|
Name |
Accession |
Description |
Interval |
E-value |
| sporang_Gsm |
NF038016 |
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ... |
43-296 |
2.05e-133 |
|
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: 380.63 E-value: 2.05e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 43 LNLRAAATTRSATVGRLANRARVTLVCKVAGEKVKGKVRTSNQWDRTASGGYVSHAYVRSNSSLPTCPAPVVPQVTVASV 122
Cdd:NF038016 1 LNVRSGPATDSAVVGTLANGAKVTVVCKVRGEQIRGTVRTTSQWDRLGSGRYVSHAYVRWSPSLPTCPWCAPKAATVATV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 123 -----------GPYTGPVVLGTVAGG-----------------------------------------------PNGTMTN 144
Cdd:NF038016 81 ttgggalnvraAAGTGAARVGTVANGatvtvecqvwgqevdgtgvwyrlgdgryvsaayvrrpwlpwcgqdppTVPRGTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 145 ADFIAAAVIPAQQSQREFRVPASVTIAQSILESGWGRSGLTVNDKNFFGIKCFtPVPGPISIGCHSYATYEFV-NGHYVA 223
Cdd:NF038016 161 AQFIAAVAPPAQQSQRATGVPASVTIAQAILESGWGRSGLTREDHNYFGIKCF-GSPGPIAVGCRSYATFECSpTGGCFD 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1125233871 224 TTAAFRTYASALDSFRDHGRFLVVNDRYAPAFAYTGNADQFLYQIWKAGYATSPTYVANVQALMHQFNLYQYD 296
Cdd:NF038016 240 TTATFRAYASAADSFRDHGRFLSVNSRYAPAFAYTDDPDQFAREIHKAGYATDPTYADKLIGLMKQYNLYQYD 312
|
|
| FlgJ |
COG1705 |
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ... |
138-294 |
8.25e-51 |
|
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];
Pssm-ID: 441311 [Multi-domain] Cd Length: 276 Bit Score: 168.99 E-value: 8.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 138 PNGTMTNADFIAAAVIPAQQSQREFRVPASVTIAQSILESGWGRSGLT-VNDKNFFGIKCFTPVPGPisigCHSYATYEF 216
Cdd:COG1705 123 AAASASPEEFIAKIAPAAQKAAKKYGVPASVLIAQAALESGWGKSELDgSPSNNLFGIKAGGSWQGK----SVEVTTTEY 198
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1125233871 217 VNGHYVATTAAFRTYASALDSFRDHGRFLVVNDRYAPAFAYTGNADQFLYQIWKAGYATSPTYVANVQALMHQFNLYQ 294
Cdd:COG1705 199 VNGKAVKIKARFRAYDSYAESFRDYARLLKNNPRYAGALANAKDYEAFAKALQKAGYATDPKYADKLISIIESYNLTQ 276
|
|
| flgJ |
PRK05684 |
flagellar assembly peptidoglycan hydrolase FlgJ; |
142-294 |
1.78e-26 |
|
flagellar assembly peptidoglycan hydrolase FlgJ;
Pssm-ID: 235559 [Multi-domain] Cd Length: 312 Bit Score: 105.73 E-value: 1.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 142 MTNADFIAAAVIPAQQSQREFRVPASVTIAQSILESGWGRSG-LTVNDK---NFFGIKCFTPVPGPISigchSYATYEFV 217
Cdd:PRK05684 150 GSSDDFVARLSPPAQKAAQQSGVPHHLLLAQAALESGWGQREiRTADGSpshNLFGIKADGSWKGPVT----EITTTEYE 225
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1125233871 218 NGHYVATTAAFRTYASALDSFRDHGRFLVVNDRYApAFAYTGNADQFLYQIWKAGYATSPTYVANVQALMHQFNLYQ 294
Cdd:PRK05684 226 NGVAVKVKAAFRVYDSYLESFNDYVSLLTNNPRYA-AVTQAASPEQFARALQDAGYATDPNYARKLVSVIQQMKSMG 301
|
|
| flagell_FlgJ |
TIGR02541 |
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ... |
133-289 |
8.99e-25 |
|
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: 100.70 E-value: 8.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 133 TVAGGPNgtmtnaDFIAAAVIPAQQSQREFRVPASVTIAQSILESGWGRSGLTVNDK----NFFGIKCFTPVPGPISigc 208
Cdd:TIGR02541 143 SVPGHPK------SFVNSMLPHARKAAQQLGVPPHLILAQAALESGWGQRQIRNADGspsyNLFGIKASGSWQGKVV--- 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 209 hSYATYEFVNGHYVATTAAFRTYASALDSFRDHGRFLVVNDRYApAFAYTGNADQFLYQIWKAGYATSPTYVANVQALMH 288
Cdd:TIGR02541 214 -TTMTTEYVDGVAQKLTAKFRSYSSYEEAFSDYARLLNNNPRYE-AVLQQRSAESFARGLQRAGYATDPRYARKLLQVIQ 291
|
.
