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Conserved domains on  [gi|1376214896|gb|PTO42975|]
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chitinase [Enterococcus mundtii]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GH18_chitinase-like super family cl10447
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ...
 39-338 1.05e-84

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.


The actual alignment was detected with superfamily member cd02871:

Pssm-ID: 471972 [Multi-domain]  Cd Length: 312  Bit Score: 266.51  E-value: 1.05e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896  39 QVSVGYYHNWmpEQGAGYQGGRPADtdlakVNPFYNVIAVSFMKGEGIPTF--------KPYNMSDSEFRQKVATLNAEN 110
Cdd:cd02871     1 KVLVGYWHNW--DNGAGSGRQDLDD-----VPSKYNVINVAFAEPTSDGGGevtfnngsSPGGYSPAEFKADIKALQAKG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 111 RVVIISLGGADSHIEL-HKGEEQAFADEIIRLVEVYGFDGLDIDLEQTAV--DAGDNKTVIPDALKIVRAHFEKEqkhFI 187
Cdd:cd02871    74 KKVLISIGGANGHVDLnHTAQEDNFVDSIVAIIKEYGFDGLDIDLESGSNplNATPVITNLISALKQLKDHYGPN---FI 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 188 ISMAPEFPYLR--------TQGKYVPYITALEQEYDFIAPQLYNQAGDGisvgtEWIAQNNDSKKFEFLYGISKAFNEG- 258
Cdd:cd02871   151 LTMAPETPYVQggyaayggIWGAYLPLIDNLRDDLTWLNVQYYNSGGMG-----GCDGQSYSQGTADFLVALADMLLTGf 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 259 ----SGGFIQIPANRLALGIPANVDAAANGFVkEPSKVYDVFEQMEKDQT-----------PLKGLMTWSINWDEGrnsa 323
Cdd:cd02871   226 piagNDRFPPLPADKVVIGLPASPSAAGGGYV-SPSEVIKALDCLMKGTNcgsyypaggypSLRGLMTWSINWDAT---- 300

                         330
                  ....*....|....*
gi 1376214896 324 gveYNESFAKSYQDL 338
Cdd:cd02871   301 ---NNYEFSKNYGAY 312
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
192-561 1.13e-39

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 153.23  E-value: 1.13e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 192 PEFPYLRTQGKYVPYITALEQEYDFIAPQLYNQAGDGISVGTEWIAQNNDSKkFEFLYGISKAFNEGSGGFIQIPANRLA 271
Cdd:COG3401    71 GRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAV-GTATTATAVAGGAATAGTYALGAGLYG 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 272 LGIPANVDAAANGFVKEPSKVYDVFEQMEKDQTPLKGLMTWSINWDEGRNSAGVEYN------ESFAKSYQDLFQEKTPD 345
Cdd:COG3401   150 VDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYyrvaatDTGGESAPSNEVSVTTP 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 346 TEKPSQPTNLAGTA-THSTVALSWTKSTDDrGVAGYYIYRDG------EQIGRATNNAYTDTKLTASTEYTYTVKAFDAA 418
Cdd:COG3401   230 TTPPSAPTGLTATAdTPGSVTLSWDPVTES-DATGYRVYRSNsgdgpfTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAA 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 419 GNVSEESKALVISTleeppaDLEAPSVPLNITASSISDKSVSLSWTQSTDNvGVVGYYVYRDG------EQVGETETNT- 491
Cdd:COG3401   309 GNESAPSNVVSVTT------DLTPPAAPSGLTATAVGSSSITLSWTASSDA-DVTGYNVYRSTsgggtyTKIAETVTTTs 381

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 492 FSDAGLTANTEYSYTVKAFDEAGNISEESKALVVTTADAPAVEAWDADTIYDLGDLVTHKGNTYRAKWWT 561
Cdd:COG3401   382 YTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNP 451
CBM_5_12 pfam02839
Carbohydrate binding domain; This short domain is found in many different glycosyl hydrolase ...
 550-574 3.05e-07

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: 46.44  E-value: 3.05e-07
                          10        20
                  ....*....|....*....|....*
gi 1376214896 550 HKGNTYRAKWWTRGNEPGTEQWGPW 574
Cdd:pfam02839   1 HNGKAYQAKWWTQGGDPPTSSGGPW 25
 
Name Accession Description Interval E-value
GH18_chitinase_D-like cd02871
GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes ...
 39-338 1.05e-84

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: 266.51  E-value: 1.05e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896  39 QVSVGYYHNWmpEQGAGYQGGRPADtdlakVNPFYNVIAVSFMKGEGIPTF--------KPYNMSDSEFRQKVATLNAEN 110
Cdd:cd02871     1 KVLVGYWHNW--DNGAGSGRQDLDD-----VPSKYNVINVAFAEPTSDGGGevtfnngsSPGGYSPAEFKADIKALQAKG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 111 RVVIISLGGADSHIEL-HKGEEQAFADEIIRLVEVYGFDGLDIDLEQTAV--DAGDNKTVIPDALKIVRAHFEKEqkhFI 187
Cdd:cd02871    74 KKVLISIGGANGHVDLnHTAQEDNFVDSIVAIIKEYGFDGLDIDLESGSNplNATPVITNLISALKQLKDHYGPN---FI 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 188 ISMAPEFPYLR--------TQGKYVPYITALEQEYDFIAPQLYNQAGDGisvgtEWIAQNNDSKKFEFLYGISKAFNEG- 258
Cdd:cd02871   151 LTMAPETPYVQggyaayggIWGAYLPLIDNLRDDLTWLNVQYYNSGGMG-----GCDGQSYSQGTADFLVALADMLLTGf 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 259 ----SGGFIQIPANRLALGIPANVDAAANGFVkEPSKVYDVFEQMEKDQT-----------PLKGLMTWSINWDEGrnsa 323
Cdd:cd02871   226 piagNDRFPPLPADKVVIGLPASPSAAGGGYV-SPSEVIKALDCLMKGTNcgsyypaggypSLRGLMTWSINWDAT---- 300

