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Conserved domains on  [gi|1831508934|ref|NP_001366720|]
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GH18 domain-containing protein [Caenorhabditis elegans]

Protein Classification

glycoside hydrolase family 18 protein( domain architecture ID 12217520)

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

CAZY:  GH18
EC:  3.2.1.-
Gene Ontology:  GO:0008061|GO:0005975|GO:0004568
PubMed:  32439576

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
Glyco_18 smart00636
Glyco_18 domain;
113-431 1.60e-97

Glyco_18 domain;


:

Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 296.13  E-value: 1.60e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934  113 RIVGYFAEFENTA----LTRKQLRMLTHIVFLFAFPK-NGTITFGGESSS-QKFEEMRRnVRKASSTLKVMISIGGQYNS 186
Cdd:smart00636   1 RVVGYFTNWGVYGrnfpVDDIPASKLTHIIYAFANIDpDGTVTIGDEWADiGNFGQLKA-LKKKNPGLKVLLSIGGWTES 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934  187 GEFSGLVSNETSRNLFVNSIATFVRDYDIDGVDIFWTWP--KHSDENNYLMFIRELRYAFTELQKklnRKETFVISLVIS 264
Cdd:smart00636  80 DNFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWEYPggRGDDRENYTALLKELREALDKEGA---EGKGYLLTIAVP 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934  265 RNVNHLSK----LVEFSNFVDFINIYS---FNSYLYQVGPDSPLYGGGS----RNVDEIMKYYICKTGQPSKFNIIVSFH 333
Cdd:smart00636 157 AGPDKIDKgygdLPAIAKYLDFINLMTydfHGAWSNPTGHNAPLYAGPGdpekYNVDYAVKYYLCKGVPPSKLVLGIPFY 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934  334 ATYWEGAELPLRDDSDDIFKDQNSAKGGFA---VRWRELLQQKwdMSNIKFHNLTKTSYMWIPGPPTrFMTLEDEKSLRE 410
Cdd:smart00636 237 GRGWTLVDGSNNGPGAPFTGPATGGPGTWEggvVDYREICKLL--GATVVYDDTAKAPYAYNPGTGQ-WVSYDDPRSIKA 313
                          330       340
                   ....*....|....*....|.
gi 1831508934  411 KNRYVADHNIGGITMWTIDQD 431
Cdd:smart00636 314 KADYVKDKGLGGVMIWELDAD 334
 
Name Accession Description Interval E-value
Glyco_18 smart00636
Glyco_18 domain;
113-431 1.60e-97

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 296.13  E-value: 1.60e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934  113 RIVGYFAEFENTA----LTRKQLRMLTHIVFLFAFPK-NGTITFGGESSS-QKFEEMRRnVRKASSTLKVMISIGGQYNS 186
Cdd:smart00636   1 RVVGYFTNWGVYGrnfpVDDIPASKLTHIIYAFANIDpDGTVTIGDEWADiGNFGQLKA-LKKKNPGLKVLLSIGGWTES 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934  187 GEFSGLVSNETSRNLFVNSIATFVRDYDIDGVDIFWTWP--KHSDENNYLMFIRELRYAFTELQKklnRKETFVISLVIS 264
Cdd:smart00636  80 DNFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWEYPggRGDDRENYTALLKELREALDKEGA---EGKGYLLTIAVP 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934  265 RNVNHLSK----LVEFSNFVDFINIYS---FNSYLYQVGPDSPLYGGGS----RNVDEIMKYYICKTGQPSKFNIIVSFH 333
Cdd:smart00636 157 AGPDKIDKgygdLPAIAKYLDFINLMTydfHGAWSNPTGHNAPLYAGPGdpekYNVDYAVKYYLCKGVPPSKLVLGIPFY 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934  334 ATYWEGAELPLRDDSDDIFKDQNSAKGGFA---VRWRELLQQKwdMSNIKFHNLTKTSYMWIPGPPTrFMTLEDEKSLRE 410
Cdd:smart00636 237 GRGWTLVDGSNNGPGAPFTGPATGGPGTWEggvVDYREICKLL--GATVVYDDTAKAPYAYNPGTGQ-WVSYDDPRSIKA 313
                          330       340
                   ....*....|....*....|.
gi 1831508934  411 KNRYVADHNIGGITMWTIDQD 431
Cdd:smart00636 314 KADYVKDKGLGGVMIWELDAD 334
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
113-431 1.00e-85

