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Conserved domains on  [gi|557255131|emb|CDI48504|]
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phage protein [Clostridium tetani 12124569]

Protein Classification

glycoside hydrolase family 73 protein( domain architecture ID 10004312)

glycoside hydrolase family 73 protein similar to Listeria monocytogenes virulence-associated peptidoglycan hydrolase Auto and Leuconostoc citreum atypical peptidoglycan hydrolase Mur

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FlgJ COG1705
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ...
 138-293 4.72e-54

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


:

Pssm-ID: 441311 [Multi-domain]  Cd Length: 276  Bit Score: 177.85  E-value: 4.72e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557255131 138 VKVSEEKEAFISALTPEAKSIYKEYDILPSIVIGQAILESDWGKSKLS-SNYNNLFGIKATKSWKGKTVKMETSENYD-- 214
Cdd:COG1705  123 AAASASPEEFIAKIAPAAQKAAKKYGVPASVLIAQAALESGWGKSELDgSPSNNLFGIKAGGSWQGKSVEVTTTEYVNgk 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557255131 215 -DTIIDVFRSYDSKGNSLKDYAKFLKDNRRYRENgVFNSKTYIEQADSITKAGYSTkkDKDgnhmYGSLLTEIIREYNLQ 293
Cdd:COG1705  203 aVKIKARFRAYDSYAESFRDYARLLKNNPRYAGA-LANAKDYEAFAKALQKAGYAT--DPK----YADKLISIIESYNLT 275
 
Name Accession Description Interval E-value
FlgJ COG1705
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ...
 138-293 4.72e-54

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


Pssm-ID: 441311 [Multi-domain]  Cd Length: 276  Bit Score: 177.85  E-value: 4.72e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557255131 138 VKVSEEKEAFISALTPEAKSIYKEYDILPSIVIGQAILESDWGKSKLS-SNYNNLFGIKATKSWKGKTVKMETSENYD-- 214
Cdd:COG1705  123 AAASASPEEFIAKIAPAAQKAAKKYGVPASVLIAQAALESGWGKSELDgSPSNNLFGIKAGGSWQGKSVEVTTTEYVNgk 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557255131 215 -DTIIDVFRSYDSKGNSLKDYAKFLKDNRRYRENgVFNSKTYIEQADSITKAGYSTkkDKDgnhmYGSLLTEIIREYNLQ 293
Cdd:COG1705  203 aVKIKARFRAYDSYAESFRDYARLLKNNPRYAGA-LANAKDYEAFAKALQKAGYAT--DPK----YADKLISIIESYNLT 275
flagell_FlgJ TIGR02541
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ...
 145-269 9.71e-28

flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts directly in flagellar rod assembly. The C-terminal region is a flagellum-specific muramidase (peptidoglycan hydrolase) required for formation of the outer membrane L ring.


Pssm-ID: 274188 [Multi-domain]  Cd Length: 294  Bit Score: 109.17  E-value: 9.71e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557255131  145 EAFISALTPEAKSIYKEYDILPSIVIGQAILESDWGKSKL----SSNYNNLFGIKATKSWKGKTVKMETSENYDDTIIDV 220
Cdd:TIGR02541 149 KSFVNSMLPHARKAAQQLGVPPHLILAQAALESGWGQRQIrnadGSPSYNLFGIKASGSWQGKVVTTMTTEYVDGVAQKL 228

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 557255131  221 ---FRSYDSKGNSLKDYAKFLKDNRRYRenGVFNSKTYIEQADSITKAGYST 269
Cdd:TIGR02541 229 takFRSYSSYEEAFSDYARLLNNNPRYE--AVLQQRSAESFARGLQRAGYAT 278
flgJ PRK05684
flagellar assembly peptidoglycan hydrolase FlgJ;
145-288 3.08e-25

flagellar assembly peptidoglycan hydrolase FlgJ;


Pssm-ID: 235559 [Multi-domain]  Cd Length: 312  Bit Score: 102.65  E-value: 3.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557255131 145 EAFISALTPEAKSIYKEYDILPSIVIGQAILESDWGKSKL------SSNynNLFGIKATKSWKGKTVKMETSEnYDDTII 218
Cdd:PRK05684 153 DDFVARLSPPAQKAAQQSGVPHHLLLAQAALESGWGQREIrtadgsPSH--NLFGIKADGSWKGPVTEITTTE-YENGVA 229

