|
Name |
Accession |
Description |
Interval |
E-value |
| ChiA |
COG3325 |
Chitinase, GH18 family [Carbohydrate transport and metabolism]; |
61-532 |
2.47e-147 |
|
Chitinase, GH18 family [Carbohydrate transport and metabolism];
Pssm-ID: 442554 [Multi-domain] Cd Length: 391 Bit Score: 437.04 E-value: 2.47e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 61 CSVYDSAgrEKMGADHPRRVIGYFTGWRTGKDGkpaYLASDIPWDKITHINYAFAHVDGGNRLSVGsdgeknaatgMTW- 139
Cdd:COG3325 4 ASVSDTA--AAATATSGKRVVGYFTQWGIYGRN---YLVKDIPASKLTHINYAFANVDPDGKCSVG----------DAWa 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 140 -PGVAGAEMDPALPYKGHFNLLNKFKKQHPDVKTMISVGGWAEtggyfaddgsrvdSGGFYSMAtkadgsVNQAGIDTFA 218
Cdd:COG3325 69 kPSVDGAADDWDQPLKGNFNQLKKLKAKNPNLKVLISIGGWTW-------------SKGFSDAA------ATPASRAAFV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 219 DSAVDFVRKYGFNGVDIDYEYPTTMKDAGNPldwsfangRRAGLVKGYAALMKTLREKLDRAGAADGRHYLLSVAAPSSG 298
Cdd:COG3325 130 DSCVDLLRKYNFDGIDIDWEYPGSGGAPGNV--------YRPEDKANFTALLKELRAQLDALGAETGKHYLLTAAAPAGP 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 299 YLLRGMETFQVQKYLDYVNIMSYDLHGAWNEYVGPNASLFDDGKDAELAAanvygsaqyggigyLNTDWAYHYF-RGSMP 377
Cdd:COG3325 202 DKLDGIELPKVAQYLDYVNVMTYDFHGAWSPTTGHQAPLYDSPKDPEAQG--------------YSVDSAVQAYlAAGVP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 378 AGRINIGLPYYTRGHKNVQGGTDGLWGRAAAStcPAGSgltkcgdgavgidnlWhdldtngkesPAGSNPMWHaknlekg 457
Cdd:COG3325 268 ASKLVLGVPFYGRGWTGVTGGNNGLYQPATGP--APGT---------------W----------EAGVNDYKD------- 313
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604860697 458 IVGDYVTDygfpadtkltGTYARKYDATLVAPWLWNAEKKVFLSTEDEQSVGAKADYVVDRGIGGAMIWELAGDY 532
Cdd:COG3325 314 LKALYLGS----------NGYTRYWDDVAKAPYLYNGDTGTFISYDDPRSIAAKADYVKDKGLGGVMFWELSGDT 378
|
|
| GH18_chitinase |
cd06548 |
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ... |
80-531 |
2.58e-103 |
|
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: 320.73 E-value: 2.58e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 80 VIGYFTGWRTGKDGKPAYLasDIPWDKITHINYAFAHVDGGNRLSVGSDGEKNAAtgmtWPGVAGAEMDPALPYKGHFNL 159
Cdd:cd06548 1 VVGYFTNWGIYGRNYFVTD--DIPADKLTHINYAFADIDGDGGVVTSDDEAADEA----AQSVDGGADTDDQPLKGNFGQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 160 LNKFKKQHPDVKTMISVGGWAEtggyfaddgsrvdSGGFYSMATkadgsvNQAGIDTFADSAVDFVRKYGFNGVDIDYEY 239
Cdd:cd06548 75 LRKLKQKNPHLKILLSIGGWTW-------------SGGFSDAAA------TEASRAKFADSAVDFIRKYGFDGIDIDWEY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 240 PTTMKDAGNPldwsfangRRAGLVKGYAALMKTLREKLDRAGAADGRHYLLSVAAPSSGYLLRGMETFQVQKYLDYVNIM 319
Cdd:cd06548 136 PGSGGAPGNV--------ARPEDKENFTLLLKELREALDALGAETGRKYLLTIAAPAGPDKLDKLEVAEIAKYLDFINLM 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 320 SYDLHGAWNEYVGPNASLFDDGKDAelaaanvygsaqygGIGYLNTDWAYHYFRGSMPAGRINIGLPYYTRGHKNvqggt 399
Cdd:cd06548 208 TYDFHGAWSNTTGHHSNLYASPADP--------------PGGYSVDAAVNYYLSAGVPPEKLVLGVPFYGRGWTG----- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 400 dglwgraaastcpagsgltkcgdgavgidnlwhdldtngkespagsnpmwhaknlekgivgdyvtdygfpadtkltgtYA 479
Cdd:cd06548 269 ------------------------------------------------------------------------------YT 270
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1604860697 480 RKYDATLVAPWLWNAEKKVFLSTEDEQSVGAKADYVVDRGIGGAMIWELAGD 531
Cdd:cd06548 271 RYWDEVAKAPYLYNPSTKTFISYDDPRSIKAKADYVKDKGLGGVMFWELSGD 322
|
|
| ChiC |
pfam06483 |
Chitinase C; This ~170 aa region is found at the C-terminus of pfam00704. |
540-709 |
4.52e-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: 4.52e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 540 QYEMGDTLTSLMYDTFKSAAPYGAKKSNADLPTEAVNVDVEFTDFKLGDSNYPITPKLRITNNTKTALPGGTEFQFDYGT 619
