|
Name |
Accession |
Description |
Interval |
E-value |
| GH18_chitolectin_chitotriosidase |
cd02872 |
This conserved domain family includes a large number of catalytically inactive chitinase-like ... |
221-586 |
1.38e-174 |
|
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: 537.91 E-value: 1.38e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 221 VLCYMSNWAFYRSGEAHFVPEQIDPNLCSAIIYSFASLDPDhLTIREFDSWVDLDNQYYRRVTSL-----GVPVLIALGG 295
Cdd:cd02872 1 VVCYFTNWAQYRPGNGKFVPENIDPFLCTHIIYAFAGLNPD-GNIIILDEWNDIDLGLYERFNALkeknpNLKTLLAIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 296 WTDSSGsKYSRLVSDNLKRRVFISSVSSFLLRHGFSGLHLDWNYPKCWQsdcsrGPVTDRPNLTKLLRELRTEFQSVDPK 375
Cdd:cd02872 80 WNFGSA-KFSAMAASPENRKTFIKSAIAFLRKYGFDGLDLDWEYPGQRG-----GPPEDKENFVTLLKELREAFEPEAPR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 376 FQLGVAISGYKEIIKEAYDFPALSDIVDYMTVMTYDYHGAWEQKTGHVSPLYGLSSDT--YPQYNTNYTMQLLLKMGARR 453
Cdd:cd02872 154 LLLTAAVSAGKETIDAAYDIPEISKYLDFINVMTYDFHGSWEGVTGHNSPLYAGSADTgdQKYLNVDYAIKYWLSKGAPP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 454 EKLVLSIPFYGQSFTLATAHQilAGPGVAASGPGDAGELTKQPGMLAYYEICQRLTKfNWISDRNLNViFGPFAMLNDQW 533
Cdd:cd02872 234 EKLVLGIPTYGRSFTLASPSN--TGVGAPASGPGTAGPYTREAGFLAYYEICEFLKS-GWTVVWDDEQ-KVPYAYKGNQW 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 442628919 534 VGYEDPTSAQAKARYAANNNFAGVAAWTIDLDDFRNLCCNESYPLLRAINRAL 586
Cdd:cd02872 310 VGYDDEESIALKVQYLKSKGLGGAMVWSIDLDDFRGTCGQGKYPLLNAINRAL 362
|
|
| GH18_chitolectin_chitotriosidase |
cd02872 |
This conserved domain family includes a large number of catalytically inactive chitinase-like ... |
967-1331 |
3.52e-166 |
|
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: 514.80 E-value: 3.52e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 967 VICYFTNWAWYRKGIGRFTPDDINTELCTHVIYGFAVLDySELVLRTHDSWADVENNFYTRVTSLKSK--GIKVSLALGG 1044
Cdd:cd02872 1 VVCYFTNWAQYRPGNGKFVPENIDPFLCTHIIYAFAGLN-PDGNIIILDEWNDIDLGLYERFNALKEKnpNLKTLLAIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1045 WNDSQGdKYSRLVRSPMARSRFVRHALEFIEKYGFEGLDLDWEYPVCWQtecnkGSTEEKDGFTAWVQELSEAFRP--RG 1122
Cdd:cd02872 80 WNFGSA-KFSAMAASPENRKTFIKSAIAFLRKYGFDGLDLDWEYPGQRG-----GPPEDKENFVTLLKELREAFEPeaPR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1123 LMLSTAVSPSRKIIDAGYDIPQLSRYFDWIAVMTYDFHGHWDKKTGHVAPLYHHPDD--DFEYFNVNYSINYWMEKGAPS 1200
Cdd:cd02872 154 LLLTAAVSAGKETIDAAYDIPEISKYLDFINVMTYDFHGSWEGVTGHNSPLYAGSADtgDQKYLNVDYAIKYWLSKGAPP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1201 QKLVMGIPLYGQSFTLENTNSSGLNAKAPAPGEAGEFTRAAGFLAYYEICERVNrQGWQVVHDEfGRMGPYAYKGTQWVS 1280
Cdd:cd02872 234 EKLVLGIPTYGRSFTLASPSNTGVGAPASGPGTAGPYTREAGFLAYYEICEFLK-SGWTVVWDD-EQKVPYAYKGNQWVG 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 442628919 1281 YDSPDMVRKKSLLVRSLKLGGGMVWALDLDDFKNRCGNGVHPLLTEIHNVL 1331
Cdd:cd02872 312 YDDEESIALKVQYLKSKGLGGAMVWSIDLDDFRGTCGQGKYPLLNAINRAL 362
|
|
| GH18_chitolectin_chitotriosidase |
cd02872 |
This conserved domain family includes a large number of catalytically inactive chitinase-like ... |
1411-1774 |
1.29e-164 |
|
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: 510.56 E-value: 1.29e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1411 IICYFTNWAWYRQGGGKFLPEDIDSDLCTHIIYGFAVLSrDNLTIQPHDSWADLDNKFYERIVAYRKKGA--KVTVAIGG 1488
Cdd:cd02872 1 VVCYFTNWAQYRPGNGKFVPENIDPFLCTHIIYAFAGLN-PDGNIIILDEWNDIDLGLYERFNALKEKNPnlKTLLAIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1489 WNDSAGdKYSRLVRNPEARSRFIRNVLDFIEEYNFDGLDLDWEYPVCWQvdckkGTAEEKIGFSALVRELFYAFQP--RG 1566
Cdd:cd02872 80 WNFGSA-KFSAMAASPENRKTFIKSAIAFLRKYGFDGLDLDWEYPGQRG-----GPPEDKENFVTLLKELREAFEPeaPR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1567 LILSAAVSPNKKVIDAGYEVAELSHYFSWISVMAYDYHGQWDKKTGHVAPMYSHPEGT---ANFNANFSMNYWISMGADR 1643
Cdd:cd02872 154 LLLTAAVSAGKETIDAAYDIPEISKYLDFINVMTYDFHGSWEGVTGHNSPLYAGSADTgdqKYLNVDYAIKYWLSKGAPP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1644 RKLVMGIPLYGQSFSLAETTKHQLNAPTYGGGEAGEATRARGFLAYYEICLKIRhHRWNVVRDTKGRiGPFAYHGDQWVS 1723
Cdd:cd02872 234 EKLVLGIPTYGRSFTLASPSNTGVGAPASGPGTAGPYTREAGFLAYYEICEFLK-SGWTVVWDDEQK-VPYAYKGNQWVG 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 442628919 1724 FDDVPMIRHKSEYIKAMGLGGAMIWALDLDDFKNVCECESYPLLKAINRVL 1774
Cdd:cd02872 312 YDDEESIALKVQYLKSKGLGGAMVWSIDLDDFRGTCGQGKYPLLNAINRAL 362
|
|
| GH18_chitolectin_chitotriosidase |
cd02872 |
This conserved domain family includes a large number of catalytically inactive chitinase-like ... |
1910-2274 |
2.73e-164 |
|
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: 509.41 E-value: 2.73e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1910 VVCYFTSWAWYRSSQGKFVPEDIDANLCTHLIYGFAVLDSKsLTIKTHDSWTDIDNRFYERVVEYKQR--GLRVMLAIGG 1987
Cdd:cd02872 1 VVCYFTNWAQYRPGNGKFVPENIDPFLCTHIIYAFAGLNPD-GNIIILDEWNDIDLGLYERFNALKEKnpNLKTLLAIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1988 WNDslGS-KYARLVLNSQSRRRFVASVISFLEQHGFEGLDLAWEFPVCWQvncnrGNPTEKDGFVALVKELSEAFKEN-- 2064
Cdd:cd02872 80 WNF--GSaKFSAMAASPENRKTFIKSAIAFLRKYGFDGLDLDWEYPGQRG-----GPPEDKENFVTLLKELREAFEPEap 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 2065 GLILSAAVSPSKMVIDAGYNVFELSPYFDWVAVMTYDFHGHWDMRTGQIAPLFHRGGD--ENLYLNGNFSIHYWLERGIP 2142
Cdd:cd02872 153 RLLLTAAVSAGKETIDAAYDIPEISKYLDFINVMTYDFHGSWEGVTGHNSPLYAGSADtgDQKYLNVDYAIKYWLSKGAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 2143 NDKLVMGMPMYGQTFTLADQNRRSLNDKTVGPGKAGTFTRADGFLAYYEICEKvVNDDWKVVRDEEGiFGSYAYSGNQWI 2222
Cdd:cd02872 233 PEKLVLGIPTYGRSFTLASPSNTGVGAPASGPGTAGPYTREAGFLAYYEICEF-LKSGWTVVWDDEQ-KVPYAYKGNQWV 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 442628919 2223 SYDDVTTIRRKSQFIKSLQLGGGMIWALDLDDFRGLCGCGKHPLLRTLSQEL 2274
Cdd:cd02872 311 GYDDEESIALKVQYLKSKGLGGAMVWSIDLDDFRGTCGQGKYPLLNAINRAL 362
|
|
| Glyco_18 |
smart00636 |
Glyco_18 domain; |
1410-1753 |
2.58e-122 |
|
Glyco_18 domain;
Pssm-ID: 214753 [Multi-domain] Cd Length: 334 Bit Score: 389.73 E-value: 2.58e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1410 KIICYFTNWAWYrqgGGKFLPEDIDSDLCTHIIYGFAVLSRDNlTIQPHDSWADLDNKFYERIVAYRKKGAKVTVAIGGW 1489
Cdd:smart00636 1 RVVGYFTNWGVY---GRNFPVDDIPASKLTHIIYAFANIDPDG-TVTIGDEWADIGNFGQLKALKKKNPGLKVLLSIGGW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1490 NDSagDKYSRLVRNPEARSRFIRNVLDFIEEYNFDGLDLDWEYPVCWQVDckkgtaeeKIGFSALVRELFYAFQ-----P 1564
Cdd:smart00636 77 TES--DNFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWEYPGGRGDD--------RENYTALLKELREALDkegaeG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1565 RGLILSAAVSPNKKVIDAGYE-VAELSHYFSWISVMAYDYHGQWDKKTGHVAPMYSHPEGTANFNANFSMNYWISMGADR 1643
Cdd:smart00636 147 KGYLLTIAVPAGPDKIDKGYGdLPAIAKYLDFINLMTYDFHGAWSNPTGHNAPLYAGPGDPEKYNVDYAVKYYLCKGVPP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1644 RKLVMGIPLYGQSFSLAETTKHQLNAPTYGGGEAGEATRARGFLAYYEICLKIrhhRWNVVRDTKGRiGPFAYHGD--QW 1721
Cdd:smart00636 227 SKLVLGIPFYGRGWTLVDGSNNGPGAPFTGPATGGPGTWEGGVVDYREICKLL---GATVVYDDTAK-APYAYNPGtgQW 302
|
330 340 350
....*....|....*....|....*....|..
gi 442628919 1722 VSFDDVPMIRHKSEYIKAMGLGGAMIWALDLD 1753
Cdd:smart00636 303 VSYDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
|
|
| Glyco_18 |
smart00636 |
Glyco_18 domain; |
1909-2253 |
3.96e-119 |
|
Glyco_18 domain;
Pssm-ID: 214753 [Multi-domain] Cd Length: 334 Bit Score: 380.49 E-value: 3.96e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1909 KVVCYFTSWAWYRSsqgKFVPEDIDANLCTHLIYGFAVLDSkSLTIKTHDSWTDIDNRFYERVVEYKQRGLRVMLAIGGW 1988
Cdd:smart00636 1 RVVGYFTNWGVYGR---NFPVDDIPASKLTHIIYAFANIDP-DGTVTIGDEWADIGNFGQLKALKKKNPGLKVLLSIGGW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1989 NDSlgSKYARLVLNSQSRRRFVASVISFLEQHGFEGLDLAWEFPVCWqvncnrgnPTEKDGFVALVKELSEAFKE----- 2063
Cdd:smart00636 77 TES--DNFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWEYPGGR--------GDDRENYTALLKELREALDKegaeg 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 2064 NGLILSAAVSPSKMVIDAGYN-VFELSPYFDWVAVMTYDFHGHWDMRTGQIAPLFHRGGDENlYLNGNFSIHYWLERGIP 2142
Cdd:smart00636 147 KGYLLTIAVPAGPDKIDKGYGdLPAIAKYLDFINLMTYDFHGAWSNPTGHNAPLYAGPGDPE-KYNVDYAVKYYLCKGVP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 2143 NDKLVMGMPMYGQTFTLADQNRRSLNDKTVGPGKAGTFTRADGFLAYYEICEKVvndDWKVVRDEEGiFGSYAYSGN--Q 2220
Cdd:smart00636 226 PSKLVLGIPFYGRGWTLVDGSNNGPGAPFTGPATGGPGTWEGGVVDYREICKLL---GATVVYDDTA-KAPYAYNPGtgQ 301
|
330 340 350
....*....|....*....|....*....|...
gi 442628919 2221 WISYDDVTTIRRKSQFIKSLQLGGGMIWALDLD 2253
Cdd:smart00636 302 WVSYDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
|
|
| Glyco_18 |
smart00636 |
Glyco_18 domain; |
966-1310 |
1.81e-116 |
|
Glyco_18 domain;
Pssm-ID: 214753 [Multi-domain] Cd Length: 334 Bit Score: 372.78 E-value: 1.81e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 966 KVICYFTNWAWYRKgigRFTPDDINTELCTHVIYGFAVLDYSELVLrTHDSWADVENNFYtrVTSLKSK--GIKVSLALG 1043
Cdd:smart00636 1 RVVGYFTNWGVYGR---NFPVDDIPASKLTHIIYAFANIDPDGTVT-IGDEWADIGNFGQ--LKALKKKnpGLKVLLSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1044 GWNDSqgDKYSRLVRSPMARSRFVRHALEFIEKYGFEGLDLDWEYPVCWqtecnkgsTEEKDGFTAWVQELSEAF----- 1118
Cdd:smart00636 75 GWTES--DNFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWEYPGGR--------GDDRENYTALLKELREALdkega 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1119 RPRGLMLSTAVSPSRKIIDAGYD-IPQLSRYFDWIAVMTYDFHGHWDKKTGHVAPLYHHPDDDfEYFNVNYSINYWMEKG 1197
Cdd:smart00636 145 EGKGYLLTIAVPAGPDKIDKGYGdLPAIAKYLDFINLMTYDFHGAWSNPTGHNAPLYAGPGDP-EKYNVDYAVKYYLCKG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1198 APSQKLVMGIPLYGQSFTLENTNSSGLNAKAPAPGEAGEFTRAAGFLAYYEICERVnrqGWQVVHDEfGRMGPYAYKGT- 1276
Cdd:smart00636 224 VPPSKLVLGIPFYGRGWTLVDGSNNGPGAPFTGPATGGPGTWEGGVVDYREICKLL---GATVVYDD-TAKAPYAYNPGt 299
|
330 340 350
....*....|....*....|....*....|....*
gi 442628919 1277 -QWVSYDSPDMVRKKSLLVRSLKLGGGMVWALDLD 1310
Cdd:smart00636 300 gQWVSYDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
|
|
| Glyco_hydro_18 |
pfam00704 |
Glycosyl hydrolases family 18; |
1410-1753 |
2.25e-105 |
|
Glycosyl hydrolases family 18;
Pssm-ID: 425828 [Multi-domain] Cd Length: 311 Bit Score: 340.20 E-value: 2.25e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1410 KIICYFTNWAWYRQGggkflpEDIDSDLCTHIIYGFAVLSRDNLTIQPHDSwadlDNKFYERIVAYRKK---GAKVTVAI 1486
Cdd:pfam00704 1 RIVGYYTSWGVYRNG------NFLPSDKLTHIIYAFANIDGSDGTLFIGDW----DLGNFEQLKKLKKQknpGVKVLLSI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1487 GGWNDSagDKYSRLVRNPEARSRFIRNVLDFIEEYNFDGLDLDWEYPvcwqvdckKGTAEEKIGFSALVRELFYAFQP-- 1564
Cdd:pfam00704 71 GGWTDS--TGFSLMASNPASRKKFADSIVSFLRKYGFDGIDIDWEYP--------GGNPEDKENYDLLLRELRAALDEak 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1565 --RGLILSAAVSPNKKVIDAGYEVAELSHYFSWISVMAYDYHGQWDKKTGHVAPMYshpeGTANFNANFSMNYWISMGAD 1642
Cdd:pfam00704 141 ggKKYLLSAAVPASYPDLDKGYDLPKIAKYLDFINVMTYDFHGSWDNVTGHHAPLY----GGGSYNVDYAVKYYLKQGVP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1643 RRKLVMGIPLYGQSFSLAETTKHqlnaptygggeageaTRARGFLAYYEICLKIRHHRWNVVRDTKGRiGPFAYHGDQWV 1722
Cdd:pfam00704 217 ASKLVLGVPFYGRSWTLVNGSGN---------------TWEDGVLAYKEICNLLKDNGATVVWDDVAK-APYVYDGDQFI 280
|
330 340 350
....*....|....*....|....*....|.
gi 442628919 1723 SFDDVPMIRHKSEYIKAMGLGGAMIWALDLD 1753
Cdd:pfam00704 281 TYDDPRSIATKVDYVKAKGLGGVMIWSLDAD 311
|
|
| Glyco_hydro_18 |
pfam00704 |
Glycosyl hydrolases family 18; |
1909-2253 |
2.15e-104 |
|
Glycosyl hydrolases family 18;
Pssm-ID: 425828 [Multi-domain] Cd Length: 311 Bit Score: 337.12 E-value: 2.15e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1909 KVVCYFTSWAWYRssQGKFvpedIDANLCTHLIYGFAVLDSKSLTIKTHDSwtdiDNRFYERVVEYKQR---GLRVMLAI 1985
Cdd:pfam00704 1 RIVGYYTSWGVYR--NGNF----LPSDKLTHIIYAFANIDGSDGTLFIGDW----DLGNFEQLKKLKKQknpGVKVLLSI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1986 GGWNDSlgSKYARLVLNSQSRRRFVASVISFLEQHGFEGLDLAWEFPVcwqvncnrGNPTEKDGFVALVKELSEAFKE-- 2063
Cdd:pfam00704 71 GGWTDS--TGFSLMASNPASRKKFADSIVSFLRKYGFDGIDIDWEYPG--------GNPEDKENYDLLLRELRAALDEak 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 2064 --NGLILSAAVSPSKMVIDAGYNVFELSPYFDWVAVMTYDFHGHWDMRTGQIAPLFhrggdENLYLNGNFSIHYWLERGI 2141
Cdd:pfam00704 141 ggKKYLLSAAVPASYPDLDKGYDLPKIAKYLDFINVMTYDFHGSWDNVTGHHAPLY-----GGGSYNVDYAVKYYLKQGV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 2142 PNDKLVMGMPMYGQTFTLAdqnrrslndktvgpgKAGTFTRADGFLAYYEICEKVVNDDWKVVRDEEGIfGSYAYSGNQW 2221
Cdd:pfam00704 216 PASKLVLGVPFYGRSWTLV---------------NGSGNTWEDGVLAYKEICNLLKDNGATVVWDDVAK-APYVYDGDQF 279
|
330 340 350
....*....|....*....|....*....|..
