NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|71995504|ref|NP_495798|]
View 

GH18 domain-containing protein [Caenorhabditis elegans]

Protein Classification

glycoside hydrolase family 18 protein( domain architecture ID 12217527)

glycoside hydrolase family 18 protein similar to chitinase, which catalyzes the random endo-hydrolysis of the 1,4-beta-linkages of N-acetylglucosamine in chitin and chitodextrins

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Glyco_18 smart00636
Glyco_18 domain;
33-376 4.74e-115

Glyco_18 domain;


:

Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 346.97  E-value: 4.74e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504     33 RRVGYITSWG----KHPFRDDQAEKLTHLVFAFFVVDSDGSVKLE-GDAAKARLEHVKEVASRHPDLKLLYAVGGWENSQ 107
Cdd:smart00636   1 RVVGYFTNWGvygrNFPVDDIPASKLTHIIYAFANIDPDGTVTIGdEWADIGNFGQLKALKKKNPGLKVLLSIGGWTESD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504    108 YFSVLTADHSRRSILISNFVKVIKEYGFDGVDIDWEYPVTGGavegtpADRRNYVNLMRELRNELRDLESEtGKSYLISF 187
Cdd:smart00636  81 NFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWEYPGGRG------DDRENYTALLKELREALDKEGAE-GKGYLLTI 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504    188 AGAAGHWVLKPGYD-LQQLMKYCDFVNVMSYDYFGAWASkwgaYTGPPAPLqFAMPKKfSGRMNVHATMKDYSCQIKATD 266
Cdd:smart00636 154 AVPAGPDKIDKGYGdLPAIAKYLDFINLMTYDFHGAWSN----PTGHNAPL-YAGPGD-PEKYNVDYAVKYYLCKGVPPS 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504    267 KINMGVPFYGRFWKNVGDAVDSTDDMWrTATATNSEGTKfEGGDVQWRDLHEKFDTTKTkFHSGSKTPFIWLSEQKTFVG 346
Cdd:smart00636 228 KLVLGIPFYGRGWTLVDGSNNGPGAPF-TGPATGGPGTW-EGGVVDYREICKLLGATVV-YDDTAKAPYAYNPGTGQWVS 304
                          330       340       350
                   ....*....|....*....|....*....|
gi 71995504    347 YENAESLKHKVDYIVENNIGGVMIWAIDFD 376
Cdd:smart00636 305 YDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
ChtBD1_GH18_2 cd10909
Hevein or type 1 chitin binding domain (ChtBD1) subfamily; in some members co-occurs with ...
418-469 6.59e-22

Hevein or type 1 chitin binding domain (ChtBD1) subfamily; in some members co-occurs with family 18 glycosyl hydrolases; This subfamily includes a Toxoplasma gondii ME49 protein annotated as a putative mannosyl-oligosaccharide glucosidase. ChtBD1 is a lectin domain found in proteins from plants and fungi that bind N-acetylglucosamine, plant endochitinases, wound-induced proteins such as hevein, a major IgE-binding allergen in natural rubber latex, and the alpha subunit of Kluyveromyces lactis killer toxin. This domain is involved in the recognition and/or binding of chitin subunits; it typically occurs N-terminal to glycosyl hydrolase domains in chitinases, together with other carbohydrate-binding domains, or by itself in tandem-repeat arrangements.


:

Pssm-ID: 211315  Cd Length: 51  Bit Score: 88.97  E-value: 6.59e-22
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 71995504 418 EELAGMCGKSSPLIDGYYPVCDPDDPgHACCGKYGYCGSGAEFCSCPECIDY 469
Cdd:cd10909   1 ERSDGRCGKGFPLLDGYPPVCDPDSE-HPCCSNGGYCGSGADHCDCPGCIDF 51
ChtBD1_GH18_2 cd10909
Hevein or type 1 chitin binding domain (ChtBD1) subfamily; in some members co-occurs with ...
496-547 2.06e-21

Hevein or type 1 chitin binding domain (ChtBD1) subfamily; in some members co-occurs with family 18 glycosyl hydrolases; This subfamily includes a Toxoplasma gondii ME49 protein annotated as a putative mannosyl-oligosaccharide glucosidase. ChtBD1 is a lectin domain found in proteins from plants and fungi that bind N-acetylglucosamine, plant endochitinases, wound-induced proteins such as hevein, a major IgE-binding allergen in natural rubber latex, and the alpha subunit of Kluyveromyces lactis killer toxin. This domain is involved in the recognition and/or binding of chitin subunits; it typically occurs N-terminal to glycosyl hydrolase domains in chitinases, together with other carbohydrate-binding domains, or by itself in tandem-repeat arrangements.


:

Pssm-ID: 211315  Cd Length: 51  Bit Score: 87.43  E-value: 2.06e-21
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 71995504 496 EGKRGRCGRDVPPLEGEAPTCNPDDANaHCCSNGGYCGNSKEHCECNGCIDF 547
Cdd:cd10909   1 ERSDGRCGKGFPLLDGYPPVCDPDSEH-PCCSNGGYCGSGADHCDCPGCIDF 51
ChtBD1_GH18_2 cd10909
Hevein or type 1 chitin binding domain (ChtBD1) subfamily; in some members co-occurs with ...
567-618 4.70e-20

Hevein or type 1 chitin binding domain (ChtBD1) subfamily; in some members co-occurs with family 18 glycosyl hydrolases; This subfamily includes a Toxoplasma gondii ME49 protein annotated as a putative mannosyl-oligosaccharide glucosidase. ChtBD1 is a lectin domain found in proteins from plants and fungi that bind N-acetylglucosamine, plant endochitinases, wound-induced proteins such as hevein, a major IgE-binding allergen in natural rubber latex, and the alpha subunit of Kluyveromyces lactis killer toxin. This domain is involved in the recognition and/or binding of chitin subunits; it typically occurs N-terminal to glycosyl hydrolase domains in chitinases, together with other carbohydrate-binding domains, or by itself in tandem-repeat arrangements.


:

Pssm-ID: 211315  Cd Length: 51  Bit Score: 83.58  E-value: 4.70e-20
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 71995504 567 PANVGRCGYNAPrLSTGKIPKCDPDSESYCCSNSGYCGKGEQYCSCLGCADF 618
Cdd:cd10909   1 ERSDGRCGKGFP-LLDGYPPVCDPDSEHPCCSNGGYCGSGADHCDCPGCIDF 51
 
Name Accession Description Interval E-value
Glyco_18 smart00636
Glyco_18 domain;
33-376 4.74e-115

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 346.97  E-value: 4.74e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504     33 RRVGYITSWG----KHPFRDDQAEKLTHLVFAFFVVDSDGSVKLE-GDAAKARLEHVKEVASRHPDLKLLYAVGGWENSQ 107
Cdd:smart00636   1 RVVGYFTNWGvygrNFPVDDIPASKLTHIIYAFANIDPDGTVTIGdEWADIGNFGQLKALKKKNPGLKVLLSIGGWTESD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504    108 YFSVLTADHSRRSILISNFVKVIKEYGFDGVDIDWEYPVTGGavegtpADRRNYVNLMRELRNELRDLESEtGKSYLISF 187
Cdd:smart00636  81 NFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWEYPGGRG------DDRENYTALLKELREALDKEGAE-GKGYLLTI 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504    188 AGAAGHWVLKPGYD-LQQLMKYCDFVNVMSYDYFGAWASkwgaYTGPPAPLqFAMPKKfSGRMNVHATMKDYSCQIKATD 266
Cdd:smart00636 154 AVPAGPDKIDKGYGdLPAIAKYLDFINLMTYDFHGAWSN----PTGHNAPL-YAGPGD-PEKYNVDYAVKYYLCKGVPPS 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504    267 KINMGVPFYGRFWKNVGDAVDSTDDMWrTATATNSEGTKfEGGDVQWRDLHEKFDTTKTkFHSGSKTPFIWLSEQKTFVG 346
Cdd:smart00636 228 KLVLGIPFYGRGWTLVDGSNNGPGAPF-TGPATGGPGTW-EGGVVDYREICKLLGATVV-YDDTAKAPYAYNPGTGQWVS 304
                          330       340       350
                   ....*....|....*....|....*....|
gi 71995504    347 YENAESLKHKVDYIVENNIGGVMIWAIDFD 376
Cdd:smart00636 305 YDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
ChiA COG3325
Chitinase, GH18 family [Carbohydrate transport and metabolism];
31-389 2.95e-106

