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Conserved domains on  [gi|2410340890|ref|WP_268382043|]
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glycoside hydrolase family 18 protein [Bacillus altitudinis]

Protein Classification

glycoside hydrolase family 18 protein( domain architecture ID 18526950)

glycoside hydrolase family 18 protein similar to Bacillus megaterium spore cortex-lytic enzyme SleL, a peptidoglycan lysin involved in germination of spores

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GH18_CFLE_spore_hydrolase cd02874
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ...
 107-421 2.82e-145

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: 416.28  E-value: 2.82e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 107 SNAYIEPRGNQVSEnlkqAAREASPYLTHLGAFSFQAQRDGTLREPPLDQLPQIAAQSRTVLSMVVTNLENDKFSDELGR 186
Cdd:cd02874     4 VLGYYTPRNGSDYE----SLRANAPYLTYIAPFWYGVDADGTLTGLPDERLIEAAKRRGVKPLLVITNLTNGNFDSELAH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 187 ILLTNQSVKTTLLNEIVRVAQKYQLKEIHFDFEYLRPVDKEAYLQFLREATTRFHQQGWTISVALAPKTSSEQKGKWYEA 266
Cdd:cd02874    80 AVLSNPEARQRLINNILALAKKYGYDGVNIDFENVPPEDREAYTQFLRELSDRLHPAGYTLSTAVVPKTSADQFGNWSGA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 267 HDYEAIGKIVDHVVLMTYEWGYSGGPAQAVSPIGPVRQVIEYALTVIPANKIVMGQNLYGYDWTLPYVQGGPiAKAVSPQ 346
Cdd:cd02874   160 YDYAAIGKIVDFVVLMTYDWHWRGGPPGPVAPIGWVERVLQYAVTQIPREKILLGIPLYGYDWTLPYKKGGK-ASTISPQ 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2410340890 347 QAIAIARENNVSILYDETAQAPYFRYTDANNKEHEVWFEDARSIQAKFNLIKELNLNGIAYWKLGLSFPQNWLLL 421
Cdd:cd02874   239 QAINLAKRYGAEIQYDEEAQSPFFRYVDEQGRRHEVWFEDARSLQAKFELAKEYGLRGVSYWRLGLEDPQNWLLL 313
LysM smart00257
Lysin motif;
5-48 1.06e-11

Lysin motif;


:

Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 59.38  E-value: 1.06e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2410340890    5 IYVVKRGDTLNEIAMRFKTTVNEIIRTNDIETPNQLVVGQTIVI 48
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
2-90 3.35e-08

LysM repeat [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 52.79  E-value: 3.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890   2 TIQIYVVKRGDTLNEIAMRFKTTVNEIIRTndietpnqlvvgqtivipirgqfYEVKQNDTLYQIGRRFQISVEELARVN 81
Cdd:COG1388    82 AAARYTVKSGDTLSGIARRYGAAAAPSPVT-----------------------YTVKKGDTLWSIARRYGVSVEELKRWN 138


                  ....*....
gi 2410340890  82 RIRPEAILP 90
Cdd:COG1388   139 GLSSDTIRP 147
 
Name Accession Description Interval E-value
GH18_CFLE_spore_hydrolase cd02874
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ...
 107-421 2.82e-145

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: 416.28  E-value: 2.82e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 107 SNAYIEPRGNQVSEnlkqAAREASPYLTHLGAFSFQAQRDGTLREPPLDQLPQIAAQSRTVLSMVVTNLENDKFSDELGR 186
Cdd:cd02874     4 VLGYYTPRNGSDYE----SLRANAPYLTYIAPFWYGVDADGTLTGLPDERLIEAAKRRGVKPLLVITNLTNGNFDSELAH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 187 ILLTNQSVKTTLLNEIVRVAQKYQLKEIHFDFEYLRPVDKEAYLQFLREATTRFHQQGWTISVALAPKTSSEQKGKWYEA 266
Cdd:cd02874    80 AVLSNPEARQRLINNILALAKKYGYDGVNIDFENVPPEDREAYTQFLRELSDRLHPAGYTLSTAVVPKTSADQFGNWSGA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 267 HDYEAIGKIVDHVVLMTYEWGYSGGPAQAVSPIGPVRQVIEYALTVIPANKIVMGQNLYGYDWTLPYVQGGPiAKAVSPQ 346
Cdd:cd02874   160 YDYAAIGKIVDFVVLMTYDWHWRGGPPGPVAPIGWVERVLQYAVTQIPREKILLGIPLYGYDWTLPYKKGGK-ASTISPQ 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2410340890 347 QAIAIARENNVSILYDETAQAPYFRYTDANNKEHEVWFEDARSIQAKFNLIKELNLNGIAYWKLGLSFPQNWLLL 421
Cdd:cd02874   239 QAINLAKRYGAEIQYDEEAQSPFFRYVDEQGRRHEVWFEDARSLQAKFELAKEYGLRGVSYWRLGLEDPQNWLLL 313
Glyco_18 smart00636
Glyco_18 domain;
130-412 1.83e-39

