|
Name |
Accession |
Description |
Interval |
E-value |
| ChiA |
COG3325 |
Chitinase, GH18 family [Carbohydrate transport and metabolism]; |
55-527 |
1.59e-146 |
|
Chitinase, GH18 family [Carbohydrate transport and metabolism];
Pssm-ID: 442554 [Multi-domain] Cd Length: 391 Bit Score: 435.11 E-value: 1.59e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 55 CSVYDTQgrEKMGADHQRRVIGYFTGWRDGKNGqpaYLAKDIPWEKITHINYAFGHIGGDNKLSVGtdgpnnaatrMTW- 133
Cdd:COG3325 4 ASVSDTA--AAATATSGKRVVGYFTQWGIYGRN---YLVKDIPASKLTHINYAFANVDPDGKCSVG----------DAWa 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 134 -PGVAGAEMDPAYAYKGHFNLLNKFKKQHPNVKTLISVGGWAEtggyfadngdrvdSGGFYSMAtnadgsVNQAGIDTFA 212
Cdd:COG3325 69 kPSVDGAADDWDQPLKGNFNQLKKLKAKNPNLKVLISIGGWTW-------------SKGFSDAA------ATPASRAAFV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 213 ASSVDFIRKYGFNGVDIDYEYPTTMKDAGNPldwqlanaRRAGLVQGYAALMKSLREKLDAAGAADGKHYLLTVAAPSSG 292
Cdd:COG3325 130 DSCVDLLRKYNFDGIDIDWEYPGSGGAPGNV--------YRPEDKANFTALLKELRAQLDALGAETGKHYLLTAAAPAGP 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 293 YLLRGMETFQMQKYLDYVNIMSYDLHGAWNEYVGPNASLFDDGKDGELAAanvygsaqygnigyLNTDWAYHYF-RGSMP 371
Cdd:COG3325 202 DKLDGIELPKVAQYLDYVNVMTYDFHGAWSPTTGHQAPLYDSPKDPEAQG--------------YSVDSAVQAYlAAGVP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 372 AGRINIGLPYYTRGHKNVQGGTDGLWGKASAttcPAGAGLtkcgdgatgidnlwhdkdtngvesPAGSNPMWHaknlekg 451
Cdd:COG3325 268 ASKLVLGVPFYGRGWTGVTGGNNGLYQPATG---PAPGTW------------------------EAGVNDYKD------- 313
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1899249394 452 IVGDYVTQygfpanttltGTYARKYDSTLVAPWLWNAQKKVFLSTEDEQSVAAKADYVVNKGIGGTMVWEMAGDYA 527
Cdd:COG3325 314 LKALYLGS----------NGYTRYWDDVAKAPYLYNGDTGTFISYDDPRSIAAKADYVKDKGLGGVMFWELSGDTA 379
|
|
| GH18_chitinase |
cd06548 |
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ... |
74-525 |
7.74e-102 |
|
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: 317.26 E-value: 7.74e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 74 VIGYFTGWRDGKNGQPAYlaKDIPWEKITHINYAFGHIGGDNKLSVGTDGPNNAAtrmtWPGVAGAEMDPAYAYKGHFNL 153
Cdd:cd06548 1 VVGYFTNWGIYGRNYFVT--DDIPADKLTHINYAFADIDGDGGVVTSDDEAADEA----AQSVDGGADTDDQPLKGNFGQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 154 LNKFKKQHPNVKTLISVGGWAEtggyfadngdrvdSGGFYSMATNadgsvnQAGIDTFAASSVDFIRKYGFNGVDIDYEY 233
Cdd:cd06548 75 LRKLKQKNPHLKILLSIGGWTW-------------SGGFSDAAAT------EASRAKFADSAVDFIRKYGFDGIDIDWEY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 234 PTTMKDAGNPldwqlanaRRAGLVQGYAALMKSLREKLDAAGAADGKHYLLTVAAPSSGYLLRGMETFQMQKYLDYVNIM 313
Cdd:cd06548 136 PGSGGAPGNV--------ARPEDKENFTLLLKELREALDALGAETGRKYLLTIAAPAGPDKLDKLEVAEIAKYLDFINLM 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 314 SYDLHGAWNEYVGPNASLFDDGKDgelaaanvygsaqyGNIGYLNTDWAYHYFRGSMPAGRINIGLPYYTRGHKNvqggt 393
Cdd:cd06548 208 TYDFHGAWSNTTGHHSNLYASPAD--------------PPGGYSVDAAVNYYLSAGVPPEKLVLGVPFYGRGWTG----- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 394 dglwgkasattcpagagltkcgdgatgidnlwhdkdtngvespagsnpmwhaknlekgivgdyvtqygfpanttltgtYA 473
Cdd:cd06548 269 ------------------------------------------------------------------------------YT 270
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1899249394 474 RKYDSTLVAPWLWNAQKKVFLSTEDEQSVAAKADYVVNKGIGGTMVWEMAGD 525
Cdd:cd06548 271 RYWDEVAKAPYLYNPSTKTFISYDDPRSIKAKADYVKDKGLGGVMFWELSGD 322
|
|
| ChiC |
pfam06483 |
Chitinase C; This ~170 aa region is found at the C-terminus of pfam00704. |
534-706 |
3.62e-99 |
|
Chitinase C; This ~170 aa region is found at the C-terminus of pfam00704.
