|
Name |
Accession |
Description |
Interval |
E-value |
| flgJ |
PRK05684 |
flagellar assembly peptidoglycan hydrolase FlgJ; |
1-328 |
7.42e-147 |
|
flagellar assembly peptidoglycan hydrolase FlgJ;
Pssm-ID: 235559 [Multi-domain] Cd Length: 312 Bit Score: 416.20 E-value: 7.42e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 1 MNKMADASQFLDLGGLDKLRAQAQQDQKAALKEVAQQFEGIFVQMLMKSMRDANAifeSDSPMNSQYTKFYEQMHDQQMS 80
Cdd:PRK05684 2 SDSLSDSGAAYDLQSLNSLKAKAGKDPKANLRAVAQQFEGMFVQMMLKSMRDANP---KDGLMNSQQTKLYTSMYDQQIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 81 VELSSKGMLGLADLMVQQLSPENSGITPASVlrgdvdnRSVAALNGGQTekisgveaaaakASALPSNDSLQQVLSGKVL 160
Cdd:PRK05684 79 QQLSAGGGLGLADMMVKQLSPEQSPAPEESA-------GAVPMKFDLET------------VQSYQNQALAQLVRKAIPQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 161 PSWRQARPAIGSQEEFVRQLYPHAKAAADALGTQPEVLLAQSALETGWGQKMVRGHKGESSNNLFNIKADRRWQGEKAAV 240
Cdd:PRK05684 140 PPLASDKPLFGSSDDFVARLSPPAQKAAQQSGVPHHLLLAQAALESGWGQREIRTADGSPSHNLFGIKADGSWKGPVTEI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 241 STLEYEQGTAVRQKADFRVYDSFEQSFNDFVSFISDNDRYSqARKMAANPGEFIKALAEAGYATDPQYANKVMKVLDTIK 320
Cdd:PRK05684 220 TTTEYENGVAVKVKAAFRVYDSYLESFNDYVSLLTNNPRYA-AVTQAASPEQFARALQDAGYATDPNYARKLVSVIQQMK 298
|
....*...
gi 1098557517 321 ADFGQLLQ 328
Cdd:PRK05684 299 SMGEKVSK 306
|
|
| flagell_FlgJ |
TIGR02541 |
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ... |
12-320 |
1.17e-85 |
|
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: 260.17 E-value: 1.17e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 12 DLGGLDKLRAQAQQDQKAALKEVAQQFEGIFVQMLMKSMRDANAIFESdspMNSQYTKFYEQMHDQQMSVELSSKGMLGL 91
Cdd:TIGR02541 4 DAQSLDSLKAKAVKDPKEQEKEAARQFEALFLNMMLKSMREATPKDGL---FDSQQTRFYTQMLDQQMAQQLSANGGIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 92 ADLMVQQLSPEnSGITPASVLRGDVDNRSVAALNGGQTEKISGVEAAAAkasalpsndslqqvLSGKVLPSWRQARPAI- 170
Cdd:TIGR02541 81 ADMIVAQLTKG-QGNEPSEGAARGAAPSPLVYRPRLDPKPRRIVKALIE--------------SVELSRPRGRSHAESVp 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 171 GSQEEFVRQLYPHAKAAADALGTQPEVLLAQSALETGWGQKMVRGHKGESSNNLFNIKADRRWQGEKAAVSTLEYEQGTA 250
Cdd:TIGR02541 146 GHPKSFVNSMLPHARKAAQQLGVPPHLILAQAALESGWGQRQIRNADGSPSYNLFGIKASGSWQGKVVTTMTTEYVDGVA 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 251 VRQKADFRVYDSFEQSFNDFVSFISDNDRYSQARKmAANPGEFIKALAEAGYATDPQYANKVMKVLDTIK 320
Cdd:TIGR02541 226 QKLTAKFRSYSSYEEAFSDYARLLNNNPRYEAVLQ-QRSAESFARGLQRAGYATDPRYARKLLQVIQSLA 294
|
|
| FlgJ |
COG1705 |
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ... |
45-320 |
2.18e-63 |
|
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];
Pssm-ID: 441311 [Multi-domain] Cd Length: 276 Bit Score: 202.51 E-value: 2.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 45 MLMKSMRDANAIFESDSPMNSQYTKFYEQMHDQQMSVELSSKGMLGLADLMVQQLSPENSGitpasVLRGDVDNRSVAAL 124
Cdd:COG1705 6 SSSASSSAGAAAQAKAAAQAAASAMASLEAAASSALSSSTSSSSKGASSSQSLEGLASALG-----GGASALSSAAALAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 125 NGGQTEKISGVEAAAAKASALPSNDSLQQVLSGKVLPSWRQARPAIGSQEEFVRQLYPHAKAAADALGTQPEVLLAQSAL 204
Cdd:COG1705 81 KSAAKSATEAGGGLASANAAATSAAALAASLSGAAALAASATAAASASPEEFIAKIAPAAQKAAKKYGVPASVLIAQAAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 205 ETGWGQKMVrghKGESSNNLFNIKADRRWQGEKAAVSTLEYEQGTAVRQKADFRVYDSFEQSFNDFVSFISDNDRYSQAR 284
Cdd:COG1705 161 ESGWGKSEL---DGSPSNNLFGIKAGGSWQGKSVEVTTTEYVNGKAVKIKARFRAYDSYAESFRDYARLLKNNPRYAGAL 237
|
250 260 270
....*....|....*....|....*....|....*.
