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Conserved domains on  [gi|1106883622|ref|WP_071866627|]
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MULTISPECIES: fibronectin type III domain-containing protein [Enterococcus]

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 4.74e-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: 264.58  E-value: 4.74e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622  39 QVSVGYYHNWVpeQGAGYQGGRPADtdlakVNPFYNVIAVSFMKGEGIPTF--------KPYNMSDTEFRQKVATLNAED 110
Cdd:cd02871     1 KVLVGYWHNWD--NGAGSGRQDLDD-----VPSKYNVINVAFAEPTSDGGGevtfnngsSPGGYSPAEFKADIKALQAKG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 111 RVVLISLGGADSHIEL-HKGEEQAFADEIIRLVEVYGFDGLDIDLEQTAV--DAGDNKTVIPDALKIVRAHFEKEqkhFI 187
Cdd:cd02871    74 KKVLISIGGANGHVDLnHTAQEDNFVDSIVAIIKEYGFDGLDIDLESGSNplNATPVITNLISALKQLKDHYGPN---FI 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 188 ISMAPEFPYLR--------TQGKYVPYITALEQEYDFIAPQLYNQAGDGisvgtEWIAQNNDSKKFEFLYGISKAFNEG- 258
Cdd:cd02871   151 LTMAPETPYVQggyaayggIWGAYLPLIDNLRDDLTWLNVQYYNSGGMG-----GCDGQSYSQGTADFLVALADMLLTGf 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 259 ----SGGFIQIPANRLALGIPANIDAAANGFVkEPSKVYDVFEQMEKDQT-----------PLKGLMTWSINWDEGrnsa 323
Cdd:cd02871   226 piagNDRFPPLPADKVVIGLPASPSAAGGGYV-SPSEVIKALDCLMKGTNcgsyypaggypSLRGLMTWSINWDAT---- 300

                         330
                  ....*....|....*
gi 1106883622 324 gveYNESFAKSYQDL 338
Cdd:cd02871   301 ---NNYEFSKNYGAY 312
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
244-561 3.80e-38

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 148.61  E-value: 3.80e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 244 KFEFLYGISKAFNEGSGGFIQIPANRLALGIPANIDAAANGFVKEPSKVYDVFEQMEKDQTPLKGLMTWSINWDEGRNSA 323
Cdd:COG3401   122 VGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEP 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 324 GVEYN------ESFAKSYQDLFQEKTPDTEKPSQPTNLAGTA-THSTVALSWTNSTDDrGVAGYYIYRDG------EQIG 390
Cdd:COG3401   202 GTTYYyrvaatDTGGESAPSNEVSVTTPTTPPSAPTGLTATAdTPGSVTLSWDPVTES-DATGYRVYRSNsgdgpfTKVA 280

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 391 RATNNAYTDTKLTASTEYTYTVKAFDAAGNVSEESKALVISTleeppaDLEAPSVPLNIAVSSISDKSVSLSWTQSTDNv 470
Cdd:COG3401   281 TVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVVSVTT------DLTPPAAPSGLTATAVGSSSITLSWTASSDA- 353

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 471 GVVGYYVYRDG------EQVGETATNT-FSDAGLTANTEYSYTVKAFDEAGNISEESKALVVTTADAPAVEAWDADTIYD 543
Cdd:COG3401   354 DVTGYNVYRSTsgggtyTKIAETVTTTsYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAV 433

                         330
                  ....*....|....*...
gi 1106883622 544 LGDIVTHKGNTYRAKWWT 561
Cdd:COG3401   434 PLTDVAGATAAASAASNP 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 1106883622 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 4.74e-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: 264.58  E-value: 4.74e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622  39 QVSVGYYHNWVpeQGAGYQGGRPADtdlakVNPFYNVIAVSFMKGEGIPTF--------KPYNMSDTEFRQKVATLNAED 110
Cdd:cd02871     1 KVLVGYWHNWD--NGAGSGRQDLDD-----VPSKYNVINVAFAEPTSDGGGevtfnngsSPGGYSPAEFKADIKALQAKG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 111 RVVLISLGGADSHIEL-HKGEEQAFADEIIRLVEVYGFDGLDIDLEQTAV--DAGDNKTVIPDALKIVRAHFEKEqkhFI 187
Cdd:cd02871    74 KKVLISIGGANGHVDLnHTAQEDNFVDSIVAIIKEYGFDGLDIDLESGSNplNATPVITNLISALKQLKDHYGPN---FI 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 188 ISMAPEFPYLR--------TQGKYVPYITALEQEYDFIAPQLYNQAGDGisvgtEWIAQNNDSKKFEFLYGISKAFNEG- 258
Cdd:cd02871   151 LTMAPETPYVQggyaayggIWGAYLPLIDNLRDDLTWLNVQYYNSGGMG-----GCDGQSYSQGTADFLVALADMLLTGf 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 259 ----SGGFIQIPANRLALGIPANIDAAANGFVkEPSKVYDVFEQMEKDQT-----------PLKGLMTWSINWDEGrnsa 323
Cdd:cd02871   226 piagNDRFPPLPADKVVIGLPASPSAAGGGYV-SPSEVIKALDCLMKGTNcgsyypaggypSLRGLMTWSINWDAT---- 300

                         330
                  ....*....|....*
gi 1106883622 324 gveYNESFAKSYQDL 338
Cdd:cd02871   301 ---NNYEFSKNYGAY 312
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
25-339 2.13e-74

