|
Name |
Accession |
Description |
Interval |
E-value |
| GH18_chitolectin_chitotriosidase |
cd02872 |
This conserved domain family includes a large number of catalytically inactive chitinase-like ... |
24-383 |
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: 593.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 24 LVCYLTNWSQYRTEAVRFFPRDVDPNLCTHVIFAFAGMDN--HQLSTVEHND--ELLYQELNSLKTKNPKLKTLLAVGGW 99
Cdd:cd02872 1 VVCYFTNWAQYRPGNGKFVPENIDPFLCTHIIYAFAGLNPdgNIIILDEWNDidLGLYERFNALKEKNPNLKTLLAIGGW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 100 TFGTQKFTDMVATASNRQTFVKSALSFLRTQGFDGLDLDWEFPGGRGSPTVDKERFTALIQDLAKAFQEEAqssgkERLL 179
Cdd:cd02872 81 NFGSAKFSAMAASPENRKTFIKSAIAFLRKYGFDGLDLDWEYPGQRGGPPEDKENFVTLLKELREAFEPEA-----PRLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 180 LTAAVPSDRGLVDAGYEVDKIAQSLDFINLMAYDFHSSLEKTTGHNSPLYKRQGESGAAAEQNVDAAVTLWLQKGTPASK 259
Cdd:cd02872 156 LTAAVSAGKETIDAAYDIPEISKYLDFINVMTYDFHGSWEGVTGHNSPLYAGSADTGDQKYLNVDYAIKYWLSKGAPPEK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 260 LILGMPTYGRSFTLASSSDNGVGAPATGPGAPGPYTKDKGVLAYYEACSWKE----RHRIEDQKVPYAFQDNQWVSFDDV 335
Cdd:cd02872 236 LVLGIPTYGRSFTLASPSNTGVGAPASGPGTAGPYTREAGFLAYYEICEFLKsgwtVVWDDEQKVPYAYKGNQWVGYDDE 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 568909678 336 ESFKAKAAYLKQKGLGGAMVWVLDLDDFKGsFCNQGPYPLIRTLRQEL 383
Cdd:cd02872 316 ESIALKVQYLKSKGLGGAMVWSIDLDDFRG-TCGQGKYPLLNAINRAL 362
|
|
| Glyco_18 |
smart00636 |
Glyco_18 domain; |
23-361 |
2.37e-146 |
|
Glyco_18 domain;
Pssm-ID: 214753 [Multi-domain] Cd Length: 334 Bit Score: 420.93 E-value: 2.37e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 23 KLVCYLTNWSQYRTeavRFFPRDVDPNLCTHVIFAFAGMDN--HQLSTVEHNDELLYQELNSLKTKNPKLKTLLAVGGWT 100
Cdd:smart00636 1 RVVGYFTNWGVYGR---NFPVDDIPASKLTHIIYAFANIDPdgTVTIGDEWADIGNFGQLKALKKKNPGLKVLLSIGGWT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 101 FGtQKFTDMVATASNRQTFVKSALSFLRTQGFDGLDLDWEFPGGRGSptvDKERFTALIQDLAKAFQEEAQSsgKERLLL 180
Cdd:smart00636 78 ES-DNFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWEYPGGRGD---DRENYTALLKELREALDKEGAE--GKGYLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 181 TAAVPSDRGLVDAGYE-VDKIAQSLDFINLMAYDFHSSLEKTTGHNSPLYKRQGESGAaaeQNVDAAVTLWLQKGTPASK 259
Cdd:smart00636 152 TIAVPAGPDKIDKGYGdLPAIAKYLDFINLMTYDFHGAWSNPTGHNAPLYAGPGDPEK---YNVDYAVKYYLCKGVPPSK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 260 LILGMPTYGRSFTLASSSDNGVGAPATGPGAPGPYTKDKGVLAYYEACSWK--ERHRIEDQKVPYAFQDN--QWVSFDDV 335
Cdd:smart00636 229 LVLGIPFYGRGWTLVDGSNNGPGAPFTGPATGGPGTWEGGVVDYREICKLLgaTVVYDDTAKAPYAYNPGtgQWVSYDDP 308
|
330 340
....*....|....*....|....*.
