|
Name |
Accession |
Description |
Interval |
E-value |
| ChiA |
COG3325 |
Chitinase, GH18 family [Carbohydrate transport and metabolism]; |
29-455 |
9.93e-143 |
|
Chitinase, GH18 family [Carbohydrate transport and metabolism];
Pssm-ID: 442554 [Multi-domain] Cd Length: 391 Bit Score: 424.32 E-value: 9.93e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 29 AKAAENVPQYRNVMYYGDWSIWGGegNFYPKDIPADQLTHLNFAFLDFNSNGDLVFTDKDAAVGapVGQEGVQWGGANAG 108
Cdd:COG3325 10 AAAATATSGKRVVGYFTQWGIYGR--NYLVKDIPASKLTHINYAFANVDPDGKCSVGDAWAKPS--VDGAADDWDQPLKG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 109 VLNAIQDLRAQNPNLKIGVSVGGWSKSGDFSTVAADPTKRANFVKNVMKFVKYTNMDFVDLDWEYPASVRDADLVDNknd 188
Cdd:COG3325 86 NFNQLKKLKAKNPNLKVLISIGGWTWSKGFSDAAATPASRAAFVDSCVDLLRKYNFDGIDIDWEYPGSGGAPGNVYR--- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 189 egtpnakPADKQNFITLLQDLRTALDKQGVDINKKYELSVALPAAKSTLEnGIDVANLFKVVDFANVMTYDLNGAWTPNS 268
Cdd:COG3325 163 -------PEDKANFTALLKELRAQLDALGAETGKHYLLTAAAPAGPDKLD-GIELPKVAQYLDYVNVMTYDFHGAWSPTT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 269 AHHTALYGNPKDPnYDSGFSVDQTVKYLKEKGAVSNKIVVGAAFYTRGWNKVAAGTDtalpGLFQAAEktnkdadgslty 348
Cdd:COG3325 235 GHQAPLYDSPKDP-EAQGYSVDSAVQAYLAAGVPASKLVLGVPFYGRGWTGVTGGNN----GLYQPAT------------ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 349 gannenpiKTGDGGRAGGVWAYRSIDALKAKTPTLKEYWDDTAKAPYLYSKETGEFYTYDNTRSIGYKAQYVKDNNLGGM 428
Cdd:COG3325 298 --------GPAPGTWEAGVNDYKDLKALYLGSNGYTRYWDDVAKAPYLYNGDTGTFISYDDPRSIAAKADYVKDKGLGGV 369
|
410 420
....*....|....*....|....*..
gi 1560718296 429 ISWMQSQDktttsTKRDELTKAIKSGL 455
Cdd:COG3325 370 MFWELSGD-----TADGTLLNAIGEGL 391
|
|
| GH18_chitinase |
cd06548 |
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ... |
40-436 |
2.27e-125 |
|
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: 376.97 E-value: 2.27e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 40 NVMYYGDWSIWGGeGNFYPKDIPADQLTHLNFAFLDFNSNGDLVFTDKDAAVGA--PVGQEGVQWGGANAGVLNAIQDLR 117
Cdd:cd06548 1 VVGYFTNWGIYGR-NYFVTDDIPADKLTHINYAFADIDGDGGVVTSDDEAADEAaqSVDGGADTDDQPLKGNFGQLRKLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 118 AQNPNLKIGVSVGGWSKSGDFSTVAADPTKRANFVKNVMKFVKYTNMDFVDLDWEYPASvrdadlvdnkNDEGTPNAKPA 197
Cdd:cd06548 80 QKNPHLKILLSIGGWTWSGGFSDAAATEASRAKFADSAVDFIRKYGFDGIDIDWEYPGS----------GGAPGNVARPE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 198 DKQNFITLLQDLRTALDKQGVDINKKYELSVALPAAKSTLENgIDVANLFKVVDFANVMTYDLNGAWTPNSAHHTALYGN 277
Cdd:cd06548 150 DKENFTLLLKELREALDALGAETGRKYLLTIAAPAGPDKLDK-LEVAEIAKYLDFINLMTYDFHGAWSNTTGHHSNLYAS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 278 PKDPNydSGFSVDQTVKYLKEKGAVSNKIVVGAAFYTRGWNKvaagtdtalpglfqaaektnkdadgsltygannenpik 357
Cdd:cd06548 229 PADPP--GGYSVDAAVNYYLSAGVPPEKLVLGVPFYGRGWTG-------------------------------------- 268
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1560718296 358 tgdggraggvwayrsidalkaktptLKEYWDDTAKAPYLYSKETGEFYTYDNTRSIGYKAQYVKDNNLGGMISWMQSQD 436
Cdd:cd06548 269 -------------------------YTRYWDEVAKAPYLYNPSTKTFISYDDPRSIKAKADYVKDKGLGGVMFWELSGD 322
|
|
| Glyco_18 |
smart00636 |
Glyco_18 domain; |
39-436 |
4.36e-104 |
|
Glyco_18 domain;
Pssm-ID: 214753 [Multi-domain] Cd Length: 334 Bit Score: 322.32 E-value: 4.36e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 39 RNVMYYGDWSIWGGegNFYPKDIPADQLTHLNFAFLDFNSNGDLVFTDKDAAVGapvgqegvqwggaNAGVLNAiqdLRA 118
Cdd:smart00636 1 RVVGYFTNWGVYGR--NFPVDDIPASKLTHIIYAFANIDPDGTVTIGDEWADIG-------------NFGQLKA---LKK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 119 QNPNLKIGVSVGGWSKSGDFSTVAADPTKRANFVKNVMKFVKYTNMDFVDLDWEYpasvrdadlvdnkndegtPNAKPAD 198
Cdd:smart00636 63 KNPGLKVLLSIGGWTESDNFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWEY------------------PGGRGDD 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 199 KQNFITLLQDLRTALDKQGVDiNKKYELSVALPAAKSTLENGID-VANLFKVVDFANVMTYDLNGAWTPNSAHHTALYGN 277
Cdd:smart00636 125 RENYTALLKELREALDKEGAE-GKGYLLTIAVPAGPDKIDKGYGdLPAIAKYLDFINLMTYDFHGAWSNPTGHNAPLYAG 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 278 PKDPNYdsgFSVDQTVKYLKEKGAVSNKIVVGAAFYTRGWNKVAAGTDTalpglfqAAEKTNKDADGsltygannenpik 357
Cdd:smart00636 204 PGDPEK---YNVDYAVKYYLCKGVPPSKLVLGIPFYGRGWTLVDGSNNG-------PGAPFTGPATG------------- 260
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1560718296 358 tGDGGRAGGVWAYRSIdalkAKTPTLKEYWDDTAKAPYLYSKETGEFYTYDNTRSIGYKAQYVKDNNLGGMISWMQSQD 436
Cdd:smart00636 261 -GPGTWEGGVVDYREI----CKLLGATVVYDDTAKAPYAYNPGTGQWVSYDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
|
|
| Glyco_hydro_18 |
pfam00704 |
Glycosyl hydrolases family 18; |
39-436 |
2.72e-85 |
|
Glycosyl hydrolases family 18;
Pssm-ID: 425828 [Multi-domain] Cd Length: 311 Bit Score: 272.41 E-value: 2.72e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 39 RNVMYYGDWSIWGgEGNFypkdIPADQLTHLNFAFLDFNS-NGDLVFTDKDAavgapvgqegvqwgganaGVLNAIQDLR 117
Cdd:pfam00704 1 RIVGYYTSWGVYR-NGNF----LPSDKLTHIIYAFANIDGsDGTLFIGDWDL------------------GNFEQLKKLK 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 118 AQ-NPNLKIGVSVGGWSKSGDFSTVAADPTKRANFVKNVMKFVKYTNMDFVDLDWEYpasvrdadlvdnkndegtPNAKP 196
Cdd:pfam00704 58 KQkNPGVKVLLSIGGWTDSTGFSLMASNPASRKKFADSIVSFLRKYGFDGIDIDWEY------------------PGGNP 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 197 ADKQNFITLLQDLRTALDKQgvDINKKYELSVALPAAKSTLENGIDVANLFKVVDFANVMTYDLNGAWTPNSAHHTALYG 276