gi 1098557517 285 KMAANPGEFIKALAEAGYATDPQYANKVMKVLDTIK 320
Cdd:COG1705 238 ANAKDYEAFAKALQKAGYATDPKYADKLISIIESYN 273
|
|
| LYZ2 |
smart00047 |
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes. |
168-316 |
4.31e-26 |
|
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
Pssm-ID: 214488 [Multi-domain] Cd Length: 147 Bit Score: 101.36 E-value: 4.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 168 PAIGSQEEFVRQLYPHAKAAADALGTQPEVLLAQSALETGWGQKMVRGhkgeSSNNLFNIKADrrWQGEKAAVSTLEYEQ 247
Cdd:smart00047 3 LAGGSTLEFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLAK----KYNNLFGIKGA--YDGRPVRMGTLEYLN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1098557517 248 GTAVRQKADFRVYdsFEQSFNDFVSFISDNDRYSqarKMAANPgefiKALAEAGYATDPQYANKVMKVL 316
Cdd:smart00047 77 GGWVTVKAAFRGY--FGEKFIDYAYVLRGQNPLY---KKRWGS----NALQTAGYATDPDYAKKLIRII 136
|
|
| sporang_Gsm |
NF038016 |
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ... |
160-317 |
5.06e-23 |
|
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: 97.12 E-value: 5.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 160 LPSWRQARPAI--GSQEEFVRQLYPHAKAAADALGTQPEVLLAQSALETGWGqkmvRGHKGESSNNLFNIKAdRRWQGEK 237
Cdd:NF038016 145 LPWCGQDPPTVprGTPAQFIAAVAPPAQQSQRATGVPASVTIAQAILESGWG----RSGLTREDHNYFGIKC-FGSPGPI 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 238 A----AVSTLEYEQ-GTAVRQKADFRVYDSFEQSFNDFVSFISDNDRYSQARKMAANPGEFIKALAEAGYATDPQYANKV 312
Cdd:NF038016 220 AvgcrSYATFECSPtGGCFDTTATFRAYASAADSFRDHGRFLSVNSRYAPAFAYTDDPDQFAREIHKAGYATDPTYADKL 299
|
....*
gi 1098557517 313 MKVLD 317
Cdd:NF038016 300 IGLMK 304
|
|
| Glucosaminidase |
pfam01832 |
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ... |
182-270 |
2.76e-18 |
|
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: 78.38 E-value: 2.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 182 PHAKAAADALGTQPEVLLAQSALETGWGQkmvrGHKGESSNNLFNIKAdrRWQGeKAAVSTLEYeqgtavRQKADFRVYD 261
Cdd:pfam01832 2 PAAIEAAKKYGIPASVLLAQAALESGWGT----SRLAKESNNLFGIKA--SWKG-KVAYDTDEV------TVAARFRKYD 68
|
....*....