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 246.59  E-value: 2.13e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622  25 AADAADTMPDISN---RQVSVGYYHNWVpeQGAGYQggrpadtDLAKVNPFYNVIAVSFMK----GEGIPTFK------- 90
Cdd:COG3469   198 ATTTATTTGPPTPglpKHVLVGYWHNFD--NGSGYI-------RLSDVPDKYDVINVAFAEptgaTNGTVTFTldpgsss 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622  91 PYNMSDTEFRQKVATLNAEDRVVLISLGGADSHIELHK-GEEQAFADEIIRLVEVYGFDGLDIDLEQ--TAVDAGDNKT- 166
Cdd:COG3469   269 PGGYTDAQFKADIAALQAQGKKVLLSIGGANGTVQLNTaAAADNFVNSVIALIDEYGFDGLDIDLEGgsNSLNAGDTDTp 348

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 167 ---VIPDALKIVRAHFekeQKHFIISMAPEFPYLRT--------QGKYVPYITALEQEYDFIAPQLYNQAGDGISVGtew 235
Cdd:COG3469   349 vitNLISALKQLKAKY---GPGFVLTMAPETPYVQGgyvayggiWGAYLPVILALRDILTLLHVQYYNSGSMLGLDG--- 422

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 236 iaQNNDSKKFEFLYGISKAFNEG------SGGFIQIPANRLALGIPANIDAAANGFVKePSKVYDVFEQMEKDQT----- 304
Cdd:COG3469   423 --QVYSQGTVDFLVAMADMLLEGfpvagnSNGFPGLRPDQVAIGLPASPSAAGGGYVS-PANVNKALDCLTKGTNcgsyk 499

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1106883622 305 ------PLKGLMTWSINWDEGrnsagveYNESFAKSYQDLF 339
Cdd:COG3469   500 prgtypGLRGLMTWSINWDAS-------NGYEFSNNVGAYL 533
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
244-561 3.80e-38

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 148.61  E-value: 3.80e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 244 KFEFLYGISKAFNEGSGGFIQIPANRLALGIPANIDAAANGFVKEPSKVYDVFEQMEKDQTPLKGLMTWSINWDEGRNSA 323
Cdd:COG3401   122 VGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEP 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 324 GVEYN------ESFAKSYQDLFQEKTPDTEKPSQPTNLAGTA-THSTVALSWTNSTDDrGVAGYYIYRDG------EQIG 390
Cdd:COG3401   202 GTTYYyrvaatDTGGESAPSNEVSVTTPTTPPSAPTGLTATAdTPGSVTLSWDPVTES-DATGYRVYRSNsgdgpfTKVA 280

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 391 RATNNAYTDTKLTASTEYTYTVKAFDAAGNVSEESKALVISTleeppaDLEAPSVPLNIAVSSISDKSVSLSWTQSTDNv 470
Cdd:COG3401   281 TVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVVSVTT------DLTPPAAPSGLTATAVGSSSITLSWTASSDA- 353

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 471 GVVGYYVYRDG------EQVGETATNT-FSDAGLTANTEYSYTVKAFDEAGNISEESKALVVTTADAPAVEAWDADTIYD 543
Cdd:COG3401   354 DVTGYNVYRSTsgggtyTKIAETVTTTsYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAV 433

                         330
                  ....*....|....*...
gi 1106883622 544 LGDIVTHKGNTYRAKWWT 561
Cdd:COG3401   434 PLTDVAGATAAASAASNP 451
ChiC_BD cd12215
Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of ...
 535-576 2.92e-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: 72.60  E-value: 2.92e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1106883622 535 AWDADTIYDLGDIVTHKGNTYRAKWWTRGNEPGTEqWGPWEL 576
Cdd:cd12215     2 AWDASTVYTGGDQVTYNGKVYEAKWWTQGEEPGTS-WGVWKL 42
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
40-317 9.18e-14

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 72.49  E-value: 9.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622  40 VSVGYYHNWvpeqgAGYQGGRPADTDLakvnpfYNVIAVSFMKGEGI-PTFKPYNMSDTEFRQ--KVATLNAEDRVVLIS 116
Cdd:pfam00704   1 RIVGYYTSW-----GVYRNGNFLPSDK------LTHIIYAFANIDGSdGTLFIGDWDLGNFEQlkKLKKQKNPGVKVLLS 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 117 LGGAD-----SHIELHKGEEQAFADEIIRLVEVYGFDGLDIDLEQTAVDAGDNKTViPDALKIVRAHFEKEQ--KHFIIS 189
Cdd:pfam00704  70 IGGWTdstgfSLMASNPASRKKFADSIVSFLRKYGFDGIDIDWEYPGGNPEDKENY-DLLLRELRAALDEAKggKKYLLS 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 190 MAPEFPY--------LRTQGKYVPYI--------TALEQEYDFIAPqLYNQAGDGISVGTE-WIAQNNDSKKFeFL---- 248
Cdd:pfam00704 149 AAVPASYpdldkgydLPKIAKYLDFInvmtydfhGSWDNVTGHHAP-LYGGGSYNVDYAVKyYLKQGVPASKL-VLgvpf 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 249 YGIS--------KAFNEGSGGFIQIPANRLALGIPANIDAAAN-GFVKEPSKV--YDVFEQME-----KDQTPLKGLMTW 312
Cdd:pfam00704 227 YGRSwtlvngsgNTWEDGVLAYKEICNLLKDNGATVVWDDVAKaPYVYDGDQFitYDDPRSIAtkvdyVKAKGLGGVMIW 306