Cdd:pfam00704 120 EDKENYDLLLRELRAALDEA--KGGKKYLLSAAVPASYPDLDKGYDLPKIAKYLDFINVMTYDFHGSWDNVTGHHAPLYG 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 277 npkdpnyDSGFSVDQTVKYLKEKGAVSNKIVVGAAFYTRGWNKVAAGTDTalpglfqaaektnkdadgsltygannenpi 356
Cdd:pfam00704 198 -------GGSYNVDYAVKYYLKQGVPASKLVLGVPFYGRSWTLVNGSGNT------------------------------ 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 357 ktgdggRAGGVWAYRSIDALKaKTPTLKEYWDDTAKAPYLYSkeTGEFYTYDNTRSIGYKAQYVKDNNLGGMISWMQSQD 436
Cdd:pfam00704 241 ------WEDGVLAYKEICNLL-KDNGATVVWDDVAKAPYVYD--GDQFITYDDPRSIATKVDYVKAKGLGGVMIWSLDAD 311
|
|
| GH18_LinChi78-like_UFR |
cd20174 |
an unknown function domain of Listeria innocua LinChi78 GH18 chitinase that is essential for ... |
471-605 |
2.75e-60 |
|
an unknown function domain of Listeria innocua LinChi78 GH18 chitinase that is essential for its catalytic activity; found in similar chitinase-like proteins; This domain is referred to as an unknown-function region (UFR) and shown to be necessary for the hydrolytic activity of LinChi78 glycosyl hydrolase family 18 (GH18) chitinase (a product of the lin0153gene) from the nonpathogenic bacterium Listeria innocua. The catalytic domain (CatD) of GH18 chitinases folds into a TIM barrel and has a conserved DXXDXDXE motif, in which the Glu residue functions as a catalytic residue; these chitinases contain additional domains such as a chitin-binding domain (ChBD) and/or a fibronectin type III-like (FnIII) domain. LinChi78 consists of a CatD, a FnIII, and a ChBD domain, and has this UFR region located between the CatD and the FnIII domain. Its catalytic site is composed of a typical CatD and a portion of this UFR, in particular the key Gln and Ile residues which are indispensable for LinChi78 to exhibit full catalytic activity. This UFR domain is also found in proteins where it is located between a CatD domain and DUF5011 and ChBD(s) domains. LinChi78 exhibits chitinase activity towards artificial and natural substrates, including colloidal chitin and chitin oligosaccharides of various lengths, and hydrolyzes these in a processive manner. Members of this family include some uncharacterized chitinase-like proteins from pathogenic bacteria such as Listeria monocytogenes and Clostridium botulinum.
Pssm-ID: 380910 Cd Length: 136 Bit Score: 199.43 E-value: 2.75e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 471 LNVVATVKPYSE-NGVGYEITITNNEKADETNEVLKSTELSFETVKLPKFYIPVKAGETLTAGDYKAGTVTTSGGNTVVD 549
Cdd:cd20174 1 LNVSATVTPYTEsGGEGYEITITNNEKLEESGEVLSAVEKAAKTIKNPKLYIKTKDGETLTSGDYKAGTVTTENGYTVVD 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1560718296 550 LASVYDAQQIPQGASYTFRLKSSASSVDVANISKIDLTQRMVKSSVEFGKQTIFGG 605
Cdd:cd20174 81 LSTVYDGKFIKPGASYTFKLKTDAGAADLSNIESIELSQRIVSSGPELGRQTIYGD 136
|
|
| ChiC_BD |
cd12215 |
Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of ... |
712-752 |
9.01e-17 |
|
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: 74.15 E-value: 9.01e-17
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1560718296 712 PAWDAAKTYNKGDRVSYKGKTYEAQWWTQGNEPGAEqWGPW 752
Cdd:cd12215 1 PAWDASTVYTGGDQVTYNGKVYEAKWWTQGEEPGTS-WGVW 40
|
|
| COG3979 |
COG3979 |
Chitodextrinase [Carbohydrate transport and metabolism]; |
616-721 |
2.60e-15 |
|
Chitodextrinase [Carbohydrate transport and metabolism];
Pssm-ID: 443178 [Multi-domain] Cd Length: 369 Bit Score: 78.27 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 616 EAPTVPKALTSSNVTDKSATLTWTASTDNKAVAGYKVYRNGTEVGSVSG-TTFTDSGLTAKTAYSYTVKAYDAAGNFSAA 694
Cdd:COG3979 1 QAPTAPTGLTASNVTSSSVSLSWDASTDNVGVTGYDVYRGGDQVATVTGlTAWTVTGLTPGTEYTFTVGACDAAGNVSAA 80
|
90 100
....*....|....*....|....*..
gi 1560718296 695 SSALTVTTLDAATPPATPAWDAAKTYN 721
Cdd:COG3979 81 SGTSTAMFGGSSTTLGSAEGVADTSGN 107
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
467-713 |
4.26e-14 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 75.81 E-value: 4.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 467 TYANLNVVATVKPYSENGVGYEITITNNEKADETNEVLKSTELSFETVKLPKFYIPVKAGETLTAGDYKAGTVTTSGGNT 546
Cdd:COG3401 107 TNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLT 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 547 VVDLASVYDAQQIPQGASYTFRLKSsassVDVANISKIDLTQRMVKSsvefgkqtifgggtvvpdpsdTEAPTVPKALTS 626
Cdd:COG3401 187 VTSTTLVDGGGDIEPGTTYYYRVAA----TDTGGESAPSNEVSVTTP---------------------TTPPSAPTGLTA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 627 SNVTDKSATLTWTASTdNKAVAGYKVYRNG------TEVGSVSGTTFTDSGLTAKTAYSYTVKAYDAAGNFSAASSALTV 700
Cdd:COG3401 242 TADTPGSVTLSWDPVT-ESDATGYRVYRSNsgdgpfTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVVSV 320
|
250
....*....|...
gi 1560718296 701 TTldAATPPATPA 713
Cdd:COG3401 321 TT--DLTPPAAPS 331
|
|
| ChtBD3 |
smart00495 |
Chitin-binding domain type 3; |
712-752 |
3.51e-13 |
|
Chitin-binding domain type 3;
Pssm-ID: 197760 [Multi-domain] Cd Length: 41 Bit Score: 64.20 E-value: 3.51e-13
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1560718296 712 PAWDAAKTYNKGDRVSYKGKTYEAQWWTQGNEPGAeQWGPW 752
Cdd:smart00495 2 PAWQAGTVYTAGDVVSYNGKVYKAKWWTQGEEPGS-SSGPW 41
|
|
| FN3 |
cd00063 |
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ... |
618-702 |
1.67e-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: 58.28 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 618 PTVPKALTSSNVTDKSATLTWTAST-DNKAVAGYKVYRNGT--------EVGSVSGTTFTDSGLTAKTAYSYTVKAYDAA 688
Cdd:cd00063 1 PSPPTNLRVTDVTSTSVTLSWTPPEdDGGPITGYVVEYREKgsgdwkevEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80
|
90
....*....|....
