|
Name |
Accession |
Description |
Interval |
E-value |
| flgJ |
PRK05684 |
flagellar assembly peptidoglycan hydrolase FlgJ; |
2-317 |
0e+00 |
|
flagellar assembly peptidoglycan hydrolase FlgJ;
Pssm-ID: 235559 [Multi-domain] Cd Length: 312 Bit Score: 515.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 2 LTDSKLLSSAAFDAQSLNDLKAKVSKDPNGNLKSVARQMEGMFVQMMLKSMREALPKDGLFSSDQTRLYTSMYDQQIAQQ 81
Cdd:PRK05684 1 MSDSLSDSGAAYDLQSLNSLKAKAGKDPKANLRAVAQQFEGMFVQMMLKSMRDANPKDGLMNSQQTKLYTSMYDQQIAQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 82 MTAGKGLGLADMMVKQMggeaaSTEQPAAAADNVAQVPMKFDIDTMNSYRNQAITQIVRQAMPKAP-TNEEPLSGDSKDF 160
Cdd:PRK05684 81 LSAGGGLGLADMMVKQL-----SPEQSPAPEESAGAVPMKFDLETVQSYQNQALAQLVRKAIPQPPlASDKPLFGSSDDF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 161 LAQLSLPAKLASQQSGVPHHLILAQAALESGWGQRQIRKENGEPSFNIFGVKATSSWKGPVTEITTTEYENGEAKKVKAK 240
Cdd:PRK05684 156 VARLSPPAQKAAQQSGVPHHLLLAQAALESGWGQREIRTADGSPSHNLFGIKADGSWKGPVTEITTTEYENGVAVKVKAA 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1875951882 241 FRVYGSYLEALSDYVGMLTRNPRYAAVTTAASAEEGAQALQNAGYATDPNYARKLTSMIQQMKSLGEKVSKAYNQDI 317
Cdd:PRK05684 236 FRVYDSYLESFNDYVSLLTNNPRYAAVTQAASPEQFARALQDAGYATDPNYARKLVSVIQQMKSMGEKVSKAYSHDL 312
|
|
| flagell_FlgJ |
TIGR02541 |
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ... |
11-303 |
1.05e-139 |
|
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: 396.91 E-value: 1.05e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 11 AAFDAQSLNDLKAKVSKDPNGNLKSVARQMEGMFVQMMLKSMREALPKDGLFSSDQTRLYTSMYDQQIAQQMTAGKGLGL 90
Cdd:TIGR02541 1 LAHDAQSLDSLKAKAVKDPKEQEKEAARQFEALFLNMMLKSMREATPKDGLFDSQQTRFYTQMLDQQMAQQLSANGGIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 91 ADMMVKQMggEAASTEQPAAAADNVA---QVPMKFDIDTMNSYRNQAITQIVRQAMPKAPTNEEPLSGDSKDFLAQLSLP 167
Cdd:TIGR02541 81 ADMIVAQL--TKGQGNEPSEGAARGAapsPLVYRPRLDPKPRRIVKALIESVELSRPRGRSHAESVPGHPKSFVNSMLPH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 168 AKLASQQSGVPHHLILAQAALESGWGQRQIRKENGEPSFNIFGVKATSSWKGPVTEITTTEYENGEAKKVKAKFRVYGSY 247
Cdd:TIGR02541 159 ARKAAQQLGVPPHLILAQAALESGWGQRQIRNADGSPSYNLFGIKASGSWQGKVVTTMTTEYVDGVAQKLTAKFRSYSSY 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1875951882 248 LEALSDYVGMLTRNPRYAAVTTAASAEEGAQALQNAGYATDPNYARKLTSMIQQMK 303
Cdd:TIGR02541 239 EEAFSDYARLLNNNPRYEAVLQQRSAESFARGLQRAGYATDPRYARKLLQVIQSLA 294
|
|
| FlgJ |
COG1705 |
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ... |
30-303 |
3.75e-67 |
