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Conserved domains on  [gi|23346471|ref|NP_694709|]
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liver-expressed antimicrobial peptide 2 precursor [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LEAP-2 super family cl06413
Liver-expressed antimicrobial peptide 2 precursor (LEAP-2); This family consists of several ...
 1-76 1.86e-30

Liver-expressed antimicrobial peptide 2 precursor (LEAP-2); This family consists of several mammalian liver-expressed antimicrobial peptide 2 (LEAP-2) sequences. LEAP-2 is a cysteine-rich, and cationic protein. LEAP-2 contains a core structure with two disulfide bonds formed by cysteine residues in relative 1-3 and 2-4 positions. LEAP-2 is synthesized as a 77-residue precursor, which is predominantly expressed in the liver and highly conserved among mammals. The largest native LEAP-2 form of 40 amino acid residues is generated from the precursor at a putative cleavage site for a furin-like endoprotease. In contrast to smaller LEAP-2 variants, this peptide exhibits dose-dependent antimicrobial activity against selected microbial model organizms. The exact function of this family is unclear.


The actual alignment was detected with superfamily member pfam07359:

Pssm-ID: 284718  Cd Length: 77  Bit Score: 101.93  E-value: 1.86e-30
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23346471    1 MLQLKLFAVLLTCLLLLGQVNSSPVPEVSSA-KRSRRMTPFWRGVSLRPIGASCRDDSECITRLCRKRRCSLSVAQE 76
Cdd:pfam07359  1 MHHLKLMAIFMFCLLLLSQVHCSPLPQQSSHlRRQRRMTPFWRGVSLRPIGASCRDDSECITRLCRKRRCSLRSAQE 77
 
Name Accession Description Interval E-value
LEAP-2 pfam07359
Liver-expressed antimicrobial peptide 2 precursor (LEAP-2); This family consists of several ...
 1-76 1.86e-30

Liver-expressed antimicrobial peptide 2 precursor (LEAP-2); This family consists of several mammalian liver-expressed antimicrobial peptide 2 (LEAP-2) sequences. LEAP-2 is a cysteine-rich, and cationic protein. LEAP-2 contains a core structure with two disulfide bonds formed by cysteine residues in relative 1-3 and 2-4 positions. LEAP-2 is synthesized as a 77-residue precursor, which is predominantly expressed in the liver and highly conserved among mammals. The largest native LEAP-2 form of 40 amino acid residues is generated from the precursor at a putative cleavage site for a furin-like endoprotease. In contrast to smaller LEAP-2 variants, this peptide exhibits dose-dependent antimicrobial activity against selected microbial model organizms. The exact function of this family is unclear.


Pssm-ID: 284718  Cd Length: 77  Bit Score: 101.93  E-value: 1.86e-30
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23346471    1 MLQLKLFAVLLTCLLLLGQVNSSPVPEVSSA-KRSRRMTPFWRGVSLRPIGASCRDDSECITRLCRKRRCSLSVAQE 76
Cdd:pfam07359  1 MHHLKLMAIFMFCLLLLSQVHCSPLPQQSSHlRRQRRMTPFWRGVSLRPIGASCRDDSECITRLCRKRRCSLRSAQE 77
 
Name Accession Description Interval E-value
LEAP-2 pfam07359
Liver-expressed antimicrobial peptide 2 precursor (LEAP-2); This family consists of several ...
 1-76 1.86e-30

Liver-expressed antimicrobial peptide 2 precursor (LEAP-2); This family consists of several mammalian liver-expressed antimicrobial peptide 2 (LEAP-2) sequences. LEAP-2 is a cysteine-rich, and cationic protein. LEAP-2 contains a core structure with two disulfide bonds formed by cysteine residues in relative 1-3 and 2-4 positions. LEAP-2 is synthesized as a 77-residue precursor, which is predominantly expressed in the liver and highly conserved among mammals. The largest native LEAP-2 form of 40 amino acid residues is generated from the precursor at a putative cleavage site for a furin-like endoprotease. In contrast to smaller LEAP-2 variants, this peptide exhibits dose-dependent antimicrobial activity against selected microbial model organizms. The exact function of this family is unclear.


Pssm-ID: 284718  Cd Length: 77  Bit Score: 101.93  E-value: 1.86e-30
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23346471    1 MLQLKLFAVLLTCLLLLGQVNSSPVPEVSSA-KRSRRMTPFWRGVSLRPIGASCRDDSECITRLCRKRRCSLSVAQE 76
Cdd:pfam07359  1 MHHLKLMAIFMFCLLLLSQVHCSPLPQQSSHlRRQRRMTPFWRGVSLRPIGASCRDDSECITRLCRKRRCSLRSAQE 77
 
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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