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Conserved domains on  [gi|5822354|pdb|1QT4|A]
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Chain A, T26q Mutant Of T4 Lysozyme

Protein Classification

bacteriophage_T4-like_lysozyme domain-containing protein (domain architecture ID 10091399)

bacteriophage_T4-like_lysozyme domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
T4_like_lys cd00735
Bacteriophage T4-like lysozymes; Bacteriophage T4-like lysozymes hydrolyze the beta-1, ...
2-160 6.41e-80

Bacteriophage T4-like lysozymes; Bacteriophage T4-like lysozymes hydrolyze the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) in peptidoglycan heteropolymers of prokaryotic cell walls. Members include a variety of bacteriophages (T4, RB49, RB69, Aeh1), as well as Dictyostelium.


:

Pssm-ID: 340361  Cd Length: 156  Bit Score: 233.43  E-value: 6.41e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QT4_A        2 NIFEMLRIDEGLRLKIYKDTEGYYQIGIGHLLTKSPSLNAAKselDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRN 81
Cdd:cd00735   1 TIFEMLRYDEGERLKPYKDTEGYPTIGIGHLIGKKPARDAAI---DKAEGSLKNGTITKDEAEKLFEQDVADAVRDMLRN 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1QT4_A       82 AKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDA 160
Cdd:cd00735  78 PKLSPVYAQLNAVRRMALINMAFQMGVTGVAKFKNMLAALEAGDWDEAADELLNSLWAKQTPNRANRVSAVIRTGTWDS 156
 
Name Accession Description Interval E-value
T4_like_lys cd00735
Bacteriophage T4-like lysozymes; Bacteriophage T4-like lysozymes hydrolyze the beta-1, ...
2-160 6.41e-80

Bacteriophage T4-like lysozymes; Bacteriophage T4-like lysozymes hydrolyze the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) in peptidoglycan heteropolymers of prokaryotic cell walls. Members include a variety of bacteriophages (T4, RB49, RB69, Aeh1), as well as Dictyostelium.


Pssm-ID: 340361  Cd Length: 156  Bit Score: 233.43  E-value: 6.41e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QT4_A        2 NIFEMLRIDEGLRLKIYKDTEGYYQIGIGHLLTKSPSLNAAKselDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRN 81
Cdd:cd00735   1 TIFEMLRYDEGERLKPYKDTEGYPTIGIGHLIGKKPARDAAI---DKAEGSLKNGTITKDEAEKLFEQDVADAVRDMLRN 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1QT4_A       82 AKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDA 160
Cdd:cd00735  78 PKLSPVYAQLNAVRRMALINMAFQMGVTGVAKFKNMLAALEAGDWDEAADELLNSLWAKQTPNRANRVSAVIRTGTWDS 156
5 PHA02596
baseplate hub subunit and tail lysozyme; Provisional
1-161 2.40e-53

baseplate hub subunit and tail lysozyme; Provisional


Pssm-ID: 222900 [Multi-domain]  Cd Length: 576  Bit Score: 177.25  E-value: 2.40e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QT4_A         1 MNIFEMLRIDEGLRLKIYKDTEGYYQIGIGHLLTKSPSLNAAK--SELDKAIGRN-TNGVITKDEAEKLFNQDVDAAVRG 77
Cdd:PHA02596 173 FTIEKMLRRDEGIRLKVYWDSEGYPTIGIGHLIIREKTRDMAQinKLLSKQVGREvTGGRITAEEASKLFARDLAKVQRD 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QT4_A        78 ILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGT 157
Cdd:PHA02596 253 ISRHSKVGPVYNKLNRSRQMALENMAFQMGVGGVAKFKNMLAAMLAGDWKKAYDALRDSLWANQTPGRASRVSKIILTGN 332

                 ....
1QT4_A       158 WDAY 161
Cdd:PHA02596 333 LESY 336
Phage_lysozyme pfam00959
Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.
24-148 9.48e-22

Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.