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 144.36  E-value: 1.83e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890  130 SPYLTHLGAFSFQAQRDGTLREPPLD-------QLPQIAAQSRTVLSMV-VTNL-ENDKFSDelgriLLTNQSVKTTLLN 200
Cdd:smart00636  23 ASKLTHIIYAFANIDPDGTVTIGDEWadignfgQLKALKKKNPGLKVLLsIGGWtESDNFSS-----MLSDPASRKKFID 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890  201 EIVRVAQKYQLKEIHFDFEY--LRPVDKEAYLQFLREATTRFHQQ-----GWTISVALAPKTSSEQKGKWYeahdYEAIG 273
Cdd:smart00636  98 SIVSFLKKYGFDGIDIDWEYpgGRGDDRENYTALLKELREALDKEgaegkGYLLTIAVPAGPDKIDKGYGD----LPAIA 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890  274 KIVDHVVLMTYEW-GYSGGPAQAVSPI-----GPVRQVIEYALTV-----IPANKIVMGQNLYGYDWTLpyVQG---GPI 339
Cdd:smart00636 174 KYLDFINLMTYDFhGAWSNPTGHNAPLyagpgDPEKYNVDYAVKYylckgVPPSKLVLGIPFYGRGWTL--VDGsnnGPG 251

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890  340 AKAVSPQQAIAIARENNV------------SILYDETAQAPYfrYTDANNKeHEVWFEDARSIQAKFNLIKELNLNGIAY 407
Cdd:smart00636 252 APFTGPATGGPGTWEGGVvdyreickllgaTVVYDDTAKAPY--AYNPGTG-QWVSYDDPRSIKAKADYVKDKGLGGVMI 328


                   ....*
gi 2410340890  408 WKLGL 412
Cdd:smart00636 329 WELDA 333
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
176-411 3.45e-27

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 110.24  E-value: 3.45e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 176 ENDKFSDelgrILLTNQSVKTtLLNEIVRVAQKYQLKEIHFDFEY--LRPVDKEAYLQFLREATTRFHQ----QGWTISV 249
Cdd:pfam00704  75 DSTGFSL----MASNPASRKK-FADSIVSFLRKYGFDGIDIDWEYpgGNPEDKENYDLLLRELRAALDEakggKKYLLSA 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 250 ALAPKtsseqKGKWYEAHDYEAIGKIVDHVVLMTYewGYSGGPAQAVSPIGPVR---------QVIEYALTVIPANKIVM 320
Cdd:pfam00704 150 AVPAS-----YPDLDKGYDLPKIAKYLDFINVMTY--DFHGSWDNVTGHHAPLYgggsynvdyAVKYYLKQGVPASKLVL 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 321 GQNLYGYDWTLPYVQGGPIAKAV-SPQQAIAIARENNVSILYDETAQAPYfrytdANNKEHEVWFEDARSIQAKFNLIKE 399
Cdd:pfam00704 223 GVPFYGRSWTLVNGSGNTWEDGVlAYKEICNLLKDNGATVVWDDVAKAPY-----VYDGDQFITYDDPRSIATKVDYVKA 297

                         250
                  ....*....|..
gi 2410340890 400 LNLNGIAYWKLG 411
Cdd:pfam00704 298 KGLGGVMIWSLD 309
ChiA COG3325
Chitinase, GH18 family [Carbohydrate transport and metabolism];
203-420 6.36e-17

Chitinase, GH18 family [Carbohydrate transport and metabolism];


Pssm-ID: 442554 [Multi-domain]  Cd Length: 391  Bit Score: 81.88  E-value: 6.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 203 VRVAQKYQLKEIHFDFEY----------LRPVDKEAYLQFLRE------ATTRFHQQGWTISVALAPktsseqkGKWYEA 266
Cdd:COG3325   133 VDLLRKYNFDGIDIDWEYpgsggapgnvYRPEDKANFTALLKElraqldALGAETGKHYLLTAAAPA-------GPDKLD 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 267 H-DYEAIGKIVDHVVLMTYewGYSGGPAQAVSPIGP--------------VRQVIEYALTV-IPANKIVMGQNLYGYDWT 330
Cdd:COG3325   206 GiELPKVAQYLDYVNVMTY--DFHGAWSPTTGHQAPlydspkdpeaqgysVDSAVQAYLAAgVPASKLVLGVPFYGRGWT 283

