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Conserved domains on  [gi|501152660|ref|WP_012197422|]
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glycosyl hydrolase family 18 protein [Shewanella baltica]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ChiA COG3325
Chitinase, GH18 family [Carbohydrate transport and metabolism];
143-559 3.69e-165

Chitinase, GH18 family [Carbohydrate transport and metabolism];


:

Pssm-ID: 442554 [Multi-domain]  Cd Length: 391  Bit Score: 485.57  E-value: 3.69e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 143 PLNAPLKENNRPYINKSGKVVGSYFVEWGVYGRKFPVDKIPAQNLTHILYGFTPICggdgindslkeidgsfqalqracs 222
Cdd:COG3325    1 SATASVSDTAAAATATSGKRVVGYFTQWGIYGRNYLVKDIPASKLTHINYAFANVD------------------------ 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 223 grEDFKVAIHDPWAAVQMPQAGVsDYSDPYKGNFGQLMALKQAHPDLKILPSVGGWTLSDPFFY-FGDKSKRDTFVASVK 301
Cdd:COG3325   57 --PDGKCSVGDAWAKPSVDGAAD-DWDQPLKGNFNQLKKLKAKNPNLKVLISIGGWTWSKGFSDaAATPASRAAFVDSCV 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 302 EFLQTWKFfDGVDIDWEYPGGGGANPNLGNANDGETYVTLMRELRAMLDELSAETGRTYELTSAIGIDAQKMAKVDYQAA 381
Cdd:COG3325  134 DLLRKYNF-DGIDIDWEYPGSGGAPGNVYRPEDKANFTALLKELRAQLDALGAETGKHYLLTAAAPAGPDKLDGIELPKV 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 382 QQYMDYIFLMSYDFNGGWTNTeLGHQTNLYEASWDP-DTRYTTDKGVKALLTQGVTPGKIVVGAAMYGRGWTGVNGytGN 460
Cdd:COG3325  213 AQYLDYVNVMTYDFHGAWSPT-TGHQAPLYDSPKDPeAQGYSVDSAVQAYLAAGVPASKLVLGVPFYGRGWTGVTG--GN 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 461 NPFTGTATGKVKGTWEDGIVDYRQIVNEYMGS-GWTYSYDETAEAPSLFKASTGDLITFDDARSVKAKGQYVLANQLGGL 539
Cdd:COG3325  290 NGLYQPATGPAPGTWEAGVNDYKDLKALYLGSnGYTRYWDDVAKAPYLYNGDTGTFISYDDPRSIAAKADYVKDKGLGGV 369
                        410       420
                 ....*....|....*....|..
gi 501152660 540 FAWEIDAD--NGDILNAMHEGL 559
Cdd:COG3325  370 MFWELSGDtaDGTLLNAIGEGL 391
ChitinaseA_N pfam08329
Chitinase A, N-terminal domain; This domain is found in a number of bacterial chitinases and ...
28-155 9.65e-66

Chitinase A, N-terminal domain; This domain is found in a number of bacterial chitinases and similar viral proteins. It is organized into a fibronectin III module domain-like fold, comprising only beta strands. Its function is not known, but it may be involved in interaction with the enzyme substrate, chitin. It is separated by a hinge region from the catalytic domain (pfam00704); this hinge region is probably mobile, allowing the N-terminal domain to have different relative positions in solution.


:

Pssm-ID: 400568  Cd Length: 130  Bit Score: 215.40  E-value: 9.65e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660   28 AAPGKPTIGWGETKFAIIEVNQAATAYNQLVTIKDAADVSVSWNLWSGDVGNKAQVLLNGNVAWEGPTGASGTANFKVNK 107
Cdd:pfam08329   1 AAPGTPSIDWGETNFAIIEVNQEATAYNNLVKVKDQADVSVSWNVWSGDIGDSAKVLFDGVQVWEGAASGSTTATFKVRK 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 501152660  108 GGRYQMQVQLCNSDGCTASDAKEILVADTDGSHLVPLNAPLKENNRPY 155
Cdd:pfam08329  81 GGRYQMQVELCNGEGCSKSAPKEIVVADTDGSHLKPLEMNVDENNKPY 128
myxo_dep_M36 super family cl45606
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
570-809 5.31e-43

myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.


The actual alignment was detected with superfamily member NF038112:

Pssm-ID: 468355 [Multi-domain]  Cd Length: 1597  Bit Score: 170.22  E-value: 5.31e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  570 NKAPIANAGADVNVTGPTDVVLNGSGSRDPENEALTYLWTQVSGPTIAITNADMANAAIQLAATQTDVAYSFSLKVTDPE 649
Cdd:NF038112 1185 NRRPVANAGPDQTVLERTTVTLNGSGSFDPDGDPLTYAWTQVSGPAVTLTGADTATPSFTAPEVTADTVLTFQLVVSDGT 1264
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  650 GLSATDSVTVTnkADTPNQAPVVSVAATATVEAGKTVSIVASASDADGDALTYAWTVPAG--VSATGQNSATLVVTGPNV 727
Cdd:NF038112 1265 KTSAPDTVTVL--VRNVNRAPVAVAGAPATVDERSTVTLDGSGTDADGDALTYAWTQTSGpaVTLTGATTATATFTAPEV 1342
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  728 TEATSYGLSVLVSDGALDASASTNLTVT----PKVIGGGCDATdPNAGNYPAWQTSVVYNTGDTVSHSqlvwkakyWTQG 803
Cdd:NF038112 1343 TADTQLTFTLTVSDGTASATDTVTVTVRnvnrAPVANAGADQT-VDERSTVTLSGSATDPDGDALTYA--------WTQT 1413

                  ....*.
gi 501152660  804 NTPSRT 809
Cdd:NF038112 1414 AGPTVT 1419
ChiC_BD cd12215
Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of ...
823-861 2.46e-10

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: 56.04  E-value: 2.46e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 501152660 823 WDASVVYNGGQTTSYNGRVWKASYWTKGDVPGVAA-VWVD 861
Cdd:cd12215    3 WDASTVYTGGDQVTYNGKVYEAKWWTQGEEPGTSWgVWKL 42
 
Name Accession Description Interval E-value
ChiA COG3325
Chitinase, GH18 family [Carbohydrate transport and metabolism];
143-559 3.69e-165

Chitinase, GH18 family [Carbohydrate transport and metabolism];


Pssm-ID: 442554 [Multi-domain]  Cd Length: 391  Bit Score: 485.57  E-value: 3.69e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 143 PLNAPLKENNRPYINKSGKVVGSYFVEWGVYGRKFPVDKIPAQNLTHILYGFTPICggdgindslkeidgsfqalqracs 222
Cdd:COG3325    1 SATASVSDTAAAATATSGKRVVGYFTQWGIYGRNYLVKDIPASKLTHINYAFANVD------------------------ 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 223 grEDFKVAIHDPWAAVQMPQAGVsDYSDPYKGNFGQLMALKQAHPDLKILPSVGGWTLSDPFFY-FGDKSKRDTFVASVK 301
Cdd:COG3325   57 --PDGKCSVGDAWAKPSVDGAAD-DWDQPLKGNFNQLKKLKAKNPNLKVLISIGGWTWSKGFSDaAATPASRAAFVDSCV 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 302 EFLQTWKFfDGVDIDWEYPGGGGANPNLGNANDGETYVTLMRELRAMLDELSAETGRTYELTSAIGIDAQKMAKVDYQAA 381
Cdd:COG3325  134 DLLRKYNF-DGIDIDWEYPGSGGAPGNVYRPEDKANFTALLKELRAQLDALGAETGKHYLLTAAAPAGPDKLDGIELPKV 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 382 QQYMDYIFLMSYDFNGGWTNTeLGHQTNLYEASWDP-DTRYTTDKGVKALLTQGVTPGKIVVGAAMYGRGWTGVNGytGN 460
Cdd:COG3325  213 AQYLDYVNVMTYDFHGAWSPT-TGHQAPLYDSPKDPeAQGYSVDSAVQAYLAAGVPASKLVLGVPFYGRGWTGVTG--GN 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 461 NPFTGTATGKVKGTWEDGIVDYRQIVNEYMGS-GWTYSYDETAEAPSLFKASTGDLITFDDARSVKAKGQYVLANQLGGL 539
Cdd:COG3325  290 NGLYQPATGPAPGTWEAGVNDYKDLKALYLGSnGYTRYWDDVAKAPYLYNGDTGTFISYDDPRSIAAKADYVKDKGLGGV 369
                        410       420
                 ....*....|....*....|..
gi 501152660 540 FAWEIDAD--NGDILNAMHEGL 559
Cdd:COG3325  370 MFWELSGDtaDGTLLNAIGEGL 391
GH18_chitinase cd06548
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ...
163-547 1.54e-132

