|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10760 |
PRK10760 |
murein hydrolase B; Provisional |
1-358 |
0e+00 |
|
murein hydrolase B; Provisional
Pssm-ID: 236754 [Multi-domain] Cd Length: 359 Bit Score: 755.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 1 MLKRRYLALLPLCVLLAACSSKPK-TPAETEMASGTGGFLLEPQHNVMQMGGDFANNPAAAQFIDKMVAKHGFDRQQLQE 79
Cdd:PRK10760 1 MFMRRYVALLPLFVLLAACSSKPKpTETATTTGTPSGGFLLEPQHNVMQMGGDFANNPNAQQFIDKMVNKHGFDRQQLHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 80 ILSQAKRLDYVLRLMDRQAPTGLPPTGPTGAWLRYKKQFITPDNVQNGVVFWNQYQDALNRAYQVYGVPPEIIVGIIGVE 159
Cdd:PRK10760 81 ILSQAKRLDWVLRLMDRQAPTTRPPSGPNGAWLRYRKKFITPDNVQNGVVFWNQYEDALNRAWQVYGVPPEIIVGIIGVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 160 TRWGRVMGKTRILDALATLSFSYPRRAEYFSSELETFLLMARSESDDPLDLKGSFAGAMGYGQFMPSSYKQYAVDFNGDG 239
Cdd:PRK10760 161 TRWGRVMGKTRILDALATLSFNYPRRAEYFSGELETFLLMARDEGDDPLNLRGSFAGAMGYGQFMPSSFKQYAVDFNGDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 240 HINLWDPVDAIGSVANYFKQHGWVSGDLVAVQALGQAPGLENGFKTKYSVSQLAAAGLTPTQPLGNHQQASLLRLDVGTG 319
Cdd:PRK10760 241 HINLWDPVDAIGSVANYFKAHGWVKGDQVAVPANGQAPGLENGFKTRYSVSQLAAAGLTPQQPLGNHQQASLLRLDVGTG 320
|
330 340 350
....*....|....*....|....*....|....*....
gi 1396648831 320 YEYWYGLPNFYTITRYNHSTHYAMAVWQLGLAVSQARGG 358
Cdd:PRK10760 321 YQYWYGLPNFYTITRYNHSTHYAMAVWQLGQAVALARVG 359
|
|
| MltB |
TIGR02282 |
lytic murein transglycosylase B; This family consists of lytic murein transglycosylases ... |
60-352 |
9.95e-157 |
|
lytic murein transglycosylase B; This family consists of lytic murein transglycosylases (murein hydrolases) in the family of MltB, which is a membrane-bound lipoprotein in Escherichia coli. The N-terminal lipoprotein modification motif is conserved in about half the members of this family. The term Slt35 describes a naturally occurring soluble fragment of MltB. Members of this family never contain the putative peptidoglycan binding domain described by pfam01471, which is associated with several classes of bacterial cell wall lytic enzymes. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 274066 [Multi-domain] Cd Length: 290 Bit Score: 441.45 E-value: 9.95e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 60 AQFIDKMVAKHGFDRQQLQEILSQAKRLDYVLRLMDrqaptglPPTGPTGAWLRYKKQFITPDNVQNGVVFWNQYQDALN 139