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 265.09  E-value: 1.00e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 113 RIVGYFAEFENTALTR-KQLRMLTHIVFLFA--FPKNGTITFGgESSSQKFEEMRRNVRKASSTLKVMISIGGQYNSGEF 189
Cdd:pfam00704   1 RIVGYYTSWGVYRNGNfLPSDKLTHIIYAFAniDGSDGTLFIG-DWDLGNFEQLKKLKKQKNPGVKVLLSIGGWTDSTGF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 190 SGLVSNETSRNLFVNSIATFVRDYDIDGVDIFWTWPKH--SDENNYLMFIRELRYAFTELQkklnRKETFVISLVISRNV 267
Cdd:pfam00704  80 SLMASNPASRKKFADSIVSFLRKYGFDGIDIDWEYPGGnpEDKENYDLLLRELRAALDEAK----GGKKYLLSAAVPASY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 268 NHLSK---LVEFSNFVDFINIYSF---NSYLYQVGPDSPLYGGGSRNVDEIMKYYICKTGQPSKFNIIVSFHATYWEGAE 341
Cdd:pfam00704 156 PDLDKgydLPKIAKYLDFINVMTYdfhGSWDNVTGHHAPLYGGGSYNVDYAVKYYLKQGVPASKLVLGVPFYGRSWTLVN 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 342 LPLRDDSDDIFkdqnsakggfavRWRELLQQKWD-MSNIKFHNLTKTSYMWIpgpPTRFMTLEDEKSLREKNRYVADHNI 420
Cdd:pfam00704 236 GSGNTWEDGVL------------AYKEICNLLKDnGATVVWDDVAKAPYVYD---GDQFITYDDPRSIATKVDYVKAKGL 300
                         330
                  ....*....|.
gi 1831508934 421 GGITMWTIDQD 431
Cdd:pfam00704 301 GGVMIWSLDAD 311
ChiA COG3325
Chitinase, GH18 family [Carbohydrate transport and metabolism];
93-444 7.39e-45

Chitinase, GH18 family [Carbohydrate transport and metabolism];


Pssm-ID: 442554 [Multi-domain]  Cd Length: 391  Bit Score: 160.85  E-value: 7.39e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934  93 TKLVQKSDENFSPPAafcGKRIVGYFAEF--ENTALTRKQLRM--LTHIVFLFAFPK-NGTITFGGESSSQK-------- 159
Cdd:COG3325     3 TASVSDTAAAATATS---GKRVVGYFTQWgiYGRNYLVKDIPAskLTHINYAFANVDpDGKCSVGDAWAKPSvdgaaddw 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 160 -------FEEMRRnVRKASSTLKVMISIGGQYNSGEFSGLVSNETSRNLFVNSIATFVRDYDIDGVDIFWTWPKHS---- 228
Cdd:COG3325    80 dqplkgnFNQLKK-LKAKNPNLKVLISIGGWTWSKGFSDAAATPASRAAFVDSCVDLLRKYNFDGIDIDWEYPGSGgapg 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 229 ------DENNYLMFIRELRYAFTELQKKLNRKetFVISLVISRNVNHLSK--LVEFSNFVDFINI--YSFN-SYLYQVGP 297
Cdd:COG3325   159 nvyrpeDKANFTALLKELRAQLDALGAETGKH--YLLTAAAPAGPDKLDGieLPKVAQYLDYVNVmtYDFHgAWSPTTGH 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 298 DSPLYG------GGSRNVDEIMKYYIcKTG-QPSKFNIIVSFHATYWEGAElplrDDSDDIFKD-QNSAKGGF---AVRW 366
Cdd:COG3325   237 QAPLYDspkdpeAQGYSVDSAVQAYL-AAGvPASKLVLGVPFYGRGWTGVT----GGNNGLYQPaTGPAPGTWeagVNDY 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 367 RELLQQKWDMSNIK--FHNLTKTSYMWIPGPPTrFMTLEDEKSLREKNRYVADHNIGGITMWTIDQDDGDHTLLKVVSSA 444
Cdd:COG3325   312 KDLKALYLGSNGYTryWDDVAKAPYLYNGDTGT-FISYDDPRSIAAKADYVKDKGLGGVMFWELSGDTADGTLLNAIGEG 390
GH18_chitinase cd06548
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ...
114-431 1.94e-36

