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Conserved domains on  [gi|665939010|ref|WP_031305057|]
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MULTISPECIES: glycoside hydrolase family 18 protein [Bacillus]

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 ...
 110-426 1.16e-158

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: 450.56  E-value: 1.16e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 110 IETNAYIEPRGESVSPALqqaaREASPYLTYLGAFSFQAKRDGTLEEPPLNNLKEIADRHRTTMMMIVTNLENEAFSDEL 189
Cdd:cd02874    2 IEVLGYYTPRNGSDYESL----RANAPYLTYIAPFWYGVDADGTLTGLPDERLIEAAKRRGVKPLLVITNLTNGNFDSEL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 190 GRIILTDQNVKNRLLDNIVAAARRYGFKDIHFDFEYLRPEDREAYNQFLRDARARFKQEGWFISTALAPKTRADQPGQWY 269
Cdd:cd02874   78 AHAVLSNPEARQRLINNILALAKKYGYDGVNIDFENVPPEDREAYTQFLRELSDRLHPAGYTLSTAVVPKTSADQFGNWS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 270 EAHDYRAHGEIVDFVVLMTYEWGYSGGPPMAVSPIGPVRDVIEYALTEMPASKIVMGQNLYGYDWTLPYtPGGQLARAIS 349
Cdd:cd02874  158 GAYDYAAIGKIVDFVVLMTYDWHWRGGPPGPVAPIGWVERVLQYAVTQIPREKILLGIPLYGYDWTLPY-KKGGKASTIS 236

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665939010 350 PQRAIAIASENNAAIQYDETAQAPFFRYTDNAGKQHEVWFEDARSIQAKFDLIRELNLRGISYWKLGLSFPQNWLLI 426
Cdd:cd02874  237 PQQAINLAKRYGAEIQYDEEAQSPFFRYVDEQGRRHEVWFEDARSLQAKFELAKEYGLRGVSYWRLGLEDPQNWLLL 313
LysM smart00257
Lysin motif;
10-53 1.58e-14

Lysin motif;


:

Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 67.47  E-value: 1.58e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 665939010    10 IYVVKRGDSLYQIANRYRTTVNEIVATNEIPNPNRLVVGQTIVI 53
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
2-103 7.93e-11

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


:

Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 60.11  E-value: 7.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010   2 RKEAFPIQIYVVKRGDSLYQIANRYRTTVNEIVATneipnpnrlvvgqtivipiagefYEVRQGDTLASIGARFNISPAE 81
Cdd:COG1388   77 EAAAAAAARYTVKSGDTLSGIARRYGAAAAPSPVT-----------------------YTVKKGDTLWSIARRYGVSVEE 133

                         90       100
                 ....*....|....*....|..
gi 665939010  82 LARINRIQvSAILPVGLLLYIP 103
Cdd:COG1388  134 LKRWNGLS-SDTIRPGQKLKIP 154
 
Name Accession Description Interval E-value
GH18_CFLE_spore_hydrolase cd02874
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ...
 110-426 1.16e-158

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: 450.56  E-value: 1.16e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 110 IETNAYIEPRGESVSPALqqaaREASPYLTYLGAFSFQAKRDGTLEEPPLNNLKEIADRHRTTMMMIVTNLENEAFSDEL 189
Cdd:cd02874    2 IEVLGYYTPRNGSDYESL----RANAPYLTYIAPFWYGVDADGTLTGLPDERLIEAAKRRGVKPLLVITNLTNGNFDSEL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 190 GRIILTDQNVKNRLLDNIVAAARRYGFKDIHFDFEYLRPEDREAYNQFLRDARARFKQEGWFISTALAPKTRADQPGQWY 269
Cdd:cd02874   78 AHAVLSNPEARQRLINNILALAKKYGYDGVNIDFENVPPEDREAYTQFLRELSDRLHPAGYTLSTAVVPKTSADQFGNWS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 270 EAHDYRAHGEIVDFVVLMTYEWGYSGGPPMAVSPIGPVRDVIEYALTEMPASKIVMGQNLYGYDWTLPYtPGGQLARAIS 349
Cdd:cd02874  158 GAYDYAAIGKIVDFVVLMTYDWHWRGGPPGPVAPIGWVERVLQYAVTQIPREKILLGIPLYGYDWTLPY-KKGGKASTIS 236

