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Conserved domains on  [gi|1242811383|ref|XP_022286365.1|]
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chitinase domain-containing protein 1-like isoform X2 [Crassostrea virginica]

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 ...
73-386 3.50e-162

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: 457.54  E-value: 3.50e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383  73 FPGITLAYVTPWNNHGYDIAKSFSQKFSYVSPVWLQIKRRkGGTFFIQGDHDIDQGWVGDVTKGNPT-QMVPRVLFDGWS 151
Cdd:cd02876     1 FQGPVLGYVTPWNSHGYDVAKKFAAKFTHVSPVWLQIKRK-GNKFVIEGTHDIDKGWIEEVRKANKNiKILPRVLFEGWS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383 152 RTDYDKLFSDESAIEDCASVLLKFINKKKFPGIVVEIWSQLGG----QYRKELVHFLQHLGEAFHTEERSLILVIPPPVY 227
Cdd:cd02876    80 YQDLQSLLNDEQEREKLIKLLVTTAKKNHFDGIVLEVWSQLAAygvpDKRKELIQLVIHLGETLHSANLKLILVIPPPRE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383 228 PGNVDGMFGRNEFEQLLPYIDAFSLMTYDFSNPSRPGPNSPLSWMESCVLALAPEDNPEvRQKILLGLNFYGNEYS-AGG 306
Cdd:cd02876   160 KGNQNGLFTRKDFEKLAPHVDGFSLMTYDYSSPQRPGPNAPLSWVRSCLELLLPESGKK-RAKILLGLNFYGNDYTlPGG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383 307 GGPIVGNQYLEILKKNKPKFKWDSNSQEHIAEYKTDWGTGVVYFPTLLSLQRRLELAKQLGTGISIWEIGQGLDYFYDLL 386
Cdd:cd02876   239 GGAITGSEYLKLLKSNKPKLQWDEKSAEHFFEYKNKGGKHAVFYPTLKSIQLRLDLAKELGTGISIWELGQGLDYFYDLL 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 ...
73-386 3.50e-162

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: 457.54  E-value: 3.50e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383  73 FPGITLAYVTPWNNHGYDIAKSFSQKFSYVSPVWLQIKRRkGGTFFIQGDHDIDQGWVGDVTKGNPT-QMVPRVLFDGWS 151
Cdd:cd02876     1 FQGPVLGYVTPWNSHGYDVAKKFAAKFTHVSPVWLQIKRK-GNKFVIEGTHDIDKGWIEEVRKANKNiKILPRVLFEGWS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383 152 RTDYDKLFSDESAIEDCASVLLKFINKKKFPGIVVEIWSQLGG----QYRKELVHFLQHLGEAFHTEERSLILVIPPPVY 227
Cdd:cd02876    80 YQDLQSLLNDEQEREKLIKLLVTTAKKNHFDGIVLEVWSQLAAygvpDKRKELIQLVIHLGETLHSANLKLILVIPPPRE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383 228 PGNVDGMFGRNEFEQLLPYIDAFSLMTYDFSNPSRPGPNSPLSWMESCVLALAPEDNPEvRQKILLGLNFYGNEYS-AGG 306
Cdd:cd02876   160 KGNQNGLFTRKDFEKLAPHVDGFSLMTYDYSSPQRPGPNAPLSWVRSCLELLLPESGKK-RAKILLGLNFYGNDYTlPGG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383 307 GGPIVGNQYLEILKKNKPKFKWDSNSQEHIAEYKTDWGTGVVYFPTLLSLQRRLELAKQLGTGISIWEIGQGLDYFYDLL 386
Cdd:cd02876   239 GGAITGSEYLKLLKSNKPKLQWDEKSAEHFFEYKNKGGKHAVFYPTLKSIQLRLDLAKELGTGISIWELGQGLDYFYDLL 318
Glyco_18 smart00636
Glyco_18 domain;
78-377 3.97e-30

