|
Name |
Accession |
Description |
Interval |
E-value |
| ChiA |
COG3325 |
Chitinase, GH18 family [Carbohydrate transport and metabolism]; |
303-777 |
3.63e-145 |
|
Chitinase, GH18 family [Carbohydrate transport and metabolism];
Pssm-ID: 442554 [Multi-domain] Cd Length: 391 Bit Score: 438.96 E-value: 3.63e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 303 EKLGPDHQRRIIGYFTSWRNGTNGqpsYLVKDIPWDKVTHINYAFAHIDSDYSISIGDTSNpdnpstgmeWPGVSGAETD 382
Cdd:COG3325 11 AAATATSGKRVVGYFTQWGIYGRN---YLVKDIPASKLTHINYAFANVDPDGKCSVGDAWA---------KPSVDGAADD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 383 PAFNYKGHFNQLAKYKKQHPDVKTLVSVGGWAETGGhlneqgdrvndggFYTMTTNAdgsvnyAGIEAFANSVVDFIRTY 462
Cdd:COG3325 79 WDQPLKGNFNQLKKLKAKNPNLKVLISIGGWTWSKG-------------FSDAAATP------ASRAAFVDSCVDLLRKY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 463 GFDGVDIDYEYPTSMNDAGNPLdfgfanplRAYLMNSYVALMRVLREKLDQAGEEDNTHYLLTIAAPSSGYLLRGMETMP 542
Cdd:COG3325 140 NFDGIDIDWEYPGSGGAPGNVY--------RPEDKANFTALLKELRAQLDALGAETGKHYLLTAAAPAGPDKLDGIELPK 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 543 ITQYLDYVNIMTYDFHGTWNEFVGHNSAIFDNGNDPELkaaniyntaqyggiGYLNIDWAVKYF-RGSMSPGRINIGTPY 621
Cdd:COG3325 212 VAQYLDYVNVMTYDFHGAWSPTTGHQAPLYDSPKDPEA--------------QGYSVDSAVQAYlAAGVPASKLVLGVPF 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 622 YTRGWQNVTSANGewGLGGTASLPnqsecPAGTggaakcgygaigidniWhdsdgngqeiGAGTNPLWHaknleqgILGS 701
Cdd:COG3325 278 YGRGWTGVTGGNN--GLYQPATGP-----APGT----------------W----------EAGVNDYKD-------LKAL 317
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1097558039 702 YIGyygldtvndpadrlVGTYTRHYDSVSQAAWLWNDTKKVFLSIEDEASMEAKAQYVIDQGLGGIMIWELAGDYA 777
Cdd:COG3325 318 YLG--------------SNGYTRYWDDVAKAPYLYNGDTGTFISYDDPRSIAAKADYVKDKGLGGVMFWELSGDTA 379
|
|
| GH18_chitinase |
cd06548 |
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ... |
313-775 |
1.27e-106 |
|
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: 335.37 E-value: 1.27e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 313 IIGYFTSWRNGTNGQPSYlvKDIPWDKVTHINYAFAHIDSDYSISIGDTSNPDNpstgmEWPGVSGAETDPAFNYKGHFN 392
Cdd:cd06548 1 VVGYFTNWGIYGRNYFVT--DDIPADKLTHINYAFADIDGDGGVVTSDDEAADE-----AAQSVDGGADTDDQPLKGNFG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 393 QLAKYKKQHPDVKTLVSVGGWAETGGhlneqgdrvndggFYTMTTNAdgsvnyAGIEAFANSVVDFIRTYGFDGVDIDYE 472
Cdd:cd06548 74 QLRKLKQKNPHLKILLSIGGWTWSGG-------------FSDAAATE------ASRAKFADSAVDFIRKYGFDGIDIDWE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 473 YPTSmndagnplDFGFANPLRAYLMNSYVALMRVLREKLDQAGEEDNTHYLLTIAAPSSGYLLRGMETMPITQYLDYVNI 552
Cdd:cd06548 135 YPGS--------GGAPGNVARPEDKENFTLLLKELREALDALGAETGRKYLLTIAAPAGPDKLDKLEVAEIAKYLDFINL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 553 MTYDFHGTWNEFVGHNSAIFDNGNDPelkaaniyntaqyggIGYLNIDWAVKYF-RGSMSPGRINIGTPYYTRGWQNvts 631
Cdd:cd06548 207 MTYDFHGAWSNTTGHHSNLYASPADP---------------PGGYSVDAAVNYYlSAGVPPEKLVLGVPFYGRGWTG--- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 632 angewglggtaslpnqsecpagtggaakcgygaigidniwhdsdgngqeigagtnplwhaknleqgilgsyigyygldtv 711
Cdd:cd06548 --------------------------------------------------------------------------------
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1097558039 712 ndpadrlvgtYTRHYDSVSQAAWLWNDTKKVFLSIEDEASMEAKAQYVIDQGLGGIMIWELAGD 775
Cdd:cd06548 269 ----------YTRYWDEVAKAPYLYNPSTKTFISYDDPRSIKAKADYVKDKGLGGVMFWELSGD 322
|
|
| Glyco_18 |
smart00636 |
Glyco_18 domain; |
312-775 |
1.05e-98 |
|
Glyco_18 domain;
Pssm-ID: 214753 [Multi-domain] Cd Length: 334 Bit Score: 314.62 E-value: 1.05e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 312 RIIGYFTSWrnGTNGqPSYLVKDIPWDKVTHINYAFAHIDSDYSISIGDtsnpdnpstgmewpgvsgaetdpAFNYKGHF 391
Cdd:smart00636 1 RVVGYFTNW--GVYG-RNFPVDDIPASKLTHIIYAFANIDPDGTVTIGD-----------------------EWADIGNF 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 392 NQLAKYKKQHPDVKTLVSVGGWAEtgghlneqgdrvnDGGFYTMTTNAdgsvnyAGIEAFANSVVDFIRTYGFDGVDIDY 471
Cdd:smart00636 55 GQLKALKKKNPGLKVLLSIGGWTE-------------SDNFSSMLSDP------ASRKKFIDSIVSFLKKYGFDGIDIDW 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 472 EYPTSMNDAGNpldfgfanplraylmnSYVALMRVLREKLDQAGEEdNTHYLLTIAAPSSG-YLLRGMETMP-ITQYLDY 549
Cdd:smart00636 116 EYPGGRGDDRE----------------NYTALLKELREALDKEGAE-GKGYLLTIAVPAGPdKIDKGYGDLPaIAKYLDF 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 550 VNIMTYDFHGTWNEFVGHNSAIFDNGNDPElkaaniyntaqyggigYLNIDWAVKYFRG-SMSPGRINIGTPYYTRGWQN 628
