|
Name |
Accession |
Description |
Interval |
E-value |
| ChiA |
COG3325 |
Chitinase, GH18 family [Carbohydrate transport and metabolism]; |
26-444 |
0e+00 |
|
Chitinase, GH18 family [Carbohydrate transport and metabolism];
Pssm-ID: 442554 [Multi-domain] Cd Length: 391 Bit Score: 538.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 26 FNGESAKASSDKSYKIIGYYPSWGAYGRDFQVWDMDASKVSHINYAFADICwegrhgnvrptgpnpqtwscqdengvidv 105
Cdd:COG3325 6 VSDTAAAATATSGKRVVGYFTQWGIYGRNYLVKDIPASKLTHINYAFANVD----------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 106 PNGSIVMGDPWIDVQKSNAGDTWDEPIRGNFKQLLKLKKNHPHLKTFISVGGWSWSNRFSDVAADPAARENFAASAVNML 185
Cdd:COG3325 57 PDGKCSVGDAWAKPSVDGAADDWDQPLKGNFNQLKKLKAKNPNLKVLISIGGWTWSKGFSDAAATPASRAAFVDSCVDLL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 186 RKYGFDGVDLDWEYPVSGGLPGNSTRPEDKRNYTLLLQDVREKLDAAEAKDGKKYLLTTVSGASPEYVSNTELDKIAETV 265
Cdd:COG3325 137 RKYNFDGIDIDWEYPGSGGAPGNVYRPEDKANFTALLKELRAQLDALGAETGKHYLLTAAAPAGPDKLDGIELPKVAQYL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 266 DWINIMTYDYNGGWQSISAHNAPLFYDPKAkeagvPNAETFNIESTVKRYKEAGVKADKLVLGTPFYGRGWSNCEPADNG 345
Cdd:COG3325 217 DYVNVMTYDFHGAWSPTTGHQAPLYDSPKD-----PEAQGYSVDSAVQAYLAAGVPASKLVLGVPFYGRGWTGVTGGNNG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 346 EYQKCGPAKEGTWEKGVFDFSDLEKNYINKNGYKRYWNDRAKVPFLYNAENGNFITYDDEESYGYKTDLIQSNGLSGAMF 425
Cdd:COG3325 292 LYQPATGPAPGTWEAGVNDYKDLKALYLGSNGYTRYWDDVAKAPYLYNGDTGTFISYDDPRSIAAKADYVKDKGLGGVMF 371
|
410 420
....*....|....*....|
gi 700653897 426 WDFSGDSHQ-TLLNKLAADL 444
Cdd:COG3325 372 WELSGDTADgTLLNAIGEGL 391
|
|
| GH18_chitinase |
cd06548 |
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ... |
41-431 |
8.23e-141 |
|
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: 411.25 E-value: 8.23e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 41 IIGYYPSWGAYGRDFQVWDM-DASKVSHINYAFADICwegrhgnvrptgpnpqtwscqdengvidvPNGSIVMGDPWIDV 119
Cdd:cd06548 1 VVGYFTNWGIYGRNYFVTDDiPADKLTHINYAFADID-----------------------------GDGGVVTSDDEAAD 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 120 Q----KSNAGDTWDEPIRGNFKQLLKLKKNHPHLKTFISVGGWSWSNRFSDVAADPAARENFAASAVNMLRKYGFDGVDL 195
Cdd:cd06548 52 EaaqsVDGGADTDDQPLKGNFGQLRKLKQKNPHLKILLSIGGWTWSGGFSDAAATEASRAKFADSAVDFIRKYGFDGIDI 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 196 DWEYPVSGGLPGNSTRPEDKRNYTLLLQDVREKLDAAEAKDGKKYLLTTVSGASPEYVSNTELDKIAETVDWINIMTYDY 275
Cdd:cd06548 132 DWEYPGSGGAPGNVARPEDKENFTLLLKELREALDALGAETGRKYLLTIAAPAGPDKLDKLEVAEIAKYLDFINLMTYDF 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 276 NGGWQSISAHNAPLFYDPKAkeagvpNAETFNIESTVKRYKEAGVKADKLVLGTPFYGRGWsncepadngeyqkcgpake 355
Cdd:cd06548 212 HGAWSNTTGHHSNLYASPAD------PPGGYSVDAAVNYYLSAGVPPEKLVLGVPFYGRGW------------------- 266
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 700653897 356 gtwekgvfdfsdleknyinkNGYKRYWNDRAKVPFLYNAENGNFITYDDEESYGYKTDLIQSNGLSGAMFWDFSGD 431
Cdd:cd06548 267 --------------------TGYTRYWDEVAKAPYLYNPSTKTFISYDDPRSIKAKADYVKDKGLGGVMFWELSGD 322
|
|
| Glyco_18 |
smart00636 |
Glyco_18 domain; |
40-431 |
5.16e-130 |
|
Glyco_18 domain;
Pssm-ID: 214753 [Multi-domain] Cd Length: 334 Bit Score: 384.34 E-value: 5.16e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 40 KIIGYYPSWGAYGRDFQVWDMDASKVSHINYAFADICwegrhgnvrptgpnpqtwscqdengvidvPNGSIVMGDPWIDV 119
Cdd:smart00636 1 RVVGYFTNWGVYGRNFPVDDIPASKLTHIIYAFANID-----------------------------PDGTVTIGDEWADI 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 120 qksnagdtwdepirGNFKQLLKLKKNHPHLKTFISVGGWSWSNRFSDVAADPAARENFAASAVNMLRKYGFDGVDLDWEY 199
Cdd:smart00636 52 --------------GNFGQLKALKKKNPGLKVLLSIGGWTESDNFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWEY 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 200 PVSGGlpgnstrpEDKRNYTLLLQDVREKLDAAEAKdGKKYLLTTVSGASPEYVSNTE--LDKIAETVDWINIMTYDYNG 277
Cdd:smart00636 118 PGGRG--------DDRENYTALLKELREALDKEGAE-GKGYLLTIAVPAGPDKIDKGYgdLPAIAKYLDFINLMTYDFHG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 278 GWQSISAHNAPLFYDPKAKEAgvpnaetFNIESTVKRYKEAGVKADKLVLGTPFYGRGWSNCEPADNGEYQ---KCGPAK 354
Cdd:smart00636 189 AWSNPTGHNAPLYAGPGDPEK-------YNVDYAVKYYLCKGVPPSKLVLGIPFYGRGWTLVDGSNNGPGApftGPATGG 261
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 700653897 355 EGTWEKGVFDFSDLEKNYinknGYKRYWNDRAKVPFLYNAENGNFITYDDEESYGYKTDLIQSNGLSGAMFWDFSGD 431
Cdd:smart00636 262 PGTWEGGVVDYREICKLL----GATVVYDDTAKAPYAYNPGTGQWVSYDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
|
|
| Glyco_hydro_18 |
pfam00704 |
Glycosyl hydrolases family 18; |
40-431 |
1.52e-100 |
|
Glycosyl hydrolases family 18;
Pssm-ID: 425828 [Multi-domain] Cd Length: 311 Bit Score: 307.84 E-value: 1.52e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 40 KIIGYYPSWGAYGRDFqvwDMDASKVSHINYAFADICWegrhgnvrptgpnpqtwscqdengvidvPNGSIVMGDpwidv 119
