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Conserved domains on  [gi|1758723744|gb|KAB2504936|]
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N-acetylmuramoyl-L-alanine amidase [Bacillus cereus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CwlA COG5632
N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis];
1-177 1.26e-72

N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 444359  Cd Length: 177  Bit Score: 221.77  E-value: 1.26e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758723744   1 MEIRKNLVDASKYgTKCPYTMNPEFITVHNTYND-ATAANEVAYMIRNDNQVSFHIAVDDKEAVQGIPLERNAWHCGDGG 79
Cdd:COG5632     3 VNIKKKLIPKNNS-YRPGYKMKPKGIVIHNTANPgATAENHANYFNNNNRSASWHYFVDDKEIIQHIPLNENAWHAGDGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758723744  80 GSGNRKSIGVEICYslSGGDRYYKAEDNAAIVVAQLMKQYNIPISKVRTHQSWSGKYCPHRMLAEG--RWNSFIERVQNA 157
Cdd:COG5632    82 GPGNRRSIGIEICE--NKDGDFAKAYENAAELIAYLMKKYGIPIDNVVRHYDWSGKNCPHGLLANGgyRWDQFKADVKSA 159

                         170       180
                  ....*....|....*....|
gi 1758723744 158 YNGSNNPvmqKPTPPSTDGT 177
Cdd:COG5632   160 LNGLSTV---KPYTKVVKAS 176
YgiM COG3103
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ...
 177-302 9.22e-19

Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family [General function prediction only];


:

Pssm-ID: 442337 [Multi-domain]  Cd Length: 119  Bit Score: 80.17  E-value: 9.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758723744 177 TKVAYINGDNVNLRKGPGTGYAVIRKLGKGECYQVWGESNGWLNL----GGDQWVYndSSYIRYTGenatapskssndgi 252
Cdd:COG3103     4 ETRYVVDADALNVRSGPGTSYRIVGTLPKGEKVTVLGRSGGWYKVrysnGKTGWVS--SRYLTVTP-------------- 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1758723744 253 GVVTITADVLRVRTGPGTNYDVVKNVYQGEKYQSWGYRDGWYNVGGDQ--WV 302
Cdd:COG3103    68 SARERLPDELNLRAGPSTSSEVLGLLPKGETVTVLKKSGGWFKVGYRGtgWV 119
 
Name Accession Description Interval E-value
CwlA COG5632
N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis];
1-177 1.26e-72

N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 444359  Cd Length: 177  Bit Score: 221.77  E-value: 1.26e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758723744   1 MEIRKNLVDASKYgTKCPYTMNPEFITVHNTYND-ATAANEVAYMIRNDNQVSFHIAVDDKEAVQGIPLERNAWHCGDGG 79
Cdd:COG5632     3 VNIKKKLIPKNNS-YRPGYKMKPKGIVIHNTANPgATAENHANYFNNNNRSASWHYFVDDKEIIQHIPLNENAWHAGDGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758723744  80 GSGNRKSIGVEICYslSGGDRYYKAEDNAAIVVAQLMKQYNIPISKVRTHQSWSGKYCPHRMLAEG--RWNSFIERVQNA 157
Cdd:COG5632    82 GPGNRRSIGIEICE--NKDGDFAKAYENAAELIAYLMKKYGIPIDNVVRHYDWSGKNCPHGLLANGgyRWDQFKADVKSA 159

                         170       180
                  ....*....|....*....|
gi 1758723744 158 YNGSNNPvmqKPTPPSTDGT 177
Cdd:COG5632   160 LNGLSTV---KPYTKVVKAS 176
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 22-141 2.45e-25

Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in certain cases, hydrolyze peptidoglycans (PGNs) of bacterial cell walls. PGRPs have been divided into three classes: short PGRPs (PGRP-S), that are small (20 kDa) extracellular proteins; intermediate PGRPs (PGRP-I) that are 40-45 kDa and are predicted to be transmembrane proteins; and long PGRPs (PGRP-L), up to 90 kDa, which may be either intracellular or transmembrane. Several structures of PGRPs are known in insects and mammals, some bound with substrates like Muramyl Tripeptide (MTP) or Tracheal Cytotoxin (TCT). The substrate binding site is conserved in PGRP-LCx, PGRP-LE, and PGRP-Ialpha proteins. This family includes Zn-dependent N-Acetylmuramoyl-L-alanine Amidase, EC:3.5.1.28. This enzyme cleaves the amide bond between N-acetylmuramoyl and L-amino acids, preferentially D-lactyl-L-Ala, in bacterial cell walls. The structure for the bacteriophage T7 lysozyme shows that two of the conserved histidines and a cysteine are zinc binding residues. Site-directed mutagenesis of T7 lysozyme indicates that two conserved residues, a Tyr and a Lys, are important for amidase activity.