Pssm-ID: 368936 Cd Length: 174 Bit Score: 304.24 E-value: 3.62e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 534 QYEMGSTLTSLMYDKFKAATPYGAKKSNATLPTQAVKIDAQFTEFKLGDSNYPITPKIKITNNTAATLPGGTEFQFDYGT 613
Cdd:pfam06483 1 EYFMGDTLTTLLYDKFKAAAPYGATKANAAMPTQVLDVSVSLTGFPLGDSNYPINPKLRITNNSGQTIPGGTEFEFDYPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 614 SAPANASDQSGFGTKVISSDHTGSNVGGLKGDFHRVSLKLPAWQSLAPGATVDLAFNYYLPVSTPSNWTVNINGTTYALA 693
Cdd:pfam06483 81 SAPDNAKDQSGFGLTVISSGHTGPNVGGLKGDFHRVAFTLPSWQTLAPGASVEVDLVYYLPVSGPSNWTVTFGGTTYALK 160
|
170
....*....|...
gi 1899249394 694 GDLARGTTVVEPG 706
Cdd:pfam06483 161 GDYPRGTTTLPTA 173
|
|
| Glyco_18 |
smart00636 |
Glyco_18 domain; |
73-525 |
1.14e-95 |
|
Glyco_18 domain;
Pssm-ID: 214753 [Multi-domain] Cd Length: 334 Bit Score: 301.52 E-value: 1.14e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 73 RVIGYFTGWRdgkNGQPAYLAKDIPWEKITHINYAFGHIGGDNKLsvgtdgpnnaatrmtwpgvagaEMDPAYAYKGHFN 152
Cdd:smart00636 1 RVVGYFTNWG---VYGRNFPVDDIPASKLTHIIYAFANIDPDGTV----------------------TIGDEWADIGNFG 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 153 LLNKFKKQHPNVKTLISVGGWAEtggyfadngdrvdSGGFYSMATNadgsvnQAGIDTFAASSVDFIRKYGFNGVDIDYE 232
Cdd:smart00636 56 QLKALKKKNPGLKVLLSIGGWTE-------------SDNFSSMLSD------PASRKKFIDSIVSFLKKYGFDGIDIDWE 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 233 YPTTMKDAGNpldwqlanarraglvqGYAALMKSLREKLDAAGAAdGKHYLLTVAAPSSG-YLLRGMETF-QMQKYLDYV 310
Cdd:smart00636 117 YPGGRGDDRE----------------NYTALLKELREALDKEGAE-GKGYLLTIAVPAGPdKIDKGYGDLpAIAKYLDFI 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 311 NIMSYDLHGAWNEYVGPNASLFDDGKDGElaaanvygsaqygnigYLNTDWAYHYFRG-SMPAGRINIGLPYYTRGHKNV 389
Cdd:smart00636 180 NLMTYDFHGAWSNPTGHNAPLYAGPGDPE----------------KYNVDYAVKYYLCkGVPPSKLVLGIPFYGRGWTLV 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 390 QGGTDGlwgkasattcpagagltkcgdgatgIDNLWHDKDTNGVESPAGSNPMWHAKNLEKGivgdyvtqygfpanttlt 469
Cdd:smart00636 244 DGSNNG-------------------------PGAPFTGPATGGPGTWEGGVVDYREICKLLG------------------ 280
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1899249394 470 gtYARKYDSTLVAPWLWNAQKKVFLSTEDEQSVAAKADYVVNKGIGGTMVWEMAGD 525
Cdd:smart00636 281 --ATVVYDDTAKAPYAYNPGTGQWVSYDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
|
|
| Glyco_hydro_18 |
pfam00704 |
Glycosyl hydrolases family 18; |
73-525 |
2.59e-71 |
|
Glycosyl hydrolases family 18;
Pssm-ID: 425828 [Multi-domain] Cd Length: 311 Bit Score: 236.20 E-value: 2.59e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 73 RVIGYFTGWRDGKNGQPaylakdIPWEKITHINYAFGHI-GGDNKLSVGtdgpnnaatrmtwpgvagaemDPAYaykGHF 151
Cdd:pfam00704 1 RIVGYYTSWGVYRNGNF------LPSDKLTHIIYAFANIdGSDGTLFIG---------------------DWDL---GNF 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 152 NLLNKFKKQ-HPNVKTLISVGGWAetggyfadngdrvDSGGFYSMATNAdgsvnqAGIDTFAASSVDFIRKYGFNGVDID 230
Cdd:pfam00704 51 EQLKKLKKQkNPGVKVLLSIGGWT-------------DSTGFSLMASNP------ASRKKFADSIVSFLRKYGFDGIDID 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 231 YEYPTtmkdaGNPLDWQlanarraglvqGYAALMKSLREKLDAAGaaDGKHYLLTVAAPSSG-YLLRGMETFQMQKYLDY 309
Cdd:pfam00704 112 WEYPG-----GNPEDKE-----------NYDLLLRELRAALDEAK--GGKKYLLSAAVPASYpDLDKGYDLPKIAKYLDF 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 310 VNIMSYDLHGAWNEYVGPNASLFDDgkdgelaaanvygsaqygniGYLNTDWAYHYF-RGSMPAGRINIGLPYYTRGHKN 388
Cdd:pfam00704 174 INVMTYDFHGSWDNVTGHHAPLYGG--------------------GSYNVDYAVKYYlKQGVPASKLVLGVPFYGRSWTL 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 389 VQGGTDglwgkasattcpagagltkcgdgatgidnlwhdkdtngvespAGSNPMWHAKNLEKGIVGDyvtqygfpanttl 468
Cdd:pfam00704 234 VNGSGN------------------------------------------TWEDGVLAYKEICNLLKDN------------- 258
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1899249394 469 tgTYARKYDSTLVAPWLWNAqkKVFLSTEDEQSVAAKADYVVNKGIGGTMVWEMAGD 525