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665939010 350 PQRAIAIASENNAAIQYDETAQAPFFRYTDNAGKQHEVWFEDARSIQAKFDLIRELNLRGISYWKLGLSFPQNWLLI 426
Cdd:cd02874  237 PQQAINLAKRYGAEIQYDEEAQSPFFRYVDEQGRRHEVWFEDARSLQAKFELAKEYGLRGVSYWRLGLEDPQNWLLL 313
Glyco_18 smart00636
Glyco_18 domain;
135-417 2.60e-42

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 152.06  E-value: 2.60e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010   135 SPYLTYLGAFSFQAKRDGTLEEPP-------LNNLKEIADRHRTTMMMI-VTNL-ENEAFSDelgriILTDQNVKNRLLD 205
Cdd:smart00636  23 ASKLTHIIYAFANIDPDGTVTIGDewadignFGQLKALKKKNPGLKVLLsIGGWtESDNFSS-----MLSDPASRKKFID 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010   206 NIVAAARRYGFKDIHFDFEY--LRPEDREAYNQFLRDARARFKQE-----GWFISTALAPKTRADQPGQWYeahdYRAHG 278
Cdd:smart00636  98 SIVSFLKKYGFDGIDIDWEYpgGRGDDRENYTALLKELREALDKEgaegkGYLLTIAVPAGPDKIDKGYGD----LPAIA 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010   279 EIVDFVVLMTYEW-GYSGGPPMAVSPI-----GPVRDVIEYALTE-----MPASKIVMGQNLYGYDWTL----------P 337
Cdd:smart00636 174 KYLDFINLMTYDFhGAWSNPTGHNAPLyagpgDPEKYNVDYAVKYylckgVPPSKLVLGIPFYGRGWTLvdgsnngpgaP 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010   338 YTPGGQLARAISPQRAIA---IASENNAAIQYDETAQAPFfRYtdNAGKQHEVWFEDARSIQAKFDLIRELNLRGISYWK 414
Cdd:smart00636 254 FTGPATGGPGTWEGGVVDyreICKLLGATVVYDDTAKAPY-AY--NPGTGQWVSYDDPRSIKAKADYVKDKGLGGVMIWE 330


                   ...
gi 665939010   415 LGL 417
Cdd:smart00636 331 LDA 333
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
158-416 9.51e-28

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 112.16  E-value: 9.51e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010  158 PLNNLKEIADRHRTTMMMIVTNLENEAFSDelgrIILTDQNVKnRLLDNIVAAARRYGFKDIHFDFEY--LRPEDREAYN 235
Cdd:pfam00704  52 QLKKLKKQKNPGVKVLLSIGGWTDSTGFSL----MASNPASRK-KFADSIVSFLRKYGFDGIDIDWEYpgGNPEDKENYD 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010  236 QFLRDARARFKQ----EGWFISTALAPKtradqPGQWYEAHDYRAHGEIVDFVVLMTY----EWGYSGGPPMAVSPIGP- 306
Cdd:pfam00704 127 LLLRELRAALDEakggKKYLLSAAVPAS-----YPDLDKGYDLPKIAKYLDFINVMTYdfhgSWDNVTGHHAPLYGGGSy 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010  307 -VRDVIEYALTE-MPASKIVMGQNLYGYDWTLPYTPGGQLARAISPQRAI-AIASENNAAIQYDETAQAPFfrYTDNagk 383
Cdd:pfam00704 202 nVDYAVKYYLKQgVPASKLVLGVPFYGRSWTLVNGSGNTWEDGVLAYKEIcNLLKDNGATVVWDDVAKAPY--VYDG--- 276

                         250       260       270
                  ....*....|....*....|....*....|...
gi 665939010  384 QHEVWFEDARSIQAKFDLIRELNLRGISYWKLG 416
Cdd:pfam00704 277 DQFITYDDPRSIATKVDYVKAKGLGGVMIWSLD 309
ChiA COG3325
Chitinase, GH18 family [Carbohydrate transport and metabolism];
185-425 2.05e-18

Chitinase, GH18 family [Carbohydrate transport and metabolism];


Pssm-ID: 442554 [Multi-domain]  Cd Length: 391  Bit Score: 86.50  E-value: 2.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 185 FSDelgrIILTDQNVKnRLLDNIVAAARRYGFKDIHFDFEY----------LRPEDREAYNQFLRDARARFKQEG----- 249
Cdd:COG3325  115 FSD----AAATPASRA-AFVDSCVDLLRKYNFDGIDIDWEYpgsggapgnvYRPEDKANFTALLKELRAQLDALGaetgk 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 250 -WFISTALAPktradqpGQWYEAH-DYRAHGEIVDFVVLMTYE----WGYSGGP--PMAVSPIGPVRD------VIEYAL 315
Cdd:COG3325  190 hYLLTAAAPA-------GPDKLDGiELPKVAQYLDYVNVMTYDfhgaWSPTTGHqaPLYDSPKDPEAQgysvdsAVQAYL 262