gi 442628919 2222 ISYDDVTTIRRKSQFIKSLQLGGGMIWALDLD 2253
Cdd:pfam00704 280 ITYDDPRSIATKVDYVKAKGLGGVMIWSLDAD 311
|
|
| Glyco_hydro_18 |
pfam00704 |
Glycosyl hydrolases family 18; |
966-1310 |
9.98e-100 |
|
Glycosyl hydrolases family 18;
Pssm-ID: 425828 [Multi-domain] Cd Length: 311 Bit Score: 323.64 E-value: 9.98e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 966 KVICYFTNWAWYRKGigrftpDDINTELCTHVIYGFAVLDYSELVLRTHDsWADVENNFYTRVTSLKSKGIKVSLALGGW 1045
Cdd:pfam00704 1 RIVGYYTSWGVYRNG------NFLPSDKLTHIIYAFANIDGSDGTLFIGD-WDLGNFEQLKKLKKQKNPGVKVLLSIGGW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1046 NDSqgDKYSRLVRSPMARSRFVRHALEFIEKYGFEGLDLDWEYPvcwqtecnKGSTEEKDGFTAWVQELSEAFRP----R 1121
Cdd:pfam00704 74 TDS--TGFSLMASNPASRKKFADSIVSFLRKYGFDGIDIDWEYP--------GGNPEDKENYDLLLRELRAALDEakggK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1122 GLMLSTAVSPSRKIIDAGYDIPQLSRYFDWIAVMTYDFHGHWDKKTGHVAPLYhhpddDFEYFNVNYSINYWMEKGAPSQ 1201
Cdd:pfam00704 144 KYLLSAAVPASYPDLDKGYDLPKIAKYLDFINVMTYDFHGSWDNVTGHHAPLY-----GGGSYNVDYAVKYYLKQGVPAS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1202 KLVMGIPLYGQSFTLentnssglnakapapGEAGEFTRAAGFLAYYEICERVNRQGWQVVHDEFGRmGPYAYKGTQWVSY 1281
Cdd:pfam00704 219 KLVLGVPFYGRSWTL---------------VNGSGNTWEDGVLAYKEICNLLKDNGATVVWDDVAK-APYVYDGDQFITY 282
|
330 340
....*....|....*....|....*....
gi 442628919 1282 DSPDMVRKKSLLVRSLKLGGGMVWALDLD 1310
Cdd:pfam00704 283 DDPRSIATKVDYVKAKGLGGVMIWSLDAD 311
|
|
| Glyco_18 |
smart00636 |
Glyco_18 domain; |
220-565 |
6.49e-98 |
|
Glyco_18 domain;
Pssm-ID: 214753 [Multi-domain] Cd Length: 334 Bit Score: 319.62 E-value: 6.49e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 220 KVLCYMSNWAFYRSGeahFVPEQIDPNLCSAIIYSFASLDPDHlTIREFDSWVDLDNQYYrrVTSL-----GVPVLIALG 294
Cdd:smart00636 1 RVVGYFTNWGVYGRN---FPVDDIPASKLTHIIYAFANIDPDG-TVTIGDEWADIGNFGQ--LKALkkknpGLKVLLSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 295 GWTDSSgsKYSRLVSDNLKRRVFISSVSSFLLRHGFSGLHLDWNYPKCWQsdcsrgpvTDRPNLTKLLRELRTEFQSVD- 373
Cdd:smart00636 75 GWTESD--NFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWEYPGGRG--------DDRENYTALLKELREALDKEGa 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 374 --PKFQLGVAISGYKEIIKEAYDF-PALSDIVDYMTVMTYDYHGAWEQKTGHVSPLYGLSSDTyPQYNTNYTMQLLLKMG 450
Cdd:smart00636 145 egKGYLLTIAVPAGPDKIDKGYGDlPAIAKYLDFINLMTYDFHGAWSNPTGHNAPLYAGPGDP-EKYNVDYAVKYYLCKG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 451 ARREKLVLSIPFYGQSFTLATahQILAGPGVAASGPGDAGELTKQPGMLAYYEICQRL-TKFNWIsdrnlNVIFGPFAML 529
Cdd:smart00636 224 VPPSKLVLGIPFYGRGWTLVD--GSNNGPGAPFTGPATGGPGTWEGGVVDYREICKLLgATVVYD-----DTAKAPYAYN 296
|
330 340 350
....*....|....*....|....*....|....*...
gi 442628919 530 --NDQWVGYEDPTSAQAKARYAANNNFAGVAAWTIDLD 565
Cdd:smart00636 297 pgTGQWVSYDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
|
|
| ChiA |
COG3325 |
Chitinase, GH18 family [Carbohydrate transport and metabolism]; |
965-1331 |
9.40e-87 |
|
Chitinase, GH18 family [Carbohydrate transport and metabolism];
Pssm-ID: 442554 [Multi-domain] Cd Length: 391 Bit Score: 289.89 E-value: 9.40e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 965 YKVICYFTNWAWYRKGigrFTPDDINTELCTHVIYGFAVLDySELVLRTHDSWA--------DVENNFYTRV----TSLK 1032
Cdd:COG3325 19 KRVVGYFTQWGIYGRN---YLVKDIPASKLTHINYAFANVD-PDGKCSVGDAWAkpsvdgaaDDWDQPLKGNfnqlKKLK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1033 SK--GIKVSLALGGWNDSQGdkYSRLVRSPMARSRFVRHALEFIEKYGFEGLDLDWEYPVCWQTECNKGSTEEKDGFTAW 1110
Cdd:COG3325 95 AKnpNLKVLISIGGWTWSKG--FSDAAATPASRAAFVDSCVDLLRKYNFDGIDIDWEYPGSGGAPGNVYRPEDKANFTAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1111 VQELSEAF------RPRGLMLSTAVSPSRKIIDaGYDIPQLSRYFDWIAVMTYDFHGHWDKKTGHVAPLYHHPDD-DFEY 1183
Cdd:COG3325 173 LKELRAQLdalgaeTGKHYLLTAAAPAGPDKLD-GIELPKVAQYLDYVNVMTYDFHGAWSPTTGHQAPLYDSPKDpEAQG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1184 FNVNYSINYWMEKGAPSQKLVMGIPLYGQSFTLENTNSSGLN--AKAPAPGeagefTRAAGFLAYYEICER-VNRQGWQV 1260
Cdd:COG3325 252 YSVDSAVQAYLAAGVPASKLVLGVPFYGRGWTGVTGGNNGLYqpATGPAPG-----TWEAGVNDYKDLKALyLGSNGYTR 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442628919 1261 VHDEFGRMgPYAYKGT--QWVSYDSPDMVRKKSLLVRSLKLGGGMVWALDLDDFKNRcgngvhpLLTEIHNVL 1331
Cdd:COG3325 327 YWDDVAKA-PYLYNGDtgTFISYDDPRSIAAKADYVKDKGLGGVMFWELSGDTADGT-------LLNAIGEGL 391
|
|
| ChiA |
COG3325 |
Chitinase, GH18 family [Carbohydrate transport and metabolism]; |
1905-2274 |
8.96e-85 |
|
Chitinase, GH18 family [Carbohydrate transport and metabolism];
Pssm-ID: 442554 [Multi-domain] Cd Length: 391 Bit Score: 284.11 E-value: 8.96e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1905 NNSYKVVCYFTSWAWYrssQGKFVPEDIDANLCTHLIYGFAVLDS-----------KSLTIKTHDSWTDIDNRFYERVVE 1973
Cdd:COG3325 16 TSGKRVVGYFTQWGIY---GRNYLVKDIPASKLTHINYAFANVDPdgkcsvgdawaKPSVDGAADDWDQPLKGNFNQLKK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1974 YKQR--GLRVMLAIGGWNDSLGskYARLVLNSQSRRRFVASVISFLEQHGFEGLDLAWEFPVCWQVNCNRGNPTEKDGFV 2051
Cdd:COG3325 93 LKAKnpNLKVLISIGGWTWSKG--FSDAAATPASRAAFVDSCVDLLRKYNFDGIDIDWEYPGSGGAPGNVYRPEDKANFT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 2052 ALVKELSEAFKENG------LILSAAV--SPSKMvidAGYNVFELSPYFDWVAVMTYDFHGHWDMRTGQIAPLFHRGGD- 2122
Cdd:COG3325 171 ALLKELRAQLDALGaetgkhYLLTAAApaGPDKL---DGIELPKVAQYLDYVNVMTYDFHGAWSPTTGHQAPLYDSPKDp 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 2123 ENLYLNGNFSIHYWLERGIPNDKLVMGMPMYGQTFTLADQNRRSLNDKTVGPGKAgtfTRADGFLAYYEICEKVVN-DDW 2201
Cdd:COG3325 248 EAQGYSVDSAVQAYLAAGVPASKLVLGVPFYGRGWTGVTGGNNGLYQPATGPAPG---TWEAGVNDYKDLKALYLGsNGY 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442628919 2202 KVVRDEEGIFgSYAYSGN--QWISYDDVTTIRRKSQFIKSLQLGGGMIWALDLDDFRGLcgcgkhpLLRTLSQEL 2274
Cdd:COG3325 325 TRYWDDVAKA-PYLYNGDtgTFISYDDPRSIAAKADYVKDKGLGGVMFWELSGDTADGT-------LLNAIGEGL 391
|
|
| Glyco_hydro_18 |
pfam00704 |
Glycosyl hydrolases family 18; |
220-565 |
1.66e-83 |
|
Glycosyl hydrolases family 18;
Pssm-ID: 425828 [Multi-domain] Cd Length: 311 Bit Score: 277.03 E-value: 1.66e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 220 KVLCYMSNWAFYRSGEAhfvpeqIDPNLCSAIIYSFASLDPDHLTIREFDSwvdlDNQYYRRVTSL------GVPVLIAL 293
Cdd:pfam00704 1 RIVGYYTSWGVYRNGNF------LPSDKLTHIIYAFANIDGSDGTLFIGDW----DLGNFEQLKKLkkqknpGVKVLLSI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 294 GGWTDSSGskYSRLVSDNLKRRVFISSVSSFLLRHGFSGLHLDWNYPKCWqsdcsrgpVTDRPNLTKLLRELRTEF--QS 371
Cdd:pfam00704 71 GGWTDSTG--FSLMASNPASRKKFADSIVSFLRKYGFDGIDIDWEYPGGN--------PEDKENYDLLLRELRAALdeAK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 372 VDPKFQLGVAISGYKEIIKEAYDFPALSDIVDYMTVMTYDYHGAWEQKTGHVSPLYGlssdtYPQYNTNYTMQLLLKMGA 451
Cdd:pfam00704 141 GGKKYLLSAAVPASYPDLDKGYDLPKIAKYLDFINVMTYDFHGSWDNVTGHHAPLYG-----GGSYNVDYAVKYYLKQGV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 452 RREKLVLSIPFYGQSFTLAtahqilagpgvaasgpgDAGELTKQPGMLAYYEICQRLTKFNWISDRNlNVIFGPFAMLND 531
Cdd:pfam00704 216 PASKLVLGVPFYGRSWTLV-----------------NGSGNTWEDGVLAYKEICNLLKDNGATVVWD-DVAKAPYVYDGD 277
|
330 340 350
....*....|....*....|....*....|....
gi 442628919 532 QWVGYEDPTSAQAKARYAANNNFAGVAAWTIDLD 565
Cdd:pfam00704 278 QFITYDDPRSIATKVDYVKAKGLGGVMIWSLDAD 311
|
|
| ChiA |
COG3325 |
Chitinase, GH18 family [Carbohydrate transport and metabolism]; |
1401-1774 |
4.29e-82 |
|
Chitinase, GH18 family [Carbohydrate transport and metabolism];
Pssm-ID: 442554 [Multi-domain] Cd Length: 391 Bit Score: 276.41 E-value: 4.29e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1401 EATEMATEFKIICYFTNWAWYrqgGGKFLPEDIDSDLCTHIIYGFAVLSRDNlTIQPHDSWA------------DLDNKF 1468
Cdd:COG3325 11 AAATATSGKRVVGYFTQWGIY---GRNYLVKDIPASKLTHINYAFANVDPDG-KCSVGDAWAkpsvdgaaddwdQPLKGN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1469 YERIVAYRKK--GAKVTVAIGGWNDSAGdkYSRLVRNPEARSRFIRNVLDFIEEYNFDGLDLDWEYPVCWQVDCKKGTAE 1546
Cdd:COG3325 87 FNQLKKLKAKnpNLKVLISIGGWTWSKG--FSDAAATPASRAAFVDSCVDLLRKYNFDGIDIDWEYPGSGGAPGNVYRPE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1547 EKIGFSALVREL------FYAFQPRGLILSAAVSPNKKVIDaGYEVAELSHYFSWISVMAYDYHGQWDKKTGHVAPMYSH 1620
Cdd:COG3325 165 DKANFTALLKELraqldaLGAETGKHYLLTAAAPAGPDKLD-GIELPKVAQYLDYVNVMTYDFHGAWSPTTGHQAPLYDS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1621 P--EGTANFNANFSMNYWISMGADRRKLVMGIPLYGQSFSLAETTKHQLNAPTYGggeAGEATRARGFLAYYEICLK-IR 1697
Cdd:COG3325 244 PkdPEAQGYSVDSAVQAYLAAGVPASKLVLGVPFYGRGWTGVTGGNNGLYQPATG---PAPGTWEAGVNDYKDLKALyLG 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442628919 1698 HHRWNVVRDTKGRiGPFAYHGD--QWVSFDDVPMIRHKSEYIKAMGLGGAMIWALDLDDFKNVcecesypLLKAINRVL 1774
Cdd:COG3325 321 SNGYTRYWDDVAK-APYLYNGDtgTFISYDDPRSIAAKADYVKDKGLGGVMFWELSGDTADGT-------LLNAIGEGL 391
|
|
| ChiA |
COG3325 |
Chitinase, GH18 family [Carbohydrate transport and metabolism]; |
219-586 |
3.35e-63 |
|
Chitinase, GH18 family [Carbohydrate transport and metabolism];
Pssm-ID: 442554 [Multi-domain] Cd Length: 391 Bit Score: 221.71 E-value: 3.35e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 219 KKVLCYMSNWAFYRSGeahFVPEQIDPNLCSAIIYSFASLDPDhLTIREFDSW--------VDLDNQYYRRV----TSL- 285
Cdd:COG3325 19 KRVVGYFTQWGIYGRN---YLVKDIPASKLTHINYAFANVDPD-GKCSVGDAWakpsvdgaADDWDQPLKGNfnqlKKLk 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 286 ----GVPVLIALGGWTDSSGskYSRLVSDNLKRRVFISSVSSFLLRHGFSGLHLDWNYPKCWQSDCSRGPVTDRPNLTKL 361
Cdd:COG3325 95 aknpNLKVLISIGGWTWSKG--FSDAAATPASRAAFVDSCVDLLRKYNFDGIDIDWEYPGSGGAPGNVYRPEDKANFTAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 362 LRELRTEF----QSVDPKFQLGVAISGYKEIIkEAYDFPALSDIVDYMTVMTYDYHGAWEQKTGHVSPLYGLSSD-TYPQ 436
Cdd:COG3325 173 LKELRAQLdalgAETGKHYLLTAAAPAGPDKL-DGIELPKVAQYLDYVNVMTYDFHGAWSPTTGHQAPLYDSPKDpEAQG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 437 YNTNYTMQLLLKMGARREKLVLSIPFYGQSFTLATAHQilAGPGVAASGPGDAgelTKQPGMLAYYEICQRL-------- 508
Cdd:COG3325 252 YSVDSAVQAYLAAGVPASKLVLGVPFYGRGWTGVTGGN--NGLYQPATGPAPG---TWEAGVNDYKDLKALYlgsngytr 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 509 -----TKFNWISDRNlnvifgpfamlNDQWVGYEDPTSAQAKARYAANNNFAGVAAWTIDLDDFRNLccnesypLLRAIN 583
Cdd:COG3325 327 ywddvAKAPYLYNGD-----------TGTFISYDDPRSIAAKADYVKDKGLGGVMFWELSGDTADGT-------LLNAIG 388
|
...
