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Conserved domains on  [gi|1980783735|ref|WP_203032602|]
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carbohydrate-binding protein [Escherichia coli]

Protein Classification

ChiC_BD and GH18_PF-ChiA-like domain-containing protein( domain architecture ID 10649531)

protein containing domains ChtBD3, ChiC_BD, and GH18_PF-ChiA-like

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GH18_PF-ChiA-like cd06543
PF-ChiA is an uncharacterized chitinase found in the hyperthermophilic archaeon Pyrococcus ...
587-892 1.51e-121

PF-ChiA is an uncharacterized chitinase found in the hyperthermophilic archaeon Pyrococcus furiosus with a glycosyl hydrolase family 18 (GH18) catalytic domain as well as a cellulose-binding domain. Members of this domain family are found not only in archaea but also in eukaryotes and prokaryotes. PF-ChiA exhibits hydrolytic activity toward both colloidal and crystalline (beta/alpha) chitins at high temperature.


:

Pssm-ID: 119360  Cd Length: 294  Bit Score: 370.08  E-value: 1.51e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980783735 587 HVYAPYVDFTLNTIPDLAALAKNHNVNHFTLAFVVSKdaNTCLPTWGTAYGM-QNYAQYSKIKALREAGGDVMLSIGGAN 665
Cdd:cd06543     1 TVFAPYVDVTLNPPPDLTTYAAATGVKAFTLAFIVAS--GGCKPAWGGSYPLdQGGWIKSDIAALRAAGGDVIVSFGGAS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980783735 666 NAPLAASCKNVDDLMQHYYDIVDNLNLKVLDFDIEGTWVADQASIERRNLAVKKVQDKWKsegkDIAIWYTLPILPTGLT 745
Cdd:cd06543    79 GTPLATSCTSADQLAAAYQKVIDAYGLTHLDFDIEGGALTDTAAIDRRAQALALLQKEYP----DLKISFTLPVLPTGLT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980783735 746 PEGMNVLSDAKAKGVELAGVNVMTMDYGNAIcqsanteGQNIHGKCATSAIANLHSQLKGLHPNKSDAEIDAMMGTTPMV 825
Cdd:cd06543   155 PDGLNVLEAAAANGVDLDTVNIMTMDYGSSA-------GSQDMGAAAISAAESLHDQLKDLYPKLSDAELWAMIGVTPMI 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1980783735 826 GVNDVQGEVFYLSDARLVMQDAQKRNLGMVGIWSIARDLPGGTNLSPEFHGLTKEQAPKYAFSEIFA 892
Cdd:cd06543   228 GVNDVGSEVFTLADAQTLVDFAKEKGLGRLSMWSLNRDRPCPGGGASPTATCSGVQQQDYDFSKIFA 294
ChiC_BD cd12215
Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of ...
461-509 1.51e-09

Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of Streptomyces griseus and related proteins. Chitinase C is a family 19 chitinase, and consists of a N-terminal chitin binding domain and a C-terminal chitin-catalytic domain that effects degradation. Chitinases function in invertebrates in the degradation of old exoskeletons, in fungi to utilize chitin in cell walls, and in bacteria which use chitin as an energy source. ChiC contains the characteristic chitin-binding aromatic residues.


:

Pssm-ID: 213178 [Multi-domain]  Cd Length: 42  Bit Score: 54.12  E-value: 1.51e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1980783735 461 AWSASTVYVKGDRVVVDGQAYEALFWTQSDNPalvanqnatGSNSRPWK 509
Cdd:cd12215     2 AWDASTVYTGGDQVTYNGKVYEAKWWTQGEEP---------GTSWGVWK 41
ChtBD3 smart00495
Chitin-binding domain type 3;
128-173 7.98e-04

Chitin-binding domain type 3;


:

Pssm-ID: 197760 [Multi-domain]  Cd Length: 41  Bit Score: 38.01  E-value: 7.98e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1980783735  128 VVAWNKQQGGQTWYVV-FNGAVYKNAWWVaSSNCPGdakgnDASNPW 173
Cdd:smart00495   1 APAWQAGTVYTAGDVVsYNGKVYKAKWWT-QGEEPG-----SSSGPW 41
ChtBD3 smart00495
Chitin-binding domain type 3;
229-265 2.33e-03