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 316 TE-MPASKIVMGQNLYGYDWTL--PYTPG-GQLARAISPQRAIA-----------IASENNAAIQYDETAQAPFFrYTdn 380
Cdd:COG3325  263 AAgVPASKLVLGVPFYGRGWTGvtGGNNGlYQPATGPAPGTWEAgvndykdlkalYLGSNGYTRYWDDVAKAPYL-YN-- 339

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 665939010 381 aGKQHEVW-FEDARSIQAKFDLIRELNLRGISYWKLGLSFPQNWLL 425
Cdd:COG3325  340 -GDTGTFIsYDDPRSIAAKADYVKDKGLGGVMFWELSGDTADGTLL 384
LysM smart00257
Lysin motif;
10-53 1.58e-14

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 67.47  E-value: 1.58e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 665939010    10 IYVVKRGDSLYQIANRYRTTVNEIVATNEIPNPNRLVVGQTIVI 53
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 9-53 8.61e-14

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: 65.20  E-value: 8.61e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 665939010   9 QIYVVKRGDSLYQIANRYRTTVNEIVATNEIPNPNRLVVGQTIVI 53
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 ...
 11-54 1.36e-13

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: 64.72  E-value: 1.36e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 665939010   11 YVVKRGDSLYQIANRYRTTVNEIVATNEIPNPNrLVVGQTIVIP 54
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPN-LYVGQKLKIP 43
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
9-54 1.38e-12

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 65.50  E-value: 1.38e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 665939010   9 QIYVVKRGDSLYQIANRYRTTVNEIVATNEIPNpNRLVVGQTIVIP 54
Cdd:COG1388  110 VTYTVKKGDTLWSIARRYGVSVEELKRWNGLSS-DTIRPGQKLKIP 154
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
2-103 7.93e-11

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 60.11  E-value: 7.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010   2 RKEAFPIQIYVVKRGDSLYQIANRYRTTVNEIVATneipnpnrlvvgqtivipiagefYEVRQGDTLASIGARFNISPAE 81
Cdd:COG1388   77 EAAAAAAARYTVKSGDTLSGIARRYGAAAAPSPVT-----------------------YTVKKGDTLWSIARRYGVSVEE 133

                         90       100
                 ....*....|....*....|..
gi 665939010  82 LARINRIQvSAILPVGLLLYIP 103
Cdd:COG1388  134 LKRWNGLS-SDTIRPGQKLKIP 154
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 59-102 1.85e-09

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: 52.87  E-value: 1.85e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 665939010  59 FYEVRQGDTLASIGARFNISPAELARINRIQVSAILPVGLLLYI 102
Cdd:cd00118    2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 10-86 1.54e-08

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 56.67  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010  10 IYVVKRGDSLYQIANRYRTTVNEIVATNEIpNPNRLVVGQTIVIPIAGEF-----------YEVRQGDTLASIGARFNIS 78
Cdd:PRK10783 345 SYKVRSGDTLSGIASRLNVSTKDLQQWNNL-RGSKLKVGQTLTIGAGSSAqrlannsdsitYRVRKGDSLSSIAKRHGVN 423


                 ....*...
gi 665939010  79 PAELARIN 86
Cdd:PRK10783 424 IKDVMRWN 431
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 60-103 6.53e-08

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: 48.55  E-value: 6.53e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 665939010   60 YEVRQGDTLASIGARFNISPAELARINRIQVSAIlPVGLLLYIP 103
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNL-YVGQKLKIP 43
LysM smart00257
Lysin motif;
59-97 4.36e-07

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 46.28  E-value: 4.36e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 665939010    59 FYEVRQGDTLASIGARFNISPAELARINRIQVSAILPVG 97
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVG 39
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 60-95 6.32e-05

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 45.11  E-value: 6.32e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 665939010  60 YEVRQGDTLASIGARFNISPAELARINRIQVSAILP 95
Cdd:PRK10783 346 YKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKV 381
 
Name Accession Description Interval E-value
GH18_CFLE_spore_hydrolase cd02874
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ...
 110-426 1.16e-158