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: 136.61  E-value: 1.94e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 114 IVGYFAEF-----ENTALTRKQLRMLTHIVFLFA--FPKNGTITFGGESSSQKFEEMR-----------------RNVRK 169
Cdd:cd06548     1 VVGYFTNWgiygrNYFVTDDIPADKLTHINYAFAdiDGDGGVVTSDDEAADEAAQSVDggadtddqplkgnfgqlRKLKQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 170 ASSTLKVMISIGGQYNSGEFSGLVSNETSRNLFVNSIATFVRDYDIDGVDIFWTWP----------KHSDENNYLMFIRE 239
Cdd:cd06548    81 KNPHLKILLSIGGWTWSGGFSDAAATEASRAKFADSAVDFIRKYGFDGIDIDWEYPgsggapgnvaRPEDKENFTLLLKE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 240 LRYAFTELQKKLNRKetFVISLVISRNVNHLSKLV--EFSNFVDFINI--YSFN-SYLYQVGPDSPLYG-----GGSRNV 309
Cdd:cd06548   161 LREALDALGAETGRK--YLLTIAAPAGPDKLDKLEvaEIAKYLDFINLmtYDFHgAWSNTTGHHSNLYAspadpPGGYSV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 310 DEIMKYYICKTGQPSKFNIIVSFHATYWEGAELplrddsddifkdqnsakggfavrwrellqqKWDmsnikfhNLTKTSY 389
Cdd:cd06548   239 DAAVNYYLSAGVPPEKLVLGVPFYGRGWTGYTR------------------------------YWD-------EVAKAPY 281
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1831508934 390 MWIPGPPTrFMTLEDEKSLREKNRYVADHNIGGITMWTIDQD 431
Cdd:cd06548   282 LYNPSTKT-FISYDDPRSIKAKADYVKDKGLGGVMFWELSGD 322
 
Name Accession Description Interval E-value
Glyco_18 smart00636
Glyco_18 domain;
113-431 1.60e-97

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 296.13  E-value: 1.60e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934  113 RIVGYFAEFENTA----LTRKQLRMLTHIVFLFAFPK-NGTITFGGESSS-QKFEEMRRnVRKASSTLKVMISIGGQYNS 186
Cdd:smart00636   1 RVVGYFTNWGVYGrnfpVDDIPASKLTHIIYAFANIDpDGTVTIGDEWADiGNFGQLKA-LKKKNPGLKVLLSIGGWTES 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934  187 GEFSGLVSNETSRNLFVNSIATFVRDYDIDGVDIFWTWP--KHSDENNYLMFIRELRYAFTELQKklnRKETFVISLVIS 264
Cdd:smart00636  80 DNFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWEYPggRGDDRENYTALLKELREALDKEGA---EGKGYLLTIAVP 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934  265 RNVNHLSK----LVEFSNFVDFINIYS---FNSYLYQVGPDSPLYGGGS----RNVDEIMKYYICKTGQPSKFNIIVSFH 333
Cdd:smart00636 157 AGPDKIDKgygdLPAIAKYLDFINLMTydfHGAWSNPTGHNAPLYAGPGdpekYNVDYAVKYYLCKGVPPSKLVLGIPFY 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934  334 ATYWEGAELPLRDDSDDIFKDQNSAKGGFA---VRWRELLQQKwdMSNIKFHNLTKTSYMWIPGPPTrFMTLEDEKSLRE 410
Cdd:smart00636 237 GRGWTLVDGSNNGPGAPFTGPATGGPGTWEggvVDYREICKLL--GATVVYDDTAKAPYAYNPGTGQ-WVSYDDPRSIKA 313
                          330       340
                   ....*....|....*....|.
gi 1831508934  411 KNRYVADHNIGGITMWTIDQD 431
Cdd:smart00636 314 KADYVKDKGLGGVMIWELDAD 334
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
113-431 1.00e-85