                  ....*
gi 1106883622 313 SINWD 317
Cdd:pfam00704 307 SLDAD 311
ChtBD3 smart00495
Chitin-binding domain type 3;
533-574 6.29e-13

Chitin-binding domain type 3;


Pssm-ID: 197760 [Multi-domain]  Cd Length: 41  Bit Score: 63.05  E-value: 6.29e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1106883622  533 VEAWDADTIYDLGDIVTHKGNTYRAKWWTRGNEPGTeQWGPW 574
Cdd:smart00495   1 APAWQAGTVYTAGDVVSYNGKVYKAKWWTQGEEPGS-SSGPW 41
Glyco_18 smart00636
Glyco_18 domain;
40-245 1.74e-10

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 62.70  E-value: 1.74e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622   40 VSVGYYHNWvPEQGAGYQggrPADTDLAKvnpfYNVIAVSF--MKGEGIPTFKPYNMSDTEFRQKVATLNAEDRV-VLIS 116
Cdd:smart00636   1 RVVGYFTNW-GVYGRNFP---VDDIPASK----LTHIIYAFanIDPDGTVTIGDEWADIGNFGQLKALKKKNPGLkVLLS 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622  117 LGG-ADSHI--ELHKGEE--QAFADEIIRLVEVYGFDGLDIDLEQTAVDAGDNKTVIpDALKIVRAHFEKEQ---KHFII 188
Cdd:smart00636  73 IGGwTESDNfsSMLSDPAsrKKFIDSIVSFLKKYGFDGIDIDWEYPGGRGDDRENYT-ALLKELREALDKEGaegKGYLL 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622  189 SMAP---------EFPYLRTQGKYVPYITALeqEYDFIAP---------QLYNQAGDGISVGTE-----WIAQNNDSKKF 245
Cdd:smart00636 152 TIAVpagpdkidkGYGDLPAIAKYLDFINLM--TYDFHGAwsnptghnaPLYAGPGDPEKYNVDyavkyYLCKGVPPSKL 229
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 1106883622 550 HKGNTYRAKWWTRGNEPGTEQWGPW 574
Cdd:pfam02839   1 HNGKAYQAKWWTQGGDPPTSSGGPW 25
fn3 pfam00041
Fibronectin type III domain;
444-520 2.05e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 43.17  E-value: 2.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 444 SVPLNIAVSSISDKSVSLSWTQSTDNVGVV-GYYV-YRdgEQVGETATNTFSDA---------GLTANTEYSYTVKAFDE 512
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPItGYEVeYR--PKNSGEPWNEITVPgtttsvtltGLKPGTEYEVRVQAVNG 78


                  ....*...
gi 1106883622 513 AGNiSEES 520
Cdd:pfam00041  79 GGE-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 4.74e-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: 264.58  E-value: 4.74e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622  39 QVSVGYYHNWVpeQGAGYQGGRPADtdlakVNPFYNVIAVSFMKGEGIPTF--------KPYNMSDTEFRQKVATLNAED 110
Cdd:cd02871     1 KVLVGYWHNWD--NGAGSGRQDLDD-----VPSKYNVINVAFAEPTSDGGGevtfnngsSPGGYSPAEFKADIKALQAKG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 111 RVVLISLGGADSHIEL-HKGEEQAFADEIIRLVEVYGFDGLDIDLEQTAV--DAGDNKTVIPDALKIVRAHFEKEqkhFI 187
Cdd:cd02871    74 KKVLISIGGANGHVDLnHTAQEDNFVDSIVAIIKEYGFDGLDIDLESGSNplNATPVITNLISALKQLKDHYGPN---FI 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 188 ISMAPEFPYLR--------TQGKYVPYITALEQEYDFIAPQLYNQAGDGisvgtEWIAQNNDSKKFEFLYGISKAFNEG- 258
Cdd:cd02871   151 LTMAPETPYVQggyaayggIWGAYLPLIDNLRDDLTWLNVQYYNSGGMG-----GCDGQSYSQGTADFLVALADMLLTGf 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 259 ----SGGFIQIPANRLALGIPANIDAAANGFVkEPSKVYDVFEQMEKDQT-----------PLKGLMTWSINWDEGrnsa 323
Cdd:cd02871   226 piagNDRFPPLPADKVVIGLPASPSAAGGGYV-SPSEVIKALDCLMKGTNcgsyypaggypSLRGLMTWSINWDAT---- 300

                         330
                  ....*....|....*
gi 1106883622 324 gveYNESFAKSYQDL 338
Cdd:cd02871   301 ---NNYEFSKNYGAY 312
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
25-339 2.13e-74

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 246.59  E-value: 2.13e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622  25 AADAADTMPDISN---RQVSVGYYHNWVpeQGAGYQggrpadtDLAKVNPFYNVIAVSFMK----GEGIPTFK------- 90
Cdd:COG3469   198 ATTTATTTGPPTPglpKHVLVGYWHNFD--NGSGYI-------RLSDVPDKYDVINVAFAEptgaTNGTVTFTldpgsss 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622  91 PYNMSDTEFRQKVATLNAEDRVVLISLGGADSHIELHK-GEEQAFADEIIRLVEVYGFDGLDIDLEQ--TAVDAGDNKT- 166
Cdd:COG3469   269 PGGYTDAQFKADIAALQAQGKKVLLSIGGANGTVQLNTaAAADNFVNSVIALIDEYGFDGLDIDLEGgsNSLNAGDTDTp 348