                         330
                  ....*....|....*
gi 1376214896 324 gveYNESFAKSYQDL 338
Cdd:cd02871   301 ---NNYEFSKNYGAY 312
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
25-339 1.54e-74

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 246.97  E-value: 1.54e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896  25 AADAADTMPDISN---RQVSVGYYHNWmpEQGAGYQggrpadtDLAKVNPFYNVIAVSFMK----GEGIPTFK------- 90
Cdd:COG3469   198 ATTTATTTGPPTPglpKHVLVGYWHNF--DNGSGYI-------RLSDVPDKYDVINVAFAEptgaTNGTVTFTldpgsss 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896  91 PYNMSDSEFRQKVATLNAENRVVIISLGGADSHIELHK-GEEQAFADEIIRLVEVYGFDGLDIDLEQ--TAVDAGDNKT- 166
Cdd:COG3469   269 PGGYTDAQFKADIAALQAQGKKVLLSIGGANGTVQLNTaAAADNFVNSVIALIDEYGFDGLDIDLEGgsNSLNAGDTDTp 348

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 167 ---VIPDALKIVRAHFekeQKHFIISMAPEFPYLRT--------QGKYVPYITALEQEYDFIAPQLYNQAGDGISVGtew 235
Cdd:COG3469   349 vitNLISALKQLKAKY---GPGFVLTMAPETPYVQGgyvayggiWGAYLPVILALRDILTLLHVQYYNSGSMLGLDG--- 422

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 236 iaQNNDSKKFEFLYGISKAFNEG------SGGFIQIPANRLALGIPANVDAAANGFVKePSKVYDVFEQMEKDQT----- 304
Cdd:COG3469   423 --QVYSQGTVDFLVAMADMLLEGfpvagnSNGFPGLRPDQVAIGLPASPSAAGGGYVS-PANVNKALDCLTKGTNcgsyk 499

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1376214896 305 ------PLKGLMTWSINWDEGrnsagveYNESFAKSYQDLF 339
Cdd:COG3469   500 prgtypGLRGLMTWSINWDAS-------NGYEFSNNVGAYL 533
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
192-561 1.13e-39

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 153.23  E-value: 1.13e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 192 PEFPYLRTQGKYVPYITALEQEYDFIAPQLYNQAGDGISVGTEWIAQNNDSKkFEFLYGISKAFNEGSGGFIQIPANRLA 271
Cdd:COG3401    71 GRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAV-GTATTATAVAGGAATAGTYALGAGLYG 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 272 LGIPANVDAAANGFVKEPSKVYDVFEQMEKDQTPLKGLMTWSINWDEGRNSAGVEYN------ESFAKSYQDLFQEKTPD 345
Cdd:COG3401   150 VDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYyrvaatDTGGESAPSNEVSVTTP 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 346 TEKPSQPTNLAGTA-THSTVALSWTKSTDDrGVAGYYIYRDG------EQIGRATNNAYTDTKLTASTEYTYTVKAFDAA 418
Cdd:COG3401   230 TTPPSAPTGLTATAdTPGSVTLSWDPVTES-DATGYRVYRSNsgdgpfTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAA 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 419 GNVSEESKALVISTleeppaDLEAPSVPLNITASSISDKSVSLSWTQSTDNvGVVGYYVYRDG------EQVGETETNT- 491
Cdd:COG3401   309 GNESAPSNVVSVTT------DLTPPAAPSGLTATAVGSSSITLSWTASSDA-DVTGYNVYRSTsgggtyTKIAETVTTTs 381

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 492 FSDAGLTANTEYSYTVKAFDEAGNISEESKALVVTTADAPAVEAWDADTIYDLGDLVTHKGNTYRAKWWT 561
Cdd:COG3401   382 YTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNP 451
ChiC_BD cd12215
Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of ...
 535-576 9.98e-16

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: 71.06  E-value: 9.98e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1376214896 535 AWDADTIYDLGDLVTHKGNTYRAKWWTRGNEPGTEqWGPWEL 576
Cdd:cd12215     2 AWDASTVYTGGDQVTYNGKVYEAKWWTQGEEPGTS-WGVWKL 42
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
40-317 7.43e-14

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 72.49  E-value: 7.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896  40 VSVGYYHNWmpeqgAGYQGGRPADTDLakvnpfYNVIAVSFMKGEGI-PTFKPYNMSDSEFRQ--KVATLNAENRVVIIS 116
Cdd:pfam00704   1 RIVGYYTSW-----GVYRNGNFLPSDK------LTHIIYAFANIDGSdGTLFIGDWDLGNFEQlkKLKKQKNPGVKVLLS 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 117 LGGAD-----SHIELHKGEEQAFADEIIRLVEVYGFDGLDIDLEQTAVDAGDNKTViPDALKIVRAHFEKEQ--KHFIIS 189
Cdd:pfam00704  70 IGGWTdstgfSLMASNPASRKKFADSIVSFLRKYGFDGIDIDWEYPGGNPEDKENY-DLLLRELRAALDEAKggKKYLLS 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 190 MAPEFPYlrTQGKYVPYITALEQEYDFIAPQLYNQAGdGISVGTEWIAQNNDSKKFEFLYGISKAFNEGsggfiqIPANR 269
Cdd:pfam00704 149 AAVPASY--PDLDKGYDLPKIAKYLDFINVMTYDFHG-SWDNVTGHHAPLYGGGSYNVDYAVKYYLKQG------VPASK 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 270 LALGIPA------NVDAAANGFVKEPSKVYDVFEQM----------EKDQTP---------------------------- 305
Cdd:pfam00704 220 LVLGVPFygrswtLVNGSGNTWEDGVLAYKEICNLLkdngatvvwdDVAKAPyvydgdqfityddprsiatkvdyvkakg 299

                         330
                  ....*....|..
gi 1376214896 306 LKGLMTWSINWD 317
Cdd:pfam00704 300 LGGVMIWSLDAD 311
ChtBD3 smart00495
Chitin-binding domain type 3;
533-574 1.01e-12