Cdd:smart00636 179 INLMTYDFHGAWSNPTGHNAPLYAGPGDPE----------------KYNVDYAVKYYLCkGVPPSKLVLGIPFYGRGWTL 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 629 VTSANGewglggtaslpnqsecpagtggaakcgygaiGIDNIWHDSDGNGQEIGAGTNPLWHAKNLEQGilgsyigyygl 708
Cdd:smart00636 243 VDGSNN-------------------------------GPGAPFTGPATGGPGTWEGGVVDYREICKLLG----------- 280
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1097558039 709 dtvndpadrlvgtYTRHYDSVSQAAWLWNDTKKVFLSIEDEASMEAKAQYVIDQGLGGIMIWELAGD 775
Cdd:smart00636 281 -------------ATVVYDDTAKAPYAYNPGTGQWVSYDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
|
|
| Glyco_hydro_18 |
pfam00704 |
Glycosyl hydrolases family 18; |
312-775 |
4.91e-76 |
|
Glycosyl hydrolases family 18;
Pssm-ID: 425828 [Multi-domain] Cd Length: 311 Bit Score: 252.76 E-value: 4.91e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 312 RIIGYFTSWRNGTNGQPsylvkdIPWDKVTHINYAFAHIDS-DYSISIGDTSnpdnpstgmewpgvsgaetdpafnyKGH 390
Cdd:pfam00704 1 RIVGYYTSWGVYRNGNF------LPSDKLTHIIYAFANIDGsDGTLFIGDWD-------------------------LGN 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 391 FNQLAKYKKQ-HPDVKTLVSVGGWAETGGhlneqgdrvndggFYTMTTNAdgsvnyAGIEAFANSVVDFIRTYGFDGVDI 469
Cdd:pfam00704 50 FEQLKKLKKQkNPGVKVLLSIGGWTDSTG-------------FSLMASNP------ASRKKFADSIVSFLRKYGFDGIDI 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 470 DYEYPTsmndaGNPLDfgfanplraylMNSYVALMRVLREKLDQAgeEDNTHYLLTIAAPSSGYLLRGMETMP-ITQYLD 548
Cdd:pfam00704 111 DWEYPG-----GNPED-----------KENYDLLLRELRAALDEA--KGGKKYLLSAAVPASYPDLDKGYDLPkIAKYLD 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 549 YVNIMTYDFHGTWNEFVGHNSAIFDNgndpelkaaniyntaqyggiGYLNIDWAVKYF-RGSMSPGRINIGTPYYTRGWQ 627
Cdd:pfam00704 173 FINVMTYDFHGSWDNVTGHHAPLYGG--------------------GSYNVDYAVKYYlKQGVPASKLVLGVPFYGRSWT 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 628 NVTSANGEWGLGgtaslpnqsecpagtggaakcgygaigidniwhdsdgngqeigagtnpLWHAKNLEQGILGsyigyyg 707
Cdd:pfam00704 233 LVNGSGNTWEDG------------------------------------------------VLAYKEICNLLKD------- 257
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1097558039 708 ldtvndpadrlvGTYTRHYDSVSQAAWLWNDTkkVFLSIEDEASMEAKAQYVIDQGLGGIMIWELAGD 775
Cdd:pfam00704 258 ------------NGATVVWDDVAKAPYVYDGD--QFITYDDPRSIATKVDYVKAKGLGGVMIWSLDAD 311
|
|
| ChiC |
pfam06483 |
Chitinase C; This ~170 aa region is found at the C-terminus of pfam00704. |
784-950 |
4.32e-70 |
|
Chitinase C; This ~170 aa region is found at the C-terminus of pfam00704.
Pssm-ID: 368936 Cd Length: 174 Bit Score: 231.05 E-value: 4.32e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 784 EYFVGSTMTGVAYEKFKSATPYREKRSNRPLPTQAVDITITVSDFKLGDQNYPLNPKLAITNNTGTTIPGGTVFEFDMPT 863
Cdd:pfam06483 1 EYFMGDTLTTLLYDKFKAAAPYGATKANAAMPTQVLDVSVSLTGFPLGDSNYPINPKLRITNNSGQTIPGGTEFEFDYPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 864 STPDTISDQSGAGLEVIESgaNAGGGNVGGLQHEFHRVRFSLPNWKDLADSESWDMTLNYYLPITGPQAYTVTINGTAYA 943
Cdd:pfam06483 81 SAPDNAKDQSGFGLTVISS--GHTGPNVGGLKGDFHRVAFTLPSWQTLAPGASVEVDLVYYLPVSGPSNWTVTFGGTTYA 158
|
....*..
gi 1097558039 944 LAFEYPD 950
Cdd:pfam06483 159 LKGDYPR 165
|
|
| CBD_like |
cd12204 |
Cellulose-binding domain, chitinase and related proteins; This group contains proteins related ... |
985-1033 |
2.72e-20 |
|
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: 85.07 E-value: 2.72e-20
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1097558039 985 SVYPVYPNWPAGDHANGGDRIVHNGSVWQAKWWTNSQPGsSDGSWTLIC 1033
Cdd:cd12204 1 AGANAYPNWPQGTHAAGGDLVSYNGAVYQAKWWTQSAPG-SDSSWTLVC 48
|
|
| Big_7 |
pfam17957 |
Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in ... |
184-247 |
6.66e-15 |
|
Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in glycosyl hydrolase enzymes.
Pssm-ID: 436171 [Multi-domain] Cd Length: 67 Bit Score: 70.33 E-value: 6.66e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1097558039 184 ISLDAPANGTTFdTGASVAITATASDtDGSLLNVEFFVDGASVGVDTTPPYQFNWTA---IEGNHTI 247
Cdd:pfam17957 1 VSITSPANGATV-SGGTVTISATASD-DGGVSKVEFYVDGTLVGTDTSAPYSFTWTTtalANGTHTI 65
|
|
| Big_7 |
pfam17957 |
Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in ... |
91-166 |
9.18e-15 |
|
Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in glycosyl hydrolase enzymes.
