|
Name |
Accession |
Description |
Interval |
E-value |
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
28-372 |
1.27e-157 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 463.07 E-value: 1.27e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 28 VTAIHIPKAHAAVASKTLVGYWHNFDNGSGFIKLRDVSPKFDIINVSFAEPTSGvTNGTIGF-------IPYNYTEADFK 100
Cdd:COG3469 200 TTATTTGPPTPGLPKHVLVGYWHNFDNGSGYIRLSDVPDKYDVINVAFAEPTGA-TNGTVTFtldpgssSPGGYTDAQFK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 101 ADVAYLQSQGKKVIISIGGANGQVQLPSTSARDNFVNSVIAIIEKYGFDGLDVDFEGHSLYLNSGDSDfknptTPVIVNL 180
Cdd:COG3469 279 ADIAALQAQGKKVLLSIGGANGTVQLNTAAAADNFVNSVIALIDEYGFDGLDIDLEGGSNSLNAGDTD-----TPVITNL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 181 ISALRTINNHFGTGpFYLTMAPETFFVQLGYSFYGGSciscdnrAGAYLPVIYATRDILDWLQVQNYNSGPITGLDDQYH 260
Cdd:COG3469 354 ISALKQLKAKYGPG-FVLTMAPETPYVQGGYVAYGGI-------WGAYLPVILALRDILTLLHVQYYNSGSMLGLDGQVY 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 261 NMGNADFHVAMADMILTGFPVAKNlNQMFPPLRPDQVVLGLPANVNA-GGGFTSVAEVHKALDALIKGVQLPSYKTRGsv 339
Cdd:COG3469 426 SQGTVDFLVAMADMLLEGFPVAGN-SNGFPGLRPDQVAIGLPASPSAaGGGYVSPANVNKALDCLTKGTNCGSYKPRG-- 502
|
330 340 350
....*....|....*....|....*....|...
gi 1024025361 340 sGYPNFRGLMTWSVNWDKFNNFEFSNSHRAYLD 372
Cdd:COG3469 503 -TYPGLRGLMTWSINWDASNGYEFSNNVGAYLD 534
|
|
| GH18_chitinase_D-like |
cd02871 |
GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes ... |
43-370 |
3.67e-140 |
|
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: 409.80 E-value: 3.67e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 43 KTLVGYWHNFDNGSGFIK--LRDVSPKFDIINVSFAEPTS---GVTNGTIGFIPYNYTEADFKADVAYLQSQGKKVIISI 117
Cdd:cd02871 1 KVLVGYWHNWDNGAGSGRqdLDDVPSKYNVINVAFAEPTSdggGEVTFNNGSSPGGYSPAEFKADIKALQAKGKKVLISI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 118 GGANGQVQLPSTSARDNFVNSVIAIIEKYGFDGLDVDFEGHSLYLNSgdsdfknptTPVIVNLISALRTINNHFGTGpFY 197
Cdd:cd02871 81 GGANGHVDLNHTAQEDNFVDSIVAIIKEYGFDGLDIDLESGSNPLNA---------TPVITNLISALKQLKDHYGPN-FI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 198 LTMAPETFFVQLGYSFYGGsciscdnRAGAYLPVIYATRDILDWLQVQNYNSGPITGLDDQYHNMGNADFHVAMADMILT 277
Cdd:cd02871 151 LTMAPETPYVQGGYAAYGG-------IWGAYLPLIDNLRDDLTWLNVQYYNSGGMGGCDGQSYSQGTADFLVALADMLLT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 278 GFPVAKnlNQMFPPLRPDQVVLGLPANVNA-GGGFTSVAEVHKALDALIKGVQLPSYKTRGsvsGYPNFRGLMTWSVNWD 356
Cdd:cd02871 224 GFPIAG--NDRFPPLPADKVVIGLPASPSAaGGGYVSPSEVIKALDCLMKGTNCGSYYPAG---GYPSLRGLMTWSINWD 298
|
330
....*....|....
gi 1024025361 357 KFNNFEFSNSHRAY 370
Cdd:cd02871 299 ATNNYEFSKNYGAY 312
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
379-601 |
1.62e-28 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 120.49 E-value: 1.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 379 PDTQPPTAPTHVTSMSKSATSVSLSWTASTDNvGVTGYIVYYGSQS-------VSVTGTSTVISGLTPDTSYTFTVKAVD 451
Cdd:COG3401 228 TPTTPPSAPTGLTATADTPGSVTLSWDPVTES-DATGYRVYRSNSGdgpftkvATVTTTSYTDTGLTNGTTYYYRVTAVD 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 452 ARGNQSAASTPLTVTTdppgtggDTTLPTAPGNVQVTAKTATSVSLSWNASTDNvGVTGYIVTYGTSSVNTA-------- 523
Cdd:COG3401 307 AAGNESAPSNVVSVTT-------DLTPPAAPSGLTATAVGSSSITLSWTASSDA-DVTGYNVYRSTSGGGTYtkiaetvt 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 524 GTSATINGLTANTSYSFTVTAKDAAGNVSAGT--IISVTTAPQSGAQPWAANVSYKVNDEVTYGGKTYICRQPHTSLTGW 601
Cdd:COG3401 379 TTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSeeVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVL 458
|
|
| Glyco_hydro_18 |
pfam00704 |
Glycosyl hydrolases family 18; |
44-356 |
3.10e-25 |
|
Glycosyl hydrolases family 18;
Pssm-ID: 425828 [Multi-domain] Cd Length: 311 Bit Score: 106.39 E-value: 3.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 44 TLVGYWHNFDN--GSGFIKlrdvSPKFDIINVSFAEPTSGvtNGTIGFIPYNYTEADFKADVAYLQSQGKKVIISIGGAN 121
Cdd:pfam00704 1 RIVGYYTSWGVyrNGNFLP----SDKLTHIIYAFANIDGS--DGTLFIGDWDLGNFEQLKKLKKQKNPGVKVLLSIGGWT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 122 GQVQ----LPSTSARDNFVNSVIAIIEKYGFDGLDVDFEghslYLNSGDSDFKNpttpvIVNLISALRTINNHFGTGP-F 196