Pssm-ID: 133475 [Multi-domain]  Cd Length: 126  Bit Score: 98.13  E-value: 2.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758723744  22 NPEFITVHNTYNDA--TAANEVAYM----IRNDNQVSFHIAVD-DKEAVQGIPLERNAWHCGdggGSGNRKSIGVEICYS 94
Cdd:cd06583     1 PVKYVVIHHTANPNcyTAAAAVRYLqnyhMRGWSDISYHFLVGgDGRIYQGRGWNYVGWHAG---GNYNSYSIGIELIGN 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1758723744  95 LSGGDRYYKAEDNAAIVVAQLMKQYNIP-ISKVRTHQSWSG-KYCPHRM 141
Cdd:cd06583    78 FDGGPPTAAQLEALAELLAYLVKRYGIPpDYRIVGHRDVSPgTECPGDA 126
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 22-140 4.89e-25

N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC:3.5.1.28. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls (preferentially: D-lactyl-L-Ala). The structure is known for the bacteriophage T7 structure and shows that two of the conserved histidines are zinc binding.


Pssm-ID: 460236 [Multi-domain]  Cd Length: 122  Bit Score: 97.04  E-value: 4.89e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758723744  22 NPEFITVHNTYNDATAANEVAYM---IRNDNQVSFHIAVDDKEAV-QGIPLERNAWHCGDGGGsgNRKSIGVEICYSLSG 97
Cdd:pfam01510   1 PIRYIVIHHTAGPSFAGALLPYAaciARGWSDVSYHYLIDRDGTIyQLVPENGRAWHAGNGGG--NDRSIGIELEGNFGG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1758723744  98 GDRYYKAEDNAAIVVAQLMKQYNIPI-SKVRTHQSWSGKYCPHR 140
Cdd:pfam01510  79 DPPTDAQYEALARLLADLCKRYGIPPdRRIVGHRDVGRKTDPGP 122
Ami_2 smart00644
Ami_2 domain;
21-138 2.18e-24

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 95.50  E-value: 2.18e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758723744   21 MNPEFITVHNTYND-ATAANEVAYMIRND-NQVSFHIAVD-DKEAVQGIPLERNAWHCGDGG-GSGNRKSIGVEICYSLS 96
Cdd:smart00644   1 PPPRGIVIHHTANSnASCANEARYMQNNHmNDIGYHFLVGgDGRVYQGVGWNYVAWHAGGAHtPGYNDISIGIEFIGSFD 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1758723744   97 GGD-RYYKAEDNAAIVVAQLMKQYNIPIS---KVRTHQSWSGKYCP 138
Cdd:smart00644  81 SDDePFAEALYAALDLLAKLLKGAGLPPDgryRIVGHRDVAPTEDP 126
YgiM COG3103
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ...
 177-302 9.22e-19

Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family [General function prediction only];


Pssm-ID: 442337 [Multi-domain]  Cd Length: 119  Bit Score: 80.17  E-value: 9.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758723744 177 TKVAYINGDNVNLRKGPGTGYAVIRKLGKGECYQVWGESNGWLNL----GGDQWVYndSSYIRYTGenatapskssndgi 252
Cdd:COG3103     4 ETRYVVDADALNVRSGPGTSYRIVGTLPKGEKVTVLGRSGGWYKVrysnGKTGWVS--SRYLTVTP-------------- 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1758723744 253 GVVTITADVLRVRTGPGTNYDVVKNVYQGEKYQSWGYRDGWYNVGGDQ--WV 302
Cdd:COG3103    68 SARERLPDELNLRAGPSTSSEVLGLLPKGETVTVLKKSGGWFKVGYRGtgWV 119
wall_bind_EntB NF040676
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ...
 251-308 2.18e-05

cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.