gi 1125233871 289 Q 289
Cdd:TIGR02541 292 S 292
|
|
| Glucosaminidase |
pfam01832 |
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ... |
155-241 |
1.80e-21 |
|
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: 86.47 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 155 AQQSQREFRVPASVTIAQSILESGWGRSGLTVNDKNFFGIKCftpvpgpisigchSYATYEFVNGHYVATTAAFRTYASA 234
Cdd:pfam01832 4 AIEAAKKYGIPASVLLAQAALESGWGTSRLAKESNNLFGIKA-------------SWKGKVAYDTDEVTVAARFRKYDSV 70
|
....*..
gi 1125233871 235 LDSFRDH 241
Cdd:pfam01832 71 EESIRDY 77
|
|
| LYZ2 |
smart00047 |
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes. |
145-296 |
4.55e-20 |
|
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
Pssm-ID: 214488 [Multi-domain] Cd Length: 147 Bit Score: 84.41 E-value: 4.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 145 ADFIAAAVIPAQQSQREFRVPASVTIAQSILESGWGRSGLTVNDKNFFGIKcfTPVPGPISigchSYATYEFVNGHYVAT 224
Cdd:smart00047 9 LEFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLAKKYNNLFGIK--GAYDGRPV----RMGTLEYLNGGWVTV 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1125233871 225 TAAFRTYASAldSFRDHGRFLV-VNDRYAPAFAYTGnadqflyqIWKAGYATSPTYVANVQALMHQFN--LYQYD 296
Cdd:smart00047 83 KAAFRGYFGE--KFIDYAYVLRgQNPLYKKRWGSNA--------LQTAGYATDPDYAKKLIRIIALYDekLKGYD 147
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| sporang_Gsm |
NF038016 |
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ... |
43-296 |
2.05e-133 |
|
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: 380.63 E-value: 2.05e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 43 LNLRAAATTRSATVGRLANRARVTLVCKVAGEKVKGKVRTSNQWDRTASGGYVSHAYVRSNSSLPTCPAPVVPQVTVASV 122
Cdd:NF038016 1 LNVRSGPATDSAVVGTLANGAKVTVVCKVRGEQIRGTVRTTSQWDRLGSGRYVSHAYVRWSPSLPTCPWCAPKAATVATV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 123 -----------GPYTGPVVLGTVAGG-----------------------------------------------PNGTMTN 144
Cdd:NF038016 81 ttgggalnvraAAGTGAARVGTVANGatvtvecqvwgqevdgtgvwyrlgdgryvsaayvrrpwlpwcgqdppTVPRGTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 145 ADFIAAAVIPAQQSQREFRVPASVTIAQSILESGWGRSGLTVNDKNFFGIKCFtPVPGPISIGCHSYATYEFV-NGHYVA 223
Cdd:NF038016 161 AQFIAAVAPPAQQSQRATGVPASVTIAQAILESGWGRSGLTREDHNYFGIKCF-GSPGPIAVGCRSYATFECSpTGGCFD 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1125233871 224 TTAAFRTYASALDSFRDHGRFLVVNDRYAPAFAYTGNADQFLYQIWKAGYATSPTYVANVQALMHQFNLYQYD 296
Cdd:NF038016 240 TTATFRAYASAADSFRDHGRFLSVNSRYAPAFAYTDDPDQFAREIHKAGYATDPTYADKLIGLMKQYNLYQYD 312
|
|
| FlgJ |
COG1705 |
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ... |
