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Conserved domains on  [gi|1207759764|ref|WP_088114956|]
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N-acetylmuramoyl-L-alanine amidase [Bacillus thuringiensis]

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];
1-172 1.37e-75

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


:

Pssm-ID: 444359  Cd Length: 177  Bit Score: 226.39  E-value: 1.37e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207759764   1 MEIRKKLVDPSKYgTKCPYTMNPEFITVHNTYN-DASAENEIAYMIRNNNEVSFHIAVDDKEAVQGIPLERNAWHCGDGG 79
Cdd:COG5632     3 VNIKKKLIPKNNS-YRPGYKMKPKGIVIHNTANpGATAENHANYFNNNNRSASWHYFVDDKEIIQHIPLNENAWHAGDGT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207759764  80 GNGNRKSIGVEICYslSGGDRYYKAENNAAIIVAQLMRQYNIPISKVRTHQSWSGKYCPHRMLDEG--RWNSFIERVQNA 157
Cdd:COG5632    82 GPGNRRSIGIEICE--NKDGDFAKAYENAAELIAYLMKKYGIPIDNVVRHYDWSGKNCPHGLLANGgyRWDQFKADVKSA 159
                         170
                  ....*....|....*
gi 1207759764 158 YNGGGNTVPSTKPSN 172
Cdd:COG5632   160 LNGLSTVKPYTKVVK 174
YgiM COG3103
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ...
178-233 1.43e-11

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: 59.75  E-value: 1.43e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207759764 178 VTVTADVLRVRTGPGTNYDIVKKVYRGERYQSWGIQNGWYNV----GGDQWVSGEYVRFE 233
Cdd:COG3103     7 YVVDADALNVRSGPGTSYRIVGTLPKGEKVTVLGRSGGWYKVrysnGKTGWVSSRYLTVT 66
 
Name Accession Description Interval E-value
CwlA COG5632
N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis];
1-172 1.37e-75

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


Pssm-ID: 444359  Cd Length: 177  Bit Score: 226.39  E-value: 1.37e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207759764   1 MEIRKKLVDPSKYgTKCPYTMNPEFITVHNTYN-DASAENEIAYMIRNNNEVSFHIAVDDKEAVQGIPLERNAWHCGDGG 79
Cdd:COG5632     3 VNIKKKLIPKNNS-YRPGYKMKPKGIVIHNTANpGATAENHANYFNNNNRSASWHYFVDDKEIIQHIPLNENAWHAGDGT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207759764  80 GNGNRKSIGVEICYslSGGDRYYKAENNAAIIVAQLMRQYNIPISKVRTHQSWSGKYCPHRMLDEG--RWNSFIERVQNA 157
Cdd:COG5632    82 GPGNRRSIGIEICE--NKDGDFAKAYENAAELIAYLMKKYGIPIDNVVRHYDWSGKNCPHGLLANGgyRWDQFKADVKSA 159
                         170
                  ....*....|....*
gi 1207759764 158 YNGGGNTVPSTKPSN 172
Cdd:COG5632   160 LNGLSTVKPYTKVVK 174
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
22-141 6.92e-26

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: 97.74  E-value: 6.92e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207759764  22 NPEFITVHNTYNDAS--AENEIAYM----IRNNNEVSFHIAVD-DKEAVQGIPLERNAWHCGdggGNGNRKSIGVEICYS 94
Cdd:cd06583     1 PVKYVVIHHTANPNCytAAAAVRYLqnyhMRGWSDISYHFLVGgDGRIYQGRGWNYVGWHAG---GNYNSYSIGIELIGN 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1207759764  95 LSGGDRYYKAENNAAIIVAQLMRQYNIP-ISKVRTHQSWSG-KYCPHRM 141
Cdd:cd06583    78 FDGGPPTAAQLEALAELLAYLVKRYGIPpDYRIVGHRDVSPgTECPGDA 126
Ami_2 smart00644
Ami_2 domain;
21-138 1.16e-25

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 97.04  E-value: 1.16e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207759764   21 MNPEFITVHNTYND-ASAENEIAYMIRNN-NEVSFHIAVD-DKEAVQGIPLERNAWHCGDGG-GNGNRKSIGVEICYSLS 96
Cdd:smart00644   1 PPPRGIVIHHTANSnASCANEARYMQNNHmNDIGYHFLVGgDGRVYQGVGWNYVAWHAGGAHtPGYNDISIGIEFIGSFD 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1207759764   97 GGD-RYYKAENNAAIIVAQLMRQYNIPIS---KVRTHQSWSGKYCP 138
Cdd:smart00644  81 SDDePFAEALYAALDLLAKLLKGAGLPPDgryRIVGHRDVAPTEDP 126
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
22-140 1.57e-24