Cdd:pfam06483 1 EYFMGDTLTTLLYDKFKAAAPYGATKANAAMPTQVLDVSVSLTGFPLGDSNYPINPKLRITNNSGQTIPGGTEFEFDYPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 620 SAPGNASDQSGFGTRVISSDHTGNNVGGLKGDFHRVSMKLPAWQSLAPGATVDLAFNYYLPVSTPSNWTVTIDGKTYALA 699
Cdd:pfam06483 81 SAPDNAKDQSGFGLTVISSGHTGPNVGGLKGDFHRVAFTLPSWQTLAPGASVEVDLVYYLPVSGPSNWTVTFGGTTYALK 160
|
170
....*....|
gi 1604860697 700 GDLARGTTVV 709
Cdd:pfam06483 161 GDYPRGTTTL 170
|
|
| Glyco_18 |
smart00636 |
Glyco_18 domain; |
79-531 |
1.97e-98 |
|
Glyco_18 domain;
Pssm-ID: 214753 [Multi-domain] Cd Length: 334 Bit Score: 308.45 E-value: 1.97e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 79 RVIGYFTGWRTGKdgkPAYLASDIPWDKITHINYAFAHVDGGNRLsvgsdgeknaatgmtwpgvagaEMDPALPYKGHFN 158
Cdd:smart00636 1 RVVGYFTNWGVYG---RNFPVDDIPASKLTHIIYAFANIDPDGTV----------------------TIGDEWADIGNFG 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 159 LLNKFKKQHPDVKTMISVGGWAetggyfaddgsrvDSGGFYSMATkadgsvNQAGIDTFADSAVDFVRKYGFNGVDIDYE 238
Cdd:smart00636 56 QLKALKKKNPGLKVLLSIGGWT-------------ESDNFSSMLS------DPASRKKFIDSIVSFLKKYGFDGIDIDWE 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 239 YPTTMKDAGNpldwsfangrraglvkGYAALMKTLREKLDRAGAAdGRHYLLSVAAPSSG-YLLRGMETF-QVQKYLDYV 316
Cdd:smart00636 117 YPGGRGDDRE----------------NYTALLKELREALDKEGAE-GKGYLLTIAVPAGPdKIDKGYGDLpAIAKYLDFI 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 317 NIMSYDLHGAWNEYVGPNASLFDDGKDAElaaanvygsaqyggigYLNTDWAYHYFRG-SMPAGRINIGLPYYTRGHKNV 395
Cdd:smart00636 180 NLMTYDFHGAWSNPTGHNAPLYAGPGDPE----------------KYNVDYAVKYYLCkGVPPSKLVLGIPFYGRGWTLV 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 396 QGGTDGlwgraaastcpagsgltkcgdgavgIDNLWHDLDTNGKESPAGSNPMWHAKNLEKGivgdyvtdygfpadtklt 475
Cdd:smart00636 244 DGSNNG-------------------------PGAPFTGPATGGPGTWEGGVVDYREICKLLG------------------ 280
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1604860697 476 gtYARKYDATLVAPWLWNAEKKVFLSTEDEQSVGAKADYVVDRGIGGAMIWELAGD 531
Cdd:smart00636 281 --ATVVYDDTAKAPYAYNPGTGQWVSYDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
|
|
| Glyco_hydro_18 |
pfam00704 |
Glycosyl hydrolases family 18; |
79-531 |
2.59e-73 |
|
Glycosyl hydrolases family 18;
Pssm-ID: 425828 [Multi-domain] Cd Length: 311 Bit Score: 241.59 E-value: 2.59e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 79 RVIGYFTGWRTGKDGKPaylasdIPWDKITHINYAFAHVDGGNRLSVGSDgeknaatgmtwpgvagaemdpalPYKGHFN 158
Cdd:pfam00704 1 RIVGYYTSWGVYRNGNF------LPSDKLTHIIYAFANIDGSDGTLFIGD-----------------------WDLGNFE 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 159 LLNKFKKQ-HPDVKTMISVGGWAetggyfaddgsrvDSGGFYSMATkadgsvNQAGIDTFADSAVDFVRKYGFNGVDIDY 237
Cdd:pfam00704 52 QLKKLKKQkNPGVKVLLSIGGWT-------------DSTGFSLMAS------NPASRKKFADSIVSFLRKYGFDGIDIDW 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 238 EYPTtmkdaGNPLDWSfangrraglvkGYAALMKTLREKLDRAGaaDGRHYLLSVAAPSSG-YLLRGMETFQVQKYLDYV 316
Cdd:pfam00704 113 EYPG-----GNPEDKE-----------NYDLLLRELRAALDEAK--GGKKYLLSAAVPASYpDLDKGYDLPKIAKYLDFI 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 317 NIMSYDLHGAWNEYVGPNASLFDDgkdaelaaanvygsaqyggiGYLNTDWAYHYF-RGSMPAGRINIGLPYYTRGHKNV 395
Cdd:pfam00704 175 NVMTYDFHGSWDNVTGHHAPLYGG--------------------GSYNVDYAVKYYlKQGVPASKLVLGVPFYGRSWTLV 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 396 QGGTDglwgraaastcpagsgltkcgdgavgidnlwhdldtngkespAGSNPMWHAKNLEKGIVGDyvtdygfpadtklt 475
Cdd:pfam00704 235 NGSGN------------------------------------------TWEDGVLAYKEICNLLKDN-------------- 258
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1604860697 476 gTYARKYDATLVAPWLWNAEkkVFLSTEDEQSVGAKADYVVDRGIGGAMIWELAGD 531
Cdd:pfam00704 259 -GATVVWDDVAKAPYVYDGD--QFITYDDPRSIATKVDYVKAKGLGGVMIWSLDAD 311
|
|
| ChiC_BD |
cd12215 |
Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of ... |
750-785 |
6.09e-11 |
|
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: 57.97 E-value: 6.09e-11
10 20 30
....*....|....*....|....*....|....*.