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 331 -LPYVQGGPIAKAVSPQQAIAIARENNVSIL-------------YDETAQAPYFrYtdaNNKEHEVW-FEDARSIQAKFN 395
Cdd:COG3325   284 gVTGGNNGLYQPATGPAPGTWEAGVNDYKDLkalylgsngytryWDDVAKAPYL-Y---NGDTGTFIsYDDPRSIAAKAD 359

                         250       260
                  ....*....|....*....|....*
gi 2410340890 396 LIKELNLNGIAYWKLGLSFPQNWLL 420
Cdd:COG3325   360 YVKDKGLGGVMFWELSGDTADGTLL 384
LysM smart00257
Lysin motif;
5-48 1.06e-11

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 59.38  E-value: 1.06e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2410340890    5 IYVVKRGDTLNEIAMRFKTTVNEIIRTNDIETPNQLVVGQTIVI 48
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 4-48 1.13e-11

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 59.04  E-value: 1.13e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2410340890   4 QIYVVKRGDTLNEIAMRFKTTVNEIIRTNDIETPNQLVVGQTIVI 48
Cdd:cd00118     1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 6-49 3.87e-11

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 57.79  E-value: 3.87e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2410340890   6 YVVKRGDTLNEIAMRFKTTVNEIIRTNDIETPNqLVVGQTIVIP 49
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPN-LYVGQKLKIP 43
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
2-49 4.96e-11

LysM repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 60.88  E-value: 4.96e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2410340890   2 TIQIYVVKRGDTLNEIAMRFKTTVNEIIRTNDIeTPNQLVVGQTIVIP 49
Cdd:COG1388   108 SPVTYTVKKGDTLWSIARRYGVSVEELKRWNGL-SSDTIRPGQKLKIP 154
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
2-90 3.35e-08

LysM repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 52.79  E-value: 3.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890   2 TIQIYVVKRGDTLNEIAMRFKTTVNEIIRTndietpnqlvvgqtivipirgqfYEVKQNDTLYQIGRRFQISVEELARVN 81
Cdd:COG1388    82 AAARYTVKSGDTLSGIARRYGAAAAPSPVT-----------------------YTVKKGDTLWSIARRYGVSVEELKRWN 138


                  ....*....
gi 2410340890  82 RIRPEAILP 90
Cdd:COG1388   139 GLSSDTIRP 147
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 55-90 2.05e-07

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 47.01  E-value: 2.05e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2410340890  55 YEVKQNDTLYQIGRRFQISVEELARVNRIRPEAILP 90
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYV 36
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 5-81 2.38e-07

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 52.81  E-value: 2.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890   5 IYVVKRGDTLNEIAMRFKTTVNEIIRTNDIETpNQLVVGQTIVIPIRGQF-----------YEVKQNDTLYQIGRRFQIS 73
Cdd:PRK10783  345 SYKVRSGDTLSGIASRLNVSTKDLQQWNNLRG-SKLKVGQTLTIGAGSSAqrlannsdsitYRVRKGDSLSSIAKRHGVN 423


                  ....*...
gi 2410340890  74 VEELARVN 81
Cdd:PRK10783  424 IKDVMRWN 431
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 53-91 7.94e-07

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 45.55  E-value: 7.94e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2410340890  53 QFYEVKQNDTLYQIGRRFQISVEELARVNRIRPEAILPV 91
Cdd:cd00118     1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYP 39
LysM smart00257
Lysin motif;
54-83 1.87e-06

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 44.36  E-value: 1.87e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 2410340890   54 FYEVKQNDTLYQIGRRFQISVEELARVNRI 83
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNI 30
 
Name Accession Description Interval E-value
GH18_CFLE_spore_hydrolase cd02874
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ...
 107-421 2.82e-145