|
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];
Pssm-ID: 441311 [Multi-domain] Cd Length: 276 Bit Score: 211.75 E-value: 3.75e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 30 NGNLKSVARQMEGMFVQMMLKSMREALPKDGLFSSDQTRLYTSMYDQQIAQQMTAGKGLGLADMMVKQMGGEAASTEQPA 109
Cdd:COG1705 2 ASLDSSSASSSAGAAAQAKAAAQAAASAMASLEAAASSALSSSTSSSSKGASSSQSLEGLASALGGGASALSSAAALALK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 110 AAADNVAQVPMKFDIDTMNSYRNQAITQIVRQAMPKAPTNEEPLSGDSKDFLAQLSLPAKLASQQSGVPHHLILAQAALE 189
Cdd:COG1705 82 SAAKSATEAGGGLASANAAATSAAALAASLSGAAALAASATAAASASPEEFIAKIAPAAQKAAKKYGVPASVLIAQAALE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 190 SGWGQRQIrkeNGEPSFNIFGVKATSSWKGPVTEITTTEYENGEAKKVKAKFRVYGSYLEALSDYVGMLTRNPRYA-AVT 268
Cdd:COG1705 162 SGWGKSEL---DGSPSNNLFGIKAGGSWQGKSVEVTTTEYVNGKAVKIKARFRAYDSYAESFRDYARLLKNNPRYAgALA 238
|
250 260 270
....*....|....*....|....*....|....*
gi 1875951882 269 TAASAEEGAQALQNAGYATDPNYARKLTSMIQQMK 303
Cdd:COG1705 239 NAKDYEAFAKALQKAGYATDPKYADKLISIIESYN 273
|
|
| LYZ2 |
smart00047 |
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes. |
151-306 |
7.39e-43 |
|
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
Pssm-ID: 214488 [Multi-domain] Cd Length: 147 Bit Score: 144.89 E-value: 7.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 151 EPLSGDSKDFLAQLSLPAKLASQQSGVPHHLILAQAALESGWGQRQIRKengePSFNIFGVKAtsSWKGPVTEITTTEYE 230
Cdd:smart00047 2 LLAGGSTLEFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLAK----KYNNLFGIKG--AYDGRPVRMGTLEYL 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1875951882 231 NGEAKKVKAKFRVYGSYLEALSDYVgMLTRNPRYAAVTtaasaeeGAQALQNAGYATDPNYARKLTSMIQQMKSLG 306
Cdd:smart00047 76 NGGWVTVKAAFRGYFGEKFIDYAYV-LRGQNPLYKKRW-------GSNALQTAGYATDPDYAKKLIRIIALYDEKL 143
|
|
| sporang_Gsm |
NF038016 |
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ... |
141-301 |
1.75e-20 |
|
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: 89.80 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 141 QAMPKAPtneeplSGDSKDFLAQLSLPAKLASQQSGVPHHLILAQAALESGWGQRQI-RKENgepsfNIFGVKATSSwKG 219
Cdd:NF038016 150 QDPPTVP------RGTPAQFIAAVAPPAQQSQRATGVPASVTIAQAILESGWGRSGLtREDH-----NYFGIKCFGS-PG 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 220 PVT----EITTTEYE-NGEAKKVKAKFRVYGSYLEALSDYVGMLTRNPRYA-AVTTAASAEEGAQALQNAGYATDPNYAR 293
Cdd:NF038016 218 PIAvgcrSYATFECSpTGGCFDTTATFRAYASAADSFRDHGRFLSVNSRYApAFAYTDDPDQFAREIHKAGYATDPTYAD 297
|
....*...