Cdd:TIGR02282 1 QAFIDTLVAKHGFDRAQLEAILAQAKYNDEVIRLID-------NPAESAKPWLEYRGIFITPKRIQDGVEFWKQHEDALN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 140 RAYQVYGVPPEIIVGIIGVETRWGRVMGKTRILDALATLSFSYPRRAEYFSSELETFLLMARSESDDPLDLKGSFAGAMG 219
Cdd:TIGR02282 74 RAEQRYGVPPEIIVAIIGVETNYGRNMGKYRVLDALTTLAFDYPRRATFFRGELGQFLLLAREEQLDPLTLKGSYAGAMG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 220 YGQFMPSSYKQYAVDFNGDGHINLWD-PVDAIGSVANYFKQHGWVSGDLVAVQALGQAPG--LENGF-KTKYSVSQLAAA 295
Cdd:TIGR02282 154 YPQFMPSSYRQYAVDFDGDGHIDLWNsPDDAIGSVANYFHAHGWVRGDPVAVPATGAAPGdqLPNKFaKPHYSLSQLAAA 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1396648831 296 GLTPTQPLGNHQQASLLRLDVGTGYEYWYGLPNFYTITRYNHSTHYAMAVWQLGLAV 352
Cdd:TIGR02282 234 GLIPQAPLGNEQKASLVDLDVGGGDQYWLGLPNFYAITRYNRSTFYAMAVYQLSQAL 290
|
|
| MltB |
COG2951 |
Membrane-bound lytic murein transglycosylase B [Cell wall/membrane/envelope biogenesis]; |
48-358 |
2.74e-137 |
|
Membrane-bound lytic murein transglycosylase B [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442193 [Multi-domain] Cd Length: 326 Bit Score: 393.38 E-value: 2.74e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 48 QMGGDFANNpaAAQFiDKMVAKHGFDRQQLQEILSQAKRLDYVLRLMDRQAPTGLPptgptgaWLRYKKQFITPDNVQNG 127
Cdd:COG2951 23 AAAADFAAW--VAAF-RQEAAAAGISRATLDAALAGATPDPRVIELDRRQPEFTKP-------WWDYLARFVSPARIARG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 128 VVFWNQYQDALNRAYQVYGVPPEIIVGIIGVETRWGRVMGKTRILDALATLSFSYpRRAEYFSSELETFLLMARSESDDP 207
Cdd:COG2951 93 RAFLRQHAALLARIEQRYGVPAEIIVAIWGVETNYGRYMGNFPVLDALATLAFDG-RRAEFFRGELIAALKILQRGDIDP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 208 LDLKGSFAGAMGYGQFMPSSYKQYAVDFNGDGHINLW-DPVDAIGSVANYFKQHGWVSGDLVAVQALGQA--PGLENGFK 284
Cdd:COG2951 172 DQMKGSWAGAMGQTQFMPSSYLRYAVDFDGDGRRDLWnSPPDALASTANYLKKHGWQRGQPWGYEVRLPAgfDYALAGLK 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1396648831 285 TKYSVSQLAAAGLTPT--QPLGNHQQASLLRLDVGTGYeYWYGLPNFYTITRYNHSTHYAMAVWQLGLAVSQARGG 358
Cdd:COG2951 252 PRRTLAEWAALGVRPAdgRPLPADGPASLLLPAGANGP-AFLVTPNFYVITRYNRSDLYALAVGHLADRIAGAFVA 326
|
|
| SLT_2 |
pfam13406 |
Transglycosylase SLT domain; This family is related to the SLT domain pfam01464. |
54-349 |
1.83e-118 |
|
Transglycosylase SLT domain; This family is related to the SLT domain pfam01464.
