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Conserved domains on  [gi|24582726|ref|NP_609190|]
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uncharacterized protein Dmel_CG8460 [Drosophila melanogaster]

Protein Classification

GH18_SI-CLP domain-containing protein( domain architecture ID 10120846)

GH18_SI-CLP domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GH18_SI-CLP cd02876
Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein ...
81-402 1.06e-174

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: 489.90  E-value: 1.06e-174
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726  81 FNGTTLGYVTPWNSHGYDVAKIFAKKFDIISPVWLQIVKQGDRYAVAGTHDIDAGWLTDVRRKGKQVhnqrtvKVFPRFI 160
Cdd:cd02876   1 FQGPVLGYVTPWNSHGYDVAKKFAAKFTHVSPVWLQIKRKGNKFVIEGTHDIDKGWIEEVRKANKNI------KILPRVL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726 161 FDHFTDRDIKLLLSDAQERTKVNDVLIKCCKDNGFDGLVLEVWSQLAGRI---DDKILYTLVLQMAKELQKQQLRLILVI 237
Cdd:cd02876  75 FEGWSYQDLQSLLNDEQEREKLIKLLVTTAKKNHFDGIVLEVWSQLAAYGvpdKRKELIQLVIHLGETLHSANLKLILVI 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726 238 PPFRK--ETGHLFGEKHMDKLFKHIYAFSLMTYDFSSVQRPGANAPLYFVRKAVETIAPEGCAdmtaKRAKILLGLNMYG 315
Cdd:cd02876 155 PPPREkgNQNGLFTRKDFEKLAPHVDGFSLMTYDYSSPQRPGPNAPLSWVRSCLELLLPESGK----KRAKILLGLNFYG 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726 316 NDYTP-DGGGPITFSQYLDLVRHVKKHLTYDERDVENFFEIKNDDGRHIVFYPTLYSINERIKLAQELGTGISIWELGQG 394
Cdd:cd02876 231 NDYTLpGGGGAITGSEYLKLLKSNKPKLQWDEKSAEHFFEYKNKGGKHAVFYPTLKSIQLRLDLAKELGTGISIWELGQG 310

                ....*...
gi 24582726 395 LNYFYDLF 402
Cdd:cd02876 311 LDYFYDLL 318
 
Name Accession Description Interval E-value
GH18_SI-CLP cd02876
Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein ...
81-402 1.06e-174

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: 489.90  E-value: 1.06e-174
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726  81 FNGTTLGYVTPWNSHGYDVAKIFAKKFDIISPVWLQIVKQGDRYAVAGTHDIDAGWLTDVRRKGKQVhnqrtvKVFPRFI 160
Cdd:cd02876   1 FQGPVLGYVTPWNSHGYDVAKKFAAKFTHVSPVWLQIKRKGNKFVIEGTHDIDKGWIEEVRKANKNI------KILPRVL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726 161 FDHFTDRDIKLLLSDAQERTKVNDVLIKCCKDNGFDGLVLEVWSQLAGRI---DDKILYTLVLQMAKELQKQQLRLILVI 237
Cdd:cd02876  75 FEGWSYQDLQSLLNDEQEREKLIKLLVTTAKKNHFDGIVLEVWSQLAAYGvpdKRKELIQLVIHLGETLHSANLKLILVI 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726 238 PPFRK--ETGHLFGEKHMDKLFKHIYAFSLMTYDFSSVQRPGANAPLYFVRKAVETIAPEGCAdmtaKRAKILLGLNMYG 315
Cdd:cd02876 155 PPPREkgNQNGLFTRKDFEKLAPHVDGFSLMTYDYSSPQRPGPNAPLSWVRSCLELLLPESGK----KRAKILLGLNFYG 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726 316 NDYTP-DGGGPITFSQYLDLVRHVKKHLTYDERDVENFFEIKNDDGRHIVFYPTLYSINERIKLAQELGTGISIWELGQG 394
Cdd:cd02876 231 NDYTLpGGGGAITGSEYLKLLKSNKPKLQWDEKSAEHFFEYKNKGGKHAVFYPTLKSIQLRLDLAKELGTGISIWELGQG 310

                ....*...
gi 24582726 395 LNYFYDLF 402
Cdd:cd02876 311 LDYFYDLL 318
Glyco_18 smart00636
Glyco_18 domain;
86-393 3.48e-34