Cdd:pfam00704 259 --GATVVWDDVAKAPYVYDG--DQFITYDDPRSIATKVDYVKAKGLGGVMIWSLDAD 311
|
|
| ChiC_BD |
cd12215 |
Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of ... |
746-789 |
3.52e-15 |
|
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: 69.91 E-value: 3.52e-15
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1899249394 746 PAYVAGTVYNAGNEVSHNGRKYKAQWWTQNETPGTTgeWGVWKD 789
Cdd:cd12215 1 PAWDASTVYTGGDQVTYNGKVYEAKWWTQGEEPGTS--WGVWKL 42
|
|
| ChtBD3 |
smart00495 |
Chitin-binding domain type 3; |
745-787 |
2.27e-11 |
|
Chitin-binding domain type 3;
Pssm-ID: 197760 [Multi-domain] Cd Length: 41 Bit Score: 59.20 E-value: 2.27e-11
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1899249394 745 VPAYVAGTVYNAGNEVSHNGRKYKAQWWTQNETPGTTgeWGVW 787
Cdd:smart00495 1 APAWQAGTVYTAGDVVSYNGKVYKAKWWTQGEEPGSS--SGPW 41
|
|
| CBM_5_12 |
pfam02839 |
Carbohydrate binding domain; This short domain is found in many different glycosyl hydrolase ... |
762-787 |
2.26e-04 |
|
Carbohydrate binding domain; This short domain is found in many different glycosyl hydrolase enzymes and is presumed to have a carbohydrate binding function. The domain has six aromatic groups that may be important for binding.
Pssm-ID: 427014 Cd Length: 25 Bit Score: 38.74 E-value: 2.26e-04
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ChiA |
COG3325 |
Chitinase, GH18 family [Carbohydrate transport and metabolism]; |
55-527 |
1.59e-146 |
|
Chitinase, GH18 family [Carbohydrate transport and metabolism];
Pssm-ID: 442554 [Multi-domain] Cd Length: 391 Bit Score: 435.11 E-value: 1.59e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 55 CSVYDTQgrEKMGADHQRRVIGYFTGWRDGKNGqpaYLAKDIPWEKITHINYAFGHIGGDNKLSVGtdgpnnaatrMTW- 133
Cdd:COG3325 4 ASVSDTA--AAATATSGKRVVGYFTQWGIYGRN---YLVKDIPASKLTHINYAFANVDPDGKCSVG----------DAWa 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 134 -PGVAGAEMDPAYAYKGHFNLLNKFKKQHPNVKTLISVGGWAEtggyfadngdrvdSGGFYSMAtnadgsVNQAGIDTFA 212
Cdd:COG3325 69 kPSVDGAADDWDQPLKGNFNQLKKLKAKNPNLKVLISIGGWTW-------------SKGFSDAA------ATPASRAAFV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 213 ASSVDFIRKYGFNGVDIDYEYPTTMKDAGNPldwqlanaRRAGLVQGYAALMKSLREKLDAAGAADGKHYLLTVAAPSSG 292
Cdd:COG3325 130 DSCVDLLRKYNFDGIDIDWEYPGSGGAPGNV--------YRPEDKANFTALLKELRAQLDALGAETGKHYLLTAAAPAGP 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 293 YLLRGMETFQMQKYLDYVNIMSYDLHGAWNEYVGPNASLFDDGKDGELAAanvygsaqygnigyLNTDWAYHYF-RGSMP 371
Cdd:COG3325 202 DKLDGIELPKVAQYLDYVNVMTYDFHGAWSPTTGHQAPLYDSPKDPEAQG--------------YSVDSAVQAYlAAGVP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 372 AGRINIGLPYYTRGHKNVQGGTDGLWGKASAttcPAGAGLtkcgdgatgidnlwhdkdtngvesPAGSNPMWHaknlekg 451
Cdd:COG3325 268 ASKLVLGVPFYGRGWTGVTGGNNGLYQPATG---PAPGTW------------------------EAGVNDYKD------- 313
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1899249394 452 IVGDYVTQygfpanttltGTYARKYDSTLVAPWLWNAQKKVFLSTEDEQSVAAKADYVVNKGIGGTMVWEMAGDYA 527
Cdd:COG3325 314 LKALYLGS----------NGYTRYWDDVAKAPYLYNGDTGTFISYDDPRSIAAKADYVKDKGLGGVMFWELSGDTA 379
|
|
| GH18_chitinase |
cd06548 |
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ... |
74-525 |
7.74e-102 |
|
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: 317.26 E-value: 7.74e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 74 VIGYFTGWRDGKNGQPAYlaKDIPWEKITHINYAFGHIGGDNKLSVGTDGPNNAAtrmtWPGVAGAEMDPAYAYKGHFNL 153
Cdd:cd06548 1 VVGYFTNWGIYGRNYFVT--DDIPADKLTHINYAFADIDGDGGVVTSDDEAADEA----AQSVDGGADTDDQPLKGNFGQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 154 LNKFKKQHPNVKTLISVGGWAEtggyfadngdrvdSGGFYSMATNadgsvnQAGIDTFAASSVDFIRKYGFNGVDIDYEY 233