gi 442628919 584 RAL 586
Cdd:COG3325 389 EGL 391
|
|
| CBM_14 |
pfam01607 |
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ... |
875-918 |
5.41e-11 |
|
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: 5.41e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 442628919 875 VPYPGNCSKYLFCLWNRLQASDCPPGLHYNERIGNCDWPA-AAKC 918
Cdd:pfam01607 9 YADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDnVVDC 53
|
|
| ChtBD2 |
smart00494 |
Chitin-binding domain type 2; |
874-913 |
8.92e-10 |
|
Chitin-binding domain type 2;
Pssm-ID: 214696 [Multi-domain] Cd Length: 49 Bit Score: 55.91 E-value: 8.92e-10
10 20 30 40
....*....|....*....|....*....|....*....|
gi 442628919 874 RVPYPGNCSKYLFCLWNRLQASDCPPGLHYNERIGNCDWP 913
Cdd:smart00494 10 LYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDWP 49
|
|
| CBM_14 |
pfam01607 |
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ... |
801-848 |
9.41e-10 |
|
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: 56.27 E-value: 9.41e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 442628919 801 TEGDYYPHRNCRKYYICVNKALVPSECGGDLHWDGIKKLCDWPEN-VQC 848
Cdd:pfam01607 5 EDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNvVDC 53
|
|
| ChtBD2 |
smart00494 |
Chitin-binding domain type 2; |
697-737 |
7.53e-09 |
|
Chitin-binding domain type 2;
Pssm-ID: 214696 [Multi-domain] Cd Length: 49 Bit Score: 53.60 E-value: 7.53e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 442628919 697 FFADSNNCNAYYHCFfAGELQQQFCPSGLHWNNEAKGCDWP 737
Cdd:smart00494 10 LYPHPTDCSKYYQCS-NGRPIVGSCPAGLVFNPATQTCDWP 49
|
|
| ChtBD2 |
smart00494 |
Chitin-binding domain type 2; |
1834-1871 |
7.83e-09 |
|
Chitin-binding domain type 2;
Pssm-ID: 214696 [Multi-domain] Cd Length: 49 Bit Score: 53.22 E-value: 7.83e-09
10 20 30 40
....*....|....*....|....*....|....*....|
gi 442628919 1834 YLAHEWDCTKYYICEHGTYVERSCPLGLQWNKT--YCDWP 1871
Cdd:smart00494 10 LYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPAtqTCDWP 49
|
|
| CBM_14 |
pfam01607 |
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ... |
697-742 |
1.20e-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: 52.80 E-value: 1.20e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 442628919 697 FFADSNNCNAYYHCFFaGELQQQFCPSGLHWNNEAKGCDWPSS-AQC 742
Cdd:pfam01607 8 YYADPGDCSKYYVCSN-GEAVEFTCPNGLVFDPTLGICDYPDNvVDC 53
|
|
| CBM_14 |
pfam01607 |
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ... |
1834-1874 |
4.04e-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: 51.65 E-value: 4.04e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 442628919 1834 YLAHEWDCTKYYICEHGTYVERSCPLGLQWNKT--YCDWPTNV 1874
Cdd:pfam01607 8 YYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTlgICDYPDNV 50
|
|
| ChtBD2 |
smart00494 |
Chitin-binding domain type 2; |
799-843 |
6.25e-08 |
|
Chitin-binding domain type 2;
Pssm-ID: 214696 [Multi-domain] Cd Length: 49 Bit Score: 50.91 E-value: 6.25e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 442628919 799 ECTEGD--YYPH-RNCRKYYICVNKALVPSECGGDLHWDGIKKLCDWP 843
Cdd:smart00494 2 ECPGRGdgLYPHpTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDWP 49
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GH18_chitolectin_chitotriosidase |
cd02872 |
This conserved domain family includes a large number of catalytically inactive chitinase-like ... |
221-586 |
1.38e-174 |
|
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: 537.91 E-value: 1.38e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 221 VLCYMSNWAFYRSGEAHFVPEQIDPNLCSAIIYSFASLDPDhLTIREFDSWVDLDNQYYRRVTSL-----GVPVLIALGG 295
Cdd:cd02872 1 VVCYFTNWAQYRPGNGKFVPENIDPFLCTHIIYAFAGLNPD-GNIIILDEWNDIDLGLYERFNALkeknpNLKTLLAIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 296 WTDSSGsKYSRLVSDNLKRRVFISSVSSFLLRHGFSGLHLDWNYPKCWQsdcsrGPVTDRPNLTKLLRELRTEFQSVDPK 375
Cdd:cd02872 80 WNFGSA-KFSAMAASPENRKTFIKSAIAFLRKYGFDGLDLDWEYPGQRG-----GPPEDKENFVTLLKELREAFEPEAPR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 376 FQLGVAISGYKEIIKEAYDFPALSDIVDYMTVMTYDYHGAWEQKTGHVSPLYGLSSDT--YPQYNTNYTMQLLLKMGARR 453
Cdd:cd02872 154 LLLTAAVSAGKETIDAAYDIPEISKYLDFINVMTYDFHGSWEGVTGHNSPLYAGSADTgdQKYLNVDYAIKYWLSKGAPP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 454 EKLVLSIPFYGQSFTLATAHQilAGPGVAASGPGDAGELTKQPGMLAYYEICQRLTKfNWISDRNLNViFGPFAMLNDQW 533
Cdd:cd02872 234 EKLVLGIPTYGRSFTLASPSN--TGVGAPASGPGTAGPYTREAGFLAYYEICEFLKS-GWTVVWDDEQ-KVPYAYKGNQW 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 442628919 534 VGYEDPTSAQAKARYAANNNFAGVAAWTIDLDDFRNLCCNESYPLLRAINRAL 586
Cdd:cd02872 310 VGYDDEESIALKVQYLKSKGLGGAMVWSIDLDDFRGTCGQGKYPLLNAINRAL 362
|
|
| GH18_chitolectin_chitotriosidase |
cd02872 |
This conserved domain family includes a large number of catalytically inactive chitinase-like ... |
967-1331 |
3.52e-166 |
|
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: 514.80 E-value: 3.52e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 967 VICYFTNWAWYRKGIGRFTPDDINTELCTHVIYGFAVLDySELVLRTHDSWADVENNFYTRVTSLKSK--GIKVSLALGG 1044
Cdd:cd02872 1 VVCYFTNWAQYRPGNGKFVPENIDPFLCTHIIYAFAGLN-PDGNIIILDEWNDIDLGLYERFNALKEKnpNLKTLLAIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1045 WNDSQGdKYSRLVRSPMARSRFVRHALEFIEKYGFEGLDLDWEYPVCWQtecnkGSTEEKDGFTAWVQELSEAFRP--RG 1122
Cdd:cd02872 80 WNFGSA-KFSAMAASPENRKTFIKSAIAFLRKYGFDGLDLDWEYPGQRG-----GPPEDKENFVTLLKELREAFEPeaPR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1123 LMLSTAVSPSRKIIDAGYDIPQLSRYFDWIAVMTYDFHGHWDKKTGHVAPLYHHPDD--DFEYFNVNYSINYWMEKGAPS 1200
Cdd:cd02872 154 LLLTAAVSAGKETIDAAYDIPEISKYLDFINVMTYDFHGSWEGVTGHNSPLYAGSADtgDQKYLNVDYAIKYWLSKGAPP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1201 QKLVMGIPLYGQSFTLENTNSSGLNAKAPAPGEAGEFTRAAGFLAYYEICERVNrQGWQVVHDEfGRMGPYAYKGTQWVS 1280
Cdd:cd02872 234 EKLVLGIPTYGRSFTLASPSNTGVGAPASGPGTAGPYTREAGFLAYYEICEFLK-SGWTVVWDD-EQKVPYAYKGNQWVG 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 442628919 1281 YDSPDMVRKKSLLVRSLKLGGGMVWALDLDDFKNRCGNGVHPLLTEIHNVL 1331
Cdd:cd02872 312 YDDEESIALKVQYLKSKGLGGAMVWSIDLDDFRGTCGQGKYPLLNAINRAL 362
|
|
| GH18_chitolectin_chitotriosidase |
cd02872 |
This conserved domain family includes a large number of catalytically inactive chitinase-like ... |
1411-1774 |
1.29e-164 |
|
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: 510.56 E-value: 1.29e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1411 IICYFTNWAWYRQGGGKFLPEDIDSDLCTHIIYGFAVLSrDNLTIQPHDSWADLDNKFYERIVAYRKKGA--KVTVAIGG 1488
Cdd:cd02872 1 VVCYFTNWAQYRPGNGKFVPENIDPFLCTHIIYAFAGLN-PDGNIIILDEWNDIDLGLYERFNALKEKNPnlKTLLAIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1489 WNDSAGdKYSRLVRNPEARSRFIRNVLDFIEEYNFDGLDLDWEYPVCWQvdckkGTAEEKIGFSALVRELFYAFQP--RG 1566
Cdd:cd02872 80 WNFGSA-KFSAMAASPENRKTFIKSAIAFLRKYGFDGLDLDWEYPGQRG-----GPPEDKENFVTLLKELREAFEPeaPR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1567 LILSAAVSPNKKVIDAGYEVAELSHYFSWISVMAYDYHGQWDKKTGHVAPMYSHPEGT---ANFNANFSMNYWISMGADR 1643
Cdd:cd02872 154 LLLTAAVSAGKETIDAAYDIPEISKYLDFINVMTYDFHGSWEGVTGHNSPLYAGSADTgdqKYLNVDYAIKYWLSKGAPP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1644 RKLVMGIPLYGQSFSLAETTKHQLNAPTYGGGEAGEATRARGFLAYYEICLKIRhHRWNVVRDTKGRiGPFAYHGDQWVS 1723
Cdd:cd02872 234 EKLVLGIPTYGRSFTLASPSNTGVGAPASGPGTAGPYTREAGFLAYYEICEFLK-SGWTVVWDDEQK-VPYAYKGNQWVG 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 442628919 1724 FDDVPMIRHKSEYIKAMGLGGAMIWALDLDDFKNVCECESYPLLKAINRVL 1774
Cdd:cd02872 312 YDDEESIALKVQYLKSKGLGGAMVWSIDLDDFRGTCGQGKYPLLNAINRAL 362
|
|
| GH18_chitolectin_chitotriosidase |
cd02872 |
This conserved domain family includes a large number of catalytically inactive chitinase-like ... |
1910-2274 |
2.73e-164 |
|
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: 509.41 E-value: 2.73e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1910 VVCYFTSWAWYRSSQGKFVPEDIDANLCTHLIYGFAVLDSKsLTIKTHDSWTDIDNRFYERVVEYKQR--GLRVMLAIGG 1987
Cdd:cd02872 1 VVCYFTNWAQYRPGNGKFVPENIDPFLCTHIIYAFAGLNPD-GNIIILDEWNDIDLGLYERFNALKEKnpNLKTLLAIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1988 WNDslGS-KYARLVLNSQSRRRFVASVISFLEQHGFEGLDLAWEFPVCWQvncnrGNPTEKDGFVALVKELSEAFKEN-- 2064
Cdd:cd02872 80 WNF--GSaKFSAMAASPENRKTFIKSAIAFLRKYGFDGLDLDWEYPGQRG-----GPPEDKENFVTLLKELREAFEPEap 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 2065 GLILSAAVSPSKMVIDAGYNVFELSPYFDWVAVMTYDFHGHWDMRTGQIAPLFHRGGD--ENLYLNGNFSIHYWLERGIP 2142
Cdd:cd02872 153 RLLLTAAVSAGKETIDAAYDIPEISKYLDFINVMTYDFHGSWEGVTGHNSPLYAGSADtgDQKYLNVDYAIKYWLSKGAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 2143 NDKLVMGMPMYGQTFTLADQNRRSLNDKTVGPGKAGTFTRADGFLAYYEICEKvVNDDWKVVRDEEGiFGSYAYSGNQWI 2222
Cdd:cd02872 233 PEKLVLGIPTYGRSFTLASPSNTGVGAPASGPGTAGPYTREAGFLAYYEICEF-LKSGWTVVWDDEQ-KVPYAYKGNQWV 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 442628919 2223 SYDDVTTIRRKSQFIKSLQLGGGMIWALDLDDFRGLCGCGKHPLLRTLSQEL 2274
Cdd:cd02872 311 GYDDEESIALKVQYLKSKGLGGAMVWSIDLDDFRGTCGQGKYPLLNAINRAL 362
|
|
| Glyco_18 |
smart00636 |
Glyco_18 domain; |
1410-1753 |
2.58e-122 |
|
Glyco_18 domain;
Pssm-ID: 214753 [Multi-domain] Cd Length: 334 Bit Score: 389.73 E-value: 2.58e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1410 KIICYFTNWAWYrqgGGKFLPEDIDSDLCTHIIYGFAVLSRDNlTIQPHDSWADLDNKFYERIVAYRKKGAKVTVAIGGW 1489
Cdd:smart00636 1 RVVGYFTNWGVY---GRNFPVDDIPASKLTHIIYAFANIDPDG-TVTIGDEWADIGNFGQLKALKKKNPGLKVLLSIGGW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1490 NDSagDKYSRLVRNPEARSRFIRNVLDFIEEYNFDGLDLDWEYPVCWQVDckkgtaeeKIGFSALVRELFYAFQ-----P 1564
Cdd:smart00636 77 TES--DNFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWEYPGGRGDD--------RENYTALLKELREALDkegaeG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1565 RGLILSAAVSPNKKVIDAGYE-VAELSHYFSWISVMAYDYHGQWDKKTGHVAPMYSHPEGTANFNANFSMNYWISMGADR 1643
Cdd:smart00636 147 KGYLLTIAVPAGPDKIDKGYGdLPAIAKYLDFINLMTYDFHGAWSNPTGHNAPLYAGPGDPEKYNVDYAVKYYLCKGVPP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1644 RKLVMGIPLYGQSFSLAETTKHQLNAPTYGGGEAGEATRARGFLAYYEICLKIrhhRWNVVRDTKGRiGPFAYHGD--QW 1721
Cdd:smart00636 227 SKLVLGIPFYGRGWTLVDGSNNGPGAPFTGPATGGPGTWEGGVVDYREICKLL---GATVVYDDTAK-APYAYNPGtgQW 302
|
330 340 350
....*....|....*....|....*....|..
gi 442628919 1722 VSFDDVPMIRHKSEYIKAMGLGGAMIWALDLD 1753
Cdd:smart00636 303 VSYDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
|
|
| Glyco_18 |
smart00636 |
Glyco_18 domain; |
1909-2253 |
3.96e-119 |
|
Glyco_18 domain;
Pssm-ID: 214753 [Multi-domain] Cd Length: 334 Bit Score: 380.49 E-value: 3.96e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1909 KVVCYFTSWAWYRSsqgKFVPEDIDANLCTHLIYGFAVLDSkSLTIKTHDSWTDIDNRFYERVVEYKQRGLRVMLAIGGW 1988
Cdd:smart00636 1 RVVGYFTNWGVYGR---NFPVDDIPASKLTHIIYAFANIDP-DGTVTIGDEWADIGNFGQLKALKKKNPGLKVLLSIGGW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1989 NDSlgSKYARLVLNSQSRRRFVASVISFLEQHGFEGLDLAWEFPVCWqvncnrgnPTEKDGFVALVKELSEAFKE----- 2063
Cdd:smart00636 77 TES--DNFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWEYPGGR--------GDDRENYTALLKELREALDKegaeg 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 2064 NGLILSAAVSPSKMVIDAGYN-VFELSPYFDWVAVMTYDFHGHWDMRTGQIAPLFHRGGDENlYLNGNFSIHYWLERGIP 2142
Cdd:smart00636 147 KGYLLTIAVPAGPDKIDKGYGdLPAIAKYLDFINLMTYDFHGAWSNPTGHNAPLYAGPGDPE-KYNVDYAVKYYLCKGVP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 2143 NDKLVMGMPMYGQTFTLADQNRRSLNDKTVGPGKAGTFTRADGFLAYYEICEKVvndDWKVVRDEEGiFGSYAYSGN--Q 2220
Cdd:smart00636 226 PSKLVLGIPFYGRGWTLVDGSNNGPGAPFTGPATGGPGTWEGGVVDYREICKLL---GATVVYDDTA-KAPYAYNPGtgQ 301
|
330 340 350
....*....|....*....|....*....|...
gi 442628919 2221 WISYDDVTTIRRKSQFIKSLQLGGGMIWALDLD 2253
Cdd:smart00636 302 WVSYDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
|
|
| Glyco_18 |
smart00636 |
Glyco_18 domain; |
966-1310 |
1.81e-116 |
|
Glyco_18 domain;
Pssm-ID: 214753 [Multi-domain] Cd Length: 334 Bit Score: 372.78 E-value: 1.81e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 966 KVICYFTNWAWYRKgigRFTPDDINTELCTHVIYGFAVLDYSELVLrTHDSWADVENNFYtrVTSLKSK--GIKVSLALG 1043
Cdd:smart00636 1 RVVGYFTNWGVYGR---NFPVDDIPASKLTHIIYAFANIDPDGTVT-IGDEWADIGNFGQ--LKALKKKnpGLKVLLSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1044 GWNDSqgDKYSRLVRSPMARSRFVRHALEFIEKYGFEGLDLDWEYPVCWqtecnkgsTEEKDGFTAWVQELSEAF----- 1118
Cdd:smart00636 75 GWTES--DNFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWEYPGGR--------GDDRENYTALLKELREALdkega 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1119 RPRGLMLSTAVSPSRKIIDAGYD-IPQLSRYFDWIAVMTYDFHGHWDKKTGHVAPLYHHPDDDfEYFNVNYSINYWMEKG 1197
Cdd:smart00636 145 EGKGYLLTIAVPAGPDKIDKGYGdLPAIAKYLDFINLMTYDFHGAWSNPTGHNAPLYAGPGDP-EKYNVDYAVKYYLCKG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1198 APSQKLVMGIPLYGQSFTLENTNSSGLNAKAPAPGEAGEFTRAAGFLAYYEICERVnrqGWQVVHDEfGRMGPYAYKGT- 1276
Cdd:smart00636 224 VPPSKLVLGIPFYGRGWTLVDGSNNGPGAPFTGPATGGPGTWEGGVVDYREICKLL---GATVVYDD-TAKAPYAYNPGt 299
|
330 340 350
....*....|....*....|....*....|....*
gi 442628919 1277 -QWVSYDSPDMVRKKSLLVRSLKLGGGMVWALDLD 1310
Cdd:smart00636 300 gQWVSYDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
|
|
| Glyco_hydro_18 |
pfam00704 |
Glycosyl hydrolases family 18; |
1410-1753 |
2.25e-105 |
|
Glycosyl hydrolases family 18;
Pssm-ID: 425828 [Multi-domain] Cd Length: 311 Bit Score: 340.20 E-value: 2.25e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1410 KIICYFTNWAWYRQGggkflpEDIDSDLCTHIIYGFAVLSRDNLTIQPHDSwadlDNKFYERIVAYRKK---GAKVTVAI 1486
Cdd:pfam00704 1 RIVGYYTSWGVYRNG------NFLPSDKLTHIIYAFANIDGSDGTLFIGDW----DLGNFEQLKKLKKQknpGVKVLLSI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1487 GGWNDSagDKYSRLVRNPEARSRFIRNVLDFIEEYNFDGLDLDWEYPvcwqvdckKGTAEEKIGFSALVRELFYAFQP-- 1564
Cdd:pfam00704 71 GGWTDS--TGFSLMASNPASRKKFADSIVSFLRKYGFDGIDIDWEYP--------GGNPEDKENYDLLLRELRAALDEak 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1565 --RGLILSAAVSPNKKVIDAGYEVAELSHYFSWISVMAYDYHGQWDKKTGHVAPMYshpeGTANFNANFSMNYWISMGAD 1642
Cdd:pfam00704 141 ggKKYLLSAAVPASYPDLDKGYDLPKIAKYLDFINVMTYDFHGSWDNVTGHHAPLY----GGGSYNVDYAVKYYLKQGVP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1643 RRKLVMGIPLYGQSFSLAETTKHqlnaptygggeageaTRARGFLAYYEICLKIRHHRWNVVRDTKGRiGPFAYHGDQWV 1722
Cdd:pfam00704 217 ASKLVLGVPFYGRSWTLVNGSGN---------------TWEDGVLAYKEICNLLKDNGATVVWDDVAK-APYVYDGDQFI 280
|
330 340 350
....*....|....*....|....*....|.
gi 442628919 1723 SFDDVPMIRHKSEYIKAMGLGGAMIWALDLD 1753
Cdd:pfam00704 281 TYDDPRSIATKVDYVKAKGLGGVMIWSLDAD 311
|
|
| Glyco_hydro_18 |
pfam00704 |
Glycosyl hydrolases family 18; |
1909-2253 |
2.15e-104 |
|
Glycosyl hydrolases family 18;
Pssm-ID: 425828 [Multi-domain] Cd Length: 311 Bit Score: 337.12 E-value: 2.15e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1909 KVVCYFTSWAWYRssQGKFvpedIDANLCTHLIYGFAVLDSKSLTIKTHDSwtdiDNRFYERVVEYKQR---GLRVMLAI 1985
Cdd:pfam00704 1 RIVGYYTSWGVYR--NGNF----LPSDKLTHIIYAFANIDGSDGTLFIGDW----DLGNFEQLKKLKKQknpGVKVLLSI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1986 GGWNDSlgSKYARLVLNSQSRRRFVASVISFLEQHGFEGLDLAWEFPVcwqvncnrGNPTEKDGFVALVKELSEAFKE-- 2063
Cdd:pfam00704 71 GGWTDS--TGFSLMASNPASRKKFADSIVSFLRKYGFDGIDIDWEYPG--------GNPEDKENYDLLLRELRAALDEak 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 2064 --NGLILSAAVSPSKMVIDAGYNVFELSPYFDWVAVMTYDFHGHWDMRTGQIAPLFhrggdENLYLNGNFSIHYWLERGI 2141
Cdd:pfam00704 141 ggKKYLLSAAVPASYPDLDKGYDLPKIAKYLDFINVMTYDFHGSWDNVTGHHAPLY-----GGGSYNVDYAVKYYLKQGV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 2142 PNDKLVMGMPMYGQTFTLAdqnrrslndktvgpgKAGTFTRADGFLAYYEICEKVVNDDWKVVRDEEGIfGSYAYSGNQW 2221
Cdd:pfam00704 216 PASKLVLGVPFYGRSWTLV---------------NGSGNTWEDGVLAYKEICNLLKDNGATVVWDDVAK-APYVYDGDQF 279
|
330 340 350
....*....|....*....|....*....|..