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 167 ---VIPDALKIVRAHFekeQKHFIISMAPEFPYLRT--------QGKYVPYITALEQEYDFIAPQLYNQAGDGISVGtew 235
Cdd:COG3469   349 vitNLISALKQLKAKY---GPGFVLTMAPETPYVQGgyvayggiWGAYLPVILALRDILTLLHVQYYNSGSMLGLDG--- 422

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 236 iaQNNDSKKFEFLYGISKAFNEG------SGGFIQIPANRLALGIPANIDAAANGFVKePSKVYDVFEQMEKDQT----- 304
Cdd:COG3469   423 --QVYSQGTVDFLVAMADMLLEGfpvagnSNGFPGLRPDQVAIGLPASPSAAGGGYVS-PANVNKALDCLTKGTNcgsyk 499

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1106883622 305 ------PLKGLMTWSINWDEGrnsagveYNESFAKSYQDLF 339
Cdd:COG3469   500 prgtypGLRGLMTWSINWDAS-------NGYEFSNNVGAYL 533
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
244-561 3.80e-38

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 148.61  E-value: 3.80e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 244 KFEFLYGISKAFNEGSGGFIQIPANRLALGIPANIDAAANGFVKEPSKVYDVFEQMEKDQTPLKGLMTWSINWDEGRNSA 323
Cdd:COG3401   122 VGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEP 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 324 GVEYN------ESFAKSYQDLFQEKTPDTEKPSQPTNLAGTA-THSTVALSWTNSTDDrGVAGYYIYRDG------EQIG 390
Cdd:COG3401   202 GTTYYyrvaatDTGGESAPSNEVSVTTPTTPPSAPTGLTATAdTPGSVTLSWDPVTES-DATGYRVYRSNsgdgpfTKVA 280

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 391 RATNNAYTDTKLTASTEYTYTVKAFDAAGNVSEESKALVISTleeppaDLEAPSVPLNIAVSSISDKSVSLSWTQSTDNv 470
Cdd:COG3401   281 TVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVVSVTT------DLTPPAAPSGLTATAVGSSSITLSWTASSDA- 353

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 471 GVVGYYVYRDG------EQVGETATNT-FSDAGLTANTEYSYTVKAFDEAGNISEESKALVVTTADAPAVEAWDADTIYD 543
Cdd:COG3401   354 DVTGYNVYRSTsgggtyTKIAETVTTTsYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAV 433

                         330
                  ....*....|....*...
gi 1106883622 544 LGDIVTHKGNTYRAKWWT 561
Cdd:COG3401   434 PLTDVAGATAAASAASNP 451
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
343-556 2.39e-19

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 91.60  E-value: 2.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 343 TPDTEKPSQPTNLAGTATHST-VALSWTNSTDDrGVAGYYIYRDGEQIGR-------ATNNAYTDTKLTASTEYTYTVKA 414
Cdd:COG3401   321 TTDLTPPAAPSGLTATAVGSSsITLSWTASSDA-DVTGYNVYRSTSGGGTytkiaetVTTTSYTDTGLTPGTTYYYKVTA 399

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 415 FDAAGNVSEESKALVISTLEEPPADLEAPSVPLNIAVSSISdKSVSLSWTQSTDNVGVVGYYVYRDGEQVGETATNTFSD 494
Cdd:COG3401   400 VDAAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVAG-ATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVT 478

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1106883622 495 AGLTANTEYSYTVKAFDEAGNISEESkalVVTTADAPAVEAWDADTIYDLGDIVTHKGNTYR 556
Cdd:COG3401   479 ATTTDTTTANLSVTTGSLVGGSGASS---VTNSVSVIGASAAAAVGGAPDGTPNVTGASPVT 537
COG3979 COG3979
Chitodextrinase [Carbohydrate transport and metabolism];
441-543 1.46e-18

Chitodextrinase [Carbohydrate transport and metabolism];


Pssm-ID: 443178 [Multi-domain]  Cd Length: 369  Bit Score: 87.52  E-value: 1.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 441 EAPSVPLNIAVSSISDKSVSLSWTQSTDNVGVVGYYVYRDGEQVGETATNT-FSDAGLTANTEYSYTVKAFDEAGNISEE 519
Cdd:COG3979     1 QAPTAPTGLTASNVTSSSVSLSWDASTDNVGVTGYDVYRGGDQVATVTGLTaWTVTGLTPGTEYTFTVGACDAAGNVSAA 80

                          90       100
                  ....*....|....*....|....
gi 1106883622 520 SKALVVTTADAPAVEAWDADTIYD 543
Cdd:COG3979    81 SGTSTAMFGGSSTTLGSAEGVADT 104
COG3979 COG3979
Chitodextrinase [Carbohydrate transport and metabolism];
347-571 1.48e-18

Chitodextrinase [Carbohydrate transport and metabolism];