Cdd:pfam00704 1 RIVGYYTSWGVYRNGN---FLPSDKLTHIIYAFANIDG----------------------------SDGTLFIGD----- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 120 qksnagdtWDEpirGNFKQLLKLKKN-HPHLKTFISVGGWSWSNRFSDVAADPAARENFAASAVNMLRKYGFDGVDLDWE 198
Cdd:pfam00704 45 --------WDL---GNFEQLKKLKKQkNPGVKVLLSIGGWTDSTGFSLMASNPASRKKFADSIVSFLRKYGFDGIDIDWE 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 199 YPVSGglpgnstrPEDKRNYTLLLQDVREKLDaaEAKDGKKYLLT-TVSGASPEYVSNTELDKIAETVDWINIMTYDYNG 277
Cdd:pfam00704 114 YPGGN--------PEDKENYDLLLRELRAALD--EAKGGKKYLLSaAVPASYPDLDKGYDLPKIAKYLDFINVMTYDFHG 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 278 GWQSISAHNAPLFYDPKakeagvpnaetFNIESTVKRYKEAGVKADKLVLGTPFYGRGWSNCEPADNgeyqkcgpakegT 357
Cdd:pfam00704 184 SWDNVTGHHAPLYGGGS-----------YNVDYAVKYYLKQGVPASKLVLGVPFYGRSWTLVNGSGN------------T 240
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 700653897 358 WEKGVFDFSDLeKNYINKNGYKRYWNDRAKVPFLYNaeNGNFITYDDEESYGYKTDLIQSNGLSGAMFWDFSGD 431
Cdd:pfam00704 241 WEDGVLAYKEI-CNLLKDNGATVVWDDVAKAPYVYD--GDQFITYDDPRSIATKVDYVKAKGLGGVMIWSLDAD 311
|
|
| ChiC_BD |
cd12215 |
Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of ... |
548-591 |
4.76e-15 |
|
Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of Streptomyces griseus and related proteins. Chitinase C is a family 19 chitinase, and consists of a N-terminal chitin binding domain and a C-terminal chitin-catalytic domain that effects degradation. Chitinases function in invertebrates in the degradation of old exoskeletons, in fungi to utilize chitin in cell walls, and in bacteria which use chitin as an energy source. ChiC contains the characteristic chitin-binding aromatic residues.
Pssm-ID: 213178 [Multi-domain] Cd Length: 42 Bit Score: 69.14 E-value: 4.76e-15
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 700653897 548 NEWKGTAVYTGGDRVVFNGKVYEAKWWRQGEQPDQAgeSGVWKL 591
Cdd:cd12215 1 PAWDASTVYTGGDQVTYNGKVYEAKWWTQGEEPGTS--WGVWKL 42
|
|
| FN3 |
smart00060 |
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
458-527 |
2.69e-12 |
|
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.
Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 62.63 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 458 SAPDNLRVTEKTATSISLAWDAPSDANIAaSYVLSYEGG-----------AVSVKDTSATIGQLKPRTTYSFTVSAKDAD 526
Cdd:smart00060 2 SPPSNLRVTDVTSTSVTLSWEPPPDDGIT-GYIVGYRVEyreegsewkevNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80
|
.
gi 700653897 527 G 527
Cdd:smart00060 81 G 81
|
|
| FN3 |
cd00063 |
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ... |
458-528 |
9.00e-12 |
|
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.
Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 61.36 E-value: 9.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 458 SAPDNLRVTEKTATSISLAWDAPSDANIAA-SYVLSYEG---------GAVSVKDTSATIGQLKPRTTYSFTVSAKDADG 527
Cdd:cd00063 2 SPPTNLRVTDVTSTSVTLSWTPPEDDGGPItGYVVEYREkgsgdwkevEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81
|
.
gi 700653897 528 K 528
Cdd:cd00063 82 E 82
|
|
| ChtBD3 |
smart00495 |
Chitin-binding domain type 3; |
547-589 |
1.77e-10 |
|
Chitin-binding domain type 3;
Pssm-ID: 197760 [Multi-domain] Cd Length: 41 Bit Score: 56.12 E-value: 1.77e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 700653897 547 YNEWKGTAVYTGGDRVVFNGKVYEAKWWRQGEQPDQAgeSGVW 589
Cdd:smart00495 1 APAWQAGTVYTAGDVVSYNGKVYKAKWWTQGEEPGSS--SGPW 41
|
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
458-528 |
4.05e-09 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 53.57 E-value: 4.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 458 SAPDNLRVTEKTATSISLAWDAPSDANIA-ASYVLSY-----EGGAVSVKD----TSATIGQLKPRTTYSFTVSAKDADG 527
Cdd:pfam00041 1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPiTGYEVEYrpknsGEPWNEITVpgttTSVTLTGLKPGTEYEVRVQAVNGGG 80
|
.
gi 700653897 528 K 528
Cdd:pfam00041 81 E 81
|
|
| COG3979 |
COG3979 |
Chitodextrinase [Carbohydrate transport and metabolism]; |
456-560 |
1.41e-08 |
|
Chitodextrinase [Carbohydrate transport and metabolism];
Pssm-ID: 443178 [Multi-domain] Cd Length: 369 Bit Score: 57.09 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 456 PSSAPDNLRVTEKTATSISLAWDAPSDANIAASYVLSYEGGAVSVKD--TSATIGQLKPRTTYSFTVSAKDADGKLHTGP 533
Cdd:COG3979 2 APTAPTGLTASNVTSSSVSLSWDASTDNVGVTGYDVYRGGDQVATVTglTAWTVTGLTPGTEYTFTVGACDAAGNVSAAS 81
|
90 100
....*....|....*....|....*..
gi 700653897 534 TIEAATNSDQMIGYNEWKGTAVYTGGD 560
Cdd:COG3979 82 GTSTAMFGGSSTTLGSAEGVADTSGNL 108
|
|
| CBM_5_12 |
pfam02839 |
Carbohydrate binding domain; This short domain is found in many different glycosyl hydrolase ... |
564-589 |
2.56e-03 |
|
Carbohydrate binding domain; This short domain is found in many different glycosyl hydrolase enzymes and is presumed to have a carbohydrate binding function. The domain has six aromatic groups that may be important for binding.
