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Conserved domains on  [gi|386764131|ref|NP_001245600|]
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chitinase 6, isoform G [Drosophila melanogaster]

Protein Classification

glycoside hydrolase family 18 protein( domain architecture ID 10120821)

glycoside hydrolase family 18 protein such as Mus musculus chitotriosidase-1 (also called chitinase-1) that degrades chitin, chitotriose and chitobiose; also contains C-terminal peritrophin-A or chitin-binding domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GH18_chitolectin_chitotriosidase cd02872
This conserved domain family includes a large number of catalytically inactive chitinase-like ...
 32-404 0e+00

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: 562.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131   32 VVCYYTNWSVYRPGTAKFNPQNINPYLCTHLVYAFGGFTKDNQMKPFDKYQDIEQGGYAKFTGLKTYNKQLKTMIAIGGW 111
Cdd:cd02872     1 VVCYFTNWAQYRPGNGKFVPENIDPFLCTHIIYAFAGLNPDGNIIILDEWNDIDLGLYERFNALKEKNPNLKTLLAIGGW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  112 NEASSRFSPLVASNERRQQFIKNILKFLRQNHFDGIDLDWEYPAHReGGKSRDRDNYAQFVQELRAEFEREAEktgrtRL 191
Cdd:cd02872    81 NFGSAKFSAMAASPENRKTFIKSAIAFLRKYGFDGLDLDWEYPGQR-GGPPEDKENFVTLLKELREAFEPEAP-----RL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  192 LLTMAVPAGIEYIDKGYDVPKLNKYLDWFNVLTYDFHSSHEPSVNHHAPLYSLEEDSEYNydAELNIDYSIKYYLKAGAD 271
Cdd:cd02872   155 LLTAAVSAGKETIDAAYDIPEISKYLDFINVMTYDFHGSWEGVTGHNSPLYAGSADTGDQ--KYLNVDYAIKYWLSKGAP 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  272 RDKLVLGIPTYGRSYTLINEESTELGAPAEGPGEQGDATREKGYLAYYEICQTLKDDpeWTVVQpNANVMGPYAYRRNQW 351
Cdd:cd02872   233 PEKLVLGIPTYGRSFTLASPSNTGVGAPASGPGTAGPYTREAGFLAYYEICEFLKSG--WTVVW-DDEQKVPYAYKGNQW 309

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386764131  352 VGYDDEAIVRKKAEYVVAQGLGGIMFWAIDNDDFRGTCNGKPYPLIEAAKEAM 404
Cdd:cd02872   310 VGYDDEESIALKVQYLKSKGLGGAMVWSIDLDDFRGTCGQGKYPLLNAINRAL 362
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 506-562 1.02e-13

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


:

Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 67.05  E-value: 1.02e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131   506 CE--EEGFFQHPRDCKKYYWCLDSGPsglgivaHMFTCPSGLYFNPAADSCDFARNVP-C 562
Cdd:pfam01607    1 CAgkEDGYYADPGDCSKYYVCSNGEA-------VEFTCPNGLVFDPTLGICDYPDNVVdC 53
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 1523-1578 1.39e-08

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


:

Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 52.42  E-value: 1.39e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 386764131  1523 RAQGNFPHPLNCRKFISCARFEETggivgwEYTCPKGLTYDGVGGMCTWSPSDQPC 1578
Cdd:pfam01607    4 KEDGYYADPGDCSKYYVCSNGEAV------EFTCPNGLVFDPTLGICDYPDNVVDC 53
 
Name Accession Description Interval E-value
GH18_chitolectin_chitotriosidase cd02872
This conserved domain family includes a large number of catalytically inactive chitinase-like ...
 32-404 0e+00

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: 562.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131   32 VVCYYTNWSVYRPGTAKFNPQNINPYLCTHLVYAFGGFTKDNQMKPFDKYQDIEQGGYAKFTGLKTYNKQLKTMIAIGGW 111
Cdd:cd02872     1 VVCYFTNWAQYRPGNGKFVPENIDPFLCTHIIYAFAGLNPDGNIIILDEWNDIDLGLYERFNALKEKNPNLKTLLAIGGW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  112 NEASSRFSPLVASNERRQQFIKNILKFLRQNHFDGIDLDWEYPAHReGGKSRDRDNYAQFVQELRAEFEREAEktgrtRL 191
Cdd:cd02872    81 NFGSAKFSAMAASPENRKTFIKSAIAFLRKYGFDGLDLDWEYPGQR-GGPPEDKENFVTLLKELREAFEPEAP-----RL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  192 LLTMAVPAGIEYIDKGYDVPKLNKYLDWFNVLTYDFHSSHEPSVNHHAPLYSLEEDSEYNydAELNIDYSIKYYLKAGAD 271
Cdd:cd02872   155 LLTAAVSAGKETIDAAYDIPEISKYLDFINVMTYDFHGSWEGVTGHNSPLYAGSADTGDQ--KYLNVDYAIKYWLSKGAP 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  272 RDKLVLGIPTYGRSYTLINEESTELGAPAEGPGEQGDATREKGYLAYYEICQTLKDDpeWTVVQpNANVMGPYAYRRNQW 351
Cdd:cd02872   233 PEKLVLGIPTYGRSFTLASPSNTGVGAPASGPGTAGPYTREAGFLAYYEICEFLKSG--WTVVW-DDEQKVPYAYKGNQW 309