Cdd:cd06548 75 LRKLKQKNPHLKILLSIGGWTW-------------SGGFSDAAAT------EASRAKFADSAVDFIRKYGFDGIDIDWEY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 234 PTTMKDAGNPldwqlanaRRAGLVQGYAALMKSLREKLDAAGAADGKHYLLTVAAPSSGYLLRGMETFQMQKYLDYVNIM 313
Cdd:cd06548 136 PGSGGAPGNV--------ARPEDKENFTLLLKELREALDALGAETGRKYLLTIAAPAGPDKLDKLEVAEIAKYLDFINLM 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 314 SYDLHGAWNEYVGPNASLFDDGKDgelaaanvygsaqyGNIGYLNTDWAYHYFRGSMPAGRINIGLPYYTRGHKNvqggt 393
Cdd:cd06548 208 TYDFHGAWSNTTGHHSNLYASPAD--------------PPGGYSVDAAVNYYLSAGVPPEKLVLGVPFYGRGWTG----- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 394 dglwgkasattcpagagltkcgdgatgidnlwhdkdtngvespagsnpmwhaknlekgivgdyvtqygfpanttltgtYA 473
Cdd:cd06548 269 ------------------------------------------------------------------------------YT 270
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1899249394 474 RKYDSTLVAPWLWNAQKKVFLSTEDEQSVAAKADYVVNKGIGGTMVWEMAGD 525
Cdd:cd06548 271 RYWDEVAKAPYLYNPSTKTFISYDDPRSIKAKADYVKDKGLGGVMFWELSGD 322
|
|
| ChiC |
pfam06483 |
Chitinase C; This ~170 aa region is found at the C-terminus of pfam00704. |
534-706 |
3.62e-99 |
|
Chitinase C; This ~170 aa region is found at the C-terminus of pfam00704.
Pssm-ID: 368936 Cd Length: 174 Bit Score: 304.24 E-value: 3.62e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 534 QYEMGSTLTSLMYDKFKAATPYGAKKSNATLPTQAVKIDAQFTEFKLGDSNYPITPKIKITNNTAATLPGGTEFQFDYGT 613
Cdd:pfam06483 1 EYFMGDTLTTLLYDKFKAAAPYGATKANAAMPTQVLDVSVSLTGFPLGDSNYPINPKLRITNNSGQTIPGGTEFEFDYPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 614 SAPANASDQSGFGTKVISSDHTGSNVGGLKGDFHRVSLKLPAWQSLAPGATVDLAFNYYLPVSTPSNWTVNINGTTYALA 693
Cdd:pfam06483 81 SAPDNAKDQSGFGLTVISSGHTGPNVGGLKGDFHRVAFTLPSWQTLAPGASVEVDLVYYLPVSGPSNWTVTFGGTTYALK 160
|
170
....*....|...
gi 1899249394 694 GDLARGTTVVEPG 706
Cdd:pfam06483 161 GDYPRGTTTLPTA 173
|
|
| Glyco_18 |
smart00636 |
Glyco_18 domain; |
73-525 |
1.14e-95 |
|
Glyco_18 domain;
Pssm-ID: 214753 [Multi-domain] Cd Length: 334 Bit Score: 301.52 E-value: 1.14e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 73 RVIGYFTGWRdgkNGQPAYLAKDIPWEKITHINYAFGHIGGDNKLsvgtdgpnnaatrmtwpgvagaEMDPAYAYKGHFN 152
Cdd:smart00636 1 RVVGYFTNWG---VYGRNFPVDDIPASKLTHIIYAFANIDPDGTV----------------------TIGDEWADIGNFG 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 153 LLNKFKKQHPNVKTLISVGGWAEtggyfadngdrvdSGGFYSMATNadgsvnQAGIDTFAASSVDFIRKYGFNGVDIDYE 232
Cdd:smart00636 56 QLKALKKKNPGLKVLLSIGGWTE-------------SDNFSSMLSD------PASRKKFIDSIVSFLKKYGFDGIDIDWE 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 233 YPTTMKDAGNpldwqlanarraglvqGYAALMKSLREKLDAAGAAdGKHYLLTVAAPSSG-YLLRGMETF-QMQKYLDYV 310
Cdd:smart00636 117 YPGGRGDDRE----------------NYTALLKELREALDKEGAE-GKGYLLTIAVPAGPdKIDKGYGDLpAIAKYLDFI 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 311 NIMSYDLHGAWNEYVGPNASLFDDGKDGElaaanvygsaqygnigYLNTDWAYHYFRG-SMPAGRINIGLPYYTRGHKNV 389
Cdd:smart00636 180 NLMTYDFHGAWSNPTGHNAPLYAGPGDPE----------------KYNVDYAVKYYLCkGVPPSKLVLGIPFYGRGWTLV 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 390 QGGTDGlwgkasattcpagagltkcgdgatgIDNLWHDKDTNGVESPAGSNPMWHAKNLEKGivgdyvtqygfpanttlt 469
Cdd:smart00636 244 DGSNNG-------------------------PGAPFTGPATGGPGTWEGGVVDYREICKLLG------------------ 280
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1899249394 470 gtYARKYDSTLVAPWLWNAQKKVFLSTEDEQSVAAKADYVVNKGIGGTMVWEMAGD 525
Cdd:smart00636 281 --ATVVYDDTAKAPYAYNPGTGQWVSYDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
|
|
| Glyco_hydro_18 |
pfam00704 |
Glycosyl hydrolases family 18; |
73-525 |
2.59e-71 |
|
Glycosyl hydrolases family 18;
Pssm-ID: 425828 [Multi-domain] Cd Length: 311 Bit Score: 236.20 E-value: 2.59e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 73 RVIGYFTGWRDGKNGQPaylakdIPWEKITHINYAFGHI-GGDNKLSVGtdgpnnaatrmtwpgvagaemDPAYaykGHF 151