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: 416.28  E-value: 2.82e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 107 SNAYIEPRGNQVSEnlkqAAREASPYLTHLGAFSFQAQRDGTLREPPLDQLPQIAAQSRTVLSMVVTNLENDKFSDELGR 186
Cdd:cd02874     4 VLGYYTPRNGSDYE----SLRANAPYLTYIAPFWYGVDADGTLTGLPDERLIEAAKRRGVKPLLVITNLTNGNFDSELAH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 187 ILLTNQSVKTTLLNEIVRVAQKYQLKEIHFDFEYLRPVDKEAYLQFLREATTRFHQQGWTISVALAPKTSSEQKGKWYEA 266
Cdd:cd02874    80 AVLSNPEARQRLINNILALAKKYGYDGVNIDFENVPPEDREAYTQFLRELSDRLHPAGYTLSTAVVPKTSADQFGNWSGA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 267 HDYEAIGKIVDHVVLMTYEWGYSGGPAQAVSPIGPVRQVIEYALTVIPANKIVMGQNLYGYDWTLPYVQGGPiAKAVSPQ 346
Cdd:cd02874   160 YDYAAIGKIVDFVVLMTYDWHWRGGPPGPVAPIGWVERVLQYAVTQIPREKILLGIPLYGYDWTLPYKKGGK-ASTISPQ 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2410340890 347 QAIAIARENNVSILYDETAQAPYFRYTDANNKEHEVWFEDARSIQAKFNLIKELNLNGIAYWKLGLSFPQNWLLL 421
Cdd:cd02874   239 QAINLAKRYGAEIQYDEEAQSPFFRYVDEQGRRHEVWFEDARSLQAKFELAKEYGLRGVSYWRLGLEDPQNWLLL 313
Glyco_18 smart00636
Glyco_18 domain;
130-412 1.83e-39

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 144.36  E-value: 1.83e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890  130 SPYLTHLGAFSFQAQRDGTLREPPLD-------QLPQIAAQSRTVLSMV-VTNL-ENDKFSDelgriLLTNQSVKTTLLN 200
Cdd:smart00636  23 ASKLTHIIYAFANIDPDGTVTIGDEWadignfgQLKALKKKNPGLKVLLsIGGWtESDNFSS-----MLSDPASRKKFID 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890  201 EIVRVAQKYQLKEIHFDFEY--LRPVDKEAYLQFLREATTRFHQQ-----GWTISVALAPKTSSEQKGKWYeahdYEAIG 273
Cdd:smart00636  98 SIVSFLKKYGFDGIDIDWEYpgGRGDDRENYTALLKELREALDKEgaegkGYLLTIAVPAGPDKIDKGYGD----LPAIA 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890  274 KIVDHVVLMTYEW-GYSGGPAQAVSPI-----GPVRQVIEYALTV-----IPANKIVMGQNLYGYDWTLpyVQG---GPI 339
Cdd:smart00636 174 KYLDFINLMTYDFhGAWSNPTGHNAPLyagpgDPEKYNVDYAVKYylckgVPPSKLVLGIPFYGRGWTL--VDGsnnGPG 251

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890  340 AKAVSPQQAIAIARENNV------------SILYDETAQAPYfrYTDANNKeHEVWFEDARSIQAKFNLIKELNLNGIAY 407
Cdd:smart00636 252 APFTGPATGGPGTWEGGVvdyreickllgaTVVYDDTAKAPY--AYNPGTG-QWVSYDDPRSIKAKADYVKDKGLGGVMI 328


                   ....*
gi 2410340890  408 WKLGL 412
Cdd:smart00636 329 WELDA 333
GH18_trifunctional cd06549
GH18 domain of an uncharacterized family of bacterial proteins, which share a common ...
 142-418 6.58e-34

GH18 domain of an uncharacterized family of bacterial proteins, which share a common three-domain architecture: an N-terminal glycosyl hydrolase family 18 (GH18) domain, a glycosyl transferase family 2 domain, and a C-terminal polysaccharide deacetylase domain.


Pssm-ID: 119366 [Multi-domain]  Cd Length: 298  Bit Score: 128.68  E-value: 6.58e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 142 QAQRDGTLREPPLDQLPQI--AAQSRTVLSMVVTNLENDKFSDELGRILLTNQSVKTTLLNEIVRVAQKYQLKEIHFDFE 219
Cdd:cd06549    34 LTGPEGRIDVFVDPQGVAIiaAAKAHPKVLPLVQNISGGAWDGKNIARLLADPSARAKFIANIAAYLERNQADGIVLDFE 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 220 YLRPVDKEAYLQFLREATTRFHQQGWTISValapkTSSEQKGKWyeahDYEAIGKIVDHVVLMTYEWGYSGGPAQAVSPI 299
Cdd:cd06549   114 ELPADDLPKYVAFLSELRRRLPAQGKQLTV-----TVPADEADW----NLKALARNADKLILMAYDEHYQGGAPGPIASQ 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 300 GPVRQVIEYALTVIPANKIVMGQNLYGYDWTlpyvQGGPIAKAVSPQQAIAIARENNVSILYDETAQAPYFrYTDANNKE 379
Cdd:cd06549   185 DWFESNLAQAVKKLPPEKLIVALGSYGYDWT----KGGNTKAISSEAAWLLAAHASAAVKFDDKASNATYF-FYDDEGVS 259