Pssm-ID: 468642 [Multi-domain]  Cd Length: 476  Bit Score: 45.93  E-value: 2.18e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1758723744 251 GIGVVT--------ITADVLRVRTGPGTNYDVVKNVYQGEKYQSWGYRDGWYNV---GGDQWVSGEYVK 308
Cdd:NF040676   14 GLGAFTttataetiVTADVLNVREKPTTESKVVEKVKNGQELKVINTEDGWSKIelnGKEVFVSSEFTK 82
SH3_3 pfam08239
Bacterial SH3 domain;
260-308 4.69e-05

Bacterial SH3 domain;


Pssm-ID: 462405 [Multi-domain]  Cd Length: 54  Bit Score: 40.31  E-value: 4.69e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1758723744 260 DVLRVRTGPGTNYDVVKNVYQGEKYQ-SWGYRDGWYNV----GGDQWVSGEYVK 308
Cdd:pfam08239   1 SGLNVRSGPSTSSEVVGTLPKGEKVEvLEEQGGGWYKVrtydGYEGWVSSSYLS 54
SH3b smart00287
Bacterial SH3 domain homologues;
177-217 3.65e-03

Bacterial SH3 domain homologues;


Pssm-ID: 214600 [Multi-domain]  Cd Length: 63  Bit Score: 35.39  E-value: 3.65e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1758723744  177 TKVAYINGDNVNLRKGPGTGYAVIRKLGKGECYQVWGESNG 217
Cdd:smart00287   1 SETAVVTGDGLNVRTGPGTSSPIIGTLKKGDKVKVLGVDGQ 41
 
Name Accession Description Interval E-value
CwlA COG5632
N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis];
1-177 1.26e-72

N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 444359  Cd Length: 177  Bit Score: 221.77  E-value: 1.26e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758723744   1 MEIRKNLVDASKYgTKCPYTMNPEFITVHNTYND-ATAANEVAYMIRNDNQVSFHIAVDDKEAVQGIPLERNAWHCGDGG 79
Cdd:COG5632     3 VNIKKKLIPKNNS-YRPGYKMKPKGIVIHNTANPgATAENHANYFNNNNRSASWHYFVDDKEIIQHIPLNENAWHAGDGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758723744  80 GSGNRKSIGVEICYslSGGDRYYKAEDNAAIVVAQLMKQYNIPISKVRTHQSWSGKYCPHRMLAEG--RWNSFIERVQNA 157
Cdd:COG5632    82 GPGNRRSIGIEICE--NKDGDFAKAYENAAELIAYLMKKYGIPIDNVVRHYDWSGKNCPHGLLANGgyRWDQFKADVKSA 159

                         170       180
                  ....*....|....*....|
gi 1758723744 158 YNGSNNPvmqKPTPPSTDGT 177
Cdd:COG5632   160 LNGLSTV---KPYTKVVKAS 176
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 22-141 2.45e-25

Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in certain cases, hydrolyze peptidoglycans (PGNs) of bacterial cell walls. PGRPs have been divided into three classes: short PGRPs (PGRP-S), that are small (20 kDa) extracellular proteins; intermediate PGRPs (PGRP-I) that are 40-45 kDa and are predicted to be transmembrane proteins; and long PGRPs (PGRP-L), up to 90 kDa, which may be either intracellular or transmembrane. Several structures of PGRPs are known in insects and mammals, some bound with substrates like Muramyl Tripeptide (MTP) or Tracheal Cytotoxin (TCT). The substrate binding site is conserved in PGRP-LCx, PGRP-LE, and PGRP-Ialpha proteins. This family includes Zn-dependent N-Acetylmuramoyl-L-alanine Amidase, EC:3.5.1.28. This enzyme cleaves the amide bond between N-acetylmuramoyl and L-amino acids, preferentially D-lactyl-L-Ala, in bacterial cell walls. The structure for the bacteriophage T7 lysozyme shows that two of the conserved histidines and a cysteine are zinc binding residues. Site-directed mutagenesis of T7 lysozyme indicates that two conserved residues, a Tyr and a Lys, are important for amidase activity.


