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Conserved domains on  [gi|584796419|gb|EWJ22550|]
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LysM domain-containing protein [Staphylococcus aureus M77225]

Protein Classification

COG3942 and LysM peptidoglycan-binding domain-containing protein( domain architecture ID 17581670)

COG3942 surface antigen and LysM peptidoglycan-binding domain-containing protein may bind N-acetylglucosamine in carbohydrates such as chitin, chitio-oligosaccharides and peptidoglycan;

CATH:  3.10.350.10
Gene Ontology:  GO:0097367
PubMed:  18430080|24652063
SCOP:  4000905

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG3942 COG3942
Surface antigen [Cell wall/membrane/envelope biogenesis];
159-279 7.55e-51

Surface antigen [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 443142 [Multi-domain]  Cd Length: 129  Bit Score: 163.24  E-value: 7.55e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796419 159 PTVPVAHNYNKSVANRGNLYAYGNCTYYAFDRRAQLGRSIGSLWGNANNWNYAAKVAGFKVDKTPEVGAIFQTA---AGP 235
Cdd:COG3942    2 RAASLGDGYPPNVVDPWNGYPYGQCTWYAAWRRAQLGGPIGSGWGNANNWADNARAAGYTVGSTPKVGAVAVFTpgvAGP 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 584796419 236 YGHVGVVESVNPNGTITVSEMNYAGFNVKSSRTIL--NPGKYNYIH 279
Cdd:COG3942   82 YGHVAVVESVNSDGSILVSEMNWGGPGIYSTRTISagNASSYGFIH 127
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 51-94 1.97e-10

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


:

Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 54.80  E-value: 1.97e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 584796419  51 TTYTVVAGDSLYKIALEHHLTLNQLYSYNPGVTP-LIFPGDVISL 94
Cdd:cd00118    1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPdCIYPGQKLKI 45
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
8-92 3.09e-06

LysM repeat [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 46.24  E-value: 3.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796419   8 TVSSVLAFLALNNAAHAQQHGTQVKTPVQHNYVSNVQAQTQSPTTYTVVAGDSLYKIALEHHLTLNQLYSYNPGVTPLIF 87
Cdd:COG1388   67 AAKAALAAAPEAAAAAAARYTVKSGDTLSGIARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIR 146


                 ....*
gi 584796419  88 PGDVI 92
Cdd:COG1388  147 PGQKL 151
 
Name Accession Description Interval E-value
COG3942 COG3942
Surface antigen [Cell wall/membrane/envelope biogenesis];
159-279 7.55e-51

Surface antigen [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443142 [Multi-domain]  Cd Length: 129  Bit Score: 163.24  E-value: 7.55e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796419 159 PTVPVAHNYNKSVANRGNLYAYGNCTYYAFDRRAQLGRSIGSLWGNANNWNYAAKVAGFKVDKTPEVGAIFQTA---AGP 235
Cdd:COG3942    2 RAASLGDGYPPNVVDPWNGYPYGQCTWYAAWRRAQLGGPIGSGWGNANNWADNARAAGYTVGSTPKVGAVAVFTpgvAGP 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 584796419 236 YGHVGVVESVNPNGTITVSEMNYAGFNVKSSRTIL--NPGKYNYIH 279
Cdd:COG3942   82 YGHVAVVESVNSDGSILVSEMNWGGPGIYSTRTISagNASSYGFIH 127
PRK08581 PRK08581
amidase domain-containing protein;
178-269 8.70e-23

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 97.55  E-value: 8.70e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796419 178 YAYGNCTYYAFDRRAQLGRSIGSLWGNANNWNYAAKVAGFKVDKTPEVGA--IF---QTAAGP-YGHVGVVESVNPNGTI 251
Cdd:PRK08581 508 YPHGQCTWYVYNRMKQFGTSISGDLGDAHNWNNRAQARGYQVSHTPKRHAavVFeagQAGADQhYGHVAFVEKVNSDGSI 587

                         90
                 ....*....|....*...
gi 584796419 252 TVSEMNYAGFNVKSSRTI 269
Cdd:PRK08581 588 VISESNVKGLGIISYRTI 605
CHAP pfam05257
CHAP domain; This domain corresponds to an amidase function. Many of these proteins are ...
 175-257 2.61e-21

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: 85.55  E-value: 2.61e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796419  175 GNLYAYGNCTYYAFDRRAQLGRsigsLWGNANNWNYAAKvAGFKVDK-TPEVGAIFQTAAG----PYGHVGVVESVNpNG 249
Cdd:pfam05257   2 GNGYPWGQCTWFVYWRVAQLGI----YLGNAGDWADAAA-GAYKVGStTPKVGDIVVFDPGgggaSYGHVAIVEKVN-DG 75