gi 442628919 2222 ISYDDVTTIRRKSQFIKSLQLGGGMIWALDLD 2253
Cdd:pfam00704 280 ITYDDPRSIATKVDYVKAKGLGGVMIWSLDAD 311
|
|
| Glyco_hydro_18 |
pfam00704 |
Glycosyl hydrolases family 18; |
966-1310 |
9.98e-100 |
|
Glycosyl hydrolases family 18;
Pssm-ID: 425828 [Multi-domain] Cd Length: 311 Bit Score: 323.64 E-value: 9.98e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 966 KVICYFTNWAWYRKGigrftpDDINTELCTHVIYGFAVLDYSELVLRTHDsWADVENNFYTRVTSLKSKGIKVSLALGGW 1045
Cdd:pfam00704 1 RIVGYYTSWGVYRNG------NFLPSDKLTHIIYAFANIDGSDGTLFIGD-WDLGNFEQLKKLKKQKNPGVKVLLSIGGW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1046 NDSqgDKYSRLVRSPMARSRFVRHALEFIEKYGFEGLDLDWEYPvcwqtecnKGSTEEKDGFTAWVQELSEAFRP----R 1121
Cdd:pfam00704 74 TDS--TGFSLMASNPASRKKFADSIVSFLRKYGFDGIDIDWEYP--------GGNPEDKENYDLLLRELRAALDEakggK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1122 GLMLSTAVSPSRKIIDAGYDIPQLSRYFDWIAVMTYDFHGHWDKKTGHVAPLYhhpddDFEYFNVNYSINYWMEKGAPSQ 1201
Cdd:pfam00704 144 KYLLSAAVPASYPDLDKGYDLPKIAKYLDFINVMTYDFHGSWDNVTGHHAPLY-----GGGSYNVDYAVKYYLKQGVPAS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1202 KLVMGIPLYGQSFTLentnssglnakapapGEAGEFTRAAGFLAYYEICERVNRQGWQVVHDEFGRmGPYAYKGTQWVSY 1281
Cdd:pfam00704 219 KLVLGVPFYGRSWTL---------------VNGSGNTWEDGVLAYKEICNLLKDNGATVVWDDVAK-APYVYDGDQFITY 282
|
330 340
....*....|....*....|....*....
gi 442628919 1282 DSPDMVRKKSLLVRSLKLGGGMVWALDLD 1310
Cdd:pfam00704 283 DDPRSIATKVDYVKAKGLGGVMIWSLDAD 311
|
|
| Glyco_18 |
smart00636 |
Glyco_18 domain; |
220-565 |
6.49e-98 |
|
Glyco_18 domain;
Pssm-ID: 214753 [Multi-domain] Cd Length: 334 Bit Score: 319.62 E-value: 6.49e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 220 KVLCYMSNWAFYRSGeahFVPEQIDPNLCSAIIYSFASLDPDHlTIREFDSWVDLDNQYYrrVTSL-----GVPVLIALG 294
Cdd:smart00636 1 RVVGYFTNWGVYGRN---FPVDDIPASKLTHIIYAFANIDPDG-TVTIGDEWADIGNFGQ--LKALkkknpGLKVLLSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 295 GWTDSSgsKYSRLVSDNLKRRVFISSVSSFLLRHGFSGLHLDWNYPKCWQsdcsrgpvTDRPNLTKLLRELRTEFQSVD- 373
Cdd:smart00636 75 GWTESD--NFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWEYPGGRG--------DDRENYTALLKELREALDKEGa 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 374 --PKFQLGVAISGYKEIIKEAYDF-PALSDIVDYMTVMTYDYHGAWEQKTGHVSPLYGLSSDTyPQYNTNYTMQLLLKMG 450
Cdd:smart00636 145 egKGYLLTIAVPAGPDKIDKGYGDlPAIAKYLDFINLMTYDFHGAWSNPTGHNAPLYAGPGDP-EKYNVDYAVKYYLCKG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 451 ARREKLVLSIPFYGQSFTLATahQILAGPGVAASGPGDAGELTKQPGMLAYYEICQRL-TKFNWIsdrnlNVIFGPFAML 529
Cdd:smart00636 224 VPPSKLVLGIPFYGRGWTLVD--GSNNGPGAPFTGPATGGPGTWEGGVVDYREICKLLgATVVYD-----DTAKAPYAYN 296
|
330 340 350
....*....|....*....|....*....|....*...
gi 442628919 530 --NDQWVGYEDPTSAQAKARYAANNNFAGVAAWTIDLD 565
Cdd:smart00636 297 pgTGQWVSYDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
|
|
| ChiA |
COG3325 |
Chitinase, GH18 family [Carbohydrate transport and metabolism]; |
965-1331 |
9.40e-87 |
|
Chitinase, GH18 family [Carbohydrate transport and metabolism];
Pssm-ID: 442554 [Multi-domain] Cd Length: 391 Bit Score: 289.89 E-value: 9.40e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 965 YKVICYFTNWAWYRKGigrFTPDDINTELCTHVIYGFAVLDySELVLRTHDSWA--------DVENNFYTRV----TSLK 1032
Cdd:COG3325 19 KRVVGYFTQWGIYGRN---YLVKDIPASKLTHINYAFANVD-PDGKCSVGDAWAkpsvdgaaDDWDQPLKGNfnqlKKLK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1033 SK--GIKVSLALGGWNDSQGdkYSRLVRSPMARSRFVRHALEFIEKYGFEGLDLDWEYPVCWQTECNKGSTEEKDGFTAW 1110
Cdd:COG3325 95 AKnpNLKVLISIGGWTWSKG--FSDAAATPASRAAFVDSCVDLLRKYNFDGIDIDWEYPGSGGAPGNVYRPEDKANFTAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1111 VQELSEAF------RPRGLMLSTAVSPSRKIIDaGYDIPQLSRYFDWIAVMTYDFHGHWDKKTGHVAPLYHHPDD-DFEY 1183
Cdd:COG3325 173 LKELRAQLdalgaeTGKHYLLTAAAPAGPDKLD-GIELPKVAQYLDYVNVMTYDFHGAWSPTTGHQAPLYDSPKDpEAQG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1184 FNVNYSINYWMEKGAPSQKLVMGIPLYGQSFTLENTNSSGLN--AKAPAPGeagefTRAAGFLAYYEICER-VNRQGWQV 1260
Cdd:COG3325 252 YSVDSAVQAYLAAGVPASKLVLGVPFYGRGWTGVTGGNNGLYqpATGPAPG-----TWEAGVNDYKDLKALyLGSNGYTR 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442628919 1261 VHDEFGRMgPYAYKGT--QWVSYDSPDMVRKKSLLVRSLKLGGGMVWALDLDDFKNRcgngvhpLLTEIHNVL 1331
Cdd:COG3325 327 YWDDVAKA-PYLYNGDtgTFISYDDPRSIAAKADYVKDKGLGGVMFWELSGDTADGT-------LLNAIGEGL 391
|
|
| ChiA |
COG3325 |
Chitinase, GH18 family [Carbohydrate transport and metabolism]; |
1905-2274 |
8.96e-85 |
|
Chitinase, GH18 family [Carbohydrate transport and metabolism];
Pssm-ID: 442554 [Multi-domain] Cd Length: 391 Bit Score: 284.11 E-value: 8.96e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1905 NNSYKVVCYFTSWAWYrssQGKFVPEDIDANLCTHLIYGFAVLDS-----------KSLTIKTHDSWTDIDNRFYERVVE 1973
Cdd:COG3325 16 TSGKRVVGYFTQWGIY---GRNYLVKDIPASKLTHINYAFANVDPdgkcsvgdawaKPSVDGAADDWDQPLKGNFNQLKK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1974 YKQR--GLRVMLAIGGWNDSLGskYARLVLNSQSRRRFVASVISFLEQHGFEGLDLAWEFPVCWQVNCNRGNPTEKDGFV 2051
Cdd:COG3325 93 LKAKnpNLKVLISIGGWTWSKG--FSDAAATPASRAAFVDSCVDLLRKYNFDGIDIDWEYPGSGGAPGNVYRPEDKANFT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 2052 ALVKELSEAFKENG------LILSAAV--SPSKMvidAGYNVFELSPYFDWVAVMTYDFHGHWDMRTGQIAPLFHRGGD- 2122
Cdd:COG3325 171 ALLKELRAQLDALGaetgkhYLLTAAApaGPDKL---DGIELPKVAQYLDYVNVMTYDFHGAWSPTTGHQAPLYDSPKDp 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 2123 ENLYLNGNFSIHYWLERGIPNDKLVMGMPMYGQTFTLADQNRRSLNDKTVGPGKAgtfTRADGFLAYYEICEKVVN-DDW 2201
Cdd:COG3325 248 EAQGYSVDSAVQAYLAAGVPASKLVLGVPFYGRGWTGVTGGNNGLYQPATGPAPG---TWEAGVNDYKDLKALYLGsNGY 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442628919 2202 KVVRDEEGIFgSYAYSGN--QWISYDDVTTIRRKSQFIKSLQLGGGMIWALDLDDFRGLcgcgkhpLLRTLSQEL 2274
Cdd:COG3325 325 TRYWDDVAKA-PYLYNGDtgTFISYDDPRSIAAKADYVKDKGLGGVMFWELSGDTADGT-------LLNAIGEGL 391
|
|
| Glyco_hydro_18 |
pfam00704 |
Glycosyl hydrolases family 18; |
220-565 |
1.66e-83 |
|
Glycosyl hydrolases family 18;
Pssm-ID: 425828 [Multi-domain] Cd Length: 311 Bit Score: 277.03 E-value: 1.66e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 220 KVLCYMSNWAFYRSGEAhfvpeqIDPNLCSAIIYSFASLDPDHLTIREFDSwvdlDNQYYRRVTSL------GVPVLIAL 293
Cdd:pfam00704 1 RIVGYYTSWGVYRNGNF------LPSDKLTHIIYAFANIDGSDGTLFIGDW----DLGNFEQLKKLkkqknpGVKVLLSI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 294 GGWTDSSGskYSRLVSDNLKRRVFISSVSSFLLRHGFSGLHLDWNYPKCWqsdcsrgpVTDRPNLTKLLRELRTEF--QS 371
Cdd:pfam00704 71 GGWTDSTG--FSLMASNPASRKKFADSIVSFLRKYGFDGIDIDWEYPGGN--------PEDKENYDLLLRELRAALdeAK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 372 VDPKFQLGVAISGYKEIIKEAYDFPALSDIVDYMTVMTYDYHGAWEQKTGHVSPLYGlssdtYPQYNTNYTMQLLLKMGA 451
Cdd:pfam00704 141 GGKKYLLSAAVPASYPDLDKGYDLPKIAKYLDFINVMTYDFHGSWDNVTGHHAPLYG-----GGSYNVDYAVKYYLKQGV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 452 RREKLVLSIPFYGQSFTLAtahqilagpgvaasgpgDAGELTKQPGMLAYYEICQRLTKFNWISDRNlNVIFGPFAMLND 531
Cdd:pfam00704 216 PASKLVLGVPFYGRSWTLV-----------------NGSGNTWEDGVLAYKEICNLLKDNGATVVWD-DVAKAPYVYDGD 277
|
330 340 350
....*....|....*....|....*....|....
gi 442628919 532 QWVGYEDPTSAQAKARYAANNNFAGVAAWTIDLD 565
Cdd:pfam00704 278 QFITYDDPRSIATKVDYVKAKGLGGVMIWSLDAD 311
|
|
| ChiA |
COG3325 |
Chitinase, GH18 family [Carbohydrate transport and metabolism]; |
1401-1774 |
4.29e-82 |
|
Chitinase, GH18 family [Carbohydrate transport and metabolism];
Pssm-ID: 442554 [Multi-domain] Cd Length: 391 Bit Score: 276.41 E-value: 4.29e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1401 EATEMATEFKIICYFTNWAWYrqgGGKFLPEDIDSDLCTHIIYGFAVLSRDNlTIQPHDSWA------------DLDNKF 1468
Cdd:COG3325 11 AAATATSGKRVVGYFTQWGIY---GRNYLVKDIPASKLTHINYAFANVDPDG-KCSVGDAWAkpsvdgaaddwdQPLKGN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1469 YERIVAYRKK--GAKVTVAIGGWNDSAGdkYSRLVRNPEARSRFIRNVLDFIEEYNFDGLDLDWEYPVCWQVDCKKGTAE 1546
Cdd:COG3325 87 FNQLKKLKAKnpNLKVLISIGGWTWSKG--FSDAAATPASRAAFVDSCVDLLRKYNFDGIDIDWEYPGSGGAPGNVYRPE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1547 EKIGFSALVREL------FYAFQPRGLILSAAVSPNKKVIDaGYEVAELSHYFSWISVMAYDYHGQWDKKTGHVAPMYSH 1620
Cdd:COG3325 165 DKANFTALLKELraqldaLGAETGKHYLLTAAAPAGPDKLD-GIELPKVAQYLDYVNVMTYDFHGAWSPTTGHQAPLYDS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1621 P--EGTANFNANFSMNYWISMGADRRKLVMGIPLYGQSFSLAETTKHQLNAPTYGggeAGEATRARGFLAYYEICLK-IR 1697
Cdd:COG3325 244 PkdPEAQGYSVDSAVQAYLAAGVPASKLVLGVPFYGRGWTGVTGGNNGLYQPATG---PAPGTWEAGVNDYKDLKALyLG 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442628919 1698 HHRWNVVRDTKGRiGPFAYHGD--QWVSFDDVPMIRHKSEYIKAMGLGGAMIWALDLDDFKNVcecesypLLKAINRVL 1774
Cdd:COG3325 321 SNGYTRYWDDVAK-APYLYNGDtgTFISYDDPRSIAAKADYVKDKGLGGVMFWELSGDTADGT-------LLNAIGEGL 391
|
|
| GH18_IDGF |
cd02873 |
The IDGF's (imaginal disc growth factors) are a family of growth factors identified in insects ... |
966-1331 |
1.72e-76 |
|
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: 261.09 E-value: 1.72e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 966 KVICYFTNWAWYRKGIGRFTPDDINTEL--CTHVIYGFAVLDYSELVLRTHDSWADVENNFYTRVTSLKSK--GIKVSLA 1041
Cdd:cd02873 1 KLVCYYDSKSYLREGLAKMSLEDLEPALqfCTHLVYGYAGIDADTYKIKSLNEDLDLDKSHYRAITSLKRKypHLKVLLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1042 LGGWNDS----QGDKYSRLVRSPMARSRFVRHALEFIEKYGFEGLDLDWEYPV------------CWQT---------EC 1096
Cdd:cd02873 81 VGGDRDTdeegENEKYLLLLESSESRNAFINSAHSLLKTYGFDGLDLAWQFPKnkpkkvrgtfgsAWHSfkklftgdsVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1097 NKGSTEEKDGFTAWVQELSEAFRPRGLMLSTAVSPSrkiIDAG--YDIPQLSRYFDWIAVMTYDFHG-HWDKKTGH-VAP 1172
Cdd:cd02873 161 DEKAAEHKEQFTALVRELKNALRPDGLLLTLTVLPH---VNSTwyFDVPAIANNVDFVNLATFDFLTpERNPEEADyTAP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1173 LYHhPDDDFEYFNVNYSINYWMEKGAPSQKLVMGIPLYGQSFTLenTNSSGLNAKAPA-----PGEAGEFTRAAGFLAYY 1247
Cdd:cd02873 238 IYE-LYERNPHHNVDYQVKYWLNQGTPASKLNLGIATYGRAWKL--TKDSGITGVPPVletdgPGPAGPQTKTPGLLSWP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1248 EICERVNRQGWQV--------VHDEFGRMGPYAYKGTQ-------WVSYDSPDMVRKKSLLVRSLKLGGGMVWALDLDDF 1312
Cdd:cd02873 315 EICSKLPNPANLKgadaplrkVGDPTKRFGSYAYRPADengehgiWVSYEDPDTAANKAGYAKAKGLGGVALFDLSLDDF 394
|
410
....*....|....*....
gi 442628919 1313 KNRCGNGVHPLLTEIHNVL 1331
Cdd:cd02873 395 RGQCTGDKFPILRSAKYRL 413
|
|
| GH18_IDGF |
cd02873 |
The IDGF's (imaginal disc growth factors) are a family of growth factors identified in insects ... |
1909-2268 |
3.88e-76 |
|
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: 259.94 E-value: 3.88e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1909 KVVCYFTSWAWYRSSQGKFVPEDID--ANLCTHLIYGFAVLDSKSLTIKTHDSWTDIDNRFYERVVEYKQR--GLRVMLA 1984
Cdd:cd02873 1 KLVCYYDSKSYLREGLAKMSLEDLEpaLQFCTHLVYGYAGIDADTYKIKSLNEDLDLDKSHYRAITSLKRKypHLKVLLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1985 IGGWNDS----LGSKYARLVLNSQSRRRFVASVISFLEQHGFEGLDLAWEFPV------------CWQ--VNCNRGNPT- 2045
Cdd:cd02873 81 VGGDRDTdeegENEKYLLLLESSESRNAFINSAHSLLKTYGFDGLDLAWQFPKnkpkkvrgtfgsAWHsfKKLFTGDSVv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 2046 ------EKDGFVALVKELSEAFKENGLILSAAVSP---SKMVIDagynVFELSPYFDWVAVMTYDFhghwdmRTGQ---- 2112
Cdd:cd02873 161 dekaaeHKEQFTALVRELKNALRPDGLLLTLTVLPhvnSTWYFD----VPAIANNVDFVNLATFDF------LTPErnpe 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 2113 ----IAPLFHRGgDENLYLNGNFSIHYWLERGIPNDKLVMGMPMYGQTFTLADQNRRS---LNDKTVGPGKAGTFTRADG 2185
Cdd:cd02873 231 eadyTAPIYELY-ERNPHHNVDYQVKYWLNQGTPASKLNLGIATYGRAWKLTKDSGITgvpPVLETDGPGPAGPQTKTPG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 2186 FLAYYEICEKVVNDDW--------KVVRDEEGIFGSYAYSGNQ-------WISYDDVTTIRRKSQFIKSLQLGGGMIWAL 2250
Cdd:cd02873 310 LLSWPEICSKLPNPANlkgadaplRKVGDPTKRFGSYAYRPADengehgiWVSYEDPDTAANKAGYAKAKGLGGVALFDL 389
|
410
....*....|....*...