Pssm-ID: 133475 [Multi-domain]  Cd Length: 126  Bit Score: 98.13  E-value: 2.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758723744  22 NPEFITVHNTYNDA--TAANEVAYM----IRNDNQVSFHIAVD-DKEAVQGIPLERNAWHCGdggGSGNRKSIGVEICYS 94
Cdd:cd06583     1 PVKYVVIHHTANPNcyTAAAAVRYLqnyhMRGWSDISYHFLVGgDGRIYQGRGWNYVGWHAG---GNYNSYSIGIELIGN 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1758723744  95 LSGGDRYYKAEDNAAIVVAQLMKQYNIP-ISKVRTHQSWSG-KYCPHRM 141
Cdd:cd06583    78 FDGGPPTAAQLEALAELLAYLVKRYGIPpDYRIVGHRDVSPgTECPGDA 126
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 22-140 4.89e-25

N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC:3.5.1.28. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls (preferentially: D-lactyl-L-Ala). The structure is known for the bacteriophage T7 structure and shows that two of the conserved histidines are zinc binding.


Pssm-ID: 460236 [Multi-domain]  Cd Length: 122  Bit Score: 97.04  E-value: 4.89e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758723744  22 NPEFITVHNTYNDATAANEVAYM---IRNDNQVSFHIAVDDKEAV-QGIPLERNAWHCGDGGGsgNRKSIGVEICYSLSG 97
Cdd:pfam01510   1 PIRYIVIHHTAGPSFAGALLPYAaciARGWSDVSYHYLIDRDGTIyQLVPENGRAWHAGNGGG--NDRSIGIELEGNFGG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1758723744  98 GDRYYKAEDNAAIVVAQLMKQYNIPI-SKVRTHQSWSGKYCPHR 140
Cdd:pfam01510  79 DPPTDAQYEALARLLADLCKRYGIPPdRRIVGHRDVGRKTDPGP 122
Ami_2 smart00644
Ami_2 domain;
21-138 2.18e-24

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 95.50  E-value: 2.18e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758723744   21 MNPEFITVHNTYND-ATAANEVAYMIRND-NQVSFHIAVD-DKEAVQGIPLERNAWHCGDGG-GSGNRKSIGVEICYSLS 96
Cdd:smart00644   1 PPPRGIVIHHTANSnASCANEARYMQNNHmNDIGYHFLVGgDGRVYQGVGWNYVAWHAGGAHtPGYNDISIGIEFIGSFD 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1758723744   97 GGD-RYYKAEDNAAIVVAQLMKQYNIPIS---KVRTHQSWSGKYCP 138
Cdd:smart00644  81 SDDePFAEALYAALDLLAKLLKGAGLPPDgryRIVGHRDVAPTEDP 126
YgiM COG3103
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ...
 177-302 9.22e-19

Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family [General function prediction only];


Pssm-ID: 442337 [Multi-domain]  Cd Length: 119  Bit Score: 80.17  E-value: 9.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758723744 177 TKVAYINGDNVNLRKGPGTGYAVIRKLGKGECYQVWGESNGWLNL----GGDQWVYndSSYIRYTGenatapskssndgi 252
Cdd:COG3103     4 ETRYVVDADALNVRSGPGTSYRIVGTLPKGEKVTVLGRSGGWYKVrysnGKTGWVS--SRYLTVTP-------------- 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1758723744 253 GVVTITADVLRVRTGPGTNYDVVKNVYQGEKYQSWGYRDGWYNVGGDQ--WV 302
Cdd:COG3103    68 SARERLPDELNLRAGPSTSSEVLGLLPKGETVTVLKKSGGWFKVGYRGtgWV 119
AmpD COG3023
N-acetyl-anhydromuramyl-L-alanine amidase AmpD [Cell wall/membrane/envelope biogenesis];
18-138 1.14e-10

N-acetyl-anhydromuramyl-L-alanine amidase AmpD [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442259  Cd Length: 167  Bit Score: 59.11  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758723744  18 PYTMNPEFITVHNTYNDaTAANEVAYMIRNDNQVSFHIAVD-DKEAVQGIPLERNAWHCG----DGGGSGNRKSIGVEIC 92
Cdd:COG3023    22 PAGAEIDLIVIHYTAGP-PGGGALDWLTDPALRVSAHYLIDrDGEIYQLVPEDDRAWHAGvsswRGRTNLNDFSIGIELE 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1758723744  93 YSLSGGDRY----YKAednAAIVVAQLMKQYNIPISKVRTHQSWSG--KYCP 138
Cdd:COG3023   101 NPGHGWAPFteaqYEA---LAALLRDLCARYGIPPDHIVGHSDIAPgrKTDP 149
YraI COG4991
Uncharacterized conserved protein YraI [Function unknown];
181-245 1.32e-09