gi 1604860697 750 YGGGTTVSHQGHTWKSKWWTKGEEPGTTgeWGVWQD 785
Cdd:cd12215 9 YTGGDQVTYNGKVYEAKWWTQGEEPGTS--WGVWKL 42
|
|
| ChtBD3 |
smart00495 |
Chitin-binding domain type 3; |
749-783 |
7.31e-07 |
|
Chitin-binding domain type 3;
Pssm-ID: 197760 [Multi-domain] Cd Length: 41 Bit Score: 46.10 E-value: 7.31e-07
10 20 30
....*....|....*....|....*....|....*
gi 1604860697 749 SYGGGTTVSHQGHTWKSKWWTKGEEPGTTgeWGVW 783
Cdd:smart00495 9 VYTAGDVVSYNGKVYKAKWWTQGEEPGSS--SGPW 41
|
|
| CBM_5_12 |
pfam02839 |
Carbohydrate binding domain; This short domain is found in many different glycosyl hydrolase ... |
758-783 |
8.29e-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: 37.20 E-value: 8.29e-04
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ChiA |
COG3325 |
Chitinase, GH18 family [Carbohydrate transport and metabolism]; |
61-532 |
2.47e-147 |
|
Chitinase, GH18 family [Carbohydrate transport and metabolism];
Pssm-ID: 442554 [Multi-domain] Cd Length: 391 Bit Score: 437.04 E-value: 2.47e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 61 CSVYDSAgrEKMGADHPRRVIGYFTGWRTGKDGkpaYLASDIPWDKITHINYAFAHVDGGNRLSVGsdgeknaatgMTW- 139
Cdd:COG3325 4 ASVSDTA--AAATATSGKRVVGYFTQWGIYGRN---YLVKDIPASKLTHINYAFANVDPDGKCSVG----------DAWa 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 140 -PGVAGAEMDPALPYKGHFNLLNKFKKQHPDVKTMISVGGWAEtggyfaddgsrvdSGGFYSMAtkadgsVNQAGIDTFA 218
Cdd:COG3325 69 kPSVDGAADDWDQPLKGNFNQLKKLKAKNPNLKVLISIGGWTW-------------SKGFSDAA------ATPASRAAFV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 219 DSAVDFVRKYGFNGVDIDYEYPTTMKDAGNPldwsfangRRAGLVKGYAALMKTLREKLDRAGAADGRHYLLSVAAPSSG 298
Cdd:COG3325 130 DSCVDLLRKYNFDGIDIDWEYPGSGGAPGNV--------YRPEDKANFTALLKELRAQLDALGAETGKHYLLTAAAPAGP 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 299 YLLRGMETFQVQKYLDYVNIMSYDLHGAWNEYVGPNASLFDDGKDAELAAanvygsaqyggigyLNTDWAYHYF-RGSMP 377
Cdd:COG3325 202 DKLDGIELPKVAQYLDYVNVMTYDFHGAWSPTTGHQAPLYDSPKDPEAQG--------------YSVDSAVQAYlAAGVP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 378 AGRINIGLPYYTRGHKNVQGGTDGLWGRAAAStcPAGSgltkcgdgavgidnlWhdldtngkesPAGSNPMWHaknlekg 457
Cdd:COG3325 268 ASKLVLGVPFYGRGWTGVTGGNNGLYQPATGP--APGT---------------W----------EAGVNDYKD------- 313
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604860697 458 IVGDYVTDygfpadtkltGTYARKYDATLVAPWLWNAEKKVFLSTEDEQSVGAKADYVVDRGIGGAMIWELAGDY 532
Cdd:COG3325 314 LKALYLGS----------NGYTRYWDDVAKAPYLYNGDTGTFISYDDPRSIAAKADYVKDKGLGGVMFWELSGDT 378
|
|
| GH18_chitinase |
cd06548 |
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ... |
80-531 |
2.58e-103 |
|
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: 320.73 E-value: 2.58e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 80 VIGYFTGWRTGKDGKPAYLasDIPWDKITHINYAFAHVDGGNRLSVGSDGEKNAAtgmtWPGVAGAEMDPALPYKGHFNL 159
Cdd:cd06548 1 VVGYFTNWGIYGRNYFVTD--DIPADKLTHINYAFADIDGDGGVVTSDDEAADEA----AQSVDGGADTDDQPLKGNFGQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 160 LNKFKKQHPDVKTMISVGGWAEtggyfaddgsrvdSGGFYSMATkadgsvNQAGIDTFADSAVDFVRKYGFNGVDIDYEY 239
