|
Name |
Accession |
Description |
Interval |
E-value |
| FlgJ |
COG1705 |
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ... |
43-188 |
1.07e-34 |
|
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];
Pssm-ID: 441311 [Multi-domain] Cd Length: 276 Bit Score: 123.54 E-value: 1.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985376730 43 TKEEFIQKIVPDAQDLGKSYGIRPSFIIAQAALDSDFGEKIL-ANKYHNLFGLLAEPGT--PSITLNDSSTGK----KQE 115
Cdd:COG1705 128 SPEEFIAKIAPAAQKAAKKYGVPASVLIAQAALESGWGKSELdGSPSNNLFGIKAGGSWqgKSVEVTTTEYVNgkavKIK 207
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 985376730 116 KQFTHYKSWKYSMYDYLAHIKSgatgkKDSYTIMVSV-KNPKTLVQKLQDSGFDNDKKYAKKMTEIIDLYDLTR 188
Cdd:COG1705 208 ARFRAYDSYAESFRDYARLLKN-----NPRYAGALANaKDYEAFAKALQKAGYATDPKYADKLISIIESYNLTQ 276
|
|
| LYZ2 |
smart00047 |
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes. |
45-190 |
1.14e-21 |
|
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
Pssm-ID: 214488 [Multi-domain] Cd Length: 147 Bit Score: 85.95 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985376730 45 EEFIQKIVPDAQDLGKSYGIRPSFIIAQAALDSDFGEKILANKYHNLFGLLAEPGTPSITLNDSSTG----KKQEKQFTH 120
Cdd:smart00047 9 LEFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLAKKYNNLFGIKGAYDGRPVRMGTLEYLnggwVTVKAAFRG 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 985376730 121 YKSWKYSMYDYLahiksgATGKKDSYTIMVSVKNPKTlvqklqdSGFDNDKKYAKKMTEIIDLYD--LTRYD 190
Cdd:smart00047 89 YFGEKFIDYAYV------LRGQNPLYKKRWGSNALQT-------AGYATDPDYAKKLIRIIALYDekLKGYD 147
|
|
| PRK08581 |
PRK08581 |
amidase domain-containing protein; |
45-191 |
1.89e-18 |
|
amidase domain-containing protein;
Pssm-ID: 236304 [Multi-domain] Cd Length: 619 Bit Score: 82.14 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985376730 45 EEFIQKIVPDAQDLGKSYGIRPSFIIAQAALDSDFGEKILANK-YHNLFGLLAEPGTPSITLNDSSTGKKQ----EKQFT 119
Cdd:PRK08581 321 RQFIKSIAKDAHRIGQDNDIYASVMIAQAILESDSGQSALAKSpNHNLFGIKGAYEGNSVSFNTLEADGNQlysiNAGFR 400
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 985376730 120 HYKSWKYSMYDYLAHIKSGATGKKDSY--TIMVSVKNPKTLVQKLQDSgFDNDKKYAKKMTEIIDLYDLTRYDK 191
Cdd:PRK08581 401 KYPSTKESLEDYADLIKNGIDGNSTIYkpTWKSEAKSYKDATSHLSKT-YATDPNYAKKLNSIIKHYNLTQFDD 473
|
|
| Glucosaminidase |
pfam01832 |
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ... |
52-131 |
1.46e-16 |
|
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: 71.06 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985376730 52 VPDAQDLGKSYGIRPSFIIAQAALDSDFGEKILANKYHNLFGLLAEPGTPSitlNDSSTGKKQEKQFTHYKSWKYSMYDY 131
Cdd:pfam01832 1 APAAIEAAKKYGIPASVLLAQAALESGWGTSRLAKESNNLFGIKASWKGKV---AYDTDEVTVAARFRKYDSVEESIRDY 77
|
|
| sporang_Gsm |
NF038016 |
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ... |
43-190 |
7.94e-12 |
|
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: 62.45 E-value: 7.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985376730 43 TKEEFIQKIVPDAQDLGKSYGIRPSFIIAQAALDSDFGEKILANKYHNLFGL--LAEPGTPSI------TLNDSSTGK-- 112
Cdd:NF038016 159 TPAQFIAAVAPPAQQSQRATGVPASVTIAQAILESGWGRSGLTREDHNYFGIkcFGSPGPIAVgcrsyaTFECSPTGGcf 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985376730 113 KQEKQFTHYKSWKYSMYDY---LAHIKSGATGKKdsYTimvsvKNPKTLVQKLQDSGFDNDKKYAKKMTEIIDLYDLTRY 189
Cdd:NF038016 239 DTTATFRAYASAADSFRDHgrfLSVNSRYAPAFA--YT-----DDPDQFAREIHKAGYATDPTYADKLIGLMKQYNLYQY 311
|
.