gi 1560718296 689 GNfSAASSALTVTT 702
Cdd:cd00063 81 GE-SPPSESVTVTT 93
|
|
| FN3 |
smart00060 |
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
618-689 |
4.01e-07 |
|
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: 48.38 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 618 PTVPKALTSSNVTDKSATLTWTASTDNKA---VAGYKVYRNGTE------VGSVSGTTFTDSGLTAKTAYSYTVKAYDAA 688
Cdd:smart00060 1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItgyIVGYRVEYREEGsewkevNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80
|
.
gi 1560718296 689 G 689
Cdd:smart00060 81 G 81
|
|
| CBM_5_12 |
pfam02839 |
Carbohydrate binding domain; This short domain is found in many different glycosyl hydrolase ... |
728-752 |
1.88e-06 |
|
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: 44.51 E-value: 1.88e-06
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
621-690 |
1.20e-05 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 43.94 E-value: 1.20e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1560718296 621 PKALTSSNVTDKSATLTWTASTD-NKAVAGYKV-YRNGTEVG-----SVSGTT--FTDSGLTAKTAYSYTVKAYDAAGN 690
Cdd:pfam00041 3 PSNLTVTDVTSTSLTVSWTPPPDgNGPITGYEVeYRPKNSGEpwneiTVPGTTtsVTLTGLKPGTEYEVRVQAVNGGGE 81
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ChiA |
COG3325 |
Chitinase, GH18 family [Carbohydrate transport and metabolism]; |
29-455 |
9.93e-143 |
|
Chitinase, GH18 family [Carbohydrate transport and metabolism];
Pssm-ID: 442554 [Multi-domain] Cd Length: 391 Bit Score: 424.32 E-value: 9.93e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 29 AKAAENVPQYRNVMYYGDWSIWGGegNFYPKDIPADQLTHLNFAFLDFNSNGDLVFTDKDAAVGapVGQEGVQWGGANAG 108
Cdd:COG3325 10 AAAATATSGKRVVGYFTQWGIYGR--NYLVKDIPASKLTHINYAFANVDPDGKCSVGDAWAKPS--VDGAADDWDQPLKG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 109 VLNAIQDLRAQNPNLKIGVSVGGWSKSGDFSTVAADPTKRANFVKNVMKFVKYTNMDFVDLDWEYPASVRDADLVDNknd 188
Cdd:COG3325 86 NFNQLKKLKAKNPNLKVLISIGGWTWSKGFSDAAATPASRAAFVDSCVDLLRKYNFDGIDIDWEYPGSGGAPGNVYR--- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 189 egtpnakPADKQNFITLLQDLRTALDKQGVDINKKYELSVALPAAKSTLEnGIDVANLFKVVDFANVMTYDLNGAWTPNS 268
Cdd:COG3325 163 -------PEDKANFTALLKELRAQLDALGAETGKHYLLTAAAPAGPDKLD-GIELPKVAQYLDYVNVMTYDFHGAWSPTT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 269 AHHTALYGNPKDPnYDSGFSVDQTVKYLKEKGAVSNKIVVGAAFYTRGWNKVAAGTDtalpGLFQAAEktnkdadgslty 348
Cdd:COG3325 235 GHQAPLYDSPKDP-EAQGYSVDSAVQAYLAAGVPASKLVLGVPFYGRGWTGVTGGNN----GLYQPAT------------ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 349 gannenpiKTGDGGRAGGVWAYRSIDALKAKTPTLKEYWDDTAKAPYLYSKETGEFYTYDNTRSIGYKAQYVKDNNLGGM 428
Cdd:COG3325 298 --------GPAPGTWEAGVNDYKDLKALYLGSNGYTRYWDDVAKAPYLYNGDTGTFISYDDPRSIAAKADYVKDKGLGGV 369
|
410 420
....*....|....*....|....*..
gi 1560718296 429 ISWMQSQDktttsTKRDELTKAIKSGL 455
Cdd:COG3325 370 MFWELSGD-----TADGTLLNAIGEGL 391
|
|
| GH18_chitinase |
cd06548 |
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ... |
40-436 |
2.27e-125 |
|
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: 376.97 E-value: 2.27e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 40 NVMYYGDWSIWGGeGNFYPKDIPADQLTHLNFAFLDFNSNGDLVFTDKDAAVGA--PVGQEGVQWGGANAGVLNAIQDLR 117
Cdd:cd06548 1 VVGYFTNWGIYGR-NYFVTDDIPADKLTHINYAFADIDGDGGVVTSDDEAADEAaqSVDGGADTDDQPLKGNFGQLRKLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 118 AQNPNLKIGVSVGGWSKSGDFSTVAADPTKRANFVKNVMKFVKYTNMDFVDLDWEYPASvrdadlvdnkNDEGTPNAKPA 197
Cdd:cd06548 80 QKNPHLKILLSIGGWTWSGGFSDAAATEASRAKFADSAVDFIRKYGFDGIDIDWEYPGS----------GGAPGNVARPE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 198 DKQNFITLLQDLRTALDKQGVDINKKYELSVALPAAKSTLENgIDVANLFKVVDFANVMTYDLNGAWTPNSAHHTALYGN 277
Cdd:cd06548 150 DKENFTLLLKELREALDALGAETGRKYLLTIAAPAGPDKLDK-LEVAEIAKYLDFINLMTYDFHGAWSNTTGHHSNLYAS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 278 PKDPNydSGFSVDQTVKYLKEKGAVSNKIVVGAAFYTRGWNKvaagtdtalpglfqaaektnkdadgsltygannenpik 357
Cdd:cd06548 229 PADPP--GGYSVDAAVNYYLSAGVPPEKLVLGVPFYGRGWTG-------------------------------------- 268
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1560718296 358 tgdggraggvwayrsidalkaktptLKEYWDDTAKAPYLYSKETGEFYTYDNTRSIGYKAQYVKDNNLGGMISWMQSQD 436
Cdd:cd06548 269 -------------------------YTRYWDEVAKAPYLYNPSTKTFISYDDPRSIKAKADYVKDKGLGGVMFWELSGD 322
|
|
| Glyco_18 |
smart00636 |
Glyco_18 domain; |
39-436 |
4.36e-104 |
|
Glyco_18 domain;
Pssm-ID: 214753 [Multi-domain] Cd Length: 334 Bit Score: 322.32 E-value: 4.36e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 39 RNVMYYGDWSIWGGegNFYPKDIPADQLTHLNFAFLDFNSNGDLVFTDKDAAVGapvgqegvqwggaNAGVLNAiqdLRA 118
Cdd:smart00636 1 RVVGYFTNWGVYGR--NFPVDDIPASKLTHIIYAFANIDPDGTVTIGDEWADIG-------------NFGQLKA---LKK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 119 QNPNLKIGVSVGGWSKSGDFSTVAADPTKRANFVKNVMKFVKYTNMDFVDLDWEYpasvrdadlvdnkndegtPNAKPAD 198
Cdd:smart00636 63 KNPGLKVLLSIGGWTESDNFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWEY------------------PGGRGDD 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 199 KQNFITLLQDLRTALDKQGVDiNKKYELSVALPAAKSTLENGID-VANLFKVVDFANVMTYDLNGAWTPNSAHHTALYGN 277