Chitinase, GH18 family [Carbohydrate transport and metabolism];


Pssm-ID: 442554 [Multi-domain]  Cd Length: 391  Bit Score: 326.48  E-value: 2.95e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504  31 GRRRVGYITSWGKH----PFRDDQAEKLTHLVFAFFVVDSDGSVKL---------------EGDAAKARLEHVKEVASRH 91
Cdd:COG3325  18 GKRVVGYFTQWGIYgrnyLVKDIPASKLTHINYAFANVDPDGKCSVgdawakpsvdgaaddWDQPLKGNFNQLKKLKAKN 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504  92 PDLKLLYAVGGWENSQYFSVLTADHSRRSILISNFVKVIKEYGFDGVDIDWEYPVTGGAV--EGTPADRRNYVNLMRELR 169
Cdd:COG3325  98 PNLKVLISIGGWTWSKGFSDAAATPASRAAFVDSCVDLLRKYNFDGIDIDWEYPGSGGAPgnVYRPEDKANFTALLKELR 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 170 NELRDLESETGKSYLISFAGAAGHWVLKpGYDLQQLMKYCDFVNVMSYDYFGAWAskwgAYTGPPAPLqFAMPKK-FSGR 248
Cdd:COG3325 178 AQLDALGAETGKHYLLTAAAPAGPDKLD-GIELPKVAQYLDYVNVMTYDFHGAWS----PTTGHQAPL-YDSPKDpEAQG 251
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 249 MNVHATMKDY-SCQIKAtDKINMGVPFYGRFWKNVGDAvdsTDDMWRTATATnSEGTkFEGGDVQWRDLHEKF---DTTK 324
Cdd:COG3325 252 YSVDSAVQAYlAAGVPA-SKLVLGVPFYGRGWTGVTGG---NNGLYQPATGP-APGT-WEAGVNDYKDLKALYlgsNGYT 325
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71995504 325 TKFHSGSKTPFIWLSEQKTFVGYENAESLKHKVDYIVENNIGGVMIWAIDFDDDQGTLLNSAAAE 389
Cdd:COG3325 326 RYWDDVAKAPYLYNGDTGTFISYDDPRSIAAKADYVKDKGLGGVMFWELSGDTADGTLLNAIGEG 390
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
33-376 5.40e-97

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 299.37  E-value: 5.40e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504    33 RRVGYITSWGKHPFRD-DQAEKLTHLVFAFFVVDSDGSVKLEGDAAKARLEHVKE-VASRHPDLKLLYAVGGWENSQYFS 110
Cdd:pfam00704   1 RIVGYYTSWGVYRNGNfLPSDKLTHIIYAFANIDGSDGTLFIGDWDLGNFEQLKKlKKQKNPGVKVLLSIGGWTDSTGFS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504   111 VLTADHSRRSILISNFVKVIKEYGFDGVDIDWEYPVtggaveGTPADRRNYVNLMRELRNELRDLesETGKSYLISFAGA 190
Cdd:pfam00704  81 LMASNPASRKKFADSIVSFLRKYGFDGIDIDWEYPG------GNPEDKENYDLLLRELRAALDEA--KGGKKYLLSAAVP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504   191 AGHWVLKPGYDLQQLMKYCDFVNVMSYDYFGAWASkwgaYTGPPAPLQfampkkFSGRMNVHATMKDYSCQIKATDKINM 270
Cdd:pfam00704 153 ASYPDLDKGYDLPKIAKYLDFINVMTYDFHGSWDN----VTGHHAPLY------GGGSYNVDYAVKYYLKQGVPASKLVL 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504   271 GVPFYGRFWKNVgdavdstddmwrtatatNSEGTKFEGGDVQWRDLHE--KFDTTKTKFHSGSKTPFIWLSEQktFVGYE 348
Cdd:pfam00704 223 GVPFYGRSWTLV-----------------NGSGNTWEDGVLAYKEICNllKDNGATVVWDDVAKAPYVYDGDQ--FITYD 283
                         330       340
                  ....*....|....*....|....*...
gi 71995504   349 NAESLKHKVDYIVENNIGGVMIWAIDFD 376
Cdd:pfam00704 284 DPRSIATKVDYVKAKGLGGVMIWSLDAD 311
GH18_chitinase cd06548
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ...
35-376 1.29e-84

The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant polymer of N-acetylglucosamine and have been identified in bacteria, fungi, insects, plants, viruses, and protozoan parasites. The structure of this domain is an eight-stranded alpha/beta barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel.


Pssm-ID: 119365 [Multi-domain]  Cd Length: 322  Bit Score: 267.96  E-value: 1.29e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504  35 VGYITSWGK-----HPFRDDQAEKLTHLVFAFFVVDSDGSVKLEGDAAKARLEHVKEVA-------------------SR 90
Cdd:cd06548   2 VGYFTNWGIygrnyFVTDDIPADKLTHINYAFADIDGDGGVVTSDDEAADEAAQSVDGGadtddqplkgnfgqlrklkQK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504  91 HPDLKLLYAVGGWENSQYFSVLTADHSRRSILISNFVKVIKEYGFDGVDIDWEYPVTGGAVE--GTPADRRNYVNLMREL 168
Cdd:cd06548  82 NPHLKILLSIGGWTWSGGFSDAAATEASRAKFADSAVDFIRKYGFDGIDIDWEYPGSGGAPGnvARPEDKENFTLLLKEL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 169 RNELRDLESETGKSYLISFAGAAGHWVLKpGYDLQQLMKYCDFVNVMSYDYFGAwaskWGAYTGPPAPLqFAMPKKFSGR 248
Cdd:cd06548 162 REALDALGAETGRKYLLTIAAPAGPDKLD-KLEVAEIAKYLDFINLMTYDFHGA----WSNTTGHHSNL-YASPADPPGG 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 249 MNVHATMKDYscqIKA---TDKINMGVPFYGRFWKnvgdavdstddmwrtatatnsegtkfeGGDVQWrdlhekfDTTkt 325
Cdd:cd06548 236 YSVDAAVNYY---LSAgvpPEKLVLGVPFYGRGWT---------------------------GYTRYW-------DEV-- 276
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 71995504 326 kfhsgSKTPFIWLSEQKTFVGYENAESLKHKVDYIVENNIGGVMIWAIDFD 376
Cdd:cd06548 277 -----AKAPYLYNPSTKTFISYDDPRSIKAKADYVKDKGLGGVMFWELSGD 322
ChtBD1_GH18_2 cd10909
Hevein or type 1 chitin binding domain (ChtBD1) subfamily; in some members co-occurs with ...
418-469 6.59e-22

Hevein or type 1 chitin binding domain (ChtBD1) subfamily; in some members co-occurs with family 18 glycosyl hydrolases; This subfamily includes a Toxoplasma gondii ME49 protein annotated as a putative mannosyl-oligosaccharide glucosidase. ChtBD1 is a lectin domain found in proteins from plants and fungi that bind N-acetylglucosamine, plant endochitinases, wound-induced proteins such as hevein, a major IgE-binding allergen in natural rubber latex, and the alpha subunit of Kluyveromyces lactis killer toxin. This domain is involved in the recognition and/or binding of chitin subunits; it typically occurs N-terminal to glycosyl hydrolase domains in chitinases, together with other carbohydrate-binding domains, or by itself in tandem-repeat arrangements.


Pssm-ID: 211315  Cd Length: 51  Bit Score: 88.97  E-value: 6.59e-22
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 71995504 418 EELAGMCGKSSPLIDGYYPVCDPDDPgHACCGKYGYCGSGAEFCSCPECIDY 469
Cdd:cd10909   1 ERSDGRCGKGFPLLDGYPPVCDPDSE-HPCCSNGGYCGSGADHCDCPGCIDF 51
ChtBD1_GH18_2 cd10909
Hevein or type 1 chitin binding domain (ChtBD1) subfamily; in some members co-occurs with ...
496-547 2.06e-21

Hevein or type 1 chitin binding domain (ChtBD1) subfamily; in some members co-occurs with family 18 glycosyl hydrolases; This subfamily includes a Toxoplasma gondii ME49 protein annotated as a putative mannosyl-oligosaccharide glucosidase. ChtBD1 is a lectin domain found in proteins from plants and fungi that bind N-acetylglucosamine, plant endochitinases, wound-induced proteins such as hevein, a major IgE-binding allergen in natural rubber latex, and the alpha subunit of Kluyveromyces lactis killer toxin. This domain is involved in the recognition and/or binding of chitin subunits; it typically occurs N-terminal to glycosyl hydrolase domains in chitinases, together with other carbohydrate-binding domains, or by itself in tandem-repeat arrangements.