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 129.34  E-value: 3.48e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726     86 LGYVTPWNSHG--YDVAKIFAKKFDIISPVWLQI-----VKQGDRYAVAGTHdidaGWLTDVRRKgkqvhnQRTVKVFPR 158
Cdd:smart00636   3 VGYFTNWGVYGrnFPVDDIPASKLTHIIYAFANIdpdgtVTIGDEWADIGNF----GQLKALKKK------NPGLKVLLS 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726    159 F----IFDHFTDrdiklLLSDAQERTKVNDVLIKCCKDNGFDGLVLEvWSQLAGRIDDKILYTLVLQMAKE------LQK 228
Cdd:smart00636  73 IggwtESDNFSS-----MLSDPASRKKFIDSIVSFLKKYGFDGIDID-WEYPGGRGDDRENYTALLKELREaldkegAEG 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726    229 QQLRLILVIPPFRKETGHLFGekHMDKLFKHIYAFSLMTYDFSSV--QRPGANAPLYFVRKAVETIAPEGCAD----MTA 302
Cdd:smart00636 147 KGYLLTIAVPAGPDKIDKGYG--DLPAIAKYLDFINLMTYDFHGAwsNPTGHNAPLYAGPGDPEKYNVDYAVKyylcKGV 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726    303 KRAKILLGLNMYGNDYT---------------PDGGGPITFSQ----YLDLVRHVKKHLTYDErDVENFFEIkNDDGRHI 363
Cdd:smart00636 225 PPSKLVLGIPFYGRGWTlvdgsnngpgapftgPATGGPGTWEGgvvdYREICKLLGATVVYDD-TAKAPYAY-NPGTGQW 302
                          330       340       350
                   ....*....|....*....|....*....|.
gi 24582726    364 VFYPTLYSINERIKLAQELGT-GISIWELGQ 393
Cdd:smart00636 303 VSYDDPRSIKAKADYVKDKGLgGVMIWELDA 333
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
84-393 1.08e-20

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 91.75  E-value: 1.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726    84 TTLGYVTPWNSHGyDVAKIFAKKFDIIspVWLQIVKQGDRYAVaGTHDIDAGWLTDVRRKGKQVHnqRTVKVFPRFIFDH 163
Cdd:pfam00704   1 RIVGYYTSWGVYR-NGNFLPSDKLTHI--IYAFANIDGSDGTL-FIGDWDLGNFEQLKKLKKQKN--PGVKVLLSIGGWT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726   164 FTDRdIKLLLSDAQERTKVNDVLIKCCKDNGFDGLVLEvWSQLAGRIDDKILYTLVLQMAKE-----LQKQQLRLILVIP 238
Cdd:pfam00704  75 DSTG-FSLMASNPASRKKFADSIVSFLRKYGFDGIDID-WEYPGGNPEDKENYDLLLRELRAaldeaKGGKKYLLSAAVP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726   239 PFRKetgHLFGEKHMDKLFKHIYAFSLMTYDFSS--VQRPGANAPLYFVRKAVETIAPEGCADMTAKRAKILLGLNMYGN 316
Cdd:pfam00704 153 ASYP---DLDKGYDLPKIAKYLDFINVMTYDFHGswDNVTGHHAPLYGGGSYNVDYAVKYYLKQGVPASKLVLGVPFYGR 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726   317 DYTPDGGGPITFS-------QYLDLVRHVKKHLTYDERDVENFFEikndDGRHIVFYPTLYSINERIKLAQE--LGtGIS 387
Cdd:pfam00704 230 SWTLVNGSGNTWEdgvlaykEICNLLKDNGATVVWDDVAKAPYVY----DGDQFITYDDPRSIATKVDYVKAkgLG-GVM 304

                  ....*.
gi 24582726   388 IWELGQ 393
Cdd:pfam00704 305 IWSLDA 310
 
Name Accession Description Interval E-value
GH18_SI-CLP cd02876
Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein ...
81-402 1.06e-174

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: 489.90  E-value: 1.06e-174
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726  81 FNGTTLGYVTPWNSHGYDVAKIFAKKFDIISPVWLQIVKQGDRYAVAGTHDIDAGWLTDVRRKGKQVhnqrtvKVFPRFI 160
Cdd:cd02876   1 FQGPVLGYVTPWNSHGYDVAKKFAAKFTHVSPVWLQIKRKGNKFVIEGTHDIDKGWIEEVRKANKNI------KILPRVL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726 161 FDHFTDRDIKLLLSDAQERTKVNDVLIKCCKDNGFDGLVLEVWSQLAGRI---DDKILYTLVLQMAKELQKQQLRLILVI 237
Cdd:cd02876  75 FEGWSYQDLQSLLNDEQEREKLIKLLVTTAKKNHFDGIVLEVWSQLAAYGvpdKRKELIQLVIHLGETLHSANLKLILVI 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726 238 PPFRK--ETGHLFGEKHMDKLFKHIYAFSLMTYDFSSVQRPGANAPLYFVRKAVETIAPEGCAdmtaKRAKILLGLNMYG 315
Cdd:cd02876 155 PPPREkgNQNGLFTRKDFEKLAPHVDGFSLMTYDYSSPQRPGPNAPLSWVRSCLELLLPESGK----KRAKILLGLNFYG 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726 316 NDYTP-DGGGPITFSQYLDLVRHVKKHLTYDERDVENFFEIKNDDGRHIVFYPTLYSINERIKLAQELGTGISIWELGQG 394
Cdd:cd02876 231 NDYTLpGGGGAITGSEYLKLLKSNKPKLQWDEKSAEHFFEYKNKGGKHAVFYPTLKSIQLRLDLAKELGTGISIWELGQG 310