Cdd:pfam00704 75 DSTGfslmASNPASRKKFADSIVSFLRKYGFDGIDIDWE----YPGGNPEDKEN-----YDLLLRELRAALDEAKGGKkY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 197 YLTMAPETFFVQLGYSFyggsciscdnragaYLPVIYatrDILDWLQVQNYN--------SGPITGLDDQYHnmGNADFh 268
Cdd:pfam00704 146 LLSAAVPASYPDLDKGY--------------DLPKIA---KYLDFINVMTYDfhgswdnvTGHHAPLYGGGS--YNVDY- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 269 vAMADMILTGFPvaknlnqmfpplrPDQVVLGLPANVNA-----GGGFTSVAEVH--KALDALIKGVQLPSYKTRGSVSG 341
Cdd:pfam00704 206 -AVKYYLKQGVP-------------ASKLVLGVPFYGRSwtlvnGSGNTWEDGVLayKEICNLLKDNGATVVWDDVAKAP 271
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1024025361 342 YP-------------------------NFRGLMTWSVNWD 356
Cdd:pfam00704 272 YVydgdqfityddprsiatkvdyvkakGLGGVMIWSLDAD 311
|
|
| Glyco_18 |
smart00636 |
Glyco_18 domain; |
44-356 |
3.24e-24 |
|
Glyco_18 domain;
Pssm-ID: 214753 [Multi-domain] Cd Length: 334 Bit Score: 103.91 E-value: 3.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 44 TLVGYWHNFDNGSGFIKLRDV-SPKFDIINVSFAEPTSgvtNGTIGFIPYNYTEADFKAdVAYLQSQ--GKKVIISIGG- 119
Cdd:smart00636 1 RVVGYFTNWGVYGRNFPVDDIpASKLTHIIYAFANIDP---DGTVTIGDEWADIGNFGQ-LKALKKKnpGLKVLLSIGGw 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 120 ---ANGQVQLPSTSARDNFVNSVIAIIEKYGFDGLDVDFEghslYLNSGDSDFKNpttpvIVNLISALRT-INNHFGTGP 195
Cdd:smart00636 77 tesDNFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWE----YPGGRGDDREN-----YTALLKELREaLDKEGAEGK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 196 FY-LTMAPETFFVQLGYSFYggsciscdnragaYLPVIYatrDILDWLQVQNYN-SGP---ITGLDDQYHNMG------N 264
Cdd:smart00636 148 GYlLTIAVPAGPDKIDKGYG-------------DLPAIA---KYLDFINLMTYDfHGAwsnPTGHNAPLYAGPgdpekyN 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 265 ADFhvAMADMILTGFPvaknlnqmfpplrPDQVVLGLPAnvnAGGGFTSVAEVHKALDALIKGVQLPSYKTR-GSVSGYP 343
Cdd:smart00636 212 VDY--AVKYYLCKGVP-------------PSKLVLGIPF---YGRGWTLVDGSNNGPGAPFTGPATGGPGTWeGGVVDYR 273
|
330
....*....|...
gi 1024025361 344 NFRGLMTWSVNWD 356
Cdd:smart00636 274 EICKLLGATVVYD 286
|
|
| ChiA1_BD |
cd12214 |
chitin-binding domain of Chi A1-like proteins; This group contains proteins related to the ... |
569-610 |
1.16e-17 |
|
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: 76.61 E-value: 1.16e-17
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1024025361 569 PWAANVSYKVNDEVTYGGKTYICRQPHTSLTGWEPPNVPALW 610
Cdd:cd12214 1 EWAAGTTYKAGDIVTYNGKLYRCLQAHTSLAGWEPPAVPALW 42
|
|
| FN3 |
smart00060 |
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
479-549 |
8.52e-13 |
|
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: 64.17 E-value: 8.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 479 PTAPGNVQVTAKTATSVSLSWNASTDNVG---VTGYIVTYGTSS-------VNTAGTSATINGLTANTSYSFTVTAKDAA 548
Cdd:smart00060 1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItgyIVGYRVEYREEGsewkevnVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80
|
.
gi 1024025361 549 G 549
Cdd:smart00060 81 G 81
|
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
481-550 |
5.42e-11 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 58.97 E-value: 5.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 481 APGNVQVTAKTATSVSLSWNASTDNVG-VTGYIVTYGTSSVNTAG---------TSATINGLTANTSYSFTVTAKDAAGN 550
Cdd:pfam00041 2 APSNLTVTDVTSTSLTVSWTPPPDGNGpITGYEVEYRPKNSGEPWneitvpgttTSVTLTGLKPGTEYEVRVQAVNGGGE 81
|
|
| PHA03255 |
PHA03255 |
BDLF3; Provisional |
401-561 |
1.81e-04 |
|
BDLF3; Provisional
Pssm-ID: 165513 [Multi-domain] Cd Length: 234 Bit Score: 43.35 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 401 SLSWTAStdnvgvtgyivyyGSQSVSVTGTSTVISGLTPDTSytftvkavdARGNQSAASTPLTVTTDP----PGTGGDT 476
Cdd:PHA03255 21 SLIWTSS-------------GSSTASAGNVTGTTAVTTPSPS---------ASGPSTNQSTTLTTTSAPitttAILSTNT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 477 TLPTAPGNvqvtakTATSVSLSWNASTDNVGVTGYIVTYGTSSVNTAGTSATINGLTANTSYSFTVTAKDAAGNVSAGTI 556
Cdd:PHA03255 79 TTVTSTGT------TVTPVPTTSNASTINVTTKVTAQNITATEAGTGTSTGVTSNVTTRSSSTTSATTRITNATTLAPTL 152
|
....*
gi 1024025361 557 ISVTT 561
Cdd:PHA03255 153 SSKGT 157
|
|
| myxo_dep_M36 |
NF038112 |
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ... |
382-560 |
6.32e-03 |
|
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.
