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Conserved domains on  [gi|3928775|gb|AAC79665|]
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chitinase A [Pseudoalteromonas sp. S9]

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];
303-784 1.33e-151

Chitinase, GH18 family [Carbohydrate transport and metabolism];


:

Pssm-ID: 442554 [Multi-domain]  Cd Length: 391  Bit Score: 456.30  E-value: 1.33e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   303 CTIYDADgrEDMGADHPRRVIGYFTSWRNGANGqpsYLVDDIPWDKITHINYAFAHVDANNKVSIGDPSAAgnpatnmew 382
Cdd:COG3325    4 ASVSDTA--AAATATSGKRVVGYFTQWGIYGRN---YLVKDIPASKLTHINYAFANVDPDGKCSVGDAWAK--------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   383 PGVAGAEMDPTLPYKGHFNLLNKYKKLHPDVKTLISVGGWAEtggyfdangnrvaSGGFYTMTTNAdgsvntAGINAFAK 462
Cdd:COG3325   70 PSVDGAADDWDQPLKGNFNQLKKLKAKNPNLKVLISIGGWTW-------------SKGFSDAAATP------ASRAAFVD 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   463 SAVEFIETYGFDGVDIDYEYPSSMNDSGH---PDDfpisnarraglNASYQVLMKTLREELDKAGELAGKHYMLTIASPS 539
Cdd:COG3325  131 SCVDLLRKYNFDGIDIDWEYPGSGGAPGNvyrPED-----------KANFTALLKELRAQLDALGAETGKHYLLTAAAPA 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   540 SGYLLRGMETFQTTKYLDYVNIMSYDLHGAWNDHVGHNAALYDTGLDSELAQWNVygtkefegigylntDWAVTYF-RGG 618
Cdd:COG3325  200 GPDKLDGIELPKVAQYLDYVNVMTYDFHGAWSPTTGHQAPLYDSPKDPEAQGYSV--------------DSAVQAYlAAG 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   619 LSAGRINIGVPYYTRGFKDVSGGENGLWGRAALPnqadcAKGTgvgeknkcgngavgidnmwhdldengneMPAGSNPLW 698
Cdd:COG3325  266 VPASKLVLGVPFYGRGWTGVTGGNNGLYQPATGP-----APGT----------------------------WEAGVNDYK 312
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   699 HVKNlqngilpSYLAAygldpandptdklvGTYTRHYDSVAVAPWLWNADKNVFLSIEDEESMGTKLDYVINKGLGGIMF 778
Cdd:COG3325  313 DLKA-------LYLGS--------------NGYTRYWDDVAKAPYLYNGDTGTFISYDDPRSIAAKADYVKDKGLGGVMF 371

                 ....*.
gi 3928775   779 WELAGD 784
Cdd:COG3325  372 WELSGD 377
ChiC super family cl05806
Chitinase C; This ~170 aa region is found at the C-terminus of pfam00704.
793-975 1.32e-42

Chitinase C; This ~170 aa region is found at the C-terminus of pfam00704.


The actual alignment was detected with superfamily member pfam06483:

Pssm-ID: 368936  Cd Length: 174  Bit Score: 153.24  E-value: 1.32e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775     793 EYFMGSTMTSLAYNKFAQAgSKYDINKGEKThqVPAEAVDVSFEVKDFPIGDDNYPIAPTFSFTNNSNIDL-SGAKVSFD 871
Cdd:pfam06483    1 EYFMGDTLTTLLYDKFKAA-APYGATKANAA--MPTQVLDVSVSLTGFPLGDSNYPINPKLRITNNSGQTIpGGTEFEFD 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775     872 VPVATSAifksnwNAQEKLGMAVDVNRSNAAGNNIGGFENEFHRFSITFvnewgGAAKSFAPGETINAQVMYYMPITGPV 951
Cdd:pfam06483   78 YPTSAPD------NAKDQSGFGLTVISSGHTGPNVGGLKGDFHRVAFTL-----PSWQTLAPGASVEVDLVYYLPVSGPS 146
                          170       180
                   ....*....|....*....|....*...
gi 3928775     952 NLVFEKDGKQYAAKFEYP----YLPDAT 975
Cdd:pfam06483  147 NWTVTFGGTTYALKGDYPrgttTLPTAT 174
CBD_like cd12204
Cellulose-binding domain, chitinase and related proteins; This group contains proteins related ...
997-1052 4.20e-15

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: 70.05  E-value: 4.20e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 3928775   997 ADIPVYPNFPQtdwagnPSHAAGGDLMVDGasTAVYKAKWWTSTEPGTSADWDSVC 1052
Cdd:cd12204    1 AGANAYPNWPQ------GTHAAGGDLVSYN--GAVYQAKWWTQSAPGSDSSWTLVC 48
Big_7 pfam17957
Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in ...
93-158 2.81e-10

Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in glycosyl hydrolase enzymes.


:

Pssm-ID: 436171 [Multi-domain]  Cd Length: 67  Bit Score: 57.23  E-value: 2.81e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3928775      93 AEVLSPMSGSSFTeGDSVVIEAQTSDsDGTVVKLEVLVDGVAIATLSSAPYSTTWLAVT---GQHQISV 158
Cdd:pfam17957    1 VSITSPANGATVS-GGTVTISATASD-DGGVSKVEFYVDGTLVGTDTSAPYSFTWTTTAlanGTHTITV 67
myxo_dep_M36 super family cl45606
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
86-281 1.39e-09

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: 62.37  E-value: 1.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775     86 QVNESPIAEVLSPmsgSSFTEGDSVVIEAQTSDSDG-TVVKLEVLVDGVAIATLSSAPYSTTWLA--VTGQHQISVRATD 162
Cdd:NF038112 1278 NVNRAPVAVAGAP---ATVDERSTVTLDGSGTDADGdALTYAWTQTSGPAVTLTGATTATATFTApeVTADTQLTFTLTV 1354
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775    163 DKGAETTSPANSVTVAEVvpdNYAPTASLTSNAssnTLNLNDNVVLNLSGSDQDGTVTSLELFQ-DGASVAQISGATGSF 241
Cdd:NF038112 1355 SDGTASATDTVTVTVRNV---NRAPVANAGADQ---TVDERSTVTLSGSATDPDGDALTYAWTQtAGPTVTLTGADTATA 1428
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 3928775    242 NFTATS-AGNTQ--FSLVATDDkGATSDAQTLSFRIVDGTTQP 281
Cdd:NF038112 1429 SFTAPEvAADTEltFQLTVSAD-GQASADVTVTVTVRNVNRAP 1470
ChiC_BD cd12215
Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of ...
35-75 3.80e-09

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: 52.96  E-value: 3.80e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 3928775    35 AEWQSGVAYTGGQQVQKANTAYEAKWWTQAD-PVTHSGQYQE 75
Cdd:cd12215    1 PAWDASTVYTGGDQVTYNGKVYEAKWWTQGEePGTSWGVWKL 42
 
Name Accession Description Interval E-value
ChiA COG3325
Chitinase, GH18 family [Carbohydrate transport and metabolism];
303-784 1.33e-151

Chitinase, GH18 family [Carbohydrate transport and metabolism];