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: 398.93  E-value: 1.54e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 163 VGSYFVEWGVYGRKFPV-DKIPAQNLTHILYGFTPICGGDGINDSLKEIDGsfqalqracsgredfkvaihdpwAAVQMP 241
Cdd:cd06548    1 VVGYFTNWGIYGRNYFVtDDIPADKLTHINYAFADIDGDGGVVTSDDEAAD-----------------------EAAQSV 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 242 QAGVSDYSDPYKGNFGQLMALKQAHPDLKILPSVGGWTLSDPFFYFG-DKSKRDTFVASVKEFLQTWkFFDGVDIDWEYP 320
Cdd:cd06548   58 DGGADTDDQPLKGNFGQLRKLKQKNPHLKILLSIGGWTWSGGFSDAAaTEASRAKFADSAVDFIRKY-GFDGIDIDWEYP 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 321 GGGGANPNLGNANDGETYVTLMRELRAMLDELSAETGRTYELTSAIGIDAQKMAKVDYQAAQQYMDYIFLMSYDFNGGWT 400
Cdd:cd06548  137 GSGGAPGNVARPEDKENFTLLLKELREALDALGAETGRKYLLTIAAPAGPDKLDKLEVAEIAKYLDFINLMTYDFHGAWS 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 401 NTeLGHQTNLYEASWDPDTRYTTDKGVKALLTQGVTPGKIVVGAAMYGRGWTgvngytgnnpftgtatgkvkgtwedgiv 480
Cdd:cd06548  217 NT-TGHHSNLYASPADPPGGYSVDAAVNYYLSAGVPPEKLVLGVPFYGRGWT---------------------------- 267
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501152660 481 dyrqivneymgsGWTYSYDETAEAPSLFKASTGDLITFDDARSVKAKGQYVLANQLGGLFAWEIDAD 547
Cdd:cd06548  268 ------------GYTRYWDEVAKAPYLYNPSTKTFISYDDPRSIKAKADYVKDKGLGGVMFWELSGD 322
Glyco_18 smart00636
Glyco_18 domain;
161-547 1.02e-125

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 381.64  E-value: 1.02e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660   161 KVVGsYFVEWGVYGRKFPVDKIPAQNLTHILYGFTPICGgdgindslkeidgsfqalqracsgreDFKVAIHDPWAAVqm 240
Cdd:smart00636   1 RVVG-YFTNWGVYGRNFPVDDIPASKLTHIIYAFANIDP--------------------------DGTVTIGDEWADI-- 51
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660   241 pqagvsdysdpykGNFGQLMALKQAHPDLKILPSVGGWTLSDPFFYF-GDKSKRDTFVASVKEFLQTWKFfDGVDIDWEY 319
Cdd:smart00636  52 -------------GNFGQLKALKKKNPGLKVLLSIGGWTESDNFSSMlSDPASRKKFIDSIVSFLKKYGF-DGIDIDWEY 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660   320 PGGGGAnpnlgnanDGETYVTLMRELRAMLDELSAEtGRTYELTSAIGIDAQKMAKVD--YQAAQQYMDYIFLMSYDFNG 397
Cdd:smart00636 118 PGGRGD--------DRENYTALLKELREALDKEGAE-GKGYLLTIAVPAGPDKIDKGYgdLPAIAKYLDFINLMTYDFHG 188
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660   398 GWTNTeLGHQTNLYEASWDPdTRYTTDKGVKALLTQGVTPGKIVVGAAMYGRGWTGVNGY--TGNNPFTGTATGkVKGTW 475
Cdd:smart00636 189 AWSNP-TGHNAPLYAGPGDP-EKYNVDYAVKYYLCKGVPPSKLVLGIPFYGRGWTLVDGSnnGPGAPFTGPATG-GPGTW 265
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501152660   476 EDGIVDYRQIVNEYmgsGWTYSYDETAEAPSLFKASTGDLITFDDARSVKAKGQYVLANQLGGLFAWEIDAD 547
Cdd:smart00636 266 EGGVVDYREICKLL---GATVVYDDTAKAPYAYNPGTGQWVSYDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
161-547 2.78e-93

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 295.90  E-value: 2.78e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  161 KVVGsYFVEWGVYGRKfpvDKIPAQNLTHILYGFTPICGGDGindslkeidgsfqalqracsgredfKVAIHDPwaavqm 240
Cdd:pfam00704   1 RIVG-YYTSWGVYRNG---NFLPSDKLTHIIYAFANIDGSDG-------------------------TLFIGDW------ 45
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  241 pqagvsdysdpYKGNFGQLMALK-QAHPDLKILPSVGGWTLSDPFFYF-GDKSKRDTFVASVKEFLQTWKFfDGVDIDWE 318
Cdd:pfam00704  46 -----------DLGNFEQLKKLKkQKNPGVKVLLSIGGWTDSTGFSLMaSNPASRKKFADSIVSFLRKYGF-DGIDIDWE 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  319 YPGGgganpnlgNANDGETYVTLMRELRAMLDElsAETGRTYELTSAI-GIDAQKMAKVDYQAAQQYMDYIFLMSYDFNG 397
Cdd:pfam00704 114 YPGG--------NPEDKENYDLLLRELRAALDE--AKGGKKYLLSAAVpASYPDLDKGYDLPKIAKYLDFINVMTYDFHG 183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  398 GWtNTELGHQTNLYEaswdpDTRYTTDKGVKALLTQGVTPGKIVVGAAMYGRGWTGVNGYtgnnpftgtatgkvKGTWED 477
Cdd:pfam00704 184 SW-DNVTGHHAPLYG-----GGSYNVDYAVKYYLKQGVPASKLVLGVPFYGRSWTLVNGS--------------GNTWED 243
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  478 GIVDYRQIVNEYMGSGWTYSYDETAEAPSLFKASTgdLITFDDARSVKAKGQYVLANQLGGLFAWEIDAD 547
Cdd:pfam00704 244 GVLAYKEICNLLKDNGATVVWDDVAKAPYVYDGDQ--FITYDDPRSIATKVDYVKAKGLGGVMIWSLDAD 311
ChitinaseA_N pfam08329
Chitinase A, N-terminal domain; This domain is found in a number of bacterial chitinases and ...
28-155 9.65e-66

Chitinase A, N-terminal domain; This domain is found in a number of bacterial chitinases and similar viral proteins. It is organized into a fibronectin III module domain-like fold, comprising only beta strands. Its function is not known, but it may be involved in interaction with the enzyme substrate, chitin. It is separated by a hinge region from the catalytic domain (pfam00704); this hinge region is probably mobile, allowing the N-terminal domain to have different relative positions in solution.


Pssm-ID: 400568  Cd Length: 130  Bit Score: 215.40  E-value: 9.65e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660   28 AAPGKPTIGWGETKFAIIEVNQAATAYNQLVTIKDAADVSVSWNLWSGDVGNKAQVLLNGNVAWEGPTGASGTANFKVNK 107
Cdd:pfam08329   1 AAPGTPSIDWGETNFAIIEVNQEATAYNNLVKVKDQADVSVSWNVWSGDIGDSAKVLFDGVQVWEGAASGSTTATFKVRK 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 501152660  108 GGRYQMQVQLCNSDGCTASDAKEILVADTDGSHLVPLNAPLKENNRPY 155
Cdd:pfam08329  81 GGRYQMQVELCNGEGCSKSAPKEIVVADTDGSHLKPLEMNVDENNKPY 128
E_set_Chitinase_N cd02848
N-terminal Early set domain associated with the catalytic domain of chitinase; E or "early" ...
30-132 2.37e-46

N-terminal Early set domain associated with the catalytic domain of chitinase; E or "early" set domains are associated with the catalytic domain of chitinase at the N-terminal end. Chitinases hydrolyze the abundant natural biopolymer chitin, producing smaller chito-oligosaccharides. Chitin consists of multiple N-acetyl-D-glucosamine (NAG) residues connected via beta-1,4-glycosidic linkages and is an important structural element of fungal cell wall and arthropod exoskeletons. On the basis of the mode of chitin hydrolysis, chitinases are classified as random, endo-, and exo-chitinases and belong to families 18 and 19 of glycosyl hydrolases based on sequence criteria. The N-terminal domain of chitinase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.