Pssm-ID: 468355 [Multi-domain] Cd Length: 1597 Bit Score: 39.64 E-value: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 382 QPPTAPTHVTSMSKSATSVSLSWTAS-TDNVGVTGYIVYYGSQSVSVTGTSTVISGLTP-----DTSYTFTVKAVDarGN 455
Cdd:NF038112 1281 RAPVAVAGAPATVDERSTVTLDGSGTdADGDALTYAWTQTSGPAVTLTGATTATATFTApevtaDTQLTFTLTVSD--GT 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 456 QSAASTpLTVT-TDPPGTggdttlPTAPGNVQVTAKTATSVSLSWNAsTDNVG---------VTGYIVTYgtSSVNTAGT 525
Cdd:NF038112 1359 ASATDT-VTVTvRNVNRA------PVANAGADQTVDERSTVTLSGSA-TDPDGdaltyawtqTAGPTVTL--TGADTATA 1428
|
170 180 190
....*....|....*....|....*....|....*
gi 1024025361 526 SATINGLTANTSYSFTVTAKdAAGNVSAGTIISVT 560
Cdd:NF038112 1429 SFTAPEVAADTELTFQLTVS-ADGQASADVTVTVT 1462
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
28-372 |
1.27e-157 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 463.07 E-value: 1.27e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 28 VTAIHIPKAHAAVASKTLVGYWHNFDNGSGFIKLRDVSPKFDIINVSFAEPTSGvTNGTIGF-------IPYNYTEADFK 100
Cdd:COG3469 200 TTATTTGPPTPGLPKHVLVGYWHNFDNGSGYIRLSDVPDKYDVINVAFAEPTGA-TNGTVTFtldpgssSPGGYTDAQFK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 101 ADVAYLQSQGKKVIISIGGANGQVQLPSTSARDNFVNSVIAIIEKYGFDGLDVDFEGHSLYLNSGDSDfknptTPVIVNL 180
Cdd:COG3469 279 ADIAALQAQGKKVLLSIGGANGTVQLNTAAAADNFVNSVIALIDEYGFDGLDIDLEGGSNSLNAGDTD-----TPVITNL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 181 ISALRTINNHFGTGpFYLTMAPETFFVQLGYSFYGGSciscdnrAGAYLPVIYATRDILDWLQVQNYNSGPITGLDDQYH 260
Cdd:COG3469 354 ISALKQLKAKYGPG-FVLTMAPETPYVQGGYVAYGGI-------WGAYLPVILALRDILTLLHVQYYNSGSMLGLDGQVY 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 261 NMGNADFHVAMADMILTGFPVAKNlNQMFPPLRPDQVVLGLPANVNA-GGGFTSVAEVHKALDALIKGVQLPSYKTRGsv 339
Cdd:COG3469 426 SQGTVDFLVAMADMLLEGFPVAGN-SNGFPGLRPDQVAIGLPASPSAaGGGYVSPANVNKALDCLTKGTNCGSYKPRG-- 502
|
330 340 350
....*....|....*....|....*....|...
gi 1024025361 340 sGYPNFRGLMTWSVNWDKFNNFEFSNSHRAYLD 372
Cdd:COG3469 503 -TYPGLRGLMTWSINWDASNGYEFSNNVGAYLD 534
|
|
| GH18_chitinase_D-like |
cd02871 |
GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes ... |
43-370 |
3.67e-140 |
|
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: 409.80 E-value: 3.67e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 43 KTLVGYWHNFDNGSGFIK--LRDVSPKFDIINVSFAEPTS---GVTNGTIGFIPYNYTEADFKADVAYLQSQGKKVIISI 117
Cdd:cd02871 1 KVLVGYWHNWDNGAGSGRqdLDDVPSKYNVINVAFAEPTSdggGEVTFNNGSSPGGYSPAEFKADIKALQAKGKKVLISI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 118 GGANGQVQLPSTSARDNFVNSVIAIIEKYGFDGLDVDFEGHSLYLNSgdsdfknptTPVIVNLISALRTINNHFGTGpFY 197
Cdd:cd02871 81 GGANGHVDLNHTAQEDNFVDSIVAIIKEYGFDGLDIDLESGSNPLNA---------TPVITNLISALKQLKDHYGPN-FI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 198 LTMAPETFFVQLGYSFYGGsciscdnRAGAYLPVIYATRDILDWLQVQNYNSGPITGLDDQYHNMGNADFHVAMADMILT 277
Cdd:cd02871 151 LTMAPETPYVQGGYAAYGG-------IWGAYLPLIDNLRDDLTWLNVQYYNSGGMGGCDGQSYSQGTADFLVALADMLLT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 278 GFPVAKnlNQMFPPLRPDQVVLGLPANVNA-GGGFTSVAEVHKALDALIKGVQLPSYKTRGsvsGYPNFRGLMTWSVNWD 356
Cdd:cd02871 224 GFPIAG--NDRFPPLPADKVVIGLPASPSAaGGGYVSPSEVIKALDCLMKGTNCGSYYPAG---GYPSLRGLMTWSINWD 298
|
330
....*....|....
gi 1024025361 357 KFNNFEFSNSHRAY 370
Cdd:cd02871 299 ATNNYEFSKNYGAY 312
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
379-601 |
1.62e-28 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 120.49 E-value: 1.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 379 PDTQPPTAPTHVTSMSKSATSVSLSWTASTDNvGVTGYIVYYGSQS-------VSVTGTSTVISGLTPDTSYTFTVKAVD 451
Cdd:COG3401 228 TPTTPPSAPTGLTATADTPGSVTLSWDPVTES-DATGYRVYRSNSGdgpftkvATVTTTSYTDTGLTNGTTYYYRVTAVD 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 452 ARGNQSAASTPLTVTTdppgtggDTTLPTAPGNVQVTAKTATSVSLSWNASTDNvGVTGYIVTYGTSSVNTA-------- 523
Cdd:COG3401 307 AAGNESAPSNVVSVTT-------DLTPPAAPSGLTATAVGSSSITLSWTASSDA-DVTGYNVYRSTSGGGTYtkiaetvt 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 524 GTSATINGLTANTSYSFTVTAKDAAGNVSAGT--IISVTTAPQSGAQPWAANVSYKVNDEVTYGGKTYICRQPHTSLTGW 601
Cdd:COG3401 379 TTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSeeVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVL 458
|
|
| Glyco_hydro_18 |
pfam00704 |
Glycosyl hydrolases family 18; |
44-356 |
3.10e-25 |
|
Glycosyl hydrolases family 18;
Pssm-ID: 425828 [Multi-domain] Cd Length: 311 Bit Score: 106.39 E-value: 3.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 44 TLVGYWHNFDN--GSGFIKlrdvSPKFDIINVSFAEPTSGvtNGTIGFIPYNYTEADFKADVAYLQSQGKKVIISIGGAN 121
Cdd:pfam00704 1 RIVGYYTSWGVyrNGNFLP----SDKLTHIIYAFANIDGS--DGTLFIGDWDLGNFEQLKKLKKQKNPGVKVLLSIGGWT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 122 GQVQ----LPSTSARDNFVNSVIAIIEKYGFDGLDVDFEghslYLNSGDSDFKNpttpvIVNLISALRTINNHFGTGP-F 196
Cdd:pfam00704 75 DSTGfslmASNPASRKKFADSIVSFLRKYGFDGIDIDWE----YPGGNPEDKEN-----YDLLLRELRAALDEAKGGKkY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 197 YLTMAPETFFVQLGYSFyggsciscdnragaYLPVIYatrDILDWLQVQNYN--------SGPITGLDDQYHnmGNADFh 268
Cdd:pfam00704 146 LLSAAVPASYPDLDKGY--------------DLPKIA---KYLDFINVMTYDfhgswdnvTGHHAPLYGGGS--YNVDY- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 269 vAMADMILTGFPvaknlnqmfpplrPDQVVLGLPANVNA-----GGGFTSVAEVH--KALDALIKGVQLPSYKTRGSVSG 341
Cdd:pfam00704 206 -AVKYYLKQGVP-------------ASKLVLGVPFYGRSwtlvnGSGNTWEDGVLayKEICNLLKDNGATVVWDDVAKAP 271
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1024025361 342 YP-------------------------NFRGLMTWSVNWD 356
Cdd:pfam00704 272 YVydgdqfityddprsiatkvdyvkakGLGGVMIWSLDAD 311
|
|