Pssm-ID: 334329  Cd Length: 108  Bit Score: 83.94  E-value: 9.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QT4_A         24 YYQIGIGHlltKSPSLNAAKSeldkaigrntngvITKDEAEKLFNQDVDAAVRGILRNAKLKpvydSLDAVRRAALINMV 103
Cdd:pfam00959   1 YWTIGIGH---NGKDVSPHPR-------------LTKSEAAGRLQIDLRTAERCINQYGKGY----DFNPNQQDALVSLA 60
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
1QT4_A        104 FQMGEtGVAGFTNSLRMLQQKRWDEAAVNLAKSR----WYNQTPNRAKR 148
Cdd:pfam00959  61 FNVGC-GKRGFSTLLRAGNIGQWIKACSAIWKSLkagkVYNGLVNRREK 108
RrrD COG3772
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];
11-148 3.17e-03

Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 226295  Cd Length: 152  Bit Score: 35.82  E-value: 3.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QT4_A       11 EGLRLKIYKDTEGYYQIGIGHLL-TKSPSLNAAKSELDKAIGRNTNgvitkdeaeklfnqDVDAAvrgilrNAKLKPVYD 89
Cdd:COG3772  19 EGCRLDPYRDPAGVWTIGYGHTGkPVGPGMTLTKEECDQANALERD--------------LAEAE------RAVNRYIKV 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
1QT4_A       90 SLDAVRRAALINMVFQMGeTGVAGFTNSLRMLQQKRWDEAAVNLaksRWYNQTPNRAKR 148
Cdd:COG3772  79 PLTQPQFDALVSFAYNIG-AGNFFSSTLLRRINAGDWSGACEQL---RRWIKAGGGKVL 133
 
Name Accession Description Interval E-value
T4_like_lys cd00735
Bacteriophage T4-like lysozymes; Bacteriophage T4-like lysozymes hydrolyze the beta-1, ...
2-160 6.41e-80

Bacteriophage T4-like lysozymes; Bacteriophage T4-like lysozymes hydrolyze the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) in peptidoglycan heteropolymers of prokaryotic cell walls. Members include a variety of bacteriophages (T4, RB49, RB69, Aeh1), as well as Dictyostelium.


Pssm-ID: 340361  Cd Length: 156  Bit Score: 233.43  E-value: 6.41e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QT4_A        2 NIFEMLRIDEGLRLKIYKDTEGYYQIGIGHLLTKSPSLNAAKselDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRN 81
Cdd:cd00735   1 TIFEMLRYDEGERLKPYKDTEGYPTIGIGHLIGKKPARDAAI---DKAEGSLKNGTITKDEAEKLFEQDVADAVRDMLRN 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1QT4_A       82 AKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDA 160
Cdd:cd00735  78 PKLSPVYAQLNAVRRMALINMAFQMGVTGVAKFKNMLAALEAGDWDEAADELLNSLWAKQTPNRANRVSAVIRTGTWDS 156
5 PHA02596
baseplate hub subunit and tail lysozyme; Provisional
1-161 2.40e-53

baseplate hub subunit and tail lysozyme; Provisional


Pssm-ID: 222900 [Multi-domain]  Cd Length: 576  Bit Score: 177.25  E-value: 2.40e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QT4_A         1 MNIFEMLRIDEGLRLKIYKDTEGYYQIGIGHLLTKSPSLNAAK--SELDKAIGRN-TNGVITKDEAEKLFNQDVDAAVRG 77
Cdd:PHA02596 173 FTIEKMLRRDEGIRLKVYWDSEGYPTIGIGHLIIREKTRDMAQinKLLSKQVGREvTGGRITAEEASKLFARDLAKVQRD 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QT4_A        78 ILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGT 157
Cdd:PHA02596 253 ISRHSKVGPVYNKLNRSRQMALENMAFQMGVGGVAKFKNMLAAMLAGDWKKAYDALRDSLWANQTPGRASRVSKIILTGN 332

                 ....
1QT4_A       158 WDAY 161
Cdd:PHA02596 333 LESY 336
Phage_lysozyme pfam00959
Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.
24-148 9.48e-22

Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.


Pssm-ID: 334329  Cd Length: 108  Bit Score: 83.94  E-value: 9.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QT4_A         24 YYQIGIGHlltKSPSLNAAKSeldkaigrntngvITKDEAEKLFNQDVDAAVRGILRNAKLKpvydSLDAVRRAALINMV 103
Cdd:pfam00959   1 YWTIGIGH---NGKDVSPHPR-------------LTKSEAAGRLQIDLRTAERCINQYGKGY----DFNPNQQDALVSLA 60
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
1QT4_A        104 FQMGEtGVAGFTNSLRMLQQKRWDEAAVNLAKSR----WYNQTPNRAKR 148
Cdd:pfam00959  61 FNVGC-GKRGFSTLLRAGNIGQWIKACSAIWKSLkagkVYNGLVNRREK 108
lyz_endolysin_autolysin cd00737
endolysin and autolysin; The dsDNA phages of eubacteria use endolysins or muralytic enzymes in ...
4-138 1.12e-19

endolysin and autolysin; The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.