Pssm-ID: 199880  Cd Length: 105  Bit Score: 160.99  E-value: 2.37e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  30 PGKPTIGWGETKFAIIEVNQAA-TAYNQLVTIKDAADVSVSWNLWSGDVGNKAQVLLNGNVAWEGP-TGASGTANFKVNK 107
Cdd:cd02848    1 PGTPSIAWGETKFSFVEVNQAAtTSYKDLVKRKDAADVPVSWDVWSGETGTTWKVLLDGVVVWSGSiTGSSGTASFEVSK 80
                         90       100
                 ....*....|....*....|....*
gi 501152660 108 GGRYQMQVQLCNSDGCTASDAKEIL 132
Cdd:cd02848   81 GGRYQMTVELCNADGCSTSAPKEIV 105
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
570-809 5.31e-43

myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.


Pssm-ID: 468355 [Multi-domain]  Cd Length: 1597  Bit Score: 170.22  E-value: 5.31e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  570 NKAPIANAGADVNVTGPTDVVLNGSGSRDPENEALTYLWTQVSGPTIAITNADMANAAIQLAATQTDVAYSFSLKVTDPE 649
Cdd:NF038112 1185 NRRPVANAGPDQTVLERTTVTLNGSGSFDPDGDPLTYAWTQVSGPAVTLTGADTATPSFTAPEVTADTVLTFQLVVSDGT 1264
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  650 GLSATDSVTVTnkADTPNQAPVVSVAATATVEAGKTVSIVASASDADGDALTYAWTVPAG--VSATGQNSATLVVTGPNV 727
Cdd:NF038112 1265 KTSAPDTVTVL--VRNVNRAPVAVAGAPATVDERSTVTLDGSGTDADGDALTYAWTQTSGpaVTLTGATTATATFTAPEV 1342
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  728 TEATSYGLSVLVSDGALDASASTNLTVT----PKVIGGGCDATdPNAGNYPAWQTSVVYNTGDTVSHSqlvwkakyWTQG 803
Cdd:NF038112 1343 TADTQLTFTLTVSDGTASATDTVTVTVRnvnrAPVANAGADQT-VDERSTVTLSGSATDPDGDALTYA--------WTQT 1413

                  ....*.
gi 501152660  804 NTPSRT 809
Cdd:NF038112 1414 AGPTVT 1419
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
565-766 1.08e-41

myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.


Pssm-ID: 468355 [Multi-domain]  Cd Length: 1597  Bit Score: 165.99  E-value: 1.08e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  565 TTPPVNKAPIANAGADVNVTGPTDVVLNGSGSrDPENEALTYLWTQVSGPTIAITNADMANAAIQLAATQTDVAYSFSLK 644
Cdd:NF038112 1368 TVRNVNRAPVANAGADQTVDERSTVTLSGSAT-DPDGDALTYAWTQTAGPTVTLTGADTATASFTAPEVAADTELTFQLT 1446
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  645 VTDPEGLSATDSVTVTnkADTPNQAPVVSVAATATVEAGKTVSIVASASDADGDALTYAWTVPAG--VSATGQNSATLVV 722
Cdd:NF038112 1447 VSADGQASADVTVTVT--VRNVNRAPVAHAGESITVDEGSTVTLDASATDPDGDTLTYAWTQVAGpsVTLTGADSAKLTF 1524
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 501152660  723 TGPNVTEATSYGLSVLVSDGALdASASTNLTVTPKVI-----GGGCDAT 766
Cdd:NF038112 1525 TAPEVSADTTLTFSLTVTDGSG-SSGPVVVTVTVKNVnrapdGGGCSST 1572
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
569-755 1.12e-37

myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.


Pssm-ID: 468355 [Multi-domain]  Cd Length: 1597  Bit Score: 153.27  E-value: 1.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  569 VNKAPIANAGADVNVTGPTDVVLNGSGSrDPENEALTYLWTQVSGPTIAITNADMANAAIQLAATQTDVAYSFSLKVTDP 648
Cdd:NF038112 1279 VNRAPVAVAGAPATVDERSTVTLDGSGT-DADGDALTYAWTQTSGPAVTLTGATTATATFTAPEVTADTQLTFTLTVSDG 1357
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  649 EgLSATDSVTVTNKadTPNQAPVVSVAATATVEAGKTVSIVASASDADGDALTYAWTVPAG--VSATGQNSATLVVTGPN 726
Cdd:NF038112 1358 T-ASATDTVTVTVR--NVNRAPVANAGADQTVDERSTVTLSGSATDPDGDALTYAWTQTAGptVTLTGADTATASFTAPE 1434
                         170       180       190
                  ....*....|....*....|....*....|
gi 501152660  727 VTEATSYGLSVLVSDGALDASAST-NLTVT 755
Cdd:NF038112 1435 VAADTELTFQLTVSADGQASADVTvTVTVR 1464
ChiC_BD cd12215
Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of ...
774-815 1.22e-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: 59.89  E-value: 1.22e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 501152660 774 PAWQTSVVYNTGDTVSHSQLVWKAKYWTQGNTPSRTADQWQL 815
Cdd:cd12215    1 PAWDASTVYTGGDQVTYNGKVYEAKWWTQGEEPGTSWGVWKL 42
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
655-755 3.96e-11

myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.


Pssm-ID: 468355 [Multi-domain]  Cd Length: 1597  Bit Score: 67.37  E-value: 3.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  655 DSVTVTNKADTP-----------NQAPVVSVAATATVEAGKTVSIVASAS-DADGDALTYAWTVPAG--VSATGQNSATL 720
Cdd:NF038112 1162 DDLKFTGITNTPftslvaepgvcNRRPVANAGPDQTVLERTTVTLNGSGSfDPDGDPLTYAWTQVSGpaVTLTGADTATP 1241
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 501152660  721 VVTGPNVTEATSYGLSVLVSDGAlDASASTNLTVT 755
Cdd:NF038112 1242 SFTAPEVTADTVLTFQLVVSDGT-KTSAPDTVTVL 1275
ChiC_BD cd12215
Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of ...
823-861 2.46e-10

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: 56.04  E-value: 2.46e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 501152660 823 WDASVVYNGGQTTSYNGRVWKASYWTKGDVPGVAA-VWVD 861
Cdd:cd12215    3 WDASTVYTGGDQVTYNGKVYEAKWWTQGEEPGTSWgVWKL 42
ChtBD3 smart00495
Chitin-binding domain type 3;
773-813 3.64e-09

Chitin-binding domain type 3;


Pssm-ID: 197760 [Multi-domain]  Cd Length: 41  Bit Score: 53.03  E-value: 3.64e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 501152660   773 YPAWQTSVVYNTGDTVSHSQLVWKAKYWTQGNTPSRTADQW 813
Cdd:smart00495   1 APAWQAGTVYTAGDVVSYNGKVYKAKWWTQGEEPGSSSGPW 41
ChtBD3 smart00495
Chitin-binding domain type 3;
823-859 1.35e-07

Chitin-binding domain type 3;


Pssm-ID: 197760 [Multi-domain]  Cd Length: 41  Bit Score: 48.41  E-value: 1.35e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 501152660   823 WDASVVYNGGQTTSYNGRVWKASYWTKGDVPG-VAAVW 859
Cdd:smart00495   4 WQAGTVYTAGDVVSYNGKVYKAKWWTQGEEPGsSSGPW 41
REJ pfam02010
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ...
573-766 3.41e-06

REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor for egg jelly Swiss:Q26627. The function of this domain is unknown. The domain is 600 amino acids long so is probably composed of multiple structural domains. There are six completely conserved cysteine residues that may form disulphide bridges. This region contains tandem PKD-like domains.


Pssm-ID: 366875 [Multi-domain]  Cd Length: 448  Bit Score: 50.58  E-value: 3.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  573 PIANAGADVNVTGPTDVVLNGSGSRDPENE-----ALTYLW--TQVSGPTIAITNADMANAAIQLAATQT---------- 635
Cdd:pfam02010  86 AVIDGGSSRVVGYNQDLTLDGSESYDPDVDpgsssGLTYLWscRRSSSGDNPLLNNDPVCFSDQNEGTLLqstsssltip 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  636 ------DVAYSFSLKVTDPEGLSATDSVTVTNKADTPnqaPVVSVAATATveAGKTVSIVA---------SASDADGDAL 700
Cdd:pfam02010 166 astlqaNVTYTFKLTVSKGSRNSASTTQTILVVDGNP---PIIILSCISN--CNRKNNPVDrlvllastcLNCSSDLSDV 240
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  701 TYAW------------TVPAGVSATGQNSATLVVTGPNVTEATSYGLSVLVS--DGALDASASTNLTVTPKVIGGGCDAT 766
Cdd:pfam02010 241 TYRWlslgsentslvlDQLNSQTSTGRSGPYLVIKAGVLQSGVSYRFTLIVTvyPGLVSGLASISFITNAPPTGGTCSVT 320
tand_rpt_95 NF012211
tandem-95 repeat; This 95-amino acid repeat occurs in tandem in proteins that may be several ...
687-756 1.37e-04

tandem-95 repeat; This 95-amino acid repeat occurs in tandem in proteins that may be several thousand amino acids long.