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 118.16  E-value: 3.97e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383   78 LAYVTPWNNHG--YDIAKSFSQKFSYVSPVWLQIKRrkGGTFFIqGDHDIDQGWVGDVT---KGNPTqmvPRVLFD--GW 150
Cdd:smart00636   3 VGYFTNWGVYGrnFPVDDIPASKLTHIIYAFANIDP--DGTVTI-GDEWADIGNFGQLKalkKKNPG---LKVLLSigGW 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383  151 srtDYDKLFS----DESAIEDCASVLLKFINKKKFPGIVVEiWSQLGGQYRKE--LVHFLQHLGEAFHTEERS---LILV 221
Cdd:smart00636  77 ---TESDNFSsmlsDPASRKKFIDSIVSFLKKYGFDGIDID-WEYPGGRGDDRenYTALLKELREALDKEGAEgkgYLLT 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383  222 IPppVYPGNVDGMFGRNEFEQLLPYIDAFSLMTYDFSNPSR--PGPNSPLSWM---------ESCVLALAPEDNPevRQK 290
Cdd:smart00636 153 IA--VPAGPDKIDKGYGDLPAIAKYLDFINLMTYDFHGAWSnpTGHNAPLYAGpgdpekynvDYAVKYYLCKGVP--PSK 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383  291 ILLGLNFYG------NEYSAGGGGPIVGNQ-------------YLEILKKNKPKFKWDSNSQehiAEYKTDWGTGV-VYF 350
Cdd:smart00636 229 LVLGIPFYGrgwtlvDGSNNGPGAPFTGPAtggpgtweggvvdYREICKLLGATVVYDDTAK---APYAYNPGTGQwVSY 305
                          330       340
                   ....*....|....*....|....*...
gi 1242811383  351 PTLLSLQRRLELAKQLGT-GISIWEIGQ 377
Cdd:smart00636 306 DDPRSIKAKADYVKDKGLgGVMIWELDA 333
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
149-377 2.47e-14

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 72.87  E-value: 2.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383 149 GWSRTD-YDKLFSDESAIEDCASVLLKFINKKKFPGIVVEI-WSQLGGQYRKELVHFLQHLGEAFH---TEERSLILVIP 223
Cdd:pfam00704  72 GWTDSTgFSLMASNPASRKKFADSIVSFLRKYGFDGIDIDWeYPGGNPEDKENYDLLLRELRAALDeakGGKKYLLSAAV 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383 224 PPVYPGNVDGMfgrnEFEQLLPYIDAFSLMTYDFSNP--SRPGPNSPLSW-----MESCVLALAPEDNPevRQKILLGLN 296
Cdd:pfam00704 152 PASYPDLDKGY----DLPKIAKYLDFINVMTYDFHGSwdNVTGHHAPLYGggsynVDYAVKYYLKQGVP--ASKLVLGVP 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383 297 FYGNEYSAGGG-------GPIVGNQYLEILKKNKPKFKWDSNSQEHIAEYKTDWGTgvvyFPTLLSLQRRLELAKQ--LG 367
Cdd:pfam00704 226 FYGRSWTLVNGsgntwedGVLAYKEICNLLKDNGATVVWDDVAKAPYVYDGDQFIT----YDDPRSIATKVDYVKAkgLG 301
                         250
                  ....*....|
gi 1242811383 368 tGISIWEIGQ 377
Cdd:pfam00704 302 -GVMIWSLDA 310
ChiA COG3325
Chitinase, GH18 family [Carbohydrate transport and metabolism];
149-377 8.15e-09

Chitinase, GH18 family [Carbohydrate transport and metabolism];