gi 985376730 190 D 190
Cdd:NF038016 312 D 312
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| FlgJ |
COG1705 |
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ... |
43-188 |
1.07e-34 |
|
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];
Pssm-ID: 441311 [Multi-domain] Cd Length: 276 Bit Score: 123.54 E-value: 1.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985376730 43 TKEEFIQKIVPDAQDLGKSYGIRPSFIIAQAALDSDFGEKIL-ANKYHNLFGLLAEPGT--PSITLNDSSTGK----KQE 115
Cdd:COG1705 128 SPEEFIAKIAPAAQKAAKKYGVPASVLIAQAALESGWGKSELdGSPSNNLFGIKAGGSWqgKSVEVTTTEYVNgkavKIK 207
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 985376730 116 KQFTHYKSWKYSMYDYLAHIKSgatgkKDSYTIMVSV-KNPKTLVQKLQDSGFDNDKKYAKKMTEIIDLYDLTR 188
Cdd:COG1705 208 ARFRAYDSYAESFRDYARLLKN-----NPRYAGALANaKDYEAFAKALQKAGYATDPKYADKLISIIESYNLTQ 276
|
|
| LYZ2 |
smart00047 |
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes. |
45-190 |
1.14e-21 |
|
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
Pssm-ID: 214488 [Multi-domain] Cd Length: 147 Bit Score: 85.95 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985376730 45 EEFIQKIVPDAQDLGKSYGIRPSFIIAQAALDSDFGEKILANKYHNLFGLLAEPGTPSITLNDSSTG----KKQEKQFTH 120
Cdd:smart00047 9 LEFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLAKKYNNLFGIKGAYDGRPVRMGTLEYLnggwVTVKAAFRG 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 985376730 121 YKSWKYSMYDYLahiksgATGKKDSYTIMVSVKNPKTlvqklqdSGFDNDKKYAKKMTEIIDLYD--LTRYD 190
Cdd:smart00047 89 YFGEKFIDYAYV------LRGQNPLYKKRWGSNALQT-------AGYATDPDYAKKLIRIIALYDekLKGYD 147
|
|
| PRK08581 |
PRK08581 |
amidase domain-containing protein; |
45-191 |
1.89e-18 |
|
amidase domain-containing protein;
Pssm-ID: 236304 [Multi-domain] Cd Length: 619 Bit Score: 82.14 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985376730 45 EEFIQKIVPDAQDLGKSYGIRPSFIIAQAALDSDFGEKILANK-YHNLFGLLAEPGTPSITLNDSSTGKKQ----EKQFT 119
Cdd:PRK08581 321 RQFIKSIAKDAHRIGQDNDIYASVMIAQAILESDSGQSALAKSpNHNLFGIKGAYEGNSVSFNTLEADGNQlysiNAGFR 400
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 985376730 120 HYKSWKYSMYDYLAHIKSGATGKKDSY--TIMVSVKNPKTLVQKLQDSgFDNDKKYAKKMTEIIDLYDLTRYDK 191
Cdd:PRK08581 401 KYPSTKESLEDYADLIKNGIDGNSTIYkpTWKSEAKSYKDATSHLSKT-YATDPNYAKKLNSIIKHYNLTQFDD 473
|
|
| Glucosaminidase |
pfam01832 |
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ... |
52-131 |
1.46e-16 |
|
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: 71.06 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985376730 52 VPDAQDLGKSYGIRPSFIIAQAALDSDFGEKILANKYHNLFGLLAEPGTPSitlNDSSTGKKQEKQFTHYKSWKYSMYDY 131
Cdd:pfam01832 1 APAAIEAAKKYGIPASVLLAQAALESGWGTSRLAKESNNLFGIKASWKGKV---AYDTDEVTVAARFRKYDSVEESIRDY 77
|
|
| flgJ |
PRK05684 |
flagellar assembly peptidoglycan hydrolase FlgJ; |
45-181 |
2.77e-13 |
|
flagellar assembly peptidoglycan hydrolase FlgJ;
Pssm-ID: 235559 [Multi-domain] Cd Length: 312 Bit Score: 66.44 E-value: 2.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985376730 45 EEFIQKIVPDAQDLGKSYGIRPSFIIAQAALDSDFGEKILANK----YHNLFGLLAE-----PGTPSITLN-DSSTGKKQ 114
Cdd:PRK05684 153 DDFVARLSPPAQKAAQQSGVPHHLLLAQAALESGWGQREIRTAdgspSHNLFGIKADgswkgPVTEITTTEyENGVAVKV 232
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 985376730 115 EKQFTHYKSWKYSMYDYLAHIKSGatgkkDSYTIMVSVKNPKTLVQKLQDSGFDNDKKYAKKMTEII 181
Cdd:PRK05684 233 KAAFRVYDSYLESFNDYVSLLTNN-----PRYAAVTQAASPEQFARALQDAGYATDPNYARKLVSVI 294
|
|
| sporang_Gsm |
NF038016 |
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ... |
43-190 |
7.94e-12 |
|
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: 62.45 E-value: 7.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985376730 43 TKEEFIQKIVPDAQDLGKSYGIRPSFIIAQAALDSDFGEKILANKYHNLFGL--LAEPGTPSI------TLNDSSTGK-- 112
Cdd:NF038016 159 TPAQFIAAVAPPAQQSQRATGVPASVTIAQAILESGWGRSGLTREDHNYFGIkcFGSPGPIAVgcrsyaTFECSPTGGcf 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985376730 113 KQEKQFTHYKSWKYSMYDY---LAHIKSGATGKKdsYTimvsvKNPKTLVQKLQDSGFDNDKKYAKKMTEIIDLYDLTRY 189
Cdd:NF038016 239 DTTATFRAYASAADSFRDHgrfLSVNSRYAPAFA--YT-----DDPDQFAREIHKAGYATDPTYADKLIGLMKQYNLYQY 311
|
.