Pssm-ID: 442554 [Multi-domain]  Cd Length: 391  Bit Score: 456.30  E-value: 1.33e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   303 CTIYDADgrEDMGADHPRRVIGYFTSWRNGANGqpsYLVDDIPWDKITHINYAFAHVDANNKVSIGDPSAAgnpatnmew 382
Cdd:COG3325    4 ASVSDTA--AAATATSGKRVVGYFTQWGIYGRN---YLVKDIPASKLTHINYAFANVDPDGKCSVGDAWAK--------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   383 PGVAGAEMDPTLPYKGHFNLLNKYKKLHPDVKTLISVGGWAEtggyfdangnrvaSGGFYTMTTNAdgsvntAGINAFAK 462
Cdd:COG3325   70 PSVDGAADDWDQPLKGNFNQLKKLKAKNPNLKVLISIGGWTW-------------SKGFSDAAATP------ASRAAFVD 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   463 SAVEFIETYGFDGVDIDYEYPSSMNDSGH---PDDfpisnarraglNASYQVLMKTLREELDKAGELAGKHYMLTIASPS 539
Cdd:COG3325  131 SCVDLLRKYNFDGIDIDWEYPGSGGAPGNvyrPED-----------KANFTALLKELRAQLDALGAETGKHYLLTAAAPA 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   540 SGYLLRGMETFQTTKYLDYVNIMSYDLHGAWNDHVGHNAALYDTGLDSELAQWNVygtkefegigylntDWAVTYF-RGG 618
Cdd:COG3325  200 GPDKLDGIELPKVAQYLDYVNVMTYDFHGAWSPTTGHQAPLYDSPKDPEAQGYSV--------------DSAVQAYlAAG 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   619 LSAGRINIGVPYYTRGFKDVSGGENGLWGRAALPnqadcAKGTgvgeknkcgngavgidnmwhdldengneMPAGSNPLW 698
Cdd:COG3325  266 VPASKLVLGVPFYGRGWTGVTGGNNGLYQPATGP-----APGT----------------------------WEAGVNDYK 312
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   699 HVKNlqngilpSYLAAygldpandptdklvGTYTRHYDSVAVAPWLWNADKNVFLSIEDEESMGTKLDYVINKGLGGIMF 778
Cdd:COG3325  313 DLKA-------LYLGS--------------NGYTRYWDDVAKAPYLYNGDTGTFISYDDPRSIAAKADYVKDKGLGGVMF 371

                 ....*.
gi 3928775   779 WELAGD 784
Cdd:COG3325  372 WELSGD 377
GH18_chitinase cd06548
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ...
322-784 2.68e-106

The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant polymer of N-acetylglucosamine and have been identified in bacteria, fungi, insects, plants, viruses, and protozoan parasites. The structure of this domain is an eight-stranded alpha/beta barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel.


Pssm-ID: 119365 [Multi-domain]  Cd Length: 322  Bit Score: 334.60  E-value: 2.68e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   322 VIGYFTSWRNGANGQPSYlvDDIPWDKITHINYAFAHVDANNKVSIGDPSAAGNpatnmEWPGVAGAEMDPTLPYKGHFN 401
Cdd:cd06548    1 VVGYFTNWGIYGRNYFVT--DDIPADKLTHINYAFADIDGDGGVVTSDDEAADE-----AAQSVDGGADTDDQPLKGNFG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   402 LLNKYKKLHPDVKTLISVGGWAetggyfdangnrvASGGFYTMTTNAdgsvntAGINAFAKSAVEFIETYGFDGVDIDYE 481
Cdd:cd06548   74 QLRKLKQKNPHLKILLSIGGWT-------------WSGGFSDAAATE------ASRAKFADSAVDFIRKYGFDGIDIDWE 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   482 YPSSmndSGHPDdfpisNARRAGLNASYQVLMKTLREELDKAGELAGKHYMLTIASPSSGYLLRGMETFQTTKYLDYVNI 561
Cdd:cd06548  135 YPGS---GGAPG-----NVARPEDKENFTLLLKELREALDALGAETGRKYLLTIAAPAGPDKLDKLEVAEIAKYLDFINL 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   562 MSYDLHGAWNDHVGHNAALYDTGLDSelaqwnvygtkefeGIGYLNTDWAVTYFRGGLSAGRINIGVPYYTRGFKDvsgg 641
Cdd:cd06548  207 MTYDFHGAWSNTTGHHSNLYASPADP--------------PGGYSVDAAVNYYLSAGVPPEKLVLGVPFYGRGWTG---- 268
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   642 englwgraalpnqadcakgtgvgeknkcgngavgidnmwhdldengnempagsnplwhvknlqngilpsylaaygldpan 721
Cdd:cd06548      --------------------------------------------------------------------------------
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3928775   722 dptdklvgtYTRHYDSVAVAPWLWNADKNVFLSIEDEESMGTKLDYVINKGLGGIMFWELAGD 784
Cdd:cd06548  269 ---------YTRYWDEVAKAPYLYNPSTKTFISYDDPRSIKAKADYVKDKGLGGVMFWELSGD 322
Glyco_18 smart00636
Glyco_18 domain;
321-784 1.34e-98

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 314.62  E-value: 1.34e-98
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775      321 RVIGYFTSWrngANGQPSYLVDDIPWDKITHINYAFAHVDANNKVSIGDPSAAgnpatnmewpgvagaemdptlpyKGHF 400
Cdd:smart00636    1 RVVGYFTNW---GVYGRNFPVDDIPASKLTHIIYAFANIDPDGTVTIGDEWAD-----------------------IGNF 54
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775      401 NLLNKYKKLHPDVKTLISVGGWAEtggyfdangnrvaSGGFYTMTTNAdgsvntAGINAFAKSAVEFIETYGFDGVDIDY 480
Cdd:smart00636   55 GQLKALKKKNPGLKVLLSIGGWTE-------------SDNFSSMLSDP------ASRKKFIDSIVSFLKKYGFDGIDIDW 115
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775      481 EYPSSMNDSGHpddfpisnarraglnaSYQVLMKTLREELDKAgELAGKHYMLTIASPSSG-YLLRGMETFQT-TKYLDY 558
Cdd:smart00636  116 EYPGGRGDDRE----------------NYTALLKELREALDKE-GAEGKGYLLTIAVPAGPdKIDKGYGDLPAiAKYLDF 178
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775      559 VNIMSYDLHGAWNDHVGHNAALYDTGLDSElaqwnvygtkefegigYLNTDWAVTYFRG-GLSAGRINIGVPYYTRGFKD 637
Cdd:smart00636  179 INLMTYDFHGAWSNPTGHNAPLYAGPGDPE----------------KYNVDYAVKYYLCkGVPPSKLVLGIPFYGRGWTL 242
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775      638 VSGGENGlwgraalpnqadcakgtgvgeknkcgngavgIDNMWHDLDENGNEMPAGSNPLWHVKNLQNGilpsylaaygl 717
Cdd:smart00636  243 VDGSNNG-------------------------------PGAPFTGPATGGPGTWEGGVVDYREICKLLG----------- 280
                           410       420       430       440       450       460
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3928775      718 dpandptdklvgtYTRHYDSVAVAPWLWNADKNVFLSIEDEESMGTKLDYVINKGLGGIMFWELAGD 784
Cdd:smart00636  281 -------------ATVVYDDTAKAPYAYNPGTGQWVSYDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
321-784 6.38e-75