gi 442628919 2251 DLDDFRGLCGCGKHPLLR 2268
Cdd:cd02873 390 SLDDFRGQCTGDKFPILR 407
|
|
| GH18_IDGF |
cd02873 |
The IDGF's (imaginal disc growth factors) are a family of growth factors identified in insects ... |
1410-1770 |
5.41e-71 |
|
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: 244.92 E-value: 5.41e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1410 KIICYFTNWAWYRQGGGKFLPEDIDSDL--CTHIIYGFAVLSRDNLTIQPHDSWADLDNKFYERIVAYRKK--GAKVTVA 1485
Cdd:cd02873 1 KLVCYYDSKSYLREGLAKMSLEDLEPALqfCTHLVYGYAGIDADTYKIKSLNEDLDLDKSHYRAITSLKRKypHLKVLLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1486 IGGWNDS----AGDKYSRLVRNPEARSRFIRNVLDFIEEYNFDGLDLDWEYPV------------CWQ-----------V 1538
Cdd:cd02873 81 VGGDRDTdeegENEKYLLLLESSESRNAFINSAHSLLKTYGFDGLDLAWQFPKnkpkkvrgtfgsAWHsfkklftgdsvV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1539 DCKkgTAEEKIGFSALVRELFYAFQPRGLILSAAVSPNKKViDAGYEVAELSHYFSWISVMAYDYHG-QWDKKTGH-VAP 1616
Cdd:cd02873 161 DEK--AAEHKEQFTALVRELKNALRPDGLLLTLTVLPHVNS-TWYFDVPAIANNVDFVNLATFDFLTpERNPEEADyTAP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1617 MYSHPEGTANFNANFSMNYWISMGADRRKLVMGIPLYGQSFSL---AETTKHQLNAPTYGGGEAGEATRARGFLAYYEIC 1693
Cdd:cd02873 238 IYELYERNPHHNVDYQVKYWLNQGTPASKLNLGIATYGRAWKLtkdSGITGVPPVLETDGPGPAGPQTKTPGLLSWPEIC 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1694 LKIRH---------HRWNVVRDTKgRIGPFAY--------HGdQWVSFDDVPMIRHKSEYIKAMGLGGAMIWALDLDDFK 1756
Cdd:cd02873 318 SKLPNpanlkgadaPLRKVGDPTK-RFGSYAYrpadengeHG-IWVSYEDPDTAANKAGYAKAKGLGGVALFDLSLDDFR 395
|
410
....*....|....
gi 442628919 1757 NVCECESYPLLKAI 1770
Cdd:cd02873 396 GQCTGDKFPILRSA 409
|
|
| GH18_chitinase |
cd06548 |
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ... |
967-1310 |
5.58e-68 |
|
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: 232.91 E-value: 5.58e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 967 VICYFTNWAWYrkGIGRFTPDDINTELCTHVIYGFAVLDYSELVLRTHDSWAD---VENNFYTRVTSLKSKG-------- 1035
Cdd:cd06548 1 VVGYFTNWGIY--GRNYFVTDDIPADKLTHINYAFADIDGDGGVVTSDDEAADeaaQSVDGGADTDDQPLKGnfgqlrkl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1036 ------IKVSLALGGWNDSQGdkYSRLVRSPMARSRFVRHALEFIEKYGFEGLDLDWEYPVCWQTECNKGSTEEKDGFTA 1109
Cdd:cd06548 79 kqknphLKILLSIGGWTWSGG--FSDAAATEASRAKFADSAVDFIRKYGFDGIDIDWEYPGSGGAPGNVARPEDKENFTL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1110 WVQELSEAF------RPRGLMLSTAVSPSRKIIDAGyDIPQLSRYFDWIAVMTYDFHGHWDKKTGHVAPLYHHPDDDFEY 1183
Cdd:cd06548 157 LLKELREALdalgaeTGRKYLLTIAAPAGPDKLDKL-EVAEIAKYLDFINLMTYDFHGAWSNTTGHHSNLYASPADPPGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1184 FNVNYSINYWMEKGAPSQKLVMGIPLYGQSFTlentnssglnakapapgeageftraagflayyeicervnrqGWQVVHD 1263
Cdd:cd06548 236 YSVDAAVNYYLSAGVPPEKLVLGVPFYGRGWT-----------------------------------------GYTRYWD 274
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 442628919 1264 EFGrMGPYAYKGT--QWVSYDSPDMVRKKSLLVRSLKLGGGMVWALDLD 1310
Cdd:cd06548 275 EVA-KAPYLYNPStkTFISYDDPRSIKAKADYVKDKGLGGVMFWELSGD 322
|
|
| GH18_chitinase |
cd06548 |
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ... |
1411-1753 |
5.73e-67 |
|
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: 230.21 E-value: 5.73e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1411 IICYFTNWAWYrqGGGKFLPEDIDSDLCTHIIYGFAVLSRDNLTIQPHDSWADL------------DNKFYERIVAYRK- 1477
Cdd:cd06548 1 VVGYFTNWGIY--GRNYFVTDDIPADKLTHINYAFADIDGDGGVVTSDDEAADEaaqsvdggadtdDQPLKGNFGQLRKl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1478 KGA----KVTVAIGGWNDSAGdkYSRLVRNPEARSRFIRNVLDFIEEYNFDGLDLDWEYPVCWQVDCKKGTAEEKIGFSA 1553
Cdd:cd06548 79 KQKnphlKILLSIGGWTWSGG--FSDAAATEASRAKFADSAVDFIRKYGFDGIDIDWEYPGSGGAPGNVARPEDKENFTL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1554 LVREL------FYAFQPRGLILSAAVSPNKKVIDAGyEVAELSHYFSWISVMAYDYHGQWDKKTGHVAPMY-SHPEGTAN 1626
Cdd:cd06548 157 LLKELrealdaLGAETGRKYLLTIAAPAGPDKLDKL-EVAEIAKYLDFINLMTYDFHGAWSNTTGHHSNLYaSPADPPGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1627 FNANFSMNYWISMGADRRKLVMGIPLYGqsfslaettkhqlnaptygggeageatraRGFlayyeiclkirhHRWNVVRD 1706
Cdd:cd06548 236 YSVDAAVNYYLSAGVPPEKLVLGVPFYG-----------------------------RGW------------TGYTRYWD 274
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 442628919 1707 TKGRiGPFAYHGD--QWVSFDDVPMIRHKSEYIKAMGLGGAMIWALDLD 1753
Cdd:cd06548 275 EVAK-APYLYNPStkTFISYDDPRSIKAKADYVKDKGLGGVMFWELSGD 322
|
|
| GH18_chitinase |
cd06548 |
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ... |
1910-2253 |
1.89e-66 |
|
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: 228.67 E-value: 1.89e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1910 VVCYFTSWAWYrsSQGKFVPEDIDANLCTHLIYGFAVLDSKSLTIKTHDSWTDI---------------DNRFYERVVEY 1974
Cdd:cd06548 1 VVGYFTNWGIY--GRNYFVTDDIPADKLTHINYAFADIDGDGGVVTSDDEAADEaaqsvdggadtddqpLKGNFGQLRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1975 KQR--GLRVMLAIGGWNDSLGskYARLVLNSQSRRRFVASVISFLEQHGFEGLDLAWEFPVCWQVNCNRGNPTEKDGFVA 2052
Cdd:cd06548 79 KQKnpHLKILLSIGGWTWSGG--FSDAAATEASRAKFADSAVDFIRKYGFDGIDIDWEYPGSGGAPGNVARPEDKENFTL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 2053 LVKELSEAFKENGLI------LSAAVS--PSKMvidAGYNVFELSPYFDWVAVMTYDFHGHWDMRTGQIAPLFHRGGDEN 2124
Cdd:cd06548 157 LLKELREALDALGAEtgrkylLTIAAPagPDKL---DKLEVAEIAKYLDFINLMTYDFHGAWSNTTGHHSNLYASPADPP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 2125 LYLNGNFSIHYWLERGIPNDKLVMGMPMYGQTFTladqnrrslndktvgpgkagtftradgflayyeicekvvndDWKVV 2204
Cdd:cd06548 234 GGYSVDAAVNYYLSAGVPPEKLVLGVPFYGRGWT-----------------------------------------GYTRY 272
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 442628919 2205 RDEEGIfGSYAYSGN--QWISYDDVTTIRRKSQFIKSLQLGGGMIWALDLD 2253
Cdd:cd06548 273 WDEVAK-APYLYNPStkTFISYDDPRSIKAKADYVKDKGLGGVMFWELSGD 322
|
|
| ChiA |
COG3325 |
Chitinase, GH18 family [Carbohydrate transport and metabolism]; |
219-586 |
3.35e-63 |
|
Chitinase, GH18 family [Carbohydrate transport and metabolism];
Pssm-ID: 442554 [Multi-domain] Cd Length: 391 Bit Score: 221.71 E-value: 3.35e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 219 KKVLCYMSNWAFYRSGeahFVPEQIDPNLCSAIIYSFASLDPDhLTIREFDSW--------VDLDNQYYRRV----TSL- 285
Cdd:COG3325 19 KRVVGYFTQWGIYGRN---YLVKDIPASKLTHINYAFANVDPD-GKCSVGDAWakpsvdgaADDWDQPLKGNfnqlKKLk 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 286 ----GVPVLIALGGWTDSSGskYSRLVSDNLKRRVFISSVSSFLLRHGFSGLHLDWNYPKCWQSDCSRGPVTDRPNLTKL 361
Cdd:COG3325 95 aknpNLKVLISIGGWTWSKG--FSDAAATPASRAAFVDSCVDLLRKYNFDGIDIDWEYPGSGGAPGNVYRPEDKANFTAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 362 LRELRTEF----QSVDPKFQLGVAISGYKEIIkEAYDFPALSDIVDYMTVMTYDYHGAWEQKTGHVSPLYGLSSD-TYPQ 436
Cdd:COG3325 173 LKELRAQLdalgAETGKHYLLTAAAPAGPDKL-DGIELPKVAQYLDYVNVMTYDFHGAWSPTTGHQAPLYDSPKDpEAQG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 437 YNTNYTMQLLLKMGARREKLVLSIPFYGQSFTLATAHQilAGPGVAASGPGDAgelTKQPGMLAYYEICQRL-------- 508
Cdd:COG3325 252 YSVDSAVQAYLAAGVPASKLVLGVPFYGRGWTGVTGGN--NGLYQPATGPAPG---TWEAGVNDYKDLKALYlgsngytr 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 509 -----TKFNWISDRNlnvifgpfamlNDQWVGYEDPTSAQAKARYAANNNFAGVAAWTIDLDDFRNLccnesypLLRAIN 583
Cdd:COG3325 327 ywddvAKAPYLYNGD-----------TGTFISYDDPRSIAAKADYVKDKGLGGVMFWELSGDTADGT-------LLNAIG 388
|
...
gi 442628919 584 RAL 586
Cdd:COG3325 389 EGL 391
|
|
| GH18_IDGF |
cd02873 |
The IDGF's (imaginal disc growth factors) are a family of growth factors identified in insects ... |
220-586 |
4.57e-63 |
|
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: 222.19 E-value: 4.57e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 220 KVLCYMSNWAFYRSGEAHFVPEQIDP--NLCSAIIYSFASLDPDHLTIREFDSWVDLDNQYYRRVTSL-----GVPVLIA 292
Cdd:cd02873 1 KLVCYYDSKSYLREGLAKMSLEDLEPalQFCTHLVYGYAGIDADTYKIKSLNEDLDLDKSHYRAITSLkrkypHLKVLLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 293 LGGWTDS----SGSKYSRLVSDNLKRRVFISSVSSFLLRHGFSGLHLDWNYPK------------CWQS---DCSRGPVT 353
Cdd:cd02873 81 VGGDRDTdeegENEKYLLLLESSESRNAFINSAHSLLKTYGFDGLDLAWQFPKnkpkkvrgtfgsAWHSfkkLFTGDSVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 354 D------RPNLTKLLRELRTEFQSvdPKFQLGVAI------SGYkeiikeaYDFPALSDIVDYMTVMTYDYHGAWEQKT- 420
Cdd:cd02873 161 DekaaehKEQFTALVRELKNALRP--DGLLLTLTVlphvnsTWY-------FDVPAIANNVDFVNLATFDFLTPERNPEe 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 421 -GHVSPLYgLSSDTYPQYNTNYTMQLLLKMGARREKLVLSIPFYGQSFTLATAHQILAGPGV-AASGPGDAGELTKQPGM 498
Cdd:cd02873 232 aDYTAPIY-ELYERNPHHNVDYQVKYWLNQGTPASKLNLGIATYGRAWKLTKDSGITGVPPVlETDGPGPAGPQTKTPGL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 499 LAYYEICQRL----------TKFNWISDrnLNVIFGPFA--MLNDQ-----WVGYEDPTSAQAKARYAANNNFAGVAAWT 561
Cdd:cd02873 311 LSWPEICSKLpnpanlkgadAPLRKVGD--PTKRFGSYAyrPADENgehgiWVSYEDPDTAANKAGYAKAKGLGGVALFD 388
|
410 420
....*....|....*....|....*
gi 442628919 562 IDLDDFRNLCCNESYPLLRAINRAL 586
Cdd:cd02873 389 LSLDDFRGQCTGDKFPILRSAKYRL 413
|
|
| GH18_chitinase |
cd06548 |
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ... |
221-565 |
1.02e-58 |
|
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: 206.33 E-value: 1.02e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 221 VLCYMSNWAFYrsGEAHFVPEQIDPNLCSAIIYSFASLDPDHLTIREFDSWVDLDNQYYR-RVTSLGVP----------- 288
Cdd:cd06548 1 VVGYFTNWGIY--GRNYFVTDDIPADKLTHINYAFADIDGDGGVVTSDDEAADEAAQSVDgGADTDDQPlkgnfgqlrkl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 289 --------VLIALGGWTDSSGskYSRLVSDNLKRRVFISSVSSFLLRHGFSGLHLDWNYPK-CWQSDCSRGPvTDRPNLT 359
Cdd:cd06548 79 kqknphlkILLSIGGWTWSGG--FSDAAATEASRAKFADSAVDFIRKYGFDGIDIDWEYPGsGGAPGNVARP-EDKENFT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 360 KLLRELRTEF----QSVDPKFQLGVAISGYKEIIKeAYDFPALSDIVDYMTVMTYDYHGAWEQKTGHVSPLYGLSSDTYP 435
Cdd:cd06548 156 LLLKELREALdalgAETGRKYLLTIAAPAGPDKLD-KLEVAEIAKYLDFINLMTYDFHGAWSNTTGHHSNLYASPADPPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 436 QYNTNYTMQLLLKMGARREKLVLSIPFYGQSFTLATAHQilagpgvaasgpgdaGELTKQPgmlayyeicqrltkfnWIS 515
Cdd:cd06548 235 GYSVDAAVNYYLSAGVPPEKLVLGVPFYGRGWTGYTRYW---------------DEVAKAP----------------YLY 283
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 442628919 516 DRNlnvifgpfamlNDQWVGYEDPTSAQAKARYAANNNFAGVAAWTIDLD 565
Cdd:cd06548 284 NPS-----------TKTFISYDDPRSIKAKADYVKDKGLGGVMFWELSGD 322
|
|
| GH18_plant_chitinase_class_V |
cd02879 |
The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the ... |
1919-2254 |
1.72e-51 |
|
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: 184.49 E-value: 1.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1919 WYRSSQgKFVPEDIDANLCTHLIYGFAVLDSKS--LTIKTHDSWTDIDnrfYERVVEYKQRGLRVMLAIGGWNDSlGSKY 1996
Cdd:cd02879 9 WPAWSE-EFPPSNIDSSLFTHLFYAFADLDPSTyeVVISPSDESEFST---FTETVKRKNPSVKTLLSIGGGGSD-SSAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1997 ARLVLNSQSRRRFVASVISFLEQHGFEGLDLAWEFPvcwqvncnrGNPTEKDGFVALVKELSEAFKEN-------GLILS 2069
Cdd:cd02879 84 AAMASDPTARKAFINSSIKVARKYGFDGLDLDWEFP---------SSQVEMENFGKLLEEWRAAVKDEarssgrpPLLLT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 2070 AAVSPSKMVIDAG----YNVFELSPYFDWVAVMTYDFHGHWDMRTGQIAPLFHrggDENLYLNGNFSIHYWLERGIPNDK 2145
Cdd:cd02879 155 AAVYFSPILFLSDdsvsYPIEAINKNLDWVNVMAYDYYGSWESNTTGPAAALY---DPNSNVSTDYGIKSWIKAGVPAKK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 2146 LVMGMPMYGQTFTladqnrrsLNDKTVGpgkagtftradgflayyeicekvvnddwkvvrdeegifGSYAYSGNQWISYD 2225
Cdd:cd02879 232 LVLGLPLYGRAWT--------LYDTTTV--------------------------------------SSYVYAGTTWIGYD 265
|
330 340
....*....|....*....|....*....
gi 442628919 2226 DVTTIRRKSQFIKSLQLGGGMIWALDLDD 2254
Cdd:cd02879 266 DVQSIAVKVKYAKQKGLLGYFAWAVGYDD 294
|
|
| GH18_plant_chitinase_class_V |
cd02879 |
The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the ... |
976-1311 |
4.36e-46 |
|
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: 169.08 E-value: 4.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 976 WYRkGIGRFTPDDINTELCTHVIYGFAVLD---YSELVLRTHDSWAdveNNFyTRVTSLKSKGIKVSLALGGWNDSQgDK 1052
Cdd:cd02879 9 WPA-WSEEFPPSNIDSSLFTHLFYAFADLDpstYEVVISPSDESEF---STF-TETVKRKNPSVKTLLSIGGGGSDS-SA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1053 YSRLVRSPMARSRFVRHALEFIEKYGFEGLDLDWEYPvcwqtecnkGSTEEKDGFTAWVQELSEAFRP-------RGLML 1125
Cdd:cd02879 83 FAAMASDPTARKAFINSSIKVARKYGFDGLDLDWEFP---------SSQVEMENFGKLLEEWRAAVKDearssgrPPLLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1126 STAVSPSRKIIDAG----YDIPQLSRYFDWIAVMTYDFHGHWDKKTGHVAPLYHHPDDDfeyFNVNYSINYWMEKGAPSQ 1201
Cdd:cd02879 154 TAAVYFSPILFLSDdsvsYPIEAINKNLDWVNVMAYDYYGSWESNTTGPAAALYDPNSN---VSTDYGIKSWIKAGVPAK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1202 KLVMGIPLYGQSFTLENTNSsglnakapapgeageftraagflayyeicervnrqgwqvvhdefgrMGPYAYKGTQWVSY 1281
Cdd:cd02879 231 KLVLGLPLYGRAWTLYDTTT----------------------------------------------VSSYVYAGTTWIGY 264
|
330 340 350
....*....|....*....|....*....|
gi 442628919 1282 DSPDMVRKKSLLVRSLKLGGGMVWALDLDD 1311
Cdd:cd02879 265 DDVQSIAVKVKYAKQKGLLGYFAWAVGYDD 294
|
|
| GH18_chitinase-like |
cd00598 |
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ... |
1910-2101 |
1.30e-44 |
|
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: 161.39 E-value: 1.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1910 VVCYFTSWAWYRSsqgkFVPEDIDANLCTHLIYGFAVLDSKSLTIKTHDSWTDIDNRFYERVVEYKqRGLRVMLAIGGWN 1989
Cdd:cd00598 1 VICYYDGWSSGRG----PDPTDIPLSLCTHIIYAFAEISSDGSLNLFGDKSEEPLKGALEELASKK-PGLKVLISIGGWT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1990 DSlgsKYARLVLNSQSRRRFVASVISFLEQHGFEGLDLAWEFPVcwqvncNRGNPtEKDGFVALVKELSEAFKENGLILS 2069
Cdd:cd00598 76 DS---SPFTLASDPASRAAFANSLVSFLKTYGFDGVDIDWEYPG------AADNS-DRENFITLLRELRSALGAANYLLT 145
|
170 180 190
....*....|....*....|....*....|..