Pssm-ID: 211315  Cd Length: 51  Bit Score: 87.43  E-value: 2.06e-21
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 71995504 496 EGKRGRCGRDVPPLEGEAPTCNPDDANaHCCSNGGYCGNSKEHCECNGCIDF 547
Cdd:cd10909   1 ERSDGRCGKGFPLLDGYPPVCDPDSEH-PCCSNGGYCGSGADHCDCPGCIDF 51
ChtBD1_GH18_2 cd10909
Hevein or type 1 chitin binding domain (ChtBD1) subfamily; in some members co-occurs with ...
567-618 4.70e-20

Hevein or type 1 chitin binding domain (ChtBD1) subfamily; in some members co-occurs with family 18 glycosyl hydrolases; This subfamily includes a Toxoplasma gondii ME49 protein annotated as a putative mannosyl-oligosaccharide glucosidase. ChtBD1 is a lectin domain found in proteins from plants and fungi that bind N-acetylglucosamine, plant endochitinases, wound-induced proteins such as hevein, a major IgE-binding allergen in natural rubber latex, and the alpha subunit of Kluyveromyces lactis killer toxin. This domain is involved in the recognition and/or binding of chitin subunits; it typically occurs N-terminal to glycosyl hydrolase domains in chitinases, together with other carbohydrate-binding domains, or by itself in tandem-repeat arrangements.


Pssm-ID: 211315  Cd Length: 51  Bit Score: 83.58  E-value: 4.70e-20
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 71995504 567 PANVGRCGYNAPrLSTGKIPKCDPDSESYCCSNSGYCGKGEQYCSCLGCADF 618
Cdd:cd10909   1 ERSDGRCGKGFP-LLDGYPPVCDPDSEHPCCSNGGYCGSGADHCDCPGCIDF 51
ChtBD1 smart00270
Chitin binding domain;
501-539 1.16e-03

Chitin binding domain;


Pssm-ID: 214593  Cd Length: 38  Bit Score: 36.96  E-value: 1.16e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 71995504    501 RCGRDvppleGEAPTCNPDdanaHCCSNGGYCGNSKEHC 539
Cdd:smart00270   1 RCGSQ-----AGGKVCPNN----LCCSQFGYCGSGDEYC 30
Chitin_bind_1 pfam00187
Chitin recognition protein;
443-462 2.42e-03

Chitin recognition protein;


Pssm-ID: 459705  Cd Length: 38  Bit Score: 35.99  E-value: 2.42e-03
                          10        20
                  ....*....|....*....|
gi 71995504   443 PGHACCGKYGYCGSGAEFCS 462
Cdd:pfam00187  12 PNNLCCSQYGYCGTTSDYCG 31
Chitin_bind_1 pfam00187
Chitin recognition protein;
521-544 3.25e-03

Chitin recognition protein;


Pssm-ID: 459705  Cd Length: 38  Bit Score: 35.60  E-value: 3.25e-03
                          10        20
                  ....*....|....*....|....
gi 71995504   521 ANAHCCSNGGYCGNSKEHCEcNGC 544
Cdd:pfam00187  12 PNNLCCSQYGYCGTTSDYCG-DGC 34
ChtBD1 smart00270
Chitin binding domain;
424-462 5.10e-03

Chitin binding domain;


Pssm-ID: 214593  Cd Length: 38  Bit Score: 35.03  E-value: 5.10e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 71995504    424 CGKSSPlidgyYPVCDPDdpghACCGKYGYCGSGAEFCS 462
Cdd:smart00270   2 CGSQAG-----GKVCPNN----LCCSQFGYCGSGDEYCG 31
ChtBD1 smart00270
Chitin binding domain;
572-611 5.30e-03

Chitin binding domain;


Pssm-ID: 214593  Cd Length: 38  Bit Score: 35.03  E-value: 5.30e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 71995504    572 RCGynaprlSTGKIPKCDPDsesYCCSNSGYCGKGEQYCS 611
Cdd:smart00270   1 RCG------SQAGGKVCPNN---LCCSQFGYCGSGDEYCG 31
 
Name Accession Description Interval E-value
Glyco_18 smart00636
Glyco_18 domain;
33-376 4.74e-115

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 346.97  E-value: 4.74e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504     33 RRVGYITSWG----KHPFRDDQAEKLTHLVFAFFVVDSDGSVKLE-GDAAKARLEHVKEVASRHPDLKLLYAVGGWENSQ 107
Cdd:smart00636   1 RVVGYFTNWGvygrNFPVDDIPASKLTHIIYAFANIDPDGTVTIGdEWADIGNFGQLKALKKKNPGLKVLLSIGGWTESD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504    108 YFSVLTADHSRRSILISNFVKVIKEYGFDGVDIDWEYPVTGGavegtpADRRNYVNLMRELRNELRDLESEtGKSYLISF 187
Cdd:smart00636  81 NFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWEYPGGRG------DDRENYTALLKELREALDKEGAE-GKGYLLTI 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504    188 AGAAGHWVLKPGYD-LQQLMKYCDFVNVMSYDYFGAWASkwgaYTGPPAPLqFAMPKKfSGRMNVHATMKDYSCQIKATD 266
Cdd:smart00636 154 AVPAGPDKIDKGYGdLPAIAKYLDFINLMTYDFHGAWSN----PTGHNAPL-YAGPGD-PEKYNVDYAVKYYLCKGVPPS 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504    267 KINMGVPFYGRFWKNVGDAVDSTDDMWrTATATNSEGTKfEGGDVQWRDLHEKFDTTKTkFHSGSKTPFIWLSEQKTFVG 346
Cdd:smart00636 228 KLVLGIPFYGRGWTLVDGSNNGPGAPF-TGPATGGPGTW-EGGVVDYREICKLLGATVV-YDDTAKAPYAYNPGTGQWVS 304
                          330       340       350
                   ....*....|....*....|....*....|
gi 71995504    347 YENAESLKHKVDYIVENNIGGVMIWAIDFD 376
Cdd:smart00636 305 YDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
ChiA COG3325
Chitinase, GH18 family [Carbohydrate transport and metabolism];
31-389 2.95e-106

Chitinase, GH18 family [Carbohydrate transport and metabolism];


Pssm-ID: 442554 [Multi-domain]  Cd Length: 391  Bit Score: 326.48  E-value: 2.95e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504  31 GRRRVGYITSWGKH----PFRDDQAEKLTHLVFAFFVVDSDGSVKL---------------EGDAAKARLEHVKEVASRH 91
Cdd:COG3325  18 GKRVVGYFTQWGIYgrnyLVKDIPASKLTHINYAFANVDPDGKCSVgdawakpsvdgaaddWDQPLKGNFNQLKKLKAKN 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504  92 PDLKLLYAVGGWENSQYFSVLTADHSRRSILISNFVKVIKEYGFDGVDIDWEYPVTGGAV--EGTPADRRNYVNLMRELR 169
Cdd:COG3325  98 PNLKVLISIGGWTWSKGFSDAAATPASRAAFVDSCVDLLRKYNFDGIDIDWEYPGSGGAPgnVYRPEDKANFTALLKELR 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 170 NELRDLESETGKSYLISFAGAAGHWVLKpGYDLQQLMKYCDFVNVMSYDYFGAWAskwgAYTGPPAPLqFAMPKK-FSGR 248
Cdd:COG3325 178 AQLDALGAETGKHYLLTAAAPAGPDKLD-GIELPKVAQYLDYVNVMTYDFHGAWS----PTTGHQAPL-YDSPKDpEAQG 251
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 249 MNVHATMKDY-SCQIKAtDKINMGVPFYGRFWKNVGDAvdsTDDMWRTATATnSEGTkFEGGDVQWRDLHEKF---DTTK 324
Cdd:COG3325 252 YSVDSAVQAYlAAGVPA-SKLVLGVPFYGRGWTGVTGG---NNGLYQPATGP-APGT-WEAGVNDYKDLKALYlgsNGYT 325
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71995504 325 TKFHSGSKTPFIWLSEQKTFVGYENAESLKHKVDYIVENNIGGVMIWAIDFDDDQGTLLNSAAAE 389
Cdd:COG3325 326 RYWDDVAKAPYLYNGDTGTFISYDDPRSIAAKADYVKDKGLGGVMFWELSGDTADGTLLNAIGEG 390
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
33-376 5.40e-97