Pssm-ID: 427014 Cd Length: 25 Bit Score: 35.65 E-value: 2.56e-03
10 20
....*....|....*....|....*.
gi 700653897 564 FNGKVYEAKWWRQGEQPDqAGESGVW 589
Cdd:pfam02839 1 HNGKAYQAKWWTQGGDPP-TSSGGPW 25
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ChiA |
COG3325 |
Chitinase, GH18 family [Carbohydrate transport and metabolism]; |
26-444 |
0e+00 |
|
Chitinase, GH18 family [Carbohydrate transport and metabolism];
Pssm-ID: 442554 [Multi-domain] Cd Length: 391 Bit Score: 538.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 26 FNGESAKASSDKSYKIIGYYPSWGAYGRDFQVWDMDASKVSHINYAFADICwegrhgnvrptgpnpqtwscqdengvidv 105
Cdd:COG3325 6 VSDTAAAATATSGKRVVGYFTQWGIYGRNYLVKDIPASKLTHINYAFANVD----------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 106 PNGSIVMGDPWIDVQKSNAGDTWDEPIRGNFKQLLKLKKNHPHLKTFISVGGWSWSNRFSDVAADPAARENFAASAVNML 185
Cdd:COG3325 57 PDGKCSVGDAWAKPSVDGAADDWDQPLKGNFNQLKKLKAKNPNLKVLISIGGWTWSKGFSDAAATPASRAAFVDSCVDLL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 186 RKYGFDGVDLDWEYPVSGGLPGNSTRPEDKRNYTLLLQDVREKLDAAEAKDGKKYLLTTVSGASPEYVSNTELDKIAETV 265
Cdd:COG3325 137 RKYNFDGIDIDWEYPGSGGAPGNVYRPEDKANFTALLKELRAQLDALGAETGKHYLLTAAAPAGPDKLDGIELPKVAQYL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 266 DWINIMTYDYNGGWQSISAHNAPLFYDPKAkeagvPNAETFNIESTVKRYKEAGVKADKLVLGTPFYGRGWSNCEPADNG 345
Cdd:COG3325 217 DYVNVMTYDFHGAWSPTTGHQAPLYDSPKD-----PEAQGYSVDSAVQAYLAAGVPASKLVLGVPFYGRGWTGVTGGNNG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 346 EYQKCGPAKEGTWEKGVFDFSDLEKNYINKNGYKRYWNDRAKVPFLYNAENGNFITYDDEESYGYKTDLIQSNGLSGAMF 425
Cdd:COG3325 292 LYQPATGPAPGTWEAGVNDYKDLKALYLGSNGYTRYWDDVAKAPYLYNGDTGTFISYDDPRSIAAKADYVKDKGLGGVMF 371
|
410 420
....*....|....*....|
gi 700653897 426 WDFSGDSHQ-TLLNKLAADL 444
Cdd:COG3325 372 WELSGDTADgTLLNAIGEGL 391
|
|
| GH18_chitinase |
cd06548 |
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ... |
41-431 |
8.23e-141 |
|
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: 411.25 E-value: 8.23e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 41 IIGYYPSWGAYGRDFQVWDM-DASKVSHINYAFADICwegrhgnvrptgpnpqtwscqdengvidvPNGSIVMGDPWIDV 119
Cdd:cd06548 1 VVGYFTNWGIYGRNYFVTDDiPADKLTHINYAFADID-----------------------------GDGGVVTSDDEAAD 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 120 Q----KSNAGDTWDEPIRGNFKQLLKLKKNHPHLKTFISVGGWSWSNRFSDVAADPAARENFAASAVNMLRKYGFDGVDL 195
Cdd:cd06548 52 EaaqsVDGGADTDDQPLKGNFGQLRKLKQKNPHLKILLSIGGWTWSGGFSDAAATEASRAKFADSAVDFIRKYGFDGIDI 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 196 DWEYPVSGGLPGNSTRPEDKRNYTLLLQDVREKLDAAEAKDGKKYLLTTVSGASPEYVSNTELDKIAETVDWINIMTYDY 275
Cdd:cd06548 132 DWEYPGSGGAPGNVARPEDKENFTLLLKELREALDALGAETGRKYLLTIAAPAGPDKLDKLEVAEIAKYLDFINLMTYDF 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 276 NGGWQSISAHNAPLFYDPKAkeagvpNAETFNIESTVKRYKEAGVKADKLVLGTPFYGRGWsncepadngeyqkcgpake 355
Cdd:cd06548 212 HGAWSNTTGHHSNLYASPAD------PPGGYSVDAAVNYYLSAGVPPEKLVLGVPFYGRGW------------------- 266
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 700653897 356 gtwekgvfdfsdleknyinkNGYKRYWNDRAKVPFLYNAENGNFITYDDEESYGYKTDLIQSNGLSGAMFWDFSGD 431
Cdd:cd06548 267 --------------------TGYTRYWDEVAKAPYLYNPSTKTFISYDDPRSIKAKADYVKDKGLGGVMFWELSGD 322
|
|
| Glyco_18 |
smart00636 |
Glyco_18 domain; |
40-431 |
5.16e-130 |
|
Glyco_18 domain;
Pssm-ID: 214753 [Multi-domain] Cd Length: 334 Bit Score: 384.34 E-value: 5.16e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 40 KIIGYYPSWGAYGRDFQVWDMDASKVSHINYAFADICwegrhgnvrptgpnpqtwscqdengvidvPNGSIVMGDPWIDV 119
Cdd:smart00636 1 RVVGYFTNWGVYGRNFPVDDIPASKLTHIIYAFANID-----------------------------PDGTVTIGDEWADI 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 120 qksnagdtwdepirGNFKQLLKLKKNHPHLKTFISVGGWSWSNRFSDVAADPAARENFAASAVNMLRKYGFDGVDLDWEY 199
Cdd:smart00636 52 --------------GNFGQLKALKKKNPGLKVLLSIGGWTESDNFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWEY 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 200 PVSGGlpgnstrpEDKRNYTLLLQDVREKLDAAEAKdGKKYLLTTVSGASPEYVSNTE--LDKIAETVDWINIMTYDYNG 277
Cdd:smart00636 118 PGGRG--------DDRENYTALLKELREALDKEGAE-GKGYLLTIAVPAGPDKIDKGYgdLPAIAKYLDFINLMTYDFHG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 278 GWQSISAHNAPLFYDPKAKEAgvpnaetFNIESTVKRYKEAGVKADKLVLGTPFYGRGWSNCEPADNGEYQ---KCGPAK 354
Cdd:smart00636 189 AWSNPTGHNAPLYAGPGDPEK-------YNVDYAVKYYLCKGVPPSKLVLGIPFYGRGWTLVDGSNNGPGApftGPATGG 261
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 700653897 355 EGTWEKGVFDFSDLEKNYinknGYKRYWNDRAKVPFLYNAENGNFITYDDEESYGYKTDLIQSNGLSGAMFWDFSGD 431
Cdd:smart00636 262 PGTWEGGVVDYREICKLL----GATVVYDDTAKAPYAYNPGTGQWVSYDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
|
|
| Glyco_hydro_18 |
pfam00704 |
Glycosyl hydrolases family 18; |
40-431 |
1.52e-100 |
|
Glycosyl hydrolases family 18;
Pssm-ID: 425828 [Multi-domain] Cd Length: 311 Bit Score: 307.84 E-value: 1.52e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 40 KIIGYYPSWGAYGRDFqvwDMDASKVSHINYAFADICWegrhgnvrptgpnpqtwscqdengvidvPNGSIVMGDpwidv 119