gi 442628919 2070 AAVSPSKMVIDAGYNVFELSPYFDWVAVMTYD 2101
Cdd:cd00598 146 IAVPASYFDLGYAYDVPAIGDYVDFVNVMTYD 177
|
|
| GH18_chitinase-like |
cd00598 |
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ... |
1411-1602 |
1.97e-44 |
|
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: 161.01 E-value: 1.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1411 IICYFTNWAWYRqgggKFLPEDIDSDLCTHIIYGFAVLSRDNLTIQPHDSWADLDNKFYERiVAYRKKGAKVTVAIGGWN 1490
Cdd:cd00598 1 VICYYDGWSSGR----GPDPTDIPLSLCTHIIYAFAEISSDGSLNLFGDKSEEPLKGALEE-LASKKPGLKVLISIGGWT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1491 DSagdKYSRLVRNPEARSRFIRNVLDFIEEYNFDGLDLDWEYPVcwqvdckKGTAEEKIGFSALVRELFYAFQPRGLILS 1570
Cdd:cd00598 76 DS---SPFTLASDPASRAAFANSLVSFLKTYGFDGVDIDWEYPG-------AADNSDRENFITLLRELRSALGAANYLLT 145
|
170 180 190
....*....|....*....|....*....|..
gi 442628919 1571 AAVSPNKKVIDAGYEVAELSHYFSWISVMAYD 1602
Cdd:cd00598 146 IAVPASYFDLGYAYDVPAIGDYVDFVNVMTYD 177
|
|
| GH18_plant_chitinase_class_V |
cd02879 |
The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the ... |
1420-1754 |
2.32e-43 |
|
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: 160.99 E-value: 2.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1420 WYrQGGGKFLPEDIDSDLCTHIIYGFAVL--SRDNLTIQPHDSWADLDnkfYERIVAYRKKGAKVTVAIGGwNDSAGDKY 1497
Cdd:cd02879 9 WP-AWSEEFPPSNIDSSLFTHLFYAFADLdpSTYEVVISPSDESEFST---FTETVKRKNPSVKTLLSIGG-GGSDSSAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1498 SRLVRNPEARSRFIRNVLDFIEEYNFDGLDLDWEYPvcwqvdckkGTAEEKIGFSALVRELFYAFQP-------RGLILS 1570
Cdd:cd02879 84 AAMASDPTARKAFINSSIKVARKYGFDGLDLDWEFP---------SSQVEMENFGKLLEEWRAAVKDearssgrPPLLLT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1571 AAV--SPNKKVIDAG--YEVAELSHYFSWISVMAYDYHGQWDKK-TGHVAPMYSHPegtANFNANFSMNYWISMGADRRK 1645
Cdd:cd02879 155 AAVyfSPILFLSDDSvsYPIEAINKNLDWVNVMAYDYYGSWESNtTGPAAALYDPN---SNVSTDYGIKSWIKAGVPAKK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1646 LVMGIPLYGQSFSLAETTkhqlnaptygggeageatrargFLAYYeiclkirhhrwnvvrdtkgrigpfAYHGDQWVSFD 1725
Cdd:cd02879 232 LVLGLPLYGRAWTLYDTT----------------------TVSSY------------------------VYAGTTWIGYD 265
|
330 340
....*....|....*....|....*....
gi 442628919 1726 DVPMIRHKSEYIKAMGLGGAMIWALDLDD 1754
Cdd:cd02879 266 DVQSIAVKVKYAKQKGLLGYFAWAVGYDD 294
|
|
| GH18_chitinase-like |
cd00598 |
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ... |
967-1158 |
1.67e-40 |
|
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: 149.84 E-value: 1.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 967 VICYFTNWAWYRKGIgrftPDDINTELCTHVIYGFAVLDYSELVLRTHDSWADVENNFYTRVTSLKsKGIKVSLALGGWN 1046
Cdd:cd00598 1 VICYYDGWSSGRGPD----PTDIPLSLCTHIIYAFAEISSDGSLNLFGDKSEEPLKGALEELASKK-PGLKVLISIGGWT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1047 DSQGDKysrLVRSPMARSRFVRHALEFIEKYGFEGLDLDWEYPVcwqtecNKGStEEKDGFTAWVQELSEAFRPRGLMLS 1126
Cdd:cd00598 76 DSSPFT---LASDPASRAAFANSLVSFLKTYGFDGVDIDWEYPG------AADN-SDRENFITLLRELRSALGAANYLLT 145
|
170 180 190
....*....|....*....|....*....|..
gi 442628919 1127 TAVSPSRKIIDAGYDIPQLSRYFDWIAVMTYD 1158
Cdd:cd00598 146 IAVPASYFDLGYAYDVPAIGDYVDFVNVMTYD 177
|
|
| GH18_chitinase-like |
cd00598 |
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ... |
221-411 |
6.90e-34 |
|
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: 130.58 E-value: 6.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 221 VLCYMSNWAFYRsgeaHFVPEQIDPNLCSAIIYSFASLDPDHLTIREFDSWVDLDNQYYRRVTSL--GVPVLIALGGWTD 298
Cdd:cd00598 1 VICYYDGWSSGR----GPDPTDIPLSLCTHIIYAFAEISSDGSLNLFGDKSEEPLKGALEELASKkpGLKVLISIGGWTD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 299 SSgskYSRLVSDNLKRRVFISSVSSFLLRHGFSGLHLDWNYPkcwqsdcSRGPVTDRPNLTKLLRELRTEFQSvdPKFQL 378
Cdd:cd00598 77 SS---PFTLASDPASRAAFANSLVSFLKTYGFDGVDIDWEYP-------GAADNSDRENFITLLRELRSALGA--ANYLL 144
|
170 180 190
....*....|....*....|....*....|...
gi 442628919 379 GVAISGYKEIIKEAYDFPALSDIVDYMTVMTYD 411
Cdd:cd00598 145 TIAVPASYFDLGYAYDVPAIGDYVDFVNVMTYD 177
|
|
| GH18_zymocin_alpha |
cd02878 |
Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle ... |
966-1310 |
4.77e-31 |
|
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: 126.65 E-value: 4.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 966 KVICYFTNWAWYRKGIgRFTPDDINTELCTHVIYGFAVL--DYSELVLRTHDSWadveNNFytrvtsLKSKGIKVSLALG 1043
Cdd:cd02878 1 KNIAYFEAYNLDRPCL-NMDVTQIDTSKYTHIHFAFANItsDFSVDVSSVQEQF----SDF------KKLKGVKKILSFG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1044 GWNDSQG-DKYSRL--VRSPMARSRFVRHALEFIEKYGFEGLDLDWEYPVCWQT-ECNKGSTEEKDGFTAWVQELSEAFr 1119
Cdd:cd02878 70 GWDFSTSpSTYQIFrdAVKPANRDTFANNVVNFVNKYNLDGVDFDWEYPGAPDIpGIPAGDPDDGKNYLEFLKLLKSKL- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1120 PRGLMLSTAVsPSRKIIDAGYDIPQLSRYFDWIAVMTYDFHGHWDKKTGHVAP-------LYHHPDDDfeyfNVNYSINY 1192
Cdd:cd02878 149 PSGKSLSIAA-PASYWYLKGFPIKDMAKYVDYIVYMTYDLHGQWDYGNKWASPgcpagncLRSHVNKT----ETLDALSM 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1193 WMEKGAPSQKLVMGIPLYGQSFTLENTNSSGLNAKAPAPGEAGEFTRAAGFLAY----YEICERVNRQGWQVVHDEfGRM 1268
Cdd:cd02878 224 ITKAGVPSNKVVVGVASYGRSFKMADPGCTGPGCTFTGPGSGAEAGRCTCTAGYgaisEIEIIDISKSKNKRWYDT-DSD 302
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 442628919 1269 GPYA-YKGTQWVSYDSPDMVRKKSLLVRSLKLGGGMVWALDLD 1310
Cdd:cd02878 303 SDILvYDDDQWVAYMSPATKAARIEWYKGLNFGGTSDWAVDLQ 345
|
|
| GH18_CFLE_spore_hydrolase |
cd02874 |
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ... |
1028-1311 |
1.60e-29 |
|
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: 121.22 E-value: 1.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1028 VTSLKSKGIKVSLALGGWNDSQ--GDKYSRLVRSPMARSRFVRHALEFIEKYGFEGLDLDWEYPvcwqtecnkgSTEEKD 1105
Cdd:cd02874 51 IEAAKRRGVKPLLVITNLTNGNfdSELAHAVLSNPEARQRLINNILALAKKYGYDGVNIDFENV----------PPEDRE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1106 GFTAWVQELSEAFRPRGLMLSTAVSPSRKIIDAG-----YDIPQLSRYFDWIAVMTYDFHgHWDKKTGHVAPLyhhpddd 1180
Cdd:cd02874 121 AYTQFLRELSDRLHPAGYTLSTAVVPKTSADQFGnwsgaYDYAAIGKIVDFVVLMTYDWH-WRGGPPGPVAPI------- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1181 feyfN-VNYSINYWMEKgAPSQKLVMGIPLYGQSFTLenTNSSGLNAKAPAPGEAgeFTRAAgflayyeicervnRQGWQ 1259
Cdd:cd02874 193 ----GwVERVLQYAVTQ-IPREKILLGIPLYGYDWTL--PYKKGGKASTISPQQA--INLAK-------------RYGAE 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 442628919 1260 VVHDEFGRMGPYAY---KGTQ-WVSYDSPDMVRKKSLLVRSLKLGGGMVWALDLDD 1311
Cdd:cd02874 251 IQYDEEAQSPFFRYvdeQGRRhEVWFEDARSLQAKFELAKEYGLRGVSYWRLGLED 306
|
|
| GH18_zymocin_alpha |
cd02878 |
Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle ... |
1410-1753 |
2.95e-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: 118.57 E-value: 2.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1410 KIICYFTNWAWYRQGggkfL---PEDIDSDLCTHIIYGFAVLSRDnLTI---QPHDSWadldNKFYERivayrkKGAKVT 1483
Cdd:cd02878 1 KNIAYFEAYNLDRPC----LnmdVTQIDTSKYTHIHFAFANITSD-FSVdvsSVQEQF----SDFKKL------KGVKKI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1484 VAIGGWNDSAG-DKYSRLvRN---PEARSRFIRNVLDFIEEYNFDGLDLDWEYPVCWQV-DCKKGTAEEKIGFSALVREL 1558
Cdd:cd02878 66 LSFGGWDFSTSpSTYQIF-RDavkPANRDTFANNVVNFVNKYNLDGVDFDWEYPGAPDIpGIPAGDPDDGKNYLEFLKLL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1559 fYAFQPRGLILSAAVsPNKKVIDAGYEVAELSHYFSWISVMAYDYHGQWDKKTGHVAP-------MYSHPEGTANFNAnf 1631
Cdd:cd02878 145 -KSKLPSGKSLSIAA-PASYWYLKGFPIKDMAKYVDYIVYMTYDLHGQWDYGNKWASPgcpagncLRSHVNKTETLDA-- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1632 smnywISM----GADRRKLVMGIPLYGQSFSLAETTKHQLNAPTYGGGEAGEATRARGFLAY---YEICLKIRHHRWNV- 1703
Cdd:cd02878 221 -----LSMitkaGVPSNKVVVGVASYGRSFKMADPGCTGPGCTFTGPGSGAEAGRCTCTAGYgaiSEIEIIDISKSKNKr 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 442628919 1704 VRDTKGRIGPFAYHGDQWVSFDDVPMIRHKSEYIKAMGLGGAMIWALDLD 1753
Cdd:cd02878 296 WYDTDSDSDILVYDDDQWVAYMSPATKAARIEWYKGLNFGGTSDWAVDLQ 345
|
|
| GH18_zymocin_alpha |
cd02878 |
Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle ... |
1909-2253 |
4.58e-24 |
|
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: 106.24 E-value: 4.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1909 KVVCYFTSWAWYRSSQGKFVPEdIDANLCTHLIYGFAVLdSKSLTI---KTHDSWtdidNRFYERVveykqrGLRVMLAI 1985
Cdd:cd02878 1 KNIAYFEAYNLDRPCLNMDVTQ-IDTSKYTHIHFAFANI-TSDFSVdvsSVQEQF----SDFKKLK------GVKKILSF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1986 GGWNDSLG-SKYARL--VLNSQSRRRFVASVISFLEQHGFEGLDLAWEFPVCWQV-NCNRGNPTEKDGFVALVKELSEAF 2061
Cdd:cd02878 69 GGWDFSTSpSTYQIFrdAVKPANRDTFANNVVNFVNKYNLDGVDFDWEYPGAPDIpGIPAGDPDDGKNYLEFLKLLKSKL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 2062 KeNGLILSAAVsPSKMVIDAGYNVFELSPYFDWVAVMTYDFHGHWDMRTGQIAPLFHRGgdenlylNGNFS------IHY 2135
Cdd:cd02878 149 P-SGKSLSIAA-PASYWYLKGFPIKDMAKYVDYIVYMTYDLHGQWDYGNKWASPGCPAG-------NCLRShvnkteTLD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 2136 WLE----RGIPNDKLVMGMPMYGQTFTLADQNRRSLNDKTVGPGKAGTFTRADGFLAYYEICE-------KVVNDDWkVV 2204
Cdd:cd02878 220 ALSmitkAGVPSNKVVVGVASYGRSFKMADPGCTGPGCTFTGPGSGAEAGRCTCTAGYGAISEieiidisKSKNKRW-YD 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 442628919 2205 RDEEGIFgsYAYSGNQWISY-DDVTTIRRKsQFIKSLQLGGGMIWALDLD 2253
Cdd:cd02878 299 TDSDSDI--LVYDDDQWVAYmSPATKAARI-EWYKGLNFGGTSDWAVDLQ 345
|
|
| GH18_plant_chitinase_class_V |
cd02879 |
The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the ... |
229-566 |
9.84e-24 |
|
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: 103.98 E-value: 9.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 229 AFYRSGEAHFVPEQIDPNLCSAIIYSFASLDPDHLTIREFDSwvdlDNQYYRRVTSL------GVPVLIALGGWTDSSgS 302
Cdd:cd02879 7 GYWPAWSEEFPPSNIDSSLFTHLFYAFADLDPSTYEVVISPS----DESEFSTFTETvkrknpSVKTLLSIGGGGSDS-S 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 303 KYSRLVSDNLKRRVFISSVSSFLLRHGFSGLHLDWNYPKcwqsdcsrgPVTDRPNLTKLLRELRTEFQ-----SVDPKFQ 377
Cdd:cd02879 82 AFAAMASDPTARKAFINSSIKVARKYGFDGLDLDWEFPS---------SQVEMENFGKLLEEWRAAVKdearsSGRPPLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 378 LGVAISgYKEIIKEAYD---FP--ALSDIVDYMTVMTYDYHGAWEQK-TGHVSPLYGLSSDtypqYNTNYTMQLLLKMGA 451
Cdd:cd02879 153 LTAAVY-FSPILFLSDDsvsYPieAINKNLDWVNVMAYDYYGSWESNtTGPAAALYDPNSN----VSTDYGIKSWIKAGV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 452 RREKLVLSIPFYGQSFTLatahqilagpgvaasgpgdageltKQPGMLAYYeicqrltkfnwisdrnlnvifgpfAMLND 531
Cdd:cd02879 228 PAKKLVLGLPLYGRAWTL------------------------YDTTTVSSY------------------------VYAGT 259
|
330 340 350
....*....|....*....|....*....|....*
gi 442628919 532 QWVGYEDPTSAQAKARYAANNNFAGVAAWTIDLDD 566
Cdd:cd02879 260 TWIGYDDVQSIAVKVKYAKQKGLLGYFAWAVGYDD 294
|
|
| GH18_CFLE_spore_hydrolase |
cd02874 |
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ... |
1442-1754 |
1.04e-23 |
|
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: 104.27 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1442 IYGFAVLSRDNLTIQPHdswadldnkfyERIVAY-RKKGAKVTVAIGGWNDS--AGDKYSRLVRNPEARSRFIRNVLDFI 1518
Cdd:cd02874 31 PFWYGVDADGTLTGLPD-----------ERLIEAaKRRGVKPLLVITNLTNGnfDSELAHAVLSNPEARQRLINNILALA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1519 EEYNFDGLDLDWE--YPvcwqvdckkgtaEEKIGFSALVRELFYAFQPRGLILSAAVSPNKKVIDAG-----YEVAELSH 1591
Cdd:cd02874 100 KKYGYDGVNIDFEnvPP------------EDREAYTQFLRELSDRLHPAGYTLSTAVVPKTSADQFGnwsgaYDYAAIGK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1592 YFSWISVMAYDYHGQWdKKTGHVAPMyshpegtanfnanfsmnYWISMGAD-------RRKLVMGIPLYGQSFSLaeTTK 1664
Cdd:cd02874 168 IVDFVVLMTYDWHWRG-GPPGPVAPI-----------------GWVERVLQyavtqipREKILLGIPLYGYDWTL--PYK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1665 HQLNAPTYGGGEAgeatrargflayyeICLKIRHHRWnVVRDTKGRIGPFAYHGDQ----WVSFDDVPMIRHKSEYIKAM 1740
Cdd:cd02874 228 KGGKASTISPQQA--------------INLAKRYGAE-IQYDEEAQSPFFRYVDEQgrrhEVWFEDARSLQAKFELAKEY 292
|
330
....*....|....
