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Conserved domains on  [gi|1570653301|gb|RYR82936|]
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CHAP domain-containing protein [Staphylococcus pseudintermedius]

Protein Classification

glucosaminidase domain-containing protein( domain architecture ID 12062372)

glucosaminidase domain-containing protein such as Staphylococcus aureus N-acetylglucosaminidase autolysin E (AtlE), which is involved in the degradation of cell wall peptidoglycan; contains an N-terminal CHAP domain

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LytD COG4193
Beta- N-acetylglucosaminidase [Carbohydrate transport and metabolism];
378-628 4.49e-71

Beta- N-acetylglucosaminidase [Carbohydrate transport and metabolism];


:

Pssm-ID: 443347 [Multi-domain]  Cd Length: 423  Bit Score: 236.02  E-value: 4.49e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570653301 378 VKENTKFVPSELKPSNNIEDKQDSKIDRIISNYSLKQALDIQFRLnpKPQTSNGVTWYTASLNQAREAMDTNKIFNNNVQ 457
Cdd:COG4193   163 VGGVAVYVDADWLNVIPTESVPGGNLKHNSYNHSLKSAAAKQYSY--SWMYYDGGGWYSASGSDIAYYMDPRNFLNDEYN 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570653301 458 VYQFLKLNQYQGISVDKLNKLLVG---KGTLQNQGQAFADGCKKYGVNEIYLIAHAFLESANGTSFFASGRT----GVYN 530
Cdd:COG4193   241 YFQFLDLRYSSNYSAEELNKYLKGtftKGILIGKGQAFIEAAKKYGVNPLYLASHALLETGNGTSKLAKGVEvngkTYYN 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570653301 531 YFGIGAFDNNP-NNAMEFARSHGWTSPAKAIIGGAEFVGKGYFD---VGQNTLYRMRWNPKKPGT-HQYATDISWAKVQA 605
Cdd:COG4193   321 LFGIGAYDSNPlENGAKYAYKQGWTSPEKAIVGGAKFIGSNYINntgYGQNTLYKMRWNPVNPGTnHQYATDPFWAEKIA 400
                         250       260
                  ....*....|....*....|...
gi 1570653301 606 KMISTMYKEIGLKGEYFIYDQYK 628
Cdd:COG4193   401 GHMYRAYKKLKDYNLYFDIPVYK 423
CHAP pfam05257
CHAP domain; This domain corresponds to an amidase function. Many of these proteins are ...
27-118 8.81e-11

CHAP domain; This domain corresponds to an amidase function. Many of these proteins are involved in cell wall metabolism of bacteria. This domain is found at the N-terminus of Swiss:P43675, where it functions as a glutathionylspermidine amidase EC:3.5.1.78. This domain is found to be the catalytic domain of PlyCA. CHAP is the amidase domain of bifunctional Escherichia coli glutathionylspermidine synthetase/amidase, and it catalyzes the hydrolysis of Gsp (glutathionylspermidine) into glutathione and spermidine.


:

Pssm-ID: 461605 [Multi-domain]  Cd Length: 83  Bit Score: 58.20  E-value: 8.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570653301  27 DVDGYYGRQCWDLPNYIFNRYWGFktPGNARDmaWYRYPAGfkiYRKTSSFIPKPGDIAIWTGGNYNwNTWGHTGIVVGp 106
Cdd:pfam05257   1 YGNGYPWGQCTWFVYWRVAQLGIY--LGNAGD--WADAAAG---AYKVGSTTPKVGDIVVFDPGGGG-ASYGHVAIVEK- 71
                          90
                  ....*....|..
gi 1570653301 107 STKDYFYSVDQN 118
Cdd:pfam05257  72 VNDGSITVSEQN 83
 
Name Accession Description Interval E-value
LytD COG4193
Beta- N-acetylglucosaminidase [Carbohydrate transport and metabolism];
378-628 4.49e-71

Beta- N-acetylglucosaminidase [Carbohydrate transport and metabolism];