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: 450.56  E-value: 1.16e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 110 IETNAYIEPRGESVSPALqqaaREASPYLTYLGAFSFQAKRDGTLEEPPLNNLKEIADRHRTTMMMIVTNLENEAFSDEL 189
Cdd:cd02874    2 IEVLGYYTPRNGSDYESL----RANAPYLTYIAPFWYGVDADGTLTGLPDERLIEAAKRRGVKPLLVITNLTNGNFDSEL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 190 GRIILTDQNVKNRLLDNIVAAARRYGFKDIHFDFEYLRPEDREAYNQFLRDARARFKQEGWFISTALAPKTRADQPGQWY 269
Cdd:cd02874   78 AHAVLSNPEARQRLINNILALAKKYGYDGVNIDFENVPPEDREAYTQFLRELSDRLHPAGYTLSTAVVPKTSADQFGNWS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 270 EAHDYRAHGEIVDFVVLMTYEWGYSGGPPMAVSPIGPVRDVIEYALTEMPASKIVMGQNLYGYDWTLPYtPGGQLARAIS 349
Cdd:cd02874  158 GAYDYAAIGKIVDFVVLMTYDWHWRGGPPGPVAPIGWVERVLQYAVTQIPREKILLGIPLYGYDWTLPY-KKGGKASTIS 236

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665939010 350 PQRAIAIASENNAAIQYDETAQAPFFRYTDNAGKQHEVWFEDARSIQAKFDLIRELNLRGISYWKLGLSFPQNWLLI 426
Cdd:cd02874  237 PQQAINLAKRYGAEIQYDEEAQSPFFRYVDEQGRRHEVWFEDARSLQAKFELAKEYGLRGVSYWRLGLEDPQNWLLL 313
Glyco_18 smart00636
Glyco_18 domain;
135-417 2.60e-42

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 152.06  E-value: 2.60e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010   135 SPYLTYLGAFSFQAKRDGTLEEPP-------LNNLKEIADRHRTTMMMI-VTNL-ENEAFSDelgriILTDQNVKNRLLD 205
Cdd:smart00636  23 ASKLTHIIYAFANIDPDGTVTIGDewadignFGQLKALKKKNPGLKVLLsIGGWtESDNFSS-----MLSDPASRKKFID 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010   206 NIVAAARRYGFKDIHFDFEY--LRPEDREAYNQFLRDARARFKQE-----GWFISTALAPKTRADQPGQWYeahdYRAHG 278
Cdd:smart00636  98 SIVSFLKKYGFDGIDIDWEYpgGRGDDRENYTALLKELREALDKEgaegkGYLLTIAVPAGPDKIDKGYGD----LPAIA 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010   279 EIVDFVVLMTYEW-GYSGGPPMAVSPI-----GPVRDVIEYALTE-----MPASKIVMGQNLYGYDWTL----------P 337
Cdd:smart00636 174 KYLDFINLMTYDFhGAWSNPTGHNAPLyagpgDPEKYNVDYAVKYylckgVPPSKLVLGIPFYGRGWTLvdgsnngpgaP 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010   338 YTPGGQLARAISPQRAIA---IASENNAAIQYDETAQAPFfRYtdNAGKQHEVWFEDARSIQAKFDLIRELNLRGISYWK 414
Cdd:smart00636 254 FTGPATGGPGTWEGGVVDyreICKLLGATVVYDDTAKAPY-AY--NPGTGQWVSYDDPRSIKAKADYVKDKGLGGVMIWE 330


                   ...
gi 665939010   415 LGL 417
Cdd:smart00636 331 LDA 333
GH18_trifunctional cd06549
GH18 domain of an uncharacterized family of bacterial proteins, which share a common ...
 151-423 7.92e-32

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: 122.91  E-value: 7.92e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 151 DGTLEEPPLNNLKEI--ADRHRTTMMMIVTNLENEAFSDELGRIILTDQNVKNRLLDNIVAAARRYGFKDIHFDFEYLRP 228
Cdd:cd06549   38 EGRIDVFVDPQGVAIiaAAKAHPKVLPLVQNISGGAWDGKNIARLLADPSARAKFIANIAAYLERNQADGIVLDFEELPA 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 229 EDREAYNQFLRDARARFKQEGWFIsTALAPKTRADQPgqwyeahdYRAHGEIVDFVVLMTYEWGYSGGPPMAVSPIGPVR 308
Cdd:cd06549  118 DDLPKYVAFLSELRRRLPAQGKQL-TVTVPADEADWN--------LKALARNADKLILMAYDEHYQGGAPGPIASQDWFE 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 309 DVIEYALTEMPASKIVMGQNLYGYDWTLpytpGGQLARAISPQRAIAIASENNAAIQYDEtAQAPFFRYTDNAGKQHEVW 388
Cdd:cd06549  189 SNLAQAVKKLPPEKLIVALGSYGYDWTK----GGNTKAISSEAAWLLAAHASAAVKFDDK-ASNATYFFYDDEGVSHEVW 263