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 557255131 219 ----DVFRSYDSKGNSLKDYAKFLKDNRRYRenGVFNSKTYIEQADSITKAGYSTkkdkDGNhmYGSLLTEIIR 288
Cdd:PRK05684 230 vkvkAAFRVYDSYLESFNDYVSLLTNNPRYA--AVTQAASPEQFARALQDAGYAT----DPN--YARKLVSVIQ 295
LYZ2 smart00047
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
 145-294 6.59e-22

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


Pssm-ID: 214488 [Multi-domain]  Cd Length: 147  Bit Score: 89.80  E-value: 6.59e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557255131   145 EAFISALTPEAKSIYKEYDILPSIVIGQAILESDWGKSKLSSNYNNLFGIKAtkSWKGKTVKMETSENYD---DTIIDVF 221
Cdd:smart00047   9 LEFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLAKKYNNLFGIKG--AYDGRPVRMGTLEYLNggwVTVKAAF 86

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557255131   222 RSYdsKGNSLKDYAKFLKdNRRYRENGVFNSKtyieqadSITKAGYSTKKDkdgnhmYGSLLTEIIREYNLQL 294
Cdd:smart00047  87 RGY--FGEKFIDYAYVLR-GQNPLYKKRWGSN-------ALQTAGYATDPD------YAKKLIRIIALYDEKL 143
Glucosaminidase pfam01832
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ...
 153-234 8.76e-22

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: 87.63  E-value: 8.76e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557255131  153 PEAKSIYKEYDILPSIVIGQAILESDWGKSKLSSNYNNLFGIKAtkSWKGKtVKMETSENyddTIIDVFRSYDSKGNSLK 232
Cdd:pfam01832   2 PAAIEAAKKYGIPASVLLAQAALESGWGTSRLAKESNNLFGIKA--SWKGK-VAYDTDEV---TVAARFRKYDSVEESIR 75


                  ..
gi 557255131  233 DY 234
Cdd:pfam01832  76 DY 77
sporang_Gsm NF038016
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ...
 145-292 4.11e-19

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: 85.95  E-value: 4.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557255131 145 EAFISALTPEAKSIYKEYDILPSIVIGQAILESDWGKSKLSSNYNNLFGIK---------------ATK--SWKGKTVKM 207
Cdd:NF038016 161 AQFIAAVAPPAQQSQRATGVPASVTIAQAILESGWGRSGLTREDHNYFGIKcfgspgpiavgcrsyATFecSPTGGCFDT 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557255131 208 EtsenyddtiiDVFRSYDSKGNSLKDYAKFLKDNRRYREngVFNSKTYIEQ-ADSITKAGYSTKKDkdgnhmYGSLLTEI 286
Cdd:NF038016 241 T----------ATFRAYASAADSFRDHGRFLSVNSRYAP--AFAYTDDPDQfAREIHKAGYATDPT------YADKLIGL 302


                 ....*.
gi 557255131 287 IREYNL 292
Cdd:NF038016 303 MKQYNL 308
 
Name Accession Description Interval E-value
FlgJ COG1705
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ...
 138-293 4.72e-54

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


Pssm-ID: 441311 [Multi-domain]  Cd Length: 276  Bit Score: 177.85  E-value: 4.72e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557255131 138 VKVSEEKEAFISALTPEAKSIYKEYDILPSIVIGQAILESDWGKSKLS-SNYNNLFGIKATKSWKGKTVKMETSENYD-- 214
Cdd:COG1705  123 AAASASPEEFIAKIAPAAQKAAKKYGVPASVLIAQAALESGWGKSELDgSPSNNLFGIKAGGSWQGKSVEVTTTEYVNgk 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557255131 215 -DTIIDVFRSYDSKGNSLKDYAKFLKDNRRYRENgVFNSKTYIEQADSITKAGYSTkkDKDgnhmYGSLLTEIIREYNLQ 293
Cdd:COG1705  203 aVKIKARFRAYDSYAESFRDYARLLKNNPRYAGA-LANAKDYEAFAKALQKAGYAT--DPK----YADKLISIIESYNLT 275
flagell_FlgJ TIGR02541
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ...
 145-269 9.71e-28

flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts directly in flagellar rod assembly. The C-terminal region is a flagellum-specific muramidase (peptidoglycan hydrolase) required for formation of the outer membrane L ring.