Pssm-ID: 443178 [Multi-domain]  Cd Length: 369  Bit Score: 87.52  E-value: 1.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 347 EKPSQPTNLAGTA-THSTVALSWTNSTDDRGVAGYYIYRDGEQIG-RATNNAYTDTKLTASTEYTYTVKAFDAAGNVSEE 424
Cdd:COG3979     1 QAPTAPTGLTASNvTSSSVSLSWDASTDNVGVTGYDVYRGGDQVAtVTGLTAWTVTGLTPGTEYTFTVGACDAAGNVSAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 425 SKALVISTLEEPPADLEAPSV---PLNIAVSSISDKSVSLSWTQSTDNVGVVGYYVYRDGEQVGETATNTFSDAGLTANT 501
Cdd:COG3979    81 SGTSTAMFGGSSTTLGSAEGVadtSGNLAASGAFFGVTTPPTPSSTLVVDGTTTVNAAATANGGTGGSGGTTTIITTGVE 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 502 EYSYTVKAFDEAGNISEESKALVVTTADAPAVEAWDADTIYDlGDIVTHKGNTYRAKWWTRGNEPGTEQW 571
Cdd:COG3979   161 GGGGSKTAQSLNAITAAGTAALNGGVVGGADEVLTCSAVKDD-GSGGAGAGNTYWALNTLGVSDTPSGTT 229
ChiC_BD cd12215
Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of ...
 535-576 2.92e-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: 72.60  E-value: 2.92e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1106883622 535 AWDADTIYDLGDIVTHKGNTYRAKWWTRGNEPGTEqWGPWEL 576
Cdd:cd12215     2 AWDASTVYTGGDQVTYNGKVYEAKWWTQGEEPGTS-WGVWKL 42
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
40-317 9.18e-14

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 72.49  E-value: 9.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622  40 VSVGYYHNWvpeqgAGYQGGRPADTDLakvnpfYNVIAVSFMKGEGI-PTFKPYNMSDTEFRQ--KVATLNAEDRVVLIS 116
Cdd:pfam00704   1 RIVGYYTSW-----GVYRNGNFLPSDK------LTHIIYAFANIDGSdGTLFIGDWDLGNFEQlkKLKKQKNPGVKVLLS 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 117 LGGAD-----SHIELHKGEEQAFADEIIRLVEVYGFDGLDIDLEQTAVDAGDNKTViPDALKIVRAHFEKEQ--KHFIIS 189
Cdd:pfam00704  70 IGGWTdstgfSLMASNPASRKKFADSIVSFLRKYGFDGIDIDWEYPGGNPEDKENY-DLLLRELRAALDEAKggKKYLLS 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 190 MAPEFPY--------LRTQGKYVPYI--------TALEQEYDFIAPqLYNQAGDGISVGTE-WIAQNNDSKKFeFL---- 248
Cdd:pfam00704 149 AAVPASYpdldkgydLPKIAKYLDFInvmtydfhGSWDNVTGHHAP-LYGGGSYNVDYAVKyYLKQGVPASKL-VLgvpf 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 249 YGIS--------KAFNEGSGGFIQIPANRLALGIPANIDAAAN-GFVKEPSKV--YDVFEQME-----KDQTPLKGLMTW 312
Cdd:pfam00704 227 YGRSwtlvngsgNTWEDGVLAYKEICNLLKDNGATVVWDDVAKaPYVYDGDQFitYDDPRSIAtkvdyVKAKGLGGVMIW 306


                  ....*
gi 1106883622 313 SINWD 317
Cdd:pfam00704 307 SLDAD 311
ChtBD3 smart00495
Chitin-binding domain type 3;
533-574 6.29e-13

Chitin-binding domain type 3;


Pssm-ID: 197760 [Multi-domain]  Cd Length: 41  Bit Score: 63.05  E-value: 6.29e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1106883622  533 VEAWDADTIYDLGDIVTHKGNTYRAKWWTRGNEPGTeQWGPW 574
Cdd:smart00495   1 APAWQAGTVYTAGDVVSYNGKVYKAKWWTQGEEPGS-SSGPW 41
GH18_chitinase-like cd00598
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ...
 42-223 9.82e-11

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: 61.62  E-value: 9.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622  42 VGYYHNWVPeqgagYQGGRPADTDLAKvnpfYNVIAVSFM--KGEGIPTFKPYNMSD------TEFRQKVATLnaedrVV 113
Cdd:cd00598     2 ICYYDGWSS-----GRGPDPTDIPLSL----CTHIIYAFAeiSSDGSLNLFGDKSEEplkgalEELASKKPGL-----KV 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 114 LISLGGADSHIELHKGEE----QAFADEIIRLVEVYGFDGLDIDLEQ-TAVDAGDnKTVIPDALKIVRAHFekEQKHFII 188
Cdd:cd00598    68 LISIGGWTDSSPFTLASDpasrAAFANSLVSFLKTYGFDGVDIDWEYpGAADNSD-RENFITLLRELRSAL--GAANYLL 144

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1106883622 189 SMAPefPYLRTQGKYVPYITALEQEYDFIAPQLYN 223
Cdd:cd00598   145 TIAV--PASYFDLGYAYDVPAIGDYVDFVNVMTYD 177
Glyco_18 smart00636
Glyco_18 domain;
40-245 1.74e-10