Cdd:pfam00704 1 RIVGYYTSWGVYRNGN---FLPSDKLTHIIYAFANIDG----------------------------SDGTLFIGD----- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 120 qksnagdtWDEpirGNFKQLLKLKKN-HPHLKTFISVGGWSWSNRFSDVAADPAARENFAASAVNMLRKYGFDGVDLDWE 198
Cdd:pfam00704 45 --------WDL---GNFEQLKKLKKQkNPGVKVLLSIGGWTDSTGFSLMASNPASRKKFADSIVSFLRKYGFDGIDIDWE 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 199 YPVSGglpgnstrPEDKRNYTLLLQDVREKLDaaEAKDGKKYLLT-TVSGASPEYVSNTELDKIAETVDWINIMTYDYNG 277
Cdd:pfam00704 114 YPGGN--------PEDKENYDLLLRELRAALD--EAKGGKKYLLSaAVPASYPDLDKGYDLPKIAKYLDFINVMTYDFHG 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 278 GWQSISAHNAPLFYDPKakeagvpnaetFNIESTVKRYKEAGVKADKLVLGTPFYGRGWSNCEPADNgeyqkcgpakegT 357
Cdd:pfam00704 184 SWDNVTGHHAPLYGGGS-----------YNVDYAVKYYLKQGVPASKLVLGVPFYGRSWTLVNGSGN------------T 240
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 700653897 358 WEKGVFDFSDLeKNYINKNGYKRYWNDRAKVPFLYNaeNGNFITYDDEESYGYKTDLIQSNGLSGAMFWDFSGD 431
Cdd:pfam00704 241 WEDGVLAYKEI-CNLLKDNGATVVWDDVAKAPYVYD--GDQFITYDDPRSIATKVDYVKAKGLGGVMIWSLDAD 311
|
|
| GH18_chitolectin_chitotriosidase |
cd02872 |
This conserved domain family includes a large number of catalytically inactive chitinase-like ... |
44-444 |
1.45e-88 |
|
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: 278.67 E-value: 1.45e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 44 YYPSWGAY----GRdFQVWDMDASKVSHINYAFADIcwegrhgnvrptgpnpqtwscqdengvidVPNGSIVMGDPWIDV 119
Cdd:cd02872 4 YFTNWAQYrpgnGK-FVPENIDPFLCTHIIYAFAGL-----------------------------NPDGNIIILDEWNDI 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 120 QKsnagdtwdepirGNFKQLLKLKKNHPHLKTFISVGGWSW-SNRFSDVAADPAARENFAASAVNMLRKYGFDGVDLDWE 198
Cdd:cd02872 54 DL------------GLYERFNALKEKNPNLKTLLAIGGWNFgSAKFSAMAASPENRKTFIKSAIAFLRKYGFDGLDLDWE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 199 YPVSGGLPgnstrPEDKRNYTLLLQDVREKLDaaeaKDGKKYLLTTVSGASPEYVSNT-ELDKIAETVDWINIMTYDYNG 277
Cdd:cd02872 122 YPGQRGGP-----PEDKENFVTLLKELREAFE----PEAPRLLLTAAVSAGKETIDAAyDIPEISKYLDFINVMTYDFHG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 278 GWQSISAHNAPLFYDPKAKEagvpNAETFNIESTVKRYKEAGVKADKLVLGTPFYGRGWSNCEPADNGEYQKC-GPAKEG 356
Cdd:cd02872 193 SWEGVTGHNSPLYAGSADTG----DQKYLNVDYAIKYWLSKGAPPEKLVLGIPTYGRSFTLASPSNTGVGAPAsGPGTAG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 357 --TWEKGVFDFSDLEKNYinKNGYKRYWNDRAKVPFLYNaeNGNFITYDDEESYGYKTDLIQSNGLSGAMFW-----DFS 429
Cdd:cd02872 269 pyTREAGFLAYYEICEFL--KSGWTVVWDDEQKVPYAYK--GNQWVGYDDEESIALKVQYLKSKGLGGAMVWsidldDFR 344
|
410
....*....|....*...
gi 700653897 430 GDSHQT---LLNKLAADL 444
Cdd:cd02872 345 GTCGQGkypLLNAINRAL 362
|
|
| GH18_plant_chitinase_class_V |
cd02879 |
The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the ... |
43-437 |
3.05e-40 |
|
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: 148.67 E-value: 3.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 43 GYYPSWGAygrDFQVWDMDASKVSHINYAFADIcwegrhgnvrptgpNPQTWScqdengvIDVPngsivmgdpwidvqks 122
Cdd:cd02879 7 GYWPAWSE---EFPPSNIDSSLFTHLFYAFADL--------------DPSTYE-------VVIS---------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 123 nagdTWDEPIRGNFKQLLKlKKNhPHLKTFISVGGW-SWSNRFSDVAADPAARENFAASAVNMLRKYGFDGVDLDWEYPV 201
Cdd:cd02879 47 ----PSDESEFSTFTETVK-RKN-PSVKTLLSIGGGgSDSSAFAAMASDPTARKAFINSSIKVARKYGFDGLDLDWEFPS 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 202 SgglpgnstrPEDKRNYTLLLQDVREKLDAAEAKDGKKYLLTTvsgASPEYVSNTEL---------DKIAETVDWINIMT 272
Cdd:cd02879 121 S---------QVEMENFGKLLEEWRAAVKDEARSSGRPPLLLT---AAVYFSPILFLsddsvsypiEAINKNLDWVNVMA 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 273 YDYNGGWQSISAHNAPLFYDPKAKeagvpnaetFNIESTVKRYKEAGVKADKLVLGTPFYGRGWSNCEPADNGEYQKCGp 352
Cdd:cd02879 189 YDYYGSWESNTTGPAAALYDPNSN---------VSTDYGIKSWIKAGVPAKKLVLGLPLYGRAWTLYDTTTVSSYVYAG- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 353 akeGTWekgvfdfsdleknyinkngykrywndrakvpflynaengnfITYDDEESYGYKTDLIQSNGLSGAMFWDFSGDS 432
Cdd:cd02879 259 ---TTW-----------------------------------------IGYDDVQSIAVKVKYAKQKGLLGYFAWAVGYDD 294
|
....*
gi 700653897 433 HQTLL 437
Cdd:cd02879 295 NNWLS 299
|
|
| GH18_chitinase-like |
cd00598 |
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ... |
41-278 |
4.21e-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: 145.21 E-value: 4.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 41 IIGYYPSWGAYgRDFQVWDMDASKVSHINYAFADICWEGRHgnvrptgpnpqtwscqdengvidvpngsivmgdpwidvq 120
Cdd:cd00598 1 VICYYDGWSSG-RGPDPTDIPLSLCTHIIYAFAEISSDGSL--------------------------------------- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 121 kSNAGDTWDEPIRGNFKQLLKLKknhPHLKTFISVGGWSWSNrFSDVAADPAARENFAASAVNMLRKYGFDGVDLDWEYP 200
Cdd:cd00598 41 -NLFGDKSEEPLKGALEELASKK---PGLKVLISIGGWTDSS-PFTLASDPASRAAFANSLVSFLKTYGFDGVDIDWEYP 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 700653897 201 VSGGLpgnstrpEDKRNYTLLLQDVREKLDAAEakdgkkYLLTTVSGASPEYVSNTE-LDKIAETVDWINIMTYDYNGG 278