gi 568909678 336 ESFKAKAAYLKQKGLGGAMVWVLDLD 361
Cdd:smart00636 309 RSIKAKADYVKDKGLGGVMIWELDAD 334
|
|
| Glyco_hydro_18 |
pfam00704 |
Glycosyl hydrolases family 18; |
23-361 |
2.16e-118 |
|
Glycosyl hydrolases family 18;
Pssm-ID: 425828 [Multi-domain] Cd Length: 311 Bit Score: 349.06 E-value: 2.16e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 23 KLVCYLTNWSQYRTEavrffpRDVDPNLCTHVIFAFAGMDNHQLSTVEHN-DELLYQELNSLKT-KNPKLKTLLAVGGWT 100
Cdd:pfam00704 1 RIVGYYTSWGVYRNG------NFLPSDKLTHIIYAFANIDGSDGTLFIGDwDLGNFEQLKKLKKqKNPGVKVLLSIGGWT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 101 FGTqKFTDMVATASNRQTFVKSALSFLRTQGFDGLDLDWEFPGGRgspTVDKERFTALIQDLAKAFQEEaqsSGKERLLL 180
Cdd:pfam00704 75 DST-GFSLMASNPASRKKFADSIVSFLRKYGFDGIDIDWEYPGGN---PEDKENYDLLLRELRAALDEA---KGGKKYLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 181 TAAVPSDRGLVDAGYEVDKIAQSLDFINLMAYDFHSSLEKTTGHNSPLYkrqgesgAAAEQNVDAAVTLWLQKGTPASKL 260
Cdd:pfam00704 148 SAAVPASYPDLDKGYDLPKIAKYLDFINVMTYDFHGSWDNVTGHHAPLY-------GGGSYNVDYAVKYYLKQGVPASKL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 261 ILGMPTYGRSFTLASSSDNgvgapatgpgapgpyTKDKGVLAYYEACS-----WKERHRIEDQKVPYAFQDNQWVSFDDV 335
Cdd:pfam00704 221 VLGVPFYGRSWTLVNGSGN---------------TWEDGVLAYKEICNllkdnGATVVWDDVAKAPYVYDGDQFITYDDP 285
|
330 340
....*....|....*....|....*.
gi 568909678 336 ESFKAKAAYLKQKGLGGAMVWVLDLD 361
Cdd:pfam00704 286 RSIATKVDYVKAKGLGGVMIWSLDAD 311
|
|
| ChiA |
COG3325 |
Chitinase, GH18 family [Carbohydrate transport and metabolism]; |
23-383 |
5.17e-107 |
|
Chitinase, GH18 family [Carbohydrate transport and metabolism];
Pssm-ID: 442554 [Multi-domain] Cd Length: 391 Bit Score: 322.63 E-value: 5.17e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 23 KLVCYLTNWSQYRTEavrFFPRDVDPNLCTHVIFAFAGMDN------------HQLSTVEHNDELLY----QELNSLKTK 86
Cdd:COG3325 20 RVVGYFTQWGIYGRN---YLVKDIPASKLTHINYAFANVDPdgkcsvgdawakPSVDGAADDWDQPLkgnfNQLKKLKAK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 87 NPKLKTLLAVGGWTfGTQKFTDMVATASNRQTFVKSALSFLRTQGFDGLDLDWEFPGGRGSPTV-----DKERFTALIQD 161
Cdd:COG3325 97 NPNLKVLISIGGWT-WSKGFSDAAATPASRAAFVDSCVDLLRKYNFDGIDIDWEYPGSGGAPGNvyrpeDKANFTALLKE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 162 LAKAFQEEAQSSGKeRLLLTAAVPSDRGLVDaGYEVDKIAQSLDFINLMAYDFHSSLEKTTGHNSPLYkRQGESGAAAEQ 241
Cdd:COG3325 176 LRAQLDALGAETGK-HYLLTAAAPAGPDKLD-GIELPKVAQYLDYVNVMTYDFHGAWSPTTGHQAPLY-DSPKDPEAQGY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 242 NVDAAVTLWLQKGTPASKLILGMPTYGRSFTLASSSDNGVGAPATGPgAPGPYTkdKGVLAY------YEACSWKERHRI 315
Cdd:COG3325 253 SVDSAVQAYLAAGVPASKLVLGVPFYGRGWTGVTGGNNGLYQPATGP-APGTWE--AGVNDYkdlkalYLGSNGYTRYWD 329
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 316 EDQKVPYAF--QDNQWVSFDDVESFKAKAAYLKQKGLGGAMVWVLDLDDFKGSfcnqgpypLIRTLRQEL 383
Cdd:COG3325 330 DVAKAPYLYngDTGTFISYDDPRSIAAKADYVKDKGLGGVMFWELSGDTADGT--------LLNAIGEGL 391
|
|
| ChtBD2 |
smart00494 |
Chitin-binding domain type 2; |
416-464 |
8.44e-12 |
|
Chitin-binding domain type 2;
Pssm-ID: 214696 [Multi-domain] Cd Length: 49 Bit Score: 59.76 E-value: 8.44e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568909678 416 NFCQGKADGVYPNPGDESTYYNCGGGRLFQQSCPPGLVFRASCKCCTWS 464
Cdd:smart00494 1 NECPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDWP 49
|
|
| CBM_14 |
pfam01607 |
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ... |
418-464 |
9.66e-12 |
|
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: 59.73 E-value: 9.66e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 568909678 418 CQGKADGVYPNPGDESTYYNCGGGRLFQQSCPPGLVFRASCKCCTWS 464
Cdd:pfam01607 1 CAGKEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYP 47
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GH18_chitolectin_chitotriosidase |
cd02872 |