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 62.70  E-value: 1.74e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622   40 VSVGYYHNWvPEQGAGYQggrPADTDLAKvnpfYNVIAVSF--MKGEGIPTFKPYNMSDTEFRQKVATLNAEDRV-VLIS 116
Cdd:smart00636   1 RVVGYFTNW-GVYGRNFP---VDDIPASK----LTHIIYAFanIDPDGTVTIGDEWADIGNFGQLKALKKKNPGLkVLLS 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622  117 LGG-ADSHI--ELHKGEE--QAFADEIIRLVEVYGFDGLDIDLEQTAVDAGDNKTVIpDALKIVRAHFEKEQ---KHFII 188
Cdd:smart00636  73 IGGwTESDNfsSMLSDPAsrKKFIDSIVSFLKKYGFDGIDIDWEYPGGRGDDRENYT-ALLKELREALDKEGaegKGYLL 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622  189 SMAP---------EFPYLRTQGKYVPYITALeqEYDFIAP---------QLYNQAGDGISVGTE-----WIAQNNDSKKF 245
Cdd:smart00636 152 TIAVpagpdkidkGYGDLPAIAKYLDFINLM--TYDFHGAwsnptghnaPLYAGPGDPEKYNVDyavkyYLCKGVPPSKL 229
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 443-527 3.68e-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: 56.74  E-value: 3.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 443 PSVPLNIAVSSISDKSVSLSWTQSTDNVG-VVGYYVYR------DGEQVGETA--TNTFSDAGLTANTEYSYTVKAFDEA 513
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGpITGYVVEYrekgsgDWKEVEVTPgsETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|....
gi 1106883622 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 5.77e-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: 53.00  E-value: 5.77e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622  443 PSVPLNIAVSSISDKSVSLSWTQSTDNVG---VVGYYVYRDGEQVGET------ATNTFSDAGLTANTEYSYTVKAFDEA 513
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItgyIVGYRVEYREEGSEWKevnvtpSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                   .
gi 1106883622  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 4.70e-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: 49.25  E-value: 4.70e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1106883622 528 ADAPAVEAWDADTIYDLGDIVTHKGNTYRAKWWTRgNEPGTEqwGPWELIG 578
Cdd:cd12204     1 AGANAYPNWPQGTHAAGGDLVSYNGAVYQAKWWTQ-SAPGSD--SSWTLVC 48
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
355-543 4.89e-08

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


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 56.11  E-value: 4.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 355 LAGTATHSTVALSWTNSTddrGVAGYYI-YRDGE----QIGRATNNAYTDTKLTASTeYTYTVKAFDAAGNVSEESKALV 429
Cdd:COG4733   545 VAQGTAVTTLTVSWDAPA---GAVAYEVeWRRDDgnwvSVPRTSGTSFEVPGIYAGD-YEVRVRAINALGVSSAWAASSE 620

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 430 ISTLeeppADLEAPSVPLNIAVSSISDkSVSLSWTQSTDnVGVVGYYVYRDGEQVGETAT--------NTFSDAGLTANT 501
Cdd:COG4733   621 TTVT----GKTAPPPAPTGLTATGGLG-GITLSWSFPVD-ADTLRTEIRYSTTGDWASATvaqalypgNTYTLAGLKAGQ 694

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1106883622 502 EYSYTVKAFDEAGNISEESkALVVTTADAPAVEAWDADTIYD 543
Cdd:COG4733   695 TYYYRARAVDRSGNVSAWW-VSGQASADAAGILDAITGQILE 735
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 349-432 1.25e-07

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: 49.80  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 349 PSQPTNLAGTATHST-VALSWTNSTDDRG-VAGYYIYR------DGEQI--GRATNNAYTDTKLTASTEYTYTVKAFDAA 418
Cdd:cd00063     1 PSPPTNLRVTDVTSTsVTLSWTPPEDDGGpITGYVVEYrekgsgDWKEVevTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|....
gi 1106883622 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 1106883622 550 HKGNTYRAKWWTRGNEPGTEQWGPW 574
Cdd:pfam02839   1 HNGKAYQAKWWTQGGDPPTSSGGPW 25
ChtBD3 cd00036
Chitin/cellulose binding domains of chitinase and related enzymes; This group contains ...
 535-568 7.16e-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: 45.83  E-value: 7.16e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1106883622 535 AWDADTIYDLGDIVTHKGNTYRAKWWTRGNEPGT 568
Cdd:cd00036     1 AWPNPTHYTAGQSVVYNGNLYTANWYTAGSVPGS 34
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 349-419 7.25e-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: 44.53  E-value: 7.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622  349 PSQPTNLAGTA-THSTVALSWTNSTDDRG---VAGYYIYRDG------EQIGRATNNAYTDTKLTASTEYTYTVKAFDAA 418
Cdd:smart00060   1 PSPPSNLRVTDvTSTSVTLSWEPPPDDGItgyIVGYRVEYREegsewkEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                   .
gi 1106883622  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 1.52e-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: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 132 QAFADEIIRLVEVYGFDGLDIDLE--QTAVDAGDNKTVipdaLKIVRAHFEKE-----QKHFIISMAPEF-PYLRTQGKY 203
Cdd:cd02879    94 KAFINSSIKVARKYGFDGLDLDWEfpSSQVEMENFGKL----LEEWRAAVKDEarssgRPPLLLTAAVYFsPILFLSDDS 169