Pssm-ID: 443347 [Multi-domain]  Cd Length: 423  Bit Score: 236.02  E-value: 4.49e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570653301 378 VKENTKFVPSELKPSNNIEDKQDSKIDRIISNYSLKQALDIQFRLnpKPQTSNGVTWYTASLNQAREAMDTNKIFNNNVQ 457
Cdd:COG4193   163 VGGVAVYVDADWLNVIPTESVPGGNLKHNSYNHSLKSAAAKQYSY--SWMYYDGGGWYSASGSDIAYYMDPRNFLNDEYN 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570653301 458 VYQFLKLNQYQGISVDKLNKLLVG---KGTLQNQGQAFADGCKKYGVNEIYLIAHAFLESANGTSFFASGRT----GVYN 530
Cdd:COG4193   241 YFQFLDLRYSSNYSAEELNKYLKGtftKGILIGKGQAFIEAAKKYGVNPLYLASHALLETGNGTSKLAKGVEvngkTYYN 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570653301 531 YFGIGAFDNNP-NNAMEFARSHGWTSPAKAIIGGAEFVGKGYFD---VGQNTLYRMRWNPKKPGT-HQYATDISWAKVQA 605
Cdd:COG4193   321 LFGIGAYDSNPlENGAKYAYKQGWTSPEKAIVGGAKFIGSNYINntgYGQNTLYKMRWNPVNPGTnHQYATDPFWAEKIA 400
                         250       260
                  ....*....|....*....|...
gi 1570653301 606 KMISTMYKEIGLKGEYFIYDQYK 628
Cdd:COG4193   401 GHMYRAYKKLKDYNLYFDIPVYK 423
LYZ2 smart00047
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
477-613 4.04e-40

Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.


Pssm-ID: 214488 [Multi-domain]  Cd Length: 147  Bit Score: 143.35  E-value: 4.04e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570653301  477 KLLVGKGTLQNQGQAFADGCKKYGVNEIY---LIAHAFLESANGTSFFAsgrTGVYNYFGI-GAFDNNPNNAM-EFARSH 551
Cdd:smart00047   1 KLLAGGSTLEFVGKIFNEAQKAYQINGVYpsiLIAQAALESGWGTSKLA---KKYNNLFGIkGAYDGRPVRMGtLEYLNG 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1570653301  552 GWTSPAKAIIG--GAEFVGKGYFDVGQNTLYRMRWNPKKPGTHQYATDISWAKVQAKMISTMYK 613
Cdd:smart00047  78 GWVTVKAAFRGyfGEKFIDYAYVLRGQNPLYKKRWGSNALQTAGYATDPDYAKKLIRIIALYDE 141
CHAP pfam05257
CHAP domain; This domain corresponds to an amidase function. Many of these proteins are ...
27-118 8.81e-11

CHAP domain; This domain corresponds to an amidase function. Many of these proteins are involved in cell wall metabolism of bacteria. This domain is found at the N-terminus of Swiss:P43675, where it functions as a glutathionylspermidine amidase EC:3.5.1.78. This domain is found to be the catalytic domain of PlyCA. CHAP is the amidase domain of bifunctional Escherichia coli glutathionylspermidine synthetase/amidase, and it catalyzes the hydrolysis of Gsp (glutathionylspermidine) into glutathione and spermidine.


Pssm-ID: 461605 [Multi-domain]  Cd Length: 83  Bit Score: 58.20  E-value: 8.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570653301  27 DVDGYYGRQCWDLPNYIFNRYWGFktPGNARDmaWYRYPAGfkiYRKTSSFIPKPGDIAIWTGGNYNwNTWGHTGIVVGp 106
Cdd:pfam05257   1 YGNGYPWGQCTWFVYWRVAQLGIY--LGNAGD--WADAAAG---AYKVGSTTPKVGDIVVFDPGGGG-ASYGHVAIVEK- 71
                          90
                  ....*....|..
gi 1570653301 107 STKDYFYSVDQN 118
Cdd:pfam05257  72 VNDGSITVSEQN 83
Glucosaminidase pfam01832
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ...
489-562 2.56e-08

Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase EC:3.2.1.96. As well as the flageller protein J that has been shown to hydrolyse peptidoglycan.


Pssm-ID: 460354 [Multi-domain]  Cd Length: 91  Bit Score: 51.80  E-value: 2.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570653301 489 GQAFADGCKKYGVNEIYLIAHAFLESANGTSFFAsgrTGVYNYFGIGA-------FDNNPNNAMEFARShgWTSPAKAII 561
Cdd:pfam01832   1 APAAIEAAKKYGIPASVLLAQAALESGWGTSRLA---KESNNLFGIKAswkgkvaYDTDEVTVAARFRK--YDSVEESIR 75

                  .
gi 1570653301 562 G 562
Cdd:pfam01832  76 D 76
 
Name Accession Description Interval E-value
LytD COG4193
Beta- N-acetylglucosaminidase [Carbohydrate transport and metabolism];
378-628 4.49e-71

Beta- N-acetylglucosaminidase [Carbohydrate transport and metabolism];