Pssm-ID: 333740 [Multi-domain]  Cd Length: 98  Bit Score: 41.85  E-value: 1.37e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501152660 687 SIVASASDADGDALTYawtvpAGVSATGQNSATLVVTG-------PNVTEATSYGLSVLVSDGALDASAST-NLTVTP 756
Cdd:NF012211  14 QLLANASDVDGDDLTV-----SNVSYSGPTNGTVTDNGdgtytytPNENFNGDDSFTYTVSDGTGATATATvFVTVNP 86
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
66-134 5.74e-03

Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.


Pssm-ID: 214510 [Multi-domain]  Cd Length: 79  Bit Score: 36.66  E-value: 5.74e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501152660    66 VSVSWNLWSGDVGNKAQV-----LLNGNVAWE-----GPTGASGTANFKVNKGGRYQMQVQLCNSDGcTASDAKEILVA 134
Cdd:smart00089   2 ADVSASPTVGVAGESVTFtatssDDGSIVSYTwdfgdGTSSTGPTVTHTYTKPGTYTVTLTVTNAVG-SASATVTVVVQ 79
 
Name Accession Description Interval E-value
ChiA COG3325
Chitinase, GH18 family [Carbohydrate transport and metabolism];
143-559 3.69e-165

Chitinase, GH18 family [Carbohydrate transport and metabolism];


Pssm-ID: 442554 [Multi-domain]  Cd Length: 391  Bit Score: 485.57  E-value: 3.69e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 143 PLNAPLKENNRPYINKSGKVVGSYFVEWGVYGRKFPVDKIPAQNLTHILYGFTPICggdgindslkeidgsfqalqracs 222
Cdd:COG3325    1 SATASVSDTAAAATATSGKRVVGYFTQWGIYGRNYLVKDIPASKLTHINYAFANVD------------------------ 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 223 grEDFKVAIHDPWAAVQMPQAGVsDYSDPYKGNFGQLMALKQAHPDLKILPSVGGWTLSDPFFY-FGDKSKRDTFVASVK 301
Cdd:COG3325   57 --PDGKCSVGDAWAKPSVDGAAD-DWDQPLKGNFNQLKKLKAKNPNLKVLISIGGWTWSKGFSDaAATPASRAAFVDSCV 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 302 EFLQTWKFfDGVDIDWEYPGGGGANPNLGNANDGETYVTLMRELRAMLDELSAETGRTYELTSAIGIDAQKMAKVDYQAA 381
Cdd:COG3325  134 DLLRKYNF-DGIDIDWEYPGSGGAPGNVYRPEDKANFTALLKELRAQLDALGAETGKHYLLTAAAPAGPDKLDGIELPKV 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 382 QQYMDYIFLMSYDFNGGWTNTeLGHQTNLYEASWDP-DTRYTTDKGVKALLTQGVTPGKIVVGAAMYGRGWTGVNGytGN 460
Cdd:COG3325  213 AQYLDYVNVMTYDFHGAWSPT-TGHQAPLYDSPKDPeAQGYSVDSAVQAYLAAGVPASKLVLGVPFYGRGWTGVTG--GN 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 461 NPFTGTATGKVKGTWEDGIVDYRQIVNEYMGS-GWTYSYDETAEAPSLFKASTGDLITFDDARSVKAKGQYVLANQLGGL 539
Cdd:COG3325  290 NGLYQPATGPAPGTWEAGVNDYKDLKALYLGSnGYTRYWDDVAKAPYLYNGDTGTFISYDDPRSIAAKADYVKDKGLGGV 369
                        410       420
                 ....*....|....*....|..
gi 501152660 540 FAWEIDAD--NGDILNAMHEGL 559
Cdd:COG3325  370 MFWELSGDtaDGTLLNAIGEGL 391
GH18_chitinase cd06548
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ...
163-547 1.54e-132

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: 398.93  E-value: 1.54e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 163 VGSYFVEWGVYGRKFPV-DKIPAQNLTHILYGFTPICGGDGINDSLKEIDGsfqalqracsgredfkvaihdpwAAVQMP 241
Cdd:cd06548    1 VVGYFTNWGIYGRNYFVtDDIPADKLTHINYAFADIDGDGGVVTSDDEAAD-----------------------EAAQSV 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 242 QAGVSDYSDPYKGNFGQLMALKQAHPDLKILPSVGGWTLSDPFFYFG-DKSKRDTFVASVKEFLQTWkFFDGVDIDWEYP 320
Cdd:cd06548   58 DGGADTDDQPLKGNFGQLRKLKQKNPHLKILLSIGGWTWSGGFSDAAaTEASRAKFADSAVDFIRKY-GFDGIDIDWEYP 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 321 GGGGANPNLGNANDGETYVTLMRELRAMLDELSAETGRTYELTSAIGIDAQKMAKVDYQAAQQYMDYIFLMSYDFNGGWT 400
Cdd:cd06548  137 GSGGAPGNVARPEDKENFTLLLKELREALDALGAETGRKYLLTIAAPAGPDKLDKLEVAEIAKYLDFINLMTYDFHGAWS 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 401 NTeLGHQTNLYEASWDPDTRYTTDKGVKALLTQGVTPGKIVVGAAMYGRGWTgvngytgnnpftgtatgkvkgtwedgiv 480
Cdd:cd06548  217 NT-TGHHSNLYASPADPPGGYSVDAAVNYYLSAGVPPEKLVLGVPFYGRGWT---------------------------- 267
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501152660 481 dyrqivneymgsGWTYSYDETAEAPSLFKASTGDLITFDDARSVKAKGQYVLANQLGGLFAWEIDAD 547
Cdd:cd06548  268 ------------GYTRYWDEVAKAPYLYNPSTKTFISYDDPRSIKAKADYVKDKGLGGVMFWELSGD 322
Glyco_18 smart00636
Glyco_18 domain;
161-547 1.02e-125

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 381.64  E-value: 1.02e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660   161 KVVGsYFVEWGVYGRKFPVDKIPAQNLTHILYGFTPICGgdgindslkeidgsfqalqracsgreDFKVAIHDPWAAVqm 240
Cdd:smart00636   1 RVVG-YFTNWGVYGRNFPVDDIPASKLTHIIYAFANIDP--------------------------DGTVTIGDEWADI-- 51
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660   241 pqagvsdysdpykGNFGQLMALKQAHPDLKILPSVGGWTLSDPFFYF-GDKSKRDTFVASVKEFLQTWKFfDGVDIDWEY 319
Cdd:smart00636  52 -------------GNFGQLKALKKKNPGLKVLLSIGGWTESDNFSSMlSDPASRKKFIDSIVSFLKKYGF-DGIDIDWEY 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660   320 PGGGGAnpnlgnanDGETYVTLMRELRAMLDELSAEtGRTYELTSAIGIDAQKMAKVD--YQAAQQYMDYIFLMSYDFNG 397
Cdd:smart00636 118 PGGRGD--------DRENYTALLKELREALDKEGAE-GKGYLLTIAVPAGPDKIDKGYgdLPAIAKYLDFINLMTYDFHG 188
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660   398 GWTNTeLGHQTNLYEASWDPdTRYTTDKGVKALLTQGVTPGKIVVGAAMYGRGWTGVNGY--TGNNPFTGTATGkVKGTW 475
Cdd:smart00636 189 AWSNP-TGHNAPLYAGPGDP-EKYNVDYAVKYYLCKGVPPSKLVLGIPFYGRGWTLVDGSnnGPGAPFTGPATG-GPGTW 265
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501152660   476 EDGIVDYRQIVNEYmgsGWTYSYDETAEAPSLFKASTGDLITFDDARSVKAKGQYVLANQLGGLFAWEIDAD 547
Cdd:smart00636 266 EGGVVDYREICKLL---GATVVYDDTAKAPYAYNPGTGQWVSYDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
161-547 2.78e-93