Cdd:cd06548 75 LRKLKQKNPHLKILLSIGGWTW-------------SGGFSDAAA------TEASRAKFADSAVDFIRKYGFDGIDIDWEY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 240 PTTMKDAGNPldwsfangRRAGLVKGYAALMKTLREKLDRAGAADGRHYLLSVAAPSSGYLLRGMETFQVQKYLDYVNIM 319
Cdd:cd06548 136 PGSGGAPGNV--------ARPEDKENFTLLLKELREALDALGAETGRKYLLTIAAPAGPDKLDKLEVAEIAKYLDFINLM 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 320 SYDLHGAWNEYVGPNASLFDDGKDAelaaanvygsaqygGIGYLNTDWAYHYFRGSMPAGRINIGLPYYTRGHKNvqggt 399
Cdd:cd06548 208 TYDFHGAWSNTTGHHSNLYASPADP--------------PGGYSVDAAVNYYLSAGVPPEKLVLGVPFYGRGWTG----- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 400 dglwgraaastcpagsgltkcgdgavgidnlwhdldtngkespagsnpmwhaknlekgivgdyvtdygfpadtkltgtYA 479
Cdd:cd06548 269 ------------------------------------------------------------------------------YT 270
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1604860697 480 RKYDATLVAPWLWNAEKKVFLSTEDEQSVGAKADYVVDRGIGGAMIWELAGD 531
Cdd:cd06548 271 RYWDEVAKAPYLYNPSTKTFISYDDPRSIKAKADYVKDKGLGGVMFWELSGD 322
|
|
| ChiC |
pfam06483 |
Chitinase C; This ~170 aa region is found at the C-terminus of pfam00704. |
540-709 |
4.52e-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: 4.52e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 540 QYEMGDTLTSLMYDTFKSAAPYGAKKSNADLPTEAVNVDVEFTDFKLGDSNYPITPKLRITNNTKTALPGGTEFQFDYGT 619
Cdd:pfam06483 1 EYFMGDTLTTLLYDKFKAAAPYGATKANAAMPTQVLDVSVSLTGFPLGDSNYPINPKLRITNNSGQTIPGGTEFEFDYPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 620 SAPGNASDQSGFGTRVISSDHTGNNVGGLKGDFHRVSMKLPAWQSLAPGATVDLAFNYYLPVSTPSNWTVTIDGKTYALA 699
Cdd:pfam06483 81 SAPDNAKDQSGFGLTVISSGHTGPNVGGLKGDFHRVAFTLPSWQTLAPGASVEVDLVYYLPVSGPSNWTVTFGGTTYALK 160
|
170
....*....|
gi 1604860697 700 GDLARGTTVV 709
Cdd:pfam06483 161 GDYPRGTTTL 170
|
|
| Glyco_18 |
smart00636 |
Glyco_18 domain; |
79-531 |
1.97e-98 |
|
Glyco_18 domain;
Pssm-ID: 214753 [Multi-domain] Cd Length: 334 Bit Score: 308.45 E-value: 1.97e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 79 RVIGYFTGWRTGKdgkPAYLASDIPWDKITHINYAFAHVDGGNRLsvgsdgeknaatgmtwpgvagaEMDPALPYKGHFN 158
Cdd:smart00636 1 RVVGYFTNWGVYG---RNFPVDDIPASKLTHIIYAFANIDPDGTV----------------------TIGDEWADIGNFG 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 159 LLNKFKKQHPDVKTMISVGGWAetggyfaddgsrvDSGGFYSMATkadgsvNQAGIDTFADSAVDFVRKYGFNGVDIDYE 238
Cdd:smart00636 56 QLKALKKKNPGLKVLLSIGGWT-------------ESDNFSSMLS------DPASRKKFIDSIVSFLKKYGFDGIDIDWE 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 239 YPTTMKDAGNpldwsfangrraglvkGYAALMKTLREKLDRAGAAdGRHYLLSVAAPSSG-YLLRGMETF-QVQKYLDYV 316
Cdd:smart00636 117 YPGGRGDDRE----------------NYTALLKELREALDKEGAE-GKGYLLTIAVPAGPdKIDKGYGDLpAIAKYLDFI 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 317 NIMSYDLHGAWNEYVGPNASLFDDGKDAElaaanvygsaqyggigYLNTDWAYHYFRG-SMPAGRINIGLPYYTRGHKNV 395