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 249.68  E-value: 6.38e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775     321 RVIGYFTSWRNGANGqpsylvDDIPWDKITHINYAFAHVD-ANNKVSIGDPSaagnpatnmewpgvagaemdptlpyKGH 399
Cdd:pfam00704    1 RIVGYYTSWGVYRNG------NFLPSDKLTHIIYAFANIDgSDGTLFIGDWD-------------------------LGN 49
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775     400 FNLLNKYKKL-HPDVKTLISVGGWAEtggyfdangnrvaSGGFYTMTTNAdgsvntAGINAFAKSAVEFIETYGFDGVDI 478
Cdd:pfam00704   50 FEQLKKLKKQkNPGVKVLLSIGGWTD-------------STGFSLMASNP------ASRKKFADSIVSFLRKYGFDGIDI 110
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775     479 DYEYPSsmndsGHPDDfpisnarraglNASYQVLMKTLREELDKAGElaGKHYMLTIASPSSGYLLRGMETFQT-TKYLD 557
Cdd:pfam00704  111 DWEYPG-----GNPED-----------KENYDLLLRELRAALDEAKG--GKKYLLSAAVPASYPDLDKGYDLPKiAKYLD 172
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775     558 YVNIMSYDLHGAWNDHVGHNAALYDTgldselaqwnvygtkefegiGYLNTDWAVTYF-RGGLSAGRINIGVPYYTRGFK 636
Cdd:pfam00704  173 FINVMTYDFHGSWDNVTGHHAPLYGG--------------------GSYNVDYAVKYYlKQGVPASKLVLGVPFYGRSWT 232
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775     637 DVSGGENglwgraalpnqadcakgtgvgeknkcgngavgidnmwhdldengnempAGSNPLWHVKNLQNGIlpsylaayg 716
Cdd:pfam00704  233 LVNGSGN------------------------------------------------TWEDGVLAYKEICNLL--------- 255
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3928775     717 ldpandptdkLVGTYTRHYDSVAVAPWLWNADknVFLSIEDEESMGTKLDYVINKGLGGIMFWELAGD 784
Cdd:pfam00704  256 ----------KDNGATVVWDDVAKAPYVYDGD--QFITYDDPRSIATKVDYVKAKGLGGVMIWSLDAD 311
ChiC pfam06483
Chitinase C; This ~170 aa region is found at the C-terminus of pfam00704.
793-975 1.32e-42

Chitinase C; This ~170 aa region is found at the C-terminus of pfam00704.


Pssm-ID: 368936  Cd Length: 174  Bit Score: 153.24  E-value: 1.32e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775     793 EYFMGSTMTSLAYNKFAQAgSKYDINKGEKThqVPAEAVDVSFEVKDFPIGDDNYPIAPTFSFTNNSNIDL-SGAKVSFD 871
Cdd:pfam06483    1 EYFMGDTLTTLLYDKFKAA-APYGATKANAA--MPTQVLDVSVSLTGFPLGDSNYPINPKLRITNNSGQTIpGGTEFEFD 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775     872 VPVATSAifksnwNAQEKLGMAVDVNRSNAAGNNIGGFENEFHRFSITFvnewgGAAKSFAPGETINAQVMYYMPITGPV 951
Cdd:pfam06483   78 YPTSAPD------NAKDQSGFGLTVISSGHTGPNVGGLKGDFHRVAFTL-----PSWQTLAPGASVEVDLVYYLPVSGPS 146
                          170       180
                   ....*....|....*....|....*...
gi 3928775     952 NLVFEKDGKQYAAKFEYP----YLPDAT 975
Cdd:pfam06483  147 NWTVTFGGTTYALKGDYPrgttTLPTAT 174
CBD_like cd12204
Cellulose-binding domain, chitinase and related proteins; This group contains proteins related ...
997-1052 4.20e-15

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: 70.05  E-value: 4.20e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 3928775   997 ADIPVYPNFPQtdwagnPSHAAGGDLMVDGasTAVYKAKWWTSTEPGTSADWDSVC 1052
Cdd:cd12204    1 AGANAYPNWPQ------GTHAAGGDLVSYN--GAVYQAKWWTQSAPGSDSSWTLVC 48
CBM_5_12_2 pfam14600
Cellulose-binding domain; This C-terminal domain belongs to the CAZy family of ...
997-1051 2.60e-10

Cellulose-binding domain; This C-terminal domain belongs to the CAZy family of carbohydrate-binding domains that are associated with glycosyl-hydrolases. It is suggested to bind cellulose.


Pssm-ID: 434062  Cd Length: 62  Bit Score: 57.11  E-value: 2.60e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 3928775     997 ADIPVYPNFPQTDWAGNP-SHAAGGDLMVdgASTAVYKAKWWTSTEPGTSADWDSV 1051
Cdd:pfam14600    5 AGVNEYPNWTAKDWAGGPyNHANAGDQMV--YQGTLYQANWYTNSVPGSDASWTFL 58
Big_7 pfam17957
Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in ...
93-158 2.81e-10

Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in glycosyl hydrolase enzymes.


Pssm-ID: 436171 [Multi-domain]  Cd Length: 67  Bit Score: 57.23  E-value: 2.81e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3928775      93 AEVLSPMSGSSFTeGDSVVIEAQTSDsDGTVVKLEVLVDGVAIATLSSAPYSTTWLAVT---GQHQISV 158
Cdd:pfam17957    1 VSITSPANGATVS-GGTVTISATASD-DGGVSKVEFYVDGTLVGTDTSAPYSFTWTTTAlanGTHTITV 67
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
86-281 1.39e-09

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: 62.37  E-value: 1.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775     86 QVNESPIAEVLSPmsgSSFTEGDSVVIEAQTSDSDG-TVVKLEVLVDGVAIATLSSAPYSTTWLA--VTGQHQISVRATD 162
Cdd:NF038112 1278 NVNRAPVAVAGAP---ATVDERSTVTLDGSGTDADGdALTYAWTQTSGPAVTLTGATTATATFTApeVTADTQLTFTLTV 1354
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775    163 DKGAETTSPANSVTVAEVvpdNYAPTASLTSNAssnTLNLNDNVVLNLSGSDQDGTVTSLELFQ-DGASVAQISGATGSF 241
Cdd:NF038112 1355 SDGTASATDTVTVTVRNV---NRAPVANAGADQ---TVDERSTVTLSGSATDPDGDALTYAWTQtAGPTVTLTGADTATA 1428
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 3928775    242 NFTATS-AGNTQ--FSLVATDDkGATSDAQTLSFRIVDGTTQP 281
Cdd:NF038112 1429 SFTAPEvAADTEltFQLTVSAD-GQASADVTVTVTVRNVNRAP 1470
ChiC_BD cd12215
Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of ...
35-75 3.80e-09

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: 52.96  E-value: 3.80e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 3928775    35 AEWQSGVAYTGGQQVQKANTAYEAKWWTQAD-PVTHSGQYQE 75
Cdd:cd12215    1 PAWDASTVYTGGDQVTYNGKVYEAKWWTQGEePGTSWGVWKL 42
ChtBD3 smart00495
Chitin-binding domain type 3;
35-73 1.81e-07

Chitin-binding domain type 3;


Pssm-ID: 197760 [Multi-domain]  Cd Length: 41  Bit Score: 48.41  E-value: 1.81e-07
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 3928775       35 AEWQSGVAYTGGQQVQKANTAYEAKWWTQADPVTHSGQY 73
Cdd:smart00495    2 PAWQAGTVYTAGDVVSYNGKVYKAKWWTQGEEPGSSSGP 40
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
86-268 2.04e-07

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: 55.43  E-value: 2.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775     86 QVNESPIAEVlspmsGSSFT--EGDSVVIEAQTSDSDGTVVKLEVLVDGVAIATLSSAPYST---TWLAVTGQHQISVRA 160
Cdd:NF038112 1371 NVNRAPVANA-----GADQTvdERSTVTLSGSATDPDGDALTYAWTQTAGPTVTLTGADTATasfTAPEVAADTELTFQL 1445
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775    161 TDdKGAETTSPANSVTVAeVVPDNYAPTASLTSNASSNTlnlNDNVVLNLSGSDQDGTVTSLELFQDGASVAQISGATGS 240
Cdd:NF038112 1446 TV-SADGQASADVTVTVT-VRNVNRAPVAHAGESITVDE---GSTVTLDASATDPDGDTLTYAWTQVAGPSVTLTGADSA 1520
                         170       180       190
                  ....*....|....*....|....*....|..
gi 3928775    241 -FNFTA--TSAGNT-QFSLVATDDKGATSDAQ 268
Cdd:NF038112 1521 kLTFTApeVSADTTlTFSLTVTDGSGSSGPVV 1552
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
165-276 1.59e-04