138-294 |
8.25e-51 |
|
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];
Pssm-ID: 441311 [Multi-domain] Cd Length: 276 Bit Score: 168.99 E-value: 8.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 138 PNGTMTNADFIAAAVIPAQQSQREFRVPASVTIAQSILESGWGRSGLT-VNDKNFFGIKCFTPVPGPisigCHSYATYEF 216
Cdd:COG1705 123 AAASASPEEFIAKIAPAAQKAAKKYGVPASVLIAQAALESGWGKSELDgSPSNNLFGIKAGGSWQGK----SVEVTTTEY 198
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1125233871 217 VNGHYVATTAAFRTYASALDSFRDHGRFLVVNDRYAPAFAYTGNADQFLYQIWKAGYATSPTYVANVQALMHQFNLYQ 294
Cdd:COG1705 199 VNGKAVKIKARFRAYDSYAESFRDYARLLKNNPRYAGALANAKDYEAFAKALQKAGYATDPKYADKLISIIESYNLTQ 276
|
|
| flgJ |
PRK05684 |
flagellar assembly peptidoglycan hydrolase FlgJ; |
142-294 |
1.78e-26 |
|
flagellar assembly peptidoglycan hydrolase FlgJ;
Pssm-ID: 235559 [Multi-domain] Cd Length: 312 Bit Score: 105.73 E-value: 1.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 142 MTNADFIAAAVIPAQQSQREFRVPASVTIAQSILESGWGRSG-LTVNDK---NFFGIKCFTPVPGPISigchSYATYEFV 217
Cdd:PRK05684 150 GSSDDFVARLSPPAQKAAQQSGVPHHLLLAQAALESGWGQREiRTADGSpshNLFGIKADGSWKGPVT----EITTTEYE 225
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1125233871 218 NGHYVATTAAFRTYASALDSFRDHGRFLVVNDRYApAFAYTGNADQFLYQIWKAGYATSPTYVANVQALMHQFNLYQ 294
Cdd:PRK05684 226 NGVAVKVKAAFRVYDSYLESFNDYVSLLTNNPRYA-AVTQAASPEQFARALQDAGYATDPNYARKLVSVIQQMKSMG 301
|
|
| flagell_FlgJ |
TIGR02541 |
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ... |
133-289 |
8.99e-25 |
|
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: 100.70 E-value: 8.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 133 TVAGGPNgtmtnaDFIAAAVIPAQQSQREFRVPASVTIAQSILESGWGRSGLTVNDK----NFFGIKCFTPVPGPISigc 208
Cdd:TIGR02541 143 SVPGHPK------SFVNSMLPHARKAAQQLGVPPHLILAQAALESGWGQRQIRNADGspsyNLFGIKASGSWQGKVV--- 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 209 hSYATYEFVNGHYVATTAAFRTYASALDSFRDHGRFLVVNDRYApAFAYTGNADQFLYQIWKAGYATSPTYVANVQALMH 288
Cdd:TIGR02541 214 -TTMTTEYVDGVAQKLTAKFRSYSSYEEAFSDYARLLNNNPRYE-AVLQQRSAESFARGLQRAGYATDPRYARKLLQVIQ 291
|
.
gi 1125233871 289 Q 289
Cdd:TIGR02541 292 S 292
|
|
| Glucosaminidase |
pfam01832 |
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ... |
155-241 |
1.80e-21 |
|
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: 86.47 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 155 AQQSQREFRVPASVTIAQSILESGWGRSGLTVNDKNFFGIKCftpvpgpisigchSYATYEFVNGHYVATTAAFRTYASA 234
Cdd:pfam01832 4 AIEAAKKYGIPASVLLAQAALESGWGTSRLAKESNNLFGIKA-------------SWKGKVAYDTDEVTVAARFRKYDSV 70
|
....*..