Cdd:pfam00704 1 RIVGYYTSWGVYRNGNF------LPSDKLTHIIYAFANIdGSDGTLFIG---------------------DWDL---GNF 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 152 NLLNKFKKQ-HPNVKTLISVGGWAetggyfadngdrvDSGGFYSMATNAdgsvnqAGIDTFAASSVDFIRKYGFNGVDID 230
Cdd:pfam00704 51 EQLKKLKKQkNPGVKVLLSIGGWT-------------DSTGFSLMASNP------ASRKKFADSIVSFLRKYGFDGIDID 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 231 YEYPTtmkdaGNPLDWQlanarraglvqGYAALMKSLREKLDAAGaaDGKHYLLTVAAPSSG-YLLRGMETFQMQKYLDY 309
Cdd:pfam00704 112 WEYPG-----GNPEDKE-----------NYDLLLRELRAALDEAK--GGKKYLLSAAVPASYpDLDKGYDLPKIAKYLDF 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 310 VNIMSYDLHGAWNEYVGPNASLFDDgkdgelaaanvygsaqygniGYLNTDWAYHYF-RGSMPAGRINIGLPYYTRGHKN 388
Cdd:pfam00704 174 INVMTYDFHGSWDNVTGHHAPLYGG--------------------GSYNVDYAVKYYlKQGVPASKLVLGVPFYGRSWTL 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 389 VQGGTDglwgkasattcpagagltkcgdgatgidnlwhdkdtngvespAGSNPMWHAKNLEKGIVGDyvtqygfpanttl 468
Cdd:pfam00704 234 VNGSGN------------------------------------------TWEDGVLAYKEICNLLKDN------------- 258
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1899249394 469 tgTYARKYDSTLVAPWLWNAqkKVFLSTEDEQSVAAKADYVVNKGIGGTMVWEMAGD 525
Cdd:pfam00704 259 --GATVVWDDVAKAPYVYDG--DQFITYDDPRSIATKVDYVKAKGLGGVMIWSLDAD 311
|
|
| GH18_chitolectin_chitotriosidase |
cd02872 |
This conserved domain family includes a large number of catalytically inactive chitinase-like ... |
74-520 |
4.59e-46 |
|
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: 168.51 E-value: 4.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 74 VIGYFTGW---RDGkNGQpaYLAKDIPWEKITHINYAFGHIGGDNKLSVgtdgpnnaatrmtwpgvagaeMDPAYAY-KG 149
Cdd:cd02872 1 VVCYFTNWaqyRPG-NGK--FVPENIDPFLCTHIIYAFAGLNPDGNIII---------------------LDEWNDIdLG 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 150 HFNLLNKFKKQHPNVKTLISVGGWAETggyfadngdrvdSGGFYSMATNAdgsVNQAgidTFAASSVDFIRKYGFNGVDI 229
Cdd:cd02872 57 LYERFNALKEKNPNLKTLLAIGGWNFG------------SAKFSAMAASP---ENRK---TFIKSAIAFLRKYGFDGLDL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 230 DYEYPTTmkdagnpldWQLANARRaglvQGYAALMKSLREKLDAagaaDGKHYLLTVAAPSS------GYLLRgmetfQM 303
Cdd:cd02872 119 DWEYPGQ---------RGGPPEDK----ENFVTLLKELREAFEP----EAPRLLLTAAVSAGketidaAYDIP-----EI 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 304 QKYLDYVNIMSYDLHGAWNEYVGPNASLFddgkdgelaaanvYGSAQYGNIGYLNTDWAYHYFRGS-MPAGRINIGLPYY 382
Cdd:cd02872 177 SKYLDFINVMTYDFHGSWEGVTGHNSPLY-------------AGSADTGDQKYLNVDYAIKYWLSKgAPPEKLVLGIPTY 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 383 TRGhknvqggtdglWGKASATTcpagaglTKCGDGATGidnlwhdkdtngvespagsnpmwhaknleKGIVGDYVTQYGF 462
Cdd:cd02872 244 GRS-----------FTLASPSN-------TGVGAPASG-----------------------------PGTAGPYTREAGF 276
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1899249394 463 PAN----TTLTGTYARKYDSTLVAPWLWnaQKKVFLSTEDEQSVAAKADYVVNKGIGGTMVW 520
Cdd:cd02872 277 LAYyeicEFLKSGWTVVWDDEQKVPYAY--KGNQWVGYDDEESIALKVQYLKSKGLGGAMVW 336
|
|
| GH18_chitinase-like |
cd00598 |
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ... |
74-317 |
4.04e-33 |
|
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: 127.11 E-value: 4.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 74 VIGYFTGWRDGkngqPAYLAKDIPWEKITHINYAFGHIGGDNKLSVGTDGPnnaatrmtwpgvagaemdpayaYKGHFNL 153
Cdd:cd00598 1 VICYYDGWSSG----RGPDPTDIPLSLCTHIIYAFAEISSDGSLNLFGDKS----------------------EEPLKGA 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 154 LNKFKKQHPNVKTLISVGGWAetggyfadngdrvDSGGFYSMATNADgsvnqagIDTFAASSVDFIRKYGFNGVDIDYEY 233
Cdd:cd00598 55 LEELASKKPGLKVLISIGGWT-------------DSSPFTLASDPAS-------RAAFANSLVSFLKTYGFDGVDIDWEY 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 234 PttmkdagnpldwqlaNARRAGLVQGYAALMKSLREKLDAAGaadgkhYLLTVAAPSSGYLLRGMETF-QMQKYLDYVNI 312