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 665939010 389 FEDARSIQAKFDLIRELNLRGISYWKLGLSFPQNW 423
Cdd:cd06549  264 MLDAVTLFNQLKAVQRLGPAGVALWRLGSEDPGLW 298
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
158-416 9.51e-28

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 112.16  E-value: 9.51e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010  158 PLNNLKEIADRHRTTMMMIVTNLENEAFSDelgrIILTDQNVKnRLLDNIVAAARRYGFKDIHFDFEY--LRPEDREAYN 235
Cdd:pfam00704  52 QLKKLKKQKNPGVKVLLSIGGWTDSTGFSL----MASNPASRK-KFADSIVSFLRKYGFDGIDIDWEYpgGNPEDKENYD 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010  236 QFLRDARARFKQ----EGWFISTALAPKtradqPGQWYEAHDYRAHGEIVDFVVLMTY----EWGYSGGPPMAVSPIGP- 306
Cdd:pfam00704 127 LLLRELRAALDEakggKKYLLSAAVPAS-----YPDLDKGYDLPKIAKYLDFINVMTYdfhgSWDNVTGHHAPLYGGGSy 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010  307 -VRDVIEYALTE-MPASKIVMGQNLYGYDWTLPYTPGGQLARAISPQRAI-AIASENNAAIQYDETAQAPFfrYTDNagk 383
Cdd:pfam00704 202 nVDYAVKYYLKQgVPASKLVLGVPFYGRSWTLVNGSGNTWEDGVLAYKEIcNLLKDNGATVVWDDVAKAPY--VYDG--- 276

                         250       260       270
                  ....*....|....*....|....*....|...
gi 665939010  384 QHEVWFEDARSIQAKFDLIRELNLRGISYWKLG 416
Cdd:pfam00704 277 DQFITYDDPRSIATKVDYVKAKGLGGVMIWSLD 309
GH18_SI-CLP cd02876
Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein ...
 183-416 3.26e-23

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: 99.30  E-value: 3.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 183 EAFSDELGRIILTDQNVKNRLLDNIVAAARRYGFkdIHFDFE-------YLRPEDREAYNQFLRDARARFKQEGWFISTA 255
Cdd:cd02876   76 EGWSYQDLQSLLNDEQEREKLIKLLVTTAKKNHF--DGIVLEvwsqlaaYGVPDKRKELIQLVIHLGETLHSANLKLILV 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 256 LAPKTRADQPGQWYEAHDYRAHGEIVDFVVLMTYEwgYSG-GPPMAVSPIGPVRDVIEYALTEMP--ASKIVMGQNLYGY 332
Cdd:cd02876  154 IPPPREKGNQNGLFTRKDFEKLAPHVDGFSLMTYD--YSSpQRPGPNAPLSWVRSCLELLLPESGkkRAKILLGLNFYGN 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 333 DwtlpYTPGGQLArAISPQRAIAIASENNAAIQYDETAQAPFFRYTDNAGKqHEVWFEDARSIQAKFDLIRELNlRGISY 412
Cdd:cd02876  232 D----YTLPGGGG-AITGSEYLKLLKSNKPKLQWDEKSAEHFFEYKNKGGK-HAVFYPTLKSIQLRLDLAKELG-TGISI 304


                 ....
gi 665939010 413 WKLG 416
Cdd:cd02876  305 WELG 308
ChiA COG3325
Chitinase, GH18 family [Carbohydrate transport and metabolism];
185-425 2.05e-18

Chitinase, GH18 family [Carbohydrate transport and metabolism];


Pssm-ID: 442554 [Multi-domain]  Cd Length: 391  Bit Score: 86.50  E-value: 2.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 185 FSDelgrIILTDQNVKnRLLDNIVAAARRYGFKDIHFDFEY----------LRPEDREAYNQFLRDARARFKQEG----- 249
Cdd:COG3325  115 FSD----AAATPASRA-AFVDSCVDLLRKYNFDGIDIDWEYpgsggapgnvYRPEDKANFTALLKELRAQLDALGaetgk 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 250 -WFISTALAPktradqpGQWYEAH-DYRAHGEIVDFVVLMTYE----WGYSGGP--PMAVSPIGPVRD------VIEYAL 315
Cdd:COG3325  190 hYLLTAAAPA-------GPDKLDGiELPKVAQYLDYVNVMTYDfhgaWSPTTGHqaPLYDSPKDPEAQgysvdsAVQAYL 262