gi 1098557517 262 SFEQSFNDF 270
Cdd:pfam01832 69 SVEESIRDY 77
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| flgJ |
PRK05684 |
flagellar assembly peptidoglycan hydrolase FlgJ; |
1-328 |
7.42e-147 |
|
flagellar assembly peptidoglycan hydrolase FlgJ;
Pssm-ID: 235559 [Multi-domain] Cd Length: 312 Bit Score: 416.20 E-value: 7.42e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 1 MNKMADASQFLDLGGLDKLRAQAQQDQKAALKEVAQQFEGIFVQMLMKSMRDANAifeSDSPMNSQYTKFYEQMHDQQMS 80
Cdd:PRK05684 2 SDSLSDSGAAYDLQSLNSLKAKAGKDPKANLRAVAQQFEGMFVQMMLKSMRDANP---KDGLMNSQQTKLYTSMYDQQIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 81 VELSSKGMLGLADLMVQQLSPENSGITPASVlrgdvdnRSVAALNGGQTekisgveaaaakASALPSNDSLQQVLSGKVL 160
Cdd:PRK05684 79 QQLSAGGGLGLADMMVKQLSPEQSPAPEESA-------GAVPMKFDLET------------VQSYQNQALAQLVRKAIPQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 161 PSWRQARPAIGSQEEFVRQLYPHAKAAADALGTQPEVLLAQSALETGWGQKMVRGHKGESSNNLFNIKADRRWQGEKAAV 240
Cdd:PRK05684 140 PPLASDKPLFGSSDDFVARLSPPAQKAAQQSGVPHHLLLAQAALESGWGQREIRTADGSPSHNLFGIKADGSWKGPVTEI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 241 STLEYEQGTAVRQKADFRVYDSFEQSFNDFVSFISDNDRYSqARKMAANPGEFIKALAEAGYATDPQYANKVMKVLDTIK 320
Cdd:PRK05684 220 TTTEYENGVAVKVKAAFRVYDSYLESFNDYVSLLTNNPRYA-AVTQAASPEQFARALQDAGYATDPNYARKLVSVIQQMK 298
|
....*...
gi 1098557517 321 ADFGQLLQ 328
Cdd:PRK05684 299 SMGEKVSK 306
|
|
| flagell_FlgJ |
TIGR02541 |
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ... |
12-320 |
1.17e-85 |
|
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: 260.17 E-value: 1.17e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 12 DLGGLDKLRAQAQQDQKAALKEVAQQFEGIFVQMLMKSMRDANAIFESdspMNSQYTKFYEQMHDQQMSVELSSKGMLGL 91
Cdd:TIGR02541 4 DAQSLDSLKAKAVKDPKEQEKEAARQFEALFLNMMLKSMREATPKDGL---FDSQQTRFYTQMLDQQMAQQLSANGGIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 92 ADLMVQQLSPEnSGITPASVLRGDVDNRSVAALNGGQTEKISGVEAAAAkasalpsndslqqvLSGKVLPSWRQARPAI- 170
Cdd:TIGR02541 81 ADMIVAQLTKG-QGNEPSEGAARGAAPSPLVYRPRLDPKPRRIVKALIE--------------SVELSRPRGRSHAESVp 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 171 GSQEEFVRQLYPHAKAAADALGTQPEVLLAQSALETGWGQKMVRGHKGESSNNLFNIKADRRWQGEKAAVSTLEYEQGTA 250
Cdd:TIGR02541 146 GHPKSFVNSMLPHARKAAQQLGVPPHLILAQAALESGWGQRQIRNADGSPSYNLFGIKASGSWQGKVVTTMTTEYVDGVA 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 251 VRQKADFRVYDSFEQSFNDFVSFISDNDRYSQARKmAANPGEFIKALAEAGYATDPQYANKVMKVLDTIK 320
Cdd:TIGR02541 226 QKLTAKFRSYSSYEEAFSDYARLLNNNPRYEAVLQ-QRSAESFARGLQRAGYATDPRYARKLLQVIQSLA 294
|
|
| FlgJ |
COG1705 |
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ... |
45-320 |
2.18e-63 |
|
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];
Pssm-ID: 441311 [Multi-domain] Cd Length: 276 Bit Score: 202.51 E-value: 2.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 45 MLMKSMRDANAIFESDSPMNSQYTKFYEQMHDQQMSVELSSKGMLGLADLMVQQLSPENSGitpasVLRGDVDNRSVAAL 124
Cdd:COG1705 6 SSSASSSAGAAAQAKAAAQAAASAMASLEAAASSALSSSTSSSSKGASSSQSLEGLASALG-----GGASALSSAAALAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 125 NGGQTEKISGVEAAAAKASALPSNDSLQQVLSGKVLPSWRQARPAIGSQEEFVRQLYPHAKAAADALGTQPEVLLAQSAL 204
Cdd:COG1705 81 KSAAKSATEAGGGLASANAAATSAAALAASLSGAAALAASATAAASASPEEFIAKIAPAAQKAAKKYGVPASVLIAQAAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 205 ETGWGQKMVrghKGESSNNLFNIKADRRWQGEKAAVSTLEYEQGTAVRQKADFRVYDSFEQSFNDFVSFISDNDRYSQAR 284
Cdd:COG1705 161 ESGWGKSEL---DGSPSNNLFGIKAGGSWQGKSVEVTTTEYVNGKAVKIKARFRAYDSYAESFRDYARLLKNNPRYAGAL 237
|
250 260 270
....*....|....*....|....*....|....*.