Chitin-binding domain type 3;


:

Pssm-ID: 197760 [Multi-domain]  Cd Length: 41  Bit Score: 36.47  E-value: 2.33e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1980783735  229 VVAWKGQEGSSTWY-VIYNGGIYKNAWWVGaANCPGDA 265
Cdd:smart00495   1 APAWQAGTVYTAGDvVSYNGKVYKAKWWTQ-GEEPGSS 37
 
Name Accession Description Interval E-value
GH18_PF-ChiA-like cd06543
PF-ChiA is an uncharacterized chitinase found in the hyperthermophilic archaeon Pyrococcus ...
587-892 1.51e-121

PF-ChiA is an uncharacterized chitinase found in the hyperthermophilic archaeon Pyrococcus furiosus with a glycosyl hydrolase family 18 (GH18) catalytic domain as well as a cellulose-binding domain. Members of this domain family are found not only in archaea but also in eukaryotes and prokaryotes. PF-ChiA exhibits hydrolytic activity toward both colloidal and crystalline (beta/alpha) chitins at high temperature.


Pssm-ID: 119360  Cd Length: 294  Bit Score: 370.08  E-value: 1.51e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980783735 587 HVYAPYVDFTLNTIPDLAALAKNHNVNHFTLAFVVSKdaNTCLPTWGTAYGM-QNYAQYSKIKALREAGGDVMLSIGGAN 665
Cdd:cd06543     1 TVFAPYVDVTLNPPPDLTTYAAATGVKAFTLAFIVAS--GGCKPAWGGSYPLdQGGWIKSDIAALRAAGGDVIVSFGGAS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980783735 666 NAPLAASCKNVDDLMQHYYDIVDNLNLKVLDFDIEGTWVADQASIERRNLAVKKVQDKWKsegkDIAIWYTLPILPTGLT 745
Cdd:cd06543    79 GTPLATSCTSADQLAAAYQKVIDAYGLTHLDFDIEGGALTDTAAIDRRAQALALLQKEYP----DLKISFTLPVLPTGLT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980783735 746 PEGMNVLSDAKAKGVELAGVNVMTMDYGNAIcqsanteGQNIHGKCATSAIANLHSQLKGLHPNKSDAEIDAMMGTTPMV 825
Cdd:cd06543   155 PDGLNVLEAAAANGVDLDTVNIMTMDYGSSA-------GSQDMGAAAISAAESLHDQLKDLYPKLSDAELWAMIGVTPMI 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1980783735 826 GVNDVQGEVFYLSDARLVMQDAQKRNLGMVGIWSIARDLPGGTNLSPEFHGLTKEQAPKYAFSEIFA 892
Cdd:cd06543   228 GVNDVGSEVFTLADAQTLVDFAKEKGLGRLSMWSLNRDRPCPGGGASPTATCSGVQQQDYDFSKIFA 294
ChiC_BD cd12215
Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of ...
461-509 1.51e-09

Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of Streptomyces griseus and related proteins. Chitinase C is a family 19 chitinase, and consists of a N-terminal chitin binding domain and a C-terminal chitin-catalytic domain that effects degradation. Chitinases function in invertebrates in the degradation of old exoskeletons, in fungi to utilize chitin in cell walls, and in bacteria which use chitin as an energy source. ChiC contains the characteristic chitin-binding aromatic residues.


Pssm-ID: 213178 [Multi-domain]  Cd Length: 42  Bit Score: 54.12  E-value: 1.51e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1980783735 461 AWSASTVYVKGDRVVVDGQAYEALFWTQSDNPalvanqnatGSNSRPWK 509
Cdd:cd12215     2 AWDASTVYTGGDQVTYNGKVYEAKWWTQGEEP---------GTSWGVWK 41
ChtBD3 smart00495
Chitin-binding domain type 3;
459-497 2.37e-07

Chitin-binding domain type 3;


Pssm-ID: 197760 [Multi-domain]  Cd Length: 41  Bit Score: 47.64  E-value: 2.37e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1980783735  459 AKAWSASTVYVKGDRVVVDGQAYEALFWTQSDNPALVAN 497
Cdd:smart00495   1 APAWQAGTVYTAGDVVSYNGKVYKAKWWTQGEEPGSSSG 39
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
611-863 9.45e-07