| GH18_chitinase-like |
cd00598 |
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ... |
45-248 |
1.95e-24 |
|
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: 101.30 E-value: 1.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 45 LVGYWHNFDNGSGFIKLRDVSPKFDIINVSFAEPTSGVTNGTIGFIPYnyteADFKADVAYLQSQ--GKKVIISIGGANG 122
Cdd:cd00598 1 VICYYDGWSSGRGPDPTDIPLSLCTHIIYAFAEISSDGSLNLFGDKSE----EPLKGALEELASKkpGLKVLISIGGWTD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 123 Q---VQLPSTSARDNFVNSVIAIIEKYGFDGLDVDFEGhslYLNSGDSDfknpttpvIVNLISALRTINNHFGTGPFYLT 199
Cdd:cd00598 77 SspfTLASDPASRAAFANSLVSFLKTYGFDGVDIDWEY---PGAADNSD--------RENFITLLRELRSALGAANYLLT 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1024025361 200 MAPetffvqlgysfyggsciSCDNRAGAYLPVIYATRDILDWLQVQNYN 248
Cdd:cd00598 146 IAV-----------------PASYFDLGYAYDVPAIGDYVDFVNVMTYD 177
|
|
| Glyco_18 |
smart00636 |
Glyco_18 domain; |
44-356 |
3.24e-24 |
|
Glyco_18 domain;
Pssm-ID: 214753 [Multi-domain] Cd Length: 334 Bit Score: 103.91 E-value: 3.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 44 TLVGYWHNFDNGSGFIKLRDV-SPKFDIINVSFAEPTSgvtNGTIGFIPYNYTEADFKAdVAYLQSQ--GKKVIISIGG- 119
Cdd:smart00636 1 RVVGYFTNWGVYGRNFPVDDIpASKLTHIIYAFANIDP---DGTVTIGDEWADIGNFGQ-LKALKKKnpGLKVLLSIGGw 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 120 ---ANGQVQLPSTSARDNFVNSVIAIIEKYGFDGLDVDFEghslYLNSGDSDFKNpttpvIVNLISALRT-INNHFGTGP 195
Cdd:smart00636 77 tesDNFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWE----YPGGRGDDREN-----YTALLKELREaLDKEGAEGK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 196 FY-LTMAPETFFVQLGYSFYggsciscdnragaYLPVIYatrDILDWLQVQNYN-SGP---ITGLDDQYHNMG------N 264
Cdd:smart00636 148 GYlLTIAVPAGPDKIDKGYG-------------DLPAIA---KYLDFINLMTYDfHGAwsnPTGHNAPLYAGPgdpekyN 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 265 ADFhvAMADMILTGFPvaknlnqmfpplrPDQVVLGLPAnvnAGGGFTSVAEVHKALDALIKGVQLPSYKTR-GSVSGYP 343
Cdd:smart00636 212 VDY--AVKYYLCKGVP-------------PSKLVLGIPF---YGRGWTLVDGSNNGPGAPFTGPATGGPGTWeGGVVDYR 273
|
330
....*....|...
gi 1024025361 344 NFRGLMTWSVNWD 356
Cdd:smart00636 274 EICKLLGATVVYD 286
|
|
| ChiA1_BD |
cd12214 |
chitin-binding domain of Chi A1-like proteins; This group contains proteins related to the ... |
569-610 |
1.16e-17 |
|
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: 76.61 E-value: 1.16e-17
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1024025361 569 PWAANVSYKVNDEVTYGGKTYICRQPHTSLTGWEPPNVPALW 610
Cdd:cd12214 1 EWAAGTTYKAGDIVTYNGKLYRCLQAHTSLAGWEPPAVPALW 42
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
379-602 |
3.47e-17 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 85.05 E-value: 3.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 379 PDTQPPTAPTHVTSMSKSATSVSLSWTASTDNvGVTGYIVYYGSQS--------VSVTGTSTVISGLTPDTSYTFTVKAV 450
Cdd:COG3401 322 TDLTPPAAPSGLTATAVGSSSITLSWTASSDA-DVTGYNVYRSTSGggtytkiaETVTTTSYTDTGLTPGTTYYYKVTAV 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 451 DARGNQSAASTPLTVTTDPPGTGGDTTLPTAPGNVQVTAKTATSVSLSWN-----ASTDNVGVTGYIVTYGTSSVNTAGT 525
Cdd:COG3401 401 DAAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNpgvsaAVLADGGDTGNAVPFTTTSSTVTAT 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024025361 526 SATINGLTANTSYSFTVTAKDAAGNVSAGTIISVTTAPQSGAQPWAANVSYKVNDEVTYGGKTYICRQPHTSLTGWE 602
Cdd:COG3401 481 TTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSA 557
|
|
| COG3979 |
COG3979 |
Chitodextrinase [Carbohydrate transport and metabolism]; |
382-606 |
9.56e-17 |
|
Chitodextrinase [Carbohydrate transport and metabolism];
Pssm-ID: 443178 [Multi-domain] Cd Length: 369 Bit Score: 82.51 E-value: 9.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 382 QPPTAPTHVTSMSKSATSVSLSWTASTDNVGVTGYIVYYGSQSVSVTG--TSTVISGLTPDTSYTFTVKAVDARGNQSAA 459
Cdd:COG3979 1 QAPTAPTGLTASNVTSSSVSLSWDASTDNVGVTGYDVYRGGDQVATVTglTAWTVTGLTPGTEYTFTVGACDAAGNVSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 460 STPLTVTTDPPGTGGDTTLPTAPGNVQVTAKTATSVSLSWNASTDNVGVTG-YIVTYGTSSVNTAGTSATINGLTANTSY 538
Cdd:COG3979 81 SGTSTAMFGGSSTTLGSAEGVADTSGNLAASGAFFGVTTPPTPSSTLVVDGtTTVNAAATANGGTGGSGGTTTIITTGVE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1024025361 539 SFTVTAKDAAGNVSAGTIISVTTAPQSGAQPWAANVSYKVNDEVTYGGKTYICRQPHTSLTGWEPPNV 606
Cdd:COG3979 161 GGGGSKTAQSLNAITAAGTAALNGGVVGGADEVLTCSAVKDDGSGGAGAGNTYWALNTLGVSDTPSGT 228
|
|
| GH18_hevamine_XipI_class_III |
cd02877 |
This conserved domain family includes xylanase inhibitor Xip-I, and the class III plant ... |
45-360 |
1.26e-15 |
|
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: 77.66 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 45 LVGYW-HNFDNGSgfikLRDV--SPKFDIINVSF-------AEPTSGVTNGTIGfiPYNYTEADFKADVAYLQSQGKKVI 114
Cdd:cd02877 3 IAVYWgQNSDEGS----LREYcdTGNYDIVNISFlnvfgsgGTPGLNFAGHCGG--STYPNCPQLGADIKHCQSKGKKVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 115 ISIGGANGQVQLPSTSARDNFVNSVIAIiekYG---------------FDGLDVDFEgHSLYLNSGDsdfknpttpvivn 179
Cdd:cd02877 77 LSIGGAGGSYSLSSDADAKDFADYLWNA---FGggtdsgvprpfgdavVDGFDFDIE-HGSPENYDA------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 180 LISALRTINNHFGTGPFYLTMAPEtffvqlgysfyggsCISCDnragAYLPVIYATRDIlDWLQVQNYNSGpitglDDQY 259
Cdd:cd02877 140 LAKRLRSLFASDPSKKYYLTAAPQ--------------CPYPD----ASLGDAIATGLF-DFIFVQFYNNP-----CCSY 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 260 HNMGNAD--FHVAMADMILTGFPVAKnlnqmfpplrpdqVVLGLPANVNA-GGGFTSVAEvhkaldaLIKGVQlpSYKTR 336
Cdd:cd02877 196 ASGNASGfnFNWDTWTSWAKATSNAK-------------VFLGLPASPEAaGSGYVDPSE-------LASLVL--PVKQK 253
|
330 340
....*....|....*....|....