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 316 TE-MPASKIVMGQNLYGYDWTL--PYTPG-GQLARAISPQRAIA-----------IASENNAAIQYDETAQAPFFrYTdn 380
Cdd:COG3325  263 AAgVPASKLVLGVPFYGRGWTGvtGGNNGlYQPATGPAPGTWEAgvndykdlkalYLGSNGYTRYWDDVAKAPYL-YN-- 339

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 665939010 381 aGKQHEVW-FEDARSIQAKFDLIRELNLRGISYWKLGLSFPQNWLL 425
Cdd:COG3325  340 -GDTGTFIsYDDPRSIAAKADYVKDKGLGGVMFWELSGDTADGTLL 384
GH18_chitobiase cd02875
Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes ...
 194-413 3.65e-17

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: 82.48  E-value: 3.65e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 194 LTDQNVKNRLLDNIVAAARRYGFKDIHFDFEY---LRPEDREAYNQFLRDARARFKQEGWF----ISTALAPKTrADqpg 266
Cdd:cd02875   91 ISNPTYRTQWIQQKVELAKSQFMDGINIDIEQpitKGSPEYYALTELVKETTKAFKKENPGyqisFDVAWSPSC-ID--- 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 267 qwYEAHDYRAHGEIVDFVVLMTYEWG--YSGGP--PMAVSPIGPV-RDVIEYALTEMPASKIVMGQNLYGYDW------- 334
Cdd:cd02875  167 --KRCYDYTGIADASDFLVVMDYDEQsqIWGKEciAGANSPYSQTlSGYNNFTKLGIDPKKLVMGLPWYGYDYpclngnl 244

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 335 -----TLPYTP--GGQLARAISPQRAIAI----ASENNAAIQYDETAQAPFFRYTDNAGKQHEVWFEDARSIQAKFDLIR 403
Cdd:cd02875  245 edvvcTIPKVPfrGANCSDAAGRQIPYSEimkqINSSIGGRLWDSEQKSPFYNYKDKQGNLHQVWYDNPQSLSIKVAYAK 324

                        250
                 ....*....|
gi 665939010 404 ELNLRGISYW 413
Cdd:cd02875  325 NLGLKGIGMW 334
GH18_chitolectin_chitotriosidase cd02872
This conserved domain family includes a large number of catalytically inactive chitinase-like ...
 212-415 7.20e-17

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: 81.45  E-value: 7.20e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 212 RRYGFKDIHFDFEY-----LRPEDREAYNQFLRDARARFKQE--GWFISTAL-APKTRADqpgqwyEAHDYRAHGEIVDF 283
Cdd:cd02872  109 RKYGFDGLDLDWEYpgqrgGPPEDKENFVTLLKELREAFEPEapRLLLTAAVsAGKETID------AAYDIPEISKYLDF 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 284 VVLMTYE----W-GYSG------GPPMAVSPIGP--VRDVIEYALTE-MPASKIVMGQNLYGYDWTLP----YTPGgqlA 345
Cdd:cd02872  183 INVMTYDfhgsWeGVTGhnsplyAGSADTGDQKYlnVDYAIKYWLSKgAPPEKLVLGIPTYGRSFTLAspsnTGVG---A 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 346 RAISPQRA--------------IAIASENNAAIQYDETAQAPfFRYTDNagkqheVW--FEDARSIQAKFDLIRELNLRG 409
Cdd:cd02872  260 PASGPGTAgpytreagflayyeICEFLKSGWTVVWDDEQKVP-YAYKGN------QWvgYDDEESIALKVQYLKSKGLGG 332


                 ....*.
gi 665939010 410 ISYWKL 415
Cdd:cd02872  333 AMVWSI 338
GH18_chitinase cd06548
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ...
 183-416 2.81e-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: 2.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 183 EAFSDelgrIILTDQNVKnRLLDNIVAAARRYGFKDIHFDFEY----------LRPEDREAYNQFLRDARARFKQEGWF- 251
Cdd:cd06548   98 GGFSD----AAATEASRA-KFADSAVDFIRKYGFDGIDIDWEYpgsggapgnvARPEDKENFTLLLKELREALDALGAEt 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 252 -----ISTALAPKTRADQPGQWYEAHDYrahgeiVDFVVLMTY----EW-----------GYSGGPPMAVSpigpVRDVI 311
Cdd:cd06548  173 grkylLTIAAPAGPDKLDKLEVAEIAKY------LDFINLMTYdfhgAWsnttghhsnlyASPADPPGGYS----VDAAV 242