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 51.69  E-value: 9.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980783735 611 NVNHFTLAFVVSKDANTCLPTWGTAYGmqNYAQYSKIKALREAGGDVMLSIGGANN----APLAASCKNVDDLMQHYYDI 686
Cdd:pfam00704  22 KLTHIIYAFANIDGSDGTLFIGDWDLG--NFEQLKKLKKQKNPGVKVLLSIGGWTDstgfSLMASNPASRKKFADSIVSF 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980783735 687 VDNLNLKVLDFDIE--GTWVADQAS----IERRNLAVKKVQDKWKSE--------GKDIAIWYTLPILptgltpegmnvl 752
Cdd:pfam00704 100 LRKYGFDGIDIDWEypGGNPEDKENydllLRELRAALDEAKGGKKYLlsaavpasYPDLDKGYDLPKI------------ 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980783735 753 sdakAKGVELagVNVMTMDYGNAICQSANTEGQNIHGKCATSAIANLHSQLKGLHPNK---------------------- 810
Cdd:pfam00704 168 ----AKYLDF--INVMTYDFHGSWDNVTGHHAPLYGGGSYNVDYAVKYYLKQGVPASKlvlgvpfygrswtlvngsgntw 241
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980783735 811 -----SDAEIDAMMGTTPMVGVNDVQGEVFYLS---------DARLV---MQDAQKRNLGMVGIWSIARD 863
Cdd:pfam00704 242 edgvlAYKEICNLLKDNGATVVWDDVAKAPYVYdgdqfitydDPRSIatkVDYVKAKGLGGVMIWSLDAD 311
ChtBD3 smart00495
Chitin-binding domain type 3;
128-173 7.98e-04

Chitin-binding domain type 3;


Pssm-ID: 197760 [Multi-domain]  Cd Length: 41  Bit Score: 38.01  E-value: 7.98e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1980783735  128 VVAWNKQQGGQTWYVV-FNGAVYKNAWWVaSSNCPGdakgnDASNPW 173
Cdd:smart00495   1 APAWQAGTVYTAGDVVsYNGKVYKAKWWT-QGEEPG-----SSSGPW 41
ChtBD3 smart00495
Chitin-binding domain type 3;
229-265 2.33e-03

Chitin-binding domain type 3;


Pssm-ID: 197760 [Multi-domain]  Cd Length: 41  Bit Score: 36.47  E-value: 2.33e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1980783735  229 VVAWKGQEGSSTWY-VIYNGGIYKNAWWVGaANCPGDA 265
Cdd:smart00495   1 APAWQAGTVYTAGDvVSYNGKVYKAKWWTQ-GEEPGSS 37
 
Name Accession Description Interval E-value
GH18_PF-ChiA-like cd06543
PF-ChiA is an uncharacterized chitinase found in the hyperthermophilic archaeon Pyrococcus ...
587-892 1.51e-121

PF-ChiA is an uncharacterized chitinase found in the hyperthermophilic archaeon Pyrococcus furiosus with a glycosyl hydrolase family 18 (GH18) catalytic domain as well as a cellulose-binding domain. Members of this domain family are found not only in archaea but also in eukaryotes and prokaryotes. PF-ChiA exhibits hydrolytic activity toward both colloidal and crystalline (beta/alpha) chitins at high temperature.