This conserved domain family includes a large number of catalytically inactive chitinase-like ... |
24-383 |
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: 593.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 24 LVCYLTNWSQYRTEAVRFFPRDVDPNLCTHVIFAFAGMDN--HQLSTVEHND--ELLYQELNSLKTKNPKLKTLLAVGGW 99
Cdd:cd02872 1 VVCYFTNWAQYRPGNGKFVPENIDPFLCTHIIYAFAGLNPdgNIIILDEWNDidLGLYERFNALKEKNPNLKTLLAIGGW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 100 TFGTQKFTDMVATASNRQTFVKSALSFLRTQGFDGLDLDWEFPGGRGSPTVDKERFTALIQDLAKAFQEEAqssgkERLL 179
Cdd:cd02872 81 NFGSAKFSAMAASPENRKTFIKSAIAFLRKYGFDGLDLDWEYPGQRGGPPEDKENFVTLLKELREAFEPEA-----PRLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 180 LTAAVPSDRGLVDAGYEVDKIAQSLDFINLMAYDFHSSLEKTTGHNSPLYKRQGESGAAAEQNVDAAVTLWLQKGTPASK 259
Cdd:cd02872 156 LTAAVSAGKETIDAAYDIPEISKYLDFINVMTYDFHGSWEGVTGHNSPLYAGSADTGDQKYLNVDYAIKYWLSKGAPPEK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 260 LILGMPTYGRSFTLASSSDNGVGAPATGPGAPGPYTKDKGVLAYYEACSWKE----RHRIEDQKVPYAFQDNQWVSFDDV 335
Cdd:cd02872 236 LVLGIPTYGRSFTLASPSNTGVGAPASGPGTAGPYTREAGFLAYYEICEFLKsgwtVVWDDEQKVPYAYKGNQWVGYDDE 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 568909678 336 ESFKAKAAYLKQKGLGGAMVWVLDLDDFKGsFCNQGPYPLIRTLRQEL 383
Cdd:cd02872 316 ESIALKVQYLKSKGLGGAMVWSIDLDDFRG-TCGQGKYPLLNAINRAL 362
|
|
| Glyco_18 |
smart00636 |
Glyco_18 domain; |
23-361 |
2.37e-146 |
|
Glyco_18 domain;
Pssm-ID: 214753 [Multi-domain] Cd Length: 334 Bit Score: 420.93 E-value: 2.37e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 23 KLVCYLTNWSQYRTeavRFFPRDVDPNLCTHVIFAFAGMDN--HQLSTVEHNDELLYQELNSLKTKNPKLKTLLAVGGWT 100
Cdd:smart00636 1 RVVGYFTNWGVYGR---NFPVDDIPASKLTHIIYAFANIDPdgTVTIGDEWADIGNFGQLKALKKKNPGLKVLLSIGGWT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 101 FGtQKFTDMVATASNRQTFVKSALSFLRTQGFDGLDLDWEFPGGRGSptvDKERFTALIQDLAKAFQEEAQSsgKERLLL 180
Cdd:smart00636 78 ES-DNFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWEYPGGRGD---DRENYTALLKELREALDKEGAE--GKGYLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 181 TAAVPSDRGLVDAGYE-VDKIAQSLDFINLMAYDFHSSLEKTTGHNSPLYKRQGESGAaaeQNVDAAVTLWLQKGTPASK 259
Cdd:smart00636 152 TIAVPAGPDKIDKGYGdLPAIAKYLDFINLMTYDFHGAWSNPTGHNAPLYAGPGDPEK---YNVDYAVKYYLCKGVPPSK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 260 LILGMPTYGRSFTLASSSDNGVGAPATGPGAPGPYTKDKGVLAYYEACSWK--ERHRIEDQKVPYAFQDN--QWVSFDDV 335
Cdd:smart00636 229 LVLGIPFYGRGWTLVDGSNNGPGAPFTGPATGGPGTWEGGVVDYREICKLLgaTVVYDDTAKAPYAYNPGtgQWVSYDDP 308
|
330 340
....*....|....*....|....*.
gi 568909678 336 ESFKAKAAYLKQKGLGGAMVWVLDLD 361
Cdd:smart00636 309 RSIKAKADYVKDKGLGGVMIWELDAD 334
|
|
| Glyco_hydro_18 |
pfam00704 |
Glycosyl hydrolases family 18; |
23-361 |
2.16e-118 |
|
Glycosyl hydrolases family 18;
Pssm-ID: 425828 [Multi-domain] Cd Length: 311 Bit Score: 349.06 E-value: 2.16e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 23 KLVCYLTNWSQYRTEavrffpRDVDPNLCTHVIFAFAGMDNHQLSTVEHN-DELLYQELNSLKT-KNPKLKTLLAVGGWT 100
Cdd:pfam00704 1 RIVGYYTSWGVYRNG------NFLPSDKLTHIIYAFANIDGSDGTLFIGDwDLGNFEQLKKLKKqKNPGVKVLLSIGGWT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 101 FGTqKFTDMVATASNRQTFVKSALSFLRTQGFDGLDLDWEFPGGRgspTVDKERFTALIQDLAKAFQEEaqsSGKERLLL 180
Cdd:pfam00704 75 DST-GFSLMASNPASRKKFADSIVSFLRKYGFDGIDIDWEYPGGN---PEDKENYDLLLRELRAALDEA---KGGKKYLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 181 TAAVPSDRGLVDAGYEVDKIAQSLDFINLMAYDFHSSLEKTTGHNSPLYkrqgesgAAAEQNVDAAVTLWLQKGTPASKL 260
Cdd:pfam00704 148 SAAVPASYPDLDKGYDLPKIAKYLDFINVMTYDFHGSWDNVTGHHAPLY-------GGGSYNVDYAVKYYLKQGVPASKL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 261 ILGMPTYGRSFTLASSSDNgvgapatgpgapgpyTKDKGVLAYYEACS-----WKERHRIEDQKVPYAFQDNQWVSFDDV 335
Cdd:pfam00704 221 VLGVPFYGRSWTLVNGSGN---------------TWEDGVLAYKEICNllkdnGATVVWDDVAKAPYVYDGDQFITYDDP 285
|
330 340
....*....|....*....|....*.