Cdd:cd00598 115 P---------------GAADNSDRENFITLLRELRSALGAAN------YLLTIAVPASYFDLGYAYDVpAIGDYVDFVNV 173
|
....*
gi 1899249394 313 MSYDL 317
Cdd:cd00598 174 MTYDL 178
|
|
| GH18_zymocin_alpha |
cd02878 |
Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle ... |
75-322 |
1.81e-24 |
|
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: 105.47 E-value: 1.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 75 IGYFTGWrdgkNGQPAYLAKD---IPWEKITHINYAFGHIGGDNKLSVGtdgpnnaatrmtwpgvagaemdpayAYKGHF 151
Cdd:cd02878 3 IAYFEAY----NLDRPCLNMDvtqIDTSKYTHIHFAFANITSDFSVDVS-------------------------SVQEQF 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 152 nllNKFKKQHpNVKTLISVGGWaetggyfadngdrvdsggfySMATNAD------GSVNQAGIDTFAASSVDFIRKYGFN 225
Cdd:cd02878 54 ---SDFKKLK-GVKKILSFGGW--------------------DFSTSPStyqifrDAVKPANRDTFANNVVNFVNKYNLD 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 226 GVDIDYEYPTTmKD-----AGNPLDwqlanarraglVQGYAALMKSLREKLdaagaadGKHYLLTVAAPSSGYLLRGMET 300
Cdd:cd02878 110 GVDFDWEYPGA-PDipgipAGDPDD-----------GKNYLEFLKLLKSKL-------PSGKSLSIAAPASYWYLKGFPI 170
|
250 260
....*....|....*....|..
gi 1899249394 301 FQMQKYLDYVNIMSYDLHGAWN 322
Cdd:cd02878 171 KDMAKYVDYIVYMTYDLHGQWD 192
|
|
| GH18_plant_chitinase_class_V |
cd02879 |
The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the ... |
95-384 |
8.99e-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: 93.58 E-value: 8.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 95 DIPWEKITHINYAFGhiggdnklsvgtdGPNNAATRMTWPGVAGAEMdpayaykGHFNllNKFKKQHPNVKTLISVGGwa 174
Cdd:cd02879 20 NIDSSLFTHLFYAFA-------------DLDPSTYEVVISPSDESEF-------STFT--ETVKRKNPSVKTLLSIGG-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 175 etggyfadngDRVDSGGFYSMATNADGSvnqagiDTFAASSVDFIRKYGFNGVDIDYEYPTTMKDAGNpldwqlanarra 254
Cdd:cd02879 76 ----------GGSDSSAFAAMASDPTAR------KAFINSSIKVARKYGFDGLDLDWEFPSSQVEMEN------------ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 255 glvqgYAALMKSLREKLDAAGAADGKH-YLLTVAAPSSGYLLRGMETFQ-----MQKYLDYVNIMSYDLHGAWNEYVGPN 328
Cdd:cd02879 128 -----FGKLLEEWRAAVKDEARSSGRPpLLLTAAVYFSPILFLSDDSVSypieaINKNLDWVNVMAYDYYGSWESNTTGP 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1899249394 329 ASLFDDGKDGElaaanvygSAQYGnigylNTDWayhyFRGSMPAGRINIGLPYYTR 384
Cdd:cd02879 203 AAALYDPNSNV--------STDYG-----IKSW----IKAGVPAKKLVLGLPLYGR 241
|
|
| ChiC_BD |
cd12215 |
Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of ... |
746-789 |
3.52e-15 |
|
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: 69.91 E-value: 3.52e-15
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1899249394 746 PAYVAGTVYNAGNEVSHNGRKYKAQWWTQNETPGTTgeWGVWKD 789
Cdd:cd12215 1 PAWDASTVYTGGDQVTYNGKVYEAKWWTQGEEPGTS--WGVWKL 42
|
|
| ChtBD3 |
smart00495 |
Chitin-binding domain type 3; |
745-787 |
2.27e-11 |
|
Chitin-binding domain type 3;
Pssm-ID: 197760 [Multi-domain] Cd Length: 41 Bit Score: 59.20 E-value: 2.27e-11
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1899249394 745 VPAYVAGTVYNAGNEVSHNGRKYKAQWWTQNETPGTTgeWGVW 787
Cdd:smart00495 1 APAWQAGTVYTAGDVVSYNGKVYKAKWWTQGEEPGSS--SGPW 41
|
|
| GH18_IDGF |
cd02873 |
The IDGF's (imaginal disc growth factors) are a family of growth factors identified in insects ... |
147-516 |
5.26e-11 |
|
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: 65.41 E-value: 5.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 147 YKGHFNLLNKFKKQHPNVKTLISVGGwaetggyFADNGDRVDSGGFYSMATNADGSVnqagidTFAASSVDFIRKYGFNG 226
Cdd:cd02873 58 DKSHYRAITSLKRKYPHLKVLLSVGG-------DRDTDEEGENEKYLLLLESSESRN------AFINSAHSLLKTYGFDG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 227 VDIDYEYPTT--MKDAGN-PLDWQ-LANARRAGLV---------QGYAALMKSLREKLDAAGaadgkhYLLTVAA-P--- 289