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386764131  352 VGYDDEAIVRKKAEYVVAQGLGGIMFWAIDNDDFRGTCNGKPYPLIEAAKEAM 404
Cdd:cd02872   310 VGYDDEESIALKVQYLKSKGLGGAMVWSIDLDDFRGTCGQGKYPLLNAINRAL 362
Glyco_18 smart00636
Glyco_18 domain;
31-383 8.39e-135

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 420.16  E-value: 8.39e-135
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131     31 RVVCYYTNWSVYRPgtaKFNPQNINPYLCTHLVYAFGGFTKDNQMKPFDKYQDIEQGGYakFTGLKTYNKQLKTMIAIGG 110
Cdd:smart00636    1 RVVGYFTNWGVYGR---NFPVDDIPASKLTHIIYAFANIDPDGTVTIGDEWADIGNFGQ--LKALKKKNPGLKVLLSIGG 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131    111 WNEaSSRFSPLVASNERRQQFIKNILKFLRQNHFDGIDLDWEYPahreGGKSRDRDNYAQFVQELRAEFEREAEktGRTR 190
Cdd:smart00636   76 WTE-SDNFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWEYP----GGRGDDRENYTALLKELREALDKEGA--EGKG 148

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131    191 LLLTMAVPAGIEYIDKGYD-VPKLNKYLDWFNVLTYDFHSSHEPSVNHHAPLYSLEEDSEYnydaeLNIDYSIKYYLKAG 269
Cdd:smart00636  149 YLLTIAVPAGPDKIDKGYGdLPAIAKYLDFINLMTYDFHGAWSNPTGHNAPLYAGPGDPEK-----YNVDYAVKYYLCKG 223

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131    270 ADRDKLVLGIPTYGRSYTLINEESTELGAPAEGPGEQGDATREKGYLAYYEICQTLKddpeWTVVQpNANVMGPYAYRRN 349
Cdd:smart00636  224 VPPSKLVLGIPFYGRGWTLVDGSNNGPGAPFTGPATGGPGTWEGGVVDYREICKLLG----ATVVY-DDTAKAPYAYNPG 298

                           330       340       350
                    ....*....|....*....|....*....|....*.
gi 386764131    350 --QWVGYDDEAIVRKKAEYVVAQGLGGIMFWAIDND 383
Cdd:smart00636  299 tgQWVSYDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
31-383 2.61e-115

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 366.01  E-value: 2.61e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131    31 RVVCYYTNWSVYRPGTAkfnpqnINPYLCTHLVYAFGG-FTKDNQMKPFDKyqdiEQGGYAKFTGLKT-YNKQLKTMIAI 108
Cdd:pfam00704    1 RIVGYYTSWGVYRNGNF------LPSDKLTHIIYAFANiDGSDGTLFIGDW----DLGNFEQLKKLKKqKNPGVKVLLSI 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131   109 GGWNEaSSRFSPLVASNERRQQFIKNILKFLRQNHFDGIDLDWEYPahreGGKSRDRDNYAQFVQELRAEFEreaEKTGR 188
Cdd:pfam00704   71 GGWTD-STGFSLMASNPASRKKFADSIVSFLRKYGFDGIDIDWEYP----GGNPEDKENYDLLLRELRAALD---EAKGG 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131   189 TRLLLTMAVPAGIEYIDKGYDVPKLNKYLDWFNVLTYDFHSSHEPSVNHHAPLYsleedseynYDAELNIDYSIKYYLKA 268
Cdd:pfam00704  143 KKYLLSAAVPASYPDLDKGYDLPKIAKYLDFINVMTYDFHGSWDNVTGHHAPLY---------GGGSYNVDYAVKYYLKQ 213

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131   269 GADRDKLVLGIPTYGRSYTLINEestelgapaegpgeqGDATREKGYLAYYEICQTLKDDPewTVVQPNANVMGPYAYRR 348
Cdd:pfam00704  214 GVPASKLVLGVPFYGRSWTLVNG---------------SGNTWEDGVLAYKEICNLLKDNG--ATVVWDDVAKAPYVYDG 276

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 386764131   349 NQWVGYDDEAIVRKKAEYVVAQGLGGIMFWAIDND 383
Cdd:pfam00704  277 DQFITYDDPRSIATKVDYVKAKGLGGVMIWSLDAD 311
ChiA COG3325
Chitinase, GH18 family [Carbohydrate transport and metabolism];
26-388 2.08e-104

Chitinase, GH18 family [Carbohydrate transport and metabolism];