gi 1125233871 235 LDSFRDH 241
Cdd:pfam01832 71 EESIRDY 77
|
|
| LYZ2 |
smart00047 |
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes. |
145-296 |
4.55e-20 |
|
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
Pssm-ID: 214488 [Multi-domain] Cd Length: 147 Bit Score: 84.41 E-value: 4.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 145 ADFIAAAVIPAQQSQREFRVPASVTIAQSILESGWGRSGLTVNDKNFFGIKcfTPVPGPISigchSYATYEFVNGHYVAT 224
Cdd:smart00047 9 LEFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLAKKYNNLFGIK--GAYDGRPV----RMGTLEYLNGGWVTV 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1125233871 225 TAAFRTYASAldSFRDHGRFLV-VNDRYAPAFAYTGnadqflyqIWKAGYATSPTYVANVQALMHQFN--LYQYD 296
Cdd:smart00047 83 KAAFRGYFGE--KFIDYAYVLRgQNPLYKKRWGSNA--------LQTAGYATDPDYAKKLIRIIALYDekLKGYD 147
|
|
| flgJ |
PRK12711 |
flagellar assembly peptidoglycan hydrolase FlgJ; |
140-288 |
5.30e-20 |
|
flagellar assembly peptidoglycan hydrolase FlgJ;
Pssm-ID: 237180 [Multi-domain] Cd Length: 392 Bit Score: 88.87 E-value: 5.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 140 GTMTNADFIAAAVIPAQQSQREFRVPASVTIAQSILESGWGRSGLT--VNDKNFFGIKCFTPVPGPISIGCHsyatyEFV 217
Cdd:PRK12711 211 GERTPEGFVAKIWTHAQKAARELGVDPRALVAQAALETGWGRRGIGngGDSNNLFGIKATGWNGDKVTTGTH-----EYV 285
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1125233871 218 NGHYVATTAAFRTYASALDSFRDHGRFLVVNDRYAPAFAYTGNADQFLYQIWKAGYATSPTYVANVQALMH 288
Cdd:PRK12711 286 NGVKTTETADFRAYGSAEESFADYVRLLKNNSRYQQALQAGTDIKGFARGLQQAGYATDPGYAAKIAAIAN 356
|
|
| flgJ |
PRK12712 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
147-279 |
1.46e-18 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 139172 [Multi-domain] Cd Length: 344 Bit Score: 84.29 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 147 FIAAAVIPAQQSQREFRVPASVTIAQSILESGWGRSGLTVNDK----NFFGIKCFTPVPGPISigchSYATYEFVNGHYV 222
Cdd:PRK12712 200 FVARMAGPAEAASRASGVPARLIVGQAALESGWGRREITHADGsttfNVFGIKAGANWKGRVA----EVTTTEYVDGQPQ 275
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1125233871 223 ATTAAFRTYASALDSFRDHGRFLVVNDRYAPAFAyTGNADQFLYQIWKAGYATSPTY 279
Cdd:PRK12712 276 KVRARFRAYGSYDEACADYARLLTSNPRYAGVVS-AASADEAAHGLQRAGYATDPAY 331
|
|
| flgJ |
PRK12713 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
146-290 |
5.46e-17 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 139173 [Multi-domain] Cd Length: 339 Bit Score: 79.79 E-value: 5.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 146 DFIA----AAVIPAQQSQrefrVPASVTIAQSILESGWGRSGLTVNDK----NFFGIKCFTPVPGPISigchSYATYEFV 217
Cdd:PRK12713 183 DFVSrmsrAANVAAQQSG----VPARLILGQAALESGWGRRELRHEDGstsyNLFGIKAGASWKGKVV----NVMTTEYV 254
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1125233871 218 NGHYVATTAAFRTYASALDSFRDHGRFLVVNDRYApAFAYTGNADQFLYQIWKAGYATSPTYVANVQALMHQF 290
Cdd:PRK12713 255 DGVAQKLVQPFRAYSSYEESFSDYARLIGNSPRYE-AVTQAGNEIEAARRIQEAGYATDPRYAEKLISIMGQL 326
|
|
| flgJ |
PRK12709 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
139-289 |
1.91e-15 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 237179 [Multi-domain] Cd Length: 320 Bit Score: 75.35 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 139 NGTMTNAD-FIAAAVIPAQQSQREFRVPASVTIAQSILESGWGRSGLTVND----KNFFGIKCFTPVPGPISigchSYAT 213
Cdd:PRK12709 167 NGGSPDADaFVDKLAAPAQAASAATGIPARFIVGQAALESGWGKREIRGADgstsYNVFGIKATKGWTGRTV----SAVT 242
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1125233871 214 YEFVNGHYVATTAAFRTYASALDSFRDHGRFLVVNDRYAPAFAYTGNADQFLYQIWKAGYATSPTYVANVQALMHQ 289
Cdd:PRK12709 243 TEYVNGKPRRVVAKFRAYDSYEHAMTDYANLLKNNPRYAGVLNASRSVEGFAHGMQKAGYATDPHYAKKLISIMQQ 318
|
|
| PRK08581 |
PRK08581 |
amidase domain-containing protein; |
125-297 |
1.72e-13 |
|
amidase domain-containing protein;
Pssm-ID: 236304 [Multi-domain] Cd Length: 619 Bit Score: 70.59 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 125 YTGPVVLGTVAGGPNGTMTNAD---FIAAAVIPAQQSQREFRVPASVTIAQSILESGWGRSGLTVNDK-NFFGIKcftpv 200
Cdd:PRK08581 298 ETGPSLSNNDDSGSFNVVDSKDtrqFIKSIAKDAHRIGQDNDIYASVMIAQAILESDSGQSALAKSPNhNLFGIK----- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 201 pGPISIGCHSYATYEFVNGHYVATTAAFRTYASALDSFRDHGRfLVVN------DRYAPAF---AYT-GNADQFLYQIwk 270
Cdd:PRK08581 373 -GAYEGNSVSFNTLEADGNQLYSINAGFRKYPSTKESLEDYAD-LIKNgidgnsTIYKPTWkseAKSyKDATSHLSKT-- 448
|
170 180
....*....|....*....|....*..