Cdd:smart00636 180 NLMTYDFHGAWSNPTGHNAPLYAGPGDPE----------------KYNVDYAVKYYLCkGVPPSKLVLGIPFYGRGWTLV 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 396 QGGTDGlwgraaastcpagsgltkcgdgavgIDNLWHDLDTNGKESPAGSNPMWHAKNLEKGivgdyvtdygfpadtklt 475
Cdd:smart00636 244 DGSNNG-------------------------PGAPFTGPATGGPGTWEGGVVDYREICKLLG------------------ 280
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1604860697 476 gtYARKYDATLVAPWLWNAEKKVFLSTEDEQSVGAKADYVVDRGIGGAMIWELAGD 531
Cdd:smart00636 281 --ATVVYDDTAKAPYAYNPGTGQWVSYDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
|
|
| Glyco_hydro_18 |
pfam00704 |
Glycosyl hydrolases family 18; |
79-531 |
2.59e-73 |
|
Glycosyl hydrolases family 18;
Pssm-ID: 425828 [Multi-domain] Cd Length: 311 Bit Score: 241.59 E-value: 2.59e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 79 RVIGYFTGWRTGKDGKPaylasdIPWDKITHINYAFAHVDGGNRLSVGSDgeknaatgmtwpgvagaemdpalPYKGHFN 158
Cdd:pfam00704 1 RIVGYYTSWGVYRNGNF------LPSDKLTHIIYAFANIDGSDGTLFIGD-----------------------WDLGNFE 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 159 LLNKFKKQ-HPDVKTMISVGGWAetggyfaddgsrvDSGGFYSMATkadgsvNQAGIDTFADSAVDFVRKYGFNGVDIDY 237
Cdd:pfam00704 52 QLKKLKKQkNPGVKVLLSIGGWT-------------DSTGFSLMAS------NPASRKKFADSIVSFLRKYGFDGIDIDW 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 238 EYPTtmkdaGNPLDWSfangrraglvkGYAALMKTLREKLDRAGaaDGRHYLLSVAAPSSG-YLLRGMETFQVQKYLDYV 316
Cdd:pfam00704 113 EYPG-----GNPEDKE-----------NYDLLLRELRAALDEAK--GGKKYLLSAAVPASYpDLDKGYDLPKIAKYLDFI 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 317 NIMSYDLHGAWNEYVGPNASLFDDgkdaelaaanvygsaqyggiGYLNTDWAYHYF-RGSMPAGRINIGLPYYTRGHKNV 395
Cdd:pfam00704 175 NVMTYDFHGSWDNVTGHHAPLYGG--------------------GSYNVDYAVKYYlKQGVPASKLVLGVPFYGRSWTLV 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 396 QGGTDglwgraaastcpagsgltkcgdgavgidnlwhdldtngkespAGSNPMWHAKNLEKGIVGDyvtdygfpadtklt 475
Cdd:pfam00704 235 NGSGN------------------------------------------TWEDGVLAYKEICNLLKDN-------------- 258
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1604860697 476 gTYARKYDATLVAPWLWNAEkkVFLSTEDEQSVGAKADYVVDRGIGGAMIWELAGD 531
Cdd:pfam00704 259 -GATVVWDDVAKAPYVYDGD--QFITYDDPRSIATKVDYVKAKGLGGVMIWSLDAD 311
|
|
| GH18_chitolectin_chitotriosidase |
cd02872 |
This conserved domain family includes a large number of catalytically inactive chitinase-like ... |
80-528 |
6.94e-45 |
|
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: 165.42 E-value: 6.94e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 80 VIGYFTGW---RTGkDGKpaYLASDIPWDKITHINYAFAhvdggnrlSVGSDGEKNaatgmtwpgvagaEMDPALPY-KG 155
Cdd:cd02872 1 VVCYFTNWaqyRPG-NGK--FVPENIDPFLCTHIIYAFA--------GLNPDGNII-------------ILDEWNDIdLG 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 156 HFNLLNKFKKQHPDVKTMISVGGWAETggyfaddgsrvdSGGFYSMATKAdgsVNQAgidTFADSAVDFVRKYGFNGVDI 235