gi 1875951882 294 KLTSMIQQ 301
Cdd:NF038016 298 KLIGLMKQ 305
|
|
| Glucosaminidase |
pfam01832 |
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ... |
168-303 |
1.19e-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: 79.15 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 168 AKLASQQSGVPHHLILAQAALESGWGQRQIRKEngepSFNIFGVKAtsSWKGPVTeITTTEYengeakKVKAKFRVYGSY 247
Cdd:pfam01832 4 AIEAAKKYGIPASVLLAQAALESGWGTSRLAKE----SNNLFGIKA--SWKGKVA-YDTDEV------TVAARFRKYDSV 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1875951882 248 LEALSDYvgmltrnpryaavttaasaeegaqalqnagyatdpnYARKLTSMIQQMK 303
Cdd:pfam01832 71 EESIRDY------------------------------------YAEKLIAIIERYN 90
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| flgJ |
PRK05684 |
flagellar assembly peptidoglycan hydrolase FlgJ; |
2-317 |
0e+00 |
|
flagellar assembly peptidoglycan hydrolase FlgJ;
Pssm-ID: 235559 [Multi-domain] Cd Length: 312 Bit Score: 515.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 2 LTDSKLLSSAAFDAQSLNDLKAKVSKDPNGNLKSVARQMEGMFVQMMLKSMREALPKDGLFSSDQTRLYTSMYDQQIAQQ 81
Cdd:PRK05684 1 MSDSLSDSGAAYDLQSLNSLKAKAGKDPKANLRAVAQQFEGMFVQMMLKSMRDANPKDGLMNSQQTKLYTSMYDQQIAQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 82 MTAGKGLGLADMMVKQMggeaaSTEQPAAAADNVAQVPMKFDIDTMNSYRNQAITQIVRQAMPKAP-TNEEPLSGDSKDF 160
Cdd:PRK05684 81 LSAGGGLGLADMMVKQL-----SPEQSPAPEESAGAVPMKFDLETVQSYQNQALAQLVRKAIPQPPlASDKPLFGSSDDF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 161 LAQLSLPAKLASQQSGVPHHLILAQAALESGWGQRQIRKENGEPSFNIFGVKATSSWKGPVTEITTTEYENGEAKKVKAK 240
Cdd:PRK05684 156 VARLSPPAQKAAQQSGVPHHLLLAQAALESGWGQREIRTADGSPSHNLFGIKADGSWKGPVTEITTTEYENGVAVKVKAA 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1875951882 241 FRVYGSYLEALSDYVGMLTRNPRYAAVTTAASAEEGAQALQNAGYATDPNYARKLTSMIQQMKSLGEKVSKAYNQDI 317
Cdd:PRK05684 236 FRVYDSYLESFNDYVSLLTNNPRYAAVTQAASPEQFARALQDAGYATDPNYARKLVSVIQQMKSMGEKVSKAYSHDL 312
|
|
| flagell_FlgJ |
TIGR02541 |
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ... |
11-303 |
1.05e-139 |
|
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: 396.91 E-value: 1.05e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 11 AAFDAQSLNDLKAKVSKDPNGNLKSVARQMEGMFVQMMLKSMREALPKDGLFSSDQTRLYTSMYDQQIAQQMTAGKGLGL 90
Cdd:TIGR02541 1 LAHDAQSLDSLKAKAVKDPKEQEKEAARQFEALFLNMMLKSMREATPKDGLFDSQQTRFYTQMLDQQMAQQLSANGGIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 91 ADMMVKQMggEAASTEQPAAAADNVA---QVPMKFDIDTMNSYRNQAITQIVRQAMPKAPTNEEPLSGDSKDFLAQLSLP 167