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 265.09  E-value: 1.00e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 113 RIVGYFAEFENTALTR-KQLRMLTHIVFLFA--FPKNGTITFGgESSSQKFEEMRRNVRKASSTLKVMISIGGQYNSGEF 189
Cdd:pfam00704   1 RIVGYYTSWGVYRNGNfLPSDKLTHIIYAFAniDGSDGTLFIG-DWDLGNFEQLKKLKKQKNPGVKVLLSIGGWTDSTGF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 190 SGLVSNETSRNLFVNSIATFVRDYDIDGVDIFWTWPKH--SDENNYLMFIRELRYAFTELQkklnRKETFVISLVISRNV 267
Cdd:pfam00704  80 SLMASNPASRKKFADSIVSFLRKYGFDGIDIDWEYPGGnpEDKENYDLLLRELRAALDEAK----GGKKYLLSAAVPASY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 268 NHLSK---LVEFSNFVDFINIYSF---NSYLYQVGPDSPLYGGGSRNVDEIMKYYICKTGQPSKFNIIVSFHATYWEGAE 341
Cdd:pfam00704 156 PDLDKgydLPKIAKYLDFINVMTYdfhGSWDNVTGHHAPLYGGGSYNVDYAVKYYLKQGVPASKLVLGVPFYGRSWTLVN 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 342 LPLRDDSDDIFkdqnsakggfavRWRELLQQKWD-MSNIKFHNLTKTSYMWIpgpPTRFMTLEDEKSLREKNRYVADHNI 420
Cdd:pfam00704 236 GSGNTWEDGVL------------AYKEICNLLKDnGATVVWDDVAKAPYVYD---GDQFITYDDPRSIATKVDYVKAKGL 300
                         330
                  ....*....|.
gi 1831508934 421 GGITMWTIDQD 431
Cdd:pfam00704 301 GGVMIWSLDAD 311
ChiA COG3325
Chitinase, GH18 family [Carbohydrate transport and metabolism];
93-444 7.39e-45

Chitinase, GH18 family [Carbohydrate transport and metabolism];


Pssm-ID: 442554 [Multi-domain]  Cd Length: 391  Bit Score: 160.85  E-value: 7.39e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934  93 TKLVQKSDENFSPPAafcGKRIVGYFAEF--ENTALTRKQLRM--LTHIVFLFAFPK-NGTITFGGESSSQK-------- 159
Cdd:COG3325     3 TASVSDTAAAATATS---GKRVVGYFTQWgiYGRNYLVKDIPAskLTHINYAFANVDpDGKCSVGDAWAKPSvdgaaddw 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 160 -------FEEMRRnVRKASSTLKVMISIGGQYNSGEFSGLVSNETSRNLFVNSIATFVRDYDIDGVDIFWTWPKHS---- 228
Cdd:COG3325    80 dqplkgnFNQLKK-LKAKNPNLKVLISIGGWTWSKGFSDAAATPASRAAFVDSCVDLLRKYNFDGIDIDWEYPGSGgapg 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 229 ------DENNYLMFIRELRYAFTELQKKLNRKetFVISLVISRNVNHLSK--LVEFSNFVDFINI--YSFN-SYLYQVGP 297
Cdd:COG3325   159 nvyrpeDKANFTALLKELRAQLDALGAETGKH--YLLTAAAPAGPDKLDGieLPKVAQYLDYVNVmtYDFHgAWSPTTGH 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 298 DSPLYG------GGSRNVDEIMKYYIcKTG-QPSKFNIIVSFHATYWEGAElplrDDSDDIFKD-QNSAKGGF---AVRW 366
Cdd:COG3325   237 QAPLYDspkdpeAQGYSVDSAVQAYL-AAGvPASKLVLGVPFYGRGWTGVT----GGNNGLYQPaTGPAPGTWeagVNDY 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 367 RELLQQKWDMSNIK--FHNLTKTSYMWIPGPPTrFMTLEDEKSLREKNRYVADHNIGGITMWTIDQDDGDHTLLKVVSSA 444
Cdd:COG3325   312 KDLKALYLGSNGYTryWDDVAKAPYLYNGDTGT-FISYDDPRSIAAKADYVKDKGLGGVMFWELSGDTADGTLLNAIGEG 390
GH18_chitinase cd06548
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ...
114-431 1.94e-36