Pssm-ID: 442554 [Multi-domain]  Cd Length: 391  Bit Score: 339.19  E-value: 2.08e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131   26 ASSEGRVVCYYTNWSVYRPGtakFNPQNINPYLCTHLVYAFGGFTKDNQMKPFDKYQDIEQGGYA------------KFT 93
Cdd:COG3325    15 ATSGKRVVGYFTQWGIYGRN---YLVKDIPASKLTHINYAFANVDPDGKCSVGDAWAKPSVDGAAddwdqplkgnfnQLK 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131   94 GLKTYNKQLKTMIAIGGWNEaSSRFSPLVASNERRQQFIKNILKFLRQNHFDGIDLDWEYPAHR--EGGKSR--DRDNYA 169
Cdd:COG3325    92 KLKAKNPNLKVLISIGGWTW-SKGFSDAAATPASRAAFVDSCVDLLRKYNFDGIDIDWEYPGSGgaPGNVYRpeDKANFT 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  170 QFVQELRAEFEREAEKTGRtRLLLTMAVPAGIEYIDkGYDVPKLNKYLDWFNVLTYDFHSSHEPSVNHHAPLYSleeDSE 249
Cdd:COG3325   171 ALLKELRAQLDALGAETGK-HYLLTAAAPAGPDKLD-GIELPKVAQYLDYVNVMTYDFHGAWSPTTGHQAPLYD---SPK 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  250 YNYDAELNIDYSIKYYLKAGADRDKLVLGIPTYGRSYTLINEESTELGAPAEGPGeqgDATREKGYLAYYEICQTLKDDP 329
Cdd:COG3325   246 DPEAQGYSVDSAVQAYLAAGVPASKLVLGVPFYGRGWTGVTGGNNGLYQPATGPA---PGTWEAGVNDYKDLKALYLGSN 322

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386764131  330 EWTVV-QPNANVmgPYAYR--RNQWVGYDDEAIVRKKAEYVVAQGLGGIMFWAIDNDDFRGT 388
Cdd:COG3325   323 GYTRYwDDVAKA--PYLYNgdTGTFISYDDPRSIAAKADYVKDKGLGGVMFWELSGDTADGT 382
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 506-562 1.02e-13

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 67.05  E-value: 1.02e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131   506 CE--EEGFFQHPRDCKKYYWCLDSGPsglgivaHMFTCPSGLYFNPAADSCDFARNVP-C 562
Cdd:pfam01607    1 CAgkEDGYYADPGDCSKYYVCSNGEA-------VEFTCPNGLVFDPTLGICDYPDNVVdC 53
ChtBD2 smart00494
Chitin-binding domain type 2;
504-557 3.05e-10

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 57.07  E-value: 3.05e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 386764131    504 FKCEEE--GFFQHPRDCKKYYWCLDsgpsglGIvAHMFTCPSGLYFNPAADSCDFA 557
Cdd:smart00494    1 NECPGRgdGLYPHPTDCSKYYQCSN------GR-PIVGSCPAGLVFNPATQTCDWP 49
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 1523-1578 1.39e-08

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 52.42  E-value: 1.39e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 386764131  1523 RAQGNFPHPLNCRKFISCARFEETggivgwEYTCPKGLTYDGVGGMCTWSPSDQPC 1578
Cdd:pfam01607    4 KEDGYYADPGDCSKYYVCSNGEAV------EFTCPNGLVFDPTLGICDYPDNVVDC 53
ChtBD2 smart00494
Chitin-binding domain type 2;
1526-1572 9.01e-07

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 47.05  E-value: 9.01e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 386764131   1526 GNFPHPLNCRKFISCarfeeTGGIVgWEYTCPKGLTYDGVGGMCTWS 1572
Cdd:smart00494    9 GLYPHPTDCSKYYQC-----SNGRP-IVGSCPAGLVFNPATQTCDWP 49
 
Name Accession Description Interval E-value
GH18_chitolectin_chitotriosidase cd02872
This conserved domain family includes a large number of catalytically inactive chitinase-like ...
 32-404 0e+00

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: 562.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131   32 VVCYYTNWSVYRPGTAKFNPQNINPYLCTHLVYAFGGFTKDNQMKPFDKYQDIEQGGYAKFTGLKTYNKQLKTMIAIGGW 111
Cdd:cd02872     1 VVCYFTNWAQYRPGNGKFVPENIDPFLCTHIIYAFAGLNPDGNIIILDEWNDIDLGLYERFNALKEKNPNLKTLLAIGGW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  112 NEASSRFSPLVASNERRQQFIKNILKFLRQNHFDGIDLDWEYPAHReGGKSRDRDNYAQFVQELRAEFEREAEktgrtRL 191
Cdd:cd02872    81 NFGSAKFSAMAASPENRKTFIKSAIAFLRKYGFDGLDLDWEYPGQR-GGPPEDKENFVTLLKELREAFEPEAP-----RL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  192 LLTMAVPAGIEYIDKGYDVPKLNKYLDWFNVLTYDFHSSHEPSVNHHAPLYSLEEDSEYNydAELNIDYSIKYYLKAGAD 271
Cdd:cd02872   155 LLTAAVSAGKETIDAAYDIPEISKYLDFINVMTYDFHGSWEGVTGHNSPLYAGSADTGDQ--KYLNVDYAIKYWLSKGAP 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  272 RDKLVLGIPTYGRSYTLINEESTELGAPAEGPGEQGDATREKGYLAYYEICQTLKDDpeWTVVQpNANVMGPYAYRRNQW 351
Cdd:cd02872   233 PEKLVLGIPTYGRSFTLASPSNTGVGAPASGPGTAGPYTREAGFLAYYEICEFLKSG--WTVVW-DDEQKVPYAYKGNQW 309