Cdd:TIGR02541 81 ADMIVAQL--TKGQGNEPSEGAARGAapsPLVYRPRLDPKPRRIVKALIESVELSRPRGRSHAESVPGHPKSFVNSMLPH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 168 AKLASQQSGVPHHLILAQAALESGWGQRQIRKENGEPSFNIFGVKATSSWKGPVTEITTTEYENGEAKKVKAKFRVYGSY 247
Cdd:TIGR02541 159 ARKAAQQLGVPPHLILAQAALESGWGQRQIRNADGSPSYNLFGIKASGSWQGKVVTTMTTEYVDGVAQKLTAKFRSYSSY 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1875951882 248 LEALSDYVGMLTRNPRYAAVTTAASAEEGAQALQNAGYATDPNYARKLTSMIQQMK 303
Cdd:TIGR02541 239 EEAFSDYARLLNNNPRYEAVLQQRSAESFARGLQRAGYATDPRYARKLLQVIQSLA 294
|
|
| flgJ |
PRK12712 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
12-304 |
3.40e-90 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 139172 [Multi-domain] Cd Length: 344 Bit Score: 273.03 E-value: 3.40e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 12 AFDAQSLNDLKAKVSKDPN-GNLKSVARQMEGMFVQMMLKSMREALPKDGLFSSDQTRLYTSMYDQQIAQQMTAgKGLGL 90
Cdd:PRK12712 17 ALDTQGFEALKHSARGGADaGTLQAAARQFEAVFTQMVLKSMRDATPQDGLFDNEQSKLYMSMMDQQLAQQMSS-RGIGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 91 ADMMVKQM----------GGEAASTEQPAAAADnvAQVPMKFD----------------IDTMNSYRNQAITQIVRQAMP 144
Cdd:PRK12712 96 ADVMVRQLaratgtqmppGMNAAGGATAGSAAD--AEMARLLDgrgagaadadagdlpaIGTIVPGQAWNPTAGLRQYQP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 145 KA-------PTNEEPLSGDSKD----FLAQLSLPAKLASQQSGVPHHLILAQAALESGWGQRQIRKENGEPSFNIFGVKA 213
Cdd:PRK12712 174 QAyadqgqgEDRLGRLPDDAPAhvsaFVARMAGPAEAASRASGVPARLIVGQAALESGWGRREITHADGSTTFNVFGIKA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 214 TSSWKGPVTEITTTEYENGEAKKVKAKFRVYGSYLEALSDYVGMLTRNPRYAAVTTAASAEEGAQALQNAGYATDPNYAR 293
Cdd:PRK12712 254 GANWKGRVAEVTTTEYVDGQPQKVRARFRAYGSYDEACADYARLLTSNPRYAGVVSAASADEAAHGLQRAGYATDPAYGH 333
|
330
....*....|.
gi 1875951882 294 KLTSMIQQMKS 304
Cdd:PRK12712 334 KLVKIMKKVSA 344
|
|
| flgJ |
PRK12709 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
12-302 |
2.06e-82 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 237179 [Multi-domain] Cd Length: 320 Bit Score: 252.15 E-value: 2.06e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 12 AFDAQSLNDLKAKVSKDPNGNLKSVARQMEGMFVQMMLKSMREALPKDGLFSSDQTRLYTSMYDQQIAQQMTAgKGLGLA 91
Cdd:PRK12709 15 ALDVQGFDALRAQAKASPQAGAKMVAGQFDAMFTQMMLKSMRDATPSDGLFDSHTSKMYTSMLDQQLAQQMSS-KGIGVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 92 DMMVKQMGGEAAstEQPAAAADNVAQVPMKFDIDTMNSYRNQAITQivrqAMPKAPTNEE---------------PLSGD 156
Cdd:PRK12709 94 DALMKQLLRNAG--VAAGAQGDAGAGGMGGLGGNEGGLAAMNALAK----AYANAANNGAlagtrgysagsaltpPLKGN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 157 SKD-----FLAQLSLPAKLASQQSGVPHHLILAQAALESGWGQRQIRKENGEPSFNIFGVKATSSWKGPVTEITTTEYEN 231