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: 45.80  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775    165 GAETTSPANsVTVAeVVPDNYAPTASLTSNAssnTLNLNDNVVLNLSGSDQDGTVTSLELFQDGASVAQISGATG-SFNF 243
Cdd:NF038112 1263 GTKTSAPDT-VTVL-VRNVNRAPVAVAGAPA---TVDERSTVTLDGSGTDADGDALTYAWTQTSGPAVTLTGATTaTATF 1337
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 3928775    244 TATS-AGNTQ--FSLVATDDKGATSDAQTLSFRIVD 276
Cdd:NF038112 1338 TAPEvTADTQltFTLTVSDGTASATDTVTVTVRNVN 1373
Big_13 pfam19077
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ...
186-274 3.57e-04

Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.


Pssm-ID: 465968 [Multi-domain]  Cd Length: 102  Bit Score: 40.71  E-value: 3.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775     186 APTASLTS---NASSNTLNLNDNVVLNLSGSDQDGTVTSLELFQDGASVAQI--SGATGSFNFTATSA---GNTQFSLVA 257
Cdd:pfam19077    4 IPTIDLAAgsdTGVSDSDNITNDTTPTFTGTNEDGDVVTVTVSIDGNGVTGTatAGADGNWSFTPPAAladGTYTLTVTV 83
                           90
                   ....*....|....*..
gi 3928775     258 TDDKGATSDAQTLSFRI 274
Cdd:pfam19077   84 TDIAGNTATSSPLSFTI 100
 
Name Accession Description Interval E-value
ChiA COG3325
Chitinase, GH18 family [Carbohydrate transport and metabolism];
303-784 1.33e-151

Chitinase, GH18 family [Carbohydrate transport and metabolism];


Pssm-ID: 442554 [Multi-domain]  Cd Length: 391  Bit Score: 456.30  E-value: 1.33e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   303 CTIYDADgrEDMGADHPRRVIGYFTSWRNGANGqpsYLVDDIPWDKITHINYAFAHVDANNKVSIGDPSAAgnpatnmew 382
Cdd:COG3325    4 ASVSDTA--AAATATSGKRVVGYFTQWGIYGRN---YLVKDIPASKLTHINYAFANVDPDGKCSVGDAWAK--------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   383 PGVAGAEMDPTLPYKGHFNLLNKYKKLHPDVKTLISVGGWAEtggyfdangnrvaSGGFYTMTTNAdgsvntAGINAFAK 462
Cdd:COG3325   70 PSVDGAADDWDQPLKGNFNQLKKLKAKNPNLKVLISIGGWTW-------------SKGFSDAAATP------ASRAAFVD 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   463 SAVEFIETYGFDGVDIDYEYPSSMNDSGH---PDDfpisnarraglNASYQVLMKTLREELDKAGELAGKHYMLTIASPS 539
Cdd:COG3325  131 SCVDLLRKYNFDGIDIDWEYPGSGGAPGNvyrPED-----------KANFTALLKELRAQLDALGAETGKHYLLTAAAPA 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   540 SGYLLRGMETFQTTKYLDYVNIMSYDLHGAWNDHVGHNAALYDTGLDSELAQWNVygtkefegigylntDWAVTYF-RGG 618
Cdd:COG3325  200 GPDKLDGIELPKVAQYLDYVNVMTYDFHGAWSPTTGHQAPLYDSPKDPEAQGYSV--------------DSAVQAYlAAG 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   619 LSAGRINIGVPYYTRGFKDVSGGENGLWGRAALPnqadcAKGTgvgeknkcgngavgidnmwhdldengneMPAGSNPLW 698
Cdd:COG3325  266 VPASKLVLGVPFYGRGWTGVTGGNNGLYQPATGP-----APGT----------------------------WEAGVNDYK 312
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   699 HVKNlqngilpSYLAAygldpandptdklvGTYTRHYDSVAVAPWLWNADKNVFLSIEDEESMGTKLDYVINKGLGGIMF 778
Cdd:COG3325  313 DLKA-------LYLGS--------------NGYTRYWDDVAKAPYLYNGDTGTFISYDDPRSIAAKADYVKDKGLGGVMF 371

                 ....*.
gi 3928775   779 WELAGD 784
Cdd:COG3325  372 WELSGD 377
GH18_chitinase cd06548
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ...
322-784 2.68e-106

The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant polymer of N-acetylglucosamine and have been identified in bacteria, fungi, insects, plants, viruses, and protozoan parasites. The structure of this domain is an eight-stranded alpha/beta barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel.


Pssm-ID: 119365 [Multi-domain]  Cd Length: 322  Bit Score: 334.60  E-value: 2.68e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   322 VIGYFTSWRNGANGQPSYlvDDIPWDKITHINYAFAHVDANNKVSIGDPSAAGNpatnmEWPGVAGAEMDPTLPYKGHFN 401
Cdd:cd06548    1 VVGYFTNWGIYGRNYFVT--DDIPADKLTHINYAFADIDGDGGVVTSDDEAADE-----AAQSVDGGADTDDQPLKGNFG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   402 LLNKYKKLHPDVKTLISVGGWAetggyfdangnrvASGGFYTMTTNAdgsvntAGINAFAKSAVEFIETYGFDGVDIDYE 481
Cdd:cd06548   74 QLRKLKQKNPHLKILLSIGGWT-------------WSGGFSDAAATE------ASRAKFADSAVDFIRKYGFDGIDIDWE 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   482 YPSSmndSGHPDdfpisNARRAGLNASYQVLMKTLREELDKAGELAGKHYMLTIASPSSGYLLRGMETFQTTKYLDYVNI 561
Cdd:cd06548  135 YPGS---GGAPG-----NVARPEDKENFTLLLKELREALDALGAETGRKYLLTIAAPAGPDKLDKLEVAEIAKYLDFINL 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   562 MSYDLHGAWNDHVGHNAALYDTGLDSelaqwnvygtkefeGIGYLNTDWAVTYFRGGLSAGRINIGVPYYTRGFKDvsgg 641
Cdd:cd06548  207 MTYDFHGAWSNTTGHHSNLYASPADP--------------PGGYSVDAAVNYYLSAGVPPEKLVLGVPFYGRGWTG---- 268
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   642 englwgraalpnqadcakgtgvgeknkcgngavgidnmwhdldengnempagsnplwhvknlqngilpsylaaygldpan 721
Cdd:cd06548      --------------------------------------------------------------------------------
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3928775   722 dptdklvgtYTRHYDSVAVAPWLWNADKNVFLSIEDEESMGTKLDYVINKGLGGIMFWELAGD 784
Cdd:cd06548  269 ---------YTRYWDEVAKAPYLYNPSTKTFISYDDPRSIKAKADYVKDKGLGGVMFWELSGD 322
Glyco_18 smart00636
Glyco_18 domain;
321-784 1.34e-98