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: 136.61  E-value: 1.94e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 114 IVGYFAEF-----ENTALTRKQLRMLTHIVFLFA--FPKNGTITFGGESSSQKFEEMR-----------------RNVRK 169
Cdd:cd06548     1 VVGYFTNWgiygrNYFVTDDIPADKLTHINYAFAdiDGDGGVVTSDDEAADEAAQSVDggadtddqplkgnfgqlRKLKQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 170 ASSTLKVMISIGGQYNSGEFSGLVSNETSRNLFVNSIATFVRDYDIDGVDIFWTWP----------KHSDENNYLMFIRE 239
Cdd:cd06548    81 KNPHLKILLSIGGWTWSGGFSDAAATEASRAKFADSAVDFIRKYGFDGIDIDWEYPgsggapgnvaRPEDKENFTLLLKE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 240 LRYAFTELQKKLNRKetFVISLVISRNVNHLSKLV--EFSNFVDFINI--YSFN-SYLYQVGPDSPLYG-----GGSRNV 309
Cdd:cd06548   161 LREALDALGAETGRK--YLLTIAAPAGPDKLDKLEvaEIAKYLDFINLmtYDFHgAWSNTTGHHSNLYAspadpPGGYSV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 310 DEIMKYYICKTGQPSKFNIIVSFHATYWEGAELplrddsddifkdqnsakggfavrwrellqqKWDmsnikfhNLTKTSY 389
Cdd:cd06548   239 DAAVNYYLSAGVPPEKLVLGVPFYGRGWTGYTR------------------------------YWD-------EVAKAPY 281
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1831508934 390 MWIPGPPTrFMTLEDEKSLREKNRYVADHNIGGITMWTIDQD 431
Cdd:cd06548   282 LYNPSTKT-FISYDDPRSIKAKADYVKDKGLGGVMFWELSGD 322
GH18_chitolectin_chitotriosidase cd02872
This conserved domain family includes a large number of catalytically inactive chitinase-like ...
135-444 7.00e-33

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: 127.68  E-value: 7.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 135 THIVFLFA-FPKNGTITFGGESSSQKFEEMRR--NVRKASSTLKVMISIGGqYN--SGEFSGLVSNETSRNLFVNSIATF 209
Cdd:cd02872    29 THIIYAFAgLNPDGNIIILDEWNDIDLGLYERfnALKEKNPNLKTLLAIGG-WNfgSAKFSAMAASPENRKTFIKSAIAF 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 210 VRDYDIDGVDIFWTWPKH-----SDENNYLMFIRELRYAFtelQKKLNRKE--------TFVISlvISRNVNHLSKLvef 276
Cdd:cd02872   108 LRKYGFDGLDLDWEYPGQrggppEDKENFVTLLKELREAF---EPEAPRLLltaavsagKETID--AAYDIPEISKY--- 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 277 snfVDFINI--YSFN-SYLYQVGPDSPLYGGGS-------RNVDEIMKYYICKTGQPSKfnIIVSFhATYweGAELPLRD 346
Cdd:cd02872   180 ---LDFINVmtYDFHgSWEGVTGHNSPLYAGSAdtgdqkyLNVDYAIKYWLSKGAPPEK--LVLGI-PTY--GRSFTLAS 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 347 DSDDIFKDQNSAKG---------GFAVRWR--ELLQQKWdmsNIKFHNLTKTSYM-----WIpgpptrfmTLEDEKSLRE 410
Cdd:cd02872   252 PSNTGVGAPASGPGtagpytreaGFLAYYEicEFLKSGW---TVVWDDEQKVPYAykgnqWV--------GYDDEESIAL 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1831508934 411 KNRYVADHNIGGITMWTIDQDD-------GDHTLLKVVSSA 444
Cdd:cd02872   321 KVQYLKSKGLGGAMVWSIDLDDfrgtcgqGKYPLLNAINRA 361
GH18_chitinase-like cd00598
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ...
114-289 2.09e-28