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386764131  352 VGYDDEAIVRKKAEYVVAQGLGGIMFWAIDNDDFRGTCNGKPYPLIEAAKEAM 404
Cdd:cd02872   310 VGYDDEESIALKVQYLKSKGLGGAMVWSIDLDDFRGTCGQGKYPLLNAINRAL 362
Glyco_18 smart00636
Glyco_18 domain;
31-383 8.39e-135

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 420.16  E-value: 8.39e-135
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131     31 RVVCYYTNWSVYRPgtaKFNPQNINPYLCTHLVYAFGGFTKDNQMKPFDKYQDIEQGGYakFTGLKTYNKQLKTMIAIGG 110
Cdd:smart00636    1 RVVGYFTNWGVYGR---NFPVDDIPASKLTHIIYAFANIDPDGTVTIGDEWADIGNFGQ--LKALKKKNPGLKVLLSIGG 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131    111 WNEaSSRFSPLVASNERRQQFIKNILKFLRQNHFDGIDLDWEYPahreGGKSRDRDNYAQFVQELRAEFEREAEktGRTR 190
Cdd:smart00636   76 WTE-SDNFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWEYP----GGRGDDRENYTALLKELREALDKEGA--EGKG 148

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131    191 LLLTMAVPAGIEYIDKGYD-VPKLNKYLDWFNVLTYDFHSSHEPSVNHHAPLYSLEEDSEYnydaeLNIDYSIKYYLKAG 269
Cdd:smart00636  149 YLLTIAVPAGPDKIDKGYGdLPAIAKYLDFINLMTYDFHGAWSNPTGHNAPLYAGPGDPEK-----YNVDYAVKYYLCKG 223

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131    270 ADRDKLVLGIPTYGRSYTLINEESTELGAPAEGPGEQGDATREKGYLAYYEICQTLKddpeWTVVQpNANVMGPYAYRRN 349
Cdd:smart00636  224 VPPSKLVLGIPFYGRGWTLVDGSNNGPGAPFTGPATGGPGTWEGGVVDYREICKLLG----ATVVY-DDTAKAPYAYNPG 298

                           330       340       350
                    ....*....|....*....|....*....|....*.
gi 386764131    350 --QWVGYDDEAIVRKKAEYVVAQGLGGIMFWAIDND 383
Cdd:smart00636  299 tgQWVSYDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
31-383 2.61e-115

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 366.01  E-value: 2.61e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131    31 RVVCYYTNWSVYRPGTAkfnpqnINPYLCTHLVYAFGG-FTKDNQMKPFDKyqdiEQGGYAKFTGLKT-YNKQLKTMIAI 108
Cdd:pfam00704    1 RIVGYYTSWGVYRNGNF------LPSDKLTHIIYAFANiDGSDGTLFIGDW----DLGNFEQLKKLKKqKNPGVKVLLSI 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131   109 GGWNEaSSRFSPLVASNERRQQFIKNILKFLRQNHFDGIDLDWEYPahreGGKSRDRDNYAQFVQELRAEFEreaEKTGR 188
Cdd:pfam00704   71 GGWTD-STGFSLMASNPASRKKFADSIVSFLRKYGFDGIDIDWEYP----GGNPEDKENYDLLLRELRAALD---EAKGG 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131   189 TRLLLTMAVPAGIEYIDKGYDVPKLNKYLDWFNVLTYDFHSSHEPSVNHHAPLYsleedseynYDAELNIDYSIKYYLKA 268
Cdd:pfam00704  143 KKYLLSAAVPASYPDLDKGYDLPKIAKYLDFINVMTYDFHGSWDNVTGHHAPLY---------GGGSYNVDYAVKYYLKQ 213

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131   269 GADRDKLVLGIPTYGRSYTLINEestelgapaegpgeqGDATREKGYLAYYEICQTLKDDPewTVVQPNANVMGPYAYRR 348
Cdd:pfam00704  214 GVPASKLVLGVPFYGRSWTLVNG---------------SGNTWEDGVLAYKEICNLLKDNG--ATVVWDDVAKAPYVYDG 276

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 386764131   349 NQWVGYDDEAIVRKKAEYVVAQGLGGIMFWAIDND 383
Cdd:pfam00704  277 DQFITYDDPRSIATKVDYVKAKGLGGVMIWSLDAD 311
ChiA COG3325
Chitinase, GH18 family [Carbohydrate transport and metabolism];
26-388 2.08e-104

Chitinase, GH18 family [Carbohydrate transport and metabolism];