Cdd:PRK12709 168 GGSpdadaFVDKLAAPAQAASAATGIPARFIVGQAALESGWGKREIRGADGSTSYNVFGIKATKGWTGRTVSAVTTEYVN 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1875951882 232 GEAKKVKAKFRVYGSYLEALSDYVGMLTRNPRYAAVTTAASAEEG-AQALQNAGYATDPNYARKLTSMIQQM 302
Cdd:PRK12709 248 GKPRRVVAKFRAYDSYEHAMTDYANLLKNNPRYAGVLNASRSVEGfAHGMQKAGYATDPHYAKKLISIMQQI 319
|
|
| flgJ |
PRK12713 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
11-304 |
2.69e-82 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 139173 [Multi-domain] Cd Length: 339 Bit Score: 252.74 E-value: 2.69e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 11 AAFDAQSLNDLKAKVSKDPNG--NLKSVARQMEGMFVQMMLKSMREALPKDGLFSSDQTRLYTSMYDQQIAQQMtAGKGL 88
Cdd:PRK12713 15 SVFDLGRLADLKRDAVKAPDGqrQQTEVARQFEALFLQMMLKRMREATPKEGLFDSQQTEMLQGMADEQLALQL-ASPGI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 89 GLADMMVKQMG-GEAASTEQPAAAADNVA-------QVPMKFDIDTMNSYRNQ---------AITQIVRQAMP--KAPTN 149
Cdd:PRK12713 94 GLAQALLGQMQqGQPPVPAAAAAGGDAAAaralagtAAPAPLVRDLRGNYVQPdpaprrevnALLDVLRSNRArdRAMAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 150 EEPLSGDSKDFLAQLSLPAKLASQQSGVPHHLILAQAALESGWGQRQIRKENGEPSFNIFGVKATSSWKGPVTEITTTEY 229
Cdd:PRK12713 174 AEGAPSHVVDFVSRMSRAANVAAQQSGVPARLILGQAALESGWGRRELRHEDGSTSYNLFGIKAGASWKGKVVNVMTTEY 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1875951882 230 ENGEAKKVKAKFRVYGSYLEALSDYVGMLTRNPRYAAVTTAASAEEGAQALQNAGYATDPNYARKLTSMIQQMKS 304
Cdd:PRK12713 254 VDGVAQKLVQPFRAYSSYEESFSDYARLIGNSPRYEAVTQAGNEIEAARRIQEAGYATDPRYAEKLISIMGQLRT 328
|
|
| FlgJ |
COG1705 |
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ... |
30-303 |
3.75e-67 |
|
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];
Pssm-ID: 441311 [Multi-domain] Cd Length: 276 Bit Score: 211.75 E-value: 3.75e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 30 NGNLKSVARQMEGMFVQMMLKSMREALPKDGLFSSDQTRLYTSMYDQQIAQQMTAGKGLGLADMMVKQMGGEAASTEQPA 109
Cdd:COG1705 2 ASLDSSSASSSAGAAAQAKAAAQAAASAMASLEAAASSALSSSTSSSSKGASSSQSLEGLASALGGGASALSSAAALALK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 110 AAADNVAQVPMKFDIDTMNSYRNQAITQIVRQAMPKAPTNEEPLSGDSKDFLAQLSLPAKLASQQSGVPHHLILAQAALE 189
Cdd:COG1705 82 SAAKSATEAGGGLASANAAATSAAALAASLSGAAALAASATAAASASPEEFIAKIAPAAQKAAKKYGVPASVLIAQAALE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 190 SGWGQRQIrkeNGEPSFNIFGVKATSSWKGPVTEITTTEYENGEAKKVKAKFRVYGSYLEALSDYVGMLTRNPRYA-AVT 268
Cdd:COG1705 162 SGWGKSEL---DGSPSNNLFGIKAGGSWQGKSVEVTTTEYVNGKAVKIKARFRAYDSYAESFRDYARLLKNNPRYAgALA 238
|
250 260 270
....*....|....*....|....*....|....*
gi 1875951882 269 TAASAEEGAQALQNAGYATDPNYARKLTSMIQQMK 303
Cdd:COG1705 239 NAKDYEAFAKALQKAGYATDPKYADKLISIIESYN 273