Cdd:smart00636 125 RENYTALLKELREALDKEGAE-GKGYLLTIAVPAGPDKIDKGYGdLPAIAKYLDFINLMTYDFHGAWSNPTGHNAPLYAG 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 278 PKDPNYdsgFSVDQTVKYLKEKGAVSNKIVVGAAFYTRGWNKVAAGTDTalpglfqAAEKTNKDADGsltygannenpik 357
Cdd:smart00636 204 PGDPEK---YNVDYAVKYYLCKGVPPSKLVLGIPFYGRGWTLVDGSNNG-------PGAPFTGPATG------------- 260
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1560718296 358 tGDGGRAGGVWAYRSIdalkAKTPTLKEYWDDTAKAPYLYSKETGEFYTYDNTRSIGYKAQYVKDNNLGGMISWMQSQD 436
Cdd:smart00636 261 -GPGTWEGGVVDYREI----CKLLGATVVYDDTAKAPYAYNPGTGQWVSYDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
|
|
| GH18_chitolectin_chitotriosidase |
cd02872 |
This conserved domain family includes a large number of catalytically inactive chitinase-like ... |
41-431 |
1.55e-87 |
|
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: 280.21 E-value: 1.55e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 41 VMYYGDWSIW-GGEGNFYPKDIPADQLTHLNFAFLDFNSNGDLVFTDkdaavgapvgqegvQWGGANAGVLNAIQDLRAQ 119
Cdd:cd02872 2 VCYFTNWAQYrPGNGKFVPENIDPFLCTHIIYAFAGLNPDGNIIILD--------------EWNDIDLGLYERFNALKEK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 120 NPNLKIGVSVGGWSK-SGDFSTVAADPTKRANFVKNVMKFVKYTNMDFVDLDWEYPASvrdadlvdnkndEGTPnakPAD 198
Cdd:cd02872 68 NPNLKTLLAIGGWNFgSAKFSAMAASPENRKTFIKSAIAFLRKYGFDGLDLDWEYPGQ------------RGGP---PED 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 199 KQNFITLLQDLRTALDKQGvdinKKYELSVALPAAKSTLENGIDVANLFKVVDFANVMTYDLNGAWTPNSAHHTALYGNP 278
Cdd:cd02872 133 KENFVTLLKELREAFEPEA----PRLLLTAAVSAGKETIDAAYDIPEISKYLDFINVMTYDFHGSWEGVTGHNSPLYAGS 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 279 KDPNYDSGFSVDQTVKYLKEKGAVSNKIVVGAAFYTRGWnkvaagtdtalpglfqaaektnkdadgSLTYGANNENPIKT 358
Cdd:cd02872 209 ADTGDQKYLNVDYAIKYWLSKGAPPEKLVLGIPTYGRSF---------------------------TLASPSNTGVGAPA 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 359 GDGGRAG------GVWAYRSI-DALKAKTptlKEYWDDTAKAPYLYSKetGEFYTYDNTRSIGYKAQYVKDNNLGGMISW 431
Cdd:cd02872 262 SGPGTAGpytreaGFLAYYEIcEFLKSGW---TVVWDDEQKVPYAYKG--NQWVGYDDEESIALKVQYLKSKGLGGAMVW 336
|
|
| Glyco_hydro_18 |
pfam00704 |
Glycosyl hydrolases family 18; |
39-436 |
2.72e-85 |
|
Glycosyl hydrolases family 18;
Pssm-ID: 425828 [Multi-domain] Cd Length: 311 Bit Score: 272.41 E-value: 2.72e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 39 RNVMYYGDWSIWGgEGNFypkdIPADQLTHLNFAFLDFNS-NGDLVFTDKDAavgapvgqegvqwgganaGVLNAIQDLR 117
Cdd:pfam00704 1 RIVGYYTSWGVYR-NGNF----LPSDKLTHIIYAFANIDGsDGTLFIGDWDL------------------GNFEQLKKLK 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 118 AQ-NPNLKIGVSVGGWSKSGDFSTVAADPTKRANFVKNVMKFVKYTNMDFVDLDWEYpasvrdadlvdnkndegtPNAKP 196
Cdd:pfam00704 58 KQkNPGVKVLLSIGGWTDSTGFSLMASNPASRKKFADSIVSFLRKYGFDGIDIDWEY------------------PGGNP 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 197 ADKQNFITLLQDLRTALDKQgvDINKKYELSVALPAAKSTLENGIDVANLFKVVDFANVMTYDLNGAWTPNSAHHTALYG 276
Cdd:pfam00704 120 EDKENYDLLLRELRAALDEA--KGGKKYLLSAAVPASYPDLDKGYDLPKIAKYLDFINVMTYDFHGSWDNVTGHHAPLYG 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 277 npkdpnyDSGFSVDQTVKYLKEKGAVSNKIVVGAAFYTRGWNKVAAGTDTalpglfqaaektnkdadgsltygannenpi 356
Cdd:pfam00704 198 -------GGSYNVDYAVKYYLKQGVPASKLVLGVPFYGRSWTLVNGSGNT------------------------------ 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 357 ktgdggRAGGVWAYRSIDALKaKTPTLKEYWDDTAKAPYLYSkeTGEFYTYDNTRSIGYKAQYVKDNNLGGMISWMQSQD 436
Cdd:pfam00704 241 ------WEDGVLAYKEICNLL-KDNGATVVWDDVAKAPYVYD--GDQFITYDDPRSIATKVDYVKAKGLGGVMIWSLDAD 311
|
|
| GH18_LinChi78-like_UFR |
cd20174 |
an unknown function domain of Listeria innocua LinChi78 GH18 chitinase that is essential for ... |
471-605 |
2.75e-60 |
|
an unknown function domain of Listeria innocua LinChi78 GH18 chitinase that is essential for its catalytic activity; found in similar chitinase-like proteins; This domain is referred to as an unknown-function region (UFR) and shown to be necessary for the hydrolytic activity of LinChi78 glycosyl hydrolase family 18 (GH18) chitinase (a product of the lin0153gene) from the nonpathogenic bacterium Listeria innocua. The catalytic domain (CatD) of GH18 chitinases folds into a TIM barrel and has a conserved DXXDXDXE motif, in which the Glu residue functions as a catalytic residue; these chitinases contain additional domains such as a chitin-binding domain (ChBD) and/or a fibronectin type III-like (FnIII) domain. LinChi78 consists of a CatD, a FnIII, and a ChBD domain, and has this UFR region located between the CatD and the FnIII domain. Its catalytic site is composed of a typical CatD and a portion of this UFR, in particular the key Gln and Ile residues which are indispensable for LinChi78 to exhibit full catalytic activity. This UFR domain is also found in proteins where it is located between a CatD domain and DUF5011 and ChBD(s) domains. LinChi78 exhibits chitinase activity towards artificial and natural substrates, including colloidal chitin and chitin oligosaccharides of various lengths, and hydrolyzes these in a processive manner. Members of this family include some uncharacterized chitinase-like proteins from pathogenic bacteria such as Listeria monocytogenes and Clostridium botulinum.