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: 111.32  E-value: 2.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 114 IVGYFAEFENTALTRK---QLRMLTHIVFLFAFPK--NGTITFGGESSSQKFEEMRRNVRKASsTLKVMISIGGQYNSGE 188
Cdd:cd00598     1 VICYYDGWSSGRGPDPtdiPLSLCTHIIYAFAEISsdGSLNLFGDKSEEPLKGALEELASKKP-GLKVLISIGGWTDSSP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 189 FSgLVSNETSRNLFVNSIATFVRDYDIDGVDIFWTWP---KHSDENNYLMFIRELRYAFtelqkklnRKETFVISLVIS- 264
Cdd:cd00598    80 FT-LASDPASRAAFANSLVSFLKTYGFDGVDIDWEYPgaaDNSDRENFITLLRELRSAL--------GAANYLLTIAVPa 150
                         170       180
                  ....*....|....*....|....*..
gi 1831508934 265 --RNVNHLSKLVEFSNFVDFINIYSFN 289
Cdd:cd00598   151 syFDLGYAYDVPAIGDYVDFVNVMTYD 177
GH18_3CO4_chitinase cd06545
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an ...
114-289 1.20e-12

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: 67.48  E-value: 1.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 114 IVGYFA--EFENTALTRKQLRMLTHIVFLFAFPK-NGTITFGGESSsqkfeEMRRNVRKA-SSTLKVMISIGGqyNS-GE 188
Cdd:cd06545     1 VVGYLPnyDDLNALSPTIDFSKLTHINLAFANPDaNGTLNANPVRS-----ELNSVVNAAhAHNVKILISLAG--GSpPE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 189 FSGLVSNETSRNLFVNSIATFVRDYDIDGVDIFWTWPkHSDENNYLMFIRELRYAFtelqkklnRKETFVISLVISRNVN 268
Cdd:cd06545    74 FTAALNDPAKRKALVDKIINYVVSYNLDGIDVDLEGP-DVTFGDYLVFIRALYAAL--------KKEGKLLTAAVSSWNG 144
                         170       180
                  ....*....|....*....|.
gi 1831508934 269 HLSKLVEFSNFvDFINIYSFN 289
Cdd:cd06545   145 GAVSDSTLAYF-DFINIMSYD 164
GH18_plant_chitinase_class_V cd02879
The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the ...
132-291 2.52e-11

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: 64.31  E-value: 2.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 132 RMLTHIVFLFAFPKNGTITFG-GESSSQKFEEMRRNVRKASSTLKVMISIGG-QYNSGEFSGLVSNETSRNLFVNSIATF 209
Cdd:cd02879    24 SLFTHLFYAFADLDPSTYEVViSPSDESEFSTFTETVKRKNPSVKTLLSIGGgGSDSSAFAAMASDPTARKAFINSSIKV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 210 VRDYDIDGVDIFWTWPK-HSDENNYLMFIRELRYAFTELQKKLNRKEtfvisLVISRNVNHLSKLV-----------EFS 277
Cdd:cd02879   104 ARKYGFDGLDLDWEFPSsQVEMENFGKLLEEWRAAVKDEARSSGRPP-----LLLTAAVYFSPILFlsddsvsypieAIN 178
                         170
                  ....*....|....
gi 1831508934 278 NFVDFINIYSFNSY 291
Cdd:cd02879   179 KNLDWVNVMAYDYY 192
GH18_IDGF cd02873
The IDGF's (imaginal disc growth factors) are a family of growth factors identified in insects ...
174-336 9.73e-11