|
|
| flgJ |
PRK12711 |
flagellar assembly peptidoglycan hydrolase FlgJ; |
20-298 |
1.17e-44 |
|
flagellar assembly peptidoglycan hydrolase FlgJ;
Pssm-ID: 237180 [Multi-domain] Cd Length: 392 Bit Score: 156.66 E-value: 1.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 20 DLKAKVSKDPnGNLKSVARQMEGMFVQMMLKSMREALPKDGLFSSdQTRLYTSMYDQQIAQQMTAGKGLGLADMMVKQMG 99
Cdd:PRK12711 9 DLNPSTKADP-AKIDKVSRQLEGQFAQMLVKSMRDASSGDPMFPG-ENQMFREMYDQQMAKALTDGKGLGLSAMISKQLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 100 GEAA-----STEQPAAAADNVAQVPMKFDIDTMNSYRNQAITQIVRQAMPKAPTNEEPLSG------------------- 155
Cdd:PRK12711 87 GDTGgpalnTALNTAKAAKAYSLVAGKRDASLPLPARDGAAAGITTSSVAAAALSAGNLSGigmsqvldliagrtgagea 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 156 -----------------------DSKD------------------------FLAQLSLPAKLASQQSGVPHHLILAQAAL 188
Cdd:PRK12711 167 gsddaaalswpsandrwsdvaasDAADanaavnasaastaaaslgertpegFVAKIWTHAQKAARELGVDPRALVAQAAL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 189 ESGWGQRQIrkENGEPSFNIFGVKATSsWKGPVTEITTTEYENGEAKKVKAKFRVYGSYLEALSDYVGMLTRNPRYAAVT 268
Cdd:PRK12711 247 ETGWGRRGI--GNGGDSNNLFGIKATG-WNGDKVTTGTHEYVNGVKTTETADFRAYGSAEESFADYVRLLKNNSRYQQAL 323
|
330 340 350
....*....|....*....|....*....|.
gi 1875951882 269 TAASAEEG-AQALQNAGYATDPNYARKLTSM 298
Cdd:PRK12711 324 QAGTDIKGfARGLQQAGYATDPGYAAKIAAI 354
|
|
| LYZ2 |
smart00047 |
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes. |
151-306 |
7.39e-43 |
|
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
Pssm-ID: 214488 [Multi-domain] Cd Length: 147 Bit Score: 144.89 E-value: 7.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 151 EPLSGDSKDFLAQLSLPAKLASQQSGVPHHLILAQAALESGWGQRQIRKengePSFNIFGVKAtsSWKGPVTEITTTEYE 230
Cdd:smart00047 2 LLAGGSTLEFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLAK----KYNNLFGIKG--AYDGRPVRMGTLEYL 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1875951882 231 NGEAKKVKAKFRVYGSYLEALSDYVgMLTRNPRYAAVTtaasaeeGAQALQNAGYATDPNYARKLTSMIQQMKSLG 306
Cdd:smart00047 76 NGGWVTVKAAFRGYFGEKFIDYAYV-LRGQNPLYKKRW-------GSNALQTAGYATDPDYAKKLIRIIALYDEKL 143
|
|
| FlgJ1 |
COG3951 |
Rod binding protein domain [Cell motility]; |
1-107 |
3.77e-41 |
|
Rod binding protein domain [Cell motility];
Pssm-ID: 443151 [Multi-domain] Cd Length: 107 Bit Score: 138.90 E-value: 3.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 1 MLTDSKLLSSAAFDAQSLNDLKAKVSKDPNGNLKSVARQMEGMFVQMMLKSMREALPKDGLFSSDQTRLYTSMYDQQIAQ 80
Cdd:COG3951 1 MSISSSLSSSLALDAQSLNALKAAAKADDDAALKEAAQQFEALFLQMMLKSMRKAVPEDGLFGSQAEDMFRDMLDQQLAK 80
|
90 100
....*....|....*....|....*..