gi 1024025361 337 gsvsgYPNFRGLMTWSVNWDKFNN 360
Cdd:cd02877 254 -----SPNFGGVMLWDASQDKQGT 272
|
|
| FN3 |
cd00063 |
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ... |
384-467 |
4.93e-15 |
|
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: 70.60 E-value: 4.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 384 PTAPTHVTSMSKSATSVSLSWTASTDNVG-VTGYIVYYGS---------QSVSVTGTSTVISGLTPDTSYTFTVKAVDAR 453
Cdd:cd00063 1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGpITGYVVEYREkgsgdwkevEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80
|
90
....*....|....
gi 1024025361 454 GnQSAASTPLTVTT 467
Cdd:cd00063 81 G-ESPPSESVTVTT 93
|
|
| FN3 |
cd00063 |
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ... |
479-561 |
2.32e-14 |
|
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: 69.06 E-value: 2.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 479 PTAPGNVQVTAKTATSVSLSWNASTDNVG-VTGYIVTYGT---------SSVNTAGTSATINGLTANTSYSFTVTAKDAA 548
Cdd:cd00063 1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGpITGYVVEYREkgsgdwkevEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80
|
90
....*....|...
gi 1024025361 549 GNVSAGTIISVTT 561
Cdd:cd00063 81 GESPPSESVTVTT 93
|
|
| FN3 |
smart00060 |
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
479-549 |
8.52e-13 |
|
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: 64.17 E-value: 8.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 479 PTAPGNVQVTAKTATSVSLSWNASTDNVG---VTGYIVTYGTSS-------VNTAGTSATINGLTANTSYSFTVTAKDAA 548
Cdd:smart00060 1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItgyIVGYRVEYREEGsewkevnVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80
|
.
gi 1024025361 549 G 549
Cdd:smart00060 81 G 81
|
|
| COG4733 |
COG4733 |
Phage-related protein, tail protein J [Mobilome: prophages, transposons]; |
372-566 |
1.08e-12 |
|
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
Pssm-ID: 443767 [Multi-domain] Cd Length: 978 Bit Score: 71.13 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 372 DALSPPLPDTQPPTAPT----HVTSMSKSATSVSLSWTASTdnvGVTGYIVYY----GS-QSVSVTGTSTVISGLTPDTS 442
Cdd:COG4733 522 GAFDDVPPQWPPVNVTTseslSVVAQGTAVTTLTVSWDAPA---GAVAYEVEWrrddGNwVSVPRTSGTSFEVPGIYAGD 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 443 YTFTVKAVDARGNQSAASTPLTVTtdppgTGGDTTLPTAPGNVQVTAKTaTSVSLSWNASTDnVGVTGYIVTYGTSS--- 519
Cdd:COG4733 599 YEVRVRAINALGVSSAWAASSETT-----VTGKTAPPPAPTGLTATGGL-GGITLSWSFPVD-ADTLRTEIRYSTTGdwa 671
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1024025361 520 ------VNTAGTSATINGLTANTSYSFTVTAKDAAGNVSAGTIISVTTAPQSG 566
Cdd:COG4733 672 satvaqALYPGNTYTLAGLKAGQTYYYRARAVDRSGNVSAWWVSGQASADAAG 724
|
|
| FN3 |
smart00060 |
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
384-454 |
1.88e-12 |
|
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.
Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 63.02 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 384 PTAPTHVTSMSKSATSVSLSWTASTDNvGVTGYIVYYGSQ-----------SVSVTGTSTVISGLTPDTSYTFTVKAVDA 452
Cdd:smart00060 1 PSPPSNLRVTDVTSTSVTLSWEPPPDD-GITGYIVGYRVEyreegsewkevNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79
|
..
gi 1024025361 453 RG 454
Cdd:smart00060 80 AG 81
|
|
| GH18_EndoS-like |
cd06542 |
Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of ... |
60-250 |
1.80e-11 |
|
Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of various asparagine (N)-linked glycans and glycoproteins. The endo-beta-N-acetylglucosaminidases have a glycosyl hydrolase family 18 (GH18) catalytic domain. Some members also have an additional C-terminal glycosyl hydrolase family 20 (GH20) domain while others have an N-terminal domain of unknown function (pfam08522). Members of this family include endo-beta-N-acetylglucosaminidase S (EndoS) from Streptococcus pyogenes, EndoF1, EndoF2, EndoF3, and EndoH from Flavobacterium meningosepticum, and EndoE from Enterococcus faecalis. EndoS is a secreted endoglycosidase from Streptococcus pyogenes that specifically hydrolyzes the glycan on human IgG between two core N-acetylglucosamine residues. EndoE is a secreted endoglycosidase, encoded by the ndoE gene in Enterococcus faecalis, that hydrolyzes the glycan on human RNase B.