Pssm-ID: 380910 Cd Length: 136 Bit Score: 199.43 E-value: 2.75e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 471 LNVVATVKPYSE-NGVGYEITITNNEKADETNEVLKSTELSFETVKLPKFYIPVKAGETLTAGDYKAGTVTTSGGNTVVD 549
Cdd:cd20174 1 LNVSATVTPYTEsGGEGYEITITNNEKLEESGEVLSAVEKAAKTIKNPKLYIKTKDGETLTSGDYKAGTVTTENGYTVVD 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1560718296 550 LASVYDAQQIPQGASYTFRLKSSASSVDVANISKIDLTQRMVKSSVEFGKQTIFGG 605
Cdd:cd20174 81 LSTVYDGKFIKPGASYTFKLKTDAGAADLSNIESIELSQRIVSSGPELGRQTIYGD 136
|
|
| GH18_chitinase-like |
cd00598 |
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ... |
41-261 |
1.66e-40 |
|
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant polymer of beta-1,4-linked N-acetylglucosamine (GlcNAc) which is a major component of the cell wall of fungi and the exoskeleton of arthropods. Chitinases have been identified in viruses, bacteria, fungi, protozoan parasites, insects, and plants. The structure of the GH18 domain is an eight-stranded beta/alpha barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel. The GH18 family includes chitotriosidase, chitobiase, hevamine, zymocin-alpha, narbonin, SI-CLP (stabilin-1 interacting chitinase-like protein), IDGF (imaginal disc growth factor), CFLE (cortical fragment-lytic enzyme) spore hydrolase, the type III and type V plant chitinases, the endo-beta-N-acetylglucosaminidases, and the chitolectins. The GH85 (glycosyl hydrolase, family 85) ENGases (endo-beta-N-acetylglucosaminidases) are closely related to the GH18 chitinases and are included in this alignment model.
Pssm-ID: 119349 [Multi-domain] Cd Length: 210 Bit Score: 147.91 E-value: 1.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 41 VMYYGDWSIWGGegnFYPKDIPADQLTHLNFAFLDFNSNGDLVFTDKDAAvgapvgqegvqwgganAGVLNAIQDLRAQN 120
Cdd:cd00598 2 ICYYDGWSSGRG---PDPTDIPLSLCTHIIYAFAEISSDGSLNLFGDKSE----------------EPLKGALEELASKK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 121 PNLKIGVSVGGWSKSGDFsTVAADPTKRANFVKNVMKFVKYTNMDFVDLDWEYPasvrdadlvDNKNDEgtpnakpaDKQ 200
Cdd:cd00598 63 PGLKVLISIGGWTDSSPF-TLASDPASRAAFANSLVSFLKTYGFDGVDIDWEYP---------GAADNS--------DRE 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1560718296 201 NFITLLQDLRTALDKQGvdinkkYELSVALPAAKSTLENGIDVANLFKVVDFANVMTYDLN 261
Cdd:cd00598 125 NFITLLRELRSALGAAN------YLLTIAVPASYFDLGYAYDVPAIGDYVDFVNVMTYDLV 179
|
|
| GH18_zymocin_alpha |
cd02878 |
Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle ... |
39-431 |
1.63e-27 |
|
Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle progression. The zymocin alpha subunit has a chitinase activity that is essential for holoenzyme action from the cell exterior while the gamma subunit contains the intracellular toxin responsible for G1 phase cell cycle arrest. The zymocin alpha and beta subunits are thought to act from the cell's exterior by docking to the cell wall-associated chitin, thus mediating gamma-toxin translocation. The alpha subunit has an eight-stranded TIM barrel fold similar to that of family 18 glycosyl hydrolases such as hevamine, chitolectin, and chitobiase.
Pssm-ID: 119357 [Multi-domain] Cd Length: 345 Bit Score: 114.33 E-value: 1.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 39 RNVMYYGDWSIWGGEGNFYPKDIPADQLTHLNFAFLDFNSNgdlvFTDKDAAVGApvgqegvQWgganagvlnaiQDLRA 118
Cdd:cd02878 1 KNIAYFEAYNLDRPCLNMDVTQIDTSKYTHIHFAFANITSD----FSVDVSSVQE-------QF-----------SDFKK 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 119 QNPNLKIgVSVGGWSKSGDFST-----VAADPTKRANFVKNVMKFVKYTNMDFVDLDWEYPASvrdADLvdnkndEGTPN 193
Cdd:cd02878 59 LKGVKKI-LSFGGWDFSTSPSTyqifrDAVKPANRDTFANNVVNFVNKYNLDGVDFDWEYPGA---PDI------PGIPA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 194 AKPADKQNFITLLQDLRTALdkqgvdiNKKYELSVALPAAKSTLEnGIDVANLFKVVDFANVMTYDLNGAWTPNSAHhtA 273
Cdd:cd02878 129 GDPDDGKNYLEFLKLLKSKL-------PSGKSLSIAAPASYWYLK-GFPIKDMAKYVDYIVYMTYDLHGQWDYGNKW--A 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 274 LYGNPKDPNYDSGFSVDQTVKYLK---EKGAVSNKIVVGAAFYTRGwnkvaagtdtalpglFQAAEKTNKDADGSLTyGA 350
Cdd:cd02878 199 SPGCPAGNCLRSHVNKTETLDALSmitKAGVPSNKVVVGVASYGRS---------------FKMADPGCTGPGCTFT-GP 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 351 NNENPIKTGDGGRAGGVWAYRSIDALKAKTPtlKEYWDDTAKAPYLysketgefyTYDNTRSIGY--------KAQYVKD 422
Cdd:cd02878 263 GSGAEAGRCTCTAGYGAISEIEIIDISKSKN--KRWYDTDSDSDIL---------VYDDDQWVAYmspatkaaRIEWYKG 331
|
....*....
gi 1560718296 423 NNLGGMISW 431
Cdd:cd02878 332 LNFGGTSDW 340
|
|
| GH18_IDGF |
cd02873 |
The IDGF's (imaginal disc growth factors) are a family of growth factors identified in insects ... |
112-427 |
5.15e-24 |
|
The IDGF's (imaginal disc growth factors) are a family of growth factors identified in insects that include at least five members, some of which are encoded by genes in a tight cluster. The IDGF's have an eight-stranded alpha/beta barrel fold and are related to the glycosyl hydrolase family 18 (GH18) chitinases, but they have an amino acid substitution known to abolish chitinase catalytic activity. IDGFs may have evolved from chitinases to gain new functions as growth factors, interacting with cell surface glycoproteins involved in growth-promoting processes.