Chitin-binding domain type 3;


Pssm-ID: 197760 [Multi-domain]  Cd Length: 41  Bit Score: 62.28  E-value: 1.01e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1376214896  533 VEAWDADTIYDLGDLVTHKGNTYRAKWWTRGNEPGTeQWGPW 574
Cdd:smart00495   1 APAWQAGTVYTAGDVVSYNGKVYKAKWWTQGEEPGS-SSGPW 41
Glyco_18 smart00636
Glyco_18 domain;
40-318 7.06e-11

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 63.85  E-value: 7.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896   40 VSVGYYHNWmPEQGAGYQggrPADTDLAKvnpfYNVIAVSF--MKGEGIPTFKPYNMSDSEFRQKVATLNAENRV-VIIS 116
Cdd:smart00636   1 RVVGYFTNW-GVYGRNFP---VDDIPASK----LTHIIYAFanIDPDGTVTIGDEWADIGNFGQLKALKKKNPGLkVLLS 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896  117 LGG-ADSHI--ELHKGEE--QAFADEIIRLVEVYGFDGLDIDLEQTAVDAGDNKTVIpDALKIVRAHFEKEQ---KHFII 188
Cdd:smart00636  73 IGGwTESDNfsSMLSDPAsrKKFIDSIVSFLKKYGFDGIDIDWEYPGGRGDDRENYT-ALLKELREALDKEGaegKGYLL 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896  189 SMAP---------EFPYLRTQGKYVPYITALeqEYDFIAP---------QLYNQAGDGISVGTEWIAQnndskkfeflYG 250
Cdd:smart00636 152 TIAVpagpdkidkGYGDLPAIAKYLDFINLM--TYDFHGAwsnptghnaPLYAGPGDPEKYNVDYAVK----------YY 219

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1376214896  251 ISKAfnegsggfiqIPANRLALGIPA------NVDAAANGFVKEPSKVYDVFEQMEKDQTP----LKGLMTWSINWDE 318
Cdd:smart00636 220 LCKG----------VPPSKLVLGIPFygrgwtLVDGSNNGPGAPFTGPATGGPGTWEGGVVdyreICKLLGATVVYDD 287
CBM_5_12 pfam02839
Carbohydrate binding domain; This short domain is found in many different glycosyl hydrolase ...
 550-574 3.05e-07

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: 46.44  E-value: 3.05e-07
                          10        20
                  ....*....|....*....|....*
gi 1376214896 550 HKGNTYRAKWWTRGNEPGTEQWGPW 574
Cdd:pfam02839   1 HNGKAYQAKWWTQGGDPPTSSGGPW 25
fn3 pfam00041
Fibronectin type III domain;
444-520 8.05e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.02  E-value: 8.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 444 SVPLNITASSISDKSVSLSWTQSTDNVGVV-GYYV-YRD-GEQVGETETNTFSDA------GLTANTEYSYTVKAFDEAG 514
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPItGYEVeYRPkNSGEPWNEITVPGTTtsvtltGLKPGTEYEVRVQAVNGGG 80


                  ....*.
gi 1376214896 515 NiSEES 520
Cdd:pfam00041  81 E-GPPS 85
 
Name Accession Description Interval E-value
GH18_chitinase_D-like cd02871
GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes ...
 39-338 1.05e-84

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: 266.51  E-value: 1.05e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896  39 QVSVGYYHNWmpEQGAGYQGGRPADtdlakVNPFYNVIAVSFMKGEGIPTF--------KPYNMSDSEFRQKVATLNAEN 110
Cdd:cd02871     1 KVLVGYWHNW--DNGAGSGRQDLDD-----VPSKYNVINVAFAEPTSDGGGevtfnngsSPGGYSPAEFKADIKALQAKG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 111 RVVIISLGGADSHIEL-HKGEEQAFADEIIRLVEVYGFDGLDIDLEQTAV--DAGDNKTVIPDALKIVRAHFEKEqkhFI 187
Cdd:cd02871    74 KKVLISIGGANGHVDLnHTAQEDNFVDSIVAIIKEYGFDGLDIDLESGSNplNATPVITNLISALKQLKDHYGPN---FI 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 188 ISMAPEFPYLR--------TQGKYVPYITALEQEYDFIAPQLYNQAGDGisvgtEWIAQNNDSKKFEFLYGISKAFNEG- 258
Cdd:cd02871   151 LTMAPETPYVQggyaayggIWGAYLPLIDNLRDDLTWLNVQYYNSGGMG-----GCDGQSYSQGTADFLVALADMLLTGf 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 259 ----SGGFIQIPANRLALGIPANVDAAANGFVkEPSKVYDVFEQMEKDQT-----------PLKGLMTWSINWDEGrnsa 323
Cdd:cd02871   226 piagNDRFPPLPADKVVIGLPASPSAAGGGYV-SPSEVIKALDCLMKGTNcgsyypaggypSLRGLMTWSINWDAT---- 300

                         330
                  ....*....|....*
gi 1376214896 324 gveYNESFAKSYQDL 338
Cdd:cd02871   301 ---NNYEFSKNYGAY 312
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
25-339 1.54e-74

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 246.97  E-value: 1.54e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896  25 AADAADTMPDISN---RQVSVGYYHNWmpEQGAGYQggrpadtDLAKVNPFYNVIAVSFMK----GEGIPTFK------- 90
Cdd:COG3469   198 ATTTATTTGPPTPglpKHVLVGYWHNF--DNGSGYI-------RLSDVPDKYDVINVAFAEptgaTNGTVTFTldpgsss 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896  91 PYNMSDSEFRQKVATLNAENRVVIISLGGADSHIELHK-GEEQAFADEIIRLVEVYGFDGLDIDLEQ--TAVDAGDNKT- 166
Cdd:COG3469   269 PGGYTDAQFKADIAALQAQGKKVLLSIGGANGTVQLNTaAAADNFVNSVIALIDEYGFDGLDIDLEGgsNSLNAGDTDTp 348