Pssm-ID: 442554 [Multi-domain]  Cd Length: 391  Bit Score: 56.84  E-value: 8.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383 149 GWSRTDYdklFSD----ESAIEDCASVLLKFINKKKFPGIVVEiW------SQLGGQYRKE-------LVHFL-QHLGEA 210
Cdd:COG3325   108 GWTWSKG---FSDaaatPASRAAFVDSCVDLLRKYNFDGIDID-WeypgsgGAPGNVYRPEdkanftaLLKELrAQLDAL 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383 211 FHTEERSLILVIPPPVYPGNVDGMfgrnEFEQLLPYIDAFSLMTYDFSNP--SRPGPNSPLswmescvlaLAPEDNPEV- 287
Cdd:COG3325   184 GAETGKHYLLTAAAPAGPDKLDGI----ELPKVAQYLDYVNVMTYDFHGAwsPTTGHQAPL---------YDSPKDPEAq 250
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383 288 -----------------RQKILLGLNFYG------NEYSAGGGGPIVG----------NQYLEILKK--NKPKFK--WDS 330
Cdd:COG3325   251 gysvdsavqaylaagvpASKLVLGVPFYGrgwtgvTGGNNGLYQPATGpapgtweagvNDYKDLKALylGSNGYTryWDD 330
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1242811383 331 NSQehiAEYKTDWGTGVVY-FPTLLSLQRRLELAKQ--LGtGISIWEIGQ 377
Cdd:COG3325   331 VAK---APYLYNGDTGTFIsYDDPRSIAAKADYVKDkgLG-GVMFWELSG 376
 
Name Accession Description Interval E-value
GH18_SI-CLP cd02876
Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein ...
73-386 3.50e-162

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: 457.54  E-value: 3.50e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383  73 FPGITLAYVTPWNNHGYDIAKSFSQKFSYVSPVWLQIKRRkGGTFFIQGDHDIDQGWVGDVTKGNPT-QMVPRVLFDGWS 151
Cdd:cd02876     1 FQGPVLGYVTPWNSHGYDVAKKFAAKFTHVSPVWLQIKRK-GNKFVIEGTHDIDKGWIEEVRKANKNiKILPRVLFEGWS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383 152 RTDYDKLFSDESAIEDCASVLLKFINKKKFPGIVVEIWSQLGG----QYRKELVHFLQHLGEAFHTEERSLILVIPPPVY 227
Cdd:cd02876    80 YQDLQSLLNDEQEREKLIKLLVTTAKKNHFDGIVLEVWSQLAAygvpDKRKELIQLVIHLGETLHSANLKLILVIPPPRE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383 228 PGNVDGMFGRNEFEQLLPYIDAFSLMTYDFSNPSRPGPNSPLSWMESCVLALAPEDNPEvRQKILLGLNFYGNEYS-AGG 306
Cdd:cd02876   160 KGNQNGLFTRKDFEKLAPHVDGFSLMTYDYSSPQRPGPNAPLSWVRSCLELLLPESGKK-RAKILLGLNFYGNDYTlPGG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383 307 GGPIVGNQYLEILKKNKPKFKWDSNSQEHIAEYKTDWGTGVVYFPTLLSLQRRLELAKQLGTGISIWEIGQGLDYFYDLL 386
Cdd:cd02876   239 GGAITGSEYLKLLKSNKPKLQWDEKSAEHFFEYKNKGGKHAVFYPTLKSIQLRLDLAKELGTGISIWELGQGLDYFYDLL 318
Glyco_18 smart00636
Glyco_18 domain;
78-377 3.97e-30

