|
Name |
Accession |
Description |
Interval |
E-value |
| PHA00368 |
PHA00368 |
internal virion protein D |
10-1332 |
0e+00 |
|
internal virion protein D
Pssm-ID: 222785 [Multi-domain] Cd Length: 1315 Bit Score: 1513.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 10 VKAAGTPYDADIQRAAEANGVSYDFLHKQLWFESEFNPKAKSPTGPRGIGQFTKATGNAYGL-VTDEDFNDPLKSIDAAA 88
Cdd:PHA00368 4 DKNKPSEYDGLFQKAADAHGVSYDLLRKVGWDESRFNPTAKSPTGPKGLMQFTKATAKALGLiVDDDDRLDPELAIDAGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 89 RHMKDILTSTKGDYLKAALAYNQGGGRLGRPQLAALDAGDTSQITHEGMNYMRNLRDVAGeSPFSSLLDSQGavtnpGIT 168
Cdd:PHA00368 84 RYLADLVGKYDGDELKAALAYNQGEGRLGAPQLEAYDKGDFASISEEGRNYLRNLLDVAK-SPKSGDLESFG-----GIT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 169 PKSDAVEFDQAMQGITADIKtVRGATPELGNMNVKGEQRDIYRKNFAEAEFDVKGAP------KGWFEGTGQVVESELAT 242
Cdd:PHA00368 158 PKAKGIPAEAAFEGIGKKGK-VGTELPESHGFSVEGKEQEAPNVPFAKDFWEATGETldeansRSTFFGFGDATEAELSN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 243 GTLGQLFRNATLST-FDPMEGYDTP---DTSAWGDPEFDAMRNAGVSPQFYPFIfdhTRGNKNRIAEAITLAKQNMEYEK 318
Cdd:PHA00368 237 SVLGVAFRAGRRDDgFDVFKDVFTPtrwNSHIWTPEELEKIRTEVKNPAYINVV---TGGSPENLDELIKLANENFEYDA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 319 KARAQSTSAQIVGGFVGAGVDPFTYMPLPGVT--GATLFSKVVTGAAASGVTAMASEGLREASTGIEAHYGTALVAGALI 396
Cdd:PHA00368 314 RAAEAGLGAKLSAGIIGAGVDPLSYVPMAGVTgkGFKLVNKALVVGAQSAALNVASEGLRTSVAGGEAHYAEAALGGALF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 397 GGGLTALtsriraaaepeqrldmwDNDLESVLARHGEAALPNDFHAASMRLEARETARQGDFEDPSRMHWQPHETVEEVA 476
Cdd:PHA00368 394 GGGMSAI-----------------SDAVAAGLRRSGETEVVNEFAGPAMRLEARETARNAGGEDLSRMPPSNDRFLSDHN 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 477 GVRFTRVPNEEGAVRLQDGSVLSAGNPLNPLTIEAFQ--NAERAAPGLSMGGFTEIGYTLTRSENPEVRGIGAQLFRSTT 554
Cdd:PHA00368 457 GVPYADLPTEPGAVVLRDGSILSDSNPLNPKTLKEFAevDPERAAKGIKLGGFTEIGLKTLRSENAEVRGIASDLVRSPT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 555 GTESGSHGKFGATAADIVERQMAQDHVSYNNIVSTLHETIKDPRYAA--MPGGREVQMESAYRRVTEALEDrtGSKKAQL 632
Cdd:PHA00368 537 GMQSGSSGKFGATASDIKERLHSTDQRTYNDLYDAMEDAMKDPEFSTggAKMSREAARQEIYRRVALAIER--PELQANL 614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 633 SSAERALMDTVDAHYSRKLEALQNPAQFGNHRATSVLGATRHEGAYVPNVYDDAVKQMWIRRMGSPEDLQEAIIQSWLAS 712
Cdd:PHA00368 615 TKAERKVMDILKEHFDLKREMMENPAIFGNTKAVSIFPGSRHKGTYVPHVYDRAAKALYIQRLGGPDGLQEAIAKSWLTS 694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 713 YASRAHVKARVDRMIVEANPgtPMTPEGIQRAVEDYARNKAYGISHTQDFNRSHLVDDQVNGLVGAENNNFLEGRHLFDS 792