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 167 ---VIPDALKIVRAHFekeQKHFIISMAPEFPYLRT--------QGKYVPYITALEQEYDFIAPQLYNQAGDGISVGtew 235
Cdd:COG3469   349 vitNLISALKQLKAKY---GPGFVLTMAPETPYVQGgyvayggiWGAYLPVILALRDILTLLHVQYYNSGSMLGLDG--- 422

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 236 iaQNNDSKKFEFLYGISKAFNEG------SGGFIQIPANRLALGIPANVDAAANGFVKePSKVYDVFEQMEKDQT----- 304
Cdd:COG3469   423 --QVYSQGTVDFLVAMADMLLEGfpvagnSNGFPGLRPDQVAIGLPASPSAAGGGYVS-PANVNKALDCLTKGTNcgsyk 499

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1376214896 305 ------PLKGLMTWSINWDEGrnsagveYNESFAKSYQDLF 339
Cdd:COG3469   500 prgtypGLRGLMTWSINWDAS-------NGYEFSNNVGAYL 533
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
192-561 1.13e-39

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 153.23  E-value: 1.13e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 192 PEFPYLRTQGKYVPYITALEQEYDFIAPQLYNQAGDGISVGTEWIAQNNDSKkFEFLYGISKAFNEGSGGFIQIPANRLA 271
Cdd:COG3401    71 GRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAV-GTATTATAVAGGAATAGTYALGAGLYG 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 272 LGIPANVDAAANGFVKEPSKVYDVFEQMEKDQTPLKGLMTWSINWDEGRNSAGVEYN------ESFAKSYQDLFQEKTPD 345
Cdd:COG3401   150 VDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYyrvaatDTGGESAPSNEVSVTTP 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 346 TEKPSQPTNLAGTA-THSTVALSWTKSTDDrGVAGYYIYRDG------EQIGRATNNAYTDTKLTASTEYTYTVKAFDAA 418
Cdd:COG3401   230 TTPPSAPTGLTATAdTPGSVTLSWDPVTES-DATGYRVYRSNsgdgpfTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAA 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 419 GNVSEESKALVISTleeppaDLEAPSVPLNITASSISDKSVSLSWTQSTDNvGVVGYYVYRDG------EQVGETETNT- 491
Cdd:COG3401   309 GNESAPSNVVSVTT------DLTPPAAPSGLTATAVGSSSITLSWTASSDA-DVTGYNVYRSTsgggtyTKIAETVTTTs 381

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 492 FSDAGLTANTEYSYTVKAFDEAGNISEESKALVVTTADAPAVEAWDADTIYDLGDLVTHKGNTYRAKWWT 561
Cdd:COG3401   382 YTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNP 451
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
343-556 1.03e-19

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 92.76  E-value: 1.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 343 TPDTEKPSQPTNLAGTATHST-VALSWTKSTDDrGVAGYYIYRDGEQIGR-------ATNNAYTDTKLTASTEYTYTVKA 414
Cdd:COG3401   321 TTDLTPPAAPSGLTATAVGSSsITLSWTASSDA-DVTGYNVYRSTSGGGTytkiaetVTTTSYTDTGLTPGTTYYYKVTA 399

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 415 FDAAGNVSEESKALVISTLEEPPADLEAPSVPLNITASSISdKSVSLSWTQSTDNVGVVGYYVYRDGEQVGETETNTFSD 494
Cdd:COG3401   400 VDAAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVAG-ATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVT 478

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1376214896 495 AGLTANTEYSYTVKAFDEAGNISEESkalVVTTADAPAVEAWDADTIYDLGDLVTHKGNTYR 556
Cdd:COG3401   479 ATTTDTTTANLSVTTGSLVGGSGASS---VTNSVSVIGASAAAAVGGAPDGTPNVTGASPVT 537
COG3979 COG3979
Chitodextrinase [Carbohydrate transport and metabolism];
441-543 3.85e-19

Chitodextrinase [Carbohydrate transport and metabolism];


Pssm-ID: 443178 [Multi-domain]  Cd Length: 369  Bit Score: 89.45  E-value: 3.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 441 EAPSVPLNITASSISDKSVSLSWTQSTDNVGVVGYYVYRDGEQVGETETNT-FSDAGLTANTEYSYTVKAFDEAGNISEE 519
Cdd:COG3979     1 QAPTAPTGLTASNVTSSSVSLSWDASTDNVGVTGYDVYRGGDQVATVTGLTaWTVTGLTPGTEYTFTVGACDAAGNVSAA 80

                          90       100
                  ....*....|....*....|....
gi 1376214896 520 SKALVVTTADAPAVEAWDADTIYD 543
Cdd:COG3979    81 SGTSTAMFGGSSTTLGSAEGVADT 104
COG3979 COG3979
Chitodextrinase [Carbohydrate transport and metabolism];
347-574 7.60e-19

Chitodextrinase [Carbohydrate transport and metabolism];


Pssm-ID: 443178 [Multi-domain]  Cd Length: 369  Bit Score: 88.68  E-value: 7.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 347 EKPSQPTNLAGTA-THSTVALSWTKSTDDRGVAGYYIYRDGEQIG-RATNNAYTDTKLTASTEYTYTVKAFDAAGNVSEE 424
Cdd:COG3979     1 QAPTAPTGLTASNvTSSSVSLSWDASTDNVGVTGYDVYRGGDQVAtVTGLTAWTVTGLTPGTEYTFTVGACDAAGNVSAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 425 SkalviSTLEEPPADLEAPSVPLNITASSISDKSVSLSWTQSTDNVGVVGYYVYRDGEQVGETETNTFSDAGLTANTEYS 504
Cdd:COG3979    81 S-----GTSTAMFGGSSTTLGSAEGVADTSGNLAASGAFFGVTTPPTPSSTLVVDGTTTVNAAATANGGTGGSGGTTTII 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 505 YTVKAFDEAGNISEESKALVVTTADAPAVEAWDADTIYDLGDLVTHKGNTYRAKWWTRGNEPGTEQWGPW 574
Cdd:COG3979   156 TTGVEGGGGSKTAQSLNAITAAGTAALNGGVVGGADEVLTCSAVKDDGSGGAGAGNTYWALNTLGVSDTP 225
ChiC_BD cd12215
Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of ...
 535-576 9.98e-16