                ....*...
gi 24582726 395 LNYFYDLF 402
Cdd:cd02876 311 LDYFYDLL 318
Glyco_18 smart00636
Glyco_18 domain;
86-393 3.48e-34

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 129.34  E-value: 3.48e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726     86 LGYVTPWNSHG--YDVAKIFAKKFDIISPVWLQI-----VKQGDRYAVAGTHdidaGWLTDVRRKgkqvhnQRTVKVFPR 158
Cdd:smart00636   3 VGYFTNWGVYGrnFPVDDIPASKLTHIIYAFANIdpdgtVTIGDEWADIGNF----GQLKALKKK------NPGLKVLLS 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726    159 F----IFDHFTDrdiklLLSDAQERTKVNDVLIKCCKDNGFDGLVLEvWSQLAGRIDDKILYTLVLQMAKE------LQK 228
Cdd:smart00636  73 IggwtESDNFSS-----MLSDPASRKKFIDSIVSFLKKYGFDGIDID-WEYPGGRGDDRENYTALLKELREaldkegAEG 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726    229 QQLRLILVIPPFRKETGHLFGekHMDKLFKHIYAFSLMTYDFSSV--QRPGANAPLYFVRKAVETIAPEGCAD----MTA 302
Cdd:smart00636 147 KGYLLTIAVPAGPDKIDKGYG--DLPAIAKYLDFINLMTYDFHGAwsNPTGHNAPLYAGPGDPEKYNVDYAVKyylcKGV 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726    303 KRAKILLGLNMYGNDYT---------------PDGGGPITFSQ----YLDLVRHVKKHLTYDErDVENFFEIkNDDGRHI 363
Cdd:smart00636 225 PPSKLVLGIPFYGRGWTlvdgsnngpgapftgPATGGPGTWEGgvvdYREICKLLGATVVYDD-TAKAPYAY-NPGTGQW 302
                          330       340       350
                   ....*....|....*....|....*....|.
gi 24582726    364 VFYPTLYSINERIKLAQELGT-GISIWELGQ 393
Cdd:smart00636 303 VSYDDPRSIKAKADYVKDKGLgGVMIWELDA 333
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
84-393 1.08e-20

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 91.75  E-value: 1.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726    84 TTLGYVTPWNSHGyDVAKIFAKKFDIIspVWLQIVKQGDRYAVaGTHDIDAGWLTDVRRKGKQVHnqRTVKVFPRFIFDH 163
Cdd:pfam00704   1 RIVGYYTSWGVYR-NGNFLPSDKLTHI--IYAFANIDGSDGTL-FIGDWDLGNFEQLKKLKKQKN--PGVKVLLSIGGWT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726   164 FTDRdIKLLLSDAQERTKVNDVLIKCCKDNGFDGLVLEvWSQLAGRIDDKILYTLVLQMAKE-----LQKQQLRLILVIP 238
Cdd:pfam00704  75 DSTG-FSLMASNPASRKKFADSIVSFLRKYGFDGIDID-WEYPGGNPEDKENYDLLLRELRAaldeaKGGKKYLLSAAVP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726   239 PFRKetgHLFGEKHMDKLFKHIYAFSLMTYDFSS--VQRPGANAPLYFVRKAVETIAPEGCADMTAKRAKILLGLNMYGN 316
Cdd:pfam00704 153 ASYP---DLDKGYDLPKIAKYLDFINVMTYDFHGswDNVTGHHAPLYGGGSYNVDYAVKYYLKQGVPASKLVLGVPFYGR 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726   317 DYTPDGGGPITFS-------QYLDLVRHVKKHLTYDERDVENFFEikndDGRHIVFYPTLYSINERIKLAQE--LGtGIS 387
Cdd:pfam00704 230 SWTLVNGSGNTWEdgvlaykEICNLLKDNGATVVWDDVAKAPYVY----DGDQFITYDDPRSIATKVDYVKAkgLG-GVM 304

                  ....*.
gi 24582726   388 IWELGQ 393
Cdd:pfam00704 305 IWSLDA 310
GH18_CFLE_spore_hydrolase cd02874
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ...
84-393 3.98e-20