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 295.90  E-value: 2.78e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  161 KVVGsYFVEWGVYGRKfpvDKIPAQNLTHILYGFTPICGGDGindslkeidgsfqalqracsgredfKVAIHDPwaavqm 240
Cdd:pfam00704   1 RIVG-YYTSWGVYRNG---NFLPSDKLTHIIYAFANIDGSDG-------------------------TLFIGDW------ 45
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  241 pqagvsdysdpYKGNFGQLMALK-QAHPDLKILPSVGGWTLSDPFFYF-GDKSKRDTFVASVKEFLQTWKFfDGVDIDWE 318
Cdd:pfam00704  46 -----------DLGNFEQLKKLKkQKNPGVKVLLSIGGWTDSTGFSLMaSNPASRKKFADSIVSFLRKYGF-DGIDIDWE 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  319 YPGGgganpnlgNANDGETYVTLMRELRAMLDElsAETGRTYELTSAI-GIDAQKMAKVDYQAAQQYMDYIFLMSYDFNG 397
Cdd:pfam00704 114 YPGG--------NPEDKENYDLLLRELRAALDE--AKGGKKYLLSAAVpASYPDLDKGYDLPKIAKYLDFINVMTYDFHG 183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  398 GWtNTELGHQTNLYEaswdpDTRYTTDKGVKALLTQGVTPGKIVVGAAMYGRGWTGVNGYtgnnpftgtatgkvKGTWED 477
Cdd:pfam00704 184 SW-DNVTGHHAPLYG-----GGSYNVDYAVKYYLKQGVPASKLVLGVPFYGRSWTLVNGS--------------GNTWED 243
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  478 GIVDYRQIVNEYMGSGWTYSYDETAEAPSLFKASTgdLITFDDARSVKAKGQYVLANQLGGLFAWEIDAD 547
Cdd:pfam00704 244 GVLAYKEICNLLKDNGATVVWDDVAKAPYVYDGDQ--FITYDDPRSIATKVDYVKAKGLGGVMIWSLDAD 311
ChitinaseA_N pfam08329
Chitinase A, N-terminal domain; This domain is found in a number of bacterial chitinases and ...
28-155 9.65e-66

Chitinase A, N-terminal domain; This domain is found in a number of bacterial chitinases and similar viral proteins. It is organized into a fibronectin III module domain-like fold, comprising only beta strands. Its function is not known, but it may be involved in interaction with the enzyme substrate, chitin. It is separated by a hinge region from the catalytic domain (pfam00704); this hinge region is probably mobile, allowing the N-terminal domain to have different relative positions in solution.


Pssm-ID: 400568  Cd Length: 130  Bit Score: 215.40  E-value: 9.65e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660   28 AAPGKPTIGWGETKFAIIEVNQAATAYNQLVTIKDAADVSVSWNLWSGDVGNKAQVLLNGNVAWEGPTGASGTANFKVNK 107
Cdd:pfam08329   1 AAPGTPSIDWGETNFAIIEVNQEATAYNNLVKVKDQADVSVSWNVWSGDIGDSAKVLFDGVQVWEGAASGSTTATFKVRK 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 501152660  108 GGRYQMQVQLCNSDGCTASDAKEILVADTDGSHLVPLNAPLKENNRPY 155
Cdd:pfam08329  81 GGRYQMQVELCNGEGCSKSAPKEIVVADTDGSHLKPLEMNVDENNKPY 128
GH18_chitolectin_chitotriosidase cd02872
This conserved domain family includes a large number of catalytically inactive chitinase-like ...
163-547 1.07e-64

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: 221.28  E-value: 1.07e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 163 VGSYFVEWGVY--GR-KFPVDKIPAQNLTHILYGFTpicggdGINDslkeiDGSFQALqracsgredfkvaihDPWAAVQ 239
Cdd:cd02872    1 VVCYFTNWAQYrpGNgKFVPENIDPFLCTHIIYAFA------GLNP-----DGNIIIL---------------DEWNDID 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 240 mpqagvsdysdpyKGNFGQLMALKQAHPDLKILPSVGGWTLSDPFF--YFGDKSKRDTFVASVKEFLQTWKFfDGVDIDW 317
Cdd:cd02872   55 -------------LGLYERFNALKEKNPNLKTLLAIGGWNFGSAKFsaMAASPENRKTFIKSAIAFLRKYGF-DGLDLDW 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 318 EYPGGGGanpnlGNANDGETYVTLMRELRamlDELSAETGRtYELTSAIGiDAQKMAKVDYQAAQ--QYMDYIFLMSYDF 395
Cdd:cd02872  121 EYPGQRG-----GPPEDKENFVTLLKELR---EAFEPEAPR-LLLTAAVS-AGKETIDAAYDIPEisKYLDFINVMTYDF 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 396 NGGWTNTeLGHQTNLYEASWDPDTR--YTTDKGVKALLTQGVTPGKIVVGAAMYGRGWTGVNG-YTGNN-PFTGTATgkv 471
Cdd:cd02872  191 HGSWEGV-TGHNSPLYAGSADTGDQkyLNVDYAIKYWLSKGAPPEKLVLGIPTYGRSFTLASPsNTGVGaPASGPGT--- 266
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501152660 472 KG--TWEDGIVDYRQIVnEYMGSGWTYSYDETAEAPSLFKastGDL-ITFDDARSVKAKGQYVLANQLGGLFAWEIDAD 547
Cdd:cd02872  267 AGpyTREAGFLAYYEIC-EFLKSGWTVVWDDEQKVPYAYK---GNQwVGYDDEESIALKVQYLKSKGLGGAMVWSIDLD 341
E_set_Chitinase_N cd02848
N-terminal Early set domain associated with the catalytic domain of chitinase; E or "early" ...
30-132 2.37e-46

N-terminal Early set domain associated with the catalytic domain of chitinase; E or "early" set domains are associated with the catalytic domain of chitinase at the N-terminal end. Chitinases hydrolyze the abundant natural biopolymer chitin, producing smaller chito-oligosaccharides. Chitin consists of multiple N-acetyl-D-glucosamine (NAG) residues connected via beta-1,4-glycosidic linkages and is an important structural element of fungal cell wall and arthropod exoskeletons. On the basis of the mode of chitin hydrolysis, chitinases are classified as random, endo-, and exo-chitinases and belong to families 18 and 19 of glycosyl hydrolases based on sequence criteria. The N-terminal domain of chitinase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.


Pssm-ID: 199880  Cd Length: 105  Bit Score: 160.99  E-value: 2.37e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  30 PGKPTIGWGETKFAIIEVNQAA-TAYNQLVTIKDAADVSVSWNLWSGDVGNKAQVLLNGNVAWEGP-TGASGTANFKVNK 107
Cdd:cd02848    1 PGTPSIAWGETKFSFVEVNQAAtTSYKDLVKRKDAADVPVSWDVWSGETGTTWKVLLDGVVVWSGSiTGSSGTASFEVSK 80
                         90       100
                 ....*....|....*....|....*
gi 501152660 108 GGRYQMQVQLCNSDGCTASDAKEIL 132
Cdd:cd02848   81 GGRYQMTVELCNADGCSTSAPKEIV 105
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
570-809 5.31e-43

myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.


Pssm-ID: 468355 [Multi-domain]  Cd Length: 1597  Bit Score: 170.22  E-value: 5.31e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  570 NKAPIANAGADVNVTGPTDVVLNGSGSRDPENEALTYLWTQVSGPTIAITNADMANAAIQLAATQTDVAYSFSLKVTDPE 649
Cdd:NF038112 1185 NRRPVANAGPDQTVLERTTVTLNGSGSFDPDGDPLTYAWTQVSGPAVTLTGADTATPSFTAPEVTADTVLTFQLVVSDGT 1264
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  650 GLSATDSVTVTnkADTPNQAPVVSVAATATVEAGKTVSIVASASDADGDALTYAWTVPAG--VSATGQNSATLVVTGPNV 727
Cdd:NF038112 1265 KTSAPDTVTVL--VRNVNRAPVAVAGAPATVDERSTVTLDGSGTDADGDALTYAWTQTSGpaVTLTGATTATATFTAPEV 1342
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  728 TEATSYGLSVLVSDGALDASASTNLTVT----PKVIGGGCDATdPNAGNYPAWQTSVVYNTGDTVSHSqlvwkakyWTQG 803
Cdd:NF038112 1343 TADTQLTFTLTVSDGTASATDTVTVTVRnvnrAPVANAGADQT-VDERSTVTLSGSATDPDGDALTYA--------WTQT 1413

                  ....*.
gi 501152660  804 NTPSRT 809
Cdd:NF038112 1414 AGPTVT 1419
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
565-766 1.08e-41

myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.