Pssm-ID: 436171 [Multi-domain] Cd Length: 67 Bit Score: 69.94 E-value: 9.18e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1097558039 91 SITSPASGTVFNkNDSVIISVDASDNSAVVSVEFFVDGTSIGTDITPPWQISWSASgtnpvlsariTDDAGQQTVT 166
Cdd:pfam17957 2 SITSPANGATVS-GGTVTISATASDDGGVSKVEFYVDGTLVGTDTSAPYSFTWTTT----------ALANGTHTIT 66
|
|
| CBM_5_12_2 |
pfam14600 |
Cellulose-binding domain; This C-terminal domain belongs to the CAZy family of ... |
989-1036 |
6.40e-10 |
|
Cellulose-binding domain; This C-terminal domain belongs to the CAZy family of carbohydrate-binding domains that are associated with glycosyl-hydrolases. It is suggested to bind cellulose.
Pssm-ID: 434062 Cd Length: 62 Bit Score: 55.95 E-value: 6.40e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1097558039 989 VYPNWPAGD-------HANGGDRIVHNGSVWQAKWWTNSQPGsSDGSWTLICSAN 1036
Cdd:pfam14600 9 EYPNWTAKDwaggpynHANAGDQMVYQGTLYQANWYTNSVPG-SDASWTFLGACA 62
|
|
| ChtBD3 |
smart00495 |
Chitin-binding domain type 3; |
990-1029 |
4.57e-06 |
|
Chitin-binding domain type 3;
Pssm-ID: 197760 [Multi-domain] Cd Length: 41 Bit Score: 44.17 E-value: 4.57e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1097558039 990 YPNWPAGDHANGGDRIVHNGSVWQAKWWT-NSQPGSSDGSW 1029
Cdd:smart00495 1 APAWQAGTVYTAGDVVSYNGKVYKAKWWTqGEEPGSSSGPW 41
|
|
| ChtBD3 |
smart00495 |
Chitin-binding domain type 3; |
27-69 |
2.39e-04 |
|
Chitin-binding domain type 3;
Pssm-ID: 197760 [Multi-domain] Cd Length: 41 Bit Score: 39.55 E-value: 2.39e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1097558039 27 PAYADGTSYNTGDQVQNNNTAYQCTvggWCTigGPYAPGVGWA 69
Cdd:smart00495 2 PAWQAGTVYTAGDVVSYNGKVYKAK---WWT--QGEEPGSSSG 39
|
|
| ChiA1_BD |
cd12214 |
chitin-binding domain of Chi A1-like proteins; This group contains proteins related to the ... |
28-59 |
1.65e-03 |
|
chitin-binding domain of Chi A1-like proteins; This group contains proteins related to the chitin binding domain of chitinase A1 (ChiA1) of Bacillus circulans WL-12. Glycosidase ChiA1 hydrolyzes chitin and is comprised of several domains: the C-terminal chitin binding domain, an N-terminal and catalytic domain, and 2 fibronectin type III-like domains. Chitinases function in invertebrates in the degradation of old exoskeletons, in fungi to utilize chitin in cell walls, and in bacteria which use chitin as an energy source. Bacillus circulans WL-12 ChiA1 facilitates invasion of fungal cell walls. The ChiAi chitin binding domain is required for the specific recognition of insoluble chitin. although topologically and structurally related, ChiA1 lacks the characteristic aromatic residues of Erwinia chrysanthemi endoglucanase Z (CBD(EGZ)).
Pssm-ID: 213177 [Multi-domain] Cd Length: 45 Bit Score: 37.32 E-value: 1.65e-03
10 20 30
....*....|....*....|....*....|..
gi 1097558039 28 AYADGTSYNTGDQVQNNNTAYQCTVGGWCTIG 59
Cdd:cd12214 1 EWAAGTTYKAGDIVTYNGKLYRCLQAHTSLAG 32
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ChiA |
COG3325 |
Chitinase, GH18 family [Carbohydrate transport and metabolism]; |
303-777 |
3.63e-145 |
|
Chitinase, GH18 family [Carbohydrate transport and metabolism];
Pssm-ID: 442554 [Multi-domain] Cd Length: 391 Bit Score: 438.96 E-value: 3.63e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 303 EKLGPDHQRRIIGYFTSWRNGTNGqpsYLVKDIPWDKVTHINYAFAHIDSDYSISIGDTSNpdnpstgmeWPGVSGAETD 382
Cdd:COG3325 11 AAATATSGKRVVGYFTQWGIYGRN---YLVKDIPASKLTHINYAFANVDPDGKCSVGDAWA---------KPSVDGAADD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 383 PAFNYKGHFNQLAKYKKQHPDVKTLVSVGGWAETGGhlneqgdrvndggFYTMTTNAdgsvnyAGIEAFANSVVDFIRTY 462
Cdd:COG3325 79 WDQPLKGNFNQLKKLKAKNPNLKVLISIGGWTWSKG-------------FSDAAATP------ASRAAFVDSCVDLLRKY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 463 GFDGVDIDYEYPTSMNDAGNPLdfgfanplRAYLMNSYVALMRVLREKLDQAGEEDNTHYLLTIAAPSSGYLLRGMETMP 542
Cdd:COG3325 140 NFDGIDIDWEYPGSGGAPGNVY--------RPEDKANFTALLKELRAQLDALGAETGKHYLLTAAAPAGPDKLDGIELPK 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 543 ITQYLDYVNIMTYDFHGTWNEFVGHNSAIFDNGNDPELkaaniyntaqyggiGYLNIDWAVKYF-RGSMSPGRINIGTPY 621
Cdd:COG3325 212 VAQYLDYVNVMTYDFHGAWSPTTGHQAPLYDSPKDPEA--------------QGYSVDSAVQAYlAAGVPASKLVLGVPF 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 622 YTRGWQNVTSANGewGLGGTASLPnqsecPAGTggaakcgygaigidniWhdsdgngqeiGAGTNPLWHaknleqgILGS 701
Cdd:COG3325 278 YGRGWTGVTGGNN--GLYQPATGP-----APGT----------------W----------EAGVNDYKD-------LKAL 317
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1097558039 702 YIGyygldtvndpadrlVGTYTRHYDSVSQAAWLWNDTKKVFLSIEDEASMEAKAQYVIDQGLGGIMIWELAGDYA 777
Cdd:COG3325 318 YLG--------------SNGYTRYWDDVAKAPYLYNGDTGTFISYDDPRSIAAKADYVKDKGLGGVMFWELSGDTA 379
|
|
| GH18_chitinase |
cd06548 |
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ... |
313-775 |
1.27e-106 |
|
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: 335.37 E-value: 1.27e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 313 IIGYFTSWRNGTNGQPSYlvKDIPWDKVTHINYAFAHIDSDYSISIGDTSNPDNpstgmEWPGVSGAETDPAFNYKGHFN 392