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 314.62  E-value: 1.34e-98
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775      321 RVIGYFTSWrngANGQPSYLVDDIPWDKITHINYAFAHVDANNKVSIGDPSAAgnpatnmewpgvagaemdptlpyKGHF 400
Cdd:smart00636    1 RVVGYFTNW---GVYGRNFPVDDIPASKLTHIIYAFANIDPDGTVTIGDEWAD-----------------------IGNF 54
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775      401 NLLNKYKKLHPDVKTLISVGGWAEtggyfdangnrvaSGGFYTMTTNAdgsvntAGINAFAKSAVEFIETYGFDGVDIDY 480
Cdd:smart00636   55 GQLKALKKKNPGLKVLLSIGGWTE-------------SDNFSSMLSDP------ASRKKFIDSIVSFLKKYGFDGIDIDW 115
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775      481 EYPSSMNDSGHpddfpisnarraglnaSYQVLMKTLREELDKAgELAGKHYMLTIASPSSG-YLLRGMETFQT-TKYLDY 558
Cdd:smart00636  116 EYPGGRGDDRE----------------NYTALLKELREALDKE-GAEGKGYLLTIAVPAGPdKIDKGYGDLPAiAKYLDF 178
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775      559 VNIMSYDLHGAWNDHVGHNAALYDTGLDSElaqwnvygtkefegigYLNTDWAVTYFRG-GLSAGRINIGVPYYTRGFKD 637
Cdd:smart00636  179 INLMTYDFHGAWSNPTGHNAPLYAGPGDPE----------------KYNVDYAVKYYLCkGVPPSKLVLGIPFYGRGWTL 242
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775      638 VSGGENGlwgraalpnqadcakgtgvgeknkcgngavgIDNMWHDLDENGNEMPAGSNPLWHVKNLQNGilpsylaaygl 717
Cdd:smart00636  243 VDGSNNG-------------------------------PGAPFTGPATGGPGTWEGGVVDYREICKLLG----------- 280
                           410       420       430       440       450       460
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3928775      718 dpandptdklvgtYTRHYDSVAVAPWLWNADKNVFLSIEDEESMGTKLDYVINKGLGGIMFWELAGD 784
Cdd:smart00636  281 -------------ATVVYDDTAKAPYAYNPGTGQWVSYDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
321-784 6.38e-75

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 249.68  E-value: 6.38e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775     321 RVIGYFTSWRNGANGqpsylvDDIPWDKITHINYAFAHVD-ANNKVSIGDPSaagnpatnmewpgvagaemdptlpyKGH 399
Cdd:pfam00704    1 RIVGYYTSWGVYRNG------NFLPSDKLTHIIYAFANIDgSDGTLFIGDWD-------------------------LGN 49
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775     400 FNLLNKYKKL-HPDVKTLISVGGWAEtggyfdangnrvaSGGFYTMTTNAdgsvntAGINAFAKSAVEFIETYGFDGVDI 478
Cdd:pfam00704   50 FEQLKKLKKQkNPGVKVLLSIGGWTD-------------STGFSLMASNP------ASRKKFADSIVSFLRKYGFDGIDI 110
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775     479 DYEYPSsmndsGHPDDfpisnarraglNASYQVLMKTLREELDKAGElaGKHYMLTIASPSSGYLLRGMETFQT-TKYLD 557
Cdd:pfam00704  111 DWEYPG-----GNPED-----------KENYDLLLRELRAALDEAKG--GKKYLLSAAVPASYPDLDKGYDLPKiAKYLD 172
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775     558 YVNIMSYDLHGAWNDHVGHNAALYDTgldselaqwnvygtkefegiGYLNTDWAVTYF-RGGLSAGRINIGVPYYTRGFK 636
Cdd:pfam00704  173 FINVMTYDFHGSWDNVTGHHAPLYGG--------------------GSYNVDYAVKYYlKQGVPASKLVLGVPFYGRSWT 232
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775     637 DVSGGENglwgraalpnqadcakgtgvgeknkcgngavgidnmwhdldengnempAGSNPLWHVKNLQNGIlpsylaayg 716
Cdd:pfam00704  233 LVNGSGN------------------------------------------------TWEDGVLAYKEICNLL--------- 255
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3928775     717 ldpandptdkLVGTYTRHYDSVAVAPWLWNADknVFLSIEDEESMGTKLDYVINKGLGGIMFWELAGD 784
Cdd:pfam00704  256 ----------KDNGATVVWDDVAKAPYVYDGD--QFITYDDPRSIATKVDYVKAKGLGGVMIWSLDAD 311
GH18_chitolectin_chitotriosidase cd02872
This conserved domain family includes a large number of catalytically inactive chitinase-like ...
322-786 1.88e-53

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: 191.23  E-value: 1.88e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   322 VIGYFTSWRNGANGQPSYLVDDIPWDKITHINYAFAHVDANNKVSIGDPSAAGNpatnmewpgvagaemdptlpyKGHFN 401
Cdd:cd02872    1 VVCYFTNWAQYRPGNGKFVPENIDPFLCTHIIYAFAGLNPDGNIIILDEWNDID---------------------LGLYE 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   402 LLNKYKKLHPDVKTLISVGGWAETggyfdangnrvaSGGFYTMTTNAdgsVNTAginAFAKSAVEFIETYGFDGVDIDYE 481
Cdd:cd02872   60 RFNALKEKNPNLKTLLAIGGWNFG------------SAKFSAMAASP---ENRK---TFIKSAIAFLRKYGFDGLDLDWE 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   482 YPSSMNdsGHPDDfpisnarraglNASYQVLMKTLREELDKAGElagkHYMLTIA------SPSSGYLLRGMetfqtTKY 555
Cdd:cd02872  122 YPGQRG--GPPED-----------KENFVTLLKELREAFEPEAP----RLLLTAAvsagkeTIDAAYDIPEI-----SKY 179
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   556 LDYVNIMSYDLHGAWNDHVGHNAALYDTGLDSelaqwnvygtkefEGIGYLNTDWAVTYF-RGGLSAGRINIGVPYYTRG 634
Cdd:cd02872  180 LDFINVMTYDFHGSWEGVTGHNSPLYAGSADT-------------GDQKYLNVDYAIKYWlSKGAPPEKLVLGIPTYGRS 246
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   635 FKDVSGGENGLwGRAAlpnqadcakgTGVGeknkcgngavgidnmwhdldengnemPAGSNplwhvkNLQNGILpsylaA 714
Cdd:cd02872  247 FTLASPSNTGV-GAPA----------SGPG--------------------------TAGPY------TREAGFL-----A 278
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3928775   715 YgldpaNDPTDKLVGTYTRHYDSVAVAPWLWNADKNVflSIEDEESMGTKLDYVINKGLGGIMFWELagDFD 786
Cdd:cd02872  279 Y-----YEICEFLKSGWTVVWDDEQKVPYAYKGNQWV--GYDDEESIALKVQYLKSKGLGGAMVWSI--DLD 341
ChiC pfam06483
Chitinase C; This ~170 aa region is found at the C-terminus of pfam00704.
793-975 1.32e-42

Chitinase C; This ~170 aa region is found at the C-terminus of pfam00704.


