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Conserved domains on  [gi|612660551|gb|EZS76817|]
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hypothetical protein W490_02095 [Staphylococcus aureus VET0191R]

Protein Classification

lysozyme family protein( domain architecture ID 63)

lysozyme family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Lyz-like super family cl00222
lysozyme-like domains; This family contains several members, including soluble lytic ...
155-231 3.74e-25

lysozyme-like domains; This family contains several members, including soluble lytic transglycosylases (SLT), goose egg-white lysozymes (GEWL), hen egg-white lysozymes (HEWL), chitinases, bacteriophage lambda lysozymes, endolysins, autolysins, chitosanases, and pesticin. Typical members are involved in the hydrolysis of beta-1,4- linked polysaccharides.


The actual alignment was detected with superfamily member pfam06737:

Pssm-ID: 469668 [Multi-domain]  Cd Length: 75  Bit Score: 94.02  E-value: 3.74e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612660551  155 VNDHLKQIAQRESGGNIhAVNPTSGAAGKYQFLQSTWDSVAPAKYKGvSPANAPESVQDAAAVKLYNTGGAGHWVTA 231
Cdd:pfam06737   1 DNSNWDAIAQCESGGNW-AINTGNGYYGGLQFSQSTWDAYGGLGYAP-SAAQASREQQIAVAEKLLATQGAGAWPTC 75
 
Name Accession Description Interval E-value
Transglycosylas pfam06737
Transglycosylase-like domain; This family of proteins are very likely to act as ...
155-231 3.74e-25

Transglycosylase-like domain; This family of proteins are very likely to act as transglycosylase enzymes related to pfam00062 and pfam01464. These other families are weakly matched by this family, and include the known active site residues.


Pssm-ID: 399604 [Multi-domain]  Cd Length: 75  Bit Score: 94.02  E-value: 3.74e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612660551  155 VNDHLKQIAQRESGGNIhAVNPTSGAAGKYQFLQSTWDSVAPAKYKGvSPANAPESVQDAAAVKLYNTGGAGHWVTA 231
Cdd:pfam06737   1 DNSNWDAIAQCESGGNW-AINTGNGYYGGLQFSQSTWDAYGGLGYAP-SAAQASREQQIAVAEKLLATQGAGAWPTC 75
RPF cd13925
core lysozyme-like domain of resuscitation-promoting factor proteins; Resuscitation-promoting ...
157-230 2.69e-18

core lysozyme-like domain of resuscitation-promoting factor proteins; Resuscitation-promoting factor (RPF) proteins, found in various (G+C)-rich Gram-positive bacteria, act to reactivate cultures from stationary phase. This protein shares elements of the structural core of lysozyme and related proteins. Furthermore, it shares a conserved active site glutamate which is required for activity, and has a polysaccharide binding cleft that corresponds to the peptidoglycan binding cleft of lysozyme. Muralytic activity of Rpf in Micrococcus luteus correlates with resuscitation, supporting a mechanism dependent on cleavage of peptidoglycan by RPF.


Pssm-ID: 381607 [Multi-domain]  Cd Length: 71  Bit Score: 75.88  E-value: 2.69e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612660551 157 DHLKQIAQRESGGNIHAVNPTSGAAGKYQFLQSTWDSVAPAKYkgvsPANAPESVQDAAAVKLYNTGGAGHWVT 230
Cdd:cd13925    1 SQWDAIAQCESGGNWNAVNTGNGYYGGLQFLQGTWKSVGGLGY----PDDATRAEQITRAERLYARQGAGAWPC 70
COG4678 COG4678
Muramidase (phage lambda lysozyme) [Cell wall/membrane/envelope biogenesis, Mobilome: ...
175-225 4.39e-06

Muramidase (phage lambda lysozyme) [Cell wall/membrane/envelope biogenesis, Mobilome: prophages, transposons];


Pssm-ID: 443714  Cd Length: 166  Bit Score: 45.30  E-value: 4.39e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 612660551 175 NPTSGAAGKYQFLQSTWDSVAPaKYKgvSPANAPESvQDAAAVKLYNTGGA 225
Cdd:COG4678   68 GNCSTAAGRYQFLNTTWDEYAK-KLG--LPDFSPES-QDRVALQLLRDRGA 114
 
Name Accession Description Interval E-value
Transglycosylas pfam06737
Transglycosylase-like domain; This family of proteins are very likely to act as ...
155-231 3.74e-25

Transglycosylase-like domain; This family of proteins are very likely to act as transglycosylase enzymes related to pfam00062 and pfam01464. These other families are weakly matched by this family, and include the known active site residues.