Pssm-ID: 468355 [Multi-domain]  Cd Length: 1597  Bit Score: 165.99  E-value: 1.08e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  565 TTPPVNKAPIANAGADVNVTGPTDVVLNGSGSrDPENEALTYLWTQVSGPTIAITNADMANAAIQLAATQTDVAYSFSLK 644
Cdd:NF038112 1368 TVRNVNRAPVANAGADQTVDERSTVTLSGSAT-DPDGDALTYAWTQTAGPTVTLTGADTATASFTAPEVAADTELTFQLT 1446
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  645 VTDPEGLSATDSVTVTnkADTPNQAPVVSVAATATVEAGKTVSIVASASDADGDALTYAWTVPAG--VSATGQNSATLVV 722
Cdd:NF038112 1447 VSADGQASADVTVTVT--VRNVNRAPVAHAGESITVDEGSTVTLDASATDPDGDTLTYAWTQVAGpsVTLTGADSAKLTF 1524
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 501152660  723 TGPNVTEATSYGLSVLVSDGALdASASTNLTVTPKVI-----GGGCDAT 766
Cdd:NF038112 1525 TAPEVSADTTLTFSLTVTDGSG-SSGPVVVTVTVKNVnrapdGGGCSST 1572
GH18_chitinase-like cd00598
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ...
166-398 2.22e-38

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: 142.13  E-value: 2.22e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 166 YFVEWGVYgRKFPVDKIPAQNLTHILYGFTPICGGDGINdslkeidgsfqalqracsgredfkvaihdpwaavqmpqAGV 245
Cdd:cd00598    4 YYDGWSSG-RGPDPTDIPLSLCTHIIYAFAEISSDGSLN--------------------------------------LFG 44
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 246 SDYSDPYKGNFGQLMALKqahPDLKILPSVGGWTLSDPFFYFGDKSKRDTFVASVKEFLQTWKfFDGVDIDWEYPGGGGa 325
Cdd:cd00598   45 DKSEEPLKGALEELASKK---PGLKVLISIGGWTDSSPFTLASDPASRAAFANSLVSFLKTYG-FDGVDIDWEYPGAAD- 119
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501152660 326 npnlgnANDGETYVTLMRELRAMLDElsaetgRTYELTSAIGIDAQ-KMAKVDYQAAQQYMDYIFLMSYDFNGG 398
Cdd:cd00598  120 ------NSDRENFITLLRELRSALGA------ANYLLTIAVPASYFdLGYAYDVPAIGDYVDFVNVMTYDLVLG 181
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
569-755 1.12e-37

myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.


Pssm-ID: 468355 [Multi-domain]  Cd Length: 1597  Bit Score: 153.27  E-value: 1.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  569 VNKAPIANAGADVNVTGPTDVVLNGSGSrDPENEALTYLWTQVSGPTIAITNADMANAAIQLAATQTDVAYSFSLKVTDP 648
Cdd:NF038112 1279 VNRAPVAVAGAPATVDERSTVTLDGSGT-DADGDALTYAWTQTSGPAVTLTGATTATATFTAPEVTADTQLTFTLTVSDG 1357
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  649 EgLSATDSVTVTNKadTPNQAPVVSVAATATVEAGKTVSIVASASDADGDALTYAWTVPAG--VSATGQNSATLVVTGPN 726
Cdd:NF038112 1358 T-ASATDTVTVTVR--NVNRAPVANAGADQTVDERSTVTLSGSATDPDGDALTYAWTQTAGptVTLTGADTATASFTAPE 1434
                         170       180       190
                  ....*....|....*....|....*....|
gi 501152660  727 VTEATSYGLSVLVSDGALDASAST-NLTVT 755
Cdd:NF038112 1435 VAADTELTFQLTVSADGQASADVTvTVTVR 1464
GH18_plant_chitinase_class_V cd02879
The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the ...
162-552 8.54e-27

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: 111.30  E-value: 8.54e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 162 VVGSYfveWGVYGRKFPVDKIPAQNLTHILYGFTpicggdgindslkEIDGSfqalqracsgreDFKVAIhDPWAAVQMp 241
Cdd:cd02879    4 VKGGY---WPAWSEEFPPSNIDSSLFTHLFYAFA-------------DLDPS------------TYEVVI-SPSDESEF- 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 242 qagvSDYSDpykgnfgqlmALKQAHPDLKILPSVGGWTLSDPFFYF--GDKSKRDTFV-ASVKEFLQtwKFFDGVDIDWE 318
Cdd:cd02879   54 ----STFTE----------TVKRKNPSVKTLLSIGGGGSDSSAFAAmaSDPTARKAFInSSIKVARK--YGFDGLDLDWE 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 319 YPGggganpnlgNANDGETYVTLMRELRAMLDELSAETGRT-YELTSAI---GIDAQKMAKVDY--QAAQQYMDYIFLMS 392
Cdd:cd02879  118 FPS---------SQVEMENFGKLLEEWRAAVKDEARSSGRPpLLLTAAVyfsPILFLSDDSVSYpiEAINKNLDWVNVMA 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 393 YDFNGGWTNTELGHQTNLYeaswDPDTRYTTDKGVKALLTQGVTPGKIVVGAAMYGRGWTGVNGYTGnnpftgtatgkvk 472
Cdd:cd02879  189 YDYYGSWESNTTGPAAALY----DPNSNVSTDYGIKSWIKAGVPAKKLVLGLPLYGRAWTLYDTTTV------------- 251
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 473 gtwedgiVDYrqivnEYMGSGWtysydetaeapslfkastgdlITFDDARSVKAKGQYVLANQLGGLFAWEIDADNGDIL 552
Cdd:cd02879  252 -------SSY-----VYAGTTW---------------------IGYDDVQSIAVKVKYAKQKGLLGYFAWAVGYDDNNWL 298
GH18_zymocin_alpha cd02878
Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle ...
178-480 1.22e-19

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: 91.22  E-value: 1.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 178 PVDKIPAQNLTHILYGFTPIcggdgindslkeidgsfqalqracsgREDFKVAIhdpwaavqmpqagvsdysDPYKGNFG 257
Cdd:cd02878   19 DVTQIDTSKYTHIHFAFANI--------------------------TSDFSVDV------------------SSVQEQFS 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 258 QLMALKqahpDLKILPSVGGWTLS-DPFFY--FGDKSK---RDTFVASVKEFLQTWKFfDGVDIDWEYPGGgganPNL-- 329
Cdd:cd02878   55 DFKKLK----GVKKILSFGGWDFStSPSTYqiFRDAVKpanRDTFANNVVNFVNKYNL-DGVDFDWEYPGA----PDIpg 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 330 ---GNANDGETYVTLMRELRAMLDE---LSAETGRTYELTSAIGIDaqKMAKvdyqaaqqYMDYIFLMSYDFNGGW---- 399
Cdd:cd02878  126 ipaGDPDDGKNYLEFLKLLKSKLPSgksLSIAAPASYWYLKGFPIK--DMAK--------YVDYIVYMTYDLHGQWdygn 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 400 --------TNTELGHQTNLYEaswdpdtryTTDkgVKALLTQ-GVTPGKIVVGAAMYGR-------GWTGVN-GYTGnnP 462
Cdd:cd02878  196 kwaspgcpAGNCLRSHVNKTE---------TLD--ALSMITKaGVPSNKVVVGVASYGRsfkmadpGCTGPGcTFTG--P 262
                        330
                 ....*....|....*...
gi 501152660 463 FTGTATGKVKGTWEDGIV 480
Cdd:cd02878  263 GSGAEAGRCTCTAGYGAI 280
GH18_IDGF cd02873
The IDGF's (imaginal disc growth factors) are a family of growth factors identified in insects ...
181-462 5.77e-16

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: 81.21  E-value: 5.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 181 KIPAQNLTHILYGFTpicggdGINDslkeidgsfqalqracsgrEDFKVAIHDPwaavqmpqagvsdYSDPYKGNFGQLM 260
Cdd:cd02873   25 EPALQFCTHLVYGYA------GIDA-------------------DTYKIKSLNE-------------DLDLDKSHYRAIT 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 261 ALKQAHPDLKILPSVGGWTLSDPFFYF-------GDKSKRDTFVASVKEFLQTWKfFDGVDIDWEYP------------- 320
Cdd:cd02873   67 SLKRKYPHLKVLLSVGGDRDTDEEGENekyllllESSESRNAFINSAHSLLKTYG-FDGLDLAWQFPknkpkkvrgtfgs 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 321 ----------GGGGANPNlgNANDGETYVTLMRELRAMLdelsaeTGRTYELT--------SAIGIDAQKMAkvdyqaaq 382
Cdd:cd02873  146 awhsfkklftGDSVVDEK--AAEHKEQFTALVRELKNAL------RPDGLLLTltvlphvnSTWYFDVPAIA-------- 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 383 QYMDYIFLMSYDFNGGWTNTELGHQTN-LYEASwDPDTRYTTDKGVKALLTQGVTPGKIVVGAAMYGRGW--TGVNGYTG 459
Cdd:cd02873  210 NNVDFVNLATFDFLTPERNPEEADYTApIYELY-ERNPHHNVDYQVKYWLNQGTPASKLNLGIATYGRAWklTKDSGITG 288

                 ...
gi 501152660 460 NNP 462
Cdd:cd02873  289 VPP 291
ChiC_BD cd12215
Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of ...
774-815 1.22e-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: 59.89  E-value: 1.22e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 501152660 774 PAWQTSVVYNTGDTVSHSQLVWKAKYWTQGNTPSRTADQWQL 815
Cdd:cd12215    1 PAWDASTVYTGGDQVTYNGKVYEAKWWTQGEEPGTSWGVWKL 42
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
655-755 3.96e-11

myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.