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: 93.96  E-value: 1.57e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207759764  22 NPEFITVHNTYNDASAENEIAYM---IRNNNEVSFHIAVDDKEAV-QGIPLERNAWHCGDGGGNGNrkSIGVEICYSLSG 97
Cdd:pfam01510   1 PIRYIVIHHTAGPSFAGALLPYAaciARGWSDVSYHYLIDRDGTIyQLVPENGRAWHAGNGGGNDR--SIGIELEGNFGG 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1207759764  98 GDRYYKAENNAAIIVAQLMRQYNIPI-SKVRTHQSWSGKYCPHR 140
Cdd:pfam01510  79 DPPTDAQYEALARLLADLCKRYGIPPdRRIVGHRDVGRKTDPGP 122
YgiM COG3103
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ...
178-233 1.43e-11

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: 59.75  E-value: 1.43e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207759764 178 VTVTADVLRVRTGPGTNYDIVKKVYRGERYQSWGIQNGWYNV----GGDQWVSGEYVRFE 233
Cdd:COG3103     7 YVVDADALNVRSGPGTSYRIVGTLPKGEKVTVLGRSGGWYKVrysnGKTGWVSSRYLTVT 66
wall_bind_EntB NF040676
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ...
180-231 3.04e-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: 44.39  E-value: 3.04e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1207759764 180 VTADVLRVRTGPGTNYDIVKKVYRGERYQSWGIQNGWYNV---GGDQWVSGEYVR 231
Cdd:NF040676   28 VTADVLNVREKPTTESKVVEKVKNGQELKVINTEDGWSKIelnGKEVFVSSEFTK 82
SH3_3 pfam08239
Bacterial SH3 domain;
183-230 6.33e-05

Bacterial SH3 domain;


Pssm-ID: 462405 [Multi-domain]  Cd Length: 54  Bit Score: 39.54  E-value: 6.33e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1207759764 183 DVLRVRTGPGTNYDIVKKVYRGERYQSWGIQNG-WYNV----GGDQWVSGEYV 230
Cdd:pfam08239   1 SGLNVRSGPSTSSEVVGTLPKGEKVEVLEEQGGgWYKVrtydGYEGWVSSSYL 53
SH3b smart00287
Bacterial SH3 domain homologues;
179-227 1.42e-03

Bacterial SH3 domain homologues;


Pssm-ID: 214600 [Multi-domain]  Cd Length: 63  Bit Score: 36.16  E-value: 1.42e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207759764  179 TVTADVLRVRTGPGTNYDIVKKVYRGERYQSWGIQN-GW----YNVGGDQWVSG 227
Cdd:smart00287   5 VVTGDGLNVRTGPGTSSPIIGTLKKGDKVKVLGVDGqDWakitYGSGQRGYVPG 58
 
Name Accession Description Interval E-value
CwlA COG5632
N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis];
1-172 1.37e-75

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


Pssm-ID: 444359  Cd Length: 177  Bit Score: 226.39  E-value: 1.37e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207759764   1 MEIRKKLVDPSKYgTKCPYTMNPEFITVHNTYN-DASAENEIAYMIRNNNEVSFHIAVDDKEAVQGIPLERNAWHCGDGG 79
Cdd:COG5632     3 VNIKKKLIPKNNS-YRPGYKMKPKGIVIHNTANpGATAENHANYFNNNNRSASWHYFVDDKEIIQHIPLNENAWHAGDGT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207759764  80 GNGNRKSIGVEICYslSGGDRYYKAENNAAIIVAQLMRQYNIPISKVRTHQSWSGKYCPHRMLDEG--RWNSFIERVQNA 157
Cdd:COG5632    82 GPGNRRSIGIEICE--NKDGDFAKAYENAAELIAYLMKKYGIPIDNVVRHYDWSGKNCPHGLLANGgyRWDQFKADVKSA 159
                         170
                  ....*....|....*
gi 1207759764 158 YNGGGNTVPSTKPSN 172
Cdd:COG5632   160 LNGLSTVKPYTKVVK 174
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
22-141 6.92e-26

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: 97.74  E-value: 6.92e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207759764  22 NPEFITVHNTYNDAS--AENEIAYM----IRNNNEVSFHIAVD-DKEAVQGIPLERNAWHCGdggGNGNRKSIGVEICYS 94
Cdd:cd06583     1 PVKYVVIHHTANPNCytAAAAVRYLqnyhMRGWSDISYHFLVGgDGRIYQGRGWNYVGWHAG---GNYNSYSIGIELIGN 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1207759764  95 LSGGDRYYKAENNAAIIVAQLMRQYNIP-ISKVRTHQSWSG-KYCPHRM 141
Cdd:cd06583    78 FDGGPPTAAQLEALAELLAYLVKRYGIPpDYRIVGHRDVSPgTECPGDA 126
Ami_2 smart00644
Ami_2 domain;
21-138 1.16e-25

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 97.04  E-value: 1.16e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207759764   21 MNPEFITVHNTYND-ASAENEIAYMIRNN-NEVSFHIAVD-DKEAVQGIPLERNAWHCGDGG-GNGNRKSIGVEICYSLS 96
Cdd:smart00644   1 PPPRGIVIHHTANSnASCANEARYMQNNHmNDIGYHFLVGgDGRVYQGVGWNYVAWHAGGAHtPGYNDISIGIEFIGSFD 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1207759764   97 GGD-RYYKAENNAAIIVAQLMRQYNIPIS---KVRTHQSWSGKYCP 138
Cdd:smart00644  81 SDDePFAEALYAALDLLAKLLKGAGLPPDgryRIVGHRDVAPTEDP 126
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
22-140 1.57e-24