gi 442628919 1741 GLGGAMIWALDLDD 1754
Cdd:cd02874 293 GLRGVSYWRLGLED 306
|
|
| GH18_3CO4_chitinase |
cd06545 |
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an ... |
1411-1658 |
4.87e-22 |
|
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: 97.91 E-value: 4.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1411 IICYFTNWAWYRQGGGKflpedIDSDLCTHIIYGFAVLSRD-NLTIQPHDSwaDLDNKfyerIVAYRKKGAKVTVAIGGw 1489
Cdd:cd06545 1 VVGYLPNYDDLNALSPT-----IDFSKLTHINLAFANPDANgTLNANPVRS--ELNSV----VNAAHAHNVKILISLAG- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1490 ndSAGDKYSRLVRNPEARSRFIRNVLDFIEEYNFDGLDLDWEYPVCWQvdckkgtaeekIGFSALVRELFYAFQPRGLIL 1569
Cdd:cd06545 69 --GSPPEFTAALNDPAKRKALVDKIINYVVSYNLDGIDVDLEGPDVTF-----------GDYLVFIRALYAALKKEGKLL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1570 SAAVSPNkkviDAGYEVAELSHYFSWISVMAYDYHGQWDKKTGHVAPMYShpegtanfNANFSMNYWISMG-ADRRKLVM 1648
Cdd:cd06545 136 TAAVSSW----NGGAVSDSTLAYFDFINIMSYDATGPWWGDNPGQHSSYD--------DAVNDLNYWNERGlASKDKLVL 203
|
250
....*....|
gi 442628919 1649 GIPLYGQSFS 1658
Cdd:cd06545 204 GLPFYGYGFY 213
|
|
| GH18_zymocin_alpha |
cd02878 |
Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle ... |
240-565 |
1.23e-21 |
|
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: 98.92 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 240 PEQIDPNLCSAIIYSFASLDPDhltireFDSWVDLDNQYYRRVTSL-GVPVLIALGGWTDSSG-SKYSRL---VSDNlKR 314
Cdd:cd02878 20 VTQIDTSKYTHIHFAFANITSD------FSVDVSSVQEQFSDFKKLkGVKKILSFGGWDFSTSpSTYQIFrdaVKPA-NR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 315 RVFISSVSSFLLRHGFSGLHLDWNYPKCWQS-DCSRGPVTDRPNLTKLLRELRTEFQSvdpKFQLGVAISGykeiikeAY 393
Cdd:cd02878 93 DTFANNVVNFVNKYNLDGVDFDWEYPGAPDIpGIPAGDPDDGKNYLEFLKLLKSKLPS---GKSLSIAAPA-------SY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 394 ----DFP--ALSDIVDYMTVMTYDYHGAWEQKTGHVSPlyGLSSDTYPQYNTNYTMQLL-LKM----GARREKLVLSIPF 462
Cdd:cd02878 163 wylkGFPikDMAKYVDYIVYMTYDLHGQWDYGNKWASP--GCPAGNCLRSHVNKTETLDaLSMitkaGVPSNKVVVGVAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 463 YGQSFTLATAHqiLAGPGVAASGPGDAGELTKQPGMLAYY--------EICQRLTKFNWISDRNLNV-IFGpfamlNDQW 533
Cdd:cd02878 241 YGRSFKMADPG--CTGPGCTFTGPGSGAEAGRCTCTAGYGaiseieiiDISKSKNKRWYDTDSDSDIlVYD-----DDQW 313
|
330 340 350
....*....|....*....|....*....|..
gi 442628919 534 VGYEDPTSAQAKARYAANNNFAGVAAWTIDLD 565
Cdd:cd02878 314 VAYMSPATKAARIEWYKGLNFGGTSDWAVDLQ 345
|
|
| GH18_CFLE_spore_hydrolase |
cd02874 |
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ... |
1968-2254 |
1.46e-21 |
|
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: 97.72 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1968 YERVVEY-KQRGLRVMLAI-----GGWNDSLGSkyaRLVLNSQSRRRFVASVISFLEQHGFEGLDLAWEFPvcwqvncnr 2041
Cdd:cd02874 47 DERLIEAaKRRGVKPLLVItnltnGNFDSELAH---AVLSNPEARQRLINNILALAKKYGYDGVNIDFENV--------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 2042 gNPTEKDGFVALVKELSEAFKENGLILSAAVSPSKMVIDAG-----YNVFELSPYFDWVAVMTYDFHGHWDmRTGQIAPL 2116
Cdd:cd02874 115 -PPEDREAYTQFLRELSDRLHPAGYTLSTAVVPKTSADQFGnwsgaYDYAAIGKIVDFVVLMTYDWHWRGG-PPGPVAPI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 2117 fhrggdenlylngnfsihYWLER-------GIPNDKLVMGMPMYGQTFTLADQnrrsLNDKTVGPGKAGTFTRADGFLAy 2189
Cdd:cd02874 193 ------------------GWVERvlqyavtQIPREKILLGIPLYGYDWTLPYK----KGGKASTISPQQAINLAKRYGA- 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442628919 2190 yeicekvvnddwKVVRDEEGIFGSYAYSGNQ----WISYDDVTTIRRKSQFIKSLQLGGGMIWALDLDD 2254
Cdd:cd02874 250 ------------EIQYDEEAQSPFFRYVDEQgrrhEVWFEDARSLQAKFELAKEYGLRGVSYWRLGLED 306
|
|
| GH18_3CO4_chitinase |
cd06545 |
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an ... |
967-1215 |
4.21e-21 |
|
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: 95.21 E-value: 4.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 967 VICYFTNWAWYRKGIGRftpddINTELCTHVIYGFAVLDySELVLRTHDSWADVEnnfyTRVTSLKSKGIKVSLALGGwn 1046
Cdd:cd06545 1 VVGYLPNYDDLNALSPT-----IDFSKLTHINLAFANPD-ANGTLNANPVRSELN----SVVNAAHAHNVKILISLAG-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1047 dSQGDKYSRLVRSPMARSRFVRHALEFIEKYGFEGLDLDWEYPVCWQtecnkgsteekDGFTAWVQELSEAFRPRGLMLS 1126
Cdd:cd06545 69 -GSPPEFTAALNDPAKRKALVDKIINYVVSYNLDGIDVDLEGPDVTF-----------GDYLVFIRALYAALKKEGKLLT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1127 TAVSPSRkiidaGYDIPQLS-RYFDWIAVMTYDFHGHWDKktghVAPLYHHPDDDFEyfnvnYSINYWMEKG-APSQKLV 1204
Cdd:cd06545 137 AAVSSWN-----GGAVSDSTlAYFDFINIMSYDATGPWWG----DNPGQHSSYDDAV-----NDLNYWNERGlASKDKLV 202
|
250
....*....|.
gi 442628919 1205 MGIPLYGQSFT 1215
Cdd:cd06545 203 LGLPFYGYGFY 213
|
|
| GH18_CFLE_spore_hydrolase |
cd02874 |
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ... |
297-566 |
2.87e-20 |
|
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial endospore germination. CFLE is expressed as an inactive preprotein (called SleB) in the forespore compartment of sporulating cells. SleB translocates across the forespore inner membrane and is deposited as a mature enzyme in the cortex layer of the spore. As part of a sensory mechanism capable of initiating germination, CFLE degrades a spore-specific peptidoglycan constituent called muramic-acid delta-lactam that comprises the outer cortex. CFLE has a C-terminal glycosyl hydrolase family 18 (GH18) catalytic domain as well as two N-terminal LysM peptidoglycan-binding domains. In addition to SleB, this family includes YaaH, YdhD, and YvbX from Bacillus subtilis.
Pssm-ID: 119353 [Multi-domain] Cd Length: 313 Bit Score: 94.25 E-value: 2.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 297 TDSSGSKYSRLVSDNLKRRVFISSVSSFLLRHGFSGLHLDWNYPkcwqsdcsrgPVTDRPNLTKLLRELRTEFQSvdPKF 376
Cdd:cd02874 71 GNFDSELAHAVLSNPEARQRLINNILALAKKYGYDGVNIDFENV----------PPEDREAYTQFLRELSDRLHP--AGY 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 377 QLGVAI-----SGYKEIIKEAYDFPALSDIVDYMTVMTYDYHGAWeQKTGHVSPLYGLSSdtypqyNTNYTMQlllKMga 451
Cdd:cd02874 139 TLSTAVvpktsADQFGNWSGAYDYAAIGKIVDFVVLMTYDWHWRG-GPPGPVAPIGWVER------VLQYAVT---QI-- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 452 RREKLVLSIPFYGQSFTLatahQILAGPGVAASGPGDAgeltkqpgmlayyeicqrltkFNWISDRNLNVIFGP------ 525
Cdd:cd02874 207 PREKILLGIPLYGYDWTL----PYKKGGKASTISPQQA---------------------INLAKRYGAEIQYDEeaqspf 261
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 442628919 526 FAMLNDQ----WVGYEDPTSAQAKARYAANNNFAGVAAWTIDLDD 566
Cdd:cd02874 262 FRYVDEQgrrhEVWFEDARSLQAKFELAKEYGLRGVSYWRLGLED 306
|
|
| GH18_3CO4_chitinase |
cd06545 |
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an ... |
1910-2158 |
5.40e-14 |
|
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: 74.03 E-value: 5.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1910 VVCYFTSWAWYRSSQGKfvpedIDANLCTHLIYGFAVLD-SKSLTIKTHDSwtDIdnrfyERVVE-YKQRGLRVMLAIGG 1987
Cdd:cd06545 1 VVGYLPNYDDLNALSPT-----IDFSKLTHINLAFANPDaNGTLNANPVRS--EL-----NSVVNaAHAHNVKILISLAG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1988 wndSLGSKYARLVLNSQSRRRFVASVISFLEQHGFEGLDLAWEFPVCWQVNcnrgnpteKDGFVAlvkELSEAFKENGLI 2067
Cdd:cd06545 69 ---GSPPEFTAALNDPAKRKALVDKIINYVVSYNLDGIDVDLEGPDVTFGD--------YLVFIR---ALYAALKKEGKL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 2068 LSAAVSpskmvidaGYNVFELS----PYFDWVAVMTYDFHGHWdmRTGQiaplfhrGGDENLYLNGNFSIHYWLERG-IP 2142
Cdd:cd06545 135 LTAAVS--------SWNGGAVSdstlAYFDFINIMSYDATGPW--WGDN-------PGQHSSYDDAVNDLNYWNERGlAS 197
|
250
....*....|....*.
gi 442628919 2143 NDKLVMGMPMYGQTFT 2158
Cdd:cd06545 198 KDKLVLGLPFYGYGFY 213
|
|
| GH18_chitobiase |
cd02875 |
Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes ... |
1060-1312 |
3.58e-13 |
|
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: 73.62 E-value: 3.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1060 PMARSRFVRHALEFIEKYGFEGLDLDWEYPVcwqtecNKGStEEKDGFTAWVQELSEAFRP--RGLMLSTAVSPSRKIID 1137
Cdd:cd02875 94 PTYRTQWIQQKVELAKSQFMDGINIDIEQPI------TKGS-PEYYALTELVKETTKAFKKenPGYQISFDVAWSPSCID 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1138 -AGYDIPQLSRYFDWIAVMTYDFHGH-WDKK--TGHVAPlyhhpdddfeYFNVNYSINYWMEKGAPSQKLVMGIPLYGQS 1213
Cdd:cd02875 167 kRCYDYTGIADASDFLVVMDYDEQSQiWGKEciAGANSP----------YSQTLSGYNNFTKLGIDPKKLVMGLPWYGYD 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1214 FTLENTN-SSGLNAKAPAPGEAGEFTRAAGF-LAYYEICERVNRQGWQVVHDEFGRMGPYAYKGTQ----WVSYDSPDMV 1287
Cdd:cd02875 237 YPCLNGNlEDVVCTIPKVPFRGANCSDAAGRqIPYSEIMKQINSSIGGRLWDSEQKSPFYNYKDKQgnlhQVWYDNPQSL 316
|
250 260
....*....|....*....|....*
gi 442628919 1288 RKKSLLVRSLKLGGGMVWALDLDDF 1312
Cdd:cd02875 317 SIKVAYAKNLGLKGIGMWNGDLLDY 341
|
|
| GH18_chitobiase |
cd02875 |
Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes ... |
1994-2258 |
5.04e-13 |
|
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: 72.85 E-value: 5.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1994 SKYARLVL----------NSQSRRRFVASVISFLEQHGFEGLDLAWEFPVcwqvncNRGnPTEKDGFVALVKELSEAFK- 2062
Cdd:cd02875 75 SKGVRLVLkgdvpleqisNPTYRTQWIQQKVELAKSQFMDGINIDIEQPI------TKG-SPEYYALTELVKETTKAFKk 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 2063 EN-GLILSAAVSPSKMVID-AGYNVFELSPYFDWVAVMTYDfhghwdMRTgQIAPLFHRGGDENLYLNGNFSIHYWLERG 2140
Cdd:cd02875 148 ENpGYQISFDVAWSPSCIDkRCYDYTGIADASDFLVVMDYD------EQS-QIWGKECIAGANSPYSQTLSGYNNFTKLG 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 2141 IPNDKLVMGMPMYGQTFTLADQNRRSlNDKTVG--PGKAGTFTRADGFLAYYEICEKVVNDDWKVVR-DEEG---IFGSY 2214
Cdd:cd02875 221 IDPKKLVMGLPWYGYDYPCLNGNLED-VVCTIPkvPFRGANCSDAAGRQIPYSEIMKQINSSIGGRLwDSEQkspFYNYK 299
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 442628919 2215 AYSGNQ---WisYDDVTTIRRKSQFIKSLQLGGGMIWALDLDDFRGL 2258
Cdd:cd02875 300 DKQGNLhqvW--YDNPQSLSIKVAYAKNLGLKGIGMWNGDLLDYSGL 344
|
|
| GH18_chitobiase |
cd02875 |
Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes ... |
358-567 |
2.62e-12 |
|
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: 70.92 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 358 LTKLLRELRTEFQSVDPKFQLG--VAISGyKEIIKEAYDFPALSDIVDYMTVMTYDyhgawEQKtgHVSPLYGLSSDTYP 435
Cdd:cd02875 134 LTELVKETTKAFKKENPGYQISfdVAWSP-SCIDKRCYDYTGIADASDFLVVMDYD-----EQS--QIWGKECIAGANSP 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 436 QYNTNYTMQLLLKMGARREKLVLSIPFYGQSFT---LATAHQILAGPGVAASGPGDAGELTKQpgmLAYYEICQRLTK-- 510
Cdd:cd02875 206 YSQTLSGYNNFTKLGIDPKKLVMGLPWYGYDYPclnGNLEDVVCTIPKVPFRGANCSDAAGRQ---IPYSEIMKQINSsi 282
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442628919 511 ------------FNWISDrnlnvifgPFAMLNDQWvgYEDPTSAQAKARYAANNNFAGVAAWTIDLDDF 567
Cdd:cd02875 283 ggrlwdseqkspFYNYKD--------KQGNLHQVW--YDNPQSLSIKVAYAKNLGLKGIGMWNGDLLDY 341
|
|
| GH18_chitobiase |
cd02875 |
Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes ... |
1503-1755 |
1.21e-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: 68.61 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1503 NPEARSRFIRNVLDFIEEYNFDGLDLDWEYPVcwqvdckKGTAEEKIGFSALVRELFYAFQP--RGLILSAAVSPNKKVI 1580
Cdd:cd02875 93 NPTYRTQWIQQKVELAKSQFMDGINIDIEQPI-------TKGSPEYYALTELVKETTKAFKKenPGYQISFDVAWSPSCI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1581 D-AGYEVAELSHYFSWISVMAYDYHGQ-WDKktghvapmyshpEGTANFNANFS-----MNYWISMGADRRKLVMGIPLY 1653
Cdd:cd02875 166 DkRCYDYTGIADASDFLVVMDYDEQSQiWGK------------ECIAGANSPYSqtlsgYNNFTKLGIDPKKLVMGLPWY 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1654 GQSFSL----AETTKHQLNAPTYGGGEAGEATrarGFLAYYEICLKIRHH-----RWNVVRDTkgrigPFAYHGD----- 1719
Cdd:cd02875 234 GYDYPClngnLEDVVCTIPKVPFRGANCSDAA---GRQIPYSEIMKQINSsiggrLWDSEQKS-----PFYNYKDkqgnl 305
|
250 260 270
....*....|....*....|....*....|....*.
gi 442628919 1720 QWVSFDDVPMIRHKSEYIKAMGLGGAMIWALDLDDF 1755
Cdd:cd02875 306 HQVWYDNPQSLSIKVAYAKNLGLKGIGMWNGDLLDY 341
|
|
| CBM_14 |
pfam01607 |
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ... |
875-918 |
5.41e-11 |
|
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: 5.41e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 442628919 875 VPYPGNCSKYLFCLWNRLQASDCPPGLHYNERIGNCDWPA-AAKC 918
Cdd:pfam01607 9 YADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDnVVDC 53
|
|
| ChtBD2 |
smart00494 |
Chitin-binding domain type 2; |
874-913 |
8.92e-10 |
|
Chitin-binding domain type 2;
Pssm-ID: 214696 [Multi-domain] Cd Length: 49 Bit Score: 55.91 E-value: 8.92e-10
10 20 30 40
....*....|....*....|....*....|....*....|
gi 442628919 874 RVPYPGNCSKYLFCLWNRLQASDCPPGLHYNERIGNCDWP 913
Cdd:smart00494 10 LYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDWP 49
|
|
| CBM_14 |
pfam01607 |
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ... |
801-848 |
9.41e-10 |
|
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: 56.27 E-value: 9.41e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 442628919 801 TEGDYYPHRNCRKYYICVNKALVPSECGGDLHWDGIKKLCDWPEN-VQC 848
Cdd:pfam01607 5 EDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNvVDC 53
|
|
| GH18_SI-CLP |
cd02876 |
Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein ... |
291-477 |
1.79e-09 |
|
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: 61.56 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 291 IALGGWTDSSgskYSRLVSDNLKRRVFISSVSSFLLRHGFSGLHLD-WNYpkcWQSDcsrGPVTDRPNLTKLLRELRTEF 369
Cdd:cd02876 73 VLFEGWSYQD---LQSLLNDEQEREKLIKLLVTTAKKNHFDGIVLEvWSQ---LAAY---GVPDKRKELIQLVIHLGETL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 370 QSVDPKFQLGVAISGYKEIIKEAY---DFPALSDIVDYMTVMTYDYHGAweQKTGHVSPLYGLssdtypqyntNYTMQLL 446
Cdd:cd02876 144 HSANLKLILVIPPPREKGNQNGLFtrkDFEKLAPHVDGFSLMTYDYSSP--QRPGPNAPLSWV----------RSCLELL 211
|
170 180 190
....*....|....*....|....*....|....*...
