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Conserved domains on  [gi|2566979679|dbj|BDW84622|]
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peptidoglycan-binding protein [Roseicyclus marinus]

Protein Classification

peptidoglycan-binding domain-containing protein( domain architecture ID 10477928)

peptidoglycan-binding domain-containing protein may be involved in bacterial cell wall degradation, similar to Vibrio cholerae type VI secretion system (T6SS) effector protein VgrG3 and bacteriophage phi KZ lytic transglycosylase gp144

CATH:  1.10.530.10
Gene Ontology:  GO:0042834

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
75-114 5.16e-08

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


:

Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 49.05  E-value: 5.16e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2566979679  75 QLALNYFGFNAGTVDGQVGNGTRAAIERFQRAMGYPVNGR 114
Cdd:pfam01471   9 QRYLNRLGYYPGPVDGYFGPSTEAAVKAFQRAFGLPVDGI 48
 
Name Accession Description Interval E-value
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
75-114 5.16e-08

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 49.05  E-value: 5.16e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2566979679  75 QLALNYFGFNAGTVDGQVGNGTRAAIERFQRAMGYPVNGR 114
Cdd:pfam01471   9 QRYLNRLGYYPGPVDGYFGPSTEAAVKAFQRAFGLPVDGI 48
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
72-113 1.28e-07

Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 48.37  E-value: 1.28e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2566979679  72 RETQLALNYFGFNAGTVDGQVGNGTRAAIERFQRAMGYPVNG 113
Cdd:COG3409    16 RELQQRLNALGYYPGPVDGIFGPATEAAVRAFQRANGLPVDG 57
 
Name Accession Description Interval E-value
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
75-114 5.16e-08

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 49.05  E-value: 5.16e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2566979679  75 QLALNYFGFNAGTVDGQVGNGTRAAIERFQRAMGYPVNGR 114
Cdd:pfam01471   9 QRYLNRLGYYPGPVDGYFGPSTEAAVKAFQRAFGLPVDGI 48
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
72-113 1.28e-07

Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 48.37  E-value: 1.28e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2566979679  72 RETQLALNYFGFNAGTVDGQVGNGTRAAIERFQRAMGYPVNG 113
Cdd:COG3409    16 RELQQRLNALGYYPGPVDGIFGPATEAAVRAFQRANGLPVDG 57
 
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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