gi 568909678 336 ESFKAKAAYLKQKGLGGAMVWVLDLD 361
Cdd:pfam00704 286 RSIATKVDYVKAKGLGGVMIWSLDAD 311
|
|
| ChiA |
COG3325 |
Chitinase, GH18 family [Carbohydrate transport and metabolism]; |
23-383 |
5.17e-107 |
|
Chitinase, GH18 family [Carbohydrate transport and metabolism];
Pssm-ID: 442554 [Multi-domain] Cd Length: 391 Bit Score: 322.63 E-value: 5.17e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 23 KLVCYLTNWSQYRTEavrFFPRDVDPNLCTHVIFAFAGMDN------------HQLSTVEHNDELLY----QELNSLKTK 86
Cdd:COG3325 20 RVVGYFTQWGIYGRN---YLVKDIPASKLTHINYAFANVDPdgkcsvgdawakPSVDGAADDWDQPLkgnfNQLKKLKAK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 87 NPKLKTLLAVGGWTfGTQKFTDMVATASNRQTFVKSALSFLRTQGFDGLDLDWEFPGGRGSPTV-----DKERFTALIQD 161
Cdd:COG3325 97 NPNLKVLISIGGWT-WSKGFSDAAATPASRAAFVDSCVDLLRKYNFDGIDIDWEYPGSGGAPGNvyrpeDKANFTALLKE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 162 LAKAFQEEAQSSGKeRLLLTAAVPSDRGLVDaGYEVDKIAQSLDFINLMAYDFHSSLEKTTGHNSPLYkRQGESGAAAEQ 241
Cdd:COG3325 176 LRAQLDALGAETGK-HYLLTAAAPAGPDKLD-GIELPKVAQYLDYVNVMTYDFHGAWSPTTGHQAPLY-DSPKDPEAQGY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 242 NVDAAVTLWLQKGTPASKLILGMPTYGRSFTLASSSDNGVGAPATGPgAPGPYTkdKGVLAY------YEACSWKERHRI 315
Cdd:COG3325 253 SVDSAVQAYLAAGVPASKLVLGVPFYGRGWTGVTGGNNGLYQPATGP-APGTWE--AGVNDYkdlkalYLGSNGYTRYWD 329
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 316 EDQKVPYAF--QDNQWVSFDDVESFKAKAAYLKQKGLGGAMVWVLDLDDFKGSfcnqgpypLIRTLRQEL 383
Cdd:COG3325 330 DVAKAPYLYngDTGTFISYDDPRSIAAKADYVKDKGLGGVMFWELSGDTADGT--------LLNAIGEGL 391
|
|
| GH18_chitinase |
cd06548 |
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ... |
25-361 |
8.81e-96 |
|
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: 291.46 E-value: 8.81e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 25 VCYLTNWSQYrtEAVRFFPRDVDPNLCTHVIFAFAGMDN---HQLSTVEHNDELLY-----------------QELNSLK 84
Cdd:cd06548 2 VGYFTNWGIY--GRNYFVTDDIPADKLTHINYAFADIDGdggVVTSDDEAADEAAQsvdggadtddqplkgnfGQLRKLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 85 TKNPKLKTLLAVGGWTFGtQKFTDMVATASNRQTFVKSALSFLRTQGFDGLDLDWEFPGGRGSPT-----VDKERFTALI 159
Cdd:cd06548 80 QKNPHLKILLSIGGWTWS-GGFSDAAATEASRAKFADSAVDFIRKYGFDGIDIDWEYPGSGGAPGnvarpEDKENFTLLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 160 QDLAKAFQEEAQSSGKeRLLLTAAVPSDRGLVDAGyEVDKIAQSLDFINLMAYDFHSSLEKTTGHNSPLYKRQGESgaAA 239
Cdd:cd06548 159 KELREALDALGAETGR-KYLLTIAAPAGPDKLDKL-EVAEIAKYLDFINLMTYDFHGAWSNTTGHHSNLYASPADP--PG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 240 EQNVDAAVTLWLQKGTPASKLILGMPTYGRSFTLAsssdngvgapatgpgapgpytkdkgvlayyeacswkERHRIEDQK 319
Cdd:cd06548 235 GYSVDAAVNYYLSAGVPPEKLVLGVPFYGRGWTGY------------------------------------TRYWDEVAK 278
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 568909678 320 VPYAF--QDNQWVSFDDVESFKAKAAYLKQKGLGGAMVWVLDLD 361
Cdd:cd06548 279 APYLYnpSTKTFISYDDPRSIKAKADYVKDKGLGGVMFWELSGD 322
|
|
| GH18_IDGF |
cd02873 |
The IDGF's (imaginal disc growth factors) are a family of growth factors identified in insects ... |
23-383 |
3.76e-78 |
|
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: 249.15 E-value: 3.76e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 23 KLVCYLTNWSQYRTEAVRFFPRDVDP--NLCTHVIFAFAGM--DNHQLSTVEHN---DELLYQELNSLKTKNPKLKTLLA 95