Uncharacterized conserved protein YraI [Function unknown];


Pssm-ID: 444015 [Multi-domain]  Cd Length: 92  Bit Score: 54.30  E-value: 1.32e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758723744 181 YINGDNVNLRKGPGTGYAVIRKLGKGECYQVWG--ESNGWL--NLGGDQ-WVYndSSYIRYTGENATAPS 245
Cdd:COG4991    25 AVATDDLNLRSGPGTGYPVVGTLPAGATVTVLGctSGGGWCkvSYGGQRgWVS--ARYLQVSYDGQPVPL 92
YraI COG4991
Uncharacterized conserved protein YraI [Function unknown];
253-309 1.32e-07

Uncharacterized conserved protein YraI [Function unknown];


Pssm-ID: 444015 [Multi-domain]  Cd Length: 92  Bit Score: 48.52  E-value: 1.32e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1758723744 253 GVVTITADVLRVRTGPGTNYDVVKNVYQGEKYQSWGYRDG--WYNV---GGDQWVSGEYVKF 309
Cdd:COG4991    22 AATAVATDDLNLRSGPGTGYPVVGTLPAGATVTVLGCTSGggWCKVsygGQRGWVSARYLQV 83
wall_bind_EntB NF040676
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ...
 251-308 2.18e-05

cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.


Pssm-ID: 468642 [Multi-domain]  Cd Length: 476  Bit Score: 45.93  E-value: 2.18e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1758723744 251 GIGVVT--------ITADVLRVRTGPGTNYDVVKNVYQGEKYQSWGYRDGWYNV---GGDQWVSGEYVK 308
Cdd:NF040676   14 GLGAFTttataetiVTADVLNVREKPTTESKVVEKVKNGQELKVINTEDGWSKIelnGKEVFVSSEFTK 82
SH3_3 pfam08239
Bacterial SH3 domain;
260-308 4.69e-05

Bacterial SH3 domain;


Pssm-ID: 462405 [Multi-domain]  Cd Length: 54  Bit Score: 40.31  E-value: 4.69e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1758723744 260 DVLRVRTGPGTNYDVVKNVYQGEKYQ-SWGYRDGWYNV----GGDQWVSGEYVK 308
Cdd:pfam08239   1 SGLNVRSGPSTSSEVVGTLPKGEKVEvLEEQGGGWYKVrtydGYEGWVSSSYLS 54
YgiM COG3103
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ...
 174-227 1.88e-04

Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family [General function prediction only];


Pssm-ID: 442337 [Multi-domain]  Cd Length: 119  Bit Score: 40.49  E-value: 1.88e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1758723744 174 TDGTKVAYINGDNVNLRKGPGTGYAVIRKLGKGECYQVWGESNGWLNLGGDQ--WV 227
Cdd:COG3103    64 TVTPSARERLPDELNLRAGPSTSSEVLGLLPKGETVTVLKKSGGWFKVGYRGtgWV 119
SH3b smart00287
Bacterial SH3 domain homologues;
177-217 3.65e-03

Bacterial SH3 domain homologues;


Pssm-ID: 214600 [Multi-domain]  Cd Length: 63  Bit Score: 35.39  E-value: 3.65e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1758723744  177 TKVAYINGDNVNLRKGPGTGYAVIRKLGKGECYQVWGESNG 217
Cdd:smart00287   1 SETAVVTGDGLNVRTGPGTSSPIIGTLKKGDKVKVLGVDGQ 41
SH3b smart00287
Bacterial SH3 domain homologues;
254-308 5.00e-03

Bacterial SH3 domain homologues;


Pssm-ID: 214600 [Multi-domain]  Cd Length: 63  Bit Score: 35.00  E-value: 5.00e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1758723744  254 VVTITADVLRVRTGPGTNYDVVKNVYQGE--KYQSWGYRDgW----YNVGGDQWVSGEYVK 308
Cdd:smart00287   3 TAVVTGDGLNVRTGPGTSSPIIGTLKKGDkvKVLGVDGQD-WakitYGSGQRGYVPGYVVN 62
 
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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