Pssm-ID: 119352 [Multi-domain] Cd Length: 413 Bit Score: 105.47 E-value: 5.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 112 AIQDLRAQNPNLKIGVSVGGWSKSGD------FSTVAADPTKRANFVKNVMKFVKYTNMDFVDLDWEYPAS--------- 176
Cdd:cd02873 64 AITSLKRKYPHLKVLLSVGGDRDTDEegenekYLLLLESSESRNAFINSAHSLLKTYGFDGLDLAWQFPKNkpkkvrgtf 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 177 ----------VRDADLVDNKNDEgtpnakpaDKQNFITLLQDLRTALDKQGVDINkkyeLSVaLPAAKSTLEngIDVANL 246
Cdd:cd02873 144 gsawhsfkklFTGDSVVDEKAAE--------HKEQFTALVRELKNALRPDGLLLT----LTV-LPHVNSTWY--FDVPAI 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 247 FKVVDFANVMTYD-LNGAWTPNSAHHTA----LYGnpKDPNYDsgfsVDQTVKYLKEKGAVSNKIVVGAAFYTRGWNKVA 321
Cdd:cd02873 209 ANNVDFVNLATFDfLTPERNPEEADYTApiyeLYE--RNPHHN----VDYQVKYWLNQGTPASKLNLGIATYGRAWKLTK 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 322 ------------------AGTDTALPGLFQAAE-----KTNKDADGSLTygannenPI-KTGDGGRAGGVWAYRSIDAlk 377
Cdd:cd02873 283 dsgitgvppvletdgpgpAGPQTKTPGLLSWPEicsklPNPANLKGADA-------PLrKVGDPTKRFGSYAYRPADE-- 353
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1560718296 378 aktptlkeywddtakapylySKETGEFYTYDNTRSIGYKAQYVKDNNLGG 427
Cdd:cd02873 354 --------------------NGEHGIWVSYEDPDTAANKAGYAKAKGLGG 383
|
|
| GH18_plant_chitinase_class_V |
cd02879 |
The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the ... |
45-317 |
2.30e-22 |
|
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: 98.21 E-value: 2.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 45 GDWSIWGGEgnFYPKDIPADQLTHLNFAFLDFNsngdlvftdkdaavgaPVGQEGVQWGGANAGVLNAIQDLRAQNPNLK 124
Cdd:cd02879 7 GYWPAWSEE--FPPSNIDSSLFTHLFYAFADLD----------------PSTYEVVISPSDESEFSTFTETVKRKNPSVK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 125 IGVSVGGWSKSGD-FSTVAADPTKRANFVKNVMKFVKYTNMDFVDLDWEYPASvrdadlvdnkndegtpnakPADKQNFI 203
Cdd:cd02879 69 TLLSIGGGGSDSSaFAAMASDPTARKAFINSSIKVARKYGFDGLDLDWEFPSS-------------------QVEMENFG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 204 TLLQDLRTALDKQGVDINKKYELSVALPAAKSTLENGID-----VANLFKVVDFANVMTYDLNGAWTPNSAHHTALYGNP 278
Cdd:cd02879 130 KLLEEWRAAVKDEARSSGRPPLLLTAAVYFSPILFLSDDsvsypIEAINKNLDWVNVMAYDYYGSWESNTTGPAAALYDP 209
|
250 260 270
....*....|....*....|....*....|....*....
gi 1560718296 279 KdpnydSGFSVDQTVKYLKEKGAVSNKIVVGAAFYTRGW 317
Cdd:cd02879 210 N-----SNVSTDYGIKSWIKAGVPAKKLVLGLPLYGRAW 243
|
|
| ChiC_BD |
cd12215 |
Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of ... |
712-752 |
9.01e-17 |
|
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: 74.15 E-value: 9.01e-17
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1560718296 712 PAWDAAKTYNKGDRVSYKGKTYEAQWWTQGNEPGAEqWGPW 752
Cdd:cd12215 1 PAWDASTVYTGGDQVTYNGKVYEAKWWTQGEEPGTS-WGVW 40
|
|
| COG3979 |
COG3979 |
Chitodextrinase [Carbohydrate transport and metabolism]; |
616-721 |
2.60e-15 |
|
Chitodextrinase [Carbohydrate transport and metabolism];
Pssm-ID: 443178 [Multi-domain] Cd Length: 369 Bit Score: 78.27 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 616 EAPTVPKALTSSNVTDKSATLTWTASTDNKAVAGYKVYRNGTEVGSVSG-TTFTDSGLTAKTAYSYTVKAYDAAGNFSAA 694
Cdd:COG3979 1 QAPTAPTGLTASNVTSSSVSLSWDASTDNVGVTGYDVYRGGDQVATVTGlTAWTVTGLTPGTEYTFTVGACDAAGNVSAA 80
|
90 100
....*....|....*....|....*..
gi 1560718296 695 SSALTVTTLDAATPPATPAWDAAKTYN 721
Cdd:COG3979 81 SGTSTAMFGGSSTTLGSAEGVADTSGN 107
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
614-727 |
1.55e-14 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 77.35 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 614 DTEAPTVPKALTSSNVTDKSATLTWTASTDNKaVAGYKVYRNGTEVGS-------VSGTTFTDSGLTAKTAYSYTVKAYD 686
Cdd:COG3401 323 DLTPPAAPSGLTATAVGSSSITLSWTASSDAD-VTGYNVYRSTSGGGTytkiaetVTTTSYTDTGLTPGTTYYYKVTAVD 401
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1560718296 687 AAGNFSAASSALTVTTLDAATPPATPAWDAAKTYNKGDRVS 727
Cdd:COG3401 402 AAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGAT 442
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
467-713 |
4.26e-14 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 75.81 E-value: 4.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 467 TYANLNVVATVKPYSENGVGYEITITNNEKADETNEVLKSTELSFETVKLPKFYIPVKAGETLTAGDYKAGTVTTSGGNT 546
Cdd:COG3401 107 TNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLT 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 547 VVDLASVYDAQQIPQGASYTFRLKSsassVDVANISKIDLTQRMVKSsvefgkqtifgggtvvpdpsdTEAPTVPKALTS 626
Cdd:COG3401 187 VTSTTLVDGGGDIEPGTTYYYRVAA----TDTGGESAPSNEVSVTTP---------------------TTPPSAPTGLTA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 627 SNVTDKSATLTWTASTdNKAVAGYKVYRNG------TEVGSVSGTTFTDSGLTAKTAYSYTVKAYDAAGNFSAASSALTV 700
Cdd:COG3401 242 TADTPGSVTLSWDPVT-ESDATGYRVYRSNsgdgpfTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVVSV 320
|
250
....*....|...
gi 1560718296 701 TTldAATPPATPA 713
Cdd:COG3401 321 TT--DLTPPAAPS 331
|
|
| GH18_3CO4_chitinase |
cd06545 |
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an ... |
50-317 |
7.44e-14 |
|
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an uncharacterized bacterial member of the family 18 glycosyl hydrolases with homologs found in Flavobacterium, Stigmatella, and Pseudomonas.
Pssm-ID: 119362 [Multi-domain] Cd Length: 253 Bit Score: 72.10 E-value: 7.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 50 WGGEGNFYPKdIPADQLTHLNFAFLDFNSNGDLVFtdkdaavgapvgqegvqwGGANAGVLNAIQDLRAQNpnLKIGVSV 129
Cdd:cd06545 8 YDDLNALSPT-IDFSKLTHINLAFANPDANGTLNA------------------NPVRSELNSVVNAAHAHN--VKILISL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 130 GGWSKSGdFSTVAADPTKRANFVKNVMKFVKYTNMDFVDLDWEYPAsvrdadlvdnkndegtpnAKPADKQNFItllQDL 209
Cdd:cd06545 67 AGGSPPE-FTAALNDPAKRKALVDKIINYVVSYNLDGIDVDLEGPD------------------VTFGDYLVFI---RAL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 210 RTALDKQGVdinkkyelsvALPAAKSTLENGIDVANLFKVVDFANVMTYDLNGAWTPNSahhtalygnpkdPNYDSGFSV 289
Cdd:cd06545 125 YAALKKEGK----------LLTAAVSSWNGGAVSDSTLAYFDFINIMSYDATGPWWGDN------------PGQHSSYDD 182
|
250 260 270
....*....|....*....|....*....|
gi 1560718296 290 DQT-VKYLKEKGAVS-NKIVVGAAFYTRGW 317
Cdd:cd06545 183 AVNdLNYWNERGLASkDKLVLGLPFYGYGF 212
|
|
| ChtBD3 |
smart00495 |
Chitin-binding domain type 3; |
712-752 |
3.51e-13 |
|
Chitin-binding domain type 3;
Pssm-ID: 197760 [Multi-domain] Cd Length: 41 Bit Score: 64.20 E-value: 3.51e-13
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1560718296 712 PAWDAAKTYNKGDRVSYKGKTYEAQWWTQGNEPGAeQWGPW 752
Cdd:smart00495 2 PAWQAGTVYTAGDVVSYNGKVYKAKWWTQGEEPGS-SSGPW 41
|
|
| GH18_CFLE_spore_hydrolase |
cd02874 |
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ... |
130-432 |
5.46e-12 |
|
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial endospore germination. CFLE is expressed as an inactive preprotein (called SleB) in the forespore compartment of sporulating cells. SleB translocates across the forespore inner membrane and is deposited as a mature enzyme in the cortex layer of the spore. As part of a sensory mechanism capable of initiating germination, CFLE degrades a spore-specific peptidoglycan constituent called muramic-acid delta-lactam that comprises the outer cortex. CFLE has a C-terminal glycosyl hydrolase family 18 (GH18) catalytic domain as well as two N-terminal LysM peptidoglycan-binding domains. In addition to SleB, this family includes YaaH, YdhD, and YvbX from Bacillus subtilis.