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 299.37  E-value: 5.40e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504    33 RRVGYITSWGKHPFRD-DQAEKLTHLVFAFFVVDSDGSVKLEGDAAKARLEHVKE-VASRHPDLKLLYAVGGWENSQYFS 110
Cdd:pfam00704   1 RIVGYYTSWGVYRNGNfLPSDKLTHIIYAFANIDGSDGTLFIGDWDLGNFEQLKKlKKQKNPGVKVLLSIGGWTDSTGFS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504   111 VLTADHSRRSILISNFVKVIKEYGFDGVDIDWEYPVtggaveGTPADRRNYVNLMRELRNELRDLesETGKSYLISFAGA 190
Cdd:pfam00704  81 LMASNPASRKKFADSIVSFLRKYGFDGIDIDWEYPG------GNPEDKENYDLLLRELRAALDEA--KGGKKYLLSAAVP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504   191 AGHWVLKPGYDLQQLMKYCDFVNVMSYDYFGAWASkwgaYTGPPAPLQfampkkFSGRMNVHATMKDYSCQIKATDKINM 270
Cdd:pfam00704 153 ASYPDLDKGYDLPKIAKYLDFINVMTYDFHGSWDN----VTGHHAPLY------GGGSYNVDYAVKYYLKQGVPASKLVL 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504   271 GVPFYGRFWKNVgdavdstddmwrtatatNSEGTKFEGGDVQWRDLHE--KFDTTKTKFHSGSKTPFIWLSEQktFVGYE 348
Cdd:pfam00704 223 GVPFYGRSWTLV-----------------NGSGNTWEDGVLAYKEICNllKDNGATVVWDDVAKAPYVYDGDQ--FITYD 283
                         330       340
                  ....*....|....*....|....*...
gi 71995504   349 NAESLKHKVDYIVENNIGGVMIWAIDFD 376
Cdd:pfam00704 284 DPRSIATKVDYVKAKGLGGVMIWSLDAD 311
GH18_chitinase cd06548
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ...
35-376 1.29e-84

The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant polymer of N-acetylglucosamine and have been identified in bacteria, fungi, insects, plants, viruses, and protozoan parasites. The structure of this domain is an eight-stranded alpha/beta barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel.


Pssm-ID: 119365 [Multi-domain]  Cd Length: 322  Bit Score: 267.96  E-value: 1.29e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504  35 VGYITSWGK-----HPFRDDQAEKLTHLVFAFFVVDSDGSVKLEGDAAKARLEHVKEVA-------------------SR 90
Cdd:cd06548   2 VGYFTNWGIygrnyFVTDDIPADKLTHINYAFADIDGDGGVVTSDDEAADEAAQSVDGGadtddqplkgnfgqlrklkQK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504  91 HPDLKLLYAVGGWENSQYFSVLTADHSRRSILISNFVKVIKEYGFDGVDIDWEYPVTGGAVE--GTPADRRNYVNLMREL 168
Cdd:cd06548  82 NPHLKILLSIGGWTWSGGFSDAAATEASRAKFADSAVDFIRKYGFDGIDIDWEYPGSGGAPGnvARPEDKENFTLLLKEL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 169 RNELRDLESETGKSYLISFAGAAGHWVLKpGYDLQQLMKYCDFVNVMSYDYFGAwaskWGAYTGPPAPLqFAMPKKFSGR 248
Cdd:cd06548 162 REALDALGAETGRKYLLTIAAPAGPDKLD-KLEVAEIAKYLDFINLMTYDFHGA----WSNTTGHHSNL-YASPADPPGG 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 249 MNVHATMKDYscqIKA---TDKINMGVPFYGRFWKnvgdavdstddmwrtatatnsegtkfeGGDVQWrdlhekfDTTkt 325
Cdd:cd06548 236 YSVDAAVNYY---LSAgvpPEKLVLGVPFYGRGWT---------------------------GYTRYW-------DEV-- 276
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 71995504 326 kfhsgSKTPFIWLSEQKTFVGYENAESLKHKVDYIVENNIGGVMIWAIDFD 376
Cdd:cd06548 277 -----AKAPYLYNPSTKTFISYDDPRSIKAKADYVKDKGLGGVMFWELSGD 322
GH18_chitolectin_chitotriosidase cd02872
This conserved domain family includes a large number of catalytically inactive chitinase-like ...
34-381 3.83e-66

This conserved domain family includes a large number of catalytically inactive chitinase-like lectins (chitolectins) including YKL-39, YKL-40 (HCGP39), YM1, oviductin, and AMCase (acidic mammalian chitinase), as well as catalytically active chitotriosidases. The conserved domain is an eight-stranded alpha/beta barrel fold belonging to the family 18 glycosyl hydrolases. The fold has a pronounced active-site cleft at the C-terminal end of the beta-barrel. The chitolectins lack a key active site glutamate (the proton donor required for hydrolytic activity) but retain highly conserved residues involved in oligosaccharide binding. Chitotriosidase is a chitinolytic enzyme expressed in maturing macrophages, which suggests that it plays a part in antimicrobial defense. Chitotriosidase hydrolyzes chitotriose, as well as colloidal chitin to yield chitobiose and is therefore considered an exochitinase. Chitotriosidase occurs in two major forms, the large form being converted to the small form by either RNA or post-translational processing. Although the small form, containing the chitinase domain alone, is sufficient for the chitinolytic activity, the additional C-terminal chitin-binding domain of the large form plays a role in processing colloidal chitin. The chitotriosidase gene is nonessential in humans, as about 35% of the population are heterozygous and 6% homozygous for an inactivated form of the gene. HCGP39 is a 39-kDa human cartilage glycoprotein thought to play a role in connective tissue remodeling and defense against pathogens.


Pssm-ID: 119351 [Multi-domain]  Cd Length: 362  Bit Score: 220.89  E-value: 3.83e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504  34 RVGYITSWGKhpFRDDQAE--------KL-THLVFAFFVVDSDGSVKLEGDAAKARLEHVKEVAS---RHPDLKLLYAVG 101
Cdd:cd02872   1 VVCYFTNWAQ--YRPGNGKfvpenidpFLcTHIIYAFAGLNPDGNIIILDEWNDIDLGLYERFNAlkeKNPNLKTLLAIG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 102 GW-ENSQYFSVLTADHSRRSILISNFVKVIKEYGFDGVDIDWEYPVTGGaveGTPADRRNYVNLMRELRNELrdlESETG 180
Cdd:cd02872  79 GWnFGSAKFSAMAASPENRKTFIKSAIAFLRKYGFDGLDLDWEYPGQRG---GPPEDKENFVTLLKELREAF---EPEAP 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 181 KsYLISFAGAAGHWVLKPGYDLQQLMKYCDFVNVMSYDYFGAWASkwgaYTGPPAPLqFAMPKKFSGR--MNVHATMKdY 258
Cdd:cd02872 153 R-LLLTAAVSAGKETIDAAYDIPEISKYLDFINVMTYDFHGSWEG----VTGHNSPL-YAGSADTGDQkyLNVDYAIK-Y 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 259 SCQIKA-TDKINMGVPFYGRFWK-------NVGDAVDStddmwrTATA---TNSEGT---------KFEGGDVQWrdlhe 318
Cdd:cd02872 226 WLSKGApPEKLVLGIPTYGRSFTlaspsntGVGAPASG------PGTAgpyTREAGFlayyeicefLKSGWTVVW----- 294
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71995504 319 kfdttktkfHSGSKTPFIWLSEQktFVGYENAESLKHKVDYIVENNIGGVMIWAIDFDDDQGT 381
Cdd:cd02872 295 ---------DDEQKVPYAYKGNQ--WVGYDDEESIALKVQYLKSKGLGGAMVWSIDLDDFRGT 346
GH18_chitinase-like cd00598
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ...
35-218 2.66e-46

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: 162.55  E-value: 2.66e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504  35 VGYITSWGKHP---FRDDQAEKLTHLVFAFFVVDSDGSVKLEGDA-AKARLEHVKEVASRHPDLKLLYAVGGWENSQYFS 110
Cdd:cd00598   2 ICYYDGWSSGRgpdPTDIPLSLCTHIIYAFAEISSDGSLNLFGDKsEEPLKGALEELASKKPGLKVLISIGGWTDSSPFT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 111 VLTADHSRRSiLISNFVKVIKEYGFDGVDIDWEYPVTGGAvegtpADRRNYVNLMRELRNELRDLEsetgksYLISFAGA 190
Cdd:cd00598  82 LASDPASRAA-FANSLVSFLKTYGFDGVDIDWEYPGAADN-----SDRENFITLLRELRSALGAAN------YLLTIAVP 149
                       170       180
                ....*....|....*....|....*...
gi 71995504 191 AGHWVLKPGYDLQQLMKYCDFVNVMSYD 218
Cdd:cd00598 150 ASYFDLGYAYDVPAIGDYVDFVNVMTYD 177
GH18_plant_chitinase_class_V cd02879
The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the ...
34-382 6.86e-31

The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the chitin-binding domain present in other GH18 enzymes. The GH18 domain of the class V chitinases has endochitinase activity in some cases and no catalytic activity in others. Included in this family is a lectin found in black locust (Robinia pseudoacacia) bark, which binds chitin but lacks chitinase activity. Also included is a chitinase-related receptor-like kinase (CHRK1) from tobacco (Nicotiana tabacum), with an N-terminal GH18 domain and a C-terminal kinase domain, which is thought to be part of a plant signaling pathway. The GH18 domain of CHRK1 is expressed extracellularly where it binds chitin but lacks chitinase activity.