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1106883622 204 VPY-ITALEQEYDFIAPQLYNQAGDGISVGTEWIAQNND-SKKFEFLYGISKAFNEGsggfiqIPANRLALGIP 275
Cdd:cd02879   170 VSYpIEAINKNLDWVNVMAYDYYGSWESNTTGPAAALYDpNSNVSTDYGIKSWIKAG------VPAKKLVLGLP 237
fn3 pfam00041
Fibronectin type III domain;
444-520 2.05e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 43.17  E-value: 2.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 444 SVPLNIAVSSISDKSVSLSWTQSTDNVGVV-GYYV-YRdgEQVGETATNTFSDA---------GLTANTEYSYTVKAFDE 512
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPItGYEVeYR--PKNSGEPWNEITVPgtttsvtltGLKPGTEYEVRVQAVNG 78


                  ....*...
gi 1106883622 513 AGNiSEES 520
Cdd:pfam00041  79 GGE-GPPS 85
GH18_hevamine_XipI_class_III cd02877
This conserved domain family includes xylanase inhibitor Xip-I, and the class III plant ...
 54-322 2.18e-04

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: 43.38  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622  54 AGYQGGRPADTDLAKV--NPFYNVIAVSFMKGEGIPTFKPYNMS---DTEFRQKVATLNAEDRV-------VLISLGGAD 121
Cdd:cd02877     4 AVYWGQNSDEGSLREYcdTGNYDIVNISFLNVFGSGGTPGLNFAghcGGSTYPNCPQLGADIKHcqskgkkVLLSIGGAG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 122 SHIELhKGEEQA--FADeiiRLVEVYG---------------FDGLDIDLEQTAVDAGDnktvipDALKIVRAHFEKEQ- 183
Cdd:cd02877    84 GSYSL-SSDADAkdFAD---YLWNAFGggtdsgvprpfgdavVDGFDFDIEHGSPENYD------ALAKRLRSLFASDPs 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 184 KHFIISMAPEFPYlrtqgkyvPYI---TALEQ-EYDFIAPQLYNQAGdgisvgteWIAQNNDSKKFEFlygiskAFNEGS 259
Cdd:cd02877   154 KKYYLTAAPQCPY--------PDAslgDAIATgLFDFIFVQFYNNPC--------CSYASGNASGFNF------NWDTWT 211

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1106883622 260 GGFIQIPANRLALGIPANIDAAANGFVkEPSKVYDVFEQMEKDQTPLKGLMTWSINWDEGRNS 322
Cdd:cd02877   212 SWAKATSNAKVFLGLPASPEAAGSGYV-DPSELASLVLPVKQKSPNFGGVMLWDASQDKQGTG 273
fn3 pfam00041
Fibronectin type III domain;
350-425 3.24e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 39.71  E-value: 3.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 350 SQPTNLAGTA-THSTVALSWTNSTDDRG-VAGYYI-YRDGEQIGRATN-------NAYTDTKLTASTEYTYTVKAFDAAG 419
Cdd:pfam00041   1 SAPSNLTVTDvTSTSLTVSWTPPPDGNGpITGYEVeYRPKNSGEPWNEitvpgttTSVTLTGLKPGTEYEVRVQAVNGGG 80


                  ....*.
gi 1106883622 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 5.81e-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: 42.23  E-value: 5.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622  41 SVGYYHNWVPeQGAGYQGGRPADTD-LAKVN-PFYNVIA----VSFMKGEGIPTFKPYNMSDTEFRQKVA-------TLN 107
Cdd:cd06548     1 VVGYFTNWGI-YGRNYFVTDDIPADkLTHINyAFADIDGdggvVTSDDEAADEAAQSVDGGADTDDQPLKgnfgqlrKLK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 108 AEDR--VVLISLGG-ADSHI--ELHKGEE--QAFADEIIRLVEVYGFDGLDIDLEQTAVDAGDNKTVIPD-------ALK 173
Cdd:cd06548    80 QKNPhlKILLSIGGwTWSGGfsDAAATEAsrAKFADSAVDFIRKYGFDGIDIDWEYPGSGGAPGNVARPEdkenftlLLK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 174 IVRAHF----EKEQKHFIISMA-PEFP-YLRTQG-----KYVPYITAleQEYDFIAP---------QLYNQAGD-GISVG 232
Cdd:cd06548   160 ELREALdalgAETGRKYLLTIAaPAGPdKLDKLEvaeiaKYLDFINL--MTYDFHGAwsnttghhsNLYASPADpPGGYS 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1106883622 233 TEWIAQNNDSKKfeflygiskafnegsggfiqIPANRLALGIPA 276
Cdd:cd06548   238 VDAAVNYYLSAG--------------------VPPEKLVLGVPF 261
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
349-549 7.83e-04

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


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 42.62  E-value: 7.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 349 PSQPTNLAGTATHSTVALSWTNSTDDrGVAGYYIYRDGEQ--------IGRATNNAYTDTKLTASTEYTYTVKAFDAAGN 420
Cdd:COG4733   630 PPAPTGLTATGGLGGITLSWSFPVDA-DTLRTEIRYSTTGdwasatvaQALYPGNTYTLAGLKAGQTYYYRARAVDRSGN 708

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 421 VSE-----ESKALVISTLEEPPADLEAPSVPLNIAVSSISDKSVSLSWTQSTDNVGVVGYYVYRDGEQVGETATNTFSDA 495
Cdd:COG4733   709 VSAwwvsgQASADAAGILDAITGQILETELGQELDAIIQNATVAEVVAATVTDVTAQIDTAVLFAGVATAAAIGAEARVA 788