Cdd:cd02873 1 KLVCYYDSKSYLREGLAKMSLEDLEPalQFCTHLVYGYAGIdaDTYKIKSLNEDldlDKSHYRAITSLKRKYPHLKVLLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 96 VGGWTF-----GTQKFTDMVATASNRQTFVKSALSFLRTQGFDGLDLDWEFP--------GG------------RGSPTV 150
Cdd:cd02873 81 VGGDRDtdeegENEKYLLLLESSESRNAFINSAHSLLKTYGFDGLDLAWQFPknkpkkvrGTfgsawhsfkklfTGDSVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 151 D------KERFTALIQDLAKAFQeeaqSSGKerlLLTAAV-PSdrglVDAG--YEVDKIAQSLDFINLMAYDFHSSLE-- 219
Cdd:cd02873 161 DekaaehKEQFTALVRELKNALR----PDGL---LLTLTVlPH----VNSTwyFDVPAIANNVDFVNLATFDFLTPERnp 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 220 KTTGHNSPLYKRQGESgaaAEQNVDAAVTLWLQKGTPASKLILGMPTYGRSFTLasSSDNGV-GAP----ATGPGAPGPY 294
Cdd:cd02873 230 EEADYTAPIYELYERN---PHHNVDYQVKYWLNQGTPASKLNLGIATYGRAWKL--TKDSGItGVPpvleTDGPGPAGPQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 295 TKDKGVLAYYEACSWKERHRIEDQKVP--------------YAFQ---DNQ----WVSFDDVESFKAKAAYLKQKGLGGA 353
Cdd:cd02873 305 TKTPGLLSWPEICSKLPNPANLKGADAplrkvgdptkrfgsYAYRpadENGehgiWVSYEDPDTAANKAGYAKAKGLGGV 384
|
410 420 430
....*....|....*....|....*....|
gi 568909678 354 MVWVLDLDDFKGSfCNQGPYPLIRTLRQEL 383
Cdd:cd02873 385 ALFDLSLDDFRGQ-CTGDKFPILRSAKYRL 413
|
|
| GH18_plant_chitinase_class_V |
cd02879 |
The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the ... |
41-362 |
3.58e-70 |
|
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: 224.94 E-value: 3.58e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 41 FFPRDVDPNLCTHVIFAFAGMDN--HQLsTVEHNDELLYQEL-NSLKTKNPKLKTLLAVGGWTFGTQKFTDMVATASNRQ 117
Cdd:cd02879 16 FPPSNIDSSLFTHLFYAFADLDPstYEV-VISPSDESEFSTFtETVKRKNPSVKTLLSIGGGGSDSSAFAAMASDPTARK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 118 TFVKSALSFLRTQGFDGLDLDWEFPggrgSPTVDKERFTALIQDLAKAFQEEAQSSGKERLLLTAAVPSDRGLVDAG--- 194
Cdd:cd02879 95 AFINSSIKVARKYGFDGLDLDWEFP----SSQVEMENFGKLLEEWRAAVKDEARSSGRPPLLLTAAVYFSPILFLSDdsv 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 195 -YEVDKIAQSLDFINLMAYDFHSSLEK-TTGHNSPLYKRqgesgaAAEQNVDAAVTLWLQKGTPASKLILGMPTYGRSFT 272
Cdd:cd02879 171 sYPIEAINKNLDWVNVMAYDYYGSWESnTTGPAAALYDP------NSNVSTDYGIKSWIKAGVPAKKLVLGLPLYGRAWT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 273 LASssdngvgaPATGpgapgpytkdkgvlayyeacswkerhriedqkVPYAFQDNQWVSFDDVESFKAKAAYLKQKGLGG 352
Cdd:cd02879 245 LYD--------TTTV--------------------------------SSYVYAGTTWIGYDDVQSIAVKVKYAKQKGLLG 284
|
330
....*....|
gi 568909678 353 AMVWVLDLDD 362
Cdd:cd02879 285 YFAWAVGYDD 294
|
|
| GH18_chitinase-like |
cd00598 |
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ... |
24-213 |
1.85e-51 |
|
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: 172.95 E-value: 1.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 24 LVCYLTNWSQYRTeavrFFPRDVDPNLCTHVIFAFAGM--DNHQLSTVEHNDELLYQELNSLKTKNPKLKTLLAVGGWTF 101
Cdd:cd00598 1 VICYYDGWSSGRG----PDPTDIPLSLCTHIIYAFAEIssDGSLNLFGDKSEEPLKGALEELASKKPGLKVLISIGGWTD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 102 GTqkFTDMVATASNRQTFVKSALSFLRTQGFDGLDLDWEFPGGRGSPtvDKERFTALIQDLAKAFqeeaqssGKERLLLT 181
Cdd:cd00598 77 SS--PFTLASDPASRAAFANSLVSFLKTYGFDGVDIDWEYPGAADNS--DRENFITLLRELRSAL-------GAANYLLT 145
|
170 180 190
....*....|....*....|....*....|..