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 118.16  E-value: 3.97e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383   78 LAYVTPWNNHG--YDIAKSFSQKFSYVSPVWLQIKRrkGGTFFIqGDHDIDQGWVGDVT---KGNPTqmvPRVLFD--GW 150
Cdd:smart00636   3 VGYFTNWGVYGrnFPVDDIPASKLTHIIYAFANIDP--DGTVTI-GDEWADIGNFGQLKalkKKNPG---LKVLLSigGW 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383  151 srtDYDKLFS----DESAIEDCASVLLKFINKKKFPGIVVEiWSQLGGQYRKE--LVHFLQHLGEAFHTEERS---LILV 221
Cdd:smart00636  77 ---TESDNFSsmlsDPASRKKFIDSIVSFLKKYGFDGIDID-WEYPGGRGDDRenYTALLKELREALDKEGAEgkgYLLT 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383  222 IPppVYPGNVDGMFGRNEFEQLLPYIDAFSLMTYDFSNPSR--PGPNSPLSWM---------ESCVLALAPEDNPevRQK 290
Cdd:smart00636 153 IA--VPAGPDKIDKGYGDLPAIAKYLDFINLMTYDFHGAWSnpTGHNAPLYAGpgdpekynvDYAVKYYLCKGVP--PSK 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383  291 ILLGLNFYG------NEYSAGGGGPIVGNQ-------------YLEILKKNKPKFKWDSNSQehiAEYKTDWGTGV-VYF 350
Cdd:smart00636 229 LVLGIPFYGrgwtlvDGSNNGPGAPFTGPAtggpgtweggvvdYREICKLLGATVVYDDTAK---APYAYNPGTGQwVSY 305
                          330       340
                   ....*....|....*....|....*...
gi 1242811383  351 PTLLSLQRRLELAKQLGT-GISIWEIGQ 377
Cdd:smart00636 306 DDPRSIKAKADYVKDKGLgGVMIWELDA 333
GH18_CFLE_spore_hydrolase cd02874
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ...
77-386 8.37e-24

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: 100.42  E-value: 8.37e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383  77 TLAYVTPWNNHGYDIAKSFSQKFSYVSPVWLQIKRRKGGTffiqgdhDIDQGWVGDVTKGNPTQMVPRVLFDGWSRTDYD 156
Cdd:cd02874     4 VLGYYTPRNGSDYESLRANAPYLTYIAPFWYGVDADGTLT-------GLPDERLIEAAKRRGVKPLLVITNLTNGNFDSE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383 157 ---KLFSDESAIEDCASVLLKFINKKKFPGIVVEIwSQLGGQYRKELVHFLQHLGEAFHTEERSLILVIPPPVYPGNVDG 233
Cdd:cd02874    77 lahAVLSNPEARQRLINNILALAKKYGYDGVNIDF-ENVPPEDREAYTQFLRELSDRLHPAGYTLSTAVVPKTSADQFGN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383 234 MFGRNEFEQLLPYIDAFSLMTYDFSNP-SRPGPNSPLSWMEScVLALAPEDNPevRQKILLGLNFYGNEYSAGGGGPIVG 312
Cdd:cd02874   156 WSGAYDYAAIGKIVDFVVLMTYDWHWRgGPPGPVAPIGWVER-VLQYAVTQIP--REKILLGIPLYGYDWTLPYKKGGKA 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383 313 -----NQYLEILKKNKPKFKWDSNSQE-HIAEYKTDWGTGVVYFPTLLSLQRRLELAKQLG-TGISIWEIGQGLDYFYDL 385
Cdd:cd02874   233 stispQQAINLAKRYGAEIQYDEEAQSpFFRYVDEQGRRHEVWFEDARSLQAKFELAKEYGlRGVSYWRLGLEDPQNWLL 312

                  .
gi 1242811383 386 L 386
Cdd:cd02874   313 L 313
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
149-377 2.47e-14