Pssm-ID: 119353 [Multi-domain] Cd Length: 313 Bit Score: 67.68 E-value: 5.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 130 GGWSKSGdFSTVAADPTKRANFVKNVMKFVKYTNMDFVDLDWEYpasVRdadlvdnkndegtpnakPADKQNFITLLQDL 209
Cdd:cd02874 71 GNFDSEL-AHAVLSNPEARQRLINNILALAKKYGYDGVNIDFEN---VP-----------------PEDREAYTQFLREL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 210 RTALDKQGvdinkkYELSVALPAAKSTLENGI-----DVANLFKVVDFANVMTYDLNGAWTPnsahHTALYGNPKdpnyd 284
Cdd:cd02874 130 SDRLHPAG------YTLSTAVVPKTSADQFGNwsgayDYAAIGKIVDFVVLMTYDWHWRGGP----PGPVAPIGW----- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 285 sgfsVDQTVKYLKEKgaV-SNKIVVGAAFYTRGWnkvaagtdtalpglfqaaektnkdadgSLTYGANNENpiktgdggr 363
Cdd:cd02874 195 ----VERVLQYAVTQ--IpREKILLGIPLYGYDW---------------------------TLPYKKGGKA--------- 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1560718296 364 aggvwayRSIDALKAKtPTLKEY-----WDDTAKAP-YLYSKETGEFYT--YDNTRSIGYKAQYVKDNNLGGMISWM 432
Cdd:cd02874 233 -------STISPQQAI-NLAKRYgaeiqYDEEAQSPfFRYVDEQGRRHEvwFEDARSLQAKFELAKEYGLRGVSYWR 301
|
|
| FN3 |
cd00063 |
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ... |
618-702 |
1.67e-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: 58.28 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 618 PTVPKALTSSNVTDKSATLTWTAST-DNKAVAGYKVYRNGT--------EVGSVSGTTFTDSGLTAKTAYSYTVKAYDAA 688
Cdd:cd00063 1 PSPPTNLRVTDVTSTSVTLSWTPPEdDGGPITGYVVEYREKgsgdwkevEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80
|
90
....*....|....
gi 1560718296 689 GNfSAASSALTVTT 702
Cdd:cd00063 81 GE-SPPSESVTVTT 93
|
|
| FN3 |
smart00060 |
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
618-689 |
4.01e-07 |
|
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: 48.38 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 618 PTVPKALTSSNVTDKSATLTWTASTDNKA---VAGYKVYRNGTE------VGSVSGTTFTDSGLTAKTAYSYTVKAYDAA 688
Cdd:smart00060 1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItgyIVGYRVEYREEGsewkevNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80
|
.
gi 1560718296 689 G 689
Cdd:smart00060 81 G 81
|
|
| CBD_like |
cd12204 |
Cellulose-binding domain, chitinase and related proteins; This group contains proteins related ... |
706-755 |
4.83e-07 |
|
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: 46.94 E-value: 4.83e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1560718296 706 ATPPATPAWDAAKTYNKGDRVSYKGKTYEAQWWTQgNEPGAEqwGPWLLI 755
Cdd:cd12204 1 AGANAYPNWPQGTHAAGGDLVSYNGAVYQAKWWTQ-SAPGSD--SSWTLV 47
|
|
| GH18_SI-CLP |
cd02876 |
Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein ... |
113-330 |
5.66e-07 |
|
Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein of unknown function that interacts with the endocytic/sorting transmembrane receptor stabilin-1 and is secreted from the lysosome. SI-CLP has a glycosyl hydrolase family 18 (GH18) domain but lacks a chitin-binding domain. The catalytic amino acids of the GH18 domain are not conserved in SI-CLP, similar to the chitolectins YKL-39, YKL-40, and YM1/2. Human SI-CLP is sorted to late endosomes and secretory lysosomes in alternatively activated macrophages.
Pssm-ID: 119355 [Multi-domain] Cd Length: 318 Bit Score: 52.31 E-value: 5.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 113 IQDLRAQNPNLKI--GVSVGGWSkSGDFSTVAADPTKRANFVKNVMKFVKYTNMDFVDLD-WEYPASvrdadlvdnknde 189
Cdd:cd02876 57 IEEVRKANKNIKIlpRVLFEGWS-YQDLQSLLNDEQEREKLIKLLVTTAKKNHFDGIVLEvWSQLAA------------- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 190 gtpNAKPADKQNFITLLQDLRTALDKQGVDInkkyeLSVALPAAKSTLENGI----DVANLFKVVDFANVMTYDlngawt 265
Cdd:cd02876 123 ---YGVPDKRKELIQLVIHLGETLHSANLKL-----ILVIPPPREKGNQNGLftrkDFEKLAPHVDGFSLMTYD------ 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1560718296 266 pnsahhtalYGNPKDPNYDSGFS-VDQTVKYL-KEKGAVSNKIVVGAAFYtrGWNKVAAGTDTALPG 330
Cdd:cd02876 189 ---------YSSPQRPGPNAPLSwVRSCLELLlPESGKKRAKILLGLNFY--GNDYTLPGGGGAITG 244
|
|
| CBM_5_12 |
pfam02839 |
Carbohydrate binding domain; This short domain is found in many different glycosyl hydrolase ... |
728-752 |
1.88e-06 |
|
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: 44.51 E-value: 1.88e-06
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
621-690 |
1.20e-05 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 43.94 E-value: 1.20e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1560718296 621 PKALTSSNVTDKSATLTWTASTD-NKAVAGYKV-YRNGTEVG-----SVSGTT--FTDSGLTAKTAYSYTVKAYDAAGN 690
Cdd:pfam00041 3 PSNLTVTDVTSTSLTVSWTPPPDgNGPITGYEVeYRPKNSGEpwneiTVPGTTtsVTLTGLKPGTEYEVRVQAVNGGGE 81
|
|
| ChtBD3 |
cd00036 |
Chitin/cellulose binding domains of chitinase and related enzymes; This group contains ... |
713-745 |
3.43e-05 |
|
Chitin/cellulose binding domains of chitinase and related enzymes; This group contains proteins related to the cellulose-binding domain of Erwinia chrysanthemi endoglucanase Z (EGZ) and Serratia marcescens chitinase B (ChiB). Gram negative plant parasite Erwinia chrysanthemi produces a variety of depolymerizing enzymes to metabolize pectin and cellulose on the host plant. Cellulase EGZ has a modular structure, with an N-terminal catalytic domain linked to a C-terminal cellulose-binding domain (CBD). CBD mediates the secretion activity of EGZ. Chitinases allow certain bacteria to utilize chitin as a energy source. Typically, non-plant chitinases are of the glycosidase family 18. Bacillus circulans Glycosidase ChiA1 hydrolyzes chitin and is comprised of several domains: the C-terminal chitin binding domain, an N-terminal catalytic domain, and 2 fibronectin type III-like domains. Bacillus circulans WL-12 ChiA1 facilitates invasion of fungal cell walls. The ChiA1 chitin binding domain is required for the specific recognition of insoluble chitin. although topologically and structurally related, ChiA1 lacks the characteristic aromatic residues of Erwinia chrysanthemi endoglucanase Z (CBD(EGZ)). Streptomyces griseus Chitinase C is a family 19 chitinase, and consists of a N-terminal chitin binding domain and a C-terminal chitin-catalytic domain that effects degradation. ChiC contains the characteristic chitin-binding aromatic residues. Chitinases function in invertebrates in the degradation of old exoskeletons, in fungi to utilize chitin in cell walls, and in bacteria which use chitin as an energy source.