Cdd:cd00598 116 GAADN-------SDRENFITLLRELRSALGAAN------YLLTIAVPASYFDLGYAYdVPAIGDYVDFVNVMTYDLVLG 181
|
|
| GH18_zymocin_alpha |
cd02878 |
Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle ... |
40-426 |
1.07e-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: 125.88 E-value: 1.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 40 KIIGYYPSWGAyGRD---FQVWDMDASKVSHINYAFADIcwegrhgnvrptgpNPqtwscqdengvidvpngsivmgDPW 116
Cdd:cd02878 1 KNIAYFEAYNL-DRPclnMDVTQIDTSKYTHIHFAFANI--------------TS----------------------DFS 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 117 IDVQKSNAGdtWDepirgNFKQLLKLKKNhphlktfISVGGWSWS------NRFSDvAADPAARENFAASAVNMLRKYGF 190
Cdd:cd02878 44 VDVSSVQEQ--FS-----DFKKLKGVKKI-------LSFGGWDFStspstyQIFRD-AVKPANRDTFANNVVNFVNKYNL 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 191 DGVDLDWEYPVSGGLPG-NSTRPEDKRNYTLLLQDVREKLdaaeaKDGKkylltTVSGASPE---YVSNTELDKIAETVD 266
Cdd:cd02878 109 DGVDFDWEYPGAPDIPGiPAGDPDDGKNYLEFLKLLKSKL-----PSGK-----SLSIAAPAsywYLKGFPIKDMAKYVD 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 267 WINIMTYDYNGGWQSISAHNAPLFYDPKAKEAGVPNAETFNIESTVKRykeAGVKADKLVLGTPFYGRGWSNCEPADNGE 346
Cdd:cd02878 179 YIVYMTYDLHGQWDYGNKWASPGCPAGNCLRSHVNKTETLDALSMITK---AGVPSNKVVVGVASYGRSFKMADPGCTGP 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 347 Y------QKCGPAKEGTWEKGVFDFSDLEKNYINKNGYKRYWNDRAKVPFL-YNaeNGNFITYDDEESYGYKTDLIQSNG 419
Cdd:cd02878 256 GctftgpGSGAEAGRCTCTAGYGAISEIEIIDISKSKNKRWYDTDSDSDILvYD--DDQWVAYMSPATKAARIEWYKGLN 333
|
....*..
gi 700653897 420 LSGAMFW 426
Cdd:cd02878 334 FGGTSDW 340
|
|
| GH18_IDGF |
cd02873 |
The IDGF's (imaginal disc growth factors) are a family of growth factors identified in insects ... |
133-431 |
6.59e-25 |
|
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: 107.40 E-value: 6.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 133 RGNFKQLLKLKKNHPHLKTFISVGG------WSWSNRFSDVAADPAARENFAASAVNMLRKYGFDGVDLDWEYP------ 200
Cdd:cd02873 59 KSHYRAITSLKRKYPHLKVLLSVGGdrdtdeEGENEKYLLLLESSESRNAFINSAHSLLKTYGFDGLDLAWQFPknkpkk 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 201 VSGGL-----------PGNSTRPED----KRNYTLLLQDVREKLDAAeakdgkKYLLT-TVsgaSPEYVSNTELD--KIA 262
Cdd:cd02873 139 VRGTFgsawhsfkklfTGDSVVDEKaaehKEQFTALVRELKNALRPD------GLLLTlTV---LPHVNSTWYFDvpAIA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 263 ETVDWINIMTYDYNGGWQS--ISAHNAPLFYDpkakeagVPNAETFNIESTVKRYKEAGVKADKLVLGTPFYGRGWS-NC 339
Cdd:cd02873 210 NNVDFVNLATFDFLTPERNpeEADYTAPIYEL-------YERNPHHNVDYQVKYWLNQGTPASKLNLGIATYGRAWKlTK 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 340 EPADNG---EYQKCGPAKEG--TWEKGVFDFSDLEKNYINKNGYKRYWNDRAKV--------PFLY-----NAENGNFIT 401
Cdd:cd02873 283 DSGITGvppVLETDGPGPAGpqTKTPGLLSWPEICSKLPNPANLKGADAPLRKVgdptkrfgSYAYrpadeNGEHGIWVS 362
|
330 340 350
....*....|....*....|....*....|
gi 700653897 402 YDDEESYGYKTDLIQSNGLSGAMFWDFSGD 431
Cdd:cd02873 363 YEDPDTAANKAGYAKAKGLGGVALFDLSLD 392
|
|
| GH18_CFLE_spore_hydrolase |
cd02874 |
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ... |
169-426 |
3.27e-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: 100.42 E-value: 3.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 169 ADPAARENFAASAVNMLRKYGFDGVDLDWEYpvsgglpgnsTRPEDKRNYTLLLQDVREKLdaaeaKDGKKYLLTTV--- 245
Cdd:cd02874 83 SNPEARQRLINNILALAKKYGYDGVNIDFEN----------VPPEDREAYTQFLRELSDRL-----HPAGYTLSTAVvpk 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 246 -SGASPEYVSNT-ELDKIAETVDWINIMTYDYNGGW---QSISahnaplfydpkakeagvPNAEtfnIESTVKrYKEAGV 320
Cdd:cd02874 148 tSADQFGNWSGAyDYAAIGKIVDFVVLMTYDWHWRGgppGPVA-----------------PIGW---VERVLQ-YAVTQI 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 321 KADKLVLGTPFYGRGWSNcepadngEYQKCGPAKEgtwekgvfdFSDLE-KNYINKNGYKRYWNDRAKVPFL-YNAENGN 398
Cdd:cd02874 207 PREKILLGIPLYGYDWTL-------PYKKGGKAST---------ISPQQaINLAKRYGAEIQYDEEAQSPFFrYVDEQGR 270
|
250 260 270
....*....|....*....|....*....|
gi 700653897 399 --FITYDDEESYGYKTDLIQSNGLSGAMFW 426
Cdd:cd02874 271 rhEVWFEDARSLQAKFELAKEYGLRGVSYW 300
|
|
| GH18_3CO4_chitinase |
cd06545 |
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an ... |
41-337 |
7.11e-16 |
|
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: 77.49 E-value: 7.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 41 IIGYYPSWgaYGRDFQVWDMDASKVSHINYAFAdicwegrhgnvrptgpNPqtwscqDENGVIDVPNGSivmgdpwidvQ 120
Cdd:cd06545 1 VVGYLPNY--DDLNALSPTIDFSKLTHINLAFA----------------NP------DANGTLNANPVR----------S 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 121 KSNAgdtwdepirgnfkqllKLKKNHPH-LKTFISVGGWSWSNrFSDVAADPAARENFAASAVNMLRKYGFDGVDLDWEY 199
Cdd:cd06545 47 ELNS----------------VVNAAHAHnVKILISLAGGSPPE-FTAALNDPAKRKALVDKIINYVVSYNLDGIDVDLEG 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 200 PVSGGLpgnstrpedkrNYTLLLQdvreKLDAAEAKDGKkyLLTTvsgASPEYVSNTELDKIAETVDWINIMTYDYNGGW 279
Cdd:cd06545 110 PDVTFG-----------DYLVFIR----ALYAALKKEGK--LLTA---AVSSWNGGAVSDSTLAYFDFINIMSYDATGPW 169