Pssm-ID: 119358 [Multi-domain]  Cd Length: 299  Bit Score: 122.47  E-value: 6.86e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504  34 RVGYITSWG-KHPFRDDQAEKLTHLVFAFFVVD-SDGSVKLEGDAAKARLEHVKEVASRHPDLKLLYAVGGW-ENSQYFS 110
Cdd:cd02879   5 KGGYWPAWSeEFPPSNIDSSLFTHLFYAFADLDpSTYEVVISPSDESEFSTFTETVKRKNPSVKTLLSIGGGgSDSSAFA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 111 VLTADHSRRSILISNFVKVIKEYGFDGVDIDWEYPvtggaveGTPADRRNYVNLMRELRNELRDLESETGKSYLISFAGA 190
Cdd:cd02879  85 AMASDPTARKAFINSSIKVARKYGFDGLDLDWEFP-------SSQVEMENFGKLLEEWRAAVKDEARSSGRPPLLLTAAV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 191 AGHWVLKPG-----YDLQQLMKYCDFVNVMSYDYFGAWaskWGAYTGPPAPLqFAMPKKFSGrmnvHATMKDYSCQIKAT 265
Cdd:cd02879 158 YFSPILFLSddsvsYPIEAINKNLDWVNVMAYDYYGSW---ESNTTGPAAAL-YDPNSNVST----DYGIKSWIKAGVPA 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 266 DKINMGVPFYGRFWKnvgdavdstddmwrtatatnsegtkfeggdvqwrdLHekfDTTKTKFHSGSKTpfiwlseqkTFV 345
Cdd:cd02879 230 KKLVLGLPLYGRAWT-----------------------------------LY---DTTTVSSYVYAGT---------TWI 262
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 71995504 346 GYENAESLKHKVDYIVENNIGGVMIWAIDFDDDQGTL 382
Cdd:cd02879 263 GYDDVQSIAVKVKYAKQKGLLGYFAWAVGYDDNNWLS 299
GH18_CFLE_spore_hydrolase cd02874
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ...
35-383 2.34e-27

Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial endospore germination. CFLE is expressed as an inactive preprotein (called SleB) in the forespore compartment of sporulating cells. SleB translocates across the forespore inner membrane and is deposited as a mature enzyme in the cortex layer of the spore. As part of a sensory mechanism capable of initiating germination, CFLE degrades a spore-specific peptidoglycan constituent called muramic-acid delta-lactam that comprises the outer cortex. CFLE has a C-terminal glycosyl hydrolase family 18 (GH18) catalytic domain as well as two N-terminal LysM peptidoglycan-binding domains. In addition to SleB, this family includes YaaH, YdhD, and YvbX from Bacillus subtilis.


Pssm-ID: 119353 [Multi-domain]  Cd Length: 313  Bit Score: 112.74  E-value: 2.34e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504  35 VGYITSWG---KHPFRDDqAEKLTHLVFAFFVVDSDGSVKLEGDA---AKARLEHVKEVASRHPDLkllyavGGWENSQY 108
Cdd:cd02874   5 LGYYTPRNgsdYESLRAN-APYLTYIAPFWYGVDADGTLTGLPDErliEAAKRRGVKPLLVITNLT------NGNFDSEL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 109 FSVLTADHSRRSILISNFVKVIKEYGFDGVDIDWEY-PvtggavegtPADRRNYVNLMRELRNELRdlesETGKSYLISF 187
Cdd:cd02874  78 AHAVLSNPEARQRLINNILALAKKYGYDGVNIDFENvP---------PEDREAYTQFLRELSDRLH----PAGYTLSTAV 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 188 A---GAAGHWVLKPGYDLQQLMKYCDFVNVMSYDYFGAWaskwgaytGPPAP----------LQFA---MPKkfsgrmnv 251
Cdd:cd02874 145 VpktSADQFGNWSGAYDYAAIGKIVDFVVLMTYDWHWRG--------GPPGPvapigwvervLQYAvtqIPR-------- 208
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 252 hatmkdyscqikatDKINMGVPFYGRFW--KNVGDAVDSTDDMWRT---ATATNSEgtkfeggdVQWrdlhekfDTTktk 326
Cdd:cd02874 209 --------------EKILLGIPLYGYDWtlPYKKGGKASTISPQQAinlAKRYGAE--------IQY-------DEE--- 256
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 327 fhsgSKTPFIWLSE---QKTFVGYENAESLKHKVDYIVENNIGGVMIWAIDFDDDQGTLL 383
Cdd:cd02874 257 ----AQSPFFRYVDeqgRRHEVWFEDARSLQAKFELAKEYGLRGVSYWRLGLEDPQNWLL 312
GH18_IDGF cd02873
The IDGF's (imaginal disc growth factors) are a family of growth factors identified in insects ...
55-381 8.75e-24

The IDGF's (imaginal disc growth factors) are a family of growth factors identified in insects that include at least five members, some of which are encoded by genes in a tight cluster. The IDGF's have an eight-stranded alpha/beta barrel fold and are related to the glycosyl hydrolase family 18 (GH18) chitinases, but they have an amino acid substitution known to abolish chitinase catalytic activity. IDGFs may have evolved from chitinases to gain new functions as growth factors, interacting with cell surface glycoproteins involved in growth-promoting processes.


Pssm-ID: 119352 [Multi-domain]  Cd Length: 413  Bit Score: 104.32  E-value: 8.75e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504  55 THLVFAFFVVDSDG----SVKLEGDAAKARLEHVKEVASRHPDLKLLYAVGG------WENSQYFSVLTADHSRRSILIS 124
Cdd:cd02873  32 THLVYGYAGIDADTykikSLNEDLDLDKSHYRAITSLKRKYPHLKVLLSVGGdrdtdeEGENEKYLLLLESSESRNAFIN 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 125 NFVKVIKEYGFDGVDIDWEYP---------------------VTGGAVEGTPAD--RRNYVNLMRELRNELRdlesetGK 181
Cdd:cd02873 112 SAHSLLKTYGFDGLDLAWQFPknkpkkvrgtfgsawhsfkklFTGDSVVDEKAAehKEQFTALVRELKNALR------PD 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 182 SYLISFAgaaghwVLkPG------YDLQQLMKYCDFVNVMSYDYFGAWASKWGA-YtgpPAPLQFAmpkkfSGRM---NV 251
Cdd:cd02873 186 GLLLTLT------VL-PHvnstwyFDVPAIANNVDFVNLATFDFLTPERNPEEAdY---TAPIYEL-----YERNphhNV 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 252 HATMKDYSCQIKATDKINMGVPFYGRFWKNVGDA-------VDSTDDMWRTATATNSEG--------------TKFEGGD 310
Cdd:cd02873 251 DYQVKYWLNQGTPASKLNLGIATYGRAWKLTKDSgitgvppVLETDGPGPAGPQTKTPGllswpeicsklpnpANLKGAD 330
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71995504 311 VQWR---DLHEKFDTTKTKFHSGSKTPFIWlseqktfVGYENAESLKHKVDYIVENNIGGVMIWAIDFDDDQGT 381
Cdd:cd02873 331 APLRkvgDPTKRFGSYAYRPADENGEHGIW-------VSYEDPDTAANKAGYAKAKGLGGVALFDLSLDDFRGQ 397
ChtBD1_GH18_2 cd10909
Hevein or type 1 chitin binding domain (ChtBD1) subfamily; in some members co-occurs with ...
418-469 6.59e-22

Hevein or type 1 chitin binding domain (ChtBD1) subfamily; in some members co-occurs with family 18 glycosyl hydrolases; This subfamily includes a Toxoplasma gondii ME49 protein annotated as a putative mannosyl-oligosaccharide glucosidase. ChtBD1 is a lectin domain found in proteins from plants and fungi that bind N-acetylglucosamine, plant endochitinases, wound-induced proteins such as hevein, a major IgE-binding allergen in natural rubber latex, and the alpha subunit of Kluyveromyces lactis killer toxin. This domain is involved in the recognition and/or binding of chitin subunits; it typically occurs N-terminal to glycosyl hydrolase domains in chitinases, together with other carbohydrate-binding domains, or by itself in tandem-repeat arrangements.