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 72.87  E-value: 2.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383 149 GWSRTD-YDKLFSDESAIEDCASVLLKFINKKKFPGIVVEI-WSQLGGQYRKELVHFLQHLGEAFH---TEERSLILVIP 223
Cdd:pfam00704  72 GWTDSTgFSLMASNPASRKKFADSIVSFLRKYGFDGIDIDWeYPGGNPEDKENYDLLLRELRAALDeakGGKKYLLSAAV 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383 224 PPVYPGNVDGMfgrnEFEQLLPYIDAFSLMTYDFSNP--SRPGPNSPLSW-----MESCVLALAPEDNPevRQKILLGLN 296
Cdd:pfam00704 152 PASYPDLDKGY----DLPKIAKYLDFINVMTYDFHGSwdNVTGHHAPLYGggsynVDYAVKYYLKQGVP--ASKLVLGVP 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383 297 FYGNEYSAGGG-------GPIVGNQYLEILKKNKPKFKWDSNSQEHIAEYKTDWGTgvvyFPTLLSLQRRLELAKQ--LG 367
Cdd:pfam00704 226 FYGRSWTLVNGsgntwedGVLAYKEICNLLKDNGATVVWDDVAKAPYVYDGDQFIT----YDDPRSIATKVDYVKAkgLG 301
                         250
                  ....*....|
gi 1242811383 368 tGISIWEIGQ 377
Cdd:pfam00704 302 -GVMIWSLDA 310
GH18_chitinase-like cd00598
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ...
79-256 1.28e-12

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: 66.25  E-value: 1.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383  79 AYVTPWNNHGYDIA-KSFSQKFSYVSPVWLQIKRRKGGTFFIQGDHDIDQGWVGDVTKGNPTqmvPRVL--FDGWSRTDY 155
Cdd:cd00598     3 CYYDGWSSGRGPDPtDIPLSLCTHIIYAFAEISSDGSLNLFGDKSEEPLKGALEELASKKPG---LKVLisIGGWTDSSP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383 156 DKLFSDESAIEDCASVLLKFINKKKFPGIVVEIW--SQLGGQYRKELVHFLQHLGEAFHTEErsLILVIPPPVYPGNVDG 233
Cdd:cd00598    80 FTLASDPASRAAFANSLVSFLKTYGFDGVDIDWEypGAADNSDRENFITLLRELRSALGAAN--YLLTIAVPASYFDLGY 157
                         170       180
                  ....*....|....*....|...
gi 1242811383 234 mfgRNEFEQLLPYIDAFSLMTYD 256
Cdd:cd00598   158 ---AYDVPAIGDYVDFVNVMTYD 177
GH18_chitolectin_chitotriosidase cd02872
This conserved domain family includes a large number of catalytically inactive chitinase-like ...
173-375 4.77e-09

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: 57.57  E-value: 4.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383 173 LKFINKKKFPGIVVEiW---SQLGG--QYRKELVHFLQHLGEAFHTEERSLILVIPPPVYPGNVDGMFgrnEFEQLLPYI 247
Cdd:cd02872   105 IAFLRKYGFDGLDLD-WeypGQRGGppEDKENFVTLLKELREAFEPEAPRLLLTAAVSAGKETIDAAY---DIPEISKYL 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383 248 DAFSLMTYDFSNPSRP--GPNSPLSWmescvlalAPEDNPEVRQ------------------KILLGLNFYGNEY----- 302
Cdd:cd02872   181 DFINVMTYDFHGSWEGvtGHNSPLYA--------GSADTGDQKYlnvdyaikywlskgappeKLVLGIPTYGRSFtlasp 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383 303 --------SAGGG--GPIVGNQ----YLEI--LKKNKPKFKWDSNSQEHIAEYKTDWgtgvVYFPTLLSLQRRLELAKQL 366
Cdd:cd02872   253 sntgvgapASGPGtaGPYTREAgflaYYEIceFLKSGWTVVWDDEQKVPYAYKGNQW----VGYDDEESIALKVQYLKSK 328
                         250
                  ....*....|
gi 1242811383 367 G-TGISIWEI 375
Cdd:cd02872   329 GlGGAMVWSI 338
ChiA COG3325
Chitinase, GH18 family [Carbohydrate transport and metabolism];
149-377 8.15e-09

Chitinase, GH18 family [Carbohydrate transport and metabolism];