Pssm-ID: 368936  Cd Length: 174  Bit Score: 153.24  E-value: 1.32e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775     793 EYFMGSTMTSLAYNKFAQAgSKYDINKGEKThqVPAEAVDVSFEVKDFPIGDDNYPIAPTFSFTNNSNIDL-SGAKVSFD 871
Cdd:pfam06483    1 EYFMGDTLTTLLYDKFKAA-APYGATKANAA--MPTQVLDVSVSLTGFPLGDSNYPINPKLRITNNSGQTIpGGTEFEFD 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775     872 VPVATSAifksnwNAQEKLGMAVDVNRSNAAGNNIGGFENEFHRFSITFvnewgGAAKSFAPGETINAQVMYYMPITGPV 951
Cdd:pfam06483   78 YPTSAPD------NAKDQSGFGLTVISSGHTGPNVGGLKGDFHRVAFTL-----PSWQTLAPGASVEVDLVYYLPVSGPS 146
                          170       180
                   ....*....|....*....|....*...
gi 3928775     952 NLVFEKDGKQYAAKFEYP----YLPDAT 975
Cdd:pfam06483  147 NWTVTFGGTTYALKGDYPrgttTLPTAT 174
GH18_chitinase-like cd00598
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ...
322-566 8.30e-32

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: 123.64  E-value: 8.30e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   322 VIGYFTSWRNGangqPSYLVDDIPWDKITHINYAFAHVDANNkvsigdpsaagnpatnmewpgvaGAEMDPTLPYKGHFN 401
Cdd:cd00598    1 VICYYDGWSSG----RGPDPTDIPLSLCTHIIYAFAEISSDG-----------------------SLNLFGDKSEEPLKG 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   402 LLNKYKKLHPDVKTLISVGGWAETGGYFDANgnrvasggfytmttnadgsvNTAGINAFAKSAVEFIETYGFDGVDIDYE 481
Cdd:cd00598   54 ALEELASKKPGLKVLISIGGWTDSSPFTLAS--------------------DPASRAAFANSLVSFLKTYGFDGVDIDWE 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   482 YPSSMNDSGHPddfpisnarraglnaSYQVLMKTLREELDKAGelagkhYMLTIASPSSGYLLRGMETFQT-TKYLDYVN 560
Cdd:cd00598  114 YPGAADNSDRE---------------NFITLLRELRSALGAAN------YLLTIAVPASYFDLGYAYDVPAiGDYVDFVN 172

                 ....*.
gi 3928775   561 IMSYDL 566
Cdd:cd00598  173 VMTYDL 178
GH18_zymocin_alpha cd02878
Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle ...
323-571 1.85e-21

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: 96.99  E-value: 1.85e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   323 IGYFTSWrNGANGQPSYLVDDIPWDKITHINYAFAHVDANNKVSIGDPSAAgnpatnmewpgvagaemdptlpykghfnl 402
Cdd:cd02878    3 IAYFEAY-NLDRPCLNMDVTQIDTSKYTHIHFAFANITSDFSVDVSSVQEQ----------------------------- 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   403 LNKYKKLHpDVKTLISVGGWAETggyfdangnrvASGGFYTMTTNAdgsVNTAGINAFAKSAVEFIETYGFDGVDIDYEY 482
Cdd:cd02878   53 FSDFKKLK-GVKKILSFGGWDFS-----------TSPSTYQIFRDA---VKPANRDTFANNVVNFVNKYNLDGVDFDWEY 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   483 PSSMNDSGHPDDFPISnarraGLNasYQVLMKTLREELdkagelaGKHYMLTIASPSSGYLLRGMETFQTTKYLDYVNIM 562
Cdd:cd02878  118 PGAPDIPGIPAGDPDD-----GKN--YLEFLKLLKSKL-------PSGKSLSIAAPASYWYLKGFPIKDMAKYVDYIVYM 183

                 ....*....
gi 3928775   563 SYDLHGAWN 571
Cdd:cd02878  184 TYDLHGQWD 192
GH18_plant_chitinase_class_V cd02879
The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the ...
343-633 3.91e-17

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: 83.18  E-value: 3.91e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   343 DIPWDKITHINYAFAHVDA-NNKVSIGDPSAagnpatnmewpgvagaemdptlPYKGHFNllNKYKKLHPDVKTLISVGG 421
Cdd:cd02879   20 NIDSSLFTHLFYAFADLDPsTYEVVISPSDE----------------------SEFSTFT--ETVKRKNPSVKTLLSIGG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   422 waetggyfdANGNRVAsggFYTMTTNADgsvNTAginAFAKSAVEFIETYGFDGVDIDYEYPSS---MNDSGhpddfpis 498
Cdd:cd02879   76 ---------GGSDSSA---FAAMASDPT---ARK---AFINSSIKVARKYGFDGLDLDWEFPSSqveMENFG-------- 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   499 narraglnasyqVLMKTLREELDKAGELAGKH-YMLTIASPSSGYLLRG-------METFQttKYLDYVNIMSYDLHGAW 570
Cdd:cd02879  130 ------------KLLEEWRAAVKDEARSSGRPpLLLTAAVYFSPILFLSddsvsypIEAIN--KNLDWVNVMAYDYYGSW 195
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3928775   571 NDHVGHNAALYDTGLDSelaqwnvygtkefegigyLNTDWAVT-YFRGGLSAGRINIGVPYYTR 633
Cdd:cd02879  196 ESNTTGPAAALYDPNSN------------------VSTDYGIKsWIKAGVPAKKLVLGLPLYGR 241
GH18_3CO4_chitinase cd06545
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an ...
322-635 4.66e-17

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: 82.11  E-value: 4.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   322 VIGYFTSWRNgangqPSYLVDDIPWDKITHINYAFAHVDANNKVSIGDPSAAGNPATNmewpgvagaemdptlpyKGHfn 401
Cdd:cd06545    1 VVGYLPNYDD-----LNALSPTIDFSKLTHINLAFANPDANGTLNANPVRSELNSVVN-----------------AAH-- 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   402 llnkykklHPDVKTLISVGGWA--ETGGYFDANGNRvasggfytmttnadgsvntagiNAFAKSAVEFIETYGFDGVDID 479
Cdd:cd06545   57 --------AHNVKILISLAGGSppEFTAALNDPAKR----------------------KALVDKIINYVVSYNLDGIDVD 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   480 YEYPSSMNdsghpddfpisnarraglnASYQVLMKTLREELDKAGELagkhymLTIASPSSgylLRGMETFQTTKYLDYV 559
Cdd:cd06545  107 LEGPDVTF-------------------GDYLVFIRALYAALKKEGKL------LTAAVSSW---NGGAVSDSTLAYFDFI 158
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3928775   560 NIMSYDLHGAWNDHVGHNAALYDTGLdSELAQWNVygtkefegigylntdwavtyfRGGLSAGRINIGVPYYTRGF 635
Cdd:cd06545  159 NIMSYDATGPWWGDNPGQHSSYDDAV-NDLNYWNE---------------------RGLASKDKLVLGLPFYGYGF 212
CBD_like cd12204
Cellulose-binding domain, chitinase and related proteins; This group contains proteins related ...
997-1052 4.20e-15

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: 70.05  E-value: 4.20e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 3928775   997 ADIPVYPNFPQtdwagnPSHAAGGDLMVDGasTAVYKAKWWTSTEPGTSADWDSVC 1052
Cdd:cd12204    1 AGANAYPNWPQ------GTHAAGGDLVSYN--GAVYQAKWWTQSAPGSDSSWTLVC 48
CBM_5_12_2 pfam14600
Cellulose-binding domain; This C-terminal domain belongs to the CAZy family of ...
997-1051 2.60e-10

Cellulose-binding domain; This C-terminal domain belongs to the CAZy family of carbohydrate-binding domains that are associated with glycosyl-hydrolases. It is suggested to bind cellulose.


Pssm-ID: 434062  Cd Length: 62  Bit Score: 57.11  E-value: 2.60e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 3928775     997 ADIPVYPNFPQTDWAGNP-SHAAGGDLMVdgASTAVYKAKWWTSTEPGTSADWDSV 1051
Cdd:pfam14600    5 AGVNEYPNWTAKDWAGGPyNHANAGDQMV--YQGTLYQANWYTNSVPGSDASWTFL 58
Big_7 pfam17957
Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in ...
93-158 2.81e-10

Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in glycosyl hydrolase enzymes.