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2410340890 380 HEVWFEDARSIQAKFNLIKELNLNGIAYWKLGLSFPQNW 418
Cdd:cd06549   260 HEVWMLDAVTLFNQLKAVQRLGPAGVALWRLGSEDPGLW 298
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
176-411 3.45e-27

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 110.24  E-value: 3.45e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 176 ENDKFSDelgrILLTNQSVKTtLLNEIVRVAQKYQLKEIHFDFEY--LRPVDKEAYLQFLREATTRFHQ----QGWTISV 249
Cdd:pfam00704  75 DSTGFSL----MASNPASRKK-FADSIVSFLRKYGFDGIDIDWEYpgGNPEDKENYDLLLRELRAALDEakggKKYLLSA 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 250 ALAPKtsseqKGKWYEAHDYEAIGKIVDHVVLMTYewGYSGGPAQAVSPIGPVR---------QVIEYALTVIPANKIVM 320
Cdd:pfam00704 150 AVPAS-----YPDLDKGYDLPKIAKYLDFINVMTY--DFHGSWDNVTGHHAPLYgggsynvdyAVKYYLKQGVPASKLVL 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 321 GQNLYGYDWTLPYVQGGPIAKAV-SPQQAIAIARENNVSILYDETAQAPYfrytdANNKEHEVWFEDARSIQAKFNLIKE 399
Cdd:pfam00704 223 GVPFYGRSWTLVNGSGNTWEDGVlAYKEICNLLKDNGATVVWDDVAKAPY-----VYDGDQFITYDDPRSIATKVDYVKA 297

                         250
                  ....*....|..
gi 2410340890 400 LNLNGIAYWKLG 411
Cdd:pfam00704 298 KGLGGVMIWSLD 309
GH18_SI-CLP cd02876
Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein ...
 178-411 5.67e-22

Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein of unknown function that interacts with the endocytic/sorting transmembrane receptor stabilin-1 and is secreted from the lysosome. SI-CLP has a glycosyl hydrolase family 18 (GH18) domain but lacks a chitin-binding domain. The catalytic amino acids of the GH18 domain are not conserved in SI-CLP, similar to the chitolectins YKL-39, YKL-40, and YM1/2. Human SI-CLP is sorted to late endosomes and secretory lysosomes in alternatively activated macrophages.


Pssm-ID: 119355 [Multi-domain]  Cd Length: 318  Bit Score: 95.84  E-value: 5.67e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 178 DKFSDELGRILLTNQSVKTTLLNEIVRVAQKYqlkeiHFD---FE-------YLRPVDKEAYLQFLREATTRFHQQGWTI 247
Cdd:cd02876    76 EGWSYQDLQSLLNDEQEREKLIKLLVTTAKKN-----HFDgivLEvwsqlaaYGVPDKRKELIQLVIHLGETLHSANLKL 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 248 SVALAPKTSSEQKGKWYEAHDYEAIGKIVDHVVLMTYEWGySGGPAQAVSPIGPVRQVIEYALTVIPAN--KIVMGQNLY 325
Cdd:cd02876   151 ILVIPPPREKGNQNGLFTRKDFEKLAPHVDGFSLMTYDYS-SPQRPGPNAPLSWVRSCLELLLPESGKKraKILLGLNFY 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 326 GYDWTLPYvQGGPIAKAvspqQAIAIARENNVSILYDETAQAPYFRYTDANNKeHEVWFEDARSIQAKFNLIKELNLnGI 405
Cdd:cd02876   230 GNDYTLPG-GGGAITGS----EYLKLLKSNKPKLQWDEKSAEHFFEYKNKGGK-HAVFYPTLKSIQLRLDLAKELGT-GI 302


                  ....*.
gi 2410340890 406 AYWKLG 411
Cdd:cd02876   303 SIWELG 308
GH18_chitobiase cd02875
Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes ...
 189-431 1.99e-21