Pssm-ID: 442554 [Multi-domain]  Cd Length: 391  Bit Score: 339.19  E-value: 2.08e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131   26 ASSEGRVVCYYTNWSVYRPGtakFNPQNINPYLCTHLVYAFGGFTKDNQMKPFDKYQDIEQGGYA------------KFT 93
Cdd:COG3325    15 ATSGKRVVGYFTQWGIYGRN---YLVKDIPASKLTHINYAFANVDPDGKCSVGDAWAKPSVDGAAddwdqplkgnfnQLK 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131   94 GLKTYNKQLKTMIAIGGWNEaSSRFSPLVASNERRQQFIKNILKFLRQNHFDGIDLDWEYPAHR--EGGKSR--DRDNYA 169
Cdd:COG3325    92 KLKAKNPNLKVLISIGGWTW-SKGFSDAAATPASRAAFVDSCVDLLRKYNFDGIDIDWEYPGSGgaPGNVYRpeDKANFT 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  170 QFVQELRAEFEREAEKTGRtRLLLTMAVPAGIEYIDkGYDVPKLNKYLDWFNVLTYDFHSSHEPSVNHHAPLYSleeDSE 249
Cdd:COG3325   171 ALLKELRAQLDALGAETGK-HYLLTAAAPAGPDKLD-GIELPKVAQYLDYVNVMTYDFHGAWSPTTGHQAPLYD---SPK 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  250 YNYDAELNIDYSIKYYLKAGADRDKLVLGIPTYGRSYTLINEESTELGAPAEGPGeqgDATREKGYLAYYEICQTLKDDP 329
Cdd:COG3325   246 DPEAQGYSVDSAVQAYLAAGVPASKLVLGVPFYGRGWTGVTGGNNGLYQPATGPA---PGTWEAGVNDYKDLKALYLGSN 322

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386764131  330 EWTVV-QPNANVmgPYAYR--RNQWVGYDDEAIVRKKAEYVVAQGLGGIMFWAIDNDDFRGT 388
Cdd:COG3325   323 GYTRYwDDVAKA--PYLYNgdTGTFISYDDPRSIAAKADYVKDKGLGGVMFWELSGDTADGT 382
GH18_chitinase cd06548
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ...
 32-383 1.36e-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: 280.29  E-value: 1.36e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131   32 VVCYYTNWSVYRPGTakFNPQNINPYLCTHLVYAFGGFTKDNQMKPFDKYQDIEQGGYAKFTG----------------L 95
Cdd:cd06548     1 VVGYFTNWGIYGRNY--FVTDDIPADKLTHINYAFADIDGDGGVVTSDDEAADEAAQSVDGGAdtddqplkgnfgqlrkL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131   96 KTYNKQLKTMIAIGGWNeASSRFSPLVASNERRQQFIKNILKFLRQNHFDGIDLDWEYP-AHREGGKSR---DRDNYAQF 171
Cdd:cd06548    79 KQKNPHLKILLSIGGWT-WSGGFSDAAATEASRAKFADSAVDFIRKYGFDGIDIDWEYPgSGGAPGNVArpeDKENFTLL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  172 VQELRAEFEREAEKTGRTrLLLTMAVPAGIEYIDKGyDVPKLNKYLDWFNVLTYDFHSSHEPSVNHHAPLYsleeDSEYN 251
Cdd:cd06548   158 LKELREALDALGAETGRK-YLLTIAAPAGPDKLDKL-EVAEIAKYLDFINLMTYDFHGAWSNTTGHHSNLY----ASPAD 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  252 YDAELNIDYSIKYYLKAGADRDKLVLGIPTYGRSYTlineestelgapaegpgeqgdatrekGYLAYYeicqtlkdDPEW 331
Cdd:cd06548   232 PPGGYSVDAAVNYYLSAGVPPEKLVLGVPFYGRGWT--------------------------GYTRYW--------DEVA 277

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 386764131  332 tvvqpnanvMGPYAY--RRNQWVGYDDEAIVRKKAEYVVAQGLGGIMFWAIDND 383
Cdd:cd06548   278 ---------KAPYLYnpSTKTFISYDDPRSIKAKADYVKDKGLGGVMFWELSGD 322
GH18_IDGF cd02873
The IDGF's (imaginal disc growth factors) are a family of growth factors identified in insects ...
 31-401 1.07e-73

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: 252.23  E-value: 1.07e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131   31 RVVCYYTNWSVYRPGTAKFNPQNINPYL--CTHLVYAFGGFTKDN-QMKPFDKYQDIEQGGYAKFTGLKTYNKQLKTMIA 107
Cdd:cd02873     1 KLVCYYDSKSYLREGLAKMSLEDLEPALqfCTHLVYGYAGIDADTyKIKSLNEDLDLDKSHYRAITSLKRKYPHLKVLLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  108 IGGWNE-----ASSRFSPLVASNERRQQFIKNILKFLRQNHFDGIDLDWEYPAHRE-------------------GGKSR 163
Cdd:cd02873    81 VGGDRDtdeegENEKYLLLLESSESRNAFINSAHSLLKTYGFDGLDLAWQFPKNKPkkvrgtfgsawhsfkklftGDSVV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  164 D------RDNYAQFVQELRAEFEREAektgrtrLLLTMAVPAGIE---YidkgYDVPKLNKYLDWFNVLTYDFHS-SHEP 233
Cdd:cd02873   161 DekaaehKEQFTALVRELKNALRPDG-------LLLTLTVLPHVNstwY----FDVPAIANNVDFVNLATFDFLTpERNP 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  234 SVNHH-APLYSLeedseYNYDAELNIDYSIKYYLKAGADRDKLVLGIPTYGRSYTLiNEESTELGAP----AEGPGEQGD 308
Cdd:cd02873   230 EEADYtAPIYEL-----YERNPHHNVDYQVKYWLNQGTPASKLNLGIATYGRAWKL-TKDSGITGVPpvleTDGPGPAGP 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  309 ATREKGYLAYYEICQTLKDDPEWTvvQPNANV---------MGPYAYRRNQ-------WVGYDDEAIVRKKAEYVVAQGL 372
Cdd:cd02873   304 QTKTPGLLSWPEICSKLPNPANLK--GADAPLrkvgdptkrFGSYAYRPADengehgiWVSYEDPDTAANKAGYAKAKGL 381