Pssm-ID: 468355 [Multi-domain]  Cd Length: 1597  Bit Score: 67.37  E-value: 3.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  655 DSVTVTNKADTP-----------NQAPVVSVAATATVEAGKTVSIVASAS-DADGDALTYAWTVPAG--VSATGQNSATL 720
Cdd:NF038112 1162 DDLKFTGITNTPftslvaepgvcNRRPVANAGPDQTVLERTTVTLNGSGSfDPDGDPLTYAWTQVSGpaVTLTGADTATP 1241
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 501152660  721 VVTGPNVTEATSYGLSVLVSDGAlDASASTNLTVT 755
Cdd:NF038112 1242 SFTAPEVTADTVLTFQLVVSDGT-KTSAPDTVTVL 1275
ChiC_BD cd12215
Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of ...
823-861 2.46e-10

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: 56.04  E-value: 2.46e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 501152660 823 WDASVVYNGGQTTSYNGRVWKASYWTKGDVPGVAA-VWVD 861
Cdd:cd12215    3 WDASTVYTGGDQVTYNGKVYEAKWWTQGEEPGTSWgVWKL 42
GH18_CFLE_spore_hydrolase cd02874
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ...
287-555 3.03e-10

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: 62.28  E-value: 3.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 287 FGDKSKRDTFVASVKEFLQTWKFfDGVDIDWEYPgggganpnlgNANDGETYVTLMRELRAMLDE-----LSAETGRTYE 361
Cdd:cd02874   82 LSNPEARQRLINNILALAKKYGY-DGVNIDFENV----------PPEDREAYTQFLRELSDRLHPagytlSTAVVPKTSA 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 362 LTSAIGIDAQkmakvDYQAAQQYMDYIFLMSYDFngGWTNTELGHQTNLyeaSWdpdtrytTDKGVKALLTQgVTPGKIV 441
Cdd:cd02874  151 DQFGNWSGAY-----DYAAIGKIVDFVVLMTYDW--HWRGGPPGPVAPI---GW-------VERVLQYAVTQ-IPREKIL 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 442 VGAAMYGRGWTGvngytgNNPFTGTATGkvkgtwedgiVDYRQIVNEYMGSGWTYSYDETAEAPslFKASTGDL-----I 516
Cdd:cd02874  213 LGIPLYGYDWTL------PYKKGGKAST----------ISPQQAINLAKRYGAEIQYDEEAQSP--FFRYVDEQgrrheV 274
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 501152660 517 TFDDARSVKAKGQYVLANQLGGLFAWEIDADNGDILNAM 555
Cdd:cd02874  275 WFEDARSLQAKFELAKEYGLRGVSYWRLGLEDPQNWLLL 313
ChtBD3 smart00495
Chitin-binding domain type 3;
773-813 3.64e-09

Chitin-binding domain type 3;


Pssm-ID: 197760 [Multi-domain]  Cd Length: 41  Bit Score: 53.03  E-value: 3.64e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 501152660   773 YPAWQTSVVYNTGDTVSHSQLVWKAKYWTQGNTPSRTADQW 813
Cdd:smart00495   1 APAWQAGTVYTAGDVVSYNGKVYKAKWWTQGEEPGSSSGPW 41
GH18_3CO4_chitinase cd06545
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an ...
265-452 4.18e-09

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: 58.23  E-value: 4.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 265 AHP-DLKILPSVGGWTLSDPFFYFGDKSKRDTFVASVKEFLQTWKFfDGVDIDWEYPgggganpnlgnANDGETYVTLMR 343
Cdd:cd06545   55 AHAhNVKILISLAGGSPPEFTAALNDPAKRKALVDKIINYVVSYNL-DGIDVDLEGP-----------DVTFGDYLVFIR 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 344 ELRAMLDElsaetgRTYELTSAIgidAQKMAKVDYQAAQQYMDYIFLMSYDFNGGWTNTELGHQTNLYEASWDPDtrYTT 423
Cdd:cd06545  123 ALYAALKK------EGKLLTAAV---SSWNGGAVSDSTLAYFDFINIMSYDATGPWWGDNPGQHSSYDDAVNDLN--YWN 191
                        170       180
                 ....*....|....*....|....*....
gi 501152660 424 DKGVKAlltqgvtPGKIVVGAAMYGRGWT 452
Cdd:cd06545  192 ERGLAS-------KDKLVLGLPFYGYGFY 213
CBD_like cd12204
Cellulose-binding domain, chitinase and related proteins; This group contains proteins related ...
768-817 1.78e-08

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: 51.17  E-value: 1.78e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 501152660 768 PNAGNYPAWQTSVVYNTGDTVSHSQLVWKAKYWTQgNTPSrTADQWQLLS 817
Cdd:cd12204    1 AGANAYPNWPQGTHAAGGDLVSYNGAVYQAKWWTQ-SAPG-SDSSWTLVC 48
ChtBD3 smart00495
Chitin-binding domain type 3;
823-859 1.35e-07

Chitin-binding domain type 3;


Pssm-ID: 197760 [Multi-domain]  Cd Length: 41  Bit Score: 48.41  E-value: 1.35e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 501152660   823 WDASVVYNGGQTTSYNGRVWKASYWTKGDVPG-VAAVW 859
Cdd:smart00495   4 WQAGTVYTAGDVVSYNGKVYKAKWWTQGEEPGsSSGPW 41
GH18_narbonin cd06544
Narbonin is a plant 2S protein from the globulin fraction of narbon bean (Vicia narbonensis L.) ...
261-345 1.70e-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: 50.45  E-value: 1.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 261 ALKQAHPDLKILPSVGGWTLSDPFFYFGDKSKR---DTFVASVKEFLQTWKfFDGVDIDWEYpgggganpnlgNANDGET 337
Cdd:cd06544   63 SIKAQHPNVKVVISIGGRGVQNNPTPFDPSNVDswvSNAVSSLTSIIQTYN-LDGIDIDYEH-----------FPADPDT 130

                 ....*...
gi 501152660 338 YVTLMREL 345
Cdd:cd06544  131 FVECIGQL 138
GH18_chitobiase cd02875
Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes ...
288-545 2.78e-06

Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes the reducing-end N-acetylglucosamine from the chitobiose core of oligosaccharides during the ordered degradation of asparagine-linked glycoproteins in eukaryotes. Chitobiase can only do so if the asparagine that joins the oligosaccharide to protein is previously removed by a glycosylasparaginase. Chitobiase is therefore the final step in the lysosomal degradation of the protein/carbohydrate linkage component of asparagine-linked glycoproteins. The catalytic domain of chitobiase is an eight-stranded alpha/beta barrel fold similar to that of other family 18 glycosyl hydrolases such as hevamine and chitotriosidase.


Pssm-ID: 119354 [Multi-domain]  Cd Length: 358  Bit Score: 50.51  E-value: 2.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 288 GDKSKRDTFVASVKEFLQTwKFFDGVDIDWEYPgggganpnlgnandgetyVTLMRELRAMLDELSAETGRTYELT---S 364
Cdd:cd02875   92 SNPTYRTQWIQQKVELAKS-QFMDGINIDIEQP------------------ITKGSPEYYALTELVKETTKAFKKEnpgY 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 365 AIGIDAQKMAK------VDYQAAQQYMDYIFLMSYDFNG-GWTNTELGHQTNLYEaswdpdtryTTDKGVKALLTQGVTP 437
Cdd:cd02875  153 QISFDVAWSPScidkrcYDYTGIADASDFLVVMDYDEQSqIWGKECIAGANSPYS---------QTLSGYNNFTKLGIDP 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 438 GKIVVGAAMYGRGWTGVNGYTGNN-------PFTGTATGKVKGTWedgiVDYRQIVNEYMGSGWTYSYDETAEAPSLF-K 509
Cdd:cd02875  224 KKLVMGLPWYGYDYPCLNGNLEDVvctipkvPFRGANCSDAAGRQ----IPYSEIMKQINSSIGGRLWDSEQKSPFYNyK 299
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 501152660 510 ASTGDL--ITFDDARSVKAKGQYVLANQLGGLFAWEID 545
Cdd:cd02875  300 DKQGNLhqVWYDNPQSLSIKVAYAKNLGLKGIGMWNGD 337
REJ pfam02010
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ...
573-766 3.41e-06

REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor for egg jelly Swiss:Q26627. The function of this domain is unknown. The domain is 600 amino acids long so is probably composed of multiple structural domains. There are six completely conserved cysteine residues that may form disulphide bridges. This region contains tandem PKD-like domains.