Pssm-ID: 119360  Cd Length: 294  Bit Score: 370.08  E-value: 1.51e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980783735 587 HVYAPYVDFTLNTIPDLAALAKNHNVNHFTLAFVVSKdaNTCLPTWGTAYGM-QNYAQYSKIKALREAGGDVMLSIGGAN 665
Cdd:cd06543     1 TVFAPYVDVTLNPPPDLTTYAAATGVKAFTLAFIVAS--GGCKPAWGGSYPLdQGGWIKSDIAALRAAGGDVIVSFGGAS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980783735 666 NAPLAASCKNVDDLMQHYYDIVDNLNLKVLDFDIEGTWVADQASIERRNLAVKKVQDKWKsegkDIAIWYTLPILPTGLT 745
Cdd:cd06543    79 GTPLATSCTSADQLAAAYQKVIDAYGLTHLDFDIEGGALTDTAAIDRRAQALALLQKEYP----DLKISFTLPVLPTGLT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980783735 746 PEGMNVLSDAKAKGVELAGVNVMTMDYGNAIcqsanteGQNIHGKCATSAIANLHSQLKGLHPNKSDAEIDAMMGTTPMV 825
Cdd:cd06543   155 PDGLNVLEAAAANGVDLDTVNIMTMDYGSSA-------GSQDMGAAAISAAESLHDQLKDLYPKLSDAELWAMIGVTPMI 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1980783735 826 GVNDVQGEVFYLSDARLVMQDAQKRNLGMVGIWSIARDLPGGTNLSPEFHGLTKEQAPKYAFSEIFA 892
Cdd:cd06543   228 GVNDVGSEVFTLADAQTLVDFAKEKGLGRLSMWSLNRDRPCPGGGASPTATCSGVQQQDYDFSKIFA 294
ChiC_BD cd12215
Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of ...
461-509 1.51e-09

Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of Streptomyces griseus and related proteins. Chitinase C is a family 19 chitinase, and consists of a N-terminal chitin binding domain and a C-terminal chitin-catalytic domain that effects degradation. Chitinases function in invertebrates in the degradation of old exoskeletons, in fungi to utilize chitin in cell walls, and in bacteria which use chitin as an energy source. ChiC contains the characteristic chitin-binding aromatic residues.


Pssm-ID: 213178 [Multi-domain]  Cd Length: 42  Bit Score: 54.12  E-value: 1.51e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1980783735 461 AWSASTVYVKGDRVVVDGQAYEALFWTQSDNPalvanqnatGSNSRPWK 509
Cdd:cd12215     2 AWDASTVYTGGDQVTYNGKVYEAKWWTQGEEP---------GTSWGVWK 41
ChtBD3 smart00495
Chitin-binding domain type 3;
459-497 2.37e-07

Chitin-binding domain type 3;


Pssm-ID: 197760 [Multi-domain]  Cd Length: 41  Bit Score: 47.64  E-value: 2.37e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1980783735  459 AKAWSASTVYVKGDRVVVDGQAYEALFWTQSDNPALVAN 497
Cdd:smart00495   1 APAWQAGTVYTAGDVVSYNGKVYKAKWWTQGEEPGSSSG 39
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
611-863 9.45e-07

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 51.69  E-value: 9.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980783735 611 NVNHFTLAFVVSKDANTCLPTWGTAYGmqNYAQYSKIKALREAGGDVMLSIGGANN----APLAASCKNVDDLMQHYYDI 686
Cdd:pfam00704  22 KLTHIIYAFANIDGSDGTLFIGDWDLG--NFEQLKKLKKQKNPGVKVLLSIGGWTDstgfSLMASNPASRKKFADSIVSF 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980783735 687 VDNLNLKVLDFDIE--GTWVADQAS----IERRNLAVKKVQDKWKSE--------GKDIAIWYTLPILptgltpegmnvl 752
Cdd:pfam00704 100 LRKYGFDGIDIDWEypGGNPEDKENydllLRELRAALDEAKGGKKYLlsaavpasYPDLDKGYDLPKI------------ 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980783735 753 sdakAKGVELagVNVMTMDYGNAICQSANTEGQNIHGKCATSAIANLHSQLKGLHPNK---------------------- 810
Cdd:pfam00704 168 ----AKYLDF--INVMTYDFHGSWDNVTGHHAPLYGGGSYNVDYAVKYYLKQGVPASKlvlgvpfygrswtlvngsgntw 241
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980783735 811 -----SDAEIDAMMGTTPMVGVNDVQGEVFYLS---------DARLV---MQDAQKRNLGMVGIWSIARD 863
Cdd:pfam00704 242 edgvlAYKEICNLLKDNGATVVWDDVAKAPYVYdgdqfitydDPRSIatkVDYVKAKGLGGVMIWSLDAD 311
GH18_chitinase-like cd00598
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ...
611-771 5.44e-06