Cdd:cd06548 1 VVGYFTNWGIYGRNYFVT--DDIPADKLTHINYAFADIDGDGGVVTSDDEAADE-----AAQSVDGGADTDDQPLKGNFG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 393 QLAKYKKQHPDVKTLVSVGGWAETGGhlneqgdrvndggFYTMTTNAdgsvnyAGIEAFANSVVDFIRTYGFDGVDIDYE 472
Cdd:cd06548 74 QLRKLKQKNPHLKILLSIGGWTWSGG-------------FSDAAATE------ASRAKFADSAVDFIRKYGFDGIDIDWE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 473 YPTSmndagnplDFGFANPLRAYLMNSYVALMRVLREKLDQAGEEDNTHYLLTIAAPSSGYLLRGMETMPITQYLDYVNI 552
Cdd:cd06548 135 YPGS--------GGAPGNVARPEDKENFTLLLKELREALDALGAETGRKYLLTIAAPAGPDKLDKLEVAEIAKYLDFINL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 553 MTYDFHGTWNEFVGHNSAIFDNGNDPelkaaniyntaqyggIGYLNIDWAVKYF-RGSMSPGRINIGTPYYTRGWQNvts 631
Cdd:cd06548 207 MTYDFHGAWSNTTGHHSNLYASPADP---------------PGGYSVDAAVNYYlSAGVPPEKLVLGVPFYGRGWTG--- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 632 angewglggtaslpnqsecpagtggaakcgygaigidniwhdsdgngqeigagtnplwhaknleqgilgsyigyygldtv 711
Cdd:cd06548 --------------------------------------------------------------------------------
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1097558039 712 ndpadrlvgtYTRHYDSVSQAAWLWNDTKKVFLSIEDEASMEAKAQYVIDQGLGGIMIWELAGD 775
Cdd:cd06548 269 ----------YTRYWDEVAKAPYLYNPSTKTFISYDDPRSIKAKADYVKDKGLGGVMFWELSGD 322
|
|
| Glyco_18 |
smart00636 |
Glyco_18 domain; |
312-775 |
1.05e-98 |
|
Glyco_18 domain;
Pssm-ID: 214753 [Multi-domain] Cd Length: 334 Bit Score: 314.62 E-value: 1.05e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 312 RIIGYFTSWrnGTNGqPSYLVKDIPWDKVTHINYAFAHIDSDYSISIGDtsnpdnpstgmewpgvsgaetdpAFNYKGHF 391
Cdd:smart00636 1 RVVGYFTNW--GVYG-RNFPVDDIPASKLTHIIYAFANIDPDGTVTIGD-----------------------EWADIGNF 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 392 NQLAKYKKQHPDVKTLVSVGGWAEtgghlneqgdrvnDGGFYTMTTNAdgsvnyAGIEAFANSVVDFIRTYGFDGVDIDY 471
Cdd:smart00636 55 GQLKALKKKNPGLKVLLSIGGWTE-------------SDNFSSMLSDP------ASRKKFIDSIVSFLKKYGFDGIDIDW 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 472 EYPTSMNDAGNpldfgfanplraylmnSYVALMRVLREKLDQAGEEdNTHYLLTIAAPSSG-YLLRGMETMP-ITQYLDY 549
Cdd:smart00636 116 EYPGGRGDDRE----------------NYTALLKELREALDKEGAE-GKGYLLTIAVPAGPdKIDKGYGDLPaIAKYLDF 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 550 VNIMTYDFHGTWNEFVGHNSAIFDNGNDPElkaaniyntaqyggigYLNIDWAVKYFRG-SMSPGRINIGTPYYTRGWQN 628
Cdd:smart00636 179 INLMTYDFHGAWSNPTGHNAPLYAGPGDPE----------------KYNVDYAVKYYLCkGVPPSKLVLGIPFYGRGWTL 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 629 VTSANGewglggtaslpnqsecpagtggaakcgygaiGIDNIWHDSDGNGQEIGAGTNPLWHAKNLEQGilgsyigyygl 708
Cdd:smart00636 243 VDGSNN-------------------------------GPGAPFTGPATGGPGTWEGGVVDYREICKLLG----------- 280
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1097558039 709 dtvndpadrlvgtYTRHYDSVSQAAWLWNDTKKVFLSIEDEASMEAKAQYVIDQGLGGIMIWELAGD 775
Cdd:smart00636 281 -------------ATVVYDDTAKAPYAYNPGTGQWVSYDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
|
|
| Glyco_hydro_18 |
pfam00704 |
Glycosyl hydrolases family 18; |
312-775 |
4.91e-76 |
|
Glycosyl hydrolases family 18;
Pssm-ID: 425828 [Multi-domain] Cd Length: 311 Bit Score: 252.76 E-value: 4.91e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 312 RIIGYFTSWRNGTNGQPsylvkdIPWDKVTHINYAFAHIDS-DYSISIGDTSnpdnpstgmewpgvsgaetdpafnyKGH 390
Cdd:pfam00704 1 RIVGYYTSWGVYRNGNF------LPSDKLTHIIYAFANIDGsDGTLFIGDWD-------------------------LGN 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 391 FNQLAKYKKQ-HPDVKTLVSVGGWAETGGhlneqgdrvndggFYTMTTNAdgsvnyAGIEAFANSVVDFIRTYGFDGVDI 469
Cdd:pfam00704 50 FEQLKKLKKQkNPGVKVLLSIGGWTDSTG-------------FSLMASNP------ASRKKFADSIVSFLRKYGFDGIDI 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 470 DYEYPTsmndaGNPLDfgfanplraylMNSYVALMRVLREKLDQAgeEDNTHYLLTIAAPSSGYLLRGMETMP-ITQYLD 548
Cdd:pfam00704 111 DWEYPG-----GNPED-----------KENYDLLLRELRAALDEA--KGGKKYLLSAAVPASYPDLDKGYDLPkIAKYLD 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 549 YVNIMTYDFHGTWNEFVGHNSAIFDNgndpelkaaniyntaqyggiGYLNIDWAVKYF-RGSMSPGRINIGTPYYTRGWQ 627
Cdd:pfam00704 173 FINVMTYDFHGSWDNVTGHHAPLYGG--------------------GSYNVDYAVKYYlKQGVPASKLVLGVPFYGRSWT 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 628 NVTSANGEWGLGgtaslpnqsecpagtggaakcgygaigidniwhdsdgngqeigagtnpLWHAKNLEQGILGsyigyyg 707
Cdd:pfam00704 233 LVNGSGNTWEDG------------------------------------------------VLAYKEICNLLKD------- 257
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1097558039 708 ldtvndpadrlvGTYTRHYDSVSQAAWLWNDTkkVFLSIEDEASMEAKAQYVIDQGLGGIMIWELAGD 775
Cdd:pfam00704 258 ------------NGATVVWDDVAKAPYVYDGD--QFITYDDPRSIATKVDYVKAKGLGGVMIWSLDAD 311
|
|
| ChiC |
pfam06483 |
Chitinase C; This ~170 aa region is found at the C-terminus of pfam00704. |
784-950 |
4.32e-70 |
|
Chitinase C; This ~170 aa region is found at the C-terminus of pfam00704.