gi 1098557517 285 KMAANPGEFIKALAEAGYATDPQYANKVMKVLDTIK 320
Cdd:COG1705 238 ANAKDYEAFAKALQKAGYATDPKYADKLISIIESYN 273
|
|
| flgJ |
PRK12709 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
11-319 |
2.99e-56 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 237179 [Multi-domain] Cd Length: 320 Bit Score: 185.51 E-value: 2.99e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 11 LDLGGLDKLRAQAQQDQKAALKEVAQQFEGIFVQMLMKSMRDANAifeSDSPMNSQYTKFYEQMHDQQMSVELSSKGmLG 90
Cdd:PRK12709 16 LDVQGFDALRAQAKASPQAGAKMVAGQFDAMFTQMMLKSMRDATP---SDGLFDSHTSKMYTSMLDQQLAQQMSSKG-IG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 91 LADLMVQQLSpENSGITPASvlrGDVDNRSVAALNGGQTEKISGVEAAAAKASALPSNDSLQQVL---SGKVLPSWRQAR 167
Cdd:PRK12709 92 VADALMKQLL-RNAGVAAGA---QGDAGAGGMGGLGGNEGGLAAMNALAKAYANAANNGALAGTRgysAGSALTPPLKGN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 168 PAIGSQEEFVRQLYPHAKAAADALGTQPEVLLAQSALETGWGQKMVRGHKGESSNNLFNIKADRRWQGEKAAVSTLEYEQ 247
Cdd:PRK12709 168 GGSPDADAFVDKLAAPAQAASAATGIPARFIVGQAALESGWGKREIRGADGSTSYNVFGIKATKGWTGRTVSAVTTEYVN 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1098557517 248 GTAVRQKADFRVYDSFEQSFNDFVSFISDNDRYSQARKMAANPGEFIKALAEAGYATDPQYANKVMKVLDTI 319
Cdd:PRK12709 248 GKPRRVVAKFRAYDSYEHAMTDYANLLKNNPRYAGVLNASRSVEGFAHGMQKAGYATDPHYAKKLISIMQQI 319
|
|
| flgJ |
PRK12713 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
11-325 |
7.24e-50 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 139173 [Multi-domain] Cd Length: 339 Bit Score: 169.54 E-value: 7.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 11 LDLGGLDKLRAQAQQD--QKAALKEVAQQFEGIFVQMLMKSMRDANAifeSDSPMNSQYTKFYEQMHDQQMSVELSSKGm 88
Cdd:PRK12713 17 FDLGRLADLKRDAVKApdGQRQQTEVARQFEALFLQMMLKRMREATP---KEGLFDSQQTEMLQGMADEQLALQLASPG- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 89 LGLADLMVQQLSPENSGITPASVLRGDVDNRSVAALNGGQTEKISGVEAAAAKASALPSNDsLQQVLSgkVLPSWRQARP 168
Cdd:PRK12713 93 IGLAQALLGQMQQGQPPVPAAAAAGGDAAAARALAGTAAPAPLVRDLRGNYVQPDPAPRRE-VNALLD--VLRSNRARDR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 169 AIGSQE-------EFVRQLYPHAKAAADALGTQPEVLLAQSALETGWGQKMVRGHKGESSNNLFNIKADRRWQGEKAAVS 241
Cdd:PRK12713 170 AMAAAEgapshvvDFVSRMSRAANVAAQQSGVPARLILGQAALESGWGRRELRHEDGSTSYNLFGIKAGASWKGKVVNVM 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 242 TLEYEQGTAVRQKADFRVYDSFEQSFNDFVSFISDNDRYsQARKMAANPGEFIKALAEAGYATDPQYANKVMKVLDTIKA 321
Cdd:PRK12713 250 TTEYVDGVAQKLVQPFRAYSSYEESFSDYARLIGNSPRY-EAVTQAGNEIEAARRIQEAGYATDPRYAEKLISIMGQLRT 328
|
....