Pssm-ID: 274188 [Multi-domain]  Cd Length: 294  Bit Score: 109.17  E-value: 9.71e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557255131  145 EAFISALTPEAKSIYKEYDILPSIVIGQAILESDWGKSKL----SSNYNNLFGIKATKSWKGKTVKMETSENYDDTIIDV 220
Cdd:TIGR02541 149 KSFVNSMLPHARKAAQQLGVPPHLILAQAALESGWGQRQIrnadGSPSYNLFGIKASGSWQGKVVTTMTTEYVDGVAQKL 228

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 557255131  221 ---FRSYDSKGNSLKDYAKFLKDNRRYRenGVFNSKTYIEQADSITKAGYST 269
Cdd:TIGR02541 229 takFRSYSSYEEAFSDYARLLNNNPRYE--AVLQQRSAESFARGLQRAGYAT 278
flgJ PRK05684
flagellar assembly peptidoglycan hydrolase FlgJ;
145-288 3.08e-25

flagellar assembly peptidoglycan hydrolase FlgJ;


Pssm-ID: 235559 [Multi-domain]  Cd Length: 312  Bit Score: 102.65  E-value: 3.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557255131 145 EAFISALTPEAKSIYKEYDILPSIVIGQAILESDWGKSKL------SSNynNLFGIKATKSWKGKTVKMETSEnYDDTII 218
Cdd:PRK05684 153 DDFVARLSPPAQKAAQQSGVPHHLLLAQAALESGWGQREIrtadgsPSH--NLFGIKADGSWKGPVTEITTTE-YENGVA 229

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 557255131 219 ----DVFRSYDSKGNSLKDYAKFLKDNRRYRenGVFNSKTYIEQADSITKAGYSTkkdkDGNhmYGSLLTEIIR 288
Cdd:PRK05684 230 vkvkAAFRVYDSYLESFNDYVSLLTNNPRYA--AVTQAASPEQFARALQDAGYAT----DPN--YARKLVSVIQ 295
flgJ PRK12709
flagellar rod assembly protein/muramidase FlgJ; Provisional
 141-269 1.03e-24

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 237179 [Multi-domain]  Cd Length: 320  Bit Score: 101.54  E-value: 1.03e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557255131 141 SEEKEAFISALTPEAKSIYKEYDILPSIVIGQAILESDWGKSKL-----SSNYNnLFGIKATKSWKGKTVKMETSENYDD 215
Cdd:PRK12709 170 SPDADAFVDKLAAPAQAASAATGIPARFIVGQAALESGWGKREIrgadgSTSYN-VFGIKATKGWTGRTVSAVTTEYVNG 248

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 557255131 216 T---IIDVFRSYDSKGNSLKDYAKFLKDNRRYreNGVFNSKTYIEQ-ADSITKAGYST 269
Cdd:PRK12709 249 KprrVVAKFRAYDSYEHAMTDYANLLKNNPRY--AGVLNASRSVEGfAHGMQKAGYAT 304
LYZ2 smart00047
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
 145-294 6.59e-22

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


Pssm-ID: 214488 [Multi-domain]  Cd Length: 147  Bit Score: 89.80  E-value: 6.59e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557255131   145 EAFISALTPEAKSIYKEYDILPSIVIGQAILESDWGKSKLSSNYNNLFGIKAtkSWKGKTVKMETSENYD---DTIIDVF 221
Cdd:smart00047   9 LEFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLAKKYNNLFGIKG--AYDGRPVRMGTLEYLNggwVTVKAAF 86

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557255131   222 RSYdsKGNSLKDYAKFLKdNRRYRENGVFNSKtyieqadSITKAGYSTKKDkdgnhmYGSLLTEIIREYNLQL 294
Cdd:smart00047  87 RGY--FGEKFIDYAYVLR-GQNPLYKKRWGSN-------ALQTAGYATDPD------YAKKLIRIIALYDEKL 143
Glucosaminidase pfam01832
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ...
 153-234 8.76e-22

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: 87.63  E-value: 8.76e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557255131  153 PEAKSIYKEYDILPSIVIGQAILESDWGKSKLSSNYNNLFGIKAtkSWKGKtVKMETSENyddTIIDVFRSYDSKGNSLK 232
Cdd:pfam01832   2 PAAIEAAKKYGIPASVLLAQAALESGWGTSRLAKESNNLFGIKA--SWKGK-VAYDTDEV---TVAARFRKYDSVEESIR 75