Cdd:PHA00368 695 YRSRPEVKARVDEFLKELHG--IDVKEVTPEMVEKYAMDKAYGISHTDQFTRSSVIEENIEGLVGIENNSFLEARNLFDS 772
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 793 DMPIPLVGGAEFSVNDLRSFDLTSITPGYDRRVNGDIGIMGATGQSTEALKDRIVAM-----GVGNESRkEYAALQDAVK 867
Cdd:PHA00368 773 DMSVTLPDGQTFSVNDLRDFDMKRIMPAYDRRVNGDIAIMGGTGKTTKELKDEILALdkkaeGDGKLKG-EVEALKDTVK 851
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 868 LLTGRARRDPDGVMATIARSLTDMSFLAKNAYMGIQGITETAALVTKGHTAMLLKGVPFLNQMMTVGSKATPEFLADMHG 947
Cdd:PHA00368 852 ILTGRARRNPDTAFETALRSLNDLSFFAKNAYMGAQNITEIAGMLAKGNVRALLHGIPILRDLAFRNKPVSASELKELHG 931
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 948 LVFGRELDNLIRPKRADIVMRLRDHADASPAMAQAVGSLKWATGEMAARWPLTRFLTESSNYIADAGRQGVLKELVDMAH 1027
Cdd:PHA00368 932 MLFGKELDQLIRPSRQDIVQRLRETTDTGPAVANVVGTLKYATQELAARSPFTKLLNGTTNYILDAARQGVLGDVVSAAL 1011
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 1028 -GTPSKMGKKLFdqkrLKSMSLTQDQYEGMLDLVR-SATTVKNGRVEITDRAAFQSDPRSMDIWRLGDKIADETILRPHK 1105
Cdd:PHA00368 1012 tGKKTKWFKERF----LKSASISPEQWEGIKQLIReHVTRGADGKFTIKDKQAFASDPRAMDLWRLADKVADETMLRPHK 1087
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 1106 LSSQDTEAYGAGVKMAMQFKNFTMRSMNARAIRAYHDTTKNGRAADSVMQAIISTGMAGAMYTAMAYVRSTGMPDKDRDA 1185
Cdd:PHA00368 1088 VSLQDSKAFGALVKMVLQFKSFVIKSLNSKFIRSFYEATKNNRAIDMALTHVISMGLAGGYYVAQAHVKAYGLPEEQRKE 1167
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 1186 YLKQAVNPTMFAYSALSRGSHIGAPLGLANMVMAPLGLDQARMVRTSITPRPKAEREkgaVQYGASKDDRVQDFLSGVLD 1265
Cdd:PHA00368 1168 YLKNALDPTMIAYAALSRSSHLGAPLSIANMVAGPLGFDDAKMVRSTILPKGEKERD---PNKAMTSRDVAGNIGGNLLE 1244
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564292474 1266 QVPAASWALGVGQAVHSAAGASATTDRAGDQAYMNSFYNGLRGVIPNDPATQYLFMKIMESEGIQAR 1332
Cdd:PHA00368 1245 QVPALGFAGNVGATGYNAAGVLTAPNKPTERDYMTGLMNTTRELVPNDPLSQQLLLKIYEANGIHIK 1311
|
|
| MltD-like |
cd16894 |
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ... |
42-118 |
2.32e-18 |
|
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases (LT) catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc). Membrane-bound lytic murein transglycosylase D protein (MltD) family members may have one or more small LysM domains, which may contribute to peptidoglycan binding. Unlike the similar "goose-type" lysozymes, LTs also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).