Pssm-ID: 368936 Cd Length: 174 Bit Score: 231.05 E-value: 4.32e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 784 EYFVGSTMTGVAYEKFKSATPYREKRSNRPLPTQAVDITITVSDFKLGDQNYPLNPKLAITNNTGTTIPGGTVFEFDMPT 863
Cdd:pfam06483 1 EYFMGDTLTTLLYDKFKAAAPYGATKANAAMPTQVLDVSVSLTGFPLGDSNYPINPKLRITNNSGQTIPGGTEFEFDYPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 864 STPDTISDQSGAGLEVIESgaNAGGGNVGGLQHEFHRVRFSLPNWKDLADSESWDMTLNYYLPITGPQAYTVTINGTAYA 943
Cdd:pfam06483 81 SAPDNAKDQSGFGLTVISS--GHTGPNVGGLKGDFHRVAFTLPSWQTLAPGASVEVDLVYYLPVSGPSNWTVTFGGTTYA 158
|
....*..
gi 1097558039 944 LAFEYPD 950
Cdd:pfam06483 159 LKGDYPR 165
|
|
| GH18_chitolectin_chitotriosidase |
cd02872 |
This conserved domain family includes a large number of catalytically inactive chitinase-like ... |
316-772 |
8.79e-56 |
|
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: 197.78 E-value: 8.79e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 316 YFTSWRNGTNGQPSYLVKDIPWDKVTHINYAFAHIDSDYSISIGDTSNPDNpstgmewpgvsgaetdpafnyKGHFNQLA 395
Cdd:cd02872 4 YFTNWAQYRPGNGKFVPENIDPFLCTHIIYAFAGLNPDGNIIILDEWNDID---------------------LGLYERFN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 396 KYKKQHPDVKTLVSVGGWaetgghlneqgdrvNDG--GFYTMTTNAdgsvnyAGIEAFANSVVDFIRTYGFDGVDIDYEY 473
Cdd:cd02872 63 ALKEKNPNLKTLLAIGGW--------------NFGsaKFSAMAASP------ENRKTFIKSAIAFLRKYGFDGLDLDWEY 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 474 PTSMNdaGNPLDfgfanplraylMNSYVALMRVLREKLDQAGEEdnthYLLTIAAPSS------GYLLRGmetmpITQYL 547
Cdd:cd02872 123 PGQRG--GPPED-----------KENFVTLLKELREAFEPEAPR----LLLTAAVSAGketidaAYDIPE-----ISKYL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 548 DYVNIMTYDFHGTWNEFVGHNSAIFDNGNDPelkaaniyntaqyGGIGYLNIDWAVKYFRGS-MSPGRINIGTPYYTRGW 626
Cdd:cd02872 181 DFINVMTYDFHGSWEGVTGHNSPLYAGSADT-------------GDQKYLNVDYAIKYWLSKgAPPEKLVLGIPTYGRSF 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 627 QNVTSANGewGLGGtaslpnqsecPAGTGGAAkcgygaigidniwhdsdgngqeiGAGTNplwhaknlEQGILgsyiGYY 706
Cdd:cd02872 248 TLASPSNT--GVGA----------PASGPGTA-----------------------GPYTR--------EAGFL----AYY 280
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1097558039 707 GLdtvndpADRLVGTYTRHYDSVSQAAWLWNDTKKVflSIEDEASMEAKAQYVIDQGLGGIMIWEL 772
Cdd:cd02872 281 EI------CEFLKSGWTVVWDDEQKVPYAYKGNQWV--GYDDEESIALKVQYLKSKGLGGAMVWSI 338
|
|
| GH18_chitinase-like |
cd00598 |
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ... |
313-556 |
4.91e-37 |
|
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: 138.66 E-value: 4.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 313 IIGYFTSWRNGTNGQPSYlvkdIPWDKVTHINYAFAHIDSDYSISIGDTSNPDNPstgmewpgvsgaetdpafnykghFN 392
Cdd:cd00598 1 VICYYDGWSSGRGPDPTD----IPLSLCTHIIYAFAEISSDGSLNLFGDKSEEPL-----------------------KG 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 393 QLAKYKKQHPDVKTLVSVGGWaetgghlneqgdrvNDGGFYTMTTNAdgsvnyAGIEAFANSVVDFIRTYGFDGVDIDYE 472
Cdd:cd00598 54 ALEELASKKPGLKVLISIGGW--------------TDSSPFTLASDP------ASRAAFANSLVSFLKTYGFDGVDIDWE 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 473 YPTSMNDAGnpldfgfanplraylMNSYVALMRVLREKLDQAGeednthYLLTIAAPSSGYLLRGMETMP-ITQYLDYVN 551
Cdd:cd00598 114 YPGAADNSD---------------RENFITLLRELRSALGAAN------YLLTIAVPASYFDLGYAYDVPaIGDYVDFVN 172
|
....*
gi 1097558039 552 IMTYD 556
Cdd:cd00598 173 VMTYD 177
|
|
| GH18_zymocin_alpha |
cd02878 |
Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle ... |
314-562 |
4.01e-25 |
|
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: 107.78 E-value: 4.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 314 IGYFTSWrNGTNGQPSYLVKDIPWDKVTHINYAFAHIDSDYSISIGDtsnpdnpstgmewpgvsgaetdpafnYKGHFNQ 393
Cdd:cd02878 3 IAYFEAY-NLDRPCLNMDVTQIDTSKYTHIHFAFANITSDFSVDVSS--------------------------VQEQFSD 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 394 LAKYKKqhpdVKTLVSVGGWAETGGHlneqgdrvndgGFYTMTTNAdgsVNYAGIEAFANSVVDFIRTYGFDGVDIDYEY 473
Cdd:cd02878 56 FKKLKG----VKKILSFGGWDFSTSP-----------STYQIFRDA---VKPANRDTFANNVVNFVNKYNLDGVDFDWEY 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 474 PTSMN----DAGNPLDfgfanplraylMNSYVALMRVLREKLDqageednTHYLLTIAAPSSGYLLRGMETMPITQYLDY 549
Cdd:cd02878 118 PGAPDipgiPAGDPDD-----------GKNYLEFLKLLKSKLP-------SGKSLSIAAPASYWYLKGFPIKDMAKYVDY 179
|
250
....*....|...