Pssm-ID: 443347 [Multi-domain]  Cd Length: 423  Bit Score: 236.02  E-value: 4.49e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570653301 378 VKENTKFVPSELKPSNNIEDKQDSKIDRIISNYSLKQALDIQFRLnpKPQTSNGVTWYTASLNQAREAMDTNKIFNNNVQ 457
Cdd:COG4193   163 VGGVAVYVDADWLNVIPTESVPGGNLKHNSYNHSLKSAAAKQYSY--SWMYYDGGGWYSASGSDIAYYMDPRNFLNDEYN 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570653301 458 VYQFLKLNQYQGISVDKLNKLLVG---KGTLQNQGQAFADGCKKYGVNEIYLIAHAFLESANGTSFFASGRT----GVYN 530
Cdd:COG4193   241 YFQFLDLRYSSNYSAEELNKYLKGtftKGILIGKGQAFIEAAKKYGVNPLYLASHALLETGNGTSKLAKGVEvngkTYYN 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570653301 531 YFGIGAFDNNP-NNAMEFARSHGWTSPAKAIIGGAEFVGKGYFD---VGQNTLYRMRWNPKKPGT-HQYATDISWAKVQA 605
Cdd:COG4193   321 LFGIGAYDSNPlENGAKYAYKQGWTSPEKAIVGGAKFIGSNYINntgYGQNTLYKMRWNPVNPGTnHQYATDPFWAEKIA 400
                         250       260
                  ....*....|....*....|...
gi 1570653301 606 KMISTMYKEIGLKGEYFIYDQYK 628
Cdd:COG4193   401 GHMYRAYKKLKDYNLYFDIPVYK 423
LYZ2 smart00047
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
477-613 4.04e-40

Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.


Pssm-ID: 214488 [Multi-domain]  Cd Length: 147  Bit Score: 143.35  E-value: 4.04e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570653301  477 KLLVGKGTLQNQGQAFADGCKKYGVNEIY---LIAHAFLESANGTSFFAsgrTGVYNYFGI-GAFDNNPNNAM-EFARSH 551
Cdd:smart00047   1 KLLAGGSTLEFVGKIFNEAQKAYQINGVYpsiLIAQAALESGWGTSKLA---KKYNNLFGIkGAYDGRPVRMGtLEYLNG 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1570653301  552 GWTSPAKAIIG--GAEFVGKGYFDVGQNTLYRMRWNPKKPGTHQYATDISWAKVQAKMISTMYK 613
Cdd:smart00047  78 GWVTVKAAFRGyfGEKFIDYAYVLRGQNPLYKKRWGSNALQTAGYATDPDYAKKLIRIIALYDE 141
CHAP pfam05257
CHAP domain; This domain corresponds to an amidase function. Many of these proteins are ...
27-118 8.81e-11

CHAP domain; This domain corresponds to an amidase function. Many of these proteins are involved in cell wall metabolism of bacteria. This domain is found at the N-terminus of Swiss:P43675, where it functions as a glutathionylspermidine amidase EC:3.5.1.78. This domain is found to be the catalytic domain of PlyCA. CHAP is the amidase domain of bifunctional Escherichia coli glutathionylspermidine synthetase/amidase, and it catalyzes the hydrolysis of Gsp (glutathionylspermidine) into glutathione and spermidine.


Pssm-ID: 461605 [Multi-domain]  Cd Length: 83  Bit Score: 58.20  E-value: 8.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570653301  27 DVDGYYGRQCWDLPNYIFNRYWGFktPGNARDmaWYRYPAGfkiYRKTSSFIPKPGDIAIWTGGNYNwNTWGHTGIVVGp 106
Cdd:pfam05257   1 YGNGYPWGQCTWFVYWRVAQLGIY--LGNAGD--WADAAAG---AYKVGSTTPKVGDIVVFDPGGGG-ASYGHVAIVEK- 71
                          90
                  ....*....|..
gi 1570653301 107 STKDYFYSVDQN 118
Cdd:pfam05257  72 VNDGSITVSEQN 83
Glucosaminidase pfam01832
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ...
489-562 2.56e-08

Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase EC:3.2.1.96. As well as the flageller protein J that has been shown to hydrolyse peptidoglycan.


Pssm-ID: 460354 [Multi-domain]  Cd Length: 91  Bit Score: 51.80  E-value: 2.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570653301 489 GQAFADGCKKYGVNEIYLIAHAFLESANGTSFFAsgrTGVYNYFGIGA-------FDNNPNNAMEFARShgWTSPAKAII 561
Cdd:pfam01832   1 APAAIEAAKKYGIPASVLLAQAALESGWGTSRLA---KESNNLFGIKAswkgkvaYDTDEVTVAARFRK--YDSVEESIR 75

                  .
gi 1570653301 562 G 562
Cdd:pfam01832  76 D 76
 
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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