                  ....*...
gi 584796419  250 TITVSEMN 257
Cdd:pfam05257  76 SITVSEQN 83
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 51-94 1.97e-10

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 54.80  E-value: 1.97e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 584796419  51 TTYTVVAGDSLYKIALEHHLTLNQLYSYNPGVTP-LIFPGDVISL 94
Cdd:cd00118    1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPdCIYPGQKLKI 45
LysM smart00257
Lysin motif;
52-94 2.15e-07

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 46.28  E-value: 2.15e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 584796419    52 TYTVVAGDSLYKIALEHHLTLNQLYSYNPGVTP-LIFPGDVISL 94
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPdNLQVGQKLKI 44
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 53-94 2.50e-07

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 46.24  E-value: 2.50e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 584796419   53 YTVVAGDSLYKIALEHHLTLNQLYSYNPGVTPLIFPGDVISL 94
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKI 42
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
8-92 3.09e-06

LysM repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 46.24  E-value: 3.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796419   8 TVSSVLAFLALNNAAHAQQHGTQVKTPVQHNYVSNVQAQTQSPTTYTVVAGDSLYKIALEHHLTLNQLYSYNPGVTPLIF 87
Cdd:COG1388   67 AAKAALAAAPEAAAAAAARYTVKSGDTLSGIARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIR 146


                 ....*
gi 584796419  88 PGDVI 92
Cdd:COG1388  147 PGQKL 151
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 33-94 1.70e-05

Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion transport and metabolism];


Pssm-ID: 441258 [Multi-domain]  Cd Length: 163  Bit Score: 44.23  E-value: 1.70e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 584796419  33 TPVQHNYVSNVQAQTQSPTTYTVVAGDSLYKIALEHHLTLNQ---LYSYNPGVTP---LIFPGDVISL 94
Cdd:COG1652   92 TVAEEAAAPSAELAPDAPKTYTVKPGDTLWGIAKRFYGDPARwpeIAEANRDQIKnpdLIYPGQVLRI 159
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 41-99 3.13e-05

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 44.73  E-value: 3.13e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 584796419  41 SNVQAQTQSPTTYTVVAGDSLYKIALEHHLTLNQLYSYNPGVTPLIFPGDVISLVPQNK 99
Cdd:PRK10783 393 AQRLANNSDSITYRVRKGDSLSSIAKRHGVNIKDVMRWNSDTAKNLQPGDKLTLFVKNN 451
 
Name Accession Description Interval E-value
COG3942 COG3942
Surface antigen [Cell wall/membrane/envelope biogenesis];
159-279 7.55e-51

Surface antigen [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443142 [Multi-domain]  Cd Length: 129  Bit Score: 163.24  E-value: 7.55e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796419 159 PTVPVAHNYNKSVANRGNLYAYGNCTYYAFDRRAQLGRSIGSLWGNANNWNYAAKVAGFKVDKTPEVGAIFQTA---AGP 235
Cdd:COG3942    2 RAASLGDGYPPNVVDPWNGYPYGQCTWYAAWRRAQLGGPIGSGWGNANNWADNARAAGYTVGSTPKVGAVAVFTpgvAGP 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 584796419 236 YGHVGVVESVNPNGTITVSEMNYAGFNVKSSRTIL--NPGKYNYIH 279
Cdd:COG3942   82 YGHVAVVESVNSDGSILVSEMNWGGPGIYSTRTISagNASSYGFIH 127
PRK08581 PRK08581
amidase domain-containing protein;
178-269 8.70e-23

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 97.55  E-value: 8.70e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796419 178 YAYGNCTYYAFDRRAQLGRSIGSLWGNANNWNYAAKVAGFKVDKTPEVGA--IF---QTAAGP-YGHVGVVESVNPNGTI 251
Cdd:PRK08581 508 YPHGQCTWYVYNRMKQFGTSISGDLGDAHNWNNRAQARGYQVSHTPKRHAavVFeagQAGADQhYGHVAFVEKVNSDGSI 587

                         90
                 ....*....|....*...
gi 584796419 252 TVSEMNYAGFNVKSSRTI 269
Cdd:PRK08581 588 VISESNVKGLGIISYRTI 605
CHAP pfam05257
CHAP domain; This domain corresponds to an amidase function. Many of these proteins are ...
 175-257 2.61e-21