Pssm-ID: 366875 [Multi-domain]  Cd Length: 448  Bit Score: 50.58  E-value: 3.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  573 PIANAGADVNVTGPTDVVLNGSGSRDPENE-----ALTYLW--TQVSGPTIAITNADMANAAIQLAATQT---------- 635
Cdd:pfam02010  86 AVIDGGSSRVVGYNQDLTLDGSESYDPDVDpgsssGLTYLWscRRSSSGDNPLLNNDPVCFSDQNEGTLLqstsssltip 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  636 ------DVAYSFSLKVTDPEGLSATDSVTVTNKADTPnqaPVVSVAATATveAGKTVSIVA---------SASDADGDAL 700
Cdd:pfam02010 166 astlqaNVTYTFKLTVSKGSRNSASTTQTILVVDGNP---PIIILSCISN--CNRKNNPVDrlvllastcLNCSSDLSDV 240
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  701 TYAW------------TVPAGVSATGQNSATLVVTGPNVTEATSYGLSVLVS--DGALDASASTNLTVTPKVIGGGCDAT 766
Cdd:pfam02010 241 TYRWlslgsentslvlDQLNSQTSTGRSGPYLVIKAGVLQSGVSYRFTLIVTvyPGLVSGLASISFITNAPPTGGTCSVT 320
ChtBD3 cd00036
Chitin/cellulose binding domains of chitinase and related enzymes; This group contains ...
823-861 4.20e-06

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: 44.29  E-value: 4.20e-06
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 501152660 823 WDASVVYNGGQTTSYNGRVWKASYWTKGDVPGVAAVWVD 861
Cdd:cd00036    2 WPNPTHYTAGQSVVYNGNLYTANWYTAGSVPGSDSSWTQ 40
Big_9 pfam17963
Bacterial Ig domain; This entry represents a wide variety of bacterial Ig domains.
652-743 5.91e-06

Bacterial Ig domain; This entry represents a wide variety of bacterial Ig domains.


Pssm-ID: 465590 [Multi-domain]  Cd Length: 90  Bit Score: 45.41  E-value: 5.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  652 SATDSVTVTNkadtPNQAPVVsVAATATVEAGktvSIVASASDADGDALTYAWTVPAGVSATGQNSATLVVTG-----PN 726
Cdd:pfam17963   1 TATVTVTVTP----VNDAPVA-VDDSVTVTED---TVLANDSDPDGDPLTITSLTVTIVTAPANGTVTVNADGtltytPN 72
                          90
                  ....*....|....*..
gi 501152660  727 VTEATSYGLSVLVSDGA 743
Cdd:pfam17963  73 AGFSGTDSFTYTVSDGS 89
PKD_4 pfam18911
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.
570-660 1.03e-05

PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.


Pssm-ID: 436824 [Multi-domain]  Cd Length: 85  Bit Score: 44.57  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  570 NKAPIANAGADVNVTGPTDVVLNGSGSRDPENEALTYLW-----TQVSGPTIAITNADMANaaiqlaatqtdvaYSFSLK 644
Cdd:pfam18911   1 NAAPVADAGGDRIVAEGETVTFDASASDDPDGDILSYRWdfgdgTTATGANVSHTYAAPGT-------------YTVTLT 67
                          90
                  ....*....|....*..
gi 501152660  645 VTDPEGLS-ATDSVTVT 660
Cdd:pfam18911  68 VTDDSGASnSTATDTVT 84
PKD_4 pfam18911
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.
667-754 1.93e-05

PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.


Pssm-ID: 436824 [Multi-domain]  Cd Length: 85  Bit Score: 43.80  E-value: 1.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660  667 NQAPVVSVAATATVEAGKTVSIVASAS-DADGDALTYAWTVPAGVSATGQNsATLVVTGPNVTEATsygLSVLVSDGALD 745
Cdd:pfam18911   1 NAAPVADAGGDRIVAEGETVTFDASASdDPDGDILSYRWDFGDGTTATGAN-VSHTYAAPGTYTVT---LTVTDDSGASN 76

                  ....*....
gi 501152660  746 ASASTNLTV 754
Cdd:pfam18911  77 STATDTVTV 85
tand_rpt_95 NF012211
tandem-95 repeat; This 95-amino acid repeat occurs in tandem in proteins that may be several ...
687-756 1.37e-04

tandem-95 repeat; This 95-amino acid repeat occurs in tandem in proteins that may be several thousand amino acids long.


Pssm-ID: 333740 [Multi-domain]  Cd Length: 98  Bit Score: 41.85  E-value: 1.37e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501152660 687 SIVASASDADGDALTYawtvpAGVSATGQNSATLVVTG-------PNVTEATSYGLSVLVSDGALDASAST-NLTVTP 756
Cdd:NF012211  14 QLLANASDVDGDDLTV-----SNVSYSGPTNGTVTDNGdgtytytPNENFNGDDSFTYTVSDGTGATATATvFVTVNP 86
CBD_like cd12204
Cellulose-binding domain, chitinase and related proteins; This group contains proteins related ...
823-859 1.33e-03

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: 37.31  E-value: 1.33e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 501152660 823 WDASVVYNGGQTTSYNGRVWKASYWTKGdVPGVAAVW 859
Cdd:cd12204    9 WPQGTHAAGGDLVSYNGAVYQAKWWTQS-APGSDSSW 44
Cadherin_4 pfam17803
Bacterial cadherin-like domain; This entry contains numerous bacterial cadherin-like domains ...
653-724 2.02e-03

Bacterial cadherin-like domain; This entry contains numerous bacterial cadherin-like domains found in extracelullar proteins.


Pssm-ID: 465514 [Multi-domain]  Cd Length: 71  Bit Score: 37.55  E-value: 2.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501152660  653 ATDSVTVTNkadtPNQAPVVsVAATATVEAGKTVSI----VASASDADGDALTYawtvpAGVSATGQNsATLVVTG 724
Cdd:pfam17803   1 ATVTITVTG----VNDAPVA-VDDTATVDEDTPVTItgnvLANDTDVDGDTLTV-----TSVTGAPAY-GTLTLNA 65
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
63-133 2.46e-03

polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.


Pssm-ID: 238084 [Multi-domain]  Cd Length: 81  Bit Score: 37.48  E-value: 2.46e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501152660  63 AADVSVSWNLWSGDVGNKAQVLLNGNvawEGPTGASGTANFKVNKGGRYQMQVQLCNSDGCTASDAKEILV 133
Cdd:cd00146   14 GASVTFSASDSSGGSIVSYKWDFGDG---EVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTKTTTVVV 81
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
66-134 5.74e-03

Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.


Pssm-ID: 214510 [Multi-domain]  Cd Length: 79  Bit Score: 36.66  E-value: 5.74e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501152660    66 VSVSWNLWSGDVGNKAQV-----LLNGNVAWE-----GPTGASGTANFKVNKGGRYQMQVQLCNSDGcTASDAKEILVA 134
Cdd:smart00089   2 ADVSASPTVGVAGESVTFtatssDDGSIVSYTwdfgdGTSSTGPTVTHTYTKPGTYTVTLTVTNAVG-SASATVTVVVQ 79
GH18_EndoS-like cd06542
Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of ...
310-409 6.75e-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: 39.28  E-value: 6.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501152660 310 FDGVDIDWEYPGGGgaNPNLGNANDgETYVTLMRELRAMLDelsaETGRTyeLTSAIGIDAQKMAKVDyqaAQQYMDYIF 389
Cdd:cd06542  105 LDGVDFDDEYSGYG--KNGTSQPSN-EAFVRLIKELRKYMG----PTDKL--LTIDGYGQALSNDGEE---VSPYVDYVI 172
                         90       100
                 ....*....|....*....|
gi 501152660 390 LMSYDFNGGWTNTELGHQTN 409
Cdd:cd06542  173 YQYYGSSSSSTQRNWNTNSP 192
ChtBD3 cd00036
Chitin/cellulose binding domains of chitinase and related enzymes; This group contains ...
775-815 9.57e-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: 34.66  E-value: 9.57e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 501152660 775 AWQTSVVYNTGDTVSHSQLVWKAKYWTQGNTPSrTADQWQL 815
Cdd:cd00036    1 AWPNPTHYTAGQSVVYNGNLYTANWYTAGSVPG-SDSSWTQ 40
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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