Pssm-ID: 404311 [Multi-domain] Cd Length: 292 Bit Score: 344.53 E-value: 1.83e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 54 ANNPAAAQFiDKMVAKHGFDRQQLQEILSQAKRLDYVLRLMDRQAPTGLPptgptgaWLRYKKQFITPDNVQNGVVFWNQ 133
Cdd:pfam13406 1 GFDAWVAAF-RQEAAAAGISRATLDAAFAGVEPDPRVIELDRRQPEFTKP-------WWDYLSRFVTPARIARGRAFLQE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 134 YQDALNRAYQVYGVPPEIIVGIIGVETRWGRVMGKTRILDALATLSFSYpRRAEYFSSELETFLLMARSESDDPLDLKGS 213
Cdd:pfam13406 73 HAALLARIEKRYGVPPEIIVAIWGVETNYGRYMGNFPVLDALATLAFDG-RRSEFFRKELIAALKILDRGDLDPEQLKGS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 214 FAGAMGYGQFMPSSYKQYAVDFNGDGHINLWD-PVDAIGSVANYFKQHGWVSGDLVAVQAL--GQAPGLENGFKTKYSVS 290
Cdd:pfam13406 152 WAGAMGQTQFMPSSYLAYAVDFDGDGRRDLWNsPPDALASVANYLKQHGWQPGEPWGREVRlpAGFDYSLAGLGTRKPLA 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1396648831 291 QLAAAGLTPT--QPLGNHQQASLLRLDVGTGyEYWYGLPNFYTITRYNHSTHYAMAVWQLG 349
Cdd:pfam13406 232 EWAALGVRPAdgGPPLADAEASLLLPAGANG-PAFLVYDNFYVITRYNRSDLYALAVGHLA 291
|
|
| Slt35-like |
cd13399 |
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ... |
145-348 |
5.53e-30 |
|
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: 110.86 E-value: 5.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 145 YGVPPEIIVGIIGVETRWGRVMGktrildalatlsfsyprraeyfsseletfllmarsesddpldlkGSFAGAMGYGQFM 224
Cdd:cd13399 1 YGVPPGILAAILGVESGFGPNAG--------------------------------------------GSPAGAQGIAQFM 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 225 PSSYKQYAVDFNGDGHINLWDPVDAIGSVANYFKQHGWVSGDlvavqalgqapglengfktkysvsqlaaagltptqplg 304
Cdd:cd13399 37 PSTWKAYGVDGNGDGKADPFNPEDAIASAANYLCRHGWDLNA-------------------------------------- 78
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1396648831 305 nhqqasllrldvgtgyeyWYGLPNFYTITRYNHST-HYAMAVWQL 348
Cdd:cd13399 79 ------------------FLGEDNFLALAAYNAGPgAYANAVLEL 105
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10760 |
PRK10760 |
murein hydrolase B; Provisional |
1-358 |
0e+00 |
|
murein hydrolase B; Provisional
Pssm-ID: 236754 [Multi-domain] Cd Length: 359 Bit Score: 755.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 1 MLKRRYLALLPLCVLLAACSSKPK-TPAETEMASGTGGFLLEPQHNVMQMGGDFANNPAAAQFIDKMVAKHGFDRQQLQE 79
Cdd:PRK10760 1 MFMRRYVALLPLFVLLAACSSKPKpTETATTTGTPSGGFLLEPQHNVMQMGGDFANNPNAQQFIDKMVNKHGFDRQQLHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 80 ILSQAKRLDYVLRLMDRQAPTGLPPTGPTGAWLRYKKQFITPDNVQNGVVFWNQYQDALNRAYQVYGVPPEIIVGIIGVE 159
Cdd:PRK10760 81 ILSQAKRLDWVLRLMDRQAPTTRPPSGPNGAWLRYRKKFITPDNVQNGVVFWNQYEDALNRAWQVYGVPPEIIVGIIGVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 160 TRWGRVMGKTRILDALATLSFSYPRRAEYFSSELETFLLMARSESDDPLDLKGSFAGAMGYGQFMPSSYKQYAVDFNGDG 239
Cdd:PRK10760 161 TRWGRVMGKTRILDALATLSFNYPRRAEYFSGELETFLLMARDEGDDPLNLRGSFAGAMGYGQFMPSSFKQYAVDFNGDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 240 HINLWDPVDAIGSVANYFKQHGWVSGDLVAVQALGQAPGLENGFKTKYSVSQLAAAGLTPTQPLGNHQQASLLRLDVGTG 319
Cdd:PRK10760 241 HINLWDPVDAIGSVANYFKAHGWVKGDQVAVPANGQAPGLENGFKTRYSVSQLAAAGLTPQQPLGNHQQASLLRLDVGTG 320
|
330 340 350
....*....|....*....|....*....|....*....
