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Conserved domains on  [gi|148709928|gb|EDL41874|]
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MMS19 (MET18 S. cerevisiae)-like, isoform CRA_d, partial [Mus musculus]

Protein Classification

MMS19_C superfamily-containing protein( domain architecture ID 711845)

MMS19_C superfamily-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Pdase_M17_N2 super family cl39644
M17 aminopeptidase N-terminal domain 2; This domain is found in the N-terminal region of M17 ...
203-290 2.31e-03

M17 aminopeptidase N-terminal domain 2; This domain is found in the N-terminal region of M17 aminopeptidase (pfam00883) present in Homo sapiens and Mus musculus. M17 aminopeptidases are Zn-dependent exopeptidases that catalyze the removal of unsubstituted amino acid residues from the N-terminus of peptides.


The actual alignment was detected with superfamily member pfam18295:

Pssm-ID: 408104  Cd Length: 121  Bit Score: 37.38  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148709928  203 GTLATLYPGAFS--RHLLPKLAEE---LHKGESDVARADG------------PTKCSRH---FRClQALSA-VSTHPSIV 261
Cdd:pfam18295   7 GTLETLNELTLQdvAHLEPRVAELidrVASAHTYLPVADGcslvlsvtvaqlPTKASRHntpARP-HAISKlVKANVSGV 85
                          90       100
                  ....*....|....*....|....*....
gi 148709928  262 KETLPLLLqhlcqankgnmVTESSEVVAV 290
Cdd:pfam18295  86 KEVVVDVL-----------VCESENVLAS 103
 
Name Accession Description Interval E-value
Pdase_M17_N2 pfam18295
M17 aminopeptidase N-terminal domain 2; This domain is found in the N-terminal region of M17 ...
203-290 2.31e-03

M17 aminopeptidase N-terminal domain 2; This domain is found in the N-terminal region of M17 aminopeptidase (pfam00883) present in Homo sapiens and Mus musculus. M17 aminopeptidases are Zn-dependent exopeptidases that catalyze the removal of unsubstituted amino acid residues from the N-terminus of peptides.


Pssm-ID: 408104  Cd Length: 121  Bit Score: 37.38  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148709928  203 GTLATLYPGAFS--RHLLPKLAEE---LHKGESDVARADG------------PTKCSRH---FRClQALSA-VSTHPSIV 261
Cdd:pfam18295   7 GTLETLNELTLQdvAHLEPRVAELidrVASAHTYLPVADGcslvlsvtvaqlPTKASRHntpARP-HAISKlVKANVSGV 85
                          90       100
                  ....*....|....*....|....*....
gi 148709928  262 KETLPLLLqhlcqankgnmVTESSEVVAV 290
Cdd:pfam18295  86 KEVVVDVL-----------VCESENVLAS 103
 
Name Accession Description Interval E-value
Pdase_M17_N2 pfam18295
M17 aminopeptidase N-terminal domain 2; This domain is found in the N-terminal region of M17 ...
203-290 2.31e-03

M17 aminopeptidase N-terminal domain 2; This domain is found in the N-terminal region of M17 aminopeptidase (pfam00883) present in Homo sapiens and Mus musculus. M17 aminopeptidases are Zn-dependent exopeptidases that catalyze the removal of unsubstituted amino acid residues from the N-terminus of peptides.


Pssm-ID: 408104  Cd Length: 121  Bit Score: 37.38  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148709928  203 GTLATLYPGAFS--RHLLPKLAEE---LHKGESDVARADG------------PTKCSRH---FRClQALSA-VSTHPSIV 261
Cdd:pfam18295   7 GTLETLNELTLQdvAHLEPRVAELidrVASAHTYLPVADGcslvlsvtvaqlPTKASRHntpARP-HAISKlVKANVSGV 85
                          90       100
                  ....*....|....*....|....*....
gi 148709928  262 KETLPLLLqhlcqankgnmVTESSEVVAV 290
Cdd:pfam18295  86 KEVVVDVL-----------VCESENVLAS 103
 
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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