Pssm-ID: 340363  Cd Length: 136  Bit Score: 79.48  E-value: 1.12e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QT4_A        4 FEMLRIDEGLRLKIYKDTEGYYQIGIGHLLTKspslnaakseldkaiGRNTNGVITKDEAEKLFNQDVDAAVRGILRNAK 83
Cdd:cd00737   2 LDLIKEFEGLRLKAYRDPAGVWTIGYGHTGGV---------------GVKPGDTITEAQAEALLRQDLARFEAAVNRLVK 66
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
1QT4_A       84 LkpvydSLDAVRRAALINMVFQMGETGVAGFTnSLRMLQQKRWDEAAVNLAksRW 138
Cdd:cd00737  67 V-----PLNQNQFDALVSFAFNVGAGAFKSST-LLRKLNAGDYAGAADEFL--RW 113
endolysin_R21_like cd16900
endolysin R21-like proteins; Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria ...
11-129 3.48e-07

endolysin R21-like proteins; Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria phage P21 has an N-terminal SAR (signal-arrest-release) domain that anchors the endolysin to the membrane in an inactive form, which act to prevent premature lysis of the infected bacterium. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.


Pssm-ID: 340386  Cd Length: 141  Bit Score: 46.78  E-value: 3.48e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QT4_A       11 EGLRLKIYKDTEGYYQIGIGHlltkspslnaakseldkaigrnTNGVI-----TKDEAEKLFNQDVDAAVRGILRNaklk 85
Cdd:cd16900  16 EGLRLTAYRDPVGVWTVCYGH----------------------TGGVKpgmryTPAECDALLAKDLQEAAAAVDRC---- 69
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
1QT4_A       86 pVYDSLDAVRRAALINMVFQmgeTGVAGFTNS--LRMLQQKRWDEA 129
Cdd:cd16900  70 -VKVPLPDYQRAALASFAYN---VGVGAFCRStlLRKLNAGDRRGA 111
lyz_P1 cd16901
P1 lysozyme Lyz-like proteins; Enterobacteria phage P1 lysozyme Lyz is secreted to the ...
11-129 3.07e-06

P1 lysozyme Lyz-like proteins; Enterobacteria phage P1 lysozyme Lyz is secreted to the Escherichia coli periplasm where it is membrane bound and inactive. Activation involves the release from the membrane, an intramolecular thiol-disulfide isomerization and extensive structural rearrangement of the N-terminal region. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.


Pssm-ID: 340387  Cd Length: 140  Bit Score: 44.12  E-value: 3.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QT4_A       11 EGLRLKIYKDTEGYYQIGIGHlltkspslnaakseldkAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKLKP---- 86
Cdd:cd16901  14 EGCRRDPYKCPAGVPTIGIGS-----------------THGVKPGDRYTDEQAAARLAKDIKKAERCLNRCFNGVPlpqg 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
1QT4_A       87 VYDsldavrraALINMVFQMGETGVAGfTNSLRMLQQKRWDEA 129
Cdd:cd16901  77 EFD--------AYVSFAFNVGCGAFCR-STIVKKLQAGDYAAA 110
RrrD COG3772
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];
11-148 3.17e-03

Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 226295  Cd Length: 152  Bit Score: 35.82  E-value: 3.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QT4_A       11 EGLRLKIYKDTEGYYQIGIGHLL-TKSPSLNAAKSELDKAIGRNTNgvitkdeaeklfnqDVDAAvrgilrNAKLKPVYD 89
Cdd:COG3772  19 EGCRLDPYRDPAGVWTIGYGHTGkPVGPGMTLTKEECDQANALERD--------------LAEAE------RAVNRYIKV 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
1QT4_A       90 SLDAVRRAALINMVFQMGeTGVAGFTNSLRMLQQKRWDEAAVNLaksRWYNQTPNRAKR 148
Cdd:COG3772  79 PLTQPQFDALVSFAYNIG-AGNFFSSTLLRRINAGDWSGACEQL---RRWIKAGGGKVL 133
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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