gi 1098557517 322 DFGQ 325
Cdd:PRK12713 329 SVAR 332
|
|
| flgJ |
PRK12710 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
12-315 |
1.70e-49 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 139170 [Multi-domain] Cd Length: 291 Bit Score: 167.28 E-value: 1.70e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 12 DLGGLDKLRAQAQQDQKAALKEVAQQFEGIFVQMLMKSMRDANAIFESDSPMNSQYTKFYEQMHDQQMSVELSSKGMLGL 91
Cdd:PRK12710 10 DFQGLNELKVQAKNNAKEALPEVAKQFEGIFLQSMLKSMRMGQHFLDESSPFSGKNEATFQEMLDTQYASTIAESKGIGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 92 ADLMVQQLspENSGITPASvlrgDVDNRSVAALNGGQTEkisgveaaaakasalpSNDSLQQVlsgkvlpswrqarpaig 171
Cdd:PRK12710 90 AALLAKQL--ENSVGDKAN----NPVNSSTEVSNTKVTN----------------SEESLSVV----------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 172 sqEEFVRQLYPHAKAAADALGTQPEVLLAQSALETGWGQKMVRGHKGESSNNLFNIKADRRWQGEKAAVSTLEYEQGTAV 251
Cdd:PRK12710 131 --DDFVKSVWPTAKQAASLIGLDPKLLVAQAALETGWGKFVTRDADGSSSNNLFNIKTGSHSEVESIQVKTTEYIADTPI 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1098557517 252 RQKADFRVYDSFEQSFNDFVSFISDNDRYSQARKMAANPGEFIKALAEAGYATDPQYANKVMKV 315
Cdd:PRK12710 209 KINASFRKYPSIEHSFHDYVSLIKGSERYQMALANAENPEIYVSELNKAGYATDPNYSNKILSI 272
|
|
| flgJ |
PRK12712 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
5-321 |
1.50e-47 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 139172 [Multi-domain] Cd Length: 344 Bit Score: 163.64 E-value: 1.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 5 ADASQ--FLDLGGLDKLRAQAQQ-DQKAALKEVAQQFEGIFVQMLMKSMRDANAifeSDSPMNSQYTKFYEQMHDQQMSV 81
Cdd:PRK12712 10 ADLSQrfALDTQGFEALKHSARGgADAGTLQAAARQFEAVFTQMVLKSMRDATP---QDGLFDNEQSKLYMSMMDQQLAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 82 ELSSKGmLGLADLMVQQLSPENSGITPASVlrgdvdnrsvAALNGGQTEKISGVEAAA---AKASALPSNDSLQQVLSGK 158
Cdd:PRK12712 87 QMSSRG-IGLADVMVRQLARATGTQMPPGM----------NAAGGATAGSAADAEMARlldGRGAGAADADAGDLPAIGT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 159 VLP--SW------RQARP---AIGSQEE----------------FVRQLYPHAKAAADALGTQPEVLLAQSALETGWGQK 211
Cdd:PRK12712 156 IVPgqAWnptaglRQYQPqayADQGQGEdrlgrlpddapahvsaFVARMAGPAEAASRASGVPARLIVGQAALESGWGRR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 212 MVRGHKGESSNNLFNIKADRRWQGEKAAVSTLEYEQGTAVRQKADFRVYDSFEQSFNDFVSFISDNDRYSqARKMAANPG 291
Cdd:PRK12712 236 EITHADGSTTFNVFGIKAGANWKGRVAEVTTTEYVDGQPQKVRARFRAYGSYDEACADYARLLTSNPRYA-GVVSAASAD 314
|
330 340 350
....*....|....*....|....*....|
gi 1098557517 292 EFIKALAEAGYATDPQYANKVMKVLDTIKA 321
Cdd:PRK12712 315 EAAHGLQRAGYATDPAYGHKLVKIMKKVSA 344
|
|
| flgJ |
PRK12711 |
flagellar assembly peptidoglycan hydrolase FlgJ; |
33-312 |
1.04e-43 |
|
flagellar assembly peptidoglycan hydrolase FlgJ;
Pssm-ID: 237180 [Multi-domain] Cd Length: 392 Bit Score: 154.74 E-value: 1.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 33 EVAQQFEGIFVQMLMKSMRDANaifeSDSPMNSQYTKFYEQMHDQQMSVELSSKGMLGLADLMVQQLS------PENSGI 106
Cdd:PRK12711 23 KVSRQLEGQFAQMLVKSMRDAS----SGDPMFPGENQMFREMYDQQMAKALTDGKGLGLSAMISKQLSgdtggpALNTAL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 107 TPASVLRGD--VDNRSVAAL-----NGGQTEKISGVEAAAAKASALPSNDSLQQVLS--------------GKVLPSW-- 163