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1106883622 496 GLTANTEYSYTVKAFDEAGNISEESKALVVTTADAPAVEAWDADTIYDLGDIVT 549
Cdd:COG4733   789 ATVAESATAAAATGTAADAAGDASGGVTAGTSGTTGAGDTAASTTRVAAAVVLA 842
GH18_3CO4_chitinase cd06545
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an ...
 98-275 1.62e-03

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: 40.51  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622  98 EFRQKVATLNAEDRVVLISLGGADSHIE----LHKGEEQAFADEIIRLVEVYGFDGLDIDLEQTAVDAGDNKTVIpdalK 173
Cdd:cd06545    47 ELNSVVNAAHAHNVKILISLAGGSPPEFtaalNDPAKRKALVDKIINYVVSYNLDGIDVDLEGPDVTFGDYLVFI----R 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 174 IVRAHFEKEQKhFIISMAPEfpylRTQGkYVPyiTALEQEYDFIAPQLYNqagdgiSVGTEWIAQNNDSKKFEFLygiSK 253
Cdd:cd06545   123 ALYAALKKEGK-LLTAAVSS----WNGG-AVS--DSTLAYFDFINIMSYD------ATGPWWGDNPGQHSSYDDA---VN 185

                         170       180
                  ....*....|....*....|....
gi 1106883622 254 AFN--EGSGgfiQIPANRLALGIP 275
Cdd:cd06545   186 DLNywNERG---LASKDKLVLGLP 206
GH18_chitolectin_chitotriosidase cd02872
This conserved domain family includes a large number of catalytically inactive chitinase-like ...
 42-275 2.37e-03

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: 40.62  E-value: 2.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622  42 VGYYHNWvpeqgAGYQGGR----PADTD----------LAKVNPFYNVIavsfmkgegipTFKPYNMSDTEFRQKVATL- 106
Cdd:cd02872     2 VCYFTNW-----AQYRPGNgkfvPENIDpflcthiiyaFAGLNPDGNII-----------ILDEWNDIDLGLYERFNALk 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 107 -NAEDRVVLISLGG------------ADSHIElhkgeeQAFADEIIRLVEVYGFDGLDIDLE---QTAVDAGDnKTVIPD 170
Cdd:cd02872    66 eKNPNLKTLLAIGGwnfgsakfsamaASPENR------KTFIKSAIAFLRKYGFDGLDLDWEypgQRGGPPED-KENFVT 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622 171 ALKIVRAHFEKEQKHFIISMAP-----------EFPYLrtqGKYVPYITALeqEYDF----------IAPqLYNQAGDgi 229
Cdd:cd02872   139 LLKELREAFEPEAPRLLLTAAVsagketidaayDIPEI---SKYLDFINVM--TYDFhgswegvtghNSP-LYAGSAD-- 210

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1106883622 230 svgTEWIAQNNDSkkfeflYGISKAFNEGSggfiqiPANRLALGIP 275
Cdd:cd02872   211 ---TGDQKYLNVD------YAIKYWLSKGA------PPEKLVLGIP 241
ChiA COG3325
Chitinase, GH18 family [Carbohydrate transport and metabolism];
25-155 2.59e-03

Chitinase, GH18 family [Carbohydrate transport and metabolism];


Pssm-ID: 442554 [Multi-domain]  Cd Length: 391  Bit Score: 40.28  E-value: 2.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622  25 AADAADTMPDISNRQVSVGYYHNWvpeqGAGYQGGRPADTDLAKVN----PFYNVIA---VSFMKGEGIPTFKPYNMSDT 97
Cdd:COG3325     5 SVSDTAAAATATSGKRVVGYFTQW----GIYGRNYLVKDIPASKLThinyAFANVDPdgkCSVGDAWAKPSVDGAADDWD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1106883622  98 E-----FRQkVATLNAE--DRVVLISLGG---AD--SHIELHKGEEQAFADEIIRLVEVYGFDGLDIDLE 155
Cdd:COG3325    81 QplkgnFNQ-LKKLKAKnpNLKVLISIGGwtwSKgfSDAAATPASRAAFVDSCVDLLRKYNFDGIDIDWE 149
ChiA1_BD cd12214
chitin-binding domain of Chi A1-like proteins; This group contains proteins related to the ...
 535-557 4.96e-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: 35.00  E-value: 4.96e-03
                          10        20
                  ....*....|....*....|...
gi 1106883622 535 AWDADTIYDLGDIVTHKGNTYRA 557
Cdd:cd12214     1 EWAAGTTYKAGDIVTYNGKLYRC 23
Big_7 pfam17957
Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in ...
 352-412 7.09e-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: 35.28  E-value: 7.09e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1106883622 352 PTNLAgTATHSTVALSWTnSTDDRGVAGYYIYRDGEQIGRATNNAYT---DTKLTASTEYTYTV 412
Cdd:pfam17957   6 PANGA-TVSGGTVTISAT-ASDDGGVSKVEFYVDGTLVGTDTSAPYSftwTTTALANGTHTITV 67
Big_7 pfam17957
Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in ...
 452-507 7.09e-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: 35.28  E-value: 7.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1106883622 452 SSISDKSVSLSWTqSTDNVGVVGYYVYRDGEQVGETATNTFS---DAGLTANTEYSYTV 507
Cdd:pfam17957  10 ATVSGGTVTISAT-ASDDGGVSKVEFYVDGTLVGTDTSAPYSftwTTTALANGTHTITV 67
 
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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