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Conserved domains on  [gi|1162406480|gb|OPX21173|]
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MAG: hypothetical protein BZ151_00485 [Desulfobacca sp. 4484_104]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AMIN super family cl46341
AMIN domain; This N-terminal domain of various bacterial protein families is crucial for the ...
 51-137 2.80e-03

AMIN domain; This N-terminal domain of various bacterial protein families is crucial for the targetting of periplasmic or extracellular proteins to specific regions of the bacterial envelope. AMIN is derived from the N-terminal domain of AmiC, an N-acetylmuramoyl-l-alanine amidase of Escherichia coli which localizes to the septal ring during division and plays a key role in the separation of daughter cells. The AMIN domain is present in several protein families besides amidases suggesting that AMIN may represent a general targetting determinant involved in the localization of periplasmic protein complexes.


The actual alignment was detected with superfamily member pfam11741:

Pssm-ID: 480681  Cd Length: 96  Bit Score: 35.74  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406480  51 LTIVLSKAVQPQispVTAVSDPQ-LVIIFPDAGARRLPPVLPGDQTLVRQVR-TLFTPGKngVRIILDLipDRPYVFWRQ 128
Cdd:pfam11741  12 LELETSGGEKYQ---VFTLSNPNrLVIDIPGAQLGLPLKRIENPSPGIKSVRvGQFDPNT--VRVVVDL--DGSVLPQVP 84


                  ....*....
gi 1162406480 129 LRPAPNGLV 137
Cdd:pfam11741  85 VFKSGEGLV 93
 
Name Accession Description Interval E-value
AMIN pfam11741
AMIN domain; This N-terminal domain of various bacterial protein families is crucial for the ...
 51-137 2.80e-03

AMIN domain; This N-terminal domain of various bacterial protein families is crucial for the targetting of periplasmic or extracellular proteins to specific regions of the bacterial envelope. AMIN is derived from the N-terminal domain of AmiC, an N-acetylmuramoyl-l-alanine amidase of Escherichia coli which localizes to the septal ring during division and plays a key role in the separation of daughter cells. The AMIN domain is present in several protein families besides amidases suggesting that AMIN may represent a general targetting determinant involved in the localization of periplasmic protein complexes.


Pssm-ID: 463338  Cd Length: 96  Bit Score: 35.74  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406480  51 LTIVLSKAVQPQispVTAVSDPQ-LVIIFPDAGARRLPPVLPGDQTLVRQVR-TLFTPGKngVRIILDLipDRPYVFWRQ 128
Cdd:pfam11741  12 LELETSGGEKYQ---VFTLSNPNrLVIDIPGAQLGLPLKRIENPSPGIKSVRvGQFDPNT--VRVVVDL--DGSVLPQVP 84


                  ....*....
gi 1162406480 129 LRPAPNGLV 137
Cdd:pfam11741  85 VFKSGEGLV 93
 
Name Accession Description Interval E-value
AMIN pfam11741
AMIN domain; This N-terminal domain of various bacterial protein families is crucial for the ...
 51-137 2.80e-03

AMIN domain; This N-terminal domain of various bacterial protein families is crucial for the targetting of periplasmic or extracellular proteins to specific regions of the bacterial envelope. AMIN is derived from the N-terminal domain of AmiC, an N-acetylmuramoyl-l-alanine amidase of Escherichia coli which localizes to the septal ring during division and plays a key role in the separation of daughter cells. The AMIN domain is present in several protein families besides amidases suggesting that AMIN may represent a general targetting determinant involved in the localization of periplasmic protein complexes.


Pssm-ID: 463338  Cd Length: 96  Bit Score: 35.74  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406480  51 LTIVLSKAVQPQispVTAVSDPQ-LVIIFPDAGARRLPPVLPGDQTLVRQVR-TLFTPGKngVRIILDLipDRPYVFWRQ 128
Cdd:pfam11741  12 LELETSGGEKYQ---VFTLSNPNrLVIDIPGAQLGLPLKRIENPSPGIKSVRvGQFDPNT--VRVVVDL--DGSVLPQVP 84


                  ....*....
gi 1162406480 129 LRPAPNGLV 137
Cdd:pfam11741  85 VFKSGEGLV 93
 
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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