Cdd:cd02872 57 LYERFNALKEKNPNLKTLLAIGGWNFG------------SAKFSAMAASP---ENRK---TFIKSAIAFLRKYGFDGLDL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 236 DYEYPTT----MKDAGNpldwsfangrraglvkgYAALMKTLREKLDRagaaDGRHYLLSVAAPSS------GYLLRgme 305
Cdd:cd02872 119 DWEYPGQrggpPEDKEN-----------------FVTLLKELREAFEP----EAPRLLLTAAVSAGketidaAYDIP--- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 306 tfQVQKYLDYVNIMSYDLHGAWNEYVGPNASLFddgkdaelaaanvYGSAQYGGIGYLNTDWAYHYFRGS-MPAGRINIG 384
Cdd:cd02872 175 --EISKYLDFINVMTYDFHGSWEGVTGHNSPLY-------------AGSADTGDQKYLNVDYAIKYWLSKgAPPEKLVLG 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 385 LPYYTRGhknvqggtdglWGRAAASTcpagsglTKCGDGAVGidnlwhdldtngkespagsnpmwhaknleKGIVGDYvt 464
Cdd:cd02872 240 IPTYGRS-----------FTLASPSN-------TGVGAPASG-----------------------------PGTAGPY-- 270
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1604860697 465 dygfpadTKLTGTYA-------RKYDATLVapwlWNAEKKV--------FLSTEDEQSVGAKADYVVDRGIGGAMIWEL 528
Cdd:cd02872 271 -------TREAGFLAyyeicefLKSGWTVV----WDDEQKVpyaykgnqWVGYDDEESIALKVQYLKSKGLGGAMVWSI 338
|
|
| GH18_chitinase-like |
cd00598 |
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ... |
80-323 |
8.60e-35 |
|
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: 131.73 E-value: 8.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 80 VIGYFTGWRTGKDGKPaylaSDIPWDKITHINYAFAHVDGGNRLSVGSDGeknaatgmtwpgvagaemdpalPYKGHFNL 159
Cdd:cd00598 1 VICYYDGWSSGRGPDP----TDIPLSLCTHIIYAFAEISSDGSLNLFGDK----------------------SEEPLKGA 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 160 LNKFKKQHPDVKTMISVGGWAetggyfaddgsrvDSGGFYSMATKADgsvnqagIDTFADSAVDFVRKYGFNGVDIDYEY 239
Cdd:cd00598 55 LEELASKKPGLKVLISIGGWT-------------DSSPFTLASDPAS-------RAAFANSLVSFLKTYGFDGVDIDWEY 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 240 PttmkdaGNPLDWSFANgrraglvkgYAALMKTLREKLDRAGaadgrhYLLSVAAPSSGYLLRGMETF-QVQKYLDYVNI 318
Cdd:cd00598 115 P------GAADNSDREN---------FITLLRELRSALGAAN------YLLTIAVPASYFDLGYAYDVpAIGDYVDFVNV 173
|
....*
gi 1604860697 319 MSYDL 323
Cdd:cd00598 174 MTYDL 178
|
|
| GH18_zymocin_alpha |
cd02878 |
Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle ... |
81-328 |
7.60e-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: 106.62 E-value: 7.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 81 IGYFTGWRTGKDGkpayLASD---IPWDKITHINYAFAHVDGGNRLSVGSDGEKNaatgmtwpgvagaemdpalpykghf 157
Cdd:cd02878 3 IAYFEAYNLDRPC----LNMDvtqIDTSKYTHIHFAFANITSDFSVDVSSVQEQF------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 158 nllNKFKKQHpDVKTMISVGGWAetggyFADDGSRvdsggfYSMATKAdgsVNQAGIDTFADSAVDFVRKYGFNGVDIDY 237
Cdd:cd02878 54 ---SDFKKLK-GVKKILSFGGWD-----FSTSPST------YQIFRDA---VKPANRDTFANNVVNFVNKYNLDGVDFDW 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 238 EYPTTMKDAGNPLDwSFANGrraglvKGYAALMKTLREKLdragaadGRHYLLSVAAPSSGYLLRGMETFQVQKYLDYVN 317
Cdd:cd02878 116 EYPGAPDIPGIPAG-DPDDG------KNYLEFLKLLKSKL-------PSGKSLSIAAPASYWYLKGFPIKDMAKYVDYIV 181
|
250
....*....|.