                         410       420
                  ....*....|....*....|....*....
gi 386764131  373 GGIMFWAIDNDDFRGTCNGKPYPLIEAAK 401
Cdd:cd02873   382 GGVALFDLSLDDFRGQCTGDKFPILRSAK 410
GH18_plant_chitinase_class_V cd02879
The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the ...
 44-384 1.83e-62

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: 215.69  E-value: 1.83e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131   44 PGTAKFNPQNINPYLCTHLVYAFGgftkdnQMKPFDKYQDIEQGG---YAKFTG-LKTYNKQLKTMIAIGGWNEASSRFS 119
Cdd:cd02879    11 AWSEEFPPSNIDSSLFTHLFYAFA------DLDPSTYEVVISPSDeseFSTFTEtVKRKNPSVKTLLSIGGGGSDSSAFA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  120 PLVASNERRQQFIKNILKFLRQNHFDGIDLDWEYPAHREggksrDRDNYAQFVQELRAEFEREAEKTGRTRLLLTMAVPA 199
Cdd:cd02879    85 AMASDPTARKAFINSSIKVARKYGFDGLDLDWEFPSSQV-----EMENFGKLLEEWRAAVKDEARSSGRPPLLLTAAVYF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  200 GIEYIDKG----YDVPKLNKYLDWFNVLTYDFHSSHEPSVN-HHAPLYsleeDSEYNYDAelniDYSIKYYLKAGADRDK 274
Cdd:cd02879   160 SPILFLSDdsvsYPIEAINKNLDWVNVMAYDYYGSWESNTTgPAAALY----DPNSNVST----DYGIKSWIKAGVPAKK 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  275 LVLGIPTYGRSYTLineestelgapaegpgeqgdatrekgylayyeicqtlkDDPEwtvvqpnanVMGPYAYRRNQWVGY 354
Cdd:cd02879   232 LVLGLPLYGRAWTL--------------------------------------YDTT---------TVSSYVYAGTTWIGY 264

                         330       340       350
                  ....*....|....*....|....*....|
gi 386764131  355 DDEAIVRKKAEYVVAQGLGGIMFWAIDNDD 384
Cdd:cd02879   265 DDVQSIAVKVKYAKQKGLLGYFAWAVGYDD 294
GH18_chitinase-like cd00598
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ...
 32-226 1.05e-49

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: 175.64  E-value: 1.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131   32 VVCYYTNWSVYRPgtakFNPQNINPYLCTHLVYAFGGFTKDN-QMKPFDKYQDIEQGGYAKFTGLKtynKQLKTMIAIGG 110
Cdd:cd00598     1 VICYYDGWSSGRG----PDPTDIPLSLCTHIIYAFAEISSDGsLNLFGDKSEEPLKGALEELASKK---PGLKVLISIGG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  111 WNEASSRFspLVASNERRQQFIKNILKFLRQNHFDGIDLDWEYPahrEGGKSRDRDNYAQFVQELRAEFereaektGRTR 190
Cdd:cd00598    74 WTDSSPFT--LASDPASRAAFANSLVSFLKTYGFDGVDIDWEYP---GAADNSDRENFITLLRELRSAL-------GAAN 141

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 386764131  191 LLLTMAVPAGIEYIDKGYDVPKLNKYLDWFNVLTYD 226
Cdd:cd00598   142 YLLTIAVPASYFDLGYAYDVPAIGDYVDFVNVMTYD 177
GH18_zymocin_alpha cd02878
Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle ...
 33-381 1.12e-35

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: 139.75  E-value: 1.12e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131   33 VCYYTNWSVYRPGTAKfNPQNI--NPYlcTHLVYAFGGFTKDnqmkpFDKYQDIEQGGYAKFTGLKTYNKqlktMIAIGG 110
Cdd:cd02878     3 IAYFEAYNLDRPCLNM-DVTQIdtSKY--THIHFAFANITSD-----FSVDVSSVQEQFSDFKKLKGVKK----ILSFGG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  111 WNEASS-----RFSPLVASnERRQQFIKNILKFLRQNHFDGIDLDWEYPAHRE-----GGKSRDRDNYAQFVQELRAEFe 180
Cdd:cd02878    71 WDFSTSpstyqIFRDAVKP-ANRDTFANNVVNFVNKYNLDGVDFDWEYPGAPDipgipAGDPDDGKNYLEFLKLLKSKL- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  181 rEAEKTgrtrllLTMAVPAGIEYIdKGYDVPKLNKYLDWFNVLTYDFH----------SSHEPSVN---HHAPLysleed 247
Cdd:cd02878   149 -PSGKS------LSIAAPASYWYL-KGFPIKDMAKYVDYIVYMTYDLHgqwdygnkwaSPGCPAGNclrSHVNK------ 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  248 seynydaeLNIDYSIKYYLKAGADRDKLVLGIPTYGRSYTLINEESTELGAPAEGPGEQGDATREK---GYLAYYEICQT 324
Cdd:cd02878   215 --------TETLDALSMITKAGVPSNKVVVGVASYGRSFKMADPGCTGPGCTFTGPGSGAEAGRCTctaGYGAISEIEII 286