gi 1097558039 550 VNIMTYDFHGTWN 562
Cdd:cd02878 180 IVYMTYDLHGQWD 192
|
|
| GH18_plant_chitinase_class_V |
cd02879 |
The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the ... |
341-626 |
1.44e-21 |
|
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: 96.28 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 341 THINYAFAHID-SDYSISIgdtSNPDNPstgmewpgvsgaetdpafnYKGHFNQLAKYKKqhPDVKTLVSVGGwaetggh 419
Cdd:cd02879 27 THLFYAFADLDpSTYEVVI---SPSDES-------------------EFSTFTETVKRKN--PSVKTLLSIGG------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 420 lneqgDRVNDGGFYTMTTNADGSvnyagiEAFANSVVDFIRTYGFDGVDIDYEYPTSMNDagnpldfgfanplraylMNS 499
Cdd:cd02879 76 -----GGSDSSAFAAMASDPTAR------KAFINSSIKVARKYGFDGLDLDWEFPSSQVE-----------------MEN 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 500 YVALMRVLREKL-DQAGEEDNTHYLLTIAAPSSGYLLRGMETMP-----ITQYLDYVNIMTYDFHGTWNEFVGHNSA-IF 572
Cdd:cd02879 128 FGKLLEEWRAAVkDEARSSGRPPLLLTAAVYFSPILFLSDDSVSypieaINKNLDWVNVMAYDYYGSWESNTTGPAAaLY 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1097558039 573 DNGNDPelkaaniynTAQYGgigylnidwAVKYFRGSMSPGRINIGTPYYTRGW 626
Cdd:cd02879 208 DPNSNV---------STDYG---------IKSWIKAGVPAKKLVLGLPLYGRAW 243
|
|
| CBD_like |
cd12204 |
Cellulose-binding domain, chitinase and related proteins; This group contains proteins related ... |
985-1033 |
2.72e-20 |
|
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: 85.07 E-value: 2.72e-20
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1097558039 985 SVYPVYPNWPAGDHANGGDRIVHNGSVWQAKWWTNSQPGsSDGSWTLIC 1033
Cdd:cd12204 1 AGANAYPNWPQGTHAAGGDLVSYNGAVYQAKWWTQSAPG-SDSSWTLVC 48
|
|
| GH18_IDGF |
cd02873 |
The IDGF's (imaginal disc growth factors) are a family of growth factors identified in insects ... |
341-775 |
1.28e-18 |
|
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: 89.68 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 341 THINYAFAHIDSD-YSISigdtsnPDNPSTGMEwpgvsgaetdpafnyKGHFNQLAKYKKQHPDVKTLVSVGGWAETGGH 419
Cdd:cd02873 32 THLVYGYAGIDADtYKIK------SLNEDLDLD---------------KSHYRAITSLKRKYPHLKVLLSVGGDRDTDEE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 420 LNEQGdrvndggFYTMTTNADGSVnyagieAFANSVVDFIRTYGFDGVDIDYEYPTS-----MNDAGNPLD-----FGFA 489
Cdd:cd02873 91 GENEK-------YLLLLESSESRN------AFINSAHSLLKTYGFDGLDLAWQFPKNkpkkvRGTFGSAWHsfkklFTGD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 490 ---NPLRAYLMNSYVALMRVLREKLDQAGeednthYLLTIAA-P---SSGYllrgMETMPITQYLDYVNIMTYDFHG-TW 561
Cdd:cd02873 158 svvDEKAAEHKEQFTALVRELKNALRPDG------LLLTLTVlPhvnSTWY----FDVPAIANNVDFVNLATFDFLTpER 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 562 NEFVGHNSAifdngndPelkaanIYntAQYGGIGYLNIDWAVKYFRGSMSPG-RINIGTPYYTRGWQnvtsANGEWGLGG 640
Cdd:cd02873 228 NPEEADYTA-------P------IY--ELYERNPHHNVDYQVKYWLNQGTPAsKLNLGIATYGRAWK----LTKDSGITG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 641 TASLPNqsecpagTGGAAKCGygaigidniwHDSDGNG----QEIGAgtnPLWHAKNLEQGIlgsyigyYGLDTVNDPAD 716
Cdd:cd02873 289 VPPVLE-------TDGPGPAG----------PQTKTPGllswPEICS---KLPNPANLKGAD-------APLRKVGDPTK 341
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 717 RLvGTYT-RHYDSvsqaawlwNDTKKVFLSIEDEASMEAKAQYVIDQGLGGIMIWELAGD 775
Cdd:cd02873 342 RF-GSYAyRPADE--------NGEHGIWVSYEDPDTAANKAGYAKAKGLGGVALFDLSLD 392
|
|
| Big_7 |
pfam17957 |
Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in ... |
184-247 |
6.66e-15 |
|
Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in glycosyl hydrolase enzymes.
Pssm-ID: 436171 [Multi-domain] Cd Length: 67 Bit Score: 70.33 E-value: 6.66e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1097558039 184 ISLDAPANGTTFdTGASVAITATASDtDGSLLNVEFFVDGASVGVDTTPPYQFNWTA---IEGNHTI 247
Cdd:pfam17957 1 VSITSPANGATV-SGGTVTISATASD-DGGVSKVEFYVDGTLVGTDTSAPYSFTWTTtalANGTHTI 65
|
|
| Big_7 |
pfam17957 |
Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in ... |
91-166 |
9.18e-15 |
|
Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in glycosyl hydrolase enzymes.