gi 568909678 182 AAVPSDRGLVDAGYEVDKIAQSLDFINLMAYD 213
Cdd:cd00598 146 IAVPASYFDLGYAYDVPAIGDYVDFVNVMTYD 177
|
|
| GH18_zymocin_alpha |
cd02878 |
Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle ... |
43-361 |
2.03e-28 |
|
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: 115.10 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 43 PRDVDPNLCTHVIFAFAGMdNHQLSTvehnDELLYQELNSLKTKNPKLKTLLAVGGWTFGT-----QKFTDMVATAsNRQ 117
Cdd:cd02878 20 VTQIDTSKYTHIHFAFANI-TSDFSV----DVSSVQEQFSDFKKLKGVKKILSFGGWDFSTspstyQIFRDAVKPA-NRD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 118 TFVKSALSFLRTQGFDGLDLDWEFPGG-------RGSPTvDKERFTALIQDLAKAFqeeaqSSGKerlLLTAAVPSDRGL 190
Cdd:cd02878 94 TFANNVVNFVNKYNLDGVDFDWEYPGApdipgipAGDPD-DGKNYLEFLKLLKSKL-----PSGK---SLSIAAPASYWY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 191 VdAGYEVDKIAQSLDFINLMAYDFHSslekTTGHNSPLYKRQGESGAAAEQNVDAAVTL----WLQK-GTPASKLILGMP 265
Cdd:cd02878 165 L-KGFPIKDMAKYVDYIVYMTYDLHG----QWDYGNKWASPGCPAGNCLRSHVNKTETLdalsMITKaGVPSNKVVVGVA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 266 TYGRSFTLASSSDNGVGAPATGPGAPGPYTKDKGVLAYYEacsWKERHRIEDQKVPYA-------------FQDNQWVSF 332
Cdd:cd02878 240 SYGRSFKMADPGCTGPGCTFTGPGSGAEAGRCTCTAGYGA---ISEIEIIDISKSKNKrwydtdsdsdilvYDDDQWVAY 316
|
330 340
....*....|....*....|....*....
gi 568909678 333 DDVESFKAKAAYLKQKGLGGAMVWVLDLD 361
Cdd:cd02878 317 MSPATKAARIEWYKGLNFGGTSDWAVDLQ 345
|
|
| GH18_CFLE_spore_hydrolase |
cd02874 |
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ... |
109-362 |
2.73e-26 |
|
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: 108.51 E-value: 2.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 109 MVATASNRQTFVKSALSFLRTQGFDGLDLDWEFpggrgSPTVDKERFTALIQDLAKAFQEEaqssGKerLLLTAAVPS-- 186
Cdd:cd02874 81 VLSNPEARQRLINNILALAKKYGYDGVNIDFEN-----VPPEDREAYTQFLRELSDRLHPA----GY--TLSTAVVPKts 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 187 --DRGLVDAGYEVDKIAQSLDFINLMAYDFHSslekttghnsplykRQGESGAAA-----EQNVDAAVTlwlqkGTPASK 259
Cdd:cd02874 150 adQFGNWSGAYDYAAIGKIVDFVVLMTYDWHW--------------RGGPPGPVApigwvERVLQYAVT-----QIPREK 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 260 LILGMPTYGRSFTLasssdngvgapatgPGAPGPYTKdkgVLAYYEACSWKERHRI-----EDQKVP-YAFQDNQ----W 329
Cdd:cd02874 211 ILLGIPLYGYDWTL--------------PYKKGGKAS---TISPQQAINLAKRYGAeiqydEEAQSPfFRYVDEQgrrhE 273
|
250 260 270
....*....|....*....|....*....|...