Pssm-ID: 211315  Cd Length: 51  Bit Score: 88.97  E-value: 6.59e-22
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 71995504 418 EELAGMCGKSSPLIDGYYPVCDPDDPgHACCGKYGYCGSGAEFCSCPECIDY 469
Cdd:cd10909   1 ERSDGRCGKGFPLLDGYPPVCDPDSE-HPCCSNGGYCGSGADHCDCPGCIDF 51
ChtBD1_GH18_2 cd10909
Hevein or type 1 chitin binding domain (ChtBD1) subfamily; in some members co-occurs with ...
496-547 2.06e-21

Hevein or type 1 chitin binding domain (ChtBD1) subfamily; in some members co-occurs with family 18 glycosyl hydrolases; This subfamily includes a Toxoplasma gondii ME49 protein annotated as a putative mannosyl-oligosaccharide glucosidase. ChtBD1 is a lectin domain found in proteins from plants and fungi that bind N-acetylglucosamine, plant endochitinases, wound-induced proteins such as hevein, a major IgE-binding allergen in natural rubber latex, and the alpha subunit of Kluyveromyces lactis killer toxin. This domain is involved in the recognition and/or binding of chitin subunits; it typically occurs N-terminal to glycosyl hydrolase domains in chitinases, together with other carbohydrate-binding domains, or by itself in tandem-repeat arrangements.


Pssm-ID: 211315  Cd Length: 51  Bit Score: 87.43  E-value: 2.06e-21
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 71995504 496 EGKRGRCGRDVPPLEGEAPTCNPDDANaHCCSNGGYCGNSKEHCECNGCIDF 547
Cdd:cd10909   1 ERSDGRCGKGFPLLDGYPPVCDPDSEH-PCCSNGGYCGSGADHCDCPGCIDF 51
GH18_zymocin_alpha cd02878
Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle ...
33-376 4.09e-21

Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle progression. The zymocin alpha subunit has a chitinase activity that is essential for holoenzyme action from the cell exterior while the gamma subunit contains the intracellular toxin responsible for G1 phase cell cycle arrest. The zymocin alpha and beta subunits are thought to act from the cell's exterior by docking to the cell wall-associated chitin, thus mediating gamma-toxin translocation. The alpha subunit has an eight-stranded TIM barrel fold similar to that of family 18 glycosyl hydrolases such as hevamine, chitolectin, and chitobiase.


Pssm-ID: 119357 [Multi-domain]  Cd Length: 345  Bit Score: 95.07  E-value: 4.09e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504  33 RRVGYI--TSWGKHPFRDD----QAEKLTHLVFAFFVVDSDGSVKLegDAAKARLEHVKEVASrhpdLKLLYAVGGWENS 106
Cdd:cd02878   1 KNIAYFeaYNLDRPCLNMDvtqiDTSKYTHIHFAFANITSDFSVDV--SSVQEQFSDFKKLKG----VKKILSFGGWDFS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 107 ------QYFSVLTADhSRRSILISNFVKVIKEYGFDGVDIDWEYPvtgGAVE------GTPADRRNYVNLMRELRNELRD 174
Cdd:cd02878  75 tspstyQIFRDAVKP-ANRDTFANNVVNFVNKYNLDGVDFDWEYP---GAPDipgipaGDPDDGKNYLEFLKLLKSKLPS 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 175 lesetGKSylISFAGAAGHWVLKPgYDLQQLMKYCDFVNVMSYDYFGAW--ASKWgAYTGPPAplqfampkkfSGRMNVH 252
Cdd:cd02878 151 -----GKS--LSIAAPASYWYLKG-FPIKDMAKYVDYIVYMTYDLHGQWdyGNKW-ASPGCPA----------GNCLRSH 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 253 A----TMKDYSCQIKA---TDKINMGVPFYGRFWKNVgdAVDSTDDM------WRTATATNSEGTKFEGGDVQWRDLHEK 319
Cdd:cd02878 212 VnkteTLDALSMITKAgvpSNKVVVGVASYGRSFKMA--DPGCTGPGctftgpGSGAEAGRCTCTAGYGAISEIEIIDIS 289
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 71995504 320 FDTTKTKFHSGSKTPFIwLSEQKTFVGYENAESLKHKVDYIVENNIGGVMIWAIDFD 376
Cdd:cd02878 290 KSKNKRWYDTDSDSDIL-VYDDDQWVAYMSPATKAARIEWYKGLNFGGTSDWAVDLQ 345
ChtBD1_GH18_2 cd10909
Hevein or type 1 chitin binding domain (ChtBD1) subfamily; in some members co-occurs with ...
567-618 4.70e-20

Hevein or type 1 chitin binding domain (ChtBD1) subfamily; in some members co-occurs with family 18 glycosyl hydrolases; This subfamily includes a Toxoplasma gondii ME49 protein annotated as a putative mannosyl-oligosaccharide glucosidase. ChtBD1 is a lectin domain found in proteins from plants and fungi that bind N-acetylglucosamine, plant endochitinases, wound-induced proteins such as hevein, a major IgE-binding allergen in natural rubber latex, and the alpha subunit of Kluyveromyces lactis killer toxin. This domain is involved in the recognition and/or binding of chitin subunits; it typically occurs N-terminal to glycosyl hydrolase domains in chitinases, together with other carbohydrate-binding domains, or by itself in tandem-repeat arrangements.


Pssm-ID: 211315  Cd Length: 51  Bit Score: 83.58  E-value: 4.70e-20
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 71995504 567 PANVGRCGYNAPrLSTGKIPKCDPDSESYCCSNSGYCGKGEQYCSCLGCADF 618
Cdd:cd10909   1 ERSDGRCGKGFP-LLDGYPPVCDPDSEHPCCSNGGYCGSGADHCDCPGCIDF 51
GH18_3CO4_chitinase cd06545
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an ...
35-279 1.48e-17

The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an uncharacterized bacterial member of the family 18 glycosyl hydrolases with homologs found in Flavobacterium, Stigmatella, and Pseudomonas.


Pssm-ID: 119362 [Multi-domain]  Cd Length: 253  Bit Score: 82.89  E-value: 1.48e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504  35 VGYITSWGKHPFRDDQAE--KLTHLVFAFFVVDSDGSVKLEGDAAkaRLEHVKEVASRHpDLKLLYAVGGWENSQYFSVL 112
Cdd:cd06545   2 VGYLPNYDDLNALSPTIDfsKLTHINLAFANPDANGTLNANPVRS--ELNSVVNAAHAH-NVKILISLAGGSPPEFTAAL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 113 TaDHSRRSILISNFVKVIKEYGFDGVDIDWEYPVTGGAvegtpadrrNYVNLMRELRNELRdlesETGKsyLISFAGAAG 192
Cdd:cd06545  79 N-DPAKRKALVDKIINYVVSYNLDGIDVDLEGPDVTFG---------DYLVFIRALYAALK----KEGK--LLTAAVSSW 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 193 HWVLKPGYDLQqlmkYCDFVNVMSYDYFGAWaskWGAYTGPPAPLQFAMpkkfsgrmnvhaTMKDY--SCQIKATDKINM 270
Cdd:cd06545 143 NGGAVSDSTLA----YFDFINIMSYDATGPW---WGDNPGQHSSYDDAV------------NDLNYwnERGLASKDKLVL 203

                ....*....
gi 71995504 271 GVPFYGRFW 279
Cdd:cd06545 204 GLPFYGYGF 212
GH18_SI-CLP cd02876
Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein ...
36-276 1.04e-10

Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein of unknown function that interacts with the endocytic/sorting transmembrane receptor stabilin-1 and is secreted from the lysosome. SI-CLP has a glycosyl hydrolase family 18 (GH18) domain but lacks a chitin-binding domain. The catalytic amino acids of the GH18 domain are not conserved in SI-CLP, similar to the chitolectins YKL-39, YKL-40, and YM1/2. Human SI-CLP is sorted to late endosomes and secretory lysosomes in alternatively activated macrophages.