Pssm-ID: 436171 [Multi-domain] Cd Length: 67 Bit Score: 69.94 E-value: 9.18e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1097558039 91 SITSPASGTVFNkNDSVIISVDASDNSAVVSVEFFVDGTSIGTDITPPWQISWSASgtnpvlsariTDDAGQQTVT 166
Cdd:pfam17957 2 SITSPANGATVS-GGTVTISATASDDGGVSKVEFYVDGTLVGTDTSAPYSFTWTTT----------ALANGTHTIT 66
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
57-472 |
4.04e-13 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 73.25 E-value: 4.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 57 TIGGPYAPGVGWAWPHAWTDLGKCGAAQDTPPQGSITSPASGTVFNkndSVIISVDASDNSAVVSVEFFVDGTSIGTDIT 136
Cdd:COG3469 3 SVSTAASPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGS---VVVAASGSAGSGTGTTAASSTAATSSTTSTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 137 PPWQISWSASGTNPVLSARITDDAGQQTVTPDIPITVnnpeGPQAPQISLDAPANGTTFDTGASVAITATASDTDGSLLN 216
Cdd:COG3469 80 ATATAAAAAATSTSATLVATSTASGANTGTSTVTTTS----TGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 217 VEFFVDGASVGVDTTPPYQFNWTAIegnhtihavatdndhlSTNSNSVYISVGEAHTGDhpcrPDGLYTTPGTAPNycdi 296
Cdd:COG3469 156 TETATGGTTTTSTTTTTTSASTTPS----------------ATTTATATTASGATTPSA----TTTATTTGPPTPG---- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 297 ydaagreklGPDHQrrIIGYFTSWRNGTNGQPsylVKDIP--WDKvthINYAFAhiDSDYSISIGDTSNPDNPSTGMewp 374
Cdd:COG3469 212 ---------LPKHV--LVGYWHNFDNGSGYIR---LSDVPdkYDV---INVAFA--EPTGATNGTVTFTLDPGSSSP--- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 375 gvsGAETDPAFNykghfNQLAKYKKQhpDVKTLVSVGGwAETGGHLNEQGDRVNdggfytmttnadgsvnyagieaFANS 454
Cdd:COG3469 270 ---GGYTDAQFK-----ADIAALQAQ--GKKVLLSIGG-ANGTVQLNTAAAADN----------------------FVNS 316
|
410
....*....|....*...
gi 1097558039 455 VVDFIRTYGFDGVDIDYE 472
Cdd:COG3469 317 VIALIDEYGFDGLDIDLE 334
|
|
| GH18_3CO4_chitinase |
cd06545 |
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an ... |
313-626 |
8.77e-13 |
|
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: 69.40 E-value: 8.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 313 IIGYFTSWRNGTNgqpsyLVKDIPWDKVTHINYAFAhidsdysisigdtsNPDNPSTGMEWPGVSGAETdpaFNYKGHfn 392
Cdd:cd06545 1 VVGYLPNYDDLNA-----LSPTIDFSKLTHINLAFA--------------NPDANGTLNANPVRSELNS---VVNAAH-- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 393 qlakykkqHPDVKTLVSVGGwaetgGHLNEQGDRVNDGgfytmttnadgsvnyAGIEAFANSVVDFIRTYGFDGVDIDYE 472
Cdd:cd06545 57 --------AHNVKILISLAG-----GSPPEFTAALNDP---------------AKRKALVDKIINYVVSYNLDGIDVDLE 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 473 YPTSMNDagnpldfgfanplraylmnSYVALMRVLREKLDQAGeednthyLLTIAAPSSGYllRGMETMPITQYLDYVNI 552
Cdd:cd06545 109 GPDVTFG-------------------DYLVFIRALYAALKKEG-------KLLTAAVSSWN--GGAVSDSTLAYFDFINI 160
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1097558039 553 MTYDFHGTWNEfvghnsaifDNGNDpelkaANIYNTAQyGGIGYLNIdwavkyfRGSMSPGRINIGTPYYTRGW 626
Cdd:cd06545 161 MSYDATGPWWG---------DNPGQ-----HSSYDDAV-NDLNYWNE-------RGLASKDKLVLGLPFYGYGF 212
|
|
| GH18_EndoS-like |
cd06542 |
Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of ... |
444-597 |
7.28e-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: 63.94 E-value: 7.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 444 NYAGIEAFANSVVDFIRTYGFDGVDIDYEYptsmndagnplDFGFANPLRAYLMNSYVALMRVLREKLdqageeDNTHYL 523
Cdd:cd06542 85 SDAAAKAYAKAIVDTVDKYGLDGVDFDDEY-----------SGYGKNGTSQPSNEAFVRLIKELRKYM------GPTDKL 147
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1097558039 524 LTIAAPsSGYLLRGMETMPitqylDYVNIMTYDFHGTWNEFVGHNSAIFDNGNDPE--LKAANIYNTAQYGGIGYL 597
Cdd:cd06542 148 LTIDGY-GQALSNDGEEVS-----PYVDYVIYQYYGSSSSSTQRNWNTNSPKIPPEkmVYTESFEEENGGNSGSSA 217
|
|
| CBM_5_12_2 |
pfam14600 |
Cellulose-binding domain; This C-terminal domain belongs to the CAZy family of ... |
989-1036 |
6.40e-10 |
|
Cellulose-binding domain; This C-terminal domain belongs to the CAZy family of carbohydrate-binding domains that are associated with glycosyl-hydrolases. It is suggested to bind cellulose.
Pssm-ID: 434062 Cd Length: 62 Bit Score: 55.95 E-value: 6.40e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1097558039 989 VYPNWPAGD-------HANGGDRIVHNGSVWQAKWWTNSQPGsSDGSWTLICSAN 1036
Cdd:pfam14600 9 EYPNWTAKDwaggpynHANAGDQMVYQGTLYQANWYTNSVPG-SDASWTFLGACA 62
|
|
| GH18_CFLE_spore_hydrolase |
cd02874 |
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ... |
451-561 |
1.63e-08 |
|
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: 57.27 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 451 FANSVVDFIRTYGFDGVDIDYEYptsmndagnpldfgfanpLRAYLMNSYVALMRVLREKLDQAGeedntHYLLTIAAPS 530
Cdd:cd02874 91 LINNILALAKKYGYDGVNIDFEN------------------VPPEDREAYTQFLRELSDRLHPAG-----YTLSTAVVPK 147
|
90 100 110
....*....|....*....|....*....|....*.