                  ..
gi 557255131  233 DY 234
Cdd:pfam01832  76 DY 77
flgJ PRK12713
flagellar rod assembly protein/muramidase FlgJ; Provisional
 147-269 9.62e-21

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 139173 [Multi-domain]  Cd Length: 339  Bit Score: 90.96  E-value: 9.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557255131 147 FISALTPEAKSIYKEYDILPSIVIGQAILESDWGKSKL-----SSNYNnLFGIKATKSWKGKTVKMETSENYD---DTII 218
Cdd:PRK12713 184 FVSRMSRAANVAAQQSGVPARLILGQAALESGWGRRELrhedgSTSYN-LFGIKAGASWKGKVVNVMTTEYVDgvaQKLV 262

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 557255131 219 DVFRSYDSKGNSLKDYAKFLKDNRRYRenGVFNSKTYIEQADSITKAGYST 269
Cdd:PRK12713 263 QPFRAYSSYEESFSDYARLIGNSPRYE--AVTQAGNEIEAARRIQEAGYAT 311
sporang_Gsm NF038016
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ...
 145-292 4.11e-19

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: 85.95  E-value: 4.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557255131 145 EAFISALTPEAKSIYKEYDILPSIVIGQAILESDWGKSKLSSNYNNLFGIK---------------ATK--SWKGKTVKM 207
Cdd:NF038016 161 AQFIAAVAPPAQQSQRATGVPASVTIAQAILESGWGRSGLTREDHNYFGIKcfgspgpiavgcrsyATFecSPTGGCFDT 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557255131 208 EtsenyddtiiDVFRSYDSKGNSLKDYAKFLKDNRRYREngVFNSKTYIEQ-ADSITKAGYSTKKDkdgnhmYGSLLTEI 286
Cdd:NF038016 241 T----------ATFRAYASAADSFRDHGRFLSVNSRYAP--AFAYTDDPDQfAREIHKAGYATDPT------YADKLIGL 302


                 ....*.
gi 557255131 287 IREYNL 292
Cdd:NF038016 303 MKQYNL 308
flgJ PRK12712
flagellar rod assembly protein/muramidase FlgJ; Provisional
 146-289 1.30e-18

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 139172 [Multi-domain]  Cd Length: 344  Bit Score: 85.06  E-value: 1.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557255131 146 AFISALTPEAKSIYKEYDILPSIVIGQAILESDWGKSKLS----SNYNNLFGIKATKSWKGKTVKMETSENYDDTIIDV- 220
Cdd:PRK12712 199 AFVARMAGPAEAASRASGVPARLIVGQAALESGWGRREIThadgSTTFNVFGIKAGANWKGRVAEVTTTEYVDGQPQKVr 278

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 557255131 221 --FRSYDSKGNSLKDYAKFLKDNRRYRenGVFNSKTYIEQADSITKAGYSTkkdkdgNHMYGSLLTEIIRE 289
Cdd:PRK12712 279 arFRAYGSYDEACADYARLLTSNPRYA--GVVSAASADEAAHGLQRAGYAT------DPAYGHKLVKIMKK 341
PRK08581 PRK08581
amidase domain-containing protein;
141-298 2.17e-17

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 82.53  E-value: 2.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557255131 141 SEEKEAFISALTPEAKSIYKEYDILPSIVIGQAILESDWGKSKLS-SNYNNLFGIKAtkSWKGKTVKMETSE---NYDDT 216
Cdd:PRK08581 317 SKDTRQFIKSIAKDAHRIGQDNDIYASVMIAQAILESDSGQSALAkSPNHNLFGIKG--AYEGNSVSFNTLEadgNQLYS 394

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557255131 217 IIDVFRSYDSKGNSLKDYAKFLKD----NRR-YRENGVFNSKTYIEQADSITKAgYSTKKDkdgnhmYGSLLTEIIREYN 291
Cdd:PRK08581 395 INAGFRKYPSTKESLEDYADLIKNgidgNSTiYKPTWKSEAKSYKDATSHLSKT-YATDPN------YAKKLNSIIKHYN 467


                 ....*..
gi 557255131 292 LQLIDNE 298
Cdd:PRK08581 468 LTQFDDE 474
flgJ PRK12711
flagellar assembly peptidoglycan hydrolase FlgJ;
145-269 4.02e-15

flagellar assembly peptidoglycan hydrolase FlgJ;