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 700653897 280 qsisahnaplfydpkAKEAGVPNAETFNIESTVKRYKEAGVK-ADKLVLGTPFYGRGWS 337
Cdd:cd06545 170 ---------------WGDNPGQHSSYDDAVNDLNYWNERGLAsKDKLVLGLPFYGYGFY 213
|
|
| ChiC_BD |
cd12215 |
Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of ... |
548-591 |
4.76e-15 |
|
Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of Streptomyces griseus and related proteins. Chitinase C is a family 19 chitinase, and consists of a N-terminal chitin binding domain and a C-terminal chitin-catalytic domain that effects degradation. Chitinases function in invertebrates in the degradation of old exoskeletons, in fungi to utilize chitin in cell walls, and in bacteria which use chitin as an energy source. ChiC contains the characteristic chitin-binding aromatic residues.
Pssm-ID: 213178 [Multi-domain] Cd Length: 42 Bit Score: 69.14 E-value: 4.76e-15
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 700653897 548 NEWKGTAVYTGGDRVVFNGKVYEAKWWRQGEQPDQAgeSGVWKL 591
Cdd:cd12215 1 PAWDASTVYTGGDQVTYNGKVYEAKWWTQGEEPGTS--WGVWKL 42
|
|
| FN3 |
smart00060 |
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
458-527 |
2.69e-12 |
|
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.
Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 62.63 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 458 SAPDNLRVTEKTATSISLAWDAPSDANIAaSYVLSYEGG-----------AVSVKDTSATIGQLKPRTTYSFTVSAKDAD 526
Cdd:smart00060 2 SPPSNLRVTDVTSTSVTLSWEPPPDDGIT-GYIVGYRVEyreegsewkevNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80
|
.
gi 700653897 527 G 527
Cdd:smart00060 81 G 81
|
|
| FN3 |
cd00063 |
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ... |
458-528 |
9.00e-12 |
|
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.
Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 61.36 E-value: 9.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 458 SAPDNLRVTEKTATSISLAWDAPSDANIAA-SYVLSYEG---------GAVSVKDTSATIGQLKPRTTYSFTVSAKDADG 527
Cdd:cd00063 2 SPPTNLRVTDVTSTSVTLSWTPPEDDGGPItGYVVEYREkgsgdwkevEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81
|
.
gi 700653897 528 K 528
Cdd:cd00063 82 E 82
|
|
| ChtBD3 |
smart00495 |
Chitin-binding domain type 3; |
547-589 |
1.77e-10 |
|
Chitin-binding domain type 3;
Pssm-ID: 197760 [Multi-domain] Cd Length: 41 Bit Score: 56.12 E-value: 1.77e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 700653897 547 YNEWKGTAVYTGGDRVVFNGKVYEAKWWRQGEQPDQAgeSGVW 589
Cdd:smart00495 1 APAWQAGTVYTAGDVVSYNGKVYKAKWWTQGEEPGSS--SGPW 41
|
|
| GH18_SI-CLP |
cd02876 |
Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein ... |
141-333 |
2.08e-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: 59.24 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 141 KLKKNHPHLKTF--ISVGGWSWsNRFSDVAADPAARENFAASAVNMLRKYGFDGVDLD-WEYPVSGGLPgnstrpeDKRN 217
Cdd:cd02876 59 EVRKANKNIKILprVLFEGWSY-QDLQSLLNDEQEREKLIKLLVTTAKKNHFDGIVLEvWSQLAAYGVP-------DKRK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 218 YtlLLQDVREKLDAAEAKDGKKYLLT---TVSGASPEYVSNTELDKIAETVDWINIMTYDYNGGwqsisahnaplfydpk 294
Cdd:cd02876 131 E--LIQLVIHLGETLHSANLKLILVIpppREKGNQNGLFTRKDFEKLAPHVDGFSLMTYDYSSP---------------- 192
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 700653897 295 aKEAGvPNAETFNIESTVKRY-KEAGVKADKLVLGTPFYG 333
Cdd:cd02876 193 -QRPG-PNAPLSWVRSCLELLlPESGKKRAKILLGLNFYG 230
|
|
| GH18_chitobiase |
cd02875 |
Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes ... |
170-431 |
3.33e-09 |
|
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: 58.98 E-value: 3.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 170 DPAARENFAASAVNMLRKYGFDGVDLDWEYPVSGGLPgnstrpedkrNYTLLLQDVREKLDAAEaKDGKKYLLTTVSGAS 249
Cdd:cd02875 93 NPTYRTQWIQQKVELAKSQFMDGINIDIEQPITKGSP----------EYYALTELVKETTKAFK-KENPGYQISFDVAWS 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 250 PEYVSNTELD--KIAETVDWINIMTYDYNG-GWQS--ISAHNAPlfydpkakeagvPNaetfNIESTVKRYKEAGVKADK 324
Cdd:cd02875 162 PSCIDKRCYDytGIADASDFLVVMDYDEQSqIWGKecIAGANSP------------YS----QTLSGYNNFTKLGIDPKK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 325 LVLGTPFYGRGWSnCEpadNGEYQ--KCGPAKEGTWEKGVFDFSDLEKNY------INKNGYKRYWNDRAKVPFL-YNAE 395
Cdd:cd02875 226 LVMGLPWYGYDYP-CL---NGNLEdvVCTIPKVPFRGANCSDAAGRQIPYseimkqINSSIGGRLWDSEQKSPFYnYKDK 301
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 700653897 396 NGNF--ITYDDEESYGYKTDLIQSNGLSGAMFW-----DFSGD 431
Cdd:cd02875 302 QGNLhqVWYDNPQSLSIKVAYAKNLGLKGIGMWngdllDYSGL 344
|
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
458-528 |
4.05e-09 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 53.57 E-value: 4.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 458 SAPDNLRVTEKTATSISLAWDAPSDANIA-ASYVLSY-----EGGAVSVKD----TSATIGQLKPRTTYSFTVSAKDADG 527
Cdd:pfam00041 1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPiTGYEVEYrpknsGEPWNEITVpgttTSVTLTGLKPGTEYEVRVQAVNGGG 80
|
.