Pssm-ID: 119355 [Multi-domain]  Cd Length: 318  Bit Score: 63.48  E-value: 1.04e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504  36 GYITSWGKHPFrdDQAE----KLTHLVFAFFVVDSDG-SVKLEG--DAAKARLEHVKEvASRHPdlKLLYAV--GGWENS 106
Cdd:cd02876   7 GYVTPWNSHGY--DVAKkfaaKFTHVSPVWLQIKRKGnKFVIEGthDIDKGWIEEVRK-ANKNI--KILPRVlfEGWSYQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 107 QYFSVLTADHSRRSiLISNFVKVIKEYGFDGVDID-WEYpvtgGAVEGTPADRRNYVNLMRELRNELRdlesetGKSYLI 185
Cdd:cd02876  82 DLQSLLNDEQEREK-LIKLLVTTAKKNHFDGIVLEvWSQ----LAAYGVPDKRKELIQLVIHLGETLH------SANLKL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 186 SFAG-AAGHWVLKPGY----DLQQLMKYCDFVNVMSYDYFGawaskwGAYTGPPAPLQFAmpkkfsgRMNVHATMKDySC 260
Cdd:cd02876 151 ILVIpPPREKGNQNGLftrkDFEKLAPHVDGFSLMTYDYSS------PQRPGPNAPLSWV-------RSCLELLLPE-SG 216
                       250
                ....*....|....*.
gi 71995504 261 QIKAtdKINMGVPFYG 276
Cdd:cd02876 217 KKRA--KILLGLNFYG 230
GH18_chitobiase cd02875
Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes ...
115-380 3.45e-08

Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes the reducing-end N-acetylglucosamine from the chitobiose core of oligosaccharides during the ordered degradation of asparagine-linked glycoproteins in eukaryotes. Chitobiase can only do so if the asparagine that joins the oligosaccharide to protein is previously removed by a glycosylasparaginase. Chitobiase is therefore the final step in the lysosomal degradation of the protein/carbohydrate linkage component of asparagine-linked glycoproteins. The catalytic domain of chitobiase is an eight-stranded alpha/beta barrel fold similar to that of other family 18 glycosyl hydrolases such as hevamine and chitotriosidase.


Pssm-ID: 119354 [Multi-domain]  Cd Length: 358  Bit Score: 55.90  E-value: 3.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 115 DHSRRSILISNFVKVIKEYGFDGVDIDWEYPVTGGAVEgtpadrrnyVNLMRELRNELRDLESETGKSYLISFAGAaghW 194
Cdd:cd02875  93 NPTYRTQWIQQKVELAKSQFMDGINIDIEQPITKGSPE---------YYALTELVKETTKAFKKENPGYQISFDVA---W 160
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 195 ----VLKPGYDLQQLMKYCDFVNVMSYDyfgAWASKWGAY--TGPPAPLqfamPKKFSGrmnvhatMKDYSCQIKATDKI 268
Cdd:cd02875 161 spscIDKRCYDYTGIADASDFLVVMDYD---EQSQIWGKEciAGANSPY----SQTLSG-------YNNFTKLGIDPKKL 226
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 269 NMGVPFYGRFWKNVGDAVDSTDDM-----WRTATATNSEGTKFEGGDV--QWRDlhekfDTTKTKFHSGSKTPFIWLSE- 340
Cdd:cd02875 227 VMGLPWYGYDYPCLNGNLEDVVCTipkvpFRGANCSDAAGRQIPYSEImkQINS-----SIGGRLWDSEQKSPFYNYKDk 301
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 71995504 341 QKTF--VGYENAESLKHKVDYIVENNIGGVMIWAIDFDDDQG 380
Cdd:cd02875 302 QGNLhqVWYDNPQSLSIKVAYAKNLGLKGIGMWNGDLLDYSG 343
GH18_narbonin cd06544
Narbonin is a plant 2S protein from the globulin fraction of narbon bean (Vicia narbonensis L.) ...
82-220 7.60e-08

Narbonin is a plant 2S protein from the globulin fraction of narbon bean (Vicia narbonensis L.) cotyledons with unknown function. Narbonin has a glycosyl hydrolase family 18 (GH18) domain without the conserved catalytic residues and with no known enzymatic activity. Narbonin amounts to up to 3% of the total seed globulins of mature seeds and was thought to be a storage protein but was found to degrade too slowly during germination. This family also includes the VfNOD32 nodulin from Vicia faba.


Pssm-ID: 119361  Cd Length: 253  Bit Score: 53.91  E-value: 7.60e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504  82 EHVKEVASRHPDLKLLYAVGGWenSQYFSVLTADHSRRSILISNFVK----VIKEYGFDGVDIDWEYpvtggavegTPAD 157
Cdd:cd06544  59 EAVKSIKAQHPNVKVVISIGGR--GVQNNPTPFDPSNVDSWVSNAVSsltsIIQTYNLDGIDIDYEH---------FPAD 127
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71995504 158 RRNYVNLMRELRNELRdlesetgKSYLISFAGAAghwvlkPGYDLQQ-----LMK----YCDFVNVMSYDYF 220
Cdd:cd06544 128 PDTFVECIGQLITELK-------NNGVIKVASIA------PSEDAEQshylaLYNaygdYIDYVNYQFYNYG 186
GH18_chitinase_D-like cd02871
GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes ...
95-188 8.95e-07

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: 51.18  E-value: 8.95e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504  95 KLLYAVGGwensQYFSVLTADHSRRSILISNFVKVIKEYGFDGVDIDWEypvtGGAVEGTPADRRNYvnlmreLRNELRD 174
Cdd:cd02871  75 KVLISIGG----ANGHVDLNHTAQEDNFVDSIVAIIKEYGFDGLDIDLE----SGSNPLNATPVITN------LISALKQ 140
                        90
                ....*....|....
gi 71995504 175 LESETGKSYLISFA 188
Cdd:cd02871 141 LKDHYGPNFILTMA 154
ChtBD1 cd00035
Hevein or type 1 chitin binding domain; Hevein or type 1 chitin binding domain (ChtBD1), a ...
501-544 1.97e-06

Hevein or type 1 chitin binding domain; Hevein or type 1 chitin binding domain (ChtBD1), a lectin domain found in proteins from plants and fungi that bind N-acetylglucosamine, plant endochitinases, wound-induced proteins such as hevein, a major IgE-binding allergen in natural rubber latex, and the alpha subunit of Kluyveromyces lactis killer toxin. This domain is involved in the recognition and/or binding of chitin subunits; it typically occurs N-terminal to glycosyl hydrolase domains in chitinases, together with other carbohydrate-binding domains, or by itself in tandem-repeat arrangements.


Pssm-ID: 211311  Cd Length: 39  Bit Score: 44.68  E-value: 1.97e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 71995504 501 RCGRDvppleGEAPTCNPDdanaHCCSNGGYCGNSKEHCeCNGC 544
Cdd:cd00035   1 RCGSQ-----AGGPPCPNN----LCCSQYGYCGTGDDYC-GEGC 34
ChtBD1 cd00035
Hevein or type 1 chitin binding domain; Hevein or type 1 chitin binding domain (ChtBD1), a ...
423-462 6.60e-06

Hevein or type 1 chitin binding domain; Hevein or type 1 chitin binding domain (ChtBD1), a lectin domain found in proteins from plants and fungi that bind N-acetylglucosamine, plant endochitinases, wound-induced proteins such as hevein, a major IgE-binding allergen in natural rubber latex, and the alpha subunit of Kluyveromyces lactis killer toxin. This domain is involved in the recognition and/or binding of chitin subunits; it typically occurs N-terminal to glycosyl hydrolase domains in chitinases, together with other carbohydrate-binding domains, or by itself in tandem-repeat arrangements.