Pssm-ID: 119359 Cd Length: 255 Bit Score: 64.71 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 60 KLRDVSPKFDIINVsFAEPTSGVTNGTIGFIPYNYTEadfkaDVAYLQSQGKKVIISIGG---ANGQVQLPSTSARDNFV 136
Cdd:cd06542 20 SLLNLPDSVDMVSL-FAANINLDAATAVQFLLTNKET-----YIRPLQAKGTKVLLSILGnhlGAGFANNLSDAAAKAYA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 137 NSVIAIIEKYGFDGLDVDFEghslYLNSGDSDFKNPTTPVIVNLISALRtinNHFGTGPFYLTMapetffvqlgysfygg 216
Cdd:cd06542 94 KAIVDTVDKYGLDGVDFDDE----YSGYGKNGTSQPSNEAFVRLIKELR---KYMGPTDKLLTI---------------- 150
|
170 180 190
....*....|....*....|....*....|....
gi 1024025361 217 sciscDNRAGAYLPVIYATRDILDWLQVQNYNSG 250
Cdd:cd06542 151 -----DGYGQALSNDGEEVSPYVDYVIYQYYGSS 179
|
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
481-550 |
5.42e-11 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 58.97 E-value: 5.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 481 APGNVQVTAKTATSVSLSWNASTDNVG-VTGYIVTYGTSSVNTAG---------TSATINGLTANTSYSFTVTAKDAAGN 550
Cdd:pfam00041 2 APSNLTVTDVTSTSLTVSWTPPPDGNGpITGYEVEYRPKNSGEPWneitvpgttTSVTLTGLKPGTEYEVRVQAVNGGGE 81
|
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
386-455 |
4.01e-10 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 56.65 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 386 APTHVTSMSKSATSVSLSWTASTDNVG-VTGYIVYY-------GSQSVSVTGT--STVISGLTPDTSYTFTVKAVDARGN 455
Cdd:pfam00041 2 APSNLTVTDVTSTSLTVSWTPPPDGNGpITGYEVEYrpknsgePWNEITVPGTttSVTLTGLKPGTEYEVRVQAVNGGGE 81
|
|
| GH18_chitinase |
cd06548 |
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ... |
46-201 |
6.72e-09 |
|
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: 57.64 E-value: 6.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 46 VGY---WHNFDNGSGFIKLRDVSpKFDIINVSFAEPTSGvtNGTIGFIPYNYTEADFKADVAYLQSQGK----------- 111
Cdd:cd06548 2 VGYftnWGIYGRNYFVTDDIPAD-KLTHINYAFADIDGD--GGVVTSDDEAADEAAQSVDGGADTDDQPlkgnfgqlrkl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 112 -------KVIISIGG---ANGQVQLPSTSA-RDNFVNSVIAIIEKYGFDGLDVDFE----GHSLYLNSGDSDFKNpttpv 176
Cdd:cd06548 79 kqknphlKILLSIGGwtwSGGFSDAAATEAsRAKFADSAVDFIRKYGFDGIDIDWEypgsGGAPGNVARPEDKEN----- 153
|
170 180
....*....|....*....|....*...
gi 1024025361 177 IVNLISALRTINNHFG--TG-PFYLTMA 201
Cdd:cd06548 154 FTLLLKELREALDALGaeTGrKYLLTIA 181
|
|
| GH18_chitolectin_chitotriosidase |
cd02872 |
This conserved domain family includes a large number of catalytically inactive chitinase-like ... |
112-156 |
3.59e-08 |
|
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: 55.64 E-value: 3.59e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1024025361 112 KVIISIGGANGQVQLPSTSA-----RDNFVNSVIAIIEKYGFDGLDVDFE 156
Cdd:cd02872 72 KTLLAIGGWNFGSAKFSAMAaspenRKTFIKSAIAFLRKYGFDGLDLDWE 121
|
|
| GH18_3CO4_chitinase |
cd06545 |
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an ... |
46-188 |
4.03e-08 |
|
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: 54.77 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 46 VGYWHNFDNGSGFIKLRDVSpKFDIINVSFAEPTSgvtNGTIGFIPYNYTEADFKADVaylQSQGKKVIISIGGANGQVQ 125
Cdd:cd06545 2 VGYLPNYDDLNALSPTIDFS-KLTHINLAFANPDA---NGTLNANPVRSELNSVVNAA---HAHNVKILISLAGGSPPEF 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1024025361 126 ---LPSTSARDNFVNSVIAIIEKYGFDGLDVDFEGHslYLNSGDSDfknpttPVIVNLISALRTIN 188
Cdd:cd06545 75 taaLNDPAKRKALVDKIINYVVSYNLDGIDVDLEGP--DVTFGDYL------VFIRALYAALKKEG 132
|
|
| COG4733 |
COG4733 |
Phage-related protein, tail protein J [Mobilome: prophages, transposons]; |
380-589 |
5.75e-08 |
|
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
Pssm-ID: 443767 [Multi-domain] Cd Length: 978 Bit Score: 56.11 E-value: 5.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 380 DTQPPTAPTHVTSMSkSATSVSLSWTASTDnVGVTGYIVYYGSQS---------VSVTGTSTVISGLTPDTSYTFTVKAV 450
Cdd:COG4733 626 KTAPPPAPTGLTATG-GLGGITLSWSFPVD-ADTLRTEIRYSTTGdwasatvaqALYPGNTYTLAGLKAGQTYYYRARAV 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 451 DARGNQSAASTPLTVTTDPPG-----TGGDTTLPTAPGNVQVtAKTATSVSLSWNASTDNVGVTGYIVTYGTSSVNTAGT 525
Cdd:COG4733 704 DRSGNVSAWWVSGQASADAAGildaiTGQILETELGQELDAI-IQNATVAEVVAATVTDVTAQIDTAVLFAGVATAAAIG 782
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1024025361 526 SATINGLTANTSYSFTVTAKDAAGNVSAGTIISVTTAPQSGAQPWAANVSYKVNDEVTYGGKTY 589
Cdd:COG4733 783 AEARVAATVAESATAAAATGTAADAAGDASGGVTAGTSGTTGAGDTAASTTRVAAAVVLAGVVV 846
|
|
| ChiA |
COG3325 |
Chitinase, GH18 family [Carbohydrate transport and metabolism]; |
36-156 |
1.06e-07 |
|
Chitinase, GH18 family [Carbohydrate transport and metabolism];
Pssm-ID: 442554 [Multi-domain] Cd Length: 391 Bit Score: 54.53 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 36 AHAAVASKTLVGYWHNFDNGSGFIKLRDVSP-KFDIINVSFAEPTSgvtNGTIGFI-PYNYTEADFKADVAYLQSQGK-- 111
Cdd:COG3325 12 AATATSGKRVVGYFTQWGIYGRNYLVKDIPAsKLTHINYAFANVDP---DGKCSVGdAWAKPSVDGAADDWDQPLKGNfn 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1024025361 112 ------------KVIISIGGANGQVQLP----STSARDNFVNSVIAIIEKYGFDGLDVDFE 156
Cdd:COG3325 89 qlkklkaknpnlKVLISIGGWTWSKGFSdaaaTPASRAAFVDSCVDLLRKYNFDGIDIDWE 149
|
|
| GH18_PF-ChiA-like |
cd06543 |
PF-ChiA is an uncharacterized chitinase found in the hyperthermophilic archaeon Pyrococcus ... |
88-157 |
1.85e-07 |
|
PF-ChiA is an uncharacterized chitinase found in the hyperthermophilic archaeon Pyrococcus furiosus with a glycosyl hydrolase family 18 (GH18) catalytic domain as well as a cellulose-binding domain. Members of this domain family are found not only in archaea but also in eukaryotes and prokaryotes. PF-ChiA exhibits hydrolytic activity toward both colloidal and crystalline (beta/alpha) chitins at high temperature.