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: 85.55  E-value: 2.61e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796419  175 GNLYAYGNCTYYAFDRRAQLGRsigsLWGNANNWNYAAKvAGFKVDK-TPEVGAIFQTAAG----PYGHVGVVESVNpNG 249
Cdd:pfam05257   2 GNGYPWGQCTWFVYWRVAQLGI----YLGNAGDWADAAA-GAYKVGStTPKVGDIVVFDPGgggaSYGHVAIVEKVN-DG 75


                  ....*...
gi 584796419  250 TITVSEMN 257
Cdd:pfam05257  76 SITVSEQN 83
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 51-94 1.97e-10

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 54.80  E-value: 1.97e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 584796419  51 TTYTVVAGDSLYKIALEHHLTLNQLYSYNPGVTP-LIFPGDVISL 94
Cdd:cd00118    1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPdCIYPGQKLKI 45
LysM smart00257
Lysin motif;
52-94 2.15e-07

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 46.28  E-value: 2.15e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 584796419    52 TYTVVAGDSLYKIALEHHLTLNQLYSYNPGVTP-LIFPGDVISL 94
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPdNLQVGQKLKI 44
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 53-94 2.50e-07

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 46.24  E-value: 2.50e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 584796419   53 YTVVAGDSLYKIALEHHLTLNQLYSYNPGVTPLIFPGDVISL 94
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKI 42
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
8-92 3.09e-06

LysM repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 46.24  E-value: 3.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796419   8 TVSSVLAFLALNNAAHAQQHGTQVKTPVQHNYVSNVQAQTQSPTTYTVVAGDSLYKIALEHHLTLNQLYSYNPGVTPLIF 87
Cdd:COG1388   67 AAKAALAAAPEAAAAAAARYTVKSGDTLSGIARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIR 146


                 ....*
gi 584796419  88 PGDVI 92
Cdd:COG1388  147 PGQKL 151
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 33-94 1.70e-05

Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion transport and metabolism];


Pssm-ID: 441258 [Multi-domain]  Cd Length: 163  Bit Score: 44.23  E-value: 1.70e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 584796419  33 TPVQHNYVSNVQAQTQSPTTYTVVAGDSLYKIALEHHLTLNQ---LYSYNPGVTP---LIFPGDVISL 94
Cdd:COG1652   92 TVAEEAAAPSAELAPDAPKTYTVKPGDTLWGIAKRFYGDPARwpeIAEANRDQIKnpdLIYPGQVLRI 159
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 41-99 3.13e-05

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 44.73  E-value: 3.13e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 584796419  41 SNVQAQTQSPTTYTVVAGDSLYKIALEHHLTLNQLYSYNPGVTPLIFPGDVISLVPQNK 99
Cdd:PRK10783 393 AQRLANNSDSITYRVRKGDSLSSIAKRHGVNIKDVMRWNSDTAKNLQPGDKLTLFVKNN 451
PRK13914 PRK13914
invasion associated endopeptidase;
21-173 3.18e-05

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 44.79  E-value: 3.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796419  21 AAHAQQHGTQVKTPVQHNYVSNVQAQT-------QSPTTYTVVAGDSLYKIALEHHLTLNQLYSYNPGVTPLIFPGDVIS 93
Cdd:PRK13914 163 AAPAAETKTEVKQTTQATTPAPKVAETketpvvdQNATTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLA 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796419  94 LvpqNKVKQTKAVKSPVR-KASQAKKVVKQPVQQASKKVVVKQAPKQAVTKTVNVAYKPAQVQKSVPTVPVAHNYNKSVA 172
Cdd:PRK13914 243 I---KQTANTATPKAEVKtEAPAAEKQAAPVVKENTNTNTATTEKKETTTQQQTAPKAPTEAAKPAPAPSTNTNANKTNT 319


                 .
gi 584796419 173 N 173
Cdd:PRK13914 320 N 320
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
41-116 7.93e-04

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 40.83  E-value: 7.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796419  41 SNVQAQTQSPTT----YTVVAGDSLYKIALEHHLTLNQLYSYNPGVTPLIFPGDVISLVPQNKVKQTKAVKSPVRKASQA 116
Cdd:PRK06347 466 TNTSKPSTNTNTnakvYTVAKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTTNNTNTAKPSTNKPSNS 545
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
47-89 8.51e-04

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 40.45  E-value: 8.51e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 584796419  47 TQSPTTYTVVAGDSLYKIALEHHLTLNQLYSYNPGVTPLIFPG 89
Cdd:PRK06347 327 TSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPG 369
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
52-89 4.24e-03

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 38.52  E-value: 4.24e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 584796419  52 TYTVVAGDSLYKIALEHHLTLNQLYSYNPGVTPLIFPG 89
Cdd:PRK06347 407 VYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPG 444
 
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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