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: 71.06  E-value: 9.98e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1376214896 535 AWDADTIYDLGDLVTHKGNTYRAKWWTRGNEPGTEqWGPWEL 576
Cdd:cd12215     2 AWDASTVYTGGDQVTYNGKVYEAKWWTQGEEPGTS-WGVWKL 42
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
40-317 7.43e-14

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 72.49  E-value: 7.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896  40 VSVGYYHNWmpeqgAGYQGGRPADTDLakvnpfYNVIAVSFMKGEGI-PTFKPYNMSDSEFRQ--KVATLNAENRVVIIS 116
Cdd:pfam00704   1 RIVGYYTSW-----GVYRNGNFLPSDK------LTHIIYAFANIDGSdGTLFIGDWDLGNFEQlkKLKKQKNPGVKVLLS 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 117 LGGAD-----SHIELHKGEEQAFADEIIRLVEVYGFDGLDIDLEQTAVDAGDNKTViPDALKIVRAHFEKEQ--KHFIIS 189
Cdd:pfam00704  70 IGGWTdstgfSLMASNPASRKKFADSIVSFLRKYGFDGIDIDWEYPGGNPEDKENY-DLLLRELRAALDEAKggKKYLLS 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 190 MAPEFPYlrTQGKYVPYITALEQEYDFIAPQLYNQAGdGISVGTEWIAQNNDSKKFEFLYGISKAFNEGsggfiqIPANR 269
Cdd:pfam00704 149 AAVPASY--PDLDKGYDLPKIAKYLDFINVMTYDFHG-SWDNVTGHHAPLYGGGSYNVDYAVKYYLKQG------VPASK 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 270 LALGIPA------NVDAAANGFVKEPSKVYDVFEQM----------EKDQTP---------------------------- 305
Cdd:pfam00704 220 LVLGVPFygrswtLVNGSGNTWEDGVLAYKEICNLLkdngatvvwdDVAKAPyvydgdqfityddprsiatkvdyvkakg 299

                         330
                  ....*....|..
gi 1376214896 306 LKGLMTWSINWD 317
Cdd:pfam00704 300 LGGVMIWSLDAD 311
ChtBD3 smart00495
Chitin-binding domain type 3;
533-574 1.01e-12

Chitin-binding domain type 3;


Pssm-ID: 197760 [Multi-domain]  Cd Length: 41  Bit Score: 62.28  E-value: 1.01e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1376214896  533 VEAWDADTIYDLGDLVTHKGNTYRAKWWTRGNEPGTeQWGPW 574
Cdd:smart00495   1 APAWQAGTVYTAGDVVSYNGKVYKAKWWTQGEEPGS-SSGPW 41
Glyco_18 smart00636
Glyco_18 domain;
40-318 7.06e-11

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 63.85  E-value: 7.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896   40 VSVGYYHNWmPEQGAGYQggrPADTDLAKvnpfYNVIAVSF--MKGEGIPTFKPYNMSDSEFRQKVATLNAENRV-VIIS 116
Cdd:smart00636   1 RVVGYFTNW-GVYGRNFP---VDDIPASK----LTHIIYAFanIDPDGTVTIGDEWADIGNFGQLKALKKKNPGLkVLLS 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896  117 LGG-ADSHI--ELHKGEE--QAFADEIIRLVEVYGFDGLDIDLEQTAVDAGDNKTVIpDALKIVRAHFEKEQ---KHFII 188
Cdd:smart00636  73 IGGwTESDNfsSMLSDPAsrKKFIDSIVSFLKKYGFDGIDIDWEYPGGRGDDRENYT-ALLKELREALDKEGaegKGYLL 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896  189 SMAP---------EFPYLRTQGKYVPYITALeqEYDFIAP---------QLYNQAGDGISVGTEWIAQnndskkfeflYG 250
Cdd:smart00636 152 TIAVpagpdkidkGYGDLPAIAKYLDFINLM--TYDFHGAwsnptghnaPLYAGPGDPEKYNVDYAVK----------YY 219

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1376214896  251 ISKAfnegsggfiqIPANRLALGIPA------NVDAAANGFVKEPSKVYDVFEQMEKDQTP----LKGLMTWSINWDE 318
Cdd:smart00636 220 LCKG----------VPPSKLVLGIPFygrgwtLVDGSNNGPGAPFTGPATGGPGTWEGGVVdyreICKLLGATVVYDD 287
GH18_chitinase-like cd00598
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ...
 42-223 1.54e-10

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: 60.85  E-value: 1.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896  42 VGYYHNWMPeqgagYQGGRPADTDLAKvnpfYNVIAVSFM--KGEGIPTFKPYNMSD------SEFRQKVATLnaenrVV 113
Cdd:cd00598     2 ICYYDGWSS-----GRGPDPTDIPLSL----CTHIIYAFAeiSSDGSLNLFGDKSEEplkgalEELASKKPGL-----KV 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 114 IISLGGADSHIELHKGEE----QAFADEIIRLVEVYGFDGLDIDLEQ-TAVDAGDnKTVIPDALKIVRAHFekEQKHFII 188
Cdd:cd00598    68 LISIGGWTDSSPFTLASDpasrAAFANSLVSFLKTYGFDGVDIDWEYpGAADNSD-RENFITLLRELRSAL--GAANYLL 144

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1376214896 189 SMAPefPYLRTQGKYVPYITALEQEYDFIAPQLYN 223
Cdd:cd00598   145 TIAV--PASYFDLGYAYDVPAIGDYVDFVNVMTYD 177
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 443-527 2.39e-10