Pssm-ID: 399604 [Multi-domain]  Cd Length: 75  Bit Score: 94.02  E-value: 3.74e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612660551  155 VNDHLKQIAQRESGGNIhAVNPTSGAAGKYQFLQSTWDSVAPAKYKGvSPANAPESVQDAAAVKLYNTGGAGHWVTA 231
Cdd:pfam06737   1 DNSNWDAIAQCESGGNW-AINTGNGYYGGLQFSQSTWDAYGGLGYAP-SAAQASREQQIAVAEKLLATQGAGAWPTC 75
RPF cd13925
core lysozyme-like domain of resuscitation-promoting factor proteins; Resuscitation-promoting ...
157-230 2.69e-18

core lysozyme-like domain of resuscitation-promoting factor proteins; Resuscitation-promoting factor (RPF) proteins, found in various (G+C)-rich Gram-positive bacteria, act to reactivate cultures from stationary phase. This protein shares elements of the structural core of lysozyme and related proteins. Furthermore, it shares a conserved active site glutamate which is required for activity, and has a polysaccharide binding cleft that corresponds to the peptidoglycan binding cleft of lysozyme. Muralytic activity of Rpf in Micrococcus luteus correlates with resuscitation, supporting a mechanism dependent on cleavage of peptidoglycan by RPF.


Pssm-ID: 381607 [Multi-domain]  Cd Length: 71  Bit Score: 75.88  E-value: 2.69e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612660551 157 DHLKQIAQRESGGNIHAVNPTSGAAGKYQFLQSTWDSVAPAKYkgvsPANAPESVQDAAAVKLYNTGGAGHWVT 230
Cdd:cd13925    1 SQWDAIAQCESGGNWNAVNTGNGYYGGLQFLQGTWKSVGGLGY----PDDATRAEQITRAERLYARQGAGAWPC 70
COG4678 COG4678
Muramidase (phage lambda lysozyme) [Cell wall/membrane/envelope biogenesis, Mobilome: ...
175-225 4.39e-06

Muramidase (phage lambda lysozyme) [Cell wall/membrane/envelope biogenesis, Mobilome: prophages, transposons];


Pssm-ID: 443714  Cd Length: 166  Bit Score: 45.30  E-value: 4.39e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 612660551 175 NPTSGAAGKYQFLQSTWDSVAPaKYKgvSPANAPESvQDAAAVKLYNTGGA 225
Cdd:COG4678   68 GNCSTAAGRYQFLNTTWDEYAK-KLG--LPDFSPES-QDRVALQLLRDRGA 114
lambda_lys-like cd00736
Bacteriophage lambda lysozyme and similar proteins; Lysozyme from bacteriophage lambda ...
157-219 4.39e-06

Bacteriophage lambda lysozyme and similar proteins; Lysozyme from bacteriophage lambda hydrolyzes the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc), as do other lysozymes. However, unlike other lysozymes, bacteriophage lambda does not produce a reducing end upon cleavage of the peptidoglycan, but rather uses the 6-OH of the same MurNAc residue to produce a 1,6-anhydromuramic acid terminal residue and is therefore a lytic transglycosylase. An identical 1,6-anhydro bond is formed in bacterial peptidoglycans by the action of the lytic transglycosylases of E. coli, though they differ structurally.


Pssm-ID: 381598  Cd Length: 141  Bit Score: 44.84  E-value: 4.39e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612660551 157 DHLKQIAQRESGGNihavnpTSGAAGKYQFLQSTWDSVAPA-KYKGVSPANapesvQDAAAVKL 219
Cdd:cd00736   36 DHPRILVCRKGGGL------KSTAAGAYQFLGRTWDDLAKQlGLPDFSPES-----QDLAAIAL 88
 
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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