NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|953514578|ref|NP_001304089|]
View 

zinc finger protein PLAGL1 isoform 1 [Homo sapiens]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 11986957)

Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
10-32 4.06e-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: 37.28  E-value: 4.06e-04
                          10        20
                  ....*....|....*....|...
gi 953514578   10 HQCAHCEKTFNRKDHLKNHLQTH 32
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5236 super family cl28715
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
28-155 6.10e-03

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


The actual alignment was detected with superfamily member COG5236:

Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 38.85  E-value: 6.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953514578  28 HLQTHDPNKMAFGCEE--CGKKYNTMLGYKRHLAlhaASSGDLTCGVCA---------LELGSTEVLLDHlkahaEEKPP 96
Cdd:COG5236  141 DVRDEMEDLLSFKCPKskCHRRCGSLKELKKHYK---AQHGFVLCSECIgnkkdfwneIRLFRSSTLRDH-----KNGGL 212
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 953514578  97 SGTKEKKH-QCDHCERCFYTRKDVRRHL-VVHTGCK--DFLCQFCAQRFGRKDHLTRHTKKTH 155
Cdd:COG5236  213 EEEGFKGHpLCIFCKIYFYDDDELRRHCrLRHEACHicDMVGPIRYQYFKSYEDLEAHFRNAH 275
 
Name Accession Description Interval E-value
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
10-32 4.06e-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: 37.28  E-value: 4.06e-04
                          10        20
                  ....*....|....*....|...
gi 953514578   10 HQCAHCEKTFNRKDHLKNHLQTH 32
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5236 COG5236
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
28-155 6.10e-03

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 38.85  E-value: 6.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953514578  28 HLQTHDPNKMAFGCEE--CGKKYNTMLGYKRHLAlhaASSGDLTCGVCA---------LELGSTEVLLDHlkahaEEKPP 96
Cdd:COG5236  141 DVRDEMEDLLSFKCPKskCHRRCGSLKELKKHYK---AQHGFVLCSECIgnkkdfwneIRLFRSSTLRDH-----KNGGL 212
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 953514578  97 SGTKEKKH-QCDHCERCFYTRKDVRRHL-VVHTGCK--DFLCQFCAQRFGRKDHLTRHTKKTH 155
Cdd:COG5236  213 EEEGFKGHpLCIFCKIYFYDDDELRRHCrLRHEACHicDMVGPIRYQYFKSYEDLEAHFRNAH 275
 
Name Accession Description Interval E-value
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
10-32 4.06e-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: 37.28  E-value: 4.06e-04
                          10        20
                  ....*....|....*....|...
gi 953514578   10 HQCAHCEKTFNRKDHLKNHLQTH 32
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5236 COG5236
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
28-155 6.10e-03

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 38.85  E-value: 6.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953514578  28 HLQTHDPNKMAFGCEE--CGKKYNTMLGYKRHLAlhaASSGDLTCGVCA---------LELGSTEVLLDHlkahaEEKPP 96
Cdd:COG5236  141 DVRDEMEDLLSFKCPKskCHRRCGSLKELKKHYK---AQHGFVLCSECIgnkkdfwneIRLFRSSTLRDH-----KNGGL 212
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 953514578  97 SGTKEKKH-QCDHCERCFYTRKDVRRHL-VVHTGCK--DFLCQFCAQRFGRKDHLTRHTKKTH 155
Cdd:COG5236  213 EEEGFKGHpLCIFCKIYFYDDDELRRHCrLRHEACHicDMVGPIRYQYFKSYEDLEAHFRNAH 275
 
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