Cdd:cd02873 125 LDLAWQFPKNkpKKVRGTfGSAWHsFKKLFTGDSVvdekaaehkEQFTALVRELKNALRPDG------LLLTLTVlPhvn 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 290 SSGYllrgMETFQMQKYLDYVNIMSYDlhgawneYVGPNaslfddgKDGELA--AANVYgsAQYGNIGYLNTDWAYHYF- 366
Cdd:cd02873 199 STWY----FDVPAIANNVDFVNLATFD-------FLTPE-------RNPEEAdyTAPIY--ELYERNPHHNVDYQVKYWl 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 367 RGSMPAGRINIGLPYYTRGHKnvqggtdgLWGKASATTCPagAGLTKCGDGATGI--------------DNLWHDKDTNG 432
Cdd:cd02873 259 NQGTPASKLNLGIATYGRAWK--------LTKDSGITGVP--PVLETDGPGPAGPqtktpgllswpeicSKLPNPANLKG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 433 VESPagsnpmwhaknLEKgiVGDyvtqygfPanTTLTGTYA-RKYDStlvapwlwNAQKKVFLSTEDEQSVAAKADYVVN 511
Cdd:cd02873 329 ADAP-----------LRK--VGD-------P--TKRFGSYAyRPADE--------NGEHGIWVSYEDPDTAANKAGYAKA 378
|
....*
gi 1899249394 512 KGIGG 516
Cdd:cd02873 379 KGLGG 383
|
|
| GH18_3CO4_chitinase |
cd06545 |
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an ... |
74-382 |
1.54e-10 |
|
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: 62.47 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 74 VIGYFTGWRDgkngQPAYLAKdIPWEKITHINYAFGHIGGDNKLSVGTDGPNNAATRmtwpgvagaemdpayaykghfnl 153
Cdd:cd06545 1 VVGYLPNYDD----LNALSPT-IDFSKLTHINLAFANPDANGTLNANPVRSELNSVV----------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 154 lNKFKKQhpNVKTLISVGGwaetggyfadnGDRVDSGGFYSMATNADGSVNQAgidtfaassVDFIRKYGFNGVDIDYEY 233
Cdd:cd06545 53 -NAAHAH--NVKILISLAG-----------GSPPEFTAALNDPAKRKALVDKI---------INYVVSYNLDGIDVDLEG 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 234 PTTMkdagnpldwqlanarraglVQGYAALMKSLREKLDAAGaadgkhyLLTVAAPSSGYllRGMETFQMQKYLDYVNIM 313
Cdd:cd06545 110 PDVT-------------------FGDYLVFIRALYAALKKEG-------KLLTAAVSSWN--GGAVSDSTLAYFDFINIM 161
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1899249394 314 SYDLHGAWNEyvgpnaslfddGKDGELAAanvYGSAQygnigylnTDWAYHYFRGSMPAGRINIGLPYY 382
Cdd:cd06545 162 SYDATGPWWG-----------DNPGQHSS---YDDAV--------NDLNYWNERGLASKDKLVLGLPFY 208
|
|
| ChtBD3 |
cd00036 |
Chitin/cellulose binding domains of chitinase and related enzymes; This group contains ... |
747-784 |
4.89e-07 |
|
Chitin/cellulose binding domains of chitinase and related enzymes; This group contains proteins related to the cellulose-binding domain of Erwinia chrysanthemi endoglucanase Z (EGZ) and Serratia marcescens chitinase B (ChiB). Gram negative plant parasite Erwinia chrysanthemi produces a variety of depolymerizing enzymes to metabolize pectin and cellulose on the host plant. Cellulase EGZ has a modular structure, with an N-terminal catalytic domain linked to a C-terminal cellulose-binding domain (CBD). CBD mediates the secretion activity of EGZ. Chitinases allow certain bacteria to utilize chitin as a energy source. Typically, non-plant chitinases are of the glycosidase family 18. Bacillus circulans Glycosidase ChiA1 hydrolyzes chitin and is comprised of several domains: the C-terminal chitin binding domain, an N-terminal catalytic domain, and 2 fibronectin type III-like domains. Bacillus circulans WL-12 ChiA1 facilitates invasion of fungal cell walls. The ChiA1 chitin binding domain is required for the specific recognition of insoluble chitin. although topologically and structurally related, ChiA1 lacks the characteristic aromatic residues of Erwinia chrysanthemi endoglucanase Z (CBD(EGZ)). Streptomyces griseus Chitinase C is a family 19 chitinase, and consists of a N-terminal chitin binding domain and a C-terminal chitin-catalytic domain that effects degradation. ChiC contains the characteristic chitin-binding aromatic residues. Chitinases function in invertebrates in the degradation of old exoskeletons, in fungi to utilize chitin in cell walls, and in bacteria which use chitin as an energy source.