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: 63.49  E-value: 9.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 174 LKVMISIGGQYNSGEFSG------LVSNETSRNLFVNSIATFVRDYDIDGVDIFWTWPK------HSDENNYLMFIR--- 238
Cdd:cd02873    75 LKVLLSVGGDRDTDEEGEnekyllLLESSESRNAFINSAHSLLKTYGFDGLDLAWQFPKnkpkkvRGTFGSAWHSFKklf 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 239 -----------ELRYAFTELQKKLN---RKETFVISLVISRNVNhlSKLV----EFSNFVDFINIYSFNSYLYQVGPD-- 298
Cdd:cd02873   155 tgdsvvdekaaEHKEQFTALVRELKnalRPDGLLLTLTVLPHVN--STWYfdvpAIANNVDFVNLATFDFLTPERNPEea 232
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1831508934 299 ---SPLYGGGSR----NVDEIMKYYICKTGQPSKFNIIVsfhATY 336
Cdd:cd02873   233 dytAPIYELYERnphhNVDYQVKYWLNQGTPASKLNLGI---ATY 274
GH18_zymocin_alpha cd02878
Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle ...
115-241 3.50e-07

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: 51.93  E-value: 3.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 115 VGYFaefENTALTRKQLRM---------LTHIVFLFAfpkngTITFGGESSSQKFEEMRRNVRKASSTLKVmISIGGQyn 185
Cdd:cd02878     3 IAYF---EAYNLDRPCLNMdvtqidtskYTHIHFAFA-----NITSDFSVDVSSVQEQFSDFKKLKGVKKI-LSFGGW-- 71
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831508934 186 sgEFSGLVS---------NETSRNLFVNSIATFVRDYDIDGVDIFWTWP-----------KHSDENNYLMFIRELR 241
Cdd:cd02878    72 --DFSTSPStyqifrdavKPANRDTFANNVVNFVNKYNLDGVDFDWEYPgapdipgipagDPDDGKNYLEFLKLLK 145
GH18_chitinase_D-like cd02871
GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes ...
112-220 2.31e-06

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: 49.26  E-value: 2.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 112 KRIVGYFAEFENTALTRKQ-LRMLTH----IVFLFAFP---KNGTITFGGESSSQKF--EEMRRNVR-KASSTLKVMISI 180
Cdd:cd02871     1 KVLVGYWHNWDNGAGSGRQdLDDVPSkynvINVAFAEPtsdGGGEVTFNNGSSPGGYspAEFKADIKaLQAKGKKVLISI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1831508934 181 GGQYNSGEfsglVSNETSRNLFVNSIATFVRDYDIDGVDI 220
Cdd:cd02871    81 GGANGHVD----LNHTAQEDNFVDSIVAIIKEYGFDGLDI 116
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
105-220 6.47e-06

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 48.60  E-value: 6.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 105 PPAAFCGKRIVGYFAEFENTAltrKQLRML----THIVFLFAFPK-----NGTITF---------GGESSSQKFEEMRRn 166
Cdd:COG3469   208 PTPGLPKHVLVGYWHNFDNGS---GYIRLSdvpdKYDVINVAFAEptgatNGTVTFtldpgssspGGYTDAQFKADIAA- 283
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1831508934 167 vrKASSTLKVMISIGGQynSGEFSglVSNETSRNLFVNSIATFVRDYDIDGVDI 220
Cdd:COG3469   284 --LQAQGKKVLLSIGGA--NGTVQ--LNTAAAADNFVNSVIALIDEYGFDGLDI 331
GH18_CFLE_spore_hydrolase cd02874
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ...
114-251 2.91e-04

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: 42.64  E-value: 2.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 114 IVGYFA--EFENTALTRKQLRMLTHIV-FLFAFPKNGTITfGGESSSQKFEEMRRNVrkasstlKVMISI----GGQYNS 186
Cdd:cd02874     4 VLGYYTprNGSDYESLRANAPYLTYIApFWYGVDADGTLT-GLPDERLIEAAKRRGV-------KPLLVItnltNGNFDS 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508934 187 GEFSGLVSNETSRNLFVNSIATFVRDYDIDGVDI-----FWtwpkhSDENNYLMFIRELRYAFTELQKKL 251
Cdd:cd02874    76 ELAHAVLSNPEARQRLINNILALAKKYGYDGVNIdfenvPP-----EDREAYTQFLRELSDRLHPAGYTL 140
 
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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