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: 94.81  E-value: 1.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 189 LTNQSVKTTLLNEIVRVAQKYQLKEIHFDFEYlrPVDK-----EAYLQFLREATTRFHQQGW----TISVALAPKTSSeq 259
Cdd:cd02875    91 ISNPTYRTQWIQQKVELAKSQFMDGINIDIEQ--PITKgspeyYALTELVKETTKAFKKENPgyqiSFDVAWSPSCID-- 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 260 kgkwYEAHDYEAIGKIVDHVVLMTYEWG--YSGGP--AQAVSPIGPVRQ-VIEYALTVIPANKIVMGQNLYGYDW----- 329
Cdd:cd02875   167 ----KRCYDYTGIADASDFLVVMDYDEQsqIWGKEciAGANSPYSQTLSgYNNFTKLGIDPKKLVMGLPWYGYDYpclng 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 330 -------TLPYV--QGGPIAKAVSPQ----QAIAIARENNVSILYDETAQAPYFRYTDANNKEHEVWFEDARSIQAKFNL 396
Cdd:cd02875   243 nledvvcTIPKVpfRGANCSDAAGRQipysEIMKQINSSIGGRLWDSEQKSPFYNYKDKQGNLHQVWYDNPQSLSIKVAY 322

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2410340890 397 IKELNLNGIAYWKLglsfpqNWLLLSDQFNIEKRT 431
Cdd:cd02875   323 AKNLGLKGIGMWNG------DLLDYSGLPIAEKQT 351
ChiA COG3325
Chitinase, GH18 family [Carbohydrate transport and metabolism];
203-420 6.36e-17

Chitinase, GH18 family [Carbohydrate transport and metabolism];


Pssm-ID: 442554 [Multi-domain]  Cd Length: 391  Bit Score: 81.88  E-value: 6.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 203 VRVAQKYQLKEIHFDFEY----------LRPVDKEAYLQFLRE------ATTRFHQQGWTISVALAPktsseqkGKWYEA 266
Cdd:COG3325   133 VDLLRKYNFDGIDIDWEYpgsggapgnvYRPEDKANFTALLKElraqldALGAETGKHYLLTAAAPA-------GPDKLD 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 267 H-DYEAIGKIVDHVVLMTYewGYSGGPAQAVSPIGP--------------VRQVIEYALTV-IPANKIVMGQNLYGYDWT 330
Cdd:COG3325   206 GiELPKVAQYLDYVNVMTY--DFHGAWSPTTGHQAPlydspkdpeaqgysVDSAVQAYLAAgVPASKLVLGVPFYGRGWT 283

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 331 -LPYVQGGPIAKAVSPQQAIAIARENNVSIL-------------YDETAQAPYFrYtdaNNKEHEVW-FEDARSIQAKFN 395
Cdd:COG3325   284 gVTGGNNGLYQPATGPAPGTWEAGVNDYKDLkalylgsngytryWDDVAKAPYL-Y---NGDTGTFIsYDDPRSIAAKAD 359

                         250       260
                  ....*....|....*....|....*
gi 2410340890 396 LIKELNLNGIAYWKLGLSFPQNWLL 420
Cdd:COG3325   360 YVKDKGLGGVMFWELSGDTADGTLL 384
GH18_chitinase cd06548
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ...
 178-411 2.15e-15

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: 76.52  E-value: 2.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 178 DKFSDelgrILLTNQSVKTtLLNEIVRVAQKYQLKEIHFDFEY----------LRPVDKEAYLQFLREATTRFHQQGWT- 246
Cdd:cd06548    98 GGFSD----AAATEASRAK-FADSAVDFIRKYGFDGIDIDWEYpgsggapgnvARPEDKENFTLLLKELREALDALGAEt 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 247 -----ISVALapkTSSEQKgkwYEAHDYEAIGKIVDHVVLMTYE-----WGYSG-------GPAQAVSPIGPVRQVIEYA 309
Cdd:cd06548   173 grkylLTIAA---PAGPDK---LDKLEVAEIAKYLDFINLMTYDfhgawSNTTGhhsnlyaSPADPPGGYSVDAAVNYYL 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 310 LTVIPANKIVMGQNLYGYDWTlpyvqggpiakavspqqaiaiarenNVSILYDETAQAPYFryTDANNKehEVW-FEDAR 388
Cdd:cd06548   247 SAGVPPEKLVLGVPFYGRGWT-------------------------GYTRYWDEVAKAPYL--YNPSTK--TFIsYDDPR 297

                         250       260
                  ....*....|....*....|...
gi 2410340890 389 SIQAKFNLIKELNLNGIAYWKLG 411
Cdd:cd06548   298 SIKAKADYVKDKGLGGVMFWELS 320
GH18_chitolectin_chitotriosidase cd02872
This conserved domain family includes a large number of catalytically inactive chitinase-like ...
 157-410 3.51e-15

