  380 dlKNDKKSETLSNSciRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLI 435
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 228-250 7.76e-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: 36.12  E-value: 7.76e-04
                          10        20
                  ....*....|....*....|...
gi 302318934  228 YKCHQCGKAFIQSFNLRRHERTH 250
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 162-250 8.58e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.47  E-value: 8.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302318934 162 RKQIHTKGKSYQCNL--CEKAYTNCFYLRRHKMT-HtgerpyachlCGKAFTQCSHLRRHEKTHTGERPYKCHQCGKAFI 238
Cdd:COG5189  340 RMLKVKDGKPYKCPVegCNKKYKNQNGLKYHMLHgH----------QNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYK 409

                         90
                 ....*....|..
gi 302318934 239 QSFNLRRHeRTH 250
Cdd:COG5189  410 NLNGLKYH-RKH 420
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
92-246 1.52e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.06  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302318934  92 MHPIIRKDTSTSMTMENSLILEDPfeYNDSGEDCTHSSTITQCLLTHSGKKP--CVSKQCGKSLRNLLSPKPRKQIH--- 166
Cdd:COG5048  302 SSPLTRHLRSVNHSGESLKPFSCP--YSLCGKLFSRNDALKRHILLHTSISPakEKLLNSSSKFSPLLNNEPPQSLQqyk 379

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302318934 167 --TKGKSYQC--NLCEKAYTNCFYLRRHKMTHTGERPYACH--LCGKAFTQCSHLRRHEKTHTGERPYKCHQCGKaFIQS 240
Cdd:COG5048  380 dlKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRD 458


                 ....*.
gi 302318934 241 FNLRRH 246
Cdd:COG5048  459 LDLSNH 464
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 200-222 2.01e-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: 2.01e-03
                          10        20
                  ....*....|....*....|...
gi 302318934  200 YACHLCGKAFTQCSHLRRHEKTH 222
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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