gi 442628919 447 LKM-GARREKLVLSIPFYGQSFTLA------TAHQILA 477
Cdd:cd02876 212 LPEsGKKRAKILLGLNFYGNDYTLPggggaiTGSEYLK 249
|
|
| GH18_EndoS-like |
cd06542 |
Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of ... |
1030-1174 |
2.10e-09 |
|
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: 60.47 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1030 SLKSKGIKVSLALGGWNDSQGDKYSRlvrSPMARSRFVRHALEFIEKYGFEGLDLDWEYpvcWQTECNKGSTEEKDGFTA 1109
Cdd:cd06542 59 PLQAKGTKVLLSILGNHLGAGFANNL---SDAAAKAYAKAIVDTVDKYGLDGVDFDDEY---SGYGKNGTSQPSNEAFVR 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1110 WVQELSEAFRPRGLMLstavspsrkIID-----AGYDIPQLSRYFDWIAVMTYdfhGHWDKKTGHVAPLY 1174
Cdd:cd06542 133 LIKELRKYMGPTDKLL---------TIDgygqaLSNDGEEVSPYVDYVIYQYY---GSSSSSTQRNWNTN 190
|
|
| ChtBD2 |
smart00494 |
Chitin-binding domain type 2; |
697-737 |
7.53e-09 |
|
Chitin-binding domain type 2;
Pssm-ID: 214696 [Multi-domain] Cd Length: 49 Bit Score: 53.60 E-value: 7.53e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 442628919 697 FFADSNNCNAYYHCFfAGELQQQFCPSGLHWNNEAKGCDWP 737
Cdd:smart00494 10 LYPHPTDCSKYYQCS-NGRPIVGSCPAGLVFNPATQTCDWP 49
|
|
| ChtBD2 |
smart00494 |
Chitin-binding domain type 2; |
1834-1871 |
7.83e-09 |
|
Chitin-binding domain type 2;
Pssm-ID: 214696 [Multi-domain] Cd Length: 49 Bit Score: 53.22 E-value: 7.83e-09
10 20 30 40
....*....|....*....|....*....|....*....|
gi 442628919 1834 YLAHEWDCTKYYICEHGTYVERSCPLGLQWNKT--YCDWP 1871
Cdd:smart00494 10 LYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPAtqTCDWP 49
|
|
| CBM_14 |
pfam01607 |
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ... |
697-742 |
1.20e-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: 52.80 E-value: 1.20e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 442628919 697 FFADSNNCNAYYHCFFaGELQQQFCPSGLHWNNEAKGCDWPSS-AQC 742
Cdd:pfam01607 8 YYADPGDCSKYYVCSN-GEAVEFTCPNGLVFDPTLGICDYPDNvVDC 53
|
|
| CBM_14 |
pfam01607 |
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ... |
1834-1874 |
4.04e-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: 51.65 E-value: 4.04e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 442628919 1834 YLAHEWDCTKYYICEHGTYVERSCPLGLQWNKT--YCDWPTNV 1874
Cdd:pfam01607 8 YYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTlgICDYPDNV 50
|
|
| ChtBD2 |
smart00494 |
Chitin-binding domain type 2; |
799-843 |
6.25e-08 |
|
Chitin-binding domain type 2;
Pssm-ID: 214696 [Multi-domain] Cd Length: 49 Bit Score: 50.91 E-value: 6.25e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 442628919 799 ECTEGD--YYPH-RNCRKYYICVNKALVPSECGGDLHWDGIKKLCDWP 843
Cdd:smart00494 2 ECPGRGdgLYPHpTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDWP 49
|
|
| GH18_chitinase_D-like |
cd02871 |
GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes ... |
1468-1627 |
2.86e-07 |
|
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: 54.65 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1468 FYERIVAYRKKGAKVTVAIGGWNDSAgdkysrLVRNPEARSRFIRNVLDFIEEYNFDGLDLDWEypvcwQVDCKKGTAEE 1547
Cdd:cd02871 62 FKADIKALQAKGKKVLISIGGANGHV------DLNHTAQEDNFVDSIVAIIKEYGFDGLDIDLE-----SGSNPLNATPV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1548 KIGFSALVRELFYAFQPrGLILSAA--------VSPNKKVIDAGY-EVAE-LSHYFSWISVMAYDYHG--QWDKKtghva 1615
Cdd:cd02871 131 ITNLISALKQLKDHYGP-NFILTMApetpyvqgGYAAYGGIWGAYlPLIDnLRDDLTWLNVQYYNSGGmgGCDGQ----- 204
|
170
....*....|..
gi 442628919 1616 pmySHPEGTANF 1627
Cdd:cd02871 205 ---SYSQGTADF 213
|
|
| GH18_trifunctional |
cd06549 |
GH18 domain of an uncharacterized family of bacterial proteins, which share a common ... |
1456-1654 |
6.79e-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: 53.57 E-value: 6.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1456 QPHDSWADLDNKFYERIVAYRKKGAKVTVAIggwNDSAGDKYS-----RLVRNPEARSRFIRNVLDFIEEYNFDGLDLDW 1530
Cdd:cd06549 36 GPEGRIDVFVDPQGVAIIAAAKAHPKVLPLV---QNISGGAWDgkniaRLLADPSARAKFIANIAAYLERNQADGIVLDF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1531 EypvcwqvdckKGTAEEKIGFSALVRELFYAFQPRGLILSAAVSpnkkVIDAGYEVAELSHYFSWISVMAYDYHGQWdkk 1610
Cdd:cd06549 113 E----------ELPADDLPKYVAFLSELRRRLPAQGKQLTVTVP----ADEADWNLKALARNADKLILMAYDEHYQG--- 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 442628919 1611 tGHVAPMYSHPEGTANFNANFSmnywismGADRRKLVMGIPLYG 1654
Cdd:cd06549 176 -GAPGPIASQDWFESNLAQAVK-------KLPPEKLIVALGSYG 211
|
|
| GH18_EndoS-like |
cd06542 |
Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of ... |
1476-1650 |
1.36e-06 |
|
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: 52.00 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1476 RKKGAKVTVAIGGWNDSAGDKYSRlvrNPEARSRFIRNVLDFIEEYNFDGLDLDWEYPVCWQVDCKKGTAEEkigFSALV 1555
Cdd:cd06542 61 QAKGTKVLLSILGNHLGAGFANNL---SDAAAKAYAKAIVDTVDKYGLDGVDFDDEYSGYGKNGTSQPSNEA---FVRLI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1556 RELFYAFQPRGLILSAAVSPNkKVIDAGYEVAELSHYFswisvmAYDYHGQWDKKTGHVA-------PM------YSHPE 1622
Cdd:cd06542 135 KELRKYMGPTDKLLTIDGYGQ-ALSNDGEEVSPYVDYV------IYQYYGSSSSSTQRNWntnspkiPPekmvytESFEE 207
|
170 180
....*....|....*....|....*...
gi 442628919 1623 GTANFNANFSMNYWISMGADRRKLVMGI 1650
Cdd:cd06542 208 ENGGNSGSSAEQYARWTPAKGGKGGIGT 235
|
|
| GH18_SI-CLP |
cd02876 |
Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein ... |
1044-1219 |
4.02e-06 |
|
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: 51.15 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1044 GWNDSQgdkYSRLVRSPMARSRFVRHALEFIEKYGFEGLDLdwEYpvcWQTECNKGSTEEKDGFTAWVQELSEAFRPRGL 1123
Cdd:cd02876 77 GWSYQD---LQSLLNDEQEREKLIKLLVTTAKKNHFDGIVL--EV---WSQLAAYGVPDKRKELIQLVIHLGETLHSANL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1124 MLSTAVSPSRKIIDAGY-----DIPQLSRYFDWIAVMTYDFHGhwDKKTGHVAPLYHhpdddfeyfnVNYSINYWM-EKG 1197
Cdd:cd02876 149 KLILVIPPPREKGNQNGlftrkDFEKLAPHVDGFSLMTYDYSS--PQRPGPNAPLSW----------VRSCLELLLpESG 216
|
170 180
....*....|....*....|..
gi 442628919 1198 APSQKLVMGIPLYGQSFTLENT 1219
Cdd:cd02876 217 KKRAKILLGLNFYGNDYTLPGG 238
|
|
| GH18_trifunctional |
cd06549 |
GH18 domain of an uncharacterized family of bacterial proteins, which share a common ... |
290-464 |
5.25e-06 |
|
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: 50.87 E-value: 5.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 290 LIALGGWTdssGSKYSRLVSDNLKRRVFISSVSSFLLRHGFSGLHLDWNypkcwqsdcsRGPVTDRPNLTKLLRELRTEF 369
Cdd:cd06549 68 NISGGAWD---GKNIARLLADPSARAKFIANIAAYLERNQADGIVLDFE----------ELPADDLPKYVAFLSELRRRL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 370 QSVDPKFQLGVAISGykeiikEAYDFPALSDIVDYMTVMTYDYHGAWeqktGHVSPlygLSSDTYpqyntnYTMQLLLKM 449
Cdd:cd06549 135 PAQGKQLTVTVPADE------ADWNLKALARNADKLILMAYDEHYQG----GAPGP---IASQDW------FESNLAQAV 195
|
170
....*....|....*.
gi 442628919 450 -GARREKLVLSIPFYG 464
Cdd:cd06549 196 kKLPPEKLIVALGSYG 211
|
|
| GH18_trifunctional |
cd06549 |
GH18 domain of an uncharacterized family of bacterial proteins, which share a common ... |
1986-2154 |
5.35e-06 |
|
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: 50.87 E-value: 5.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1986 GGWNdslGSKYARLVLNSQSRRRFVASVISFLEQHGFEGLDLAWEfpvcwqvncnRGNPTEKDGFVALVKELSEAFKENG 2065
Cdd:cd06549 72 GAWD---GKNIARLLADPSARAKFIANIAAYLERNQADGIVLDFE----------ELPADDLPKYVAFLSELRRRLPAQG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 2066 LILSAAVsPSKmviDAGYNVFELSPYFDWVAVMTYDFHGHWDmRTGQIAPlfhrggdenlylngnfsiHYWLE------- 2138
Cdd:cd06549 139 KQLTVTV-PAD---EADWNLKALARNADKLILMAYDEHYQGG-APGPIAS------------------QDWFEsnlaqav 195
|
170
....*....|....*.
gi 442628919 2139 RGIPNDKLVMGMPMYG 2154
Cdd:cd06549 196 KKLPPEKLIVALGSYG 211
|
|
| GH18_CTS3_chitinase |
cd06546 |
GH18 domain of CTS3 (chitinase 3), an uncharacterized protein from the human fungal pathogen ... |
1439-1533 |
8.91e-06 |
|
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: 49.64 E-value: 8.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1439 THIIYGFAVLSRD-NLTI---QPHDS-----WADLDnkfyerivAYRKKGAKVTVAIGGWndsAGDKYSRLVRNPEARSR 1509
Cdd:cd06546 31 THLIVAALHINDDgNIHLndhPPDHPrfttlWTELA--------ILQSSGVKVMGMLGGA---APGSFSRLDDDDEDFER 99
|
90 100
....*....|....*....|....
gi 442628919 1510 FIRNVLDFIEEYNFDGLDLDWEYP 1533
Cdd:cd06546 100 YYGQLRDMIRRRGLDGLDLDVEEP 123
|
|
| GH18_CTS3_chitinase |
cd06546 |
GH18 domain of CTS3 (chitinase 3), an uncharacterized protein from the human fungal pathogen ... |
1909-2072 |
3.28e-05 |
|
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: 47.71 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1909 KVVCYFTSwawYRSSQGKFVPEDI-----DANLcTHLIYG-FAVLDSKSLTIKTH---DS-----WTDIDnrfyervvEY 1974
Cdd:cd06546 1 RLVIYYQT---THPSNGDPISSLLlvtekGIAL-THLIVAaLHINDDGNIHLNDHppdHPrfttlWTELA--------IL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1975 KQRGLRVMLAIGGWndSLGSkYARLVLNSQSRRRFVASVISFLEQHGFEGLDLAWEfpvcwqvncnrgNPTEKDGFVALV 2054
Cdd:cd06546 69 QSSGVKVMGMLGGA--APGS-FSRLDDDDEDFERYYGQLRDMIRRRGLDGLDLDVE------------EPMSLDGIIRLI 133
|
170
....*....|....*...
gi 442628919 2055 KELSEAFKENGLILSAAV 2072
Cdd:cd06546 134 DRLRSDFGPDFIITLAPV 151
|
|
| GH18_SI-CLP |
cd02876 |
Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein ... |
1987-2162 |
4.72e-05 |
|
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: 47.69 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1987 GWNDSLgskYARLVLNSQSRRRFVASVISFLEQHGFEGLDL-AWefpVCWQVncnRGNPTEKDGFVALVKELSEAFKENG 2065
Cdd:cd02876 77 GWSYQD---LQSLLNDEQEREKLIKLLVTTAKKNHFDGIVLeVW---SQLAA---YGVPDKRKELIQLVIHLGETLHSAN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 2066 LILSAAVSPSKMVIDAGYNV----FE-LSPYFDWVAVMTYDFHGhwDMRTGQIAPLfhrggdenlylngnfsihYWLERG 2140
Cdd:cd02876 148 LKLILVIPPPREKGNQNGLFtrkdFEkLAPHVDGFSLMTYDYSS--PQRPGPNAPL------------------SWVRSC 207
|
170 180 190
....*....|....*....|....*....|.
gi 442628919 2141 I----PND-----KLVMGMPMYGQTFTLADQ 2162
Cdd:cd02876 208 LelllPESgkkraKILLGLNFYGNDYTLPGG 238
|
|
| GH18_trifunctional |
cd06549 |
GH18 domain of an uncharacterized family of bacterial proteins, which share a common ... |
1038-1211 |
6.05e-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: 47.41 E-value: 6.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1038 VSLALGGWNDSQGdkYSRLVRSPMARSRFVRHALEFIEKYGFEGLDLDWEypvcwqtecnKGSTEEKDGFTAWVQELSEA 1117
Cdd:cd06549 66 VQNISGGAWDGKN--IARLLADPSARAKFIANIAAYLERNQADGIVLDFE----------ELPADDLPKYVAFLSELRRR 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1118 FRPRGLMLSTAVsPSRkiiDAGYDIPQLSRYFDWIAVMTYDFHGhwdkKTGHVAPLYhhPDDDFEYfNVNYSInywmeKG 1197
Cdd:cd06549 134 LPAQGKQLTVTV-PAD---EADWNLKALARNADKLILMAYDEHY----QGGAPGPIA--SQDWFES-NLAQAV-----KK 197
|
170
....*....|....
gi 442628919 1198 APSQKLVMGIPLYG 1211
Cdd:cd06549 198 LPPEKLIVALGSYG 211
|
|
| GH18_3CO4_chitinase |
cd06545 |
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an ... |
286-468 |
6.77e-05 |
|
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: 46.68 E-value: 6.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 286 GVPVLIALGGwtdSSGSKYSRLVSDNLKRRVFISSVSSFLLRHGFSGLHLDWnypkcwqsdcsRGPVTDRPNLTKLLREL 365
Cdd:cd06545 59 NVKILISLAG---GSPPEFTAALNDPAKRKALVDKIINYVVSYNLDGIDVDL-----------EGPDVTFGDYLVFIRAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 366 RTEFQSVDPKFQLGVAiSGYKEIIKEAYdFPALsdivDYMTVMTYDYHGAWEQKTG--HVSplYglsSDTYPQYNTnYTM 443
Cdd:cd06545 125 YAALKKEGKLLTAAVS-SWNGGAVSDST-LAYF----DFINIMSYDATGPWWGDNPgqHSS--Y---DDAVNDLNY-WNE 192
|
170 180
....*....|....*....|....*
gi 442628919 444 QLLLKmgarREKLVLSIPFYGQSFT 468
Cdd:cd06545 193 RGLAS----KDKLVLGLPFYGYGFY 213
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
1465-1531 |
9.26e-05 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 47.44 E-value: 9.26e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442628919 1465 DNKFYERIVAYRKKGAKVTVAIGGWNDSAgdkysrLVRNPEARSRFIRNVLDFIEEYNFDGLDLDWE 1531
Cdd:COG3469 274 DAQFKADIAALQAQGKKVLLSIGGANGTV------QLNTAAAADNFVNSVIALIDEYGFDGLDIDLE 334
|
|
| GH18_chitinase_D-like |
cd02871 |
GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes ... |
1975-2151 |
2.77e-04 |
|
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: 45.40 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1975 KQRGLRVMLAIGGwndslgsKYARLVLNS-QSRRRFVASVISFLEQHGFEGLDLAWEfpvcwQVNCNRGNPTEKDGFVAL 2053
Cdd:cd02871 70 QAKGKKVLISIGG-------ANGHVDLNHtAQEDNFVDSIVAIIKEYGFDGLDIDLE-----SGSNPLNATPVITNLISA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 2054 VKELSEAFKENgLILSAA------VSPSKMVIDAGYNVFE----LSPYFDWVAVMTY----------DFH--GHWDMRTG 2111
Cdd:cd02871 138 LKQLKDHYGPN-FILTMApetpyvQGGYAAYGGIWGAYLPlidnLRDDLTWLNVQYYnsggmggcdgQSYsqGTADFLVA 216
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 442628919 2112 QIAPLFHRGGDENlylNGNFSihywlerGIPNDKLVMGMP 2151
Cdd:cd02871 217 LADMLLTGFPIAG---NDRFP-------PLPADKVVIGLP 246
|
|
| GH18_chitinase_D-like |
cd02871 |
GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes ... |
1028-1157 |
2.97e-04 |
|
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: 45.40 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1028 VTSLKSKGIKVSLALGGWNDSQgdkysrLVRSPMARSRFVRHALEFIEKYGFEGLDLDWEypvcwQTECNKGSTEEKDGF 1107
Cdd:cd02871 66 IKALQAKGKKVLISIGGANGHV------DLNHTAQEDNFVDSIVAIIKEYGFDGLDIDLE-----SGSNPLNATPVITNL 134
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442628919 1108 TAWVQELSEAFRPrGLMLSTAvsPSRKIIDAGYD------------IPQLSRYFDWIAVMTY 1157
Cdd:cd02871 135 ISALKQLKDHYGP-NFILTMA--PETPYVQGGYAayggiwgaylplIDNLRDDLTWLNVQYY 193
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
1028-1087 |
8.31e-04 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 44.36 E-value: 8.31e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1028 VTSLKSKGIKVSLALGGWNDSQgdkysrLVRSPMARSRFVRHALEFIEKYGFEGLDLDWE 1087
Cdd:COG3469 281 IAALQAQGKKVLLSIGGANGTV------QLNTAAAADNFVNSVIALIDEYGFDGLDIDLE 334
|
|
| GH18_SI-CLP |
cd02876 |
Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein ... |
1484-1659 |
1.94e-03 |
|
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: 42.68 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1484 VAIGGWNdsaGDKYSRLVRNPEARSRFIRNVLDFIEEYNFDGLDLdwEYPVCWQVDckkGTAEEKIGFSALVRELFYAFQ 1563
Cdd:cd02876 73 VLFEGWS---YQDLQSLLNDEQEREKLIKLLVTTAKKNHFDGIVL--EVWSQLAAY---GVPDKRKELIQLVIHLGETLH 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628919 1564 PRGLILSAAVSPNKKVIDAGYEVAE-----LSHYFSWISVMAYDYHGQwdKKTGHVAPMyshpegtanfnanfsmnYWI- 1637
Cdd:cd02876 145 SANLKLILVIPPPREKGNQNGLFTRkdfekLAPHVDGFSLMTYDYSSP--QRPGPNAPL-----------------SWVr 205
|
170 180 190
....*....|....*....|....*....|
gi 442628919 1638 --------SMGADRRKLVMGIPLYGQSFSL 1659
Cdd:cd02876 206 sclelllpESGKKRAKILLGLNFYGNDYTL 235
|
|
| GH18_CTS3_chitinase |
cd06546 |
GH18 domain of CTS3 (chitinase 3), an uncharacterized protein from the human fungal pathogen ... |
1025-1089 |
5.84e-03 |
|
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: 40.78 E-value: 5.84e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442628919 1025 YTRVTSLKSKGIKVSLALGGWndSQGdKYSRLVRSPMARSRFVRHALEFIEKYGFEGLDLDWEYP 1089
Cdd:cd06546 62 WTELAILQSSGVKVMGMLGGA--APG-SFSRLDDDDEDFERYYGQLRDMIRRRGLDGLDLDVEEP 123
|
|
| |