Pssm-ID: 436171 [Multi-domain]  Cd Length: 67  Bit Score: 57.23  E-value: 2.81e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3928775      93 AEVLSPMSGSSFTeGDSVVIEAQTSDsDGTVVKLEVLVDGVAIATLSSAPYSTTWLAVT---GQHQISV 158
Cdd:pfam17957    1 VSITSPANGATVS-GGTVTISATASD-DGGVSKVEFYVDGTLVGTDTSAPYSFTWTTTAlanGTHTITV 67
GH18_IDGF cd02873
The IDGF's (imaginal disc growth factors) are a family of growth factors identified in insects ...
350-784 3.26e-10

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: 63.49  E-value: 3.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   350 THINYAFAHVDA-NNKVSigdpsaagnpatnmewpgvagaEMDPTLPY-KGHFNLLNKYKKLHPDVKTLISVGGWAETGG 427
Cdd:cd02873   32 THLVYGYAGIDAdTYKIK----------------------SLNEDLDLdKSHYRAITSLKRKYPHLKVLLSVGGDRDTDE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   428 YFDANgnrvasggfYTMTTNADGSVNTAGINafakSAVEFIETYGFDGVDIDYEypssmndsghpddFPISNAR--RAGL 505
Cdd:cd02873   90 EGENE---------KYLLLLESSESRNAFIN----SAHSLLKTYGFDGLDLAWQ-------------FPKNKPKkvRGTF 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   506 NASYQVLMKTLREEL---DKAGE---------------LAGKHYMLTIAS-P---SSGYllrgMETFQTTKYLDYVNIMS 563
Cdd:cd02873  144 GSAWHSFKKLFTGDSvvdEKAAEhkeqftalvrelknaLRPDGLLLTLTVlPhvnSTWY----FDVPAIANNVDFVNLAT 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   564 YD-LHGAWNDHVGHNAA-LYDtgLDSELAQWNVygtkefegigylntDWAVTYF-RGGLSAGRINIGVPYYTRGFKDVSg 640
Cdd:cd02873  220 FDfLTPERNPEEADYTApIYE--LYERNPHHNV--------------DYQVKYWlNQGTPASKLNLGIATYGRAWKLTK- 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   641 gENGLWGRAALPnQADcakgtGVGeknkcgngavgidnmwhdldengnemPAGsnPLWHVKNLQN-----GILPSYLAAY 715
Cdd:cd02873  283 -DSGITGVPPVL-ETD-----GPG--------------------------PAG--PQTKTPGLLSwpeicSKLPNPANLK 327
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3928775   716 GLDP----ANDPTdKLVGTYT-RHYDSvavapwlwNADKNVFLSIEDEESMGTKLDYVINKGLGGIMFWELAGD 784
Cdd:cd02873  328 GADAplrkVGDPT-KRFGSYAyRPADE--------NGEHGIWVSYEDPDTAANKAGYAKAKGLGGVALFDLSLD 392
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
86-281 1.39e-09

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: 62.37  E-value: 1.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775     86 QVNESPIAEVLSPmsgSSFTEGDSVVIEAQTSDSDG-TVVKLEVLVDGVAIATLSSAPYSTTWLA--VTGQHQISVRATD 162
Cdd:NF038112 1278 NVNRAPVAVAGAP---ATVDERSTVTLDGSGTDADGdALTYAWTQTSGPAVTLTGATTATATFTApeVTADTQLTFTLTV 1354
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775    163 DKGAETTSPANSVTVAEVvpdNYAPTASLTSNAssnTLNLNDNVVLNLSGSDQDGTVTSLELFQ-DGASVAQISGATGSF 241
Cdd:NF038112 1355 SDGTASATDTVTVTVRNV---NRAPVANAGADQ---TVDERSTVTLSGSATDPDGDALTYAWTQtAGPTVTLTGADTATA 1428
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 3928775    242 NFTATS-AGNTQ--FSLVATDDkGATSDAQTLSFRIVDGTTQP 281
Cdd:NF038112 1429 SFTAPEvAADTEltFQLTVSAD-GQASADVTVTVTVRNVNRAP 1470
ChiC_BD cd12215
Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of ...
35-75 3.80e-09

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: 52.96  E-value: 3.80e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 3928775    35 AEWQSGVAYTGGQQVQKANTAYEAKWWTQAD-PVTHSGQYQE 75
Cdd:cd12215    1 PAWDASTVYTGGDQVTYNGKVYEAKWWTQGEePGTSWGVWKL 42
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
66-499 1.06e-08

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 59.00  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775    66 PVTHSGQYQEWKNLGACSDGQVNESPIAEVLSPMSGSSFTEGDSVVIEAQTSDSDGTVVKLEVLVDGVAIATLSSAPYST 145
Cdd:COG3469    5 STAASPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTATATA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   146 TWLAVTGQHQISVRATDDKGAETTSPANSVTVAevvpdNYAPTASLTSNASSNTLNLNDNVVLNLSGSDQDGTVTSLELF 225
Cdd:COG3469   85 AAAAATSTSATLVATSTASGANTGTSTVTTTST-----GAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   226 qdgasvaqISGATGSFNFTATSAGNTQFSLVATDDKGATSDAQTLSFRIVDGTTQPgdrdackpeglyqtPGVNTPycti 305
Cdd:COG3469  160 --------TGGTTTTSTTTTTTSASTTPSATTTATATTASGATTPSATTTATTTGP--------------PTPGLP---- 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   306 ydadgredmgadhPRRVIGYFTSWRNGANGQPsylVDDIP--WDKIthiNYAFAHVDANnkvSIGDPSAAGNPATnmEWP 383
Cdd:COG3469  214 -------------KHVLVGYWHNFDNGSGYIR---LSDVPdkYDVI---NVAFAEPTGA---TNGTVTFTLDPGS--SSP 269
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   384 GVAG-----AEMDpTLPYKGhfnllnkykklhpdVKTLISVGGwaetggyfdangnrvasggfytmttnADGSV---NTA 455
Cdd:COG3469  270 GGYTdaqfkADIA-ALQAQG--------------KKVLLSIGG--------------------------ANGTVqlnTAA 308
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 3928775   456 GINAFAKSAVEFIETYGFDGVDIDYEYPSSMNDSGHPDDFPISN 499
Cdd:COG3469  309 AADNFVNSVIALIDEYGFDGLDIDLEGGSNSLNAGDTDTPVITN 352
GH18_EndoS-like cd06542
Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of ...
453-588 1.64e-08

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: 56.62  E-value: 1.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   453 NTAGINAFAKSAVEFIETYGFDGVDIDYEYpssmnDSGHPDDFPISNarraglNASYQVLMKTLREELDKAGELagkhym 532
Cdd:cd06542   85 SDAAAKAYAKAIVDTVDKYGLDGVDFDDEY-----SGYGKNGTSQPS------NEAFVRLIKELRKYMGPTDKL------ 147
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 3928775   533 LTIASPsSGYLLRGMEtfQTTKYLDYVNIMSYdlhGAWNDHVGHNAALYDTGLDSE 588
Cdd:cd06542  148 LTIDGY-GQALSNDGE--EVSPYVDYVIYQYY---GSSSSSTQRNWNTNSPKIPPE 197
ChtBD3 smart00495
Chitin-binding domain type 3;
35-73 1.81e-07

Chitin-binding domain type 3;


Pssm-ID: 197760 [Multi-domain]  Cd Length: 41  Bit Score: 48.41  E-value: 1.81e-07
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 3928775       35 AEWQSGVAYTGGQQVQKANTAYEAKWWTQADPVTHSGQY 73
Cdd:smart00495    2 PAWQAGTVYTAGDVVSYNGKVYKAKWWTQGEEPGSSSGP 40
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
86-268 2.04e-07