Pssm-ID: 119360 Cd Length: 294 Bit Score: 53.07 E-value: 1.85e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 88 GFIPYNYTeADFKADVAYLQSQGKKVIISIGGANGQVQLPSTSARDNFVNSVIAIIEKYGFDGLDVDFEG 157
Cdd:cd06543 46 GSYPLDQG-GWIKSDIAALRAAGGDVIVSFGGASGTPLATSCTSADQLAAAYQKVIDAYGLTHLDFDIEG 114
|
|
| GH18_plant_chitinase_class_V |
cd02879 |
The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the ... |
112-302 |
1.66e-06 |
|
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: 50.06 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 112 KVIISIGGANGQVQLPST-----SARDNFVNSVIAIIEKYGFDGLDVDFEghslylnsgdsdfkNPTTPV--------IV 178
Cdd:cd02879 68 KTLLSIGGGGSDSSAFAAmasdpTARKAFINSSIKVARKYGFDGLDLDWE--------------FPSSQVemenfgklLE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 179 NLISALRTINNHFGTGPFYLTMAPeTFFVQLGYSFYGgsciscdnragaylpVIYATRDI---LDWLQVQNYN------- 248
Cdd:cd02879 134 EWRAAVKDEARSSGRPPLLLTAAV-YFSPILFLSDDS---------------VSYPIEAInknLDWVNVMAYDyygswes 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1024025361 249 --SGPITGLDDqyhNMGNADFHVAMADMILTGFPvaknlnqmfpplrPDQVVLGLP 302
Cdd:cd02879 198 ntTGPAAALYD---PNSNVSTDYGIKSWIKAGVP-------------AKKLVLGLP 237
|
|
| GH18_CTS3_chitinase |
cd06546 |
GH18 domain of CTS3 (chitinase 3), an uncharacterized protein from the human fungal pathogen ... |
21-351 |
1.98e-06 |
|
GH18 domain of CTS3 (chitinase 3), an uncharacterized protein from the human fungal pathogen Coccidioides posadasii. CTS3 has a chitinase-like glycosyl hydrolase family 18 (GH18) domain; and has homologs in bacteria as well as fungi.
Pssm-ID: 119363 Cd Length: 256 Bit Score: 49.64 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 21 VVLSLLQVTAIHIPKAHAAVASktlvgyWHNFDNGSgfIKLRDVSPKFDiinvsfaeptsgvtngtigfipyNYTEadFK 100
Cdd:cd06546 16 PISSLLLVTEKGIALTHLIVAA------LHINDDGN--IHLNDHPPDHP-----------------------RFTT--LW 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 101 ADVAYLQSQGKKVIISIGGA-NGQVQLPSTSARD--NFVNSVIAIIEKYGFDGLDVDFEGH-SLylnsgdsdfknpttPV 176
Cdd:cd06546 63 TELAILQSSGVKVMGMLGGAaPGSFSRLDDDDEDfeRYYGQLRDMIRRRGLDGLDLDVEEPmSL--------------DG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 177 IVNLISALRTinnHFGTGpFYLTMAPetffvqLGYSFYGGSciscDNRAG-AYLPVIYATRDILDWLQVQNYNSgpitgl 255
Cdd:cd06546 129 IIRLIDRLRS---DFGPD-FIITLAP------VASALTGGE----ANLSGfDYRELEQARGDKIDFYNAQFYNG------ 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 256 ddqYHNMGNADfhvaMADMILTGfpvaknlnqmfpPLRPDQVVLGLPANVNAGGGFTSVAEVHKALDALikgvqlpsykt 335
Cdd:cd06546 189 ---FGSMSSPS----DYDAIVAQ------------GWDPERIVIGLLTNPDNGQGFVPFDTLSSTLSTL----------- 238
|
330
....*....|....*.
gi 1024025361 336 rgsVSGYPNFRGLMTW 351
Cdd:cd06546 239 ---RQRYPNFGGVMGW 251
|
|
| GH18_CFLE_spore_hydrolase |
cd02874 |
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ... |
93-157 |
3.37e-05 |
|
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: 46.10 E-value: 3.37e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1024025361 93 NYTEADFKADVAylqsqgkkviisiggangQVQLPSTSARDNFVNSVIAIIEKYGFDGLDVDFEG 157
Cdd:cd02874 67 NLTNGNFDSELA------------------HAVLSNPEARQRLINNILALAKKYGYDGVNIDFEN 113
|
|
| GH18_narbonin |
cd06544 |
Narbonin is a plant 2S protein from the globulin fraction of narbon bean (Vicia narbonensis L.) ... |
68-156 |
3.39e-05 |
|
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: 45.83 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 68 FDIInVSFA---EPTSGVTNGTigFIPYNYTEADFKADVAYLQSQGK--KVIISIGGANGQVQL----PSTSAR--DNFV 136
Cdd:cd06544 26 FHFI-LSFAidyDTESNPTNGK--FNPYWDTENLTPEAVKSIKAQHPnvKVVISIGGRGVQNNPtpfdPSNVDSwvSNAV 102
|
90 100
....*....|....*....|
gi 1024025361 137 NSVIAIIEKYGFDGLDVDFE 156
Cdd:cd06544 103 SSLTSIIQTYNLDGIDIDYE 122
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
381-565 |
1.43e-04 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 44.57 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 381 TQPPTAPTHVTSMSKSATSVSLSWTASTDNVGvtgyivyygsqsvsvTGTST-VISGLTPDTSYTFTVKAVDARGNQSAA 459
Cdd:pfam17823 63 ATAAPAPVTLTKGTSAAHLNSTEVTAEHTPHG---------------TDLSEpATREGAADGAASRALAAAASSSPSSAA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 460 STPLTVTTDPPGTGGDT---TLPTAPGNVQVTAKTATSVSLSWNASTDNVGVTGYIVTYGTSSVNTAGTSATINGLTANT 536
Cdd:pfam17823 128 QSLPAAIAALPSEAFSApraAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLT 207
|
170 180 190
....*....|....*....|....*....|...