Cdd:PRK12711 99 NTAKAAKAYslVAGKRDASLplparDGAAAGITTSSVAAAALSAGNLSGIGMSQVLDliagrtgageagsdDAAALSWps 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 164 -------------------------RQARPAIGSQ--EEFVRQLYPHAKAAADALGTQPEVLLAQSALETGWGQKMVrgH 216
Cdd:PRK12711 179 andrwsdvaasdaadanaavnasaaSTAAASLGERtpEGFVAKIWTHAQKAARELGVDPRALVAQAALETGWGRRGI--G 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 217 KGESSNNLFNIKADRrWQGEKAAVSTLEYEQGTAVRQKADFRVYDSFEQSFNDFVSFISDNDRYSQARKMAANPGEFIKA 296
Cdd:PRK12711 257 NGGDSNNLFGIKATG-WNGDKVTTGTHEYVNGVKTTETADFRAYGSAEESFADYVRLLKNNSRYQQALQAGTDIKGFARG 335
|
330
....*....|....*.
gi 1098557517 297 LAEAGYATDPQYANKV 312
Cdd:PRK12711 336 LQQAGYATDPGYAAKI 351
|
|
| FlgJ1 |
COG3951 |
Rod binding protein domain [Cell motility]; |
5-105 |
3.51e-30 |
|
Rod binding protein domain [Cell motility];
Pssm-ID: 443151 [Multi-domain] Cd Length: 107 Bit Score: 110.78 E-value: 3.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 5 ADASQFLDLGGLDKLRAQAQQDQKAALKEVAQQFEGIFVQMLMKSMRDANaifESDSPMNSQYTKFYEQMHDQQMSVELS 84
Cdd:COG3951 7 LSSSLALDAQSLNALKAAAKADDDAALKEAAQQFEALFLQMMLKSMRKAV---PEDGLFGSQAEDMFRDMLDQQLAKELA 83
|
90 100
....*....|....*....|.
gi 1098557517 85 SKGMLGLADLMVQQLSPENSG 105
Cdd:COG3951 84 KGGGLGLADMIYRQLSRQQEA 104
|
|
| LYZ2 |
smart00047 |
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes. |
168-316 |
4.31e-26 |
|
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
Pssm-ID: 214488 [Multi-domain] Cd Length: 147 Bit Score: 101.36 E-value: 4.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 168 PAIGSQEEFVRQLYPHAKAAADALGTQPEVLLAQSALETGWGQKMVRGhkgeSSNNLFNIKADrrWQGEKAAVSTLEYEQ 247
Cdd:smart00047 3 LAGGSTLEFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLAK----KYNNLFGIKGA--YDGRPVRMGTLEYLN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1098557517 248 GTAVRQKADFRVYdsFEQSFNDFVSFISDNDRYSqarKMAANPgefiKALAEAGYATDPQYANKVMKVL 316
Cdd:smart00047 77 GGWVTVKAAFRGY--FGEKFIDYAYVLRGQNPLY---KKRWGS----NALQTAGYATDPDYAKKLIRII 136
|
|
| sporang_Gsm |
NF038016 |
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ... |
160-317 |
5.06e-23 |
|
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: 97.12 E-value: 5.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 160 LPSWRQARPAI--GSQEEFVRQLYPHAKAAADALGTQPEVLLAQSALETGWGqkmvRGHKGESSNNLFNIKAdRRWQGEK 237
Cdd:NF038016 145 LPWCGQDPPTVprGTPAQFIAAVAPPAQQSQRATGVPASVTIAQAILESGWG----RSGLTREDHNYFGIKC-FGSPGPI 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 238 A----AVSTLEYEQ-GTAVRQKADFRVYDSFEQSFNDFVSFISDNDRYSQARKMAANPGEFIKALAEAGYATDPQYANKV 312
Cdd:NF038016 220 AvgcrSYATFECSPtGGCFDTTATFRAYASAADSFRDHGRFLSVNSRYAPAFAYTDDPDQFAREIHKAGYATDPTYADKL 299
|
....*
gi 1098557517 313 MKVLD 317
Cdd:NF038016 300 IGLMK 304
|
|
| Glucosaminidase |
pfam01832 |
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ... |
182-270 |
2.76e-18 |
|
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: 78.38 E-value: 2.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 182 PHAKAAADALGTQPEVLLAQSALETGWGQkmvrGHKGESSNNLFNIKAdrRWQGeKAAVSTLEYeqgtavRQKADFRVYD 261
Cdd:pfam01832 2 PAAIEAAKKYGIPASVLLAQAALESGWGT----SRLAKESNNLFGIKA--SWKG-KVAYDTDEV------TVAARFRKYD 68
|
....*....