gi 568909678 330 VSFDDVESFKAKAAYLKQKGLGGAMVWVLDLDD 362
Cdd:cd02874 274 VWFEDARSLQAKFELAKEYGLRGVSYWRLGLED 306
|
|
| GH18_3CO4_chitinase |
cd06545 |
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an ... |
25-272 |
5.06e-18 |
|
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: 83.27 E-value: 5.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 25 VCYLTNWSQYRTeavrFFPRdVDPNLCTHVIFAFAGMD-NHQLSTVEHNDELLYQeLNSLKTKNpkLKTLLAVGGWTFGT 103
Cdd:cd06545 2 VGYLPNYDDLNA----LSPT-IDFSKLTHINLAFANPDaNGTLNANPVRSELNSV-VNAAHAHN--VKILISLAGGSPPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 104 qkFTDMVATASNRQTFVKSALSFLRTQGFDGLDLDWEfpggrgSPTVDKERFTALIQDLAKAFQeeaqssgKERLLLTAA 183
Cdd:cd06545 74 --FTAALNDPAKRKALVDKIINYVVSYNLDGIDVDLE------GPDVTFGDYLVFIRALYAALK-------KEGKLLTAA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 184 VPSDRGlvdaGYEVDKIAQSLDFINLMAYDfhsslekttgHNSPLYKRQGESGAAAEQNVDaAVTLWLQKG-TPASKLIL 262
Cdd:cd06545 139 VSSWNG----GAVSDSTLAYFDFINIMSYD----------ATGPWWGDNPGQHSSYDDAVN-DLNYWNERGlASKDKLVL 203
|
250
....*....|
gi 568909678 263 GMPTYGRSFT 272
Cdd:cd06545 204 GLPFYGYGFY 213
|
|
| GH18_chitobiase |
cd02875 |
Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes ... |
114-365 |
2.08e-15 |
|
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: 77.47 E-value: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 114 SNRQTFVKSALSFLRTQGFDGLDLDWEFPGGRGSPTVDKerFTALIQDLAKAFQEEAQSSGkerllLTAAVPSDRGLVD- 192
Cdd:cd02875 95 TYRTQWIQQKVELAKSQFMDGINIDIEQPITKGSPEYYA--LTELVKETTKAFKKENPGYQ-----ISFDVAWSPSCIDk 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 193 AGYEVDKIAQSLDFINLMAYDFHS---SLEKTTGHNSPLykrqgesgaaaeQNVDAAVTLWLQKGTPASKLILGMPTYGR 269
Cdd:cd02875 168 RCYDYTGIADASDFLVVMDYDEQSqiwGKECIAGANSPY------------SQTLSGYNNFTKLGIDPKKLVMGLPWYGY 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 270 SFT-LASSSDNGV---------GAPAT-GPGAPGPYTK-DKGVLAYYEACSWKerhriEDQKVPYAFQDN-----QWVSF 332
Cdd:cd02875 236 DYPcLNGNLEDVVctipkvpfrGANCSdAAGRQIPYSEiMKQINSSIGGRLWD-----SEQKSPFYNYKDkqgnlHQVWY 310
|
250 260 270
....*....|....*....|....*....|...
gi 568909678 333 DDVESFKAKAAYLKQKGLGGAMVWVLDLDDFKG 365
Cdd:cd02875 311 DNPQSLSIKVAYAKNLGLKGIGMWNGDLLDYSG 343
|
|
| ChtBD2 |
smart00494 |
Chitin-binding domain type 2; |
416-464 |
8.44e-12 |
|
Chitin-binding domain type 2;
Pssm-ID: 214696 [Multi-domain] Cd Length: 49 Bit Score: 59.76 E-value: 8.44e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568909678 416 NFCQGKADGVYPNPGDESTYYNCGGGRLFQQSCPPGLVFRASCKCCTWS 464
Cdd:smart00494 1 NECPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDWP 49
|
|
| CBM_14 |
pfam01607 |
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ... |
418-464 |
9.66e-12 |
|
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: 59.73 E-value: 9.66e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 568909678 418 CQGKADGVYPNPGDESTYYNCGGGRLFQQSCPPGLVFRASCKCCTWS 464
Cdd:pfam01607 1 CAGKEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYP 47
|
|
| GH18_SI-CLP |
cd02876 |
Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein ... |
83-287 |
1.09e-08 |
|
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: 56.55 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 83 LKTKNPKLKTL--LAVGGWTFgtQKFTDMVATASNRQTFVKSALSFLRTQGFDGLDLD-WEFPGGRGSPTVDKERFTaLI 159
Cdd:cd02876 60 VRKANKNIKILprVLFEGWSY--QDLQSLLNDEQEREKLIKLLVTTAKKNHFDGIVLEvWSQLAAYGVPDKRKELIQ-LV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 160 QDLAKAFQeeaqsSGKERLLLTAAVPSDRGLVDAGY---EVDKIAQSLDFINLMAYDFhSSLEKtTGHNSPLYKrqgesg 236
Cdd:cd02876 137 IHLGETLH-----SANLKLILVIPPPREKGNQNGLFtrkDFEKLAPHVDGFSLMTYDY-SSPQR-PGPNAPLSW------ 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568909678 237 aaaeqnVDAAVTLWLQKGTP-ASKLILGMPTYGRSFTLasssdNGVGAPATG 287
Cdd:cd02876 204 ------VRSCLELLLPESGKkRAKILLGLNFYGNDYTL-----PGGGGAITG 244
|
|
| GH18_trifunctional |
cd06549 |
GH18 domain of an uncharacterized family of bacterial proteins, which share a common ... |