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 312 EYALTE-MPASKIVMGQNLYGYDWTlpytpggqlaraispqraiaiasenNAAIQYDETAQAPffrYTDNAGKQHEVWFE 390
Cdd:cd06548  243 NYYLSAgVPPEKLVLGVPFYGRGWT-------------------------GYTRYWDEVAKAP---YLYNPSTKTFISYD 294

                        250       260
                 ....*....|....*....|....*.
gi 665939010 391 DARSIQAKFDLIRELNLRGISYWKLG 416
Cdd:cd06548  295 DPRSIKAKADYVKDKGLGGVMFWELS 320
LysM smart00257
Lysin motif;
10-53 1.58e-14

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 67.47  E-value: 1.58e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 665939010    10 IYVVKRGDSLYQIANRYRTTVNEIVATNEIPNPNRLVVGQTIVI 53
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 9-53 8.61e-14

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: 65.20  E-value: 8.61e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 665939010   9 QIYVVKRGDSLYQIANRYRTTVNEIVATNEIPNPNRLVVGQTIVI 53
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 ...
 11-54 1.36e-13

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: 64.72  E-value: 1.36e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 665939010   11 YVVKRGDSLYQIANRYRTTVNEIVATNEIPNPNrLVVGQTIVIP 54
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPN-LYVGQKLKIP 43
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
9-54 1.38e-12

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 65.50  E-value: 1.38e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 665939010   9 QIYVVKRGDSLYQIANRYRTTVNEIVATNEIPNpNRLVVGQTIVIP 54
Cdd:COG1388  110 VTYTVKKGDTLWSIARRYGVSVEELKRWNGLSS-DTIRPGQKLKIP 154
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
2-103 7.93e-11

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 60.11  E-value: 7.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010   2 RKEAFPIQIYVVKRGDSLYQIANRYRTTVNEIVATneipnpnrlvvgqtivipiagefYEVRQGDTLASIGARFNISPAE 81
Cdd:COG1388   77 EAAAAAAARYTVKSGDTLSGIARRYGAAAAPSPVT-----------------------YTVKKGDTLWSIARRYGVSVEE 133

                         90       100
                 ....*....|....*....|..
gi 665939010  82 LARINRIQvSAILPVGLLLYIP 103
Cdd:COG1388  134 LKRWNGLS-SDTIRPGQKLKIP 154
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 59-102 1.85e-09

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: 52.87  E-value: 1.85e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 665939010  59 FYEVRQGDTLASIGARFNISPAELARINRIQVSAILPVGLLLYI 102
Cdd:cd00118    2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
GH18_chitinase-like cd00598
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ...
 155-289 9.22e-09

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: 55.46  E-value: 9.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 155 EEPPLNNLKEIADRHRTT--MMMIVTNLENEAFSDelgriILTDQNVKNrLLDNIVAAARRYGFKDIHFDFEY---LRPE 229
Cdd:cd00598   48 EEPLKGALEELASKKPGLkvLISIGGWTDSSPFTL-----ASDPASRAA-FANSLVSFLKTYGFDGVDIDWEYpgaADNS 121

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 230 DREAYNQFLRDARARFKQEGWFISTALAPKtradqPGQWYEAHDYRAHGEIVDFVVLMTY 289
Cdd:cd00598  122 DRENFITLLRELRSALGAANYLLTIAVPAS-----YFDLGYAYDVPAIGDYVDFVNVMTY 176
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 10-86 1.54e-08

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 56.67  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010  10 IYVVKRGDSLYQIANRYRTTVNEIVATNEIpNPNRLVVGQTIVIPIAGEF-----------YEVRQGDTLASIGARFNIS 78
Cdd:PRK10783 345 SYKVRSGDTLSGIASRLNVSTKDLQQWNNL-RGSKLKVGQTLTIGAGSSAqrlannsdsitYRVRKGDSLSSIAKRHGVN 423


                 ....*...
gi 665939010  79 PAELARIN 86
Cdd:PRK10783 424 IKDVMRWN 431
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 60-103 6.53e-08

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: 48.55  E-value: 6.53e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 665939010   60 YEVRQGDTLASIGARFNISPAELARINRIQVSAIlPVGLLLYIP 103
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNL-YVGQKLKIP 43
GH18_plant_chitinase_class_V cd02879
The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the ...
 208-416 7.65e-08