The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant polymer of beta-1,4-linked N-acetylglucosamine (GlcNAc) which is a major component of the cell wall of fungi and the exoskeleton of arthropods. Chitinases have been identified in viruses, bacteria, fungi, protozoan parasites, insects, and plants. The structure of the GH18 domain is an eight-stranded beta/alpha barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel. The GH18 family includes chitotriosidase, chitobiase, hevamine, zymocin-alpha, narbonin, SI-CLP (stabilin-1 interacting chitinase-like protein), IDGF (imaginal disc growth factor), CFLE (cortical fragment-lytic enzyme) spore hydrolase, the type III and type V plant chitinases, the endo-beta-N-acetylglucosaminidases, and the chitolectins. The GH85 (glycosyl hydrolase, family 85) ENGases (endo-beta-N-acetylglucosaminidases) are closely related to the GH18 chitinases and are included in this alignment model.


Pssm-ID: 119349 [Multi-domain]  Cd Length: 210  Bit Score: 48.14  E-value: 5.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980783735 611 NVNHFTLAFVVSKDANTcLPTWGTAYGMQnyaQYSKIKALREAGGD--VMLSIGGANNAP---LAASCKNVDDLMQHYYD 685
Cdd:cd00598    23 LCTHIIYAFAEISSDGS-LNLFGDKSEEP---LKGALEELASKKPGlkVLISIGGWTDSSpftLASDPASRAAFANSLVS 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980783735 686 IVDNLNLKVLDFDIEgtWVADQASIERRNLA--VKKVQDKWKSEGKDIAIWytlpiLPTGltPEGMNVLSDAKAKGVELA 763
Cdd:cd00598    99 FLKTYGFDGVDIDWE--YPGAADNSDRENFItlLRELRSALGAANYLLTIA-----VPAS--YFDLGYAYDVPAIGDYVD 169

                  ....*...
gi 1980783735 764 GVNVMTMD 771
Cdd:cd00598   170 FVNVMTYD 177
ChtBD3 smart00495
Chitin-binding domain type 3;
128-173 7.98e-04

Chitin-binding domain type 3;


Pssm-ID: 197760 [Multi-domain]  Cd Length: 41  Bit Score: 38.01  E-value: 7.98e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1980783735  128 VVAWNKQQGGQTWYVV-FNGAVYKNAWWVaSSNCPGdakgnDASNPW 173
Cdd:smart00495   1 APAWQAGTVYTAGDVVsYNGKVYKAKWWT-QGEEPG-----SSSGPW 41
ChtBD3 smart00495
Chitin-binding domain type 3;
229-265 2.33e-03

Chitin-binding domain type 3;


Pssm-ID: 197760 [Multi-domain]  Cd Length: 41  Bit Score: 36.47  E-value: 2.33e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1980783735  229 VVAWKGQEGSSTWY-VIYNGGIYKNAWWVGaANCPGDA 265
Cdd:smart00495   1 APAWQAGTVYTAGDvVSYNGKVYKAKWWTQ-GEEPGSS 37
GH18_chitinase_D-like cd02871
GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes ...
604-726 7.67e-03

GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes the 1,4-beta-linkages of N-acetylglucosamine in chitin and chitodextrins. The domain architecture of ChiD includes a catalytic glycosyl hydrolase family 18 (GH18) domain, a chitin-binding domain, and a fibronectin type III domain. The chitin-binding and fibronectin type III domains are located either N-terminal or C-terminal to the catalytic domain. This family includes exochitinase Chi36 from Bacillus cereus.


Pssm-ID: 119350 [Multi-domain]  Cd Length: 312  Bit Score: 39.24  E-value: 7.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980783735 604 AALAKNHNVNHFTLAFvvskdantclpTWGTAYGMQNYAQY-SKIKALREAGGDVMLSIGGANNAPLAASCKNVDDLMQH 682
Cdd:cd02871    33 VAFAEPTSDGGGEVTF-----------NNGSSPGGYSPAEFkADIKALQAKGKKVLISIGGANGHVDLNHTAQEDNFVDS 101
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1980783735 683 YYDIVDNLNLKVLDFDIEGTWVADQASIERRNL--AVKKVQDKWKS 726
Cdd:cd02871   102 IVAIIKEYGFDGLDIDLESGSNPLNATPVITNLisALKQLKDHYGP 147
 
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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