gi 1875951882 81 QMTAGKGLGLADMMVKQMGGEAASTEQ 107
Cdd:COG3951 81 ELAKGGGLGLADMIYRQLSRQQEAAAA 107
|
|
| flgJ |
PRK12710 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
9-298 |
1.78e-34 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 139170 [Multi-domain] Cd Length: 291 Bit Score: 127.22 E-value: 1.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 9 SSAAFDAQSLNDLKAKVSKDPNGNLKSVARQMEGMFVQMMLKSMREA---LPKDGLFSSDQTRLYTSMYDQQIAQQMTAG 85
Cdd:PRK12710 5 SIATSDFQGLNELKVQAKNNAKEALPEVAKQFEGIFLQSMLKSMRMGqhfLDESSPFSGKNEATFQEMLDTQYASTIAES 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 86 KGLGLADMMVKQM----GGEAASTEQPAAAADNVaqvpmkfdidtmnsyrnqaitqivrqampKAPTNEEPLSGdSKDFL 161
Cdd:PRK12710 85 KGIGLAALLAKQLensvGDKANNPVNSSTEVSNT-----------------------------KVTNSEESLSV-VDDFV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 162 AQLSLPAKLASQQSGVPHHLILAQAALESGWGQRQIRKENGEPSFNIFGVKATSSWKGPVTEITTTEYENGEAKKVKAKF 241
Cdd:PRK12710 135 KSVWPTAKQAASLIGLDPKLLVAQAALETGWGKFVTRDADGSSSNNLFNIKTGSHSEVESIQVKTTEYIADTPIKINASF 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1875951882 242 RVYGSYLEALSDYVGMLTRNPRYA-AVTTAASAEEGAQALQNAGYATDPNYARKLTSM 298
Cdd:PRK12710 215 RKYPSIEHSFHDYVSLIKGSERYQmALANAENPEIYVSELNKAGYATDPNYSNKILSI 272
|
|
| sporang_Gsm |
NF038016 |
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ... |
141-301 |
1.75e-20 |
|
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: 89.80 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 141 QAMPKAPtneeplSGDSKDFLAQLSLPAKLASQQSGVPHHLILAQAALESGWGQRQI-RKENgepsfNIFGVKATSSwKG 219
Cdd:NF038016 150 QDPPTVP------RGTPAQFIAAVAPPAQQSQRATGVPASVTIAQAILESGWGRSGLtREDH-----NYFGIKCFGS-PG 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 220 PVT----EITTTEYE-NGEAKKVKAKFRVYGSYLEALSDYVGMLTRNPRYA-AVTTAASAEEGAQALQNAGYATDPNYAR 293
Cdd:NF038016 218 PIAvgcrSYATFECSpTGGCFDTTATFRAYASAADSFRDHGRFLSVNSRYApAFAYTDDPDQFAREIHKAGYATDPTYAD 297
|
....*...
gi 1875951882 294 KLTSMIQQ 301
Cdd:NF038016 298 KLIGLMKQ 305
|
|
| Glucosaminidase |
pfam01832 |
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ... |
168-303 |
1.19e-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: 79.15 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 168 AKLASQQSGVPHHLILAQAALESGWGQRQIRKEngepSFNIFGVKAtsSWKGPVTeITTTEYengeakKVKAKFRVYGSY 247
Cdd:pfam01832 4 AIEAAKKYGIPASVLLAQAALESGWGTSRLAKE----SNNLFGIKA--SWKGKVA-YDTDEV------TVAARFRKYDSV 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1875951882 248 LEALSDYvgmltrnpryaavttaasaeegaqalqnagyatdpnYARKLTSMIQQMK 303
Cdd:pfam01832 71 EESIRDY------------------------------------YAEKLIAIIERYN 90
|
|
| PRK08581 |
PRK08581 |
amidase domain-containing protein; |
154-300 |
1.27e-18 |
|
amidase domain-containing protein;
Pssm-ID: 236304 [Multi-domain] Cd Length: 619 Bit Score: 86.38 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 154 SGDSKDFLAQLSLPAKLASQQSGVPHHLILAQAALESGWGQRQIRKEngePSFNIFGVKAtsSWKGPVTEITTTEYENGE 233