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: 57.51  E-value: 2.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 443 PSVPLNITASSISDKSVSLSWTQSTDNVG-VVGYYVYRDGEQVGETE--------TNTFSDAGLTANTEYSYTVKAFDEA 513
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGpITGYVVEYREKGSGDWKevevtpgsETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|....
gi 1376214896 514 GnISEESKALVVTT 527
Cdd:cd00063    81 G-ESPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 443-514 1.99e-09

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: 54.54  E-value: 1.99e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896  443 PSVPLNITASSISDKSVSLSWTQSTDNVG---VVGYYVYRDGEQVGETE------TNTFSDAGLTANTEYSYTVKAFDEA 513
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItgyIVGYRVEYREEGSEWKEvnvtpsSTSYTLTGLKPGTEYEFRVRAVNGA 80


                   .
gi 1376214896  514 G 514
Cdd:smart00060  81 G 81
CBD_like cd12204
Cellulose-binding domain, chitinase and related proteins; This group contains proteins related ...
 528-578 3.21e-08

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: 50.02  E-value: 3.21e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1376214896 528 ADAPAVEAWDADTIYDLGDLVTHKGNTYRAKWWTRgNEPGTEqwGPWELIG 578
Cdd:cd12204     1 AGANAYPNWPQGTHAAGGDLVSYNGAVYQAKWWTQ-SAPGSD--SSWTLVC 48
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 349-432 5.80e-08

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: 50.57  E-value: 5.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 349 PSQPTNLAGTATHST-VALSWTKSTDDRG-VAGYYIYR------DGEQI--GRATNNAYTDTKLTASTEYTYTVKAFDAA 418
Cdd:cd00063     1 PSPPTNLRVTDVTSTsVTLSWTPPEDDGGpITGYVVEYrekgsgDWKEVevTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|....
gi 1376214896 419 GnVSEESKALVIST 432
Cdd:cd00063    81 G-ESPPSESVTVTT 93
CBM_5_12 pfam02839
Carbohydrate binding domain; This short domain is found in many different glycosyl hydrolase ...
 550-574 3.05e-07

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: 46.44  E-value: 3.05e-07
                          10        20
                  ....*....|....*....|....*
gi 1376214896 550 HKGNTYRAKWWTRGNEPGTEQWGPW 574
Cdd:pfam02839   1 HNGKAYQAKWWTQGGDPPTSSGGPW 25
ChtBD3 cd00036
Chitin/cellulose binding domains of chitinase and related enzymes; This group contains ...
 535-568 3.20e-07

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: 46.99  E-value: 3.20e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1376214896 535 AWDADTIYDLGDLVTHKGNTYRAKWWTRGNEPGT 568
Cdd:cd00036     1 AWPNPTHYTAGQSVVYNGNLYTANWYTAGSVPGS 34
fn3 pfam00041
Fibronectin type III domain;
444-520 8.05e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.02  E-value: 8.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 444 SVPLNITASSISDKSVSLSWTQSTDNVGVV-GYYV-YRD-GEQVGETETNTFSDA------GLTANTEYSYTVKAFDEAG 514
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPItGYEVeYRPkNSGEPWNEITVPGTTtsvtltGLKPGTEYEVRVQAVNGGG 80


                  ....*.
gi 1376214896 515 NiSEES 520
Cdd:pfam00041  81 E-GPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 349-419 4.32e-06

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: 44.91  E-value: 4.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896  349 PSQPTNLAGTA-THSTVALSWTKSTDDRG---VAGYYIYRDG------EQIGRATNNAYTDTKLTASTEYTYTVKAFDAA 418
Cdd:smart00060   1 PSPPSNLRVTDvTSTSVTLSWEPPPDDGItgyIVGYRVEYREegsewkEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                   .
gi 1376214896  419 G 419
Cdd:smart00060  81 G 81
GH18_plant_chitinase_class_V cd02879
The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the ...
 132-275 1.47e-05

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: 46.97  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 132 QAFADEIIRLVEVYGFDGLDIDLE--QTAVDAGDNKTVipdaLKIVRAHFEKE-----QKHFIISMAPEF-PYLRTQGKY 203
Cdd:cd02879    94 KAFINSSIKVARKYGFDGLDLDWEfpSSQVEMENFGKL----LEEWRAAVKDEarssgRPPLLLTAAVYFsPILFLSDDS 169

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1376214896 204 VPY-ITALEQEYDFIAPQLYNQAGDGISVGTEWIAQNND-SKKFEFLYGISKAFNEGsggfiqIPANRLALGIP 275
Cdd:cd02879   170 VSYpIEAINKNLDWVNVMAYDYYGSWESNTTGPAAALYDpNSNVSTDYGIKSWIKAG------VPAKKLVLGLP 237
GH18_hevamine_XipI_class_III cd02877
This conserved domain family includes xylanase inhibitor Xip-I, and the class III plant ...
 54-322 6.45e-05

This conserved domain family includes xylanase inhibitor Xip-I, and the class III plant chitinases such as hevamine, concanavalin B, and PPL2, all of which have a glycosyl hydrolase family 18 (GH18) domain. Hevamine is a class III endochitinase that hydrolyzes the linear polysaccharide chains of chitin and peptidoglycan and is important for defense against pathogenic bacteria and fungi. PPL2 (Parkia platycephala lectin 2) is a class III chitinase from Parkia platycephala seeds that hydrolyzes beta(1-4) glycosidic bonds linking 2-acetoamido-2-deoxy-beta-D-glucopyranose units in chitin.