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: 93.96  E-value: 1.57e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207759764  22 NPEFITVHNTYNDASAENEIAYM---IRNNNEVSFHIAVDDKEAV-QGIPLERNAWHCGDGGGNGNrkSIGVEICYSLSG 97
Cdd:pfam01510   1 PIRYIVIHHTAGPSFAGALLPYAaciARGWSDVSYHYLIDRDGTIyQLVPENGRAWHAGNGGGNDR--SIGIELEGNFGG 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1207759764  98 GDRYYKAENNAAIIVAQLMRQYNIPI-SKVRTHQSWSGKYCPHR 140
Cdd:pfam01510  79 DPPTDAQYEALARLLADLCKRYGIPPdRRIVGHRDVGRKTDPGP 122
AmpD COG3023
N-acetyl-anhydromuramyl-L-alanine amidase AmpD [Cell wall/membrane/envelope biogenesis];
18-155 4.38e-12

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


Pssm-ID: 442259  Cd Length: 167  Bit Score: 62.19  E-value: 4.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207759764  18 PYTMNPEFITVHNTYNDaSAENEIAYMIRNNNEVSFHIAVD-DKEAVQGIPLERNAWHCG----DGGGNGNRKSIGVEIC 92
Cdd:COG3023    22 PAGAEIDLIVIHYTAGP-PGGGALDWLTDPALRVSAHYLIDrDGEIYQLVPEDDRAWHAGvsswRGRTNLNDFSIGIELE 100
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207759764  93 YSLSGGDRY----YKAennAAIIVAQLMRQYNIPISKVRTHQSWSG--KYCPHRMLDegrWNSFIERVQ 155
Cdd:COG3023   101 NPGHGWAPFteaqYEA---LAALLRDLCARYGIPPDHIVGHSDIAPgrKTDPGPAFP---WARLAALLA 163
YgiM COG3103
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ...
178-233 1.43e-11

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: 59.75  E-value: 1.43e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207759764 178 VTVTADVLRVRTGPGTNYDIVKKVYRGERYQSWGIQNGWYNV----GGDQWVSGEYVRFE 233
Cdd:COG3103     7 YVVDADALNVRSGPGTSYRIVGTLPKGEKVTVLGRSGGWYKVrysnGKTGWVSSRYLTVT 66
YraI COG4991
Uncharacterized conserved protein YraI [Function unknown];
178-234 6.09e-09

Uncharacterized conserved protein YraI [Function unknown];


Pssm-ID: 444015 [Multi-domain]  Cd Length: 92  Bit Score: 51.60  E-value: 6.09e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207759764 178 VTVTADVLRVRTGPGTNYDIVKKVYRGERYQSWG--IQNGWYNV---GGDQWVSGEYVRFEG 234
Cdd:COG4991    24 TAVATDDLNLRSGPGTGYPVVGTLPAGATVTVLGctSGGGWCKVsygGQRGWVSARYLQVSY 85
YgiM COG3103
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ...
178-225 8.44e-06

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: 43.57  E-value: 8.44e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1207759764 178 VTVTADVLRVRTGPGTNYDIVKKVYRGERYQSWGIQNGWYNVGGDQ--WV 225
Cdd:COG3103    70 RERLPDELNLRAGPSTSSEVLGLLPKGETVTVLKKSGGWFKVGYRGtgWV 119
wall_bind_EntB NF040676
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ...
180-231 3.04e-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: 44.39  E-value: 3.04e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1207759764 180 VTADVLRVRTGPGTNYDIVKKVYRGERYQSWGIQNGWYNV---GGDQWVSGEYVR 231
Cdd:NF040676   28 VTADVLNVREKPTTESKVVEKVKNGQELKVINTEDGWSKIelnGKEVFVSSEFTK 82
SH3_3 pfam08239
Bacterial SH3 domain;
183-230 6.33e-05

Bacterial SH3 domain;


Pssm-ID: 462405 [Multi-domain]  Cd Length: 54  Bit Score: 39.54  E-value: 6.33e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1207759764 183 DVLRVRTGPGTNYDIVKKVYRGERYQSWGIQNG-WYNV----GGDQWVSGEYV 230
Cdd:pfam08239   1 SGLNVRSGPSTSSEVVGTLPKGEKVEVLEEQGGgWYKVrtydGYEGWVSSSYL 53
SH3b smart00287
Bacterial SH3 domain homologues;
179-227 1.42e-03

Bacterial SH3 domain homologues;


Pssm-ID: 214600 [Multi-domain]  Cd Length: 63  Bit Score: 36.16  E-value: 1.42e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207759764  179 TVTADVLRVRTGPGTNYDIVKKVYRGERYQSWGIQN-GW----YNVGGDQWVSG 227
Cdd:smart00287   5 VVTGDGLNVRTGPGTSSPIIGTLKKGDKVKVLGVDGqDWakitYGSGQRGYVPG 58
 
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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