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: 55.43  E-value: 2.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775     86 QVNESPIAEVlspmsGSSFT--EGDSVVIEAQTSDSDGTVVKLEVLVDGVAIATLSSAPYST---TWLAVTGQHQISVRA 160
Cdd:NF038112 1371 NVNRAPVANA-----GADQTvdERSTVTLSGSATDPDGDALTYAWTQTAGPTVTLTGADTATasfTAPEVAADTELTFQL 1445
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775    161 TDdKGAETTSPANSVTVAeVVPDNYAPTASLTSNASSNTlnlNDNVVLNLSGSDQDGTVTSLELFQDGASVAQISGATGS 240
Cdd:NF038112 1446 TV-SADGQASADVTVTVT-VRNVNRAPVAHAGESITVDE---GSTVTLDASATDPDGDTLTYAWTQVAGPSVTLTGADSA 1520
                         170       180       190
                  ....*....|....*....|....*....|..
gi 3928775    241 -FNFTA--TSAGNT-QFSLVATDDKGATSDAQ 268
Cdd:NF038112 1521 kLTFTApeVSADTTlTFSLTVTDGSGSSGPVV 1552
GH18_narbonin cd06544
Narbonin is a plant 2S protein from the globulin fraction of narbon bean (Vicia narbonensis L.) ...
405-496 5.56e-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: 48.91  E-value: 5.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   405 KYKKLHPDVKTLISVGGWaetggyfdangnrvasgGFYTMTTNADGSVNTAGINAFAKSAVEFIETYGFDGVDIDYEyps 484
Cdd:cd06544   63 SIKAQHPNVKVVISIGGR-----------------GVQNNPTPFDPSNVDSWVSNAVSSLTSIIQTYNLDGIDIDYE--- 122
                         90
                 ....*....|..
gi 3928775   485 smNDSGHPDDFP 496
Cdd:cd06544  123 --HFPADPDTFV 132
GH18_chitinase_D-like cd02871
GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes ...
322-493 9.91e-05

GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes the 1,4-beta-linkages of N-acetylglucosamine in chitin and chitodextrins. The domain architecture of ChiD includes a catalytic glycosyl hydrolase family 18 (GH18) domain, a chitin-binding domain, and a fibronectin type III domain. The chitin-binding and fibronectin type III domains are located either N-terminal or C-terminal to the catalytic domain. This family includes exochitinase Chi36 from Bacillus cereus.


Pssm-ID: 119350 [Multi-domain]  Cd Length: 312  Bit Score: 45.79  E-value: 9.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   322 VIGYFTSWRNGANGQPSYLvDDIPwDKITHINYAFAHVDannkvsigdpsaagnPATNMEWPGVAGAEMDPTLP--YKGH 399
Cdd:cd02871    3 LVGYWHNWDNGAGSGRQDL-DDVP-SKYNVINVAFAEPT---------------SDGGGEVTFNNGSSPGGYSPaeFKAD 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   400 FNLLNKYKKlhpdvKTLISVGGwaetggyfdANGNRVASggfytmttnadgsvNTAGINAFAKSAVEFIETYGFDGVDID 479
Cdd:cd02871   66 IKALQAKGK-----KVLISIGG---------ANGHVDLN--------------HTAQEDNFVDSIVAIIKEYGFDGLDID 117
                        170
                 ....*....|....
gi 3928775   480 YEypSSMNDSGHPD 493
Cdd:cd02871  118 LE--SGSNPLNATP 129
GH18_CFLE_spore_hydrolase cd02874
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ...
458-570 1.49e-04

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: 44.95  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775   458 NAFAKSAVEFIETYGFDGVDIDYEYpssMNdsghPDDfpisnarRAGLNAsyqvLMKTLREELDKAGelagkHYMLTIAS 537
Cdd:cd02874   89 QRLINNILALAKKYGYDGVNIDFEN---VP----PED-------REAYTQ----FLRELSDRLHPAG-----YTLSTAVV 145
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 3928775   538 P--SSGYLLRGMETF---QTTKYLDYVNIMSYDLHGAW 570
Cdd:cd02874  146 PktSADQFGNWSGAYdyaAIGKIVDFVVLMTYDWHWRG 183
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
165-276 1.59e-04

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: 45.80  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775    165 GAETTSPANsVTVAeVVPDNYAPTASLTSNAssnTLNLNDNVVLNLSGSDQDGTVTSLELFQDGASVAQISGATG-SFNF 243
Cdd:NF038112 1263 GTKTSAPDT-VTVL-VRNVNRAPVAVAGAPA---TVDERSTVTLDGSGTDADGDALTYAWTQTSGPAVTLTGATTaTATF 1337
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 3928775    244 TATS-AGNTQ--FSLVATDDKGATSDAQTLSFRIVD 276
Cdd:NF038112 1338 TAPEvTADTQltFTLTVSDGTASATDTVTVTVRNVN 1373
Big_13 pfam19077
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ...
186-274 3.57e-04

Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.


Pssm-ID: 465968 [Multi-domain]  Cd Length: 102  Bit Score: 40.71  E-value: 3.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3928775     186 APTASLTS---NASSNTLNLNDNVVLNLSGSDQDGTVTSLELFQDGASVAQI--SGATGSFNFTATSA---GNTQFSLVA 257
Cdd:pfam19077    4 IPTIDLAAgsdTGVSDSDNITNDTTPTFTGTNEDGDVVTVTVSIDGNGVTGTatAGADGNWSFTPPAAladGTYTLTVTV 83
                           90
                   ....*....|....*..
gi 3928775     258 TDDKGATSDAQTLSFRI 274
Cdd:pfam19077   84 TDIAGNTATSSPLSFTI 100
Glucodextran_B pfam09136
Glucodextranase, domain B; Members of this family adopt a structure consisting of seven ...
91-169 3.61e-04

Glucodextranase, domain B; Members of this family adopt a structure consisting of seven/eight-strand antiparallel beta-sheets, in a Greek-key topology, similar to the immunoglobulin beta-sandwich fold. They act as cell wall anchors, where they interact with the S-layer present in the cell wall of Gram-positive bacteria by hydrophobic interactions. In glucodextranase, Domain B is buried in the S-layer, and a flexible linker located between domain B and the catalytic unit confers motion to the catalytic unit, which is capable of efficient hydrolysis of the substrates located close to the cell surface.


Pssm-ID: 430428 [Multi-domain]  Cd Length: 83  Bit Score: 40.16  E-value: 3.61e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3928775      91 PIAEVLSPMSGSSfTEGDSVVIEAQTSDSDGTVVKlevlVDGVAIATLSSAPYSTTWLAVTGQHQISVRATDDKGAETT 169
Cdd:pfam09136    1 PELTITSPADGLT-TNRETVTVTGTVADANLDSVT----VNGIAATVYKDGTFSKRILLVEGENVITVIAVDSAGNTVT 74
Big_7 pfam17957
Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in ...
189-257 5.27e-04

Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in glycosyl hydrolase enzymes.


Pssm-ID: 436171 [Multi-domain]  Cd Length: 67  Bit Score: 39.13  E-value: 5.27e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3928775     189 ASLTSNASSNTLNlNDNVVLNLSGSDqDGTVTSLELFQDGASVAQISGATGSFNFTATSAGNTQFSLVA 257
Cdd:pfam17957    1 VSITSPANGATVS-GGTVTISATASD-DGGVSKVEFYVDGTLVGTDTSAPYSFTWTTTALANGTHTITV 67
 
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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