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  325 LKDD---PEWTVVQPNANVMgpyAYRRNQWVGYDDEAIVRKKAEYVVAQGLGGIMFWAID 381
Cdd:cd02878   287 DISKsknKRWYDTDSDSDIL---VYDDDQWVAYMSPATKAARIEWYKGLNFGGTSDWAVD 343
GH18_CFLE_spore_hydrolase cd02874
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ...
 108-384 2.05e-22

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: 100.03  E-value: 2.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  108 IGGWNEASSRFSPLVASNERRQQFIKNILKFLRQNHFDGIDLDWE--YPAhreggksrDRDNYAQFVQELRAEFEREaek 185
Cdd:cd02874    68 LTNGNFDSELAHAVLSNPEARQRLINNILALAKKYGYDGVNIDFEnvPPE--------DREAYTQFLRELSDRLHPA--- 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  186 tgrtRLLLTMAVPAGIEYIDKG-----YDVPKLNKYLDWFNVLTYDFH---SSHEPSvnhhAPLYSLEEdseynydaelN 257
Cdd:cd02874   137 ----GYTLSTAVVPKTSADQFGnwsgaYDYAAIGKIVDFVVLMTYDWHwrgGPPGPV----APIGWVER----------V 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  258 IDYSIkyylkAGADRDKLVLGIPTYGRSYTLINeestELGAPAEGPGEQGDATREKGYLAyyeicqTLKDDPEWTVVqpn 337
Cdd:cd02874   199 LQYAV-----TQIPREKILLGIPLYGYDWTLPY----KKGGKASTISPQQAINLAKRYGA------EIQYDEEAQSP--- 260

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 386764131  338 anvmgPYAYR----RNQWVGYDDEAIVRKKAEYVVAQGLGGIMFWAIDNDD 384
Cdd:cd02874   261 -----FFRYVdeqgRRHEVWFEDARSLQAKFELAKEYGLRGVSYWRLGLED 306
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 506-562 1.02e-13

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 67.05  E-value: 1.02e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131   506 CE--EEGFFQHPRDCKKYYWCLDSGPsglgivaHMFTCPSGLYFNPAADSCDFARNVP-C 562
Cdd:pfam01607    1 CAgkEDGYYADPGDCSKYYVCSNGEA-------VEFTCPNGLVFDPTLGICDYPDNVVdC 53
GH18_3CO4_chitinase cd06545
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an ...
 100-287 8.53e-13

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: 70.17  E-value: 8.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  100 KQLKTMIAIGGwnEASSRFSPLVASNERRQQFIKNILKFLRQNHFDGIDLDWEYPaHREGGksrdrdNYAQFVQELRAEF 179
Cdd:cd06545    58 HNVKILISLAG--GSPPEFTAALNDPAKRKALVDKIINYVVSYNLDGIDVDLEGP-DVTFG------DYLVFIRALYAAL 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  180 EREAektgrtrLLLTMAVPAGieyiDKGYDVPKLNKYLDWFNVLTYD---FHSSHEPsvNHHAPlYSleedseynyDAEL 256
Cdd:cd06545   129 KKEG-------KLLTAAVSSW----NGGAVSDSTLAYFDFINIMSYDatgPWWGDNP--GQHSS-YD---------DAVN 185

                         170       180       190
                  ....*....|....*....|....*....|.
gi 386764131  257 NIDYsikYYLKAGADRDKLVLGIPTYGRSYT 287
Cdd:cd06545   186 DLNY---WNERGLASKDKLVLGLPFYGYGFY 213
GH18_SI-CLP cd02876
Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein ...
 82-288 2.84e-11

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: 66.56  E-value: 2.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131   82 QDIEQGGYAKftgLKTYNKQLKTM--IAIGGWNeaSSRFSPLVASNERRQQFIKNILKFLRQNHFDGIDLD-WEYPAHRe 158
Cdd:cd02876    50 HDIDKGWIEE---VRKANKNIKILprVLFEGWS--YQDLQSLLNDEQEREKLIKLLVTTAKKNHFDGIVLEvWSQLAAY- 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  159 gGKSRDRDNYAQFVQELraefereAEKTGRTRLLLTMAVPAGIEYIDKGY-----DVPKLNKYLDWFNVLTYDFHSSHEP 233
Cdd:cd02876   124 -GVPDKRKELIQLVIHL-------GETLHSANLKLILVIPPPREKGNQNGlftrkDFEKLAPHVDGFSLMTYDYSSPQRP 195

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 386764131  234 SVNhhAPLYSleedseynydaelnIDYSIKYYLKAGAD-RDKLVLGIPTYGRSYTL 288
Cdd:cd02876   196 GPN--APLSW--------------VRSCLELLLPESGKkRAKILLGLNFYGNDYTL 235
GH18_chitobiase cd02875
Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes ...
 124-392 6.03e-11