gi 1097558039 531 -----SGYLLRGMETMPITQYLDYVNIMTYDFHGTW 561
Cdd:cd02874 148 tsadqFGNWSGAYDYAAIGKIVDFVVLMTYDWHWRG 183
|
|
| ChiC_BD |
cd12215 |
Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of ... |
991-1031 |
1.97e-08 |
|
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: 51.03 E-value: 1.97e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1097558039 991 PNWPAGDHANGGDRIVHNGSVWQAKWWT-NSQPGSSDGSWTL 1031
Cdd:cd12215 1 PAWDASTVYTGGDQVTYNGKVYEAKWWTqGEEPGTSWGVWKL 42
|
|
| GH18_narbonin |
cd06544 |
Narbonin is a plant 2S protein from the globulin fraction of narbon bean (Vicia narbonensis L.) ... |
393-472 |
3.62e-06 |
|
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: 49.68 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 393 QLAKYKKQHPDVKTLVSVGGWAetgghlneqgdrVNDGGFYTMTTNADGSVNYAgieafANSVVDFIRTYGFDGVDIDYE 472
Cdd:cd06544 60 AVKSIKAQHPNVKVVISIGGRG------------VQNNPTPFDPSNVDSWVSNA-----VSSLTSIIQTYNLDGIDIDYE 122
|
|
| ChtBD3 |
smart00495 |
Chitin-binding domain type 3; |
990-1029 |
4.57e-06 |
|
Chitin-binding domain type 3;
Pssm-ID: 197760 [Multi-domain] Cd Length: 41 Bit Score: 44.17 E-value: 4.57e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1097558039 990 YPNWPAGDHANGGDRIVHNGSVWQAKWWT-NSQPGSSDGSW 1029
Cdd:smart00495 1 APAWQAGTVYTAGDVVSYNGKVYKAKWWTqGEEPGSSSGPW 41
|
|
| GH18_chitinase_D-like |
cd02871 |
GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes ... |
313-482 |
1.28e-05 |
|
GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes the 1,4-beta-linkages of N-acetylglucosamine in chitin and chitodextrins. The domain architecture of ChiD includes a catalytic glycosyl hydrolase family 18 (GH18) domain, a chitin-binding domain, and a fibronectin type III domain. The chitin-binding and fibronectin type III domains are located either N-terminal or C-terminal to the catalytic domain. This family includes exochitinase Chi36 from Bacillus cereus.
Pssm-ID: 119350 [Multi-domain] Cd Length: 312 Bit Score: 48.49 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 313 IIGYFTSWRNGTNGQPSYLvKDIPwDKVTHINYAFAHIDSDysisigdtsnpdnpsTGMEWPgvSGAETDPAFNYKGHFN 392
Cdd:cd02871 3 LVGYWHNWDNGAGSGRQDL-DDVP-SKYNVINVAFAEPTSD---------------GGGEVT--FNNGSSPGGYSPAEFK 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 393 QLAKYKKQHpDVKTLVSVGGwaETGGHLNeqgdrvndggfyTMTTNADgsvnyagieAFANSVVDFIRTYGFDGVDIDYE 472
Cdd:cd02871 64 ADIKALQAK-GKKVLISIGG--ANGHVDL------------NHTAQED---------NFVDSIVAIIKEYGFDGLDIDLE 119
|
170
....*....|
gi 1097558039 473 ypTSMNDAGN 482
Cdd:cd02871 120 --SGSNPLNA 127
|
|
| ChtBD3 |
smart00495 |
Chitin-binding domain type 3; |
27-69 |
2.39e-04 |
|
Chitin-binding domain type 3;
Pssm-ID: 197760 [Multi-domain] Cd Length: 41 Bit Score: 39.55 E-value: 2.39e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1097558039 27 PAYADGTSYNTGDQVQNNNTAYQCTvggWCTigGPYAPGVGWA 69
Cdd:smart00495 2 PAWQAGTVYTAGDVVSYNGKVYKAK---WWT--QGEEPGSSSG 39
|
|
| GH18_CTS3_chitinase |
cd06546 |
GH18 domain of CTS3 (chitinase 3), an uncharacterized protein from the human fungal pathogen ... |
312-478 |
4.21e-04 |
|
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: 43.09 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 312 RIIGYFTSWRNGtNGQPsYLVKDIPWDK---VTHINYAFAHIDSDYSISIGDTSnPDNPSTGMEWpgvsgAETDpAFNYK 388
Cdd:cd06546 1 RLVIYYQTTHPS-NGDP-ISSLLLVTEKgiaLTHLIVAALHINDDGNIHLNDHP-PDHPRFTTLW-----TELA-ILQSS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097558039 389 GhfnqlakykkqhpdVKTLVSVGGWAEtgghlneqgdrvndgGFYTMTTNADGSvnyagIEAFANSVVDFIRTYGFDGVD 468
Cdd:cd06546 72 G--------------VKVMGMLGGAAP---------------GSFSRLDDDDED-----FERYYGQLRDMIRRRGLDGLD 117
|
170
....*....|
gi 1097558039 469 IDYEYPTSMN 478
Cdd:cd06546 118 LDVEEPMSLD 127
|
|
| ChiA1_BD |
cd12214 |
chitin-binding domain of Chi A1-like proteins; This group contains proteins related to the ... |
28-59 |
1.65e-03 |
|
chitin-binding domain of Chi A1-like proteins; This group contains proteins related to the chitin binding domain of chitinase A1 (ChiA1) of Bacillus circulans WL-12. Glycosidase ChiA1 hydrolyzes chitin and is comprised of several domains: the C-terminal chitin binding domain, an N-terminal and catalytic domain, and 2 fibronectin type III-like domains. Chitinases function in invertebrates in the degradation of old exoskeletons, in fungi to utilize chitin in cell walls, and in bacteria which use chitin as an energy source. Bacillus circulans WL-12 ChiA1 facilitates invasion of fungal cell walls. The ChiAi chitin binding domain is required for the specific recognition of insoluble chitin. although topologically and structurally related, ChiA1 lacks the characteristic aromatic residues of Erwinia chrysanthemi endoglucanase Z (CBD(EGZ)).
Pssm-ID: 213177 [Multi-domain] Cd Length: 45 Bit Score: 37.32 E-value: 1.65e-03
10 20 30
....*....|....*....|....*....|..
gi 1097558039 28 AYADGTSYNTGDQVQNNNTAYQCTVGGWCTIG 59
Cdd:cd12214 1 EWAAGTTYKAGDIVTYNGKLYRCLQAHTSLAG 32
|
|
| ChtBD3 |
cd00036 |
Chitin/cellulose binding domains of chitinase and related enzymes; This group contains ... |
993-1031 |
6.58e-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: 35.43 E-value: 6.58e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1097558039 993 WPAGDHANGGDRIVHNGSVWQAKWWT-NSQPGSSDgSWTL 1031
Cdd:cd00036 2 WPNPTHYTAGQSVVYNGNLYTANWYTaGSVPGSDS-SWTQ 40
|
|
| |