Pssm-ID: 119356 [Multi-domain]  Cd Length: 280  Bit Score: 44.92  E-value: 6.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896  54 AGYQGGRPADTDLAKV--NPFYNVIAVSFMKGEGIPTFKPYNMS---DSEFRQKVATLNAE-------NRVVIISLGGAD 121
Cdd:cd02877     4 AVYWGQNSDEGSLREYcdTGNYDIVNISFLNVFGSGGTPGLNFAghcGGSTYPNCPQLGADikhcqskGKKVLLSIGGAG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 122 SHIELhKGEEQA--FADeiiRLVEVYG---------------FDGLDIDLEQTAVDAGDnktvipDALKIVRAHFEKEQ- 183
Cdd:cd02877    84 GSYSL-SSDADAkdFAD---YLWNAFGggtdsgvprpfgdavVDGFDFDIEHGSPENYD------ALAKRLRSLFASDPs 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 184 KHFIISMAPEFPYlrtqgkyvPYI---TALEQ-EYDFIAPQLYNQAGdgisvgteWIAQNNDSKKFEFlygiskAFNEGS 259
Cdd:cd02877   154 KKYYLTAAPQCPY--------PDAslgDAIATgLFDFIFVQFYNNPC--------CSYASGNASGFNF------NWDTWT 211

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1376214896 260 GGFIQIPANRLALGIPANVDAAANGFVkEPSKVYDVFEQMEKDQTPLKGLMTWSINWDEGRNS 322
Cdd:cd02877   212 SWAKATSNAKVFLGLPASPEAAGSGYV-DPSELASLVLPVKQKSPNFGGVMLWDASQDKQGTG 273
fn3 pfam00041
Fibronectin type III domain;
350-425 9.06e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 41.25  E-value: 9.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 350 SQPTNLAGTA-THSTVALSWTKSTDDRG-VAGYYI-YRDGEQIGRATN-------NAYTDTKLTASTEYTYTVKAFDAAG 419
Cdd:pfam00041   1 SAPSNLTVTDvTSTSLTVSWTPPPDGNGpITGYEVeYRPKNSGEPWNEitvpgttTSVTLTGLKPGTEYEVRVQAVNGGG 80


                  ....*.
gi 1376214896 420 NvSEES 425
Cdd:pfam00041  81 E-GPPS 85
GH18_chitinase cd06548
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ...
 41-276 2.32e-04

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: 43.39  E-value: 2.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896  41 SVGYYHNWMPeQGAGYQGGRPADTD-LAKVN-PFYNVIA----VSFMKGEGIPTFKPYNMSDSEFRQKVA-------TLN 107
Cdd:cd06548     1 VVGYFTNWGI-YGRNYFVTDDIPADkLTHINyAFADIDGdggvVTSDDEAADEAAQSVDGGADTDDQPLKgnfgqlrKLK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 108 AENR--VVIISLGG-ADSHI--ELHKGEE--QAFADEIIRLVEVYGFDGLDIDLEQTAVDAGDNKTVIPD-------ALK 173
Cdd:cd06548    80 QKNPhlKILLSIGGwTWSGGfsDAAATEAsrAKFADSAVDFIRKYGFDGIDIDWEYPGSGGAPGNVARPEdkenftlLLK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 174 IVRAHF----EKEQKHFIISMA-PEFP-YLRTQG-----KYVPYITAleQEYDFIAP---------QLYNQAGD-GISVG 232
Cdd:cd06548   160 ELREALdalgAETGRKYLLTIAaPAGPdKLDKLEvaeiaKYLDFINL--MTYDFHGAwsnttghhsNLYASPADpPGGYS 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1376214896 233 TEWIAQNNDSKKfeflygiskafnegsggfiqIPANRLALGIPA 276
Cdd:cd06548   238 VDAAVNYYLSAG--------------------VPPEKLVLGVPF 261
ChiA COG3325
Chitinase, GH18 family [Carbohydrate transport and metabolism];
25-285 4.91e-04

Chitinase, GH18 family [Carbohydrate transport and metabolism];


Pssm-ID: 442554 [Multi-domain]  Cd Length: 391  Bit Score: 42.59  E-value: 4.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896  25 AADAADTMPDISNRQVSVGYYHNWmpeqGAGYQGGRPADTDLAKVN----PFYNVIA---VSFMKGEGIPTFKPYNMSDS 97
Cdd:COG3325     5 SVSDTAAAATATSGKRVVGYFTQW----GIYGRNYLVKDIPASKLThinyAFANVDPdgkCSVGDAWAKPSVDGAADDWD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896  98 E-----FRQkVATLNAENR--VVIISLGG---AD--SHIELHKGEEQAFADEIIRLVEVYGFDGLDIDLEQTAVDAGDNK 165
Cdd:COG3325    81 QplkgnFNQ-LKKLKAKNPnlKVLISIGGwtwSKgfSDAAATPASRAAFVDSCVDLLRKYNFDGIDIDWEYPGSGGAPGN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 166 TVIPD-------ALKIVRAHF----EKEQKHFIISMA-PEFPYLRTQ------GKYVPYITAleQEYDF----------I 217
Cdd:COG3325   160 VYRPEdkanftaLLKELRAQLdalgAETGKHYLLTAAaPAGPDKLDGielpkvAQYLDYVNV--MTYDFhgawspttghQ 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1376214896 218 APqLYNQAGDGISVG--TEWIAQNndskkfeFLygiskafnegSGGfiqIPANRLALGIP------ANVDAAANGF 285
Cdd:COG3325   238 AP-LYDSPKDPEAQGysVDSAVQA-------YL----------AAG---VPASKLVLGVPfygrgwTGVTGGNNGL 292
GH18_chitolectin_chitotriosidase cd02872
This conserved domain family includes a large number of catalytically inactive chitinase-like ...
 42-275 6.28e-04

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: 42.16  E-value: 6.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896  42 VGYYHNWmpeqgAGYQGGR----PADTD----------LAKVNPFYNVIavsfmkgegipTFKPYNMSDSEFRQKVATLN 107
Cdd:cd02872     2 VCYFTNW-----AQYRPGNgkfvPENIDpflcthiiyaFAGLNPDGNII-----------ILDEWNDIDLGLYERFNALK 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 108 AENR--VVIISLGG------------ADSHIElhkgeeQAFADEIIRLVEVYGFDGLDIDLE---QTAVDAGDnKTVIPD 170
Cdd:cd02872    66 EKNPnlKTLLAIGGwnfgsakfsamaASPENR------KTFIKSAIAFLRKYGFDGLDLDWEypgQRGGPPED-KENFVT 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 171 ALKIVRAHFEKEQKHFIISMAP-----------EFPYLrtqGKYVPYITALeqEYDF----------IAPqLYNQAGDgi 229
Cdd:cd02872   139 LLKELREAFEPEAPRLLLTAAVsagketidaayDIPEI---SKYLDFINVM--TYDFhgswegvtghNSP-LYAGSAD-- 210

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1376214896 230 svgTEWIAQNNDSkkfeflYGISKAFNEGSggfiqiPANRLALGIP 275
Cdd:cd02872   211 ---TGDQKYLNVD------YAIKYWLSKGA------PPEKLVLGIP 241
GH18_3CO4_chitinase cd06545
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an ...
 97-275 7.87e-04

The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an uncharacterized bacterial member of the family 18 glycosyl hydrolases with homologs found in Flavobacterium, Stigmatella, and Pseudomonas.