gi 1604860697 318 IMSYDLHGAWN 328
Cdd:cd02878 182 YMTYDLHGQWD 192
|
|
| GH18_plant_chitinase_class_V |
cd02879 |
The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the ... |
99-390 |
6.93e-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: 93.97 E-value: 6.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 99 ASDIPWDKITHINYAFAHVDG-GNRLSVGSDGEknaatgmtwpgvagaemdpalPYKGHFNllNKFKKQHPDVKTMISVG 177
Cdd:cd02879 18 PSNIDSSLFTHLFYAFADLDPsTYEVVISPSDE---------------------SEFSTFT--ETVKRKNPSVKTLLSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 178 GwaetggyfadDGSrvDSGGFYSMATKADGSvnqagiDTFADSAVDFVRKYGFNGVDIDYEYPTTMKDAGNpldwsfang 257
Cdd:cd02879 75 G----------GGS--DSSAFAAMASDPTAR------KAFINSSIKVARKYGFDGLDLDWEFPSSQVEMEN--------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 258 rraglvkgYAALMKTLREKL-DRAGAADGRHYLLSVAAPSSGYLLRGMETFQ-----VQKYLDYVNIMSYDLHGAWNEYV 331
Cdd:cd02879 128 --------FGKLLEEWRAAVkDEARSSGRPPLLLTAAVYFSPILFLSDDSVSypieaINKNLDWVNVMAYDYYGSWESNT 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1604860697 332 GPNASLFDDgkdaelAAANVygSAQYGgigylNTDWayhyFRGSMPAGRINIGLPYYTR 390
Cdd:cd02879 200 TGPAAALYD------PNSNV--STDYG-----IKSW----IKAGVPAKKLVLGLPLYGR 241
|
|
| GH18_3CO4_chitinase |
cd06545 |
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an ... |
80-388 |
1.35e-12 |
|
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: 68.63 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 80 VIGYFTGWrtgkDGKPAYLASdIPWDKITHINYAFAHVDGGNRLSVGSDGEKNAAtgmtwpgvagaemdpalpykghfnL 159
Cdd:cd06545 1 VVGYLPNY----DDLNALSPT-IDFSKLTHINLAFANPDANGTLNANPVRSELNS------------------------V 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 160 LNKFKKQhpDVKTMISVGGwaetggyfaddGSRVDSGGFYSMATKadgsvnqagIDTFADSAVDFVRKYGFNGVDIDYEy 239
Cdd:cd06545 52 VNAAHAH--NVKILISLAG-----------GSPPEFTAALNDPAK---------RKALVDKIINYVVSYNLDGIDVDLE- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 240 pttmkdagnpldWSFANGrraglvKGYAALMKTLREKLDRAGaadgrhyLLSVAAPSSGYllRGMETFQVQKYLDYVNIM 319
Cdd:cd06545 109 ------------GPDVTF------GDYLVFIRALYAALKKEG-------KLLTAAVSSWN--GGAVSDSTLAYFDFINIM 161
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1604860697 320 SYDLHGAWNEYVGPNASLFDDGKdaelaaanvygsaqyggigylnTDWAYHYFRGSMPAGRINIGLPYY 388
Cdd:cd06545 162 SYDATGPWWGDNPGQHSSYDDAV----------------------NDLNYWNERGLASKDKLVLGLPFY 208
|
|
| GH18_IDGF |
cd02873 |
The IDGF's (imaginal disc growth factors) are a family of growth factors identified in insects ... |
153-531 |
8.70e-12 |
|
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: 67.72 E-value: 8.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 153 YKGHFNLLNKFKKQHPDVKTMISVGGwaetggyFADDGSRVDSGGFYSMATkadgsvNQAGIDTFADSAVDFVRKYGFNG 232
Cdd:cd02873 58 DKSHYRAITSLKRKYPHLKVLLSVGG-------DRDTDEEGENEKYLLLLE------SSESRNAFINSAHSLLKTYGFDG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 233 VDIDYEYPTT--MKDAGN-PLDW-SFANGRRAGLVK---------GYAALMKTLREKLDRAGaadgrhYLLSVAA-P--- 295
Cdd:cd02873 125 LDLAWQFPKNkpKKVRGTfGSAWhSFKKLFTGDSVVdekaaehkeQFTALVRELKNALRPDG------LLLTLTVlPhvn 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 296 SSGYllrgMETFQVQKYLDYVNIMSYDlhgawneYVGPNAslfdDGKDAELAAAnVYgsAQYGGIGYLNTDWAYHYF-RG 374
Cdd:cd02873 199 STWY----FDVPAIANNVDFVNLATFD-------FLTPER----NPEEADYTAP-IY--ELYERNPHHNVDYQVKYWlNQ 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 375 SMPAGRINIGLPYYTRGHKNVQggtdglwgraaastcpaGSGLT-------KCGDGAVGidnlwHDLDTNGKESPAGSNP 447
Cdd:cd02873 261 GTPASKLNLGIATYGRAWKLTK-----------------DSGITgvppvleTDGPGPAG-----PQTKTPGLLSWPEICS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 448 MWHAKNLEKGIVGDY--VTDygfpaDTKLTGTYA-RKYDAtlvapwlwNAEKKVFLSTEDEQSVGAKADYVVDRGIGGAM 524
Cdd:cd02873 319 KLPNPANLKGADAPLrkVGD-----PTKRFGSYAyRPADE--------NGEHGIWVSYEDPDTAANKAGYAKAKGLGGVA 385
|
....*..
gi 1604860697 525 IWELAGD 531
Cdd:cd02873 386 LFDLSLD 392
|
|
| ChiC_BD |
cd12215 |
Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of ... |
750-785 |
6.09e-11 |
|
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: 57.97 E-value: 6.09e-11
10 20 30
....*....|....*....|....*....|....*.