gi 1396648831 320 YEYWYGLPNFYTITRYNHSTHYAMAVWQLGLAVSQARGG 358
Cdd:PRK10760 321 YQYWYGLPNFYTITRYNHSTHYAMAVWQLGQAVALARVG 359
|
|
| MltB |
TIGR02282 |
lytic murein transglycosylase B; This family consists of lytic murein transglycosylases ... |
60-352 |
9.95e-157 |
|
lytic murein transglycosylase B; This family consists of lytic murein transglycosylases (murein hydrolases) in the family of MltB, which is a membrane-bound lipoprotein in Escherichia coli. The N-terminal lipoprotein modification motif is conserved in about half the members of this family. The term Slt35 describes a naturally occurring soluble fragment of MltB. Members of this family never contain the putative peptidoglycan binding domain described by pfam01471, which is associated with several classes of bacterial cell wall lytic enzymes. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 274066 [Multi-domain] Cd Length: 290 Bit Score: 441.45 E-value: 9.95e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 60 AQFIDKMVAKHGFDRQQLQEILSQAKRLDYVLRLMDrqaptglPPTGPTGAWLRYKKQFITPDNVQNGVVFWNQYQDALN 139
Cdd:TIGR02282 1 QAFIDTLVAKHGFDRAQLEAILAQAKYNDEVIRLID-------NPAESAKPWLEYRGIFITPKRIQDGVEFWKQHEDALN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 140 RAYQVYGVPPEIIVGIIGVETRWGRVMGKTRILDALATLSFSYPRRAEYFSSELETFLLMARSESDDPLDLKGSFAGAMG 219
Cdd:TIGR02282 74 RAEQRYGVPPEIIVAIIGVETNYGRNMGKYRVLDALTTLAFDYPRRATFFRGELGQFLLLAREEQLDPLTLKGSYAGAMG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 220 YGQFMPSSYKQYAVDFNGDGHINLWD-PVDAIGSVANYFKQHGWVSGDLVAVQALGQAPG--LENGF-KTKYSVSQLAAA 295
Cdd:TIGR02282 154 YPQFMPSSYRQYAVDFDGDGHIDLWNsPDDAIGSVANYFHAHGWVRGDPVAVPATGAAPGdqLPNKFaKPHYSLSQLAAA 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1396648831 296 GLTPTQPLGNHQQASLLRLDVGTGYEYWYGLPNFYTITRYNHSTHYAMAVWQLGLAV 352
Cdd:TIGR02282 234 GLIPQAPLGNEQKASLVDLDVGGGDQYWLGLPNFYAITRYNRSTFYAMAVYQLSQAL 290
|
|
| MltB |
COG2951 |
Membrane-bound lytic murein transglycosylase B [Cell wall/membrane/envelope biogenesis]; |
48-358 |
2.74e-137 |
|
Membrane-bound lytic murein transglycosylase B [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442193 [Multi-domain] Cd Length: 326 Bit Score: 393.38 E-value: 2.74e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 48 QMGGDFANNpaAAQFiDKMVAKHGFDRQQLQEILSQAKRLDYVLRLMDRQAPTGLPptgptgaWLRYKKQFITPDNVQNG 127
Cdd:COG2951 23 AAAADFAAW--VAAF-RQEAAAAGISRATLDAALAGATPDPRVIELDRRQPEFTKP-------WWDYLARFVSPARIARG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 128 VVFWNQYQDALNRAYQVYGVPPEIIVGIIGVETRWGRVMGKTRILDALATLSFSYpRRAEYFSSELETFLLMARSESDDP 207
Cdd:COG2951 93 RAFLRQHAALLARIEQRYGVPAEIIVAIWGVETNYGRYMGNFPVLDALATLAFDG-RRAEFFRGELIAALKILQRGDIDP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 208 LDLKGSFAGAMGYGQFMPSSYKQYAVDFNGDGHINLW-DPVDAIGSVANYFKQHGWVSGDLVAVQALGQA--PGLENGFK 284
Cdd:COG2951 172 DQMKGSWAGAMGQTQFMPSSYLRYAVDFDGDGRRDLWnSPPDALASTANYLKKHGWQRGQPWGYEVRLPAgfDYALAGLK 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1396648831 285 TKYSVSQLAAAGLTPT--QPLGNHQQASLLRLDVGTGYeYWYGLPNFYTITRYNHSTHYAMAVWQLGLAVSQARGG 358
Cdd:COG2951 252 PRRTLAEWAALGVRPAdgRPLPADGPASLLLPAGANGP-AFLVTPNFYVITRYNRSDLYALAVGHLADRIAGAFVA 326
|
|
| SLT_2 |
pfam13406 |
Transglycosylase SLT domain; This family is related to the SLT domain pfam01464. |
54-349 |
1.83e-118 |
|
Transglycosylase SLT domain; This family is related to the SLT domain pfam01464.