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: 65.92  E-value: 6.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  124 SNER-RQQFIKNILKFLRQNHFDGIDLDWEYPAHREggkSRDRDNYAQFVQELRAEFEREAEKTGrtrllLTMAVPAGIE 202
Cdd:cd02875    92 SNPTyRTQWIQQKVELAKSQFMDGINIDIEQPITKG---SPEYYALTELVKETTKAFKKENPGYQ-----ISFDVAWSPS 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  203 YIDK-GYDVPKLNKYLDWFNVLTYDFHSShepsvnhhapLYSLE----EDSEYNydaelNIDYSIKYYLKAGADRDKLVL 277
Cdd:cd02875   164 CIDKrCYDYTGIADASDFLVVMDYDEQSQ----------IWGKEciagANSPYS-----QTLSGYNNFTKLGIDPKKLVM 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  278 GIPTYGRSYTLIN----------EESTELGAP-AEGPGEQgdatrekgyLAYYEICQTLKDDP---EWTVVQpnanvmGP 343
Cdd:cd02875   229 GLPWYGYDYPCLNgnledvvctiPKVPFRGANcSDAAGRQ---------IPYSEIMKQINSSIggrLWDSEQ------KS 293

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386764131  344 YAYRRNQWVG------YDDEAIVRKKAEYVVAQGLGGIMFWAIDNDDFRGTCNGK 392
Cdd:cd02875   294 PFYNYKDKQGnlhqvwYDNPQSLSIKVAYAKNLGLKGIGMWNGDLLDYSGLPIAE 348
ChtBD2 smart00494
Chitin-binding domain type 2;
504-557 3.05e-10

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 57.07  E-value: 3.05e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 386764131    504 FKCEEE--GFFQHPRDCKKYYWCLDsgpsglGIvAHMFTCPSGLYFNPAADSCDFA 557
Cdd:smart00494    1 NECPGRgdGLYPHPTDCSKYYQCSN------GR-PIVGSCPAGLVFNPATQTCDWP 49
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 1523-1578 1.39e-08

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 52.42  E-value: 1.39e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 386764131  1523 RAQGNFPHPLNCRKFISCARFEETggivgwEYTCPKGLTYDGVGGMCTWSPSDQPC 1578
Cdd:pfam01607    4 KEDGYYADPGDCSKYYVCSNGEAV------EFTCPNGLVFDPTLGICDYPDNVVDC 53
GH18_trifunctional cd06549
GH18 domain of an uncharacterized family of bacterial proteins, which share a common ...
 121-302 6.36e-07

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: 53.18  E-value: 6.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  121 LVASNERRQQFIKNILKFLRQNHFDGIDLDWEypahreGGKSRDRDNYAQFVQELRAEFereaektGRTRLLLTMAVPAG 200
Cdd:cd06549    82 LLADPSARAKFIANIAAYLERNQADGIVLDFE------ELPADDLPKYVAFLSELRRRL-------PAQGKQLTVTVPAD 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  201 ieyiDKGYDVPKLNKYLDWFNVLTYDfhsshEPSVNHHA-PLYSleEDSEYNYDAELNidysikyylkAGADRDKLVLGI 279
Cdd:cd06549   149 ----EADWNLKALARNADKLILMAYD-----EHYQGGAPgPIAS--QDWFESNLAQAV----------KKLPPEKLIVAL 207

                         170       180
                  ....*....|....*....|....*....
gi 386764131  280 PTYGRSYT------LINEESTELGAPAEG 302
Cdd:cd06549   208 GSYGYDWTkggntkAISSEAAWLLAAHAS 236
ChtBD2 smart00494
Chitin-binding domain type 2;
1526-1572 9.01e-07

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 47.05  E-value: 9.01e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 386764131   1526 GNFPHPLNCRKFISCarfeeTGGIVgWEYTCPKGLTYDGVGGMCTWS 1572
Cdd:smart00494    9 GLYPHPTDCSKYYQC-----SNGRP-IVGSCPAGLVFNPATQTCDWP 49
GH18_EndoS-like cd06542
Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of ...
 124-242 2.55e-04

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: 44.68  E-value: 2.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764131  124 SNERRQQFIKNILKFLRQNHFDGIDLDWEY-PAHREGGKSRDRDNYAQFVQELRAEFereaektGRTRLLLTMAVPAGIE 202
Cdd:cd06542    85 SDAAAKAYAKAIVDTVDKYGLDGVDFDDEYsGYGKNGTSQPSNEAFVRLIKELRKYM-------GPTDKLLTIDGYGQAL 157

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 386764131  203 YidkgYDVPKLNKYLDWFNVLTYDFHSSHEPSVNHHAPLY 242
Cdd:cd06542   158 S----NDGEEVSPYVDYVIYQYYGSSSSSTQRNWNTNSPK 193
GH18_CTS3_chitinase cd06546
GH18 domain of CTS3 (chitinase 3), an uncharacterized protein from the human fungal pathogen ...
 102-179 3.15e-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: 44.25  E-value: 3.15e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386764131  102 LKTMIAIGGWNEASsrFSPLVASNERRQQFIKNILKFLRQNHFDGIDLDWEYPAhreggksrDRDNYAQFVQELRAEF 179
Cdd:cd06546    73 VKVMGMLGGAAPGS--FSRLDDDDEDFERYYGQLRDMIRRRGLDGLDLDVEEPM--------SLDGIIRLIDRLRSDF 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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