Pssm-ID: 442554 [Multi-domain]  Cd Length: 391  Bit Score: 56.84  E-value: 8.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383 149 GWSRTDYdklFSD----ESAIEDCASVLLKFINKKKFPGIVVEiW------SQLGGQYRKE-------LVHFL-QHLGEA 210
Cdd:COG3325   108 GWTWSKG---FSDaaatPASRAAFVDSCVDLLRKYNFDGIDID-WeypgsgGAPGNVYRPEdkanftaLLKELrAQLDAL 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383 211 FHTEERSLILVIPPPVYPGNVDGMfgrnEFEQLLPYIDAFSLMTYDFSNP--SRPGPNSPLswmescvlaLAPEDNPEV- 287
Cdd:COG3325   184 GAETGKHYLLTAAAPAGPDKLDGI----ELPKVAQYLDYVNVMTYDFHGAwsPTTGHQAPL---------YDSPKDPEAq 250
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383 288 -----------------RQKILLGLNFYG------NEYSAGGGGPIVG----------NQYLEILKK--NKPKFK--WDS 330
Cdd:COG3325   251 gysvdsavqaylaagvpASKLVLGVPFYGrgwtgvTGGNNGLYQPATGpapgtweagvNDYKDLKALylGSNGYTryWDD 330
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1242811383 331 NSQehiAEYKTDWGTGVVY-FPTLLSLQRRLELAKQ--LGtGISIWEIGQ 377
Cdd:COG3325   331 VAK---APYLYNGDTGTFIsYDDPRSIAAKADYVKDkgLG-GVMFWELSG 376
GH18_trifunctional cd06549
GH18 domain of an uncharacterized family of bacterial proteins, which share a common ...
76-309 3.07e-08

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: 54.72  E-value: 3.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383  76 ITLAYVTPWNnhgyDIAK-SFSQKF---SYVSPVWLQIKrrkggtffiQGDHDIDQGwVGDVTKG-------NPT--QMV 142
Cdd:cd06549     1 IALAFYTPWD----DASFaSLKRHAprlDWLVPEWLNLT---------GPEGRIDVF-VDPQGVAiiaaakaHPKvlPLV 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383 143 PRVLFDGWSRTDYDKLFSDESAIEDCASVLLKFINKKKFPGIVVEiWSQLGGQYRKELVHFLQHLGEAFHTEERSLILVI 222
Cdd:cd06549    67 QNISGGAWDGKNIARLLADPSARAKFIANIAAYLERNQADGIVLD-FEELPADDLPKYVAFLSELRRRLPAQGKQLTVTV 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383 223 PppvypgnVDGMFgrNEFEQLLPYIDAFSLMTYD-FSNPSRPGPNSPLSWMESCVLALAPEDNPEvrqKILLGLNFYGNE 301
Cdd:cd06549   146 P-------ADEAD--WNLKALARNADKLILMAYDeHYQGGAPGPIASQDWFESNLAQAVKKLPPE---KLIVALGSYGYD 213

                  ....*...
gi 1242811383 302 YSAGGGGP 309
Cdd:cd06549   214 WTKGGNTK 221
GH18_3CO4_chitinase cd06545
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an ...
244-377 2.63e-04

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: 42.05  E-value: 2.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242811383 244 LPYIDAFSLMTYD---FSNPSRPGPNSPLS--------WMESCVLAlapednpevRQKILLGLNFYGNEYSAGGggpivg 312
Cdd:cd06545   152 LAYFDFINIMSYDatgPWWGDNPGQHSSYDdavndlnyWNERGLAS---------KDKLVLGLPFYGYGFYYNG------ 216
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1242811383 313 nqyleilkknkpkfkwdsnsqehiaeyktdwgtgvvyFPTllsLQRRLELAKQLGTGISIWEIGQ 377
Cdd:cd06545   217 -------------------------------------IPT---IRNKVAFAKQNYGGVMIWELSQ 241
 
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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