gi 985376730 190 D 190
Cdd:NF038016 312 D 312
|
|
| flgJ |
PRK12709 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
45-181 |
5.14e-11 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 237179 [Multi-domain] Cd Length: 320 Bit Score: 60.32 E-value: 5.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985376730 45 EEFIQKIVPDAQDLGKSYGIRPSFIIAQAALDSDFGEKIL----ANKYHNLFGLLAEPGTPSITLNDSST----GKKQE- 115
Cdd:PRK12709 174 DAFVDKLAAPAQAASAATGIPARFIVGQAALESGWGKREIrgadGSTSYNVFGIKATKGWTGRTVSAVTTeyvnGKPRRv 253
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 985376730 116 -KQFTHYKSWKYSMYDYLAHIKSGAtgkkdSYT-IMVSVKNPKTLVQKLQDSGFDNDKKYAKKMTEII 181
Cdd:PRK12709 254 vAKFRAYDSYEHAMTDYANLLKNNP-----RYAgVLNASRSVEGFAHGMQKAGYATDPHYAKKLISIM 316
|
|
| PRK06347 |
PRK06347 |
1,4-beta-N-acetylmuramoylhydrolase; |
43-190 |
2.02e-08 |
|
1,4-beta-N-acetylmuramoylhydrolase;
Pssm-ID: 180536 [Multi-domain] Cd Length: 592 Bit Score: 53.16 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985376730 43 TKEEFIQKIVPDAQDLGKSYGIRPSFIIAQAALDSDFGEKILANK-YHNLFGLLAEPGTPSIT---LNDSSTGKKQE--K 116
Cdd:PRK06347 149 TVQSFIQTIQASSSQIAAENDLYASVMIAQAILESAYGTSELGSApNYNLFGIKGAYNGQSYTkqtLEDDGKGNYYTitA 228
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 985376730 117 QFTHYKSWKYSMYDYLAHIKSGATGKKDSYTIM--VSVKNPKTLVQKLQDSgFDNDKKYAKKMTEIIDLYDLTRYD 190
Cdd:PRK06347 229 KFRKYPSYHQSLEDYAQVIRKGPSWNPNYYSKVwkSNTTSYKDATKALTGT-YATDTAYATKLNDLISRYNLTQYD 303
|
|
| flgJ |
PRK12710 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
35-180 |
1.14e-07 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 139170 [Multi-domain] Cd Length: 291 Bit Score: 50.56 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985376730 35 NSRQSVTYTkEEFIQKIVPDAQDLGKSYGIRPSFIIAQAALDSDFGEKIL----ANKYHNLFGLL--AEPGTPSITLNDS 108
Cdd:PRK12710 122 NSEESLSVV-DDFVKSVWPTAKQAASLIGLDPKLLVAQAALETGWGKFVTrdadGSSSNNLFNIKtgSHSEVESIQVKTT 200
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 985376730 109 S----TGKKQEKQFTHYKSWKYSMYDYLAHIKsgatGKKDSYTIMVSVKNPKTLVQKLQDSGFDNDKKYAKKMTEI 180
Cdd:PRK12710 201 EyiadTPIKINASFRKYPSIEHSFHDYVSLIK----GSERYQMALANAENPEIYVSELNKAGYATDPNYSNKILSI 272
|
|
| flgJ |
PRK12711 |
flagellar assembly peptidoglycan hydrolase FlgJ; |
43-180 |
2.35e-07 |
|
flagellar assembly peptidoglycan hydrolase FlgJ;
Pssm-ID: 237180 [Multi-domain] Cd Length: 392 Bit Score: 49.58 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985376730 43 TKEEFIQKIVPDAQDLGKSYGIRPSFIIAQAALDSDFGEKILAN--KYHNLFGLLAE--PGTPSIT-LNDSSTGKKQEK- 116
Cdd:PRK12711 214 TPEGFVAKIWTHAQKAARELGVDPRALVAQAALETGWGRRGIGNggDSNNLFGIKATgwNGDKVTTgTHEYVNGVKTTEt 293
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 985376730 117 -QFTHYKSWKYSMYDYLAHIKSGATGKkdsyTIMVSVKNPKTLVQKLQDSGFDNDKKYAKKMTEI 180
Cdd:PRK12711 294 aDFRAYGSAEESFADYVRLLKNNSRYQ----QALQAGTDIKGFARGLQQAGYATDPGYAAKIAAI 354
|
|
|