gi 1098557517 262 SFEQSFNDF 270
Cdd:pfam01832 69 SVEESIRDY 77
|
|
| flgJ |
PRK12708 |
peptidoglycan hydrolase; Reviewed |
31-101 |
2.71e-13 |
|
peptidoglycan hydrolase; Reviewed
Pssm-ID: 139168 [Multi-domain] Cd Length: 134 Bit Score: 66.02 E-value: 2.71e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1098557517 31 LKEVAQQFEGIFVQMLMKSMRDA-NAIFESDSPMNSQYTKFYEQMHDQQMSVELSSKGMLGLADLMVQQLSP 101
Cdd:PRK12708 28 LKLAAQQFEAQFLQTVLKQMRSAsDVMADEDDPFNSKNQGMYRDFYDAELASRLSSQRSMGLAEVMIKQLSS 99
|
|
| Rod-binding |
pfam10135 |
Rod binding protein; Members of this family are involved in the assembly of the prokaryotic ... |
48-98 |
1.73e-10 |
|
Rod binding protein; Members of this family are involved in the assembly of the prokaryotic flagellar rod.
Pssm-ID: 431078 [Multi-domain] Cd Length: 50 Bit Score: 55.68 E-value: 1.73e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1098557517 48 KSMRDAnaIFESDSPMN-SQYTKFYEQMHDQQMSVELSSKGMLGLADLMVQQ 98
Cdd:pfam10135 1 KSMRKT--VPKEDGLFDgSEAEDMFRDMLDQQLAKQLAKGGGLGLADMLYRQ 50
|
|
| PRK08581 |
PRK08581 |
amidase domain-containing protein; |
197-311 |
1.30e-09 |
|
amidase domain-containing protein;
Pssm-ID: 236304 [Multi-domain] Cd Length: 619 Bit Score: 59.42 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 197 VLLAQSALETGWGQKMVrghkGESSN-NLFNIKADrrWQGEKAAVSTLEYEQGTAVRQKADFRVYDSFEQSFNDFVSFIS 275
Cdd:PRK08581 344 VMIAQAILESDSGQSAL----AKSPNhNLFGIKGA--YEGNSVSFNTLEADGNQLYSINAGFRKYPSTKESLEDYADLIK 417
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1098557517 276 -----DNDRYSQARKM-AANPGEFIKALAEAgYATDPQYANK 311
Cdd:PRK08581 418 ngidgNSTIYKPTWKSeAKSYKDATSHLSKT-YATDPNYAKK 458
|
|
| PRK06347 |
PRK06347 |
1,4-beta-N-acetylmuramoylhydrolase; |
197-318 |
1.56e-07 |
|
1,4-beta-N-acetylmuramoylhydrolase;
Pssm-ID: 180536 [Multi-domain] Cd Length: 592 Bit Score: 52.77 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098557517 197 VLLAQSALETGWGQKMVrghkGESSN-NLFNIKAdrRWQGEKAAVSTLEYE-QGTAVRQKADFRVYDSFEQSFNDFVSFI 274
Cdd:PRK06347 174 VMIAQAILESAYGTSEL----GSAPNyNLFGIKG--AYNGQSYTKQTLEDDgKGNYYTITAKFRKYPSYHQSLEDYAQVI 247
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1098557517 275 S-----DNDRYSQARKMAANP-GEFIKALAeAGYATDPQYANKVMKVLDT 318
Cdd:PRK06347 248 RkgpswNPNYYSKVWKSNTTSyKDATKALT-GTYATDTAYATKLNDLISR 296
|
|
| |