Pssm-ID: 213175 Cd Length: 40 Bit Score: 46.60 E-value: 4.89e-07
10 20 30
....*....|....*....|....*....|....*...
gi 1899249394 747 AYVAGTVYNAGNEVSHNGRKYKAQWWTQNETPGTTGEW 784
Cdd:cd00036 1 AWPNPTHYTAGQSVVYNGNLYTANWYTAGSVPGSDSSW 38
|
|
| CBD_like |
cd12204 |
Cellulose-binding domain, chitinase and related proteins; This group contains proteins related ... |
746-784 |
6.22e-07 |
|
Cellulose-binding domain, chitinase and related proteins; This group contains proteins related to the cellulose-binding domain of Erwinia chrysanthemi endoglucanase Z (EGZ) and Serratia marcescens chitinase B (ChiB). Gram negative plant parasite Erwinia chrysanthemi produces a variety of depolymerizing enzymes to metabolize pectin and cellulose on the host plant. Cellulase EGZ has a modular structure, with N-terminal catalytic domain linked to a C-terminal cellulose-binding domain (CBD). CBD mediates the secretion activity of EGZ. Chitinases allow certain bacteria to utilize chitin as a energy source. Typically, non-plant chitinases are of the glycosidase family 18.
Pssm-ID: 213176 Cd Length: 48 Bit Score: 46.55 E-value: 6.22e-07
10 20 30
....*....|....*....|....*....|....*....
gi 1899249394 746 PAYVAGTVYNAGNEVSHNGRKYKAQWWTQNEtPGTTGEW 784
Cdd:cd12204 7 PNWPQGTHAAGGDLVSYNGAVYQAKWWTQSA-PGSDSSW 44
|
|
| GH18_narbonin |
cd06544 |
Narbonin is a plant 2S protein from the globulin fraction of narbon bean (Vicia narbonensis L.) ... |
156-232 |
1.02e-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: 50.83 E-value: 1.02e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1899249394 156 KFKKQHPNVKTLISVGGWaetggyfadngdrvdsgGFYSMATNADGSVNQAGIDTFAASSVDFIRKYGFNGVDIDYE 232
Cdd:cd06544 63 SIKAQHPNVKVVISIGGR-----------------GVQNNPTPFDPSNVDSWVSNAVSSLTSIIQTYNLDGIDIDYE 122
|
|
| GH18_CFLE_spore_hydrolase |
cd02874 |
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ... |
209-520 |
2.03e-06 |
|
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: 50.34 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 209 DTFAASSVDFIRKYGFNGVDIDYEY-PTTMKDAgnpldwqlanarraglvqgYAALMKSLREKLDAAGaadgkHYLLTVA 287
Cdd:cd02874 89 QRLINNILALAKKYGYDGVNIDFENvPPEDREA-------------------YTQFLRELSDRLHPAG-----YTLSTAV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 288 AP--SSGYLLRGMETF---QMQKYLDYVNIMSYDLHGAWNEyVGPNASLfddgkdgelaaANVYGSAQYGNIGylntdwa 362
Cdd:cd02874 145 VPktSADQFGNWSGAYdyaAIGKIVDFVVLMTYDWHWRGGP-PGPVAPI-----------GWVERVLQYAVTQ------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 363 yhyfrgsMPAGRINIGLPYYTRghknvqggtdglwgkasattcpagagltkcgdgatgidnLWHDKDTNGVESPAGSnpM 442
Cdd:cd02874 206 -------IPREKILLGIPLYGY---------------------------------------DWTLPYKKGGKASTIS--P 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 443 WHAKNLEKgivgdyvtQYGFPANttltgtyarkYDSTLVAPW--LWNAQK---KVFLstEDEQSVAAKADYVVNKGIGGT 517
Cdd:cd02874 238 QQAINLAK--------RYGAEIQ----------YDEEAQSPFfrYVDEQGrrhEVWF--EDARSLQAKFELAKEYGLRGV 297
|
...
gi 1899249394 518 MVW 520
Cdd:cd02874 298 SYW 300
|
|
| CBM_5_12 |
pfam02839 |
Carbohydrate binding domain; This short domain is found in many different glycosyl hydrolase ... |
762-787 |
2.26e-04 |
|
Carbohydrate binding domain; This short domain is found in many different glycosyl hydrolase enzymes and is presumed to have a carbohydrate binding function. The domain has six aromatic groups that may be important for binding.
Pssm-ID: 427014 Cd Length: 25 Bit Score: 38.74 E-value: 2.26e-04
|
| GH18_EndoS-like |
cd06542 |
Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of ... |
204-357 |
2.42e-03 |
|
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: 40.44 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899249394 204 NQAGIDTFAASSVDFIRKYGFNGVDIDYEYPTtmkdAGNPLDWQLANARraglvqgYAALMKSLREKLDAAGAadgkhyL 283
Cdd:cd06542 85 SDAAAKAYAKAIVDTVDKYGLDGVDFDDEYSG----YGKNGTSQPSNEA-------FVRLIKELRKYMGPTDK------L 147
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1899249394 284 LTVAAPsSGYLLRGMEtfQMQKYLDYVNIMSYdlhGAWNEYVGPNASLFDDGKDGE--LAAANVYGSAQYGNIGYL 357
Cdd:cd06542 148 LTIDGY-GQALSNDGE--EVSPYVDYVIYQYY---GSSSSSTQRNWNTNSPKIPPEkmVYTESFEEENGGNSGSSA 217
|
|
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