gi 700653897 528 K 528
Cdd:pfam00041 81 E 81
|
|
| COG3979 |
COG3979 |
Chitodextrinase [Carbohydrate transport and metabolism]; |
456-560 |
1.41e-08 |
|
Chitodextrinase [Carbohydrate transport and metabolism];
Pssm-ID: 443178 [Multi-domain] Cd Length: 369 Bit Score: 57.09 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 456 PSSAPDNLRVTEKTATSISLAWDAPSDANIAASYVLSYEGGAVSVKD--TSATIGQLKPRTTYSFTVSAKDADGKLHTGP 533
Cdd:COG3979 2 APTAPTGLTASNVTSSSVSLSWDASTDNVGVTGYDVYRGGDQVATVTglTAWTVTGLTPGTEYTFTVGACDAAGNVSAAS 81
|
90 100
....*....|....*....|....*..
gi 700653897 534 TIEAATNSDQMIGYNEWKGTAVYTGGD 560
Cdd:COG3979 82 GTSTAMFGGSSTTLGSAEGVADTSGNL 108
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
455-527 |
2.60e-08 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 56.93 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 455 PPSSAPDNLRVTEKTATSISLAWDAPSDANiAASYVL--------SYEGGAVSVKDTSATIGQLKPRTTYSFTVSAKDAD 526
Cdd:COG3401 325 TPPAAPSGLTATAVGSSSITLSWTASSDAD-VTGYNVyrstsgggTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAA 403
|
.
gi 700653897 527 G 527
Cdd:COG3401 404 G 404
|
|
| CBD_like |
cd12204 |
Cellulose-binding domain, chitinase and related proteins; This group contains proteins related ... |
547-593 |
1.75e-06 |
|
Cellulose-binding domain, chitinase and related proteins; This group contains proteins related to the cellulose-binding domain of Erwinia chrysanthemi endoglucanase Z (EGZ) and Serratia marcescens chitinase B (ChiB). Gram negative plant parasite Erwinia chrysanthemi produces a variety of depolymerizing enzymes to metabolize pectin and cellulose on the host plant. Cellulase EGZ has a modular structure, with N-terminal catalytic domain linked to a C-terminal cellulose-binding domain (CBD). CBD mediates the secretion activity of EGZ. Chitinases allow certain bacteria to utilize chitin as a energy source. Typically, non-plant chitinases are of the glycosidase family 18.
Pssm-ID: 213176 Cd Length: 48 Bit Score: 45.01 E-value: 1.75e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 700653897 547 YNEWKGTAVYTGGDRVVFNGKVYEAKWWRQGEqpdqAGESGVWKLIG 593
Cdd:cd12204 6 YPNWPQGTHAAGGDLVSYNGAVYQAKWWTQSA----PGSDSSWTLVC 48
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
170-330 |
3.50e-06 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 49.75 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 170 DPAARENFAASAVNMLRKYGFDGVDLDWEypvSGGLPGNSTrpedkRNYTLLLQDVREKLDAAEAKDGKKYLLTtvsgAS 249
Cdd:COG3469 306 TAAAADNFVNSVIALIDEYGFDGLDIDLE---GGSNSLNAG-----DTDTPVITNLISALKQLKAKYGPGFVLT----MA 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 250 PE--YVSNTE-------------LDKIAETVDWINimTYDYNGGwqSIsahnapLFYDPKAKEAGVPN---------AET 305
Cdd:COG3469 374 PEtpYVQGGYvayggiwgaylpvILALRDILTLLH--VQYYNSG--SM------LGLDGQVYSQGTVDflvamadmlLEG 443
|
170 180
....*....|....*....|....*
gi 700653897 306 FNIESTVKRYkeAGVKADKLVLGTP 330
Cdd:COG3469 444 FPVAGNSNGF--PGLRPDQVAIGLP 466
|
|
| GH18_trifunctional |
cd06549 |
GH18 domain of an uncharacterized family of bacterial proteins, which share a common ... |
116-336 |
7.16e-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: 48.18 E-value: 7.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 116 WIDVqkSNAGDTWDEPIRGNFKQLLKLKKNHPHLKTF---ISVGGWSWSNrFSDVAADPAARENFAASAVNMLRKYGFDG 192
Cdd:cd06549 31 WLNL--TGPEGRIDVFVDPQGVAIIAAAKAHPKVLPLvqnISGGAWDGKN-IARLLADPSARAKFIANIAAYLERNQADG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 193 VDLDWEypvsgglpgnSTRPEDKRNYTLLLQDVREKLdaaeAKDGKKYLLTTVSGASPEyvsntELDKIAETVDWINIMT 272
Cdd:cd06549 108 IVLDFE----------ELPADDLPKYVAFLSELRRRL----PAQGKQLTVTVPADEADW-----NLKALARNADKLILMA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 700653897 273 YDYNggWQsisahnaplFYDPKakeagvPNAETFNIESTVKRyKEAGVKADKLVLGTPFYGRGW 336
Cdd:cd06549 169 YDEH--YQ---------GGAPG------PIASQDWFESNLAQ-AVKKLPPEKLIVALGSYGYDW 214
|
|
| GH18_chitinase_D-like |
cd02871 |
GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes ... |
150-330 |
1.12e-05 |
|
GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes the 1,4-beta-linkages of N-acetylglucosamine in chitin and chitodextrins. The domain architecture of ChiD includes a catalytic glycosyl hydrolase family 18 (GH18) domain, a chitin-binding domain, and a fibronectin type III domain. The chitin-binding and fibronectin type III domains are located either N-terminal or C-terminal to the catalytic domain. This family includes exochitinase Chi36 from Bacillus cereus.