Cdd:PRK08581 317 SKDTRQFIKSIAKDAHRIGQDNDIYASVMIAQAILESDSGQSALAKS---PNHNLFGIKG--AYEGNSVSFNTLEADGNQ 391
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1875951882 234 AKKVKAKFRVYGSYLEALSDYVGML----TRNPRYAAVT---TAASAEEGAQALQNAgYATDPNYARKLTSMIQ 300
Cdd:PRK08581 392 LYSINAGFRKYPSTKESLEDYADLIkngiDGNSTIYKPTwksEAKSYKDATSHLSKT-YATDPNYAKKLNSIIK 464
|
|
| Rod-binding |
pfam10135 |
Rod binding protein; Members of this family are involved in the assembly of the prokaryotic ... |
50-97 |
4.75e-14 |
|
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: 65.31 E-value: 4.75e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1875951882 50 KSMREALPK-DGLF-SSDQTRLYTSMYDQQIAQQMTAGKGLGLADMMVKQ 97
Cdd:pfam10135 1 KSMRKTVPKeDGLFdGSEAEDMFRDMLDQQLAKQLAKGGGLGLADMLYRQ 50
|
|
| flgJ |
PRK12708 |
peptidoglycan hydrolase; Reviewed |
31-110 |
1.78e-11 |
|
peptidoglycan hydrolase; Reviewed
Pssm-ID: 139168 [Multi-domain] Cd Length: 134 Bit Score: 61.01 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 31 GNLKSVARQMEGMFVQMMLKSMREA----LPKDGLFSSDQTRLYTSMYDQQIAQQMTAGKGLGLADMMVKQMGGEAASTE 106
Cdd:PRK12708 26 GALKLAAQQFEAQFLQTVLKQMRSAsdvmADEDDPFNSKNQGMYRDFYDAELASRLSSQRSMGLAEVMIKQLSSKLKSAP 105
|
....
gi 1875951882 107 QPAA 110
Cdd:PRK12708 106 EVVA 109
|
|
| PRK06347 |
PRK06347 |
1,4-beta-N-acetylmuramoylhydrolase; |
181-299 |
5.76e-10 |
|
1,4-beta-N-acetylmuramoylhydrolase;
Pssm-ID: 180536 [Multi-domain] Cd Length: 592 Bit Score: 60.09 E-value: 5.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 181 LILAQAALESGWGQRQIrkeNGEPSFNIFGVKATSSWKGpVTEITTTEYENGEAKKVKAKFRVYGSYLEALSDYVGMLTR 260
Cdd:PRK06347 174 VMIAQAILESAYGTSEL---GSAPNYNLFGIKGAYNGQS-YTKQTLEDDGKGNYYTITAKFRKYPSYHQSLEDYAQVIRK 249
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1875951882 261 NPR-----YAAV--TTAASAEEGAQALQNAgYATDPNYARKLTSMI 299
Cdd:PRK06347 250 GPSwnpnyYSKVwkSNTTSYKDATKALTGT-YATDTAYATKLNDLI 294
|
|
| PRK10356 |
PRK10356 |
protein bax; |
169-305 |
4.04e-04 |
|
protein bax;
Pssm-ID: 182404 Cd Length: 274 Bit Score: 41.40 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875951882 169 KLASQQSGVPHHLILAQAALESGWGQRQIRKENGepsfNIFGVKATsswkgpvteittteyeNGEAKKVKAK---FRVYG 245
Cdd:PRK10356 141 TLLERVDIIPTSMVATMAAAESGWGTSKLARNNN----NLFGMKCM----------------KGRCTNAPGKvkgYSQFS 200
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1875951882 246 SYLEALSDYVGMLTRNPRYAAVTTAASAEEGAQALQNA--------GYAT-DPNYARKLTSMIQQMKSL 305
Cdd:PRK10356 201 SVKESVSAYVTNLNTHPAYSSFRKSRAQLRKADQEVTAtamihklkGYSTkGSSYNNYLFAMYQDNQRL 269
|
|
| Bax |
COG2992 |
Uncharacterized FlgJ-related protein [General function prediction only]; |
150-210 |
3.10e-03 |
|
Uncharacterized FlgJ-related protein [General function prediction only];
Pssm-ID: 442231 Cd Length: 253 Bit Score: 38.37 E-value: 3.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1875951882 150 EEPLSGDSKDFLAQLS----LPAKLASQQS---------GVPHHLILAQAALESGWGQ-RQIRKENgepsfNIFG 210
Cdd:COG2992 79 LKSLSPEEQAWLSALAkkyrVKNDLLDEADleellkrvdIIPPSLVLAQAANESGWGTsRFAREGN-----NLFG 148
|
|
| |