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: 76.44  E-value: 3.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 157 LPQIAAQSRTVLSMVVTNLENDKFSDelgriLLTNQSVKTTLLNEIVRVAQKYQLKEIHFDFEY-----LRPVDKEAYLQ 231
Cdd:cd02872    64 LKEKNPNLKTLLAIGGWNFGSAKFSA-----MAASPENRKTFIKSAIAFLRKYGFDGLDLDWEYpgqrgGPPEDKENFVT 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 232 FLREATTRFHQQGW----TISVALAPKTSSEqkgkwyeAHDYEAIGKIVDHVVLMTYE----WG---------YSGGPAQ 294
Cdd:cd02872   139 LLKELREAFEPEAPrlllTAAVSAGKETIDA-------AYDIPEISKYLDFINVMTYDfhgsWEgvtghnsplYAGSADT 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 295 AVSPIGPVRQVIEYALTV-IPANKIVMGQNLYGYDWTLPY-VQGGPIAKAVSPQQAIAIARE--------------NNVS 358
Cdd:cd02872   212 GDQKYLNVDYAIKYWLSKgAPPEKLVLGIPTYGRSFTLASpSNTGVGAPASGPGTAGPYTREagflayyeiceflkSGWT 291

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2410340890 359 ILYDETAQAPYfrytdANNKEHEVWFEDARSIQAKFNLIKELNLNGIAYWKL 410
Cdd:cd02872   292 VVWDDEQKVPY-----AYKGNQWVGYDDEESIALKVQYLKSKGLGGAMVWSI 338
LysM smart00257
Lysin motif;
5-48 1.06e-11

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 59.38  E-value: 1.06e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2410340890    5 IYVVKRGDTLNEIAMRFKTTVNEIIRTNDIETPNQLVVGQTIVI 48
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 4-48 1.13e-11

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 59.04  E-value: 1.13e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2410340890   4 QIYVVKRGDTLNEIAMRFKTTVNEIIRTNDIETPNQLVVGQTIVI 48
Cdd:cd00118     1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 6-49 3.87e-11

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 57.79  E-value: 3.87e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2410340890   6 YVVKRGDTLNEIAMRFKTTVNEIIRTNDIETPNqLVVGQTIVIP 49
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPN-LYVGQKLKIP 43
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
2-49 4.96e-11

LysM repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 60.88  E-value: 4.96e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2410340890   2 TIQIYVVKRGDTLNEIAMRFKTTVNEIIRTNDIeTPNQLVVGQTIVIP 49
Cdd:COG1388   108 SPVTYTVKKGDTLWSIARRYGVSVEELKRWNGL-SSDTIRPGQKLKIP 154
GH18_chitinase-like cd00598
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ...
 185-284 6.79e-11

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: 61.62  E-value: 6.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 185 GRILLTNQSVKTTLLNEIVRVAQKYQLKEIHFDFEY---LRPVDKEAYLQFLREATTRFHQQGWTISVALAPKTSSEQKG 261
Cdd:cd00598    79 PFTLASDPASRAAFANSLVSFLKTYGFDGVDIDWEYpgaADNSDRENFITLLRELRSALGAANYLLTIAVPASYFDLGYA 158

                          90       100
                  ....*....|....*....|...
gi 2410340890 262 KwyeahDYEAIGKIVDHVVLMTY 284
Cdd:cd00598   159 Y-----DVPAIGDYVDFVNVMTY 176
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
2-90 3.35e-08

LysM repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 52.79  E-value: 3.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890   2 TIQIYVVKRGDTLNEIAMRFKTTVNEIIRTndietpnqlvvgqtivipirgqfYEVKQNDTLYQIGRRFQISVEELARVN 81
Cdd:COG1388    82 AAARYTVKSGDTLSGIARRYGAAAAPSPVT-----------------------YTVKKGDTLWSIARRYGVSVEELKRWN 138


                  ....*....
gi 2410340890  82 RIRPEAILP 90
Cdd:COG1388   139 GLSSDTIRP 147
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 55-90 2.05e-07

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 47.01  E-value: 2.05e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2410340890  55 YEVKQNDTLYQIGRRFQISVEELARVNRIRPEAILP 90
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYV 36
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 5-81 2.38e-07

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 52.81  E-value: 2.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890   5 IYVVKRGDTLNEIAMRFKTTVNEIIRTNDIETpNQLVVGQTIVIPIRGQF-----------YEVKQNDTLYQIGRRFQIS 73
Cdd:PRK10783  345 SYKVRSGDTLSGIASRLNVSTKDLQQWNNLRG-SKLKVGQTLTIGAGSSAqrlannsdsitYRVRKGDSLSSIAKRHGVN 423


                  ....*...
gi 2410340890  74 VEELARVN 81
Cdd:PRK10783  424 IKDVMRWN 431
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 53-91 7.94e-07

