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Conserved domains on  [gi|499656316|ref|WP_011337050|]
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peptidoglycan-binding protein [Cereibacter sphaeroides]

Protein Classification

peptidoglycan-binding domain-containing protein( domain architecture ID 11465558)

peptidoglycan-binding domain-containing protein may function as a peptidoglycan hydrolase

CATH:  1.10.101.10
Gene Ontology:  GO:0042834
SCOP:  3001357

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
77-118 8.73e-08

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


:

Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 49.14  E-value: 8.73e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 499656316  77 KEVQTALNYFGYPVGTVDGVLGSRSRSAVSQFQVLMGYQPTG 118
Cdd:COG3409   16 RELQQRLNALGYYPGPVDGIFGPATEAAVRAFQRANGLPVDG 57
 
Name Accession Description Interval E-value
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
77-118 8.73e-08

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


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 49.14  E-value: 8.73e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 499656316  77 KEVQTALNYFGYPVGTVDGVLGSRSRSAVSQFQVLMGYQPTG 118
Cdd:COG3409   16 RELQQRLNALGYYPGPVDGIFGPATEAAVRAFQRANGLPVDG 57
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
77-122 9.53e-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: 48.67  E-value: 9.53e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 499656316   77 KEVQTALNYFGYPVGTVDGVLGSRSRSAVSQFQVLMGYQPTGQLTE 122
Cdd:pfam01471   6 KELQRYLNRLGYYPGPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDP 51
 
Name Accession Description Interval E-value
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
77-118 8.73e-08

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


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 49.14  E-value: 8.73e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 499656316  77 KEVQTALNYFGYPVGTVDGVLGSRSRSAVSQFQVLMGYQPTG 118
Cdd:COG3409   16 RELQQRLNALGYYPGPVDGIFGPATEAAVRAFQRANGLPVDG 57
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
77-122 9.53e-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: 48.67  E-value: 9.53e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 499656316   77 KEVQTALNYFGYPVGTVDGVLGSRSRSAVSQFQVLMGYQPTGQLTE 122
Cdd:pfam01471   6 KELQRYLNRLGYYPGPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDP 51
 
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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