Pssm-ID: 404311 [Multi-domain] Cd Length: 292 Bit Score: 344.53 E-value: 1.83e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 54 ANNPAAAQFiDKMVAKHGFDRQQLQEILSQAKRLDYVLRLMDRQAPTGLPptgptgaWLRYKKQFITPDNVQNGVVFWNQ 133
Cdd:pfam13406 1 GFDAWVAAF-RQEAAAAGISRATLDAAFAGVEPDPRVIELDRRQPEFTKP-------WWDYLSRFVTPARIARGRAFLQE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 134 YQDALNRAYQVYGVPPEIIVGIIGVETRWGRVMGKTRILDALATLSFSYpRRAEYFSSELETFLLMARSESDDPLDLKGS 213
Cdd:pfam13406 73 HAALLARIEKRYGVPPEIIVAIWGVETNYGRYMGNFPVLDALATLAFDG-RRSEFFRKELIAALKILDRGDLDPEQLKGS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 214 FAGAMGYGQFMPSSYKQYAVDFNGDGHINLWD-PVDAIGSVANYFKQHGWVSGDLVAVQAL--GQAPGLENGFKTKYSVS 290
Cdd:pfam13406 152 WAGAMGQTQFMPSSYLAYAVDFDGDGRRDLWNsPPDALASVANYLKQHGWQPGEPWGREVRlpAGFDYSLAGLGTRKPLA 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1396648831 291 QLAAAGLTPT--QPLGNHQQASLLRLDVGTGyEYWYGLPNFYTITRYNHSTHYAMAVWQLG 349
Cdd:pfam13406 232 EWAALGVRPAdgGPPLADAEASLLLPAGANG-PAFLVYDNFYVITRYNRSDLYALAVGHLA 291
|
|
| MltB_2 |
TIGR02283 |
lytic murein transglycosylase; Members of this family are closely related to the MltB family ... |
60-345 |
3.48e-57 |
|
lytic murein transglycosylase; Members of this family are closely related to the MltB family lytic murein transglycosylases described by TIGR02282 and are likewise all proteobacterial, although that family and this one form clearly distinct clades. Several species have one member of each family. Many members of this family (unlike the MltB family) contain an additional C-terminal domain, a putative peptidoglycan binding domain (pfam01471), not included in region described by this model. Many sequences appear to contain N-terminal lipoprotein attachment sites, as does E. coli MltB in TIGR02282. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 274067 [Multi-domain] Cd Length: 300 Bit Score: 187.97 E-value: 3.48e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 60 AQFIDKMVAKhGFDRQQLQEILSQAKRLD-YVLRLMDRQAPTGLPPTgptgawlRYKKQFITPDNVQNGVVFWNQYQDAL 138
Cdd:TIGR02283 7 AQLRAEAAAK-GISAATFDRAFAGIKEPDqSVLNLDRNQPEFTQTFW-------DYLSRRVSPRRIAIGRAMLQRYAALL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 139 NRAYQVYGVPPEIIVGIIGVETRWGRVMGKTRILDALATLSFSyPRRAEYFSSELETFLLMARSESDDPLDLKGSFAGAM 218
Cdd:TIGR02283 79 ARIEKRYGVPAEILLAIWGMESDFGAYQGKFDVIRSLATLAYD-GRRKDYFRTELIAALKILQRGDLTRAAMKGSWAGAM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 219 GYGQFMPSSYKQYAVDFNGDGHINLW-DPVDAIGSVANYFKQHGWVSGD--LVAVQALGQAPGLENGFKTKYSVSQLAAA 295
Cdd:TIGR02283 158 GQTQFLPSSYLNYAVDFDGDGRRDIWnSVPDALASTANYLVNGGWKRGEpwGYEVQLPAGFDYALSGSQIKKPIAEWQRL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1396648831 296 GLTPT--QPLGN---HQQASLLRLDVGTGYEYwYGLPNFYTITRYNHSTHYAMAV 345
Cdd:TIGR02283 238 GVTRVdgRPLPAsaaNAEASLLLPDGRKGPAF-LVTPNFRVIKEWNRSDYYALTI 291
|
|
| Slt35-like |
cd13399 |
