NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2091597088|ref|NP_001382906|]
View 

zinc finger protein LOC728743 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PHA00733 super family cl26169
hypothetical protein
36-77 1.04e-03

hypothetical protein


The actual alignment was detected with superfamily member PHA00733:

Pssm-ID: 177301  Cd Length: 128  Bit Score: 35.62  E-value: 1.04e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2091597088  36 PYRCPLCGQTFSQQPSLVRHQKAHAGAGraaafVCPECGKAF 77
Cdd:PHA00733   73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK-----VCPVCGKEF 109
 
Name Accession Description Interval E-value
PHA00733 PHA00733
hypothetical protein
36-77 1.04e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 35.62  E-value: 1.04e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2091597088  36 PYRCPLCGQTFSQQPSLVRHQKAHAGAGraaafVCPECGKAF 77
Cdd:PHA00733   73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK-----VCPVCGKEF 109
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
37-57 2.38e-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: 32.66  E-value: 2.38e-03
                         10        20
                 ....*....|....*....|.
gi 2091597088 37 YRCPLCGQTFSQQPSLVRHQK 57
Cdd:pfam00096  1 YKCPDCGKSFSRKSNLKRHLR 21
 
Name Accession Description Interval E-value
PHA00733 PHA00733
hypothetical protein
36-77 1.04e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 35.62  E-value: 1.04e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2091597088  36 PYRCPLCGQTFSQQPSLVRHQKAHAGAGraaafVCPECGKAF 77
Cdd:PHA00733   73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK-----VCPVCGKEF 109
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
37-57 2.38e-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: 32.66  E-value: 2.38e-03
                         10        20
                 ....*....|....*....|.
gi 2091597088 37 YRCPLCGQTFSQQPSLVRHQK 57
Cdd:pfam00096  1 YKCPDCGKSFSRKSNLKRHLR 21
HypA pfam01155
Hydrogenase/urease nickel incorporation, metallochaperone, hypA; HypA is a metallochaperone ...
26-92 9.41e-03

Hydrogenase/urease nickel incorporation, metallochaperone, hypA; HypA is a metallochaperone that binds nickel to bring it safely to its target. The targets for Hypa are the nickel-containing enzymes [Ni,Fe]-hydrogenase and urease. The nickel coordinates with four nitrogens within the protein. The four conserved cysteines towards the C-terminus bind one zinc moiety probably to stabilize the protein fold.


Pssm-ID: 460085  Cd Length: 111  Bit Score: 32.49  E-value: 9.41e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2091597088  26 LVIhhpaEEQP--YRCPLCGQTFSQQpslvrhqkahagagrAAAFVCPECGkafsvKHNLELQSGQDLK 92
Cdd:pfam01155  61 LEI----EEVParARCRDCGKEFELE---------------ERDLVCPRCG-----SPDVEILSGRELR 105
 
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