Pssm-ID: 119350 [Multi-domain] Cd Length: 312 Bit Score: 47.72 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 150 KTFISVGGWSWSNRFSDvaadPAARENFAASAVNMLRKYGFDGVDLDWEypvSGGLPGNSTrpEDKRNYTLLLQDVREKL 229
Cdd:cd02871 75 KVLISIGGANGHVDLNH----TAQEDNFVDSIVAIIKEYGFDGLDIDLE---SGSNPLNAT--PVITNLISALKQLKDHY 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 230 daaeakdGKKYLLTtvsgASPE-------YVSNTE--------LDKIAETVDWINimTYDYNGGWQsisahnapLFYDPK 294
Cdd:cd02871 146 -------GPNFILT----MAPEtpyvqggYAAYGGiwgaylplIDNLRDDLTWLN--VQYYNSGGM--------GGCDGQ 204
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 700653897 295 AKEAGVPNAETFNIESTVKRYKEAG------VKADKLVLGTP 330
Cdd:cd02871 205 SYSQGTADFLVALADMLLTGFPIAGndrfppLPADKVVIGLP 246
|
|
| ChtBD3 |
cd00036 |
Chitin/cellulose binding domains of chitinase and related enzymes; This group contains ... |
550-591 |
1.31e-05 |
|
Chitin/cellulose binding domains of chitinase and related enzymes; This group contains proteins related to the cellulose-binding domain of Erwinia chrysanthemi endoglucanase Z (EGZ) and Serratia marcescens chitinase B (ChiB). Gram negative plant parasite Erwinia chrysanthemi produces a variety of depolymerizing enzymes to metabolize pectin and cellulose on the host plant. Cellulase EGZ has a modular structure, with an N-terminal catalytic domain linked to a C-terminal cellulose-binding domain (CBD). CBD mediates the secretion activity of EGZ. Chitinases allow certain bacteria to utilize chitin as a energy source. Typically, non-plant chitinases are of the glycosidase family 18. Bacillus circulans Glycosidase ChiA1 hydrolyzes chitin and is comprised of several domains: the C-terminal chitin binding domain, an N-terminal catalytic domain, and 2 fibronectin type III-like domains. Bacillus circulans WL-12 ChiA1 facilitates invasion of fungal cell walls. The ChiA1 chitin binding domain is required for the specific recognition of insoluble chitin. although topologically and structurally related, ChiA1 lacks the characteristic aromatic residues of Erwinia chrysanthemi endoglucanase Z (CBD(EGZ)). Streptomyces griseus Chitinase C is a family 19 chitinase, and consists of a N-terminal chitin binding domain and a C-terminal chitin-catalytic domain that effects degradation. ChiC contains the characteristic chitin-binding aromatic residues. Chitinases function in invertebrates in the degradation of old exoskeletons, in fungi to utilize chitin in cell walls, and in bacteria which use chitin as an energy source.
Pssm-ID: 213175 Cd Length: 40 Bit Score: 42.36 E-value: 1.31e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 700653897 550 WKGTAVYTGGDRVVFNGKVYEAKWWRQGEQPdqaGESGVWKL 591
Cdd:cd00036 2 WPNPTHYTAGQSVVYNGNLYTANWYTAGSVP---GSDSSWTQ 40
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
454-527 |
1.81e-04 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 44.61 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 454 EPPSsAPDNLRVTEKTATSISLAWDAPSDANiAASYVLSYEGGA-------VSVKDTSATIGQLKPRTTYSFTVSAKDAD 526
Cdd:COG3401 231 TPPS-APTGLTATADTPGSVTLSWDPVTESD-ATGYRVYRSNSGdgpftkvATVTTTSYTDTGLTNGTTYYYRVTAVDAA 308
|
.
gi 700653897 527 G 527
Cdd:COG3401 309 G 309
|
|
| GH18_narbonin |
cd06544 |
Narbonin is a plant 2S protein from the globulin fraction of narbon bean (Vicia narbonensis L.) ... |
141-198 |
1.91e-04 |
|
Narbonin is a plant 2S protein from the globulin fraction of narbon bean (Vicia narbonensis L.) cotyledons with unknown function. Narbonin has a glycosyl hydrolase family 18 (GH18) domain without the conserved catalytic residues and with no known enzymatic activity. Narbonin amounts to up to 3% of the total seed globulins of mature seeds and was thought to be a storage protein but was found to degrade too slowly during germination. This family also includes the VfNOD32 nodulin from Vicia faba.
Pssm-ID: 119361 Cd Length: 253 Bit Score: 43.51 E-value: 1.91e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 700653897 141 KLKKNHPHLKTFISVGGWSWSNRFsdVAADPAARE----NFAASAVNMLRKYGFDGVDLDWE 198
Cdd:cd06544 63 SIKAQHPNVKVVISIGGRGVQNNP--TPFDPSNVDswvsNAVSSLTSIIQTYNLDGIDIDYE 122
|
|
| GH18_EndoS-like |
cd06542 |
Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of ... |
170-320 |
3.15e-04 |
|
Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of various asparagine (N)-linked glycans and glycoproteins. The endo-beta-N-acetylglucosaminidases have a glycosyl hydrolase family 18 (GH18) catalytic domain. Some members also have an additional C-terminal glycosyl hydrolase family 20 (GH20) domain while others have an N-terminal domain of unknown function (pfam08522). Members of this family include endo-beta-N-acetylglucosaminidase S (EndoS) from Streptococcus pyogenes, EndoF1, EndoF2, EndoF3, and EndoH from Flavobacterium meningosepticum, and EndoE from Enterococcus faecalis. EndoS is a secreted endoglycosidase from Streptococcus pyogenes that specifically hydrolyzes the glycan on human IgG between two core N-acetylglucosamine residues. EndoE is a secreted endoglycosidase, encoded by the ndoE gene in Enterococcus faecalis, that hydrolyzes the glycan on human RNase B.
Pssm-ID: 119359 Cd Length: 255 Bit Score: 42.75 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700653897 170 DPAARENFAASAVNMLRKYGFDGVDLDWEYpvSGGLPgNSTRPEDKRNYTLLLQDVREKLDAAeakdGKkyLLTTVSGAS 249
Cdd:cd06542 85 SDAAAKAYAKAIVDTVDKYGLDGVDFDDEY--SGYGK-NGTSQPSNEAFVRLIKELRKYMGPT----DK--LLTIDGYGQ 155
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 700653897 250 PEYVSNTeldkiaETVDWINIMTYDYNGGWQSISAHNAPLFYDPKAKEAGVPnaeTFNIESTVKRYKEAGV 320
Cdd:cd06542 156 ALSNDGE------EVSPYVDYVIYQYYGSSSSSTQRNWNTNSPKIPPEKMVY---TESFEEENGGNSGSSA 217
|
|
| CBM_5_12 |
pfam02839 |
Carbohydrate binding domain; This short domain is found in many different glycosyl hydrolase ... |
564-589 |
2.56e-03 |
|
Carbohydrate binding domain; This short domain is found in many different glycosyl hydrolase enzymes and is presumed to have a carbohydrate binding function. The domain has six aromatic groups that may be important for binding.
Pssm-ID: 427014 Cd Length: 25 Bit Score: 35.65 E-value: 2.56e-03
10 20
....*....|....*....|....*.
gi 700653897 564 FNGKVYEAKWWRQGEQPDqAGESGVW 589
Cdd:pfam02839 1 HNGKAYQAKWWTQGGDPP-TSSGGPW 25
|
|
| |