Pssm-ID: 381615 [Multi-domain] Cd Length: 129 Bit Score: 82.57 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 42 ESEFNPKAKSPTGPRGIGQFTKATGNAYGLVTDEDFN---DPLKSIDAAARHMKDiLTSTKGDYLKAALAYNQGGGRLGR 118
Cdd:cd16894 17 ESGFNPDAVSSAGAAGLWQFMPATAREYGLRVDSWVDerrDPEKSTRAAARYLKD-LYKRFGDWLLALAAYNAGEGRVRR 95
|
|
| SLT |
pfam01464 |
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ... |
21-118 |
2.58e-18 |
|
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found in phages, type II, type III and type IV secretion systems.
Pssm-ID: 396169 [Multi-domain] Cd Length: 114 Bit Score: 81.97 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 21 IQRAAEANGVSYDFLHKQLWFESEFNPKAKSPTGPRGIGQFTKATGNAYGL---VTDEDFNDPLKSIDAAARHMKDILTS 97
Cdd:pfam01464 1 IIKAAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLrvnPGVDDLFDPEKNIKAGTKYLKELYKQ 80
|
90 100
....*....|....*....|.
gi 564292474 98 TKGDYLKAALAYNQGGGRLGR 118
Cdd:pfam01464 81 YGGDLWLALAAYNAGPGRVRK 101
|
|
| MltE |
COG0741 |
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ... |
1-118 |
3.88e-17 |
|
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin domain) [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440504 [Multi-domain] Cd Length: 244 Bit Score: 82.35 E-value: 3.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 1 MTRQERYAQVKAAGTPYDADIQRAAEANGVSYDFLHKQLWFESEFNPKAKSPTGPRGIGQFTKATGNAYGLVTDEDFN-- 78
Cdd:COG0741 87 AELLALAALLLRRPLPYLPLIEEAAKKYGVDPALVLALIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKLGLGPSpd 166
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 564292474 79 ---DPLKSIDAAARHMKDILTSTKGDYLKAALAYNQGGGRLGR 118
Cdd:COG0741 167 dlfDPETNIRAGAAYLRELLDRFDGDLVLALAAYNAGPGRVRR 209
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PHA00368 |
PHA00368 |
internal virion protein D |
10-1332 |
0e+00 |
|
internal virion protein D
Pssm-ID: 222785 [Multi-domain] Cd Length: 1315 Bit Score: 1513.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 10 VKAAGTPYDADIQRAAEANGVSYDFLHKQLWFESEFNPKAKSPTGPRGIGQFTKATGNAYGL-VTDEDFNDPLKSIDAAA 88
Cdd:PHA00368 4 DKNKPSEYDGLFQKAADAHGVSYDLLRKVGWDESRFNPTAKSPTGPKGLMQFTKATAKALGLiVDDDDRLDPELAIDAGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 89 RHMKDILTSTKGDYLKAALAYNQGGGRLGRPQLAALDAGDTSQITHEGMNYMRNLRDVAGeSPFSSLLDSQGavtnpGIT 168
Cdd:PHA00368 84 RYLADLVGKYDGDELKAALAYNQGEGRLGAPQLEAYDKGDFASISEEGRNYLRNLLDVAK-SPKSGDLESFG-----GIT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 169 PKSDAVEFDQAMQGITADIKtVRGATPELGNMNVKGEQRDIYRKNFAEAEFDVKGAP------KGWFEGTGQVVESELAT 242
Cdd:PHA00368 158 PKAKGIPAEAAFEGIGKKGK-VGTELPESHGFSVEGKEQEAPNVPFAKDFWEATGETldeansRSTFFGFGDATEAELSN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 243 GTLGQLFRNATLST-FDPMEGYDTP---DTSAWGDPEFDAMRNAGVSPQFYPFIfdhTRGNKNRIAEAITLAKQNMEYEK 318
Cdd:PHA00368 237 SVLGVAFRAGRRDDgFDVFKDVFTPtrwNSHIWTPEELEKIRTEVKNPAYINVV---TGGSPENLDELIKLANENFEYDA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 319 KARAQSTSAQIVGGFVGAGVDPFTYMPLPGVT--GATLFSKVVTGAAASGVTAMASEGLREASTGIEAHYGTALVAGALI 396
Cdd:PHA00368 314 RAAEAGLGAKLSAGIIGAGVDPLSYVPMAGVTgkGFKLVNKALVVGAQSAALNVASEGLRTSVAGGEAHYAEAALGGALF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 397 GGGLTALtsriraaaepeqrldmwDNDLESVLARHGEAALPNDFHAASMRLEARETARQGDFEDPSRMHWQPHETVEEVA 476
Cdd:PHA00368 394 GGGMSAI-----------------SDAVAAGLRRSGETEVVNEFAGPAMRLEARETARNAGGEDLSRMPPSNDRFLSDHN 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 477 GVRFTRVPNEEGAVRLQDGSVLSAGNPLNPLTIEAFQ--NAERAAPGLSMGGFTEIGYTLTRSENPEVRGIGAQLFRSTT 554
Cdd:PHA00368 457 GVPYADLPTEPGAVVLRDGSILSDSNPLNPKTLKEFAevDPERAAKGIKLGGFTEIGLKTLRSENAEVRGIASDLVRSPT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 555 GTESGSHGKFGATAADIVERQMAQDHVSYNNIVSTLHETIKDPRYAA--MPGGREVQMESAYRRVTEALEDrtGSKKAQL 632
Cdd:PHA00368 537 GMQSGSSGKFGATASDIKERLHSTDQRTYNDLYDAMEDAMKDPEFSTggAKMSREAARQEIYRRVALAIER--PELQANL 614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 633 SSAERALMDTVDAHYSRKLEALQNPAQFGNHRATSVLGATRHEGAYVPNVYDDAVKQMWIRRMGSPEDLQEAIIQSWLAS 712
Cdd:PHA00368 615 TKAERKVMDILKEHFDLKREMMENPAIFGNTKAVSIFPGSRHKGTYVPHVYDRAAKALYIQRLGGPDGLQEAIAKSWLTS 694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 713 YASRAHVKARVDRMIVEANPgtPMTPEGIQRAVEDYARNKAYGISHTQDFNRSHLVDDQVNGLVGAENNNFLEGRHLFDS 792
Cdd:PHA00368 695 YRSRPEVKARVDEFLKELHG--IDVKEVTPEMVEKYAMDKAYGISHTDQFTRSSVIEENIEGLVGIENNSFLEARNLFDS 772
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 793 DMPIPLVGGAEFSVNDLRSFDLTSITPGYDRRVNGDIGIMGATGQSTEALKDRIVAM-----GVGNESRkEYAALQDAVK 867
Cdd:PHA00368 773 DMSVTLPDGQTFSVNDLRDFDMKRIMPAYDRRVNGDIAIMGGTGKTTKELKDEILALdkkaeGDGKLKG-EVEALKDTVK 851
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 868 LLTGRARRDPDGVMATIARSLTDMSFLAKNAYMGIQGITETAALVTKGHTAMLLKGVPFLNQMMTVGSKATPEFLADMHG 947
Cdd:PHA00368 852 ILTGRARRNPDTAFETALRSLNDLSFFAKNAYMGAQNITEIAGMLAKGNVRALLHGIPILRDLAFRNKPVSASELKELHG 931
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 948 LVFGRELDNLIRPKRADIVMRLRDHADASPAMAQAVGSLKWATGEMAARWPLTRFLTESSNYIADAGRQGVLKELVDMAH 1027
Cdd:PHA00368 932 MLFGKELDQLIRPSRQDIVQRLRETTDTGPAVANVVGTLKYATQELAARSPFTKLLNGTTNYILDAARQGVLGDVVSAAL 1011
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 1028 -GTPSKMGKKLFdqkrLKSMSLTQDQYEGMLDLVR-SATTVKNGRVEITDRAAFQSDPRSMDIWRLGDKIADETILRPHK 1105
Cdd:PHA00368 1012 tGKKTKWFKERF----LKSASISPEQWEGIKQLIReHVTRGADGKFTIKDKQAFASDPRAMDLWRLADKVADETMLRPHK 1087
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 1106 LSSQDTEAYGAGVKMAMQFKNFTMRSMNARAIRAYHDTTKNGRAADSVMQAIISTGMAGAMYTAMAYVRSTGMPDKDRDA 1185
Cdd:PHA00368 1088 VSLQDSKAFGALVKMVLQFKSFVIKSLNSKFIRSFYEATKNNRAIDMALTHVISMGLAGGYYVAQAHVKAYGLPEEQRKE 1167
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 1186 YLKQAVNPTMFAYSALSRGSHIGAPLGLANMVMAPLGLDQARMVRTSITPRPKAEREkgaVQYGASKDDRVQDFLSGVLD 1265
Cdd:PHA00368 1168 YLKNALDPTMIAYAALSRSSHLGAPLSIANMVAGPLGFDDAKMVRSTILPKGEKERD---PNKAMTSRDVAGNIGGNLLE 1244
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564292474 1266 QVPAASWALGVGQAVHSAAGASATTDRAGDQAYMNSFYNGLRGVIPNDPATQYLFMKIMESEGIQAR 1332
Cdd:PHA00368 1245 QVPALGFAGNVGATGYNAAGVLTAPNKPTERDYMTGLMNTTRELVPNDPLSQQLLLKIYEANGIHIK 1311
|
|
| MltD-like |
cd16894 |
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ... |
42-118 |
2.32e-18 |
|
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases (LT) catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc). Membrane-bound lytic murein transglycosylase D protein (MltD) family members may have one or more small LysM domains, which may contribute to peptidoglycan binding. Unlike the similar "goose-type" lysozymes, LTs also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).
Pssm-ID: 381615 [Multi-domain] Cd Length: 129 Bit Score: 82.57 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 42 ESEFNPKAKSPTGPRGIGQFTKATGNAYGLVTDEDFN---DPLKSIDAAARHMKDiLTSTKGDYLKAALAYNQGGGRLGR 118
Cdd:cd16894 17 ESGFNPDAVSSAGAAGLWQFMPATAREYGLRVDSWVDerrDPEKSTRAAARYLKD-LYKRFGDWLLALAAYNAGEGRVRR 95
|
|
| SLT |
pfam01464 |
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ... |
21-118 |
2.58e-18 |
|
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found in phages, type II, type III and type IV secretion systems.
Pssm-ID: 396169 [Multi-domain] Cd Length: 114 Bit Score: 81.97 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 21 IQRAAEANGVSYDFLHKQLWFESEFNPKAKSPTGPRGIGQFTKATGNAYGL---VTDEDFNDPLKSIDAAARHMKDILTS 97
Cdd:pfam01464 1 IIKAAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLrvnPGVDDLFDPEKNIKAGTKYLKELYKQ 80
|
90 100
....*....|....*....|.
gi 564292474 98 TKGDYLKAALAYNQGGGRLGR 118
Cdd:pfam01464 81 YGGDLWLALAAYNAGPGRVRK 101
|
|
| MltE |
COG0741 |
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ... |
1-118 |
3.88e-17 |
|
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin domain) [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440504 [Multi-domain] Cd Length: 244 Bit Score: 82.35 E-value: 3.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 1 MTRQERYAQVKAAGTPYDADIQRAAEANGVSYDFLHKQLWFESEFNPKAKSPTGPRGIGQFTKATGNAYGLVTDEDFN-- 78
Cdd:COG0741 87 AELLALAALLLRRPLPYLPLIEEAAKKYGVDPALVLALIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKLGLGPSpd 166
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 564292474 79 ---DPLKSIDAAARHMKDILTSTKGDYLKAALAYNQGGGRLGR 118
Cdd:COG0741 167 dlfDPETNIRAGAAYLRELLDRFDGDLVLALAAYNAGPGRVRR 209
|
|
| MltF |
COG4623 |
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ... |
16-116 |
6.48e-17 |
|
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];
Pssm-ID: 443662 [Multi-domain] Cd Length: 421 Bit Score: 84.73 E-value: 6.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 16 PYDADIQRAAEANGVSYDFLHKQLWFESEFNPKAKSPTGPRGIGQFTKATGNAYGLvtdEDFNDPLKSIDAAARHMKDIL 95
Cdd:COG4623 263 PYDPLFEKYAEEYGLDWRLLAALAYQESHWNPRARSPTGARGLMQLMPATAKELGV---DDRLDPEQSIRAGAKYLRWLY 339
|
90 100
....*....|....*....|....*..
gi 564292474 96 -----TSTKGDYLKAALA-YNQGGGRL 116
Cdd:COG4623 340 drfpeAIDEPDRWWFALAaYNAGPGHV 366
|
|
| LT-like |
cd00254 |
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ... |
42-118 |
3.20e-16 |
|
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble membrane-bound LTs in bacteria and LTs in bacteriophage lambda. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.
Pssm-ID: 381594 [Multi-domain] Cd Length: 111 Bit Score: 75.71 E-value: 3.20e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564292474 42 ESEFNPKAKSPTGPRGIGQFTKATGNAYGLVTDEDFNDPLKSIDAAARHMKDILTSTKGDYLKAALAYNQGGGRLGR 118
Cdd:cd00254 11 ESGFNPRAVSPAGARGLMQLMPGTARDLGRRGVDDLFDPEENIRAGARYLRELLDRFGGDLELALAAYNAGPGAVDR 87
|
|
| MLTF-like |
cd13403 |
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily ... |
21-116 |
8.70e-14 |
|
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily includes membrane-bound lytic murein transglycosylase F (MltF, murein lyase F) that degrades murein glycan strands. It is responsible for catalyzing the release of 1,6-anhydromuropeptides from peptidoglycan. Lytic transglycosylase catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc) as do goose-type lysozymes. However, in addition, it also makes a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.
Pssm-ID: 381606 [Multi-domain] Cd Length: 161 Bit Score: 70.26 E-value: 8.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 21 IQRAAEANGVSYDFLHKQLWFESEFNPKAKSPTGPRGIGQFTKATGNAYGLvtdEDFNDPLKSIDAAARHMKDILTSTKG 100
Cdd:cd13403 1 FKKYAEKYGFDWRLLAAQAYQESRFNPNARSPAGARGLMQLMPSTARELGV---NDRLDPEQNIHAGAKYLRYLRDRFPP 77
|
90 100
....*....|....*....|..
gi 564292474 101 DY-----LKAALA-YNQGGGRL 116
Cdd:cd13403 78 DIdepdrLKFALAaYNAGPGHV 99
|
|
| Slt70-like |
cd13401 |
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ... |
15-118 |
2.98e-12 |
|
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the 70kda soluble lytic transglycosylase (LT)-like proteins, which also have an N-terminal U-shaped U-domain and a linker L-domain. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda.
Pssm-ID: 381604 [Multi-domain] Cd Length: 152 Bit Score: 65.58 E-value: 2.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 15 TPYDADIQRAAEANGVSYDFLH---KQlwfESEFNPKAKSPTGPRGIGQFTKATGNA----YGL--VTDEDFNDPLKSID 85
Cdd:cd13401 4 LPYRDLVERAAKKNGLDPALVYaiiRQ---ESAFDPDAVSPAGALGLMQLMPATAKDvakkLGLpyYSPRDLFDPEYNIR 80
|
90 100 110
....*....|....*....|....*....|...
gi 564292474 86 AAARHMKDILTSTKGDYLKAALAYNQGGGRLGR 118
Cdd:cd13401 81 LGSAYLAELLDRFDGNPVLALAAYNAGPGRVRR 113
|
|
| Slt35-like |
cd13399 |
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ... |
29-112 |
1.27e-07 |
|
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic transglycosylase Slt35 and Pseudomonas aeruginosa Sltb1. Lytic transglycosylase (LT) catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc) as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).
Pssm-ID: 381602 [Multi-domain] Cd Length: 108 Bit Score: 51.16 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 29 GVSYDFLHKQLWFESEFNPKA-KSPTGPRGIGQFTKATGNAYGLVTDED----FNDPLKSIDAAARHMK----DILTSTK 99
Cdd:cd13399 2 GVPPGILAAILGVESGFGPNAgGSPAGAQGIAQFMPSTWKAYGVDGNGDgkadPFNPEDAIASAANYLCrhgwDLNAFLG 81
|
90
....*....|...
gi 564292474 100 GDYLKAALAYNQG 112
Cdd:cd13399 82 EDNFLALAAYNAG 94
|
|
| PRK10859 |
PRK10859 |
membrane-bound lytic murein transglycosylase MltF; |
42-116 |
8.71e-07 |
|
membrane-bound lytic murein transglycosylase MltF;
Pssm-ID: 236778 [Multi-domain] Cd Length: 482 Bit Score: 53.34 E-value: 8.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 42 ESEFNPKAKSPTGPRGIGQFTKATGNAYGlVTDEdfNDPLKSIDAAARHMKDIL-----TSTKGDYLKAALA-YNQGGGR 115
Cdd:PRK10859 313 ESHWNPQATSPTGVRGLMMLTRNTAQSMG-VTDR--LDPEQSIRGGARYLQDLMerlpeSIPEPERIWFALAaYNIGYGH 389
|
.
gi 564292474 116 L 116
Cdd:PRK10859 390 M 390
|
|
| mltD |
PRK10783 |
membrane-bound lytic murein transglycosylase D; Provisional |
42-115 |
4.07e-05 |
|
membrane-bound lytic murein transglycosylase D; Provisional
Pssm-ID: 182727 [Multi-domain] Cd Length: 456 Bit Score: 47.81 E-value: 4.07e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564292474 42 ESEFNPKAKSPTGPRGIGQFTKATGNAYGLVTDEDFN---DPLKSIDAAARHMKDILTSTKGDYLKAALAYNQGGGR 115
Cdd:PRK10783 128 ESAFDPHATSGANAAGIWQIIPSTGRNYGLKQTRWYDarrDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGR 204
|
|
| Lyz-like |
cd00442 |
lysozyme-like domains; This family contains several members, including soluble lytic ... |
40-90 |
2.60e-04 |
|
lysozyme-like domains; This family contains several members, including soluble lytic transglycosylases (SLT), goose egg-white lysozymes (GEWL), hen egg-white lysozymes (HEWL), chitinases, bacteriophage lambda lysozymes, endolysins, autolysins, chitosanases, and pesticin. Typical members are involved in the hydrolysis of beta-1,4- linked polysaccharides.
Pssm-ID: 381596 [Multi-domain] Cd Length: 59 Bit Score: 40.09 E-value: 2.60e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 564292474 40 WFESEFNPKA--KSPTGPRGIGQFTKATGNAYGLVTDEDFNDPLKSIDAAARH 90
Cdd:cd00442 7 GQESGGNKPAnaGSGSGAAGLFQFMPGTWKAYGKNSSSDLNDPEASIEAAAKY 59
|
|
| LT_Slt70-like |
cd16896 |
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ... |
16-115 |
3.58e-04 |
|
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized lytic transglycosylase (LT) with a conserved sequence pattern suggesting similarity to the Slt70, a 70kda soluble lytic transglycosylase which also has an N-terminal U-shaped U-domain and a linker L-domain. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.
Pssm-ID: 381617 [Multi-domain] Cd Length: 146 Bit Score: 42.11 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564292474 16 PYDADIQRAAEANGVSYDFLHKQLWFESEFNPKAKSPTGPRGIGQFTKATG----NAYGL--VTDEDFNDPLKSIDAAAR 89
Cdd:cd16896 3 KYREYIEKYAKEYGVDPLLVAAVIKVESNFNPNAVSSKGAIGLMQIMPETAewiaEKLGLedFSEDDLYDPETNIRLGTW 82
|
90 100
....*....|....*....|....*.
gi 564292474 90 HMKDILTSTKGDYLKAALAYNQGGGR 115
Cdd:cd16896 83 YLSYLLKEFDGNLVLALAAYNAGPGN 108
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