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: 53.52  E-value: 7.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 208 VAAARRYGFKDIHFDFEYLR-PEDREAYNQFLRDARARFKQEGW------FISTA---LAPKTRADQPGQWYEAhdyRAH 277
Cdd:cd02879  101 IKVARKYGFDGLDLDWEFPSsQVEMENFGKLLEEWRAAVKDEARssgrppLLLTAavyFSPILFLSDDSVSYPI---EAI 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 278 GEIVDFVVLMTYE-----WGYSGGPPMA-------VSPIGPVRDVIEYAlteMPASKIVMGQNLYGYDWTLpytpggqla 345
Cdd:cd02879  178 NKNLDWVNVMAYDyygswESNTTGPAAAlydpnsnVSTDYGIKSWIKAG---VPAKKLVLGLPLYGRAWTL--------- 245

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665939010 346 raispqraiaiasennaaiqYDETAQApFFRYTDNagkqheVW--FEDARSIQAKFDLIRELNLRGISYWKLG 416
Cdd:cd02879  246 --------------------YDTTTVS-SYVYAGT------TWigYDDVQSIAVKVKYAKQKGLLGYFAWAVG 291
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 9-54 9.79e-08

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: 51.55  E-value: 9.79e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 665939010   9 QIYVVKRGDSLYQIANRY---RTTVNEIVATNE--IPNPNRLVVGQTIVIP 54
Cdd:COG1652  110 KTYTVKPGDTLWGIAKRFygdPARWPEIAEANRdqIKNPDLIYPGQVLRIP 160
LysM smart00257
Lysin motif;
59-97 4.36e-07

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 46.28  E-value: 4.36e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 665939010    59 FYEVRQGDTLASIGARFNISPAELARINRIQVSAILPVG 97
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVG 39
GH18_3CO4_chitinase cd06545
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an ...
 137-335 8.90e-06

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: 47.06  E-value: 8.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 137 YLTYLGAFSFQAKRDGTLE-EPPLNNLKEIADRHRTTMMMIVTNLENEAFSDELGRIIlTDQNVKNrLLDNIVAAARRYG 215
Cdd:cd06545   22 KLTHINLAFANPDANGTLNaNPVRSELNSVVNAAHAHNVKILISLAGGSPPEFTAALN-DPAKRKA-LVDKIINYVVSYN 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665939010 216 FKDIHFDFEYlrpEDR--EAYNQFLRDARARFKQEGWFISTALAPKTRADQPGQWYEAHDyrahgeivdFVVLMTYEwgy 293
Cdd:cd06545  100 LDGIDVDLEG---PDVtfGDYLVFIRALYAALKKEGKLLTAAVSSWNGGAVSDSTLAYFD---------FINIMSYD--- 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 665939010 294 SGGPPMAVSPiGP-------VRDVIEYALTE-MPASKIVMGQNLYGYDWT 335
Cdd:cd06545  165 ATGPWWGDNP-GQhssyddaVNDLNYWNERGlASKDKLVLGLPFYGYGFY 213
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
8-53 2.66e-05

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 46.61  E-value: 2.66e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 665939010   8 IQIYVVKRGDSLYQIANRYRTTVNEIVATNEIPNpNRLVVGQTIVI 53
Cdd:PRK06347 547 VKTYTVKKGDSLWAISRQYKTTVDNIKAWNKLTS-NMIHVGQKLTI 591
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 60-95 6.32e-05

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 45.11  E-value: 6.32e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 665939010  60 YEVRQGDTLASIGARFNISPAELARINRIQVSAILP 95
Cdd:PRK10783 346 YKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKV 381
PRK11198 PRK11198
LysM domain/BON superfamily protein; Provisional
 9-54 6.45e-04

LysM domain/BON superfamily protein; Provisional


Pssm-ID: 236880 [Multi-domain]  Cd Length: 147  Bit Score: 39.90  E-value: 6.45e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 665939010   9 QIYVVKRGDSLYQIA-------NRYrttvNEIVATNE--IPNPNRLVVGQTIVIP 54
Cdd:PRK11198  96 QFYTVKSGDTLSAIAkkvygnaNKY----NKIFEANKpmLKSPDKIYPGQVLRIP 146
nlpD PRK10871
murein hydrolase activator NlpD;
9-51 2.63e-03

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 39.82  E-value: 2.63e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 665939010   9 QIYVVKRGDSLYQIA----NRYRttvnEIVATNEIPNPNRLVVGQTI 51
Cdd:PRK10871  61 STYTVKKGDTLFYIAwitgNDFR----DLAQRNNIQAPYSLNVGQTL 103
 
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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