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Conserved domains on  [gi|1777569004|ref|WP_154261939|]
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MULTISPECIES: NHLP-related RiPP peptide [Stenotrophomonas]

Protein Classification

mod_pep_NH_fam family protein( domain architecture ID 10025275)

mod_pep_NH_fam family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
mod_pep_NH_fam TIGR04509
putative modified peptide; Members of this family average 110 residues in length, with strong ...
 6-90 5.33e-28

putative modified peptide; Members of this family average 110 residues in length, with strong N-terminal homology to both the nitrile hydratase (NH) alpha subunit and family TIGR03793 of NH-related ribosomally translated natural product precursors. A neighboring gene resembles SagB, the dehydrogenase of many thiazole and oxazole modified peptide systems, supporting the hypothesis that members of this family are post-translationally modified.


:

Pssm-ID: 275302  Cd Length: 85  Bit Score: 97.04  E-value: 5.33e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777569004  6 RLSAADASTLLDHLIGNDEFRSHFTASPAQALASIGLDA-AVGENDCMKIDTLASVEELGQVRDALQDHLSgSVAAMTVV 84
Cdd:TIGR04509  1 PLSPAVADALLDLLSTDDAFRALFQSDPAAALAQLGHAElGAAVVPCCLNGQLASKEEIAAARDQLVAMLT-SGAAFTVP 79


                 ....*.
gi 1777569004 85 FCFEAG 90
Cdd:TIGR04509 80 FLFEGG 85
 
Name Accession Description Interval E-value
mod_pep_NH_fam TIGR04509
putative modified peptide; Members of this family average 110 residues in length, with strong ...
 6-90 5.33e-28

putative modified peptide; Members of this family average 110 residues in length, with strong N-terminal homology to both the nitrile hydratase (NH) alpha subunit and family TIGR03793 of NH-related ribosomally translated natural product precursors. A neighboring gene resembles SagB, the dehydrogenase of many thiazole and oxazole modified peptide systems, supporting the hypothesis that members of this family are post-translationally modified.


Pssm-ID: 275302  Cd Length: 85  Bit Score: 97.04  E-value: 5.33e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777569004  6 RLSAADASTLLDHLIGNDEFRSHFTASPAQALASIGLDA-AVGENDCMKIDTLASVEELGQVRDALQDHLSgSVAAMTVV 84
Cdd:TIGR04509  1 PLSPAVADALLDLLSTDDAFRALFQSDPAAALAQLGHAElGAAVVPCCLNGQLASKEEIAAARDQLVAMLT-SGAAFTVP 79


                 ....*.
gi 1777569004 85 FCFEAG 90
Cdd:TIGR04509 80 FLFEGG 85
 
Name Accession Description Interval E-value
mod_pep_NH_fam TIGR04509
putative modified peptide; Members of this family average 110 residues in length, with strong ...
 6-90 5.33e-28

putative modified peptide; Members of this family average 110 residues in length, with strong N-terminal homology to both the nitrile hydratase (NH) alpha subunit and family TIGR03793 of NH-related ribosomally translated natural product precursors. A neighboring gene resembles SagB, the dehydrogenase of many thiazole and oxazole modified peptide systems, supporting the hypothesis that members of this family are post-translationally modified.


Pssm-ID: 275302  Cd Length: 85  Bit Score: 97.04  E-value: 5.33e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777569004  6 RLSAADASTLLDHLIGNDEFRSHFTASPAQALASIGLDA-AVGENDCMKIDTLASVEELGQVRDALQDHLSgSVAAMTVV 84
Cdd:TIGR04509  1 PLSPAVADALLDLLSTDDAFRALFQSDPAAALAQLGHAElGAAVVPCCLNGQLASKEEIAAARDQLVAMLT-SGAAFTVP 79


                 ....*.
gi 1777569004 85 FCFEAG 90
Cdd:TIGR04509 80 FLFEGG 85
 
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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