Pssm-ID: 213175 Cd Length: 40 Bit Score: 41.59 E-value: 3.43e-05
10 20 30
....*....|....*....|....*....|...
gi 1560718296 713 AWDAAKTYNKGDRVSYKGKTYEAQWWTQGNEPG 745
Cdd:cd00036 1 AWPNPTHYTAGQSVVYNGNLYTANWYTAGSVPG 33
|
|
| GH18_chitobiase |
cd02875 |
Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes ... |
144-431 |
6.09e-05 |
|
Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes the reducing-end N-acetylglucosamine from the chitobiose core of oligosaccharides during the ordered degradation of asparagine-linked glycoproteins in eukaryotes. Chitobiase can only do so if the asparagine that joins the oligosaccharide to protein is previously removed by a glycosylasparaginase. Chitobiase is therefore the final step in the lysosomal degradation of the protein/carbohydrate linkage component of asparagine-linked glycoproteins. The catalytic domain of chitobiase is an eight-stranded alpha/beta barrel fold similar to that of other family 18 glycosyl hydrolases such as hevamine and chitotriosidase.
Pssm-ID: 119354 [Multi-domain] Cd Length: 358 Bit Score: 45.89 E-value: 6.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 144 DPTKRANFVKNVMKFVKYTNMDFVDLDWEYPasvrdadlvdnkNDEGTPNAkpadkQNFITLLQDLRTALDKqgvdINKK 223
Cdd:cd02875 93 NPTYRTQWIQQKVELAKSQFMDGINIDIEQP------------ITKGSPEY-----YALTELVKETTKAFKK----ENPG 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 224 YELSVALPAAKSTLE-NGIDVANLFKVVDFANVMTYD----------LNGAWTPNSahhTALYGnpkdpnydsgfsvdqT 292
Cdd:cd02875 152 YQISFDVAWSPSCIDkRCYDYTGIADASDFLVVMDYDeqsqiwgkecIAGANSPYS---QTLSG---------------Y 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 293 VKYLKeKGAVSNKIVVGAAFYtrGWNKVAAGTDTalpglfqaaektnKDADGSLT----YGANNENPiktgdggrAGGVW 368
Cdd:cd02875 214 NNFTK-LGIDPKKLVMGLPWY--GYDYPCLNGNL-------------EDVVCTIPkvpfRGANCSDA--------AGRQI 269
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1560718296 369 AYRSIdaLKAKTPTLK-EYWDDTAKAPYL-YSKETGEFYT--YDNTRSIGYKAQYVKDNNLGGMISW 431
Cdd:cd02875 270 PYSEI--MKQINSSIGgRLWDSEQKSPFYnYKDKQGNLHQvwYDNPQSLSIKVAYAKNLGLKGIGMW 334
|
|
| COG4733 |
COG4733 |
Phage-related protein, tail protein J [Mobilome: prophages, transposons]; |
551-711 |
4.76e-04 |
|
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
Pssm-ID: 443767 [Multi-domain] Cd Length: 978 Bit Score: 43.78 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 551 ASVYDAQQIPQGASYTFRLKSSASSVDVANISKIDLTQRmVKSSVEFGKQTIFGGGTVVPDPSDTEAPTVPKALTSSNVT 630
Cdd:COG4733 564 AVAYEVEWRRDDGNWVSVPRTSGTSFEVPGIYAGDYEVR-VRAINALGVSSAWAASSETTVTGKTAPPPAPTGLTATGGL 642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 631 DkSATLTWTASTDNkAVAGYKVYRNGT--------EVGSVSGTTFTDSGLTAKTAYSYTVKAYDAAGNFSAAsSALTVTT 702
Cdd:COG4733 643 G-GITLSWSFPVDA-DTLRTEIRYSTTgdwasatvAQALYPGNTYTLAGLKAGQTYYYRARAVDRSGNVSAW-WVSGQAS 719
|
....*....
gi 1560718296 703 LDAATPPAT 711
Cdd:COG4733 720 ADAAGILDA 728
|
|
| ChiA1_BD |
cd12214 |
chitin-binding domain of Chi A1-like proteins; This group contains proteins related to the ... |
713-753 |
6.16e-04 |
|
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: 38.09 E-value: 6.16e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1560718296 713 AWDAAKTYNKGDRVSYKGKTYEAQ---WWTQGNEPGAeqwGPWL 753
Cdd:cd12214 1 EWAAGTTYKAGDIVTYNGKLYRCLqahTSLAGWEPPA---VPAL 41
|
|
| GH18_narbonin |
cd06544 |
Narbonin is a plant 2S protein from the globulin fraction of narbon bean (Vicia narbonensis L.) ... |
73-172 |
3.59e-03 |
|
Narbonin is a plant 2S protein from the globulin fraction of narbon bean (Vicia narbonensis L.) cotyledons with unknown function. Narbonin has a glycosyl hydrolase family 18 (GH18) domain without the conserved catalytic residues and with no known enzymatic activity. Narbonin amounts to up to 3% of the total seed globulins of mature seeds and was thought to be a storage protein but was found to degrade too slowly during germination. This family also includes the VfNOD32 nodulin from Vicia faba.
Pssm-ID: 119361 Cd Length: 253 Bit Score: 40.05 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560718296 73 FLDFNSNGDLVF-------TDKDAAVGAPVGQEGVQWGGANAGVlNAIQDLRAQNPNLKIGVSVGGWSKsgDFSTVAADP 145
Cdd:cd06544 15 FSDVPINPKVEFhfilsfaIDYDTESNPTNGKFNPYWDTENLTP-EAVKSIKAQHPNVKVVISIGGRGV--QNNPTPFDP 91
|
90 100 110
....*....|....*....|....*....|.
gi 1560718296 146 TKR----ANFVKNVMKFVKYTNMDFVDLDWE 172
Cdd:cd06544 92 SNVdswvSNAVSSLTSIIQTYNLDGIDIDYE 122
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