gi 1604860697 750 YGGGTTVSHQGHTWKSKWWTKGEEPGTTgeWGVWQD 785
Cdd:cd12215 9 YTGGDQVTYNGKVYEAKWWTQGEEPGTS--WGVWKL 42
|
|
| ChtBD3 |
smart00495 |
Chitin-binding domain type 3; |
749-783 |
7.31e-07 |
|
Chitin-binding domain type 3;
Pssm-ID: 197760 [Multi-domain] Cd Length: 41 Bit Score: 46.10 E-value: 7.31e-07
10 20 30
....*....|....*....|....*....|....*
gi 1604860697 749 SYGGGTTVSHQGHTWKSKWWTKGEEPGTTgeWGVW 783
Cdd:smart00495 9 VYTAGDVVSYNGKVYKAKWWTQGEEPGSS--SGPW 41
|
|
| GH18_CFLE_spore_hydrolase |
cd02874 |
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ... |
215-337 |
5.41e-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: 49.19 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 215 DTFADSAVDFVRKYGFNGVDIDYEY-PTTMKDAgnpldwsfangrraglvkgYAALMKTLREKLDRAGaadgrHYLLSVA 293
Cdd:cd02874 89 QRLINNILALAKKYGYDGVNIDFENvPPEDREA-------------------YTQFLRELSDRLHPAG-----YTLSTAV 144
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1604860697 294 AP--SSGYLLRGMETF---QVQKYLDYVNIMSYDLHGAWNEyVGPNASL 337
Cdd:cd02874 145 VPktSADQFGNWSGAYdyaAIGKIVDFVVLMTYDWHWRGGP-PGPVAPI 192
|
|
| GH18_narbonin |
cd06544 |
Narbonin is a plant 2S protein from the globulin fraction of narbon bean (Vicia narbonensis L.) ... |
162-238 |
1.62e-05 |
|
Narbonin is a plant 2S protein from the globulin fraction of narbon bean (Vicia narbonensis L.) cotyledons with unknown function. Narbonin has a glycosyl hydrolase family 18 (GH18) domain without the conserved catalytic residues and with no known enzymatic activity. Narbonin amounts to up to 3% of the total seed globulins of mature seeds and was thought to be a storage protein but was found to degrade too slowly during germination. This family also includes the VfNOD32 nodulin from Vicia faba.
Pssm-ID: 119361 Cd Length: 253 Bit Score: 46.98 E-value: 1.62e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1604860697 162 KFKKQHPDVKTMISVGGWaetggyfaddgsrvdsgGFYSMATKADGSVNQAGIDTFADSAVDFVRKYGFNGVDIDYE 238
Cdd:cd06544 63 SIKAQHPNVKVVISIGGR-----------------GVQNNPTPFDPSNVDSWVSNAVSSLTSIIQTYNLDGIDIDYE 122
|
|
| GH18_EndoS-like |
cd06542 |
Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of ... |
210-374 |
1.97e-04 |
|
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: 43.91 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 210 NQAGIDTFADSAVDFVRKYGFNGVDIDYEYpttmkDAGNPLDWSFANGRRaglvkgYAALMKTLREKLDRAGAadgrhyL 289
Cdd:cd06542 85 SDAAAKAYAKAIVDTVDKYGLDGVDFDDEY-----SGYGKNGTSQPSNEA------FVRLIKELRKYMGPTDK------L 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604860697 290 LSVAAPsSGYLLRGMEtfQVQKYLDYVNIMSYD-----LHGAWNEYV-------------GPNASLFDDGKDAELAAANV 351
Cdd:cd06542 148 LTIDGY-GQALSNDGE--EVSPYVDYVIYQYYGsssssTQRNWNTNSpkippekmvytesFEEENGGNSGSSAEQYARWT 224
|
170 180
....*....|....*....|....*
gi 1604860697 352 YGSAQYGGIG--YLNTDWAYHYFRG 374
Cdd:cd06542 225 PAKGGKGGIGtyALDRDYYRPYDSA 249
|
|
| CBD_like |
cd12204 |
Cellulose-binding domain, chitinase and related proteins; This group contains proteins related ... |
750-780 |
3.11e-04 |
|
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: 38.85 E-value: 3.11e-04
10 20 30
....*....|....*....|....*....|.
gi 1604860697 750 YGGGTTVSHQGHTWKSKWWTKGeEPGTTGEW 780
Cdd:cd12204 15 AAGGDLVSYNGAVYQAKWWTQS-APGSDSSW 44
|
|
| ChtBD3 |
cd00036 |
Chitin/cellulose binding domains of chitinase and related enzymes; This group contains ... |
750-780 |
5.40e-04 |
|
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: 38.13 E-value: 5.40e-04
10 20 30
....*....|....*....|....*....|.
gi 1604860697 750 YGGGTTVSHQGHTWKSKWWTKGEEPGTTGEW 780
Cdd:cd00036 8 YTAGQSVVYNGNLYTANWYTAGSVPGSDSSW 38
|
|
| CBM_5_12 |
pfam02839 |
Carbohydrate binding domain; This short domain is found in many different glycosyl hydrolase ... |
758-783 |
8.29e-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: 37.20 E-value: 8.29e-04
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| |