Pssm-ID: 119362 [Multi-domain]  Cd Length: 253  Bit Score: 41.67  E-value: 7.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896  97 SEFRQKVATLNAENRVVIISLGGADSHIE----LHKGEEQAFADEIIRLVEVYGFDGLDIDLEQTAVDAGDNKTVIpdal 172
Cdd:cd06545    46 SELNSVVNAAHAHNVKILISLAGGSPPEFtaalNDPAKRKALVDKIINYVVSYNLDGIDVDLEGPDVTFGDYLVFI---- 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 173 KIVRAHFEKEQKhFIISMAPEfpylRTQGkYVPyiTALEQEYDFIAPQLYNqagdgiSVGTEWIAQNNDSKKFEFLygiS 252
Cdd:cd06545   122 RALYAALKKEGK-LLTAAVSS----WNGG-AVS--DSTLAYFDFINIMSYD------ATGPWWGDNPGQHSSYDDA---V 184

                         170       180
                  ....*....|....*....|....*
gi 1376214896 253 KAFN--EGSGgfiQIPANRLALGIP 275
Cdd:cd06545   185 NDLNywNERG---LASKDKLVLGLP 206
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
349-542 1.35e-03

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 41.85  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 349 PSQPTNLAGTATHSTVALSWTKSTDDrGVAGYYIYRDGEQ--------IGRATNNAYTDTKLTASTEYTYTVKAFDAAGN 420
Cdd:COG4733   630 PPAPTGLTATGGLGGITLSWSFPVDA-DTLRTEIRYSTTGdwasatvaQALYPGNTYTLAGLKAGQTYYYRARAVDRSGN 708

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896 421 VSE-----ESKALVISTLEEPPADLEAPSVPLNITASSISDKSVSLSWTQSTDNVGVVGYYVYRDGEQVGETETNTFSDA 495
Cdd:COG4733   709 VSAwwvsgQASADAAGILDAITGQILETELGQELDAIIQNATVAEVVAATVTDVTAQIDTAVLFAGVATAAAIGAEARVA 788

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1376214896 496 GLTANTEYSYTVKAFDEAGNISEESKALVVTTADAPAVEAWDADTIY 542
Cdd:COG4733   789 ATVAESATAAAATGTAADAAGDASGGVTAGTSGTTGAGDTAASTTRV 835
Big_7 pfam17957
Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in ...
 352-412 6.00e-03

Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in glycosyl hydrolase enzymes.


Pssm-ID: 436171 [Multi-domain]  Cd Length: 67  Bit Score: 35.66  E-value: 6.00e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1376214896 352 PTNLAgTATHSTVALSWTkSTDDRGVAGYYIYRDGEQIGRATNNAYT---DTKLTASTEYTYTV 412
Cdd:pfam17957   6 PANGA-TVSGGTVTISAT-ASDDGGVSKVEFYVDGTLVGTDTSAPYSftwTTTALANGTHTITV 67
GH18_PF-ChiA-like cd06543
PF-ChiA is an uncharacterized chitinase found in the hyperthermophilic archaeon Pyrococcus ...
 95-177 9.37e-03

PF-ChiA is an uncharacterized chitinase found in the hyperthermophilic archaeon Pyrococcus furiosus with a glycosyl hydrolase family 18 (GH18) catalytic domain as well as a cellulose-binding domain. Members of this domain family are found not only in archaea but also in eukaryotes and prokaryotes. PF-ChiA exhibits hydrolytic activity toward both colloidal and crystalline (beta/alpha) chitins at high temperature.


Pssm-ID: 119360  Cd Length: 294  Bit Score: 38.43  E-value: 9.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376214896  95 SDSEFRQKVATLNAENRVVIISLGGA-DSHIELHKGEEQAFADEIIRLVEVYGFDGLDIDLEQTAVDAGDNKTVIPDALK 173
Cdd:cd06543    52 QGGWIKSDIAALRAAGGDVIVSFGGAsGTPLATSCTSADQLAAAYQKVIDAYGLTHLDFDIEGGALTDTAAIDRRAQALA 131


                  ....
gi 1376214896 174 IVRA 177
Cdd:cd06543   132 LLQK 135
ChiA1_BD cd12214
chitin-binding domain of Chi A1-like proteins; This group contains proteins related to the ...
 535-557 9.41e-03

chitin-binding domain of Chi A1-like proteins; This group contains proteins related to the chitin binding domain of chitinase A1 (ChiA1) of Bacillus circulans WL-12. Glycosidase ChiA1 hydrolyzes chitin and is comprised of several domains: the C-terminal chitin binding domain, an N-terminal and catalytic domain, and 2 fibronectin type III-like domains. 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. Bacillus circulans WL-12 ChiA1 facilitates invasion of fungal cell walls. The ChiAi 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)).


Pssm-ID: 213177 [Multi-domain]  Cd Length: 45  Bit Score: 34.23  E-value: 9.41e-03
                          10        20
                  ....*....|....*....|...
gi 1376214896 535 AWDADTIYDLGDLVTHKGNTYRA 557
Cdd:cd12214     1 EWAAGTTYKAGDIVTYNGKLYRC 23
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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