gi 1125233871 271 agYATSPTYVANVQALMHQFNLYQYDL 297
Cdd:PRK08581 449 --YATDPNYAKKLNSIIKHYNLTQFDD 473
|
|
| flgJ |
PRK12710 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
146-294 |
4.85e-12 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 139170 [Multi-domain] Cd Length: 291 Bit Score: 65.20 E-value: 4.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 146 DFIAAAVIPAQQSQREFRVPASVTIAQSILESGWG----RSGLTVNDKNFFGIKcftpvpgpisIGCHS------YATYE 215
Cdd:PRK12710 132 DFVKSVWPTAKQAASLIGLDPKLLVAQAALETGWGkfvtRDADGSSSNNLFNIK----------TGSHSevesiqVKTTE 201
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1125233871 216 FVNGHYVATTAAFRTYASALDSFRDHGRFLVVNDRYAPAFAYTGNADQFLYQIWKAGYATSPTYVANVQALMHQFNLYQ 294
Cdd:PRK12710 202 YIADTPIKINASFRKYPSIEHSFHDYVSLIKGSERYQMALANAENPEIYVSELNKAGYATDPNYSNKILSIYHGDELNQ 280
|
|
| PRK06347 |
PRK06347 |
1,4-beta-N-acetylmuramoylhydrolase; |
107-296 |
8.76e-10 |
|
1,4-beta-N-acetylmuramoylhydrolase;
Pssm-ID: 180536 [Multi-domain] Cd Length: 592 Bit Score: 59.32 E-value: 8.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 107 PTCPAPVVPQVTVASVGPytgpvvlGTVAGGPNGT-------------------MTNADFIAAAVIPAQQSQREFRVPAS 167
Cdd:PRK06347 101 PEEKQPAAKQVEKAPAEP-------ATVSNPDNATssstpatynllqksalrsgATVQSFIQTIQASSSQIAAENDLYAS 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 168 VTIAQSILESGWGRSGL-TVNDKNFFGIKcftpvpGPISIGCHSYATYE-FVNGHYVATTAAFRTYASALDSFRDHGRFL 245
Cdd:PRK06347 174 VMIAQAILESAYGTSELgSAPNYNLFGIK------GAYNGQSYTKQTLEdDGKGNYYTITAKFRKYPSYHQSLEDYAQVI 247
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1125233871 246 vvndRYAPAFaytgNADqFLYQIWKAG--------------YATSPTYVANVQALMHQFNLYQYD 296
Cdd:PRK06347 248 ----RKGPSW----NPN-YYSKVWKSNttsykdatkaltgtYATDTAYATKLNDLISRYNLTQYD 303
|
|
| PRK10356 |
PRK10356 |
protein bax; |
164-239 |
2.11e-05 |
|
protein bax;
Pssm-ID: 182404 Cd Length: 274 Bit Score: 45.25 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 164 VPASVTIAQSILESGWGRSGLTVNDKNFFGIKCF----TPVPGPISigchSYATYEFVNGHYVATTAAFRTYaSALDSFR 239
Cdd:PRK10356 149 IPTSMVATMAAAESGWGTSKLARNNNNLFGMKCMkgrcTNAPGKVK----GYSQFSSVKESVSAYVTNLNTH-PAYSSFR 223
|
|
| SH3_3 |
pfam08239 |
Bacterial SH3 domain; |
41-100 |
2.49e-03 |
|
Bacterial SH3 domain;
Pssm-ID: 462405 [Multi-domain] Cd Length: 54 Bit Score: 35.30 E-value: 2.49e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 41 GPLNLRAAATTRSATVGRLANRARVTLVCKVAGEKVkgKVRTSNqwDRTasgGYVSHAYV 100
Cdd:pfam08239 1 SGLNVRSGPSTSSEVVGTLPKGEKVEVLEEQGGGWY--KVRTYD--GYE---GWVSSSYL 53
|
|
|