gi 1024025361 537 SYSFTVTAKDAAGNVSAGTIIS----VTTAPQS 565
Cdd:pfam17823 208 PARGISTAATATGHPAAGTALAavgnSSPAAGT 240
|
|
| PHA03255 |
PHA03255 |
BDLF3; Provisional |
401-561 |
1.81e-04 |
|
BDLF3; Provisional
Pssm-ID: 165513 [Multi-domain] Cd Length: 234 Bit Score: 43.35 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 401 SLSWTAStdnvgvtgyivyyGSQSVSVTGTSTVISGLTPDTSytftvkavdARGNQSAASTPLTVTTDP----PGTGGDT 476
Cdd:PHA03255 21 SLIWTSS-------------GSSTASAGNVTGTTAVTTPSPS---------ASGPSTNQSTTLTTTSAPitttAILSTNT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 477 TLPTAPGNvqvtakTATSVSLSWNASTDNVGVTGYIVTYGTSSVNTAGTSATINGLTANTSYSFTVTAKDAAGNVSAGTI 556
Cdd:PHA03255 79 TTVTSTGT------TVTPVPTTSNASTINVTTKVTAQNITATEAGTGTSTGVTSNVTTRSSSTTSATTRITNATTLAPTL 152
|
....*
gi 1024025361 557 ISVTT 561
Cdd:PHA03255 153 SSKGT 157
|
|
| GH18_zymocin_alpha |
cd02878 |
Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle ... |
46-156 |
1.84e-04 |
|
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: 43.84 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 46 VGYWHNFDNGSGfiKLR-DV----SPKFDIINVSFAEPTSgvtngtigfipynyteaDFKADVAYLQSQ--------GKK 112
Cdd:cd02878 3 IAYFEAYNLDRP--CLNmDVtqidTSKYTHIHFAFANITS-----------------DFSVDVSSVQEQfsdfkklkGVK 63
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1024025361 113 VIISIGGANGQVQlPST----------SARDNFVNSVIAIIEKYGFDGLDVDFE 156
Cdd:cd02878 64 KILSFGGWDFSTS-PSTyqifrdavkpANRDTFANNVVNFVNKYNLDGVDFDWE 116
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
377-583 |
3.91e-04 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 43.45 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 377 PLPDTQPPTAPTHVTSMSKSATSVSLSW---TASTDNVGVTGYIVYYGSQSVSVTGTSTVISGLTPDTSYTFTVKAVDAR 453
Cdd:COG3401 42 VVLSVTTKESPGTLLVAAGLSSGGGLGTggrAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 454 GNQSAASTPLTVTTDPPGTGGDTTLPTAPGNVQVTAKTATSVSLSWNASTDNVGVTGYIVTYGTSSVNTaGTSATINGLT 533
Cdd:COG3401 122 VGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTST-TLVDGGGDIE 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1024025361 534 ANTSYSFTVTAKDAAGNVSAGTIISVTTAPQSGAQPWAANVSYKVNDEVT 583
Cdd:COG3401 201 PGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVT 250
|
|
| GH18_IDGF |
cd02873 |
The IDGF's (imaginal disc growth factors) are a family of growth factors identified in insects ... |
112-196 |
4.36e-04 |
|
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: 43.07 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 112 KVIISIGGANGQVQ----------LPSTSARDNFVNSVIAIIEKYGFDGLDVDFEghslylnsgdsdF-KNPTTPVIVNL 180
Cdd:cd02873 76 KVLLSVGGDRDTDEegenekylllLESSESRNAFINSAHSLLKTYGFDGLDLAWQ------------FpKNKPKKVRGTF 143
|
90
....*....|....*.
gi 1024025361 181 ISALRTINNHFGTGPF 196
Cdd:cd02873 144 GSAWHSFKKLFTGDSV 159
|
|
| ChtBD3 |
smart00495 |
Chitin-binding domain type 3; |
567-610 |
2.66e-03 |
|
Chitin-binding domain type 3;
Pssm-ID: 197760 [Multi-domain] Cd Length: 41 Bit Score: 35.70 E-value: 2.66e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1024025361 567 AQPWAANVSYKVNDEVTYGGKTYICrqphTSLTGWEPPN-VPALW 610
Cdd:smart00495 1 APAWQAGTVYTAGDVVSYNGKVYKA----KWWTQGEEPGsSSGPW 41
|
|
| ChtBD3 |
cd00036 |
Chitin/cellulose binding domains of chitinase and related enzymes; This group contains ... |
570-610 |
6.00e-03 |
|
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: 35.04 E-value: 6.00e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1024025361 570 WAANVSYKVNDEVTYGGKTYICRQPHtslTGWEPPNVpALW 610
Cdd:cd00036 2 WPNPTHYTAGQSVVYNGNLYTANWYT---AGSVPGSD-SSW 38
|
|
| myxo_dep_M36 |
NF038112 |
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ... |
382-560 |
6.32e-03 |
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myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.
Pssm-ID: 468355 [Multi-domain] Cd Length: 1597 Bit Score: 39.64 E-value: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 382 QPPTAPTHVTSMSKSATSVSLSWTAS-TDNVGVTGYIVYYGSQSVSVTGTSTVISGLTP-----DTSYTFTVKAVDarGN 455
Cdd:NF038112 1281 RAPVAVAGAPATVDERSTVTLDGSGTdADGDALTYAWTQTSGPAVTLTGATTATATFTApevtaDTQLTFTLTVSD--GT 1358
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024025361 456 QSAASTpLTVT-TDPPGTggdttlPTAPGNVQVTAKTATSVSLSWNAsTDNVG---------VTGYIVTYgtSSVNTAGT 525
Cdd:NF038112 1359 ASATDT-VTVTvRNVNRA------PVANAGADQTVDERSTVTLSGSA-TDPDGdaltyawtqTAGPTVTL--TGADTATA 1428
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170 180 190
....*....|....*....|....*....|....*
gi 1024025361 526 SATINGLTANTSYSFTVTAKdAAGNVSAGTIISVT 560
Cdd:NF038112 1429 SFTAPEVAADTELTFQLTVS-ADGQASADVTVTVT 1462
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