59-290 |
1.07e-05 |
|
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: 47.02 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 59 AGMDNHQLSTVEHNDELlYQELNSLKTKNPKLKTLLAVGGWTFgtQKFTDMVATASNRQTFVKSALSFLRTQGFDGLDLD 138
Cdd:cd06549 35 TGPEGRIDVFVDPQGVA-IIAAAKAHPKVLPLVQNISGGAWDG--KNIARLLADPSARAKFIANIAAYLERNQADGIVLD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 139 WEfpggrgSPTVDKER-FTALIQDLAKAFqeeaqssGKERLLLTAAVPSDrglvDAGYEVDKIAQSLDFINLMAYDFHSS 217
Cdd:cd06549 112 FE------ELPADDLPkYVAFLSELRRRL-------PAQGKQLTVTVPAD----EADWNLKALARNADKLILMAYDEHYQ 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568909678 218 lekttghnsplykrQGESGAAAEQ-----NVDAAVtlwlqKGTPASKLILGMPTYGRSFTLasssdNGVGAPATGPGA 290
Cdd:cd06549 175 --------------GGAPGPIASQdwfesNLAQAV-----KKLPPEKLIVALGSYGYDWTK-----GGNTKAISSEAA 228
|
|
| GH18_chitinase_D-like |
cd02871 |
GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes ... |
24-266 |
4.90e-05 |
|
GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes the 1,4-beta-linkages of N-acetylglucosamine in chitin and chitodextrins. The domain architecture of ChiD includes a catalytic glycosyl hydrolase family 18 (GH18) domain, a chitin-binding domain, and a fibronectin type III domain. The chitin-binding and fibronectin type III domains are located either N-terminal or C-terminal to the catalytic domain. This family includes exochitinase Chi36 from Bacillus cereus.
Pssm-ID: 119350 [Multi-domain] Cd Length: 312 Bit Score: 45.02 E-value: 4.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 24 LVCYLTNWSQYrTEAVRFFPRDVDP--NLcthVIFAFAGMDNHQLSTVEHN---------DELLYQELNSLKTKNPKlkT 92
Cdd:cd02871 3 LVGYWHNWDNG-AGSGRQDLDDVPSkyNV---INVAFAEPTSDGGGEVTFNngsspggysPAEFKADIKALQAKGKK--V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 93 LLAVGGwtfgtQKFTDMVATASNRQTFVKSALSFLRTQGFDGLDLDWEfpggRGSPTVDKerfTALIQDLAKAFQEEAQS 172
Cdd:cd02871 77 LISIGG-----ANGHVDLNHTAQEDNFVDSIVAIIKEYGFDGLDIDLE----SGSNPLNA---TPVITNLISALKQLKDH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 173 SGKErLLLTAAvP---------SDRGLVDAGYE--VDKIAQSLDFINLMAYDfhsslekttghNSPLYKRQGESGAAAEQ 241
Cdd:cd02871 145 YGPN-FILTMA-PetpyvqggyAAYGGIWGAYLplIDNLRDDLTWLNVQYYN-----------SGGMGGCDGQSYSQGTA 211
|
250 260 270
....*....|....*....|....*....|....*.
gi 568909678 242 NVDAAVTLWLQKGT-----------PASKLILGMPT 266
Cdd:cd02871 212 DFLVALADMLLTGFpiagndrfpplPADKVVIGLPA 247
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
91-140 |
1.28e-03 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 41.28 E-value: 1.28e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 568909678 91 KTLLAVGGwtfgtQKFTDMVATASNRQTFVKSALSFLRTQGFDGLDLDWE 140
Cdd:COG3469 290 KVLLSIGG-----ANGTVQLNTAAAADNFVNSVIALIDEYGFDGLDIDLE 334
|
|
| GH18_narbonin |
cd06544 |
Narbonin is a plant 2S protein from the globulin fraction of narbon bean (Vicia narbonensis L.) ... |
38-162 |
2.49e-03 |
|
Narbonin is a plant 2S protein from the globulin fraction of narbon bean (Vicia narbonensis L.) cotyledons with unknown function. Narbonin has a glycosyl hydrolase family 18 (GH18) domain without the conserved catalytic residues and with no known enzymatic activity. Narbonin amounts to up to 3% of the total seed globulins of mature seeds and was thought to be a storage protein but was found to degrade too slowly during germination. This family also includes the VfNOD32 nodulin from Vicia faba.
Pssm-ID: 119361 Cd Length: 253 Bit Score: 39.66 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909678 38 AVRF--FPrdVDPNLCTHVIFAFA-GMDNHQLST-----VEHNDELLYQE-LNSLKTKNPKLKTLLAVGGWTFGTQ-KFT 107
Cdd:cd06544 12 GVTFsdVP--INPKVEFHFILSFAiDYDTESNPTngkfnPYWDTENLTPEaVKSIKAQHPNVKVVISIGGRGVQNNpTPF 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 568909678 108 DMVATASNRQTFVKSALSFLRTQGFDGLDLDWE-FPggrgsptVDKERFTALIQDL 162
Cdd:cd06544 90 DPSNVDSWVSNAVSSLTSIIQTYNLDGIDIDYEhFP-------ADPDTFVECIGQL 138
|
|
| |