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: 90.02  E-value: 3.98e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726  84 TTLGYVTPWNSHGYDVAKIFAKKFDIISPVWLQIVKQGDRYAVAGTHDIDAGWltdvrrkgkqvhnQRTVKVFPRF--IF 161
Cdd:cd02874   3 EVLGYYTPRNGSDYESLRANAPYLTYIAPFWYGVDADGTLTGLPDERLIEAAK-------------RRGVKPLLVItnLT 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726 162 DHFTDRD-IKLLLSDAQERTKVNDVLIKCCKDNGFDGLVLE---VwsqlagRIDDKILYT-LVLQMAKELQKQQLRL-IL 235
Cdd:cd02874  70 NGNFDSElAHAVLSNPEARQRLINNILALAKKYGYDGVNIDfenV------PPEDREAYTqFLRELSDRLHPAGYTLsTA 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726 236 VIPPFRKETGHLFGEKH-MDKLFKHIYAFSLMTYDF---SSVqrPGANAPLYFVRK----AVETIAPEgcadmtakraKI 307
Cdd:cd02874 144 VVPKTSADQFGNWSGAYdYAAIGKIVDFVVLMTYDWhwrGGP--PGPVAPIGWVERvlqyAVTQIPRE----------KI 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726 308 LLGLNMYGNDYT--PDGGGP---ITFSQYLDLVRHVKKHLTYDERDVENFFEIKNDDGR-HIVFYPTLYSINERIKLAQE 381
Cdd:cd02874 212 LLGIPLYGYDWTlpYKKGGKastISPQQAINLAKRYGAEIQYDEEAQSPFFRYVDEQGRrHEVWFEDARSLQAKFELAKE 291
                       330
                ....*....|...
gi 24582726 382 LG-TGISIWELGQ 393
Cdd:cd02874 292 YGlRGVSYWRLGL 304
GH18_trifunctional cd06549
GH18 domain of an uncharacterized family of bacterial proteins, which share a common ...
86-393 7.11e-09

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: 56.65  E-value: 7.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726  86 LGYVTPWNSHGYDVAKIFAKKFDIISPVWLQIVKQGDRYAVAgthdidagwlTDVRRKGKQVHNQRTVKVFP---RFIFD 162
Cdd:cd06549   3 LAFYTPWDDASFASLKRHAPRLDWLVPEWLNLTGPEGRIDVF----------VDPQGVAIIAAAKAHPKVLPlvqNISGG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726 163 HFTDRDIKLLLSDAQERTKVNDVLIKCCKDNGFDGLVLEVWSQLAgriDDKILYtlvLQMAKELQKQ---QLRLILVIPP 239
Cdd:cd06549  73 AWDGKNIARLLADPSARAKFIANIAAYLERNQADGIVLDFEELPA---DDLPKY---VAFLSELRRRlpaQGKQLTVTVP 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726 240 FRKETGHLFGE-KHMDKLFkhiyafsLMTYDFSSVQ-RPGANAPLYF----VRKAVETIAPEgcadmtakraKILLGLNM 313
Cdd:cd06549 147 ADEADWNLKALaRNADKLI-------LMAYDEHYQGgAPGPIASQDWfesnLAQAVKKLPPE----------KLIVALGS 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726 314 YGNDYTPDGGGP-ITFSQYLDLVRHVKKHLTYDERDVENFFEIKNDDG-RHIVFYPTLYSINERIKLAQELG-TGISIWE 390
Cdd:cd06549 210 YGYDWTKGGNTKaISSEAAWLLAAHASAAVKFDDKASNATYFFYDDEGvSHEVWMLDAVTLFNQLKAVQRLGpAGVALWR 289

                ...
gi 24582726 391 LGQ 393
Cdd:cd06549 290 LGS 292
GH18_chitinase-like cd00598
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ...
87-280 1.58e-08

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: 54.31  E-value: 1.58e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726  87 GYVTPWNSH-GYDVAKIFAKKFDIISPVWLQIVKQGDR-YAVAGTHDIDAGWLTDVRRKGKqvhnqrTVKVFPRFIFdhF 164
Cdd:cd00598   3 CYYDGWSSGrGPDPTDIPLSLCTHIIYAFAEISSDGSLnLFGDKSEEPLKGALEELASKKP------GLKVLISIGG--W 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582726 165 TDRDIKLLLSDAQERTKVNDVLIKCCKDNGFDGLVLEVWSQLAGRIDDKILYTLVLqmaKELQKQ--QLRLILVIPPFRK 242
Cdd:cd00598  75 TDSSPFTLASDPASRAAFANSLVSFLKTYGFDGVDIDWEYPGAADNSDRENFITLL---RELRSAlgAANYLLTIAVPAS 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 24582726 243 ETGHLFGEKhMDKLFKHIYAFSLMTYD------FSSVQRPGANA 280
Cdd:cd00598 152 YFDLGYAYD-VPAIGDYVDFVNVMTYDlvlgvpFYSLGAKAKYA 194
 
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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