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ... |
145-348 |
5.53e-30 |
|
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: 110.86 E-value: 5.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 145 YGVPPEIIVGIIGVETRWGRVMGktrildalatlsfsyprraeyfsseletfllmarsesddpldlkGSFAGAMGYGQFM 224
Cdd:cd13399 1 YGVPPGILAAILGVESGFGPNAG--------------------------------------------GSPAGAQGIAQFM 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 225 PSSYKQYAVDFNGDGHINLWDPVDAIGSVANYFKQHGWVSGDlvavqalgqapglengfktkysvsqlaaagltptqplg 304
Cdd:cd13399 37 PSTWKAYGVDGNGDGKADPFNPEDAIASAANYLCRHGWDLNA-------------------------------------- 78
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1396648831 305 nhqqasllrldvgtgyeyWYGLPNFYTITRYNHST-HYAMAVWQL 348
Cdd:cd13399 79 ------------------FLGEDNFLALAAYNAGPgAYANAVLEL 105
|
|
| Lyz-like |
cd00442 |
lysozyme-like domains; This family contains several members, including soluble lytic ... |
197-256 |
9.68e-07 |
|
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: 45.48 E-value: 9.68e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1396648831 197 LLMARSES-DDPLDLKGSFAGAMGYGQFMPSSYKQYAvdfnGDGHINLWDPVDAIGSVANY 256
Cdd:cd00442 3 AAIIGQESgGNKPANAGSGSGAAGLFQFMPGTWKAYG----KNSSSDLNDPEASIEAAAKY 59
|
|
| LT-like |
cd00254 |
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ... |
199-260 |
3.12e-05 |
|
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: 42.59 E-value: 3.12e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1396648831 199 MARSESD-DPLdlKGSFAGAMGYGQFMPSSykqyAVDFNGDGHINLWDPVDAIGSVANYFKQH 260
Cdd:cd00254 7 VIRVESGfNPR--AVSPAGARGLMQLMPGT----ARDLGRRGVDDLFDPEENIRAGARYLREL 63
|
|
| MltE |
COG0741 |
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ... |
130-250 |
1.46e-03 |
|
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: 39.59 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648831 130 FWNQYQDALNRAYQVYGVPPEIIVGIIGVETRWgrvmgktrilDALATlsfsyprraeyfsseletfllmarsesddpld 209
Cdd:COG0741 99 RPLPYLPLIEEAAKKYGVDPALVLALIRQESAF----------NPNAV-------------------------------- 136
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1396648831 210 lkgSFAGAMGYGQFMPSSYKQYAVDFN-GDGHINLWDPVDAI 250
Cdd:COG0741 137 ---SPAGARGLMQLMPATARRLGLKLGlGPSPDDLFDPETNI 175
|
|
| GEWL |
cd01021 |
Goose egg-white lysozyme; Eukaryotic goose-type or G-type lysozyme (goose egg-white lysozyme; ... |
132-168 |
4.77e-03 |
|
Goose egg-white lysozyme; Eukaryotic goose-type or G-type lysozyme (goose egg-white lysozyme; GEWL) catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc). Mammals have two lysozymes. This family corresponds to human and mouse lysozyme G-like protein 2.
Pssm-ID: 381601 [Multi-domain] Cd Length: 174 Bit Score: 37.58 E-value: 4.77e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1396648831 132 NQYQDALNRAYQVYGVPPEIIVGIIGVETRWGRVMGK 168
Cdd:cd01021 35 NKYKDCIKQVGKKLCIDPALIAAIISRESRAGAALDK 71
|
|
| |