Pssm-ID: 211311  Cd Length: 39  Bit Score: 43.14  E-value: 6.60e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 71995504 423 MCGKsspliDGYYPVCdpddPGHACCGKYGYCGSGAEFCS 462
Cdd:cd00035   1 RCGS-----QAGGPPC----PNNLCCSQYGYCGTGDDYCG 31
GH18_EndoS-like cd06542
Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of ...
127-236 9.28e-06

Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of various asparagine (N)-linked glycans and glycoproteins. The endo-beta-N-acetylglucosaminidases have a glycosyl hydrolase family 18 (GH18) catalytic domain. Some members also have an additional C-terminal glycosyl hydrolase family 20 (GH20) domain while others have an N-terminal domain of unknown function (pfam08522). Members of this family include endo-beta-N-acetylglucosaminidase S (EndoS) from Streptococcus pyogenes, EndoF1, EndoF2, EndoF3, and EndoH from Flavobacterium meningosepticum, and EndoE from Enterococcus faecalis. EndoS is a secreted endoglycosidase from Streptococcus pyogenes that specifically hydrolyzes the glycan on human IgG between two core N-acetylglucosamine residues. EndoE is a secreted endoglycosidase, encoded by the ndoE gene in Enterococcus faecalis, that hydrolyzes the glycan on human RNase B.


Pssm-ID: 119359  Cd Length: 255  Bit Score: 47.37  E-value: 9.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 127 VKVIKEYGFDGVDIDWEYPvTGGAVEGTPADRRNYVNLMRELRNELRdlesETGKSYLISFAGAAGHWvlkpgyDLQQLM 206
Cdd:cd06542  97 VDTVDKYGLDGVDFDDEYS-GYGKNGTSQPSNEAFVRLIKELRKYMG----PTDKLLTIDGYGQALSN------DGEEVS 165
                        90       100       110
                ....*....|....*....|....*....|
gi 71995504 207 KYCDFVnvmSYDYFGAWASKWGAYTGPPAP 236
Cdd:cd06542 166 PYVDYV---IYQYYGSSSSSTQRNWNTNSP 192
ChtBD1 cd00035
Hevein or type 1 chitin binding domain; Hevein or type 1 chitin binding domain (ChtBD1), a ...
572-611 2.00e-05

Hevein or type 1 chitin binding domain; Hevein or type 1 chitin binding domain (ChtBD1), a lectin domain found in proteins from plants and fungi that bind N-acetylglucosamine, plant endochitinases, wound-induced proteins such as hevein, a major IgE-binding allergen in natural rubber latex, and the alpha subunit of Kluyveromyces lactis killer toxin. This domain is involved in the recognition and/or binding of chitin subunits; it typically occurs N-terminal to glycosyl hydrolase domains in chitinases, together with other carbohydrate-binding domains, or by itself in tandem-repeat arrangements.


Pssm-ID: 211311  Cd Length: 39  Bit Score: 41.99  E-value: 2.00e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 71995504 572 RCGYNAprlstgKIPKCDPDsesYCCSNSGYCGKGEQYCS 611
Cdd:cd00035   1 RCGSQA------GGPPCPNN---LCCSQYGYCGTGDDYCG 31
GH18_CTS3_chitinase cd06546
GH18 domain of CTS3 (chitinase 3), an uncharacterized protein from the human fungal pathogen ...
29-221 4.73e-04

GH18 domain of CTS3 (chitinase 3), an uncharacterized protein from the human fungal pathogen Coccidioides posadasii. CTS3 has a chitinase-like glycosyl hydrolase family 18 (GH18) domain; and has homologs in bacteria as well as fungi.


Pssm-ID: 119363  Cd Length: 256  Bit Score: 42.32  E-value: 4.73e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504  29 SCGRRRVGYITSWGKHPfrddqaeKLTHLVFAFFVVDSDGSVKLE----GDAAKARLEhvKEVAS-RHPDLKLLYAVGGW 103
Cdd:cd06546  12 SNGDPISSLLLVTEKGI-------ALTHLIVAALHINDDGNIHLNdhppDHPRFTTLW--TELAIlQSSGVKVMGMLGGA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504 104 -ENSqyFSVLTADHSRRSILISNFVKVIKEYGFDGVDIDWEYPVTGGAVegtpadrrnyVNLMRELRnelrdleSETGKS 182
Cdd:cd06546  83 aPGS--FSRLDDDDEDFERYYGQLRDMIRRRGLDGLDLDVEEPMSLDGI----------IRLIDRLR-------SDFGPD 143
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 71995504 183 YLISFAGAA-----GHWVLKpGYDLQQLMKY----CDFVNVMSYDYFG 221
Cdd:cd06546 144 FIITLAPVAsaltgGEANLS-GFDYRELEQArgdkIDFYNAQFYNGFG 190
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
95-188 1.15e-03

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 42.05  E-value: 1.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504  95 KLLYAVGGwENSQyfsVLTADHSRRSILISNFVKVIKEYGFDGVDIDWEypvtGGA--VEGTPADRRNYVNLMrelrNEL 172
Cdd:COG3469 290 KVLLSIGG-ANGT---VQLNTAAAADNFVNSVIALIDEYGFDGLDIDLE----GGSnsLNAGDTDTPVITNLI----SAL 357
                        90
                ....*....|....*.
gi 71995504 173 RDLESETGKSYLISFA 188
Cdd:COG3469 358 KQLKAKYGPGFVLTMA 373
ChtBD1 smart00270
Chitin binding domain;
501-539 1.16e-03

Chitin binding domain;


Pssm-ID: 214593  Cd Length: 38  Bit Score: 36.96  E-value: 1.16e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 71995504    501 RCGRDvppleGEAPTCNPDdanaHCCSNGGYCGNSKEHC 539
Cdd:smart00270   1 RCGSQ-----AGGKVCPNN----LCCSQFGYCGSGDEYC 30
GH18_trifunctional cd06549
GH18 domain of an uncharacterized family of bacterial proteins, which share a common ...
79-218 1.84e-03

GH18 domain of an uncharacterized family of bacterial proteins, which share a common three-domain architecture: an N-terminal glycosyl hydrolase family 18 (GH18) domain, a glycosyl transferase family 2 domain, and a C-terminal polysaccharide deacetylase domain.


Pssm-ID: 119366 [Multi-domain]  Cd Length: 298  Bit Score: 40.86  E-value: 1.84e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995504  79 ARLEHVKEVASRHPDLKLLY--AVGGWENSQYFSVLTADHSRRSILISNFVKVIKEYGFDGVDIDWEypvtggavEGTPA 156
Cdd:cd06549  47 PQGVAIIAAAKAHPKVLPLVqnISGGAWDGKNIARLLADPSARAKFIANIAAYLERNQADGIVLDFE--------ELPAD 118
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71995504 157 DRRNYVNLMRELRNELRdlesETGKSYLISfAGAAGHWvlkpgYDLQQLMKYCDFVNVMSYD 218
Cdd:cd06549 119 DLPKYVAFLSELRRRLP----AQGKQLTVT-VPADEAD-----WNLKALARNADKLILMAYD 170
Chitin_bind_1 pfam00187
Chitin recognition protein;
443-462 2.42e-03

Chitin recognition protein;


Pssm-ID: 459705  Cd Length: 38  Bit Score: 35.99  E-value: 2.42e-03
                          10        20
                  ....*....|....*....|
gi 71995504   443 PGHACCGKYGYCGSGAEFCS 462
Cdd:pfam00187  12 PNNLCCSQYGYCGTTSDYCG 31
Chitin_bind_1 pfam00187
Chitin recognition protein;
521-544 3.25e-03

Chitin recognition protein;


Pssm-ID: 459705  Cd Length: 38  Bit Score: 35.60  E-value: 3.25e-03
                          10        20
                  ....*....|....*....|....
gi 71995504   521 ANAHCCSNGGYCGNSKEHCEcNGC 544
Cdd:pfam00187  12 PNNLCCSQYGYCGTTSDYCG-DGC 34
ChtBD1 smart00270
Chitin binding domain;
424-462 5.10e-03

Chitin binding domain;


Pssm-ID: 214593  Cd Length: 38  Bit Score: 35.03  E-value: 5.10e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 71995504    424 CGKSSPlidgyYPVCDPDdpghACCGKYGYCGSGAEFCS 462
Cdd:smart00270   2 CGSQAG-----GKVCPNN----LCCSQFGYCGSGDEYCG 31
ChtBD1 smart00270
Chitin binding domain;
572-611 5.30e-03

Chitin binding domain;


Pssm-ID: 214593  Cd Length: 38  Bit Score: 35.03  E-value: 5.30e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 71995504    572 RCGynaprlSTGKIPKCDPDsesYCCSNSGYCGKGEQYCS 611
Cdd:smart00270   1 RCG------SQAGGKVCPNN---LCCSQFGYCGSGDEYCG 31
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH