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Conserved domains on  [gi|1195006606|gb|ARS41881|]
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hemagglutinin [Sphingobacteriaceae bacterium GW460-11-11-14-LB5]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FlgJ super family cl43493
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ...
 17-154 1.13e-20

Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];


The actual alignment was detected with superfamily member COG1705:

Pssm-ID: 441311 [Multi-domain]  Cd Length: 276  Bit Score: 87.33  E-value: 1.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195006606  17 VASAQDTDEYIAEHVEYAQDLMRDHKIPASIILAVAIHESAAGNSKI-AQHLNNHFGVKGPNNN---------TE----- 81
Cdd:COG1705   123 AAASASPEEFIAKIAPAAQKAAKKYGVPASVLIAQAALESGWGKSELdGSPSNNLFGIKAGGSWqgksvevttTEyvngk 202

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1195006606  82 ---IRSSYRDYLNADESYSHFVEIMETREPFNNLFGKydQYDYKGWAYGIRRCGYASSRSWASQVIGLIKKYELYQ 154
Cdd:COG1705   203 avkIKARFRAYDSYAESFRDYARLLKNNPRYAGALAN--AKDYEAFAKALQKAGYATDPKYADKLISIIESYNLTQ 276
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
164-224 2.04e-16

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


:

Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 73.59  E-value: 2.04e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1195006606 164 EPVYAAPARHRSKSRRTTKSYTVKSGDNLSIIAKKKGTTVKALMQKNGIKKANLKPGQKLK 224
Cdd:COG1388    92 DTLSGIARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLK 152
 
Name Accession Description Interval E-value
FlgJ COG1705
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ...
 17-154 1.13e-20

Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];


Pssm-ID: 441311 [Multi-domain]  Cd Length: 276  Bit Score: 87.33  E-value: 1.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195006606  17 VASAQDTDEYIAEHVEYAQDLMRDHKIPASIILAVAIHESAAGNSKI-AQHLNNHFGVKGPNNN---------TE----- 81
Cdd:COG1705   123 AAASASPEEFIAKIAPAAQKAAKKYGVPASVLIAQAALESGWGKSELdGSPSNNLFGIKAGGSWqgksvevttTEyvngk 202

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1195006606  82 ---IRSSYRDYLNADESYSHFVEIMETREPFNNLFGKydQYDYKGWAYGIRRCGYASSRSWASQVIGLIKKYELYQ 154
Cdd:COG1705   203 avkIKARFRAYDSYAESFRDYARLLKNNPRYAGALAN--AKDYEAFAKALQKAGYATDPKYADKLISIIESYNLTQ 276
sporang_Gsm NF038016
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ...
 17-156 2.70e-17

sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA occurs in some sporangia-forming members of the Actinobacteria, such as Actinoplanes missouriensis, and is required for proper separation of spores. GsmA proteins have one or two SH3 domains N-terminal to the hydrolase domain.


Pssm-ID: 411609 [Multi-domain]  Cd Length: 312  Bit Score: 78.63  E-value: 2.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195006606  17 VASAQDTDEYIAEHVEYAQDLMRDHKIPASIILAVAIHESAAGNSKIAQHLNNHFGVK--------------------GP 76
Cdd:NF038016  154 TVPRGTPAQFIAAVAPPAQQSQRATGVPASVTIAQAILESGWGRSGLTREDHNYFGIKcfgspgpiavgcrsyatfecSP 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195006606  77 NNN-TEIRSSYRDYLNADESY----------SHFVEIME-TREPfnnlfgkyDQYdykgwAYGIRRCGYASSRSWASQVI 144
Cdd:NF038016  234 TGGcFDTTATFRAYASAADSFrdhgrflsvnSRYAPAFAyTDDP--------DQF-----AREIHKAGYATDPTYADKLI 300

                         170
                  ....*....|..
gi 1195006606 145 GLIKKYELYQYD 156
Cdd:NF038016  301 GLMKQYNLYQYD 312
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
164-224 2.04e-16

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 73.59  E-value: 2.04e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1195006606 164 EPVYAAPARHRSKSRRTTKSYTVKSGDNLSIIAKKKGTTVKALMQKNGIKKANLKPGQKLK 224
Cdd:COG1388    92 DTLSGIARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLK 152
Glucosaminidase pfam01832
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ...
 31-105 1.64e-14

Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase EC:3.2.1.96. As well as the flageller protein J that has been shown to hydrolyse peptidoglycan.


Pssm-ID: 460354 [Multi-domain]  Cd Length: 91  Bit Score: 66.44  E-value: 1.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195006606  31 VEYAQDLMRDHKIPASIILAVAIHESAAGNSKIAQHLNNHFGVKG--------PNNNTEIRSSYRDYLNADESYSHF--- 99
Cdd:pfam01832   1 APAAIEAAKKYGIPASVLLAQAALESGWGTSRLAKESNNLFGIKAswkgkvayDTDEVTVAARFRKYDSVEESIRDYyae 80


                  ....*...
gi 1195006606 100 --VEIMET 105
Cdd:pfam01832  81 klIAIIER 88
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
40-224 2.26e-14

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 71.26  E-value: 2.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195006606  40 DHKIPASIILAVAIHESAAGNSKIAQHLN-NHFGVKGPNNNTE----------------IRSSYRDYLNADESYSHFVEI 102
Cdd:PRK06347  167 ENDLYASVMIAQAILESAYGTSELGSAPNyNLFGIKGAYNGQSytkqtleddgkgnyytITAKFRKYPSYHQSLEDYAQV 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195006606 103 METREPFN-NLFGKYDQYDYKGWAYGIRRCG--YASSRSWASQVIGLIKKYELYQYD--ERPEGYEEPVYAAPARHRSKS 177
Cdd:PRK06347  247 IRKGPSWNpNYYSKVWKSNTTSYKDATKALTgtYATDTAYATKLNDLISRYNLTQYDsgKTTGGNSGSTGNSSNSSNTGN 326

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1195006606 178 RRTTKSYTVKSGDNLSIIAKKKGTTVKALMQKNGIKKANLKPGQKLK 224
Cdd:PRK06347  327 TSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLK 373
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 184-224 3.00e-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: 61.64  E-value: 3.00e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1195006606 184 YTVKSGDNLSIIAKKKGTTVKALMQKNGIKKANLKPGQKLK 224
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLK 41
LYZ2 smart00047
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
 17-156 6.65e-12

Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.


Pssm-ID: 214488 [Multi-domain]  Cd Length: 147  Bit Score: 60.91  E-value: 6.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195006606   17 VASAQDTDEYIAEHVEYAQDLMRDHKIPASIILAVAIHESAAGNSKIAQHLNNHFGVKGPNNNTEIRSSYRDYLNA--DE 94
Cdd:smart00047   2 LLAGGSTLEFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLAKKYNNLFGIKGAYDGRPVRMGTLEYLNGgwVT 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1195006606   95 SYSHFveimetREPFNNLFGKYDQYDY-------KGW-AYGIRRCGYASSRSWASQVIGLIKKY--ELYQYD 156
Cdd:smart00047  82 VKAAF------RGYFGEKFIDYAYVLRgqnplykKRWgSNALQTAGYATDPDYAKKLIRIIALYdeKLKGYD 147
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 182-224 2.96e-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: 56.34  E-value: 2.96e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1195006606 182 KSYTVKSGDNLSIIAKKKGTTVKALMQKNGIKKAN-LKPGQKLK 224
Cdd:cd00118     1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDcIYPGQKLK 44
LysM smart00257
Lysin motif;
184-224 3.08e-11

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 56.30  E-value: 3.08e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1195006606  184 YTVKSGDNLSIIAKKKGTTVKALMQKNGIKKAN-LKPGQKLK 224
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDPDnLQVGQKLK 43
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 177-224 5.78e-09

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 55.51  E-value: 5.78e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1195006606 177 SRRTTKSYTVKSGDNLSIIAKKKGTTVKALMQKNGIKKANLKPGQKLK 224
Cdd:PRK10783  339 TPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLT 386
 
Name Accession Description Interval E-value
FlgJ COG1705
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ...
 17-154 1.13e-20

Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];


Pssm-ID: 441311 [Multi-domain]  Cd Length: 276  Bit Score: 87.33  E-value: 1.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195006606  17 VASAQDTDEYIAEHVEYAQDLMRDHKIPASIILAVAIHESAAGNSKI-AQHLNNHFGVKGPNNN---------TE----- 81
Cdd:COG1705   123 AAASASPEEFIAKIAPAAQKAAKKYGVPASVLIAQAALESGWGKSELdGSPSNNLFGIKAGGSWqgksvevttTEyvngk 202

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1195006606  82 ---IRSSYRDYLNADESYSHFVEIMETREPFNNLFGKydQYDYKGWAYGIRRCGYASSRSWASQVIGLIKKYELYQ 154
Cdd:COG1705   203 avkIKARFRAYDSYAESFRDYARLLKNNPRYAGALAN--AKDYEAFAKALQKAGYATDPKYADKLISIIESYNLTQ 276
sporang_Gsm NF038016
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ...
 17-156 2.70e-17

sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA occurs in some sporangia-forming members of the Actinobacteria, such as Actinoplanes missouriensis, and is required for proper separation of spores. GsmA proteins have one or two SH3 domains N-terminal to the hydrolase domain.


Pssm-ID: 411609 [Multi-domain]  Cd Length: 312  Bit Score: 78.63  E-value: 2.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195006606  17 VASAQDTDEYIAEHVEYAQDLMRDHKIPASIILAVAIHESAAGNSKIAQHLNNHFGVK--------------------GP 76
Cdd:NF038016  154 TVPRGTPAQFIAAVAPPAQQSQRATGVPASVTIAQAILESGWGRSGLTREDHNYFGIKcfgspgpiavgcrsyatfecSP 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195006606  77 NNN-TEIRSSYRDYLNADESY----------SHFVEIME-TREPfnnlfgkyDQYdykgwAYGIRRCGYASSRSWASQVI 144
Cdd:NF038016  234 TGGcFDTTATFRAYASAADSFrdhgrflsvnSRYAPAFAyTDDP--------DQF-----AREIHKAGYATDPTYADKLI 300

                         170
                  ....*....|..
gi 1195006606 145 GLIKKYELYQYD 156
Cdd:NF038016  301 GLMKQYNLYQYD 312
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
164-224 2.04e-16

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 73.59  E-value: 2.04e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1195006606 164 EPVYAAPARHRSKSRRTTKSYTVKSGDNLSIIAKKKGTTVKALMQKNGIKKANLKPGQKLK 224
Cdd:COG1388    92 DTLSGIARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLK 152
Glucosaminidase pfam01832
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ...
 31-105 1.64e-14

Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase EC:3.2.1.96. As well as the flageller protein J that has been shown to hydrolyse peptidoglycan.


Pssm-ID: 460354 [Multi-domain]  Cd Length: 91  Bit Score: 66.44  E-value: 1.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195006606  31 VEYAQDLMRDHKIPASIILAVAIHESAAGNSKIAQHLNNHFGVKG--------PNNNTEIRSSYRDYLNADESYSHF--- 99
Cdd:pfam01832   1 APAAIEAAKKYGIPASVLLAQAALESGWGTSRLAKESNNLFGIKAswkgkvayDTDEVTVAARFRKYDSVEESIRDYyae 80


                  ....*...
gi 1195006606 100 --VEIMET 105
Cdd:pfam01832  81 klIAIIER 88
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
40-224 2.26e-14

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 71.26  E-value: 2.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195006606  40 DHKIPASIILAVAIHESAAGNSKIAQHLN-NHFGVKGPNNNTE----------------IRSSYRDYLNADESYSHFVEI 102
Cdd:PRK06347  167 ENDLYASVMIAQAILESAYGTSELGSAPNyNLFGIKGAYNGQSytkqtleddgkgnyytITAKFRKYPSYHQSLEDYAQV 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195006606 103 METREPFN-NLFGKYDQYDYKGWAYGIRRCG--YASSRSWASQVIGLIKKYELYQYD--ERPEGYEEPVYAAPARHRSKS 177
Cdd:PRK06347  247 IRKGPSWNpNYYSKVWKSNTTSYKDATKALTgtYATDTAYATKLNDLISRYNLTQYDsgKTTGGNSGSTGNSSNSSNTGN 326

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1195006606 178 RRTTKSYTVKSGDNLSIIAKKKGTTVKALMQKNGIKKANLKPGQKLK 224
Cdd:PRK06347  327 TSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLK 373
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 184-224 3.00e-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: 61.64  E-value: 3.00e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1195006606 184 YTVKSGDNLSIIAKKKGTTVKALMQKNGIKKANLKPGQKLK 224
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLK 41
PRK08581 PRK08581
amidase domain-containing protein;
17-156 5.91e-12

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 64.42  E-value: 5.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195006606  17 VASAQDTDEYIAEHVEYAQDLMRDHKIPASIILAVAIHESAAGNSKIAQHLN-NHFGVKGP---------------NNNT 80
Cdd:PRK08581  314 VVDSKDTRQFIKSIAKDAHRIGQDNDIYASVMIAQAILESDSGQSALAKSPNhNLFGIKGAyegnsvsfntleadgNQLY 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195006606  81 EIRSSYRDYLNADESYSHFVEIMETREPFNNLF----GKYDQYDYKGWAYGIRRCgYASSRSWASQVIGLIKKYELYQYD 156
Cdd:PRK08581  394 SINAGFRKYPSTKESLEDYADLIKNGIDGNSTIykptWKSEAKSYKDATSHLSKT-YATDPNYAKKLNSIIKHYNLTQFD 472
LYZ2 smart00047
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
 17-156 6.65e-12

Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.


Pssm-ID: 214488 [Multi-domain]  Cd Length: 147  Bit Score: 60.91  E-value: 6.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195006606   17 VASAQDTDEYIAEHVEYAQDLMRDHKIPASIILAVAIHESAAGNSKIAQHLNNHFGVKGPNNNTEIRSSYRDYLNA--DE 94
Cdd:smart00047   2 LLAGGSTLEFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLAKKYNNLFGIKGAYDGRPVRMGTLEYLNGgwVT 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1195006606   95 SYSHFveimetREPFNNLFGKYDQYDY-------KGW-AYGIRRCGYASSRSWASQVIGLIKKY--ELYQYD 156
Cdd:smart00047  82 VKAAF------RGYFGEKFIDYAYVLRgqnplykKRWgSNALQTAGYATDPDYAKKLIRIIALYdeKLKGYD 147
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 182-224 2.96e-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: 56.34  E-value: 2.96e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1195006606 182 KSYTVKSGDNLSIIAKKKGTTVKALMQKNGIKKAN-LKPGQKLK 224
Cdd:cd00118     1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDcIYPGQKLK 44
LysM smart00257
Lysin motif;
184-224 3.08e-11

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 56.30  E-value: 3.08e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1195006606  184 YTVKSGDNLSIIAKKKGTTVKALMQKNGIKKAN-LKPGQKLK 224
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDPDnLQVGQKLK 43
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 177-224 5.78e-09

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 55.51  E-value: 5.78e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1195006606 177 SRRTTKSYTVKSGDNLSIIAKKKGTTVKALMQKNGIKKANLKPGQKLK 224
Cdd:PRK10783  339 TPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLT 386
OapA COG3061
Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell ...
 165-225 1.76e-06

Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442295 [Multi-domain]  Cd Length: 425  Bit Score: 47.74  E-value: 1.76e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1195006606 165 PVYAAPARHrSKSRRTTKSYTVKSGDNLSIIAKKKG---TTVKALMQKNGIKKA--NLKPGQKLKF 225
Cdd:COG3061    54 PAAAAPAAP-AAPEGEWQEYTVQSGDTLSQIFRRLGlsaSDLYALLAAEGDAKPlsRLKPGQELRF 118
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 157-225 1.27e-05

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: 44.23  E-value: 1.27e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1195006606 157 ERPEGYEEPVYAAPARHRSKSrrTTKSYTVKSGDNLSIIAKK---KGTTVKALMQKN--GIKKANL-KPGQKLKF 225
Cdd:COG1652    87 LSPAVTVAEEAAAPSAELAPD--APKTYTVKPGDTLWGIAKRfygDPARWPEIAEANrdQIKNPDLiYPGQVLRI 159
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
171-224 2.44e-05

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 44.69  E-value: 2.44e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1195006606 171 ARHRSKSRRTTKSYTVKSGDNLSIIAKKKGTTVKALMQKNGIKKANLKPGQKLK 224
Cdd:PRK06347  469 SKPSTNTNTNAKVYTVAKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLK 522
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 175-223 2.76e-05

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 44.34  E-value: 2.76e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1195006606 175 SKSRRTTKS----YTVKSGDNLSIIAKKKGTTVKALMQKNGIKKANLKPGQKL 223
Cdd:PRK10783  392 SAQRLANNSdsitYRVRKGDSLSSIAKRHGVNIKDVMRWNSDTAKNLQPGDKL 444
PRK13914 PRK13914
invasion associated endopeptidase;
167-224 8.41e-05

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 42.87  E-value: 8.41e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1195006606 167 YAAParhrskSRRTTKSYTVKSGDNLSIIAKKKGTTVKALMQKNGIKKANLKPGQKLK 224
Cdd:PRK13914   19 FAAP------TIASASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQ 70
OapA pfam04225
Opacity-associated protein A LysM-like domain; The OapA domain gets its name from the ...
 182-225 4.56e-03

Opacity-associated protein A LysM-like domain; The OapA domain gets its name from the Haemophilus influenzae protein OapA, which is required for the expression of colony opacity, thus opacity- associated protein A. The OapA protein is required for efficient nasopharyngeal mucosal colonization, and its expression is associated with a distinctive transparent colony phenotype. OapA is thought to be a secreted protein, and its expression exhibits high-frequency phase variation. The OapA domain has been shown to bind to peptidoglycan in the E. coli protein YtfB. A screen to identify factors that affect cell division in E. coli discovered that overproducing a fragment of YtfB, including its OapA domain, caused cells to grow as long filaments. OapA domains are commonly associated with other domains that are involved in breaking peptidoglycan cross-links. The OapA domain is distantly related to pfam01476.


Pssm-ID: 427799 [Multi-domain]  Cd Length: 85  Bit Score: 35.02  E-value: 4.56e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1195006606 182 KSYTVKSGDNLSIIAKKKG---TTVKALMQKNGIKKA--NLKPGQKLKF 225
Cdd:pfam04225   3 KTYTVPKGDTLAQLFRDNNlpiSDVNAMAKVEGADKPlsNIKSGQLVRI 51
PRK11198 PRK11198
LysM domain/BON superfamily protein; Provisional
 184-223 6.86e-03

LysM domain/BON superfamily protein; Provisional


Pssm-ID: 236880 [Multi-domain]  Cd Length: 147  Bit Score: 35.66  E-value: 6.86e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1195006606 184 YTVKSGDNLSIIAKK---KGttvkalMQKNGIKKAN---LK------PGQKL 223
Cdd:PRK11198   98 YTVKSGDTLSAIAKKvygNA------NKYNKIFEANkpmLKspdkiyPGQVL 143
 
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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