Pssm-ID: 237180 [Multi-domain]  Cd Length: 392  Bit Score: 75.00  E-value: 4.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557255131 145 EAFISALTPEAKSIYKEYDILPSIVIGQAILESDWGKSKL--SSNYNNLFGIKATkSWKGKTVKMETSENYD---DTIID 219
Cdd:PRK12711 216 EGFVAKIWTHAQKAARELGVDPRALVAQAALETGWGRRGIgnGGDSNNLFGIKAT-GWNGDKVTTGTHEYVNgvkTTETA 294

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 557255131 220 VFRSYDSKGNSLKDYAKFLKDNRRYREngVFNSKTYIEQ-ADSITKAGYST 269
Cdd:PRK12711 295 DFRAYGSAEESFADYVRLLKNNSRYQQ--ALQAGTDIKGfARGLQQAGYAT 343
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
145-297 1.62e-14

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 73.96  E-value: 1.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557255131 145 EAFISALTPEAKSIYKEYDILPSIVIGQAILESDWGKSKLSSNYN-NLFGIKAT---KSWKGKTVKMETSENYdDTIIDV 220
Cdd:PRK06347 151 QSFIQTIQASSSQIAAENDLYASVMIAQAILESAYGTSELGSAPNyNLFGIKGAyngQSYTKQTLEDDGKGNY-YTITAK 229

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557255131 221 FRSYDSKGNSLKDYAKFLKDNRRYRENgvFNSKTYIEQADSITKAGYSTKKDKDGNHMYGSLLTEIIREYNLQLIDN 297
Cdd:PRK06347 230 FRKYPSYHQSLEDYAQVIRKGPSWNPN--YYSKVWKSNTTSYKDATKALTGTYATDTAYATKLNDLISRYNLTQYDS 304
flgJ PRK12710
flagellar rod assembly protein/muramidase FlgJ; Provisional
 147-269 4.12e-09

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 139170 [Multi-domain]  Cd Length: 291  Bit Score: 56.72  E-value: 4.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557255131 147 FISALTPEAKSIYKEYDILPSIVIGQAILESDWGK----SKLSSNYNNLFGIKATKSWKGKTVKMETSENYDDTIIDV-- 220
Cdd:PRK12710 133 FVKSVWPTAKQAASLIGLDPKLLVAQAALETGWGKfvtrDADGSSSNNLFNIKTGSHSEVESIQVKTTEYIADTPIKIna 212

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 557255131 221 -FRSYDSKGNSLKDYAKFLKDNRRYRE--NGVFNSKTYIEQadsITKAGYST 269
Cdd:PRK12710 213 sFRKYPSIEHSFHDYVSLIKGSERYQMalANAENPEIYVSE---LNKAGYAT 261
PRK10356 PRK10356
protein bax;
163-279 3.31e-05

protein bax;


Pssm-ID: 182404  Cd Length: 274  Bit Score: 44.48  E-value: 3.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557255131 163 DILP-SIVIGQAILESDWGKSKLSSNYNNLFGIKATK----SWKGKTVKMETSENYDDTIIdvfrSYDSKGNSLKDYAKF 237
Cdd:PRK10356 147 DIIPtSMVATMAAAESGWGTSKLARNNNNLFGMKCMKgrctNAPGKVKGYSQFSSVKESVS----AYVTNLNTHPAYSSF 222

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 557255131 238 LKDNRRYREngvfnSKTYIEQADSITK-AGYSTKKDKDGNHMY 279
Cdd:PRK10356 223 RKSRAQLRK-----ADQEVTATAMIHKlKGYSTKGSSYNNYLF 260
LytD COG4193
Beta- N-acetylglucosaminidase [Carbohydrate transport and metabolism];
160-197 1.51e-03

Beta- N-acetylglucosaminidase [Carbohydrate transport and metabolism];


Pssm-ID: 443347 [Multi-domain]  Cd Length: 423  Bit Score: 39.95  E-value: 1.51e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 557255131 160 KEYDILPSIVIGQAILESDWGKSKLSS-------NYNNLFGIKAT 197
Cdd:COG4193  283 KKYGVNPLYLASHALLETGNGTSKLAKgvevngkTYYNLFGIGAY 327
 
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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