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 45.55  E-value: 7.94e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2410340890  53 QFYEVKQNDTLYQIGRRFQISVEELARVNRIRPEAILPV 91
Cdd:cd00118     1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYP 39
LysM smart00257
Lysin motif;
54-83 1.87e-06

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 44.36  E-value: 1.87e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 2410340890   54 FYEVKQNDTLYQIGRRFQISVEELARVNRI 83
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNI 30
GH18_plant_chitinase_class_V cd02879
The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the ...
 270-411 2.68e-06

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: 48.90  E-value: 2.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 270 EAIGKIVDHVVLMTYE-----WGYSGGPAQA-------VSPIGPVRQVIEYALtviPANKIVMGQNLYGYDWTlpyvqgg 337
Cdd:cd02879   175 EAINKNLDWVNVMAYDyygswESNTTGPAAAlydpnsnVSTDYGIKSWIKAGV---PAKKLVLGLPLYGRAWT------- 244

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2410340890 338 piakavspqqaiaiarennvsiLYDETAQAPYfrytdanNKEHEVW--FEDARSIQAKFNLIKELNLNGIAYWKLG 411
Cdd:cd02879   245 ----------------------LYDTTTVSSY-------VYAGTTWigYDDVQSIAVKVKYAKQKGLLGYFAWAVG 291
GH18_zymocin_alpha cd02878
Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle ...
 197-408 4.78e-06

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: 48.46  E-value: 4.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 197 TLLNEIVRVAQKYQLKEIHFDFEYL-----------RPVDKEAYLQFLREATTRFhQQGWTISVAlAPKTSseqkgkWY- 264
Cdd:cd02878    94 TFANNVVNFVNKYNLDGVDFDWEYPgapdipgipagDPDDGKNYLEFLKLLKSKL-PSGKSLSIA-APASY------WYl 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 265 EAHDYEAIGKIVDHVVLMTYE----WGYSGGPAQAVSPIG-------PVRQVIEyALTVI-----PANKIVMGQNLYG-- 326
Cdd:cd02878   166 KGFPIKDMAKYVDYIVYMTYDlhgqWDYGNKWASPGCPAGnclrshvNKTETLD-ALSMItkagvPSNKVVVGVASYGrs 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 327 --------YDWTLPYVQGGPIAKA----------VSPQQAIAIARENNVSILYDETAQAPYFRYTDANNkeheVWFEDAR 388
Cdd:cd02878   245 fkmadpgcTGPGCTFTGPGSGAEAgrctctagygAISEIEIIDISKSKNKRWYDTDSDSDILVYDDDQW----VAYMSPA 320

                         250       260
                  ....*....|....*....|
gi 2410340890 389 SIQAKFNLIKELNLNGIAYW 408
Cdd:cd02878   321 TKAARIEWYKGLNFGGTSDW 340
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 4-49 4.86e-06

Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion transport and metabolism];


Pssm-ID: 441258 [Multi-domain]  Cd Length: 163  Bit Score: 46.54  E-value: 4.86e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2410340890   4 QIYVVKRGDTLNEIAMRF---KTTVNEIIRTN--DIETPNQLVVGQTIVIP 49
Cdd:COG1652   110 KTYTVKPGDTLWGIAKRFygdPARWPEIAEANrdQIKNPDLIYPGQVLRIP 160
GH18_3CO4_chitinase cd06545
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an ...
 132-330 3.20e-04

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: 42.05  E-value: 3.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 132 YLTHLGAFSFQAQRDGTLR-EPPLDQLPQI--AAQSRTVLsmVVTNLENDKFSDELGRILlTNQSVKTtLLNEIVRVAQK 208
Cdd:cd06545    22 KLTHINLAFANPDANGTLNaNPVRSELNSVvnAAHAHNVK--ILISLAGGSPPEFTAALN-DPAKRKA-LVDKIINYVVS 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410340890 209 YQLKEIHFDFEYLRpVDKEAYLQFLREATTRFHQQGWTISVALAPKTSSEQKGKWYEAHDYeaigkivdhVVLMTYE--- 285
Cdd:cd06545    98 YNLDGIDVDLEGPD-VTFGDYLVFIRALYAALKKEGKLLTAAVSSWNGGAVSDSTLAYFDF---------INIMSYDatg 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2410340890 286 --WGYSGGP----AQAVSPIG--PVRQVIeyaltviPANKIVMGQNLYGYDWT 330
Cdd:cd06545   168 pwWGDNPGQhssyDDAVNDLNywNERGLA-------SKDKLVLGLPFYGYGFY 213
 
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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