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Conserved domains on  [gi|489959120|ref|WP_003862427|]
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MULTISPECIES: membrane-bound lytic murein transglycosylase MltC [Enterobacter]

Protein Classification

membrane-bound lytic murein transglycosylase C( domain architecture ID 11485457)

membrane-bound lytic murein transglycosylase C catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine residues

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
mltC PRK11671
membrane-bound lytic murein transglycosylase MltC;
16-358 0e+00

membrane-bound lytic murein transglycosylase MltC;


:

Pssm-ID: 183271 [Multi-domain]  Cd Length: 359  Bit Score: 754.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120  16 SC-SSKKGDEYNEAWVKDTNGFDILMGQFAHNIENIWGFNEVLIAGPKDYVKYTDAYQTRSHINFDDGTITVETIAGTEP 94
Cdd:PRK11671  16 SCsSTKKGDTYNEAWVKDTNGFDILMGQFAHNIENIWGFNEVLIAGPKDYVKYTDQYQTRSHINFDDGTITIETIAGTNP 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120  95 AAHLRQAIIKTLLMGDDPGSIDLYSDADDITISKEPFLYGQVVDQTGQPIRWEGRATKFADYLLQTRLKSRTNGLKVIYS 174
Cdd:PRK11671  96 AAHLRQAIIKTLLMGDDPGSIDLYSDVDDIPISKEPFLYGQVLDNTGQPIRWEGRASNFADYLLQNKLQSRSNGLRIIYS 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120 175 VTINLVPNHLDKRAHKYLGMVRQASRKYGVDESLILAIMQTESSFNPYAVSRSDALGLMQVVQHSAGKDVFRAQGKSGTP 254
Cdd:PRK11671 176 VTINMVPNHLDKRAHKYLPMVRKASRKYGVDESLILAIMQTESSFNPYAVSRSDALGLMQVVQHTAGKDVFRMKGKSGQP 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120 255 SRSYLFDPQSNIDTGTAYLAMLNNVYLGGIDNPTSRRYAVITAYNGGAGSVLRVFSNDKVQAANIINSMAPGDVYATLTT 334
Cdd:PRK11671 256 SRSYLFDPANNIDTGTAYLAILQNVYLGGITNPTSRRYAVITAYNGGAGSVLRVFSNDKIQAANIINTMSPGDVYQTLTT 335

                        330       340
                 ....*....|....*....|....
gi 489959120 335 RHPSAESRRYLYKVNTAQKNYRRR 358
Cdd:PRK11671 336 RHPSAESRRYLYKVNTAQKSYRRR 359
 
Name Accession Description Interval E-value
mltC PRK11671
membrane-bound lytic murein transglycosylase MltC;
16-358 0e+00

membrane-bound lytic murein transglycosylase MltC;


Pssm-ID: 183271 [Multi-domain]  Cd Length: 359  Bit Score: 754.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120  16 SC-SSKKGDEYNEAWVKDTNGFDILMGQFAHNIENIWGFNEVLIAGPKDYVKYTDAYQTRSHINFDDGTITVETIAGTEP 94
Cdd:PRK11671  16 SCsSTKKGDTYNEAWVKDTNGFDILMGQFAHNIENIWGFNEVLIAGPKDYVKYTDQYQTRSHINFDDGTITIETIAGTNP 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120  95 AAHLRQAIIKTLLMGDDPGSIDLYSDADDITISKEPFLYGQVVDQTGQPIRWEGRATKFADYLLQTRLKSRTNGLKVIYS 174
Cdd:PRK11671  96 AAHLRQAIIKTLLMGDDPGSIDLYSDVDDIPISKEPFLYGQVLDNTGQPIRWEGRASNFADYLLQNKLQSRSNGLRIIYS 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120 175 VTINLVPNHLDKRAHKYLGMVRQASRKYGVDESLILAIMQTESSFNPYAVSRSDALGLMQVVQHSAGKDVFRAQGKSGTP 254
Cdd:PRK11671 176 VTINMVPNHLDKRAHKYLPMVRKASRKYGVDESLILAIMQTESSFNPYAVSRSDALGLMQVVQHTAGKDVFRMKGKSGQP 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120 255 SRSYLFDPQSNIDTGTAYLAMLNNVYLGGIDNPTSRRYAVITAYNGGAGSVLRVFSNDKVQAANIINSMAPGDVYATLTT 334
Cdd:PRK11671 256 SRSYLFDPANNIDTGTAYLAILQNVYLGGITNPTSRRYAVITAYNGGAGSVLRVFSNDKIQAANIINTMSPGDVYQTLTT 335

                        330       340
                 ....*....|....*....|....
gi 489959120 335 RHPSAESRRYLYKVNTAQKNYRRR 358
Cdd:PRK11671 336 RHPSAESRRYLYKVNTAQKSYRRR 359
Mltc_N pfam11873
Membrane-bound lytic murein transglycosylase C, N-terminal domain; This domain is found ...
 29-190 1.70e-98

Membrane-bound lytic murein transglycosylase C, N-terminal domain; This domain is found associated with pfam01464. It is the N-terminal structural domain of MltC (Membrane-bound lytic murein transglycosylase C), one of the seven lytic transglycosylases found in the genome of the Gram-negative bacterium Escherichia coli. The role of the N-terminal domain is suggested to be important not as a mere structural extension of the active site beyond what is seen in other lytic transglycosylases but one that creates a peptide-binding site at position +2.


Pssm-ID: 432150  Cd Length: 161  Bit Score: 288.76  E-value: 1.70e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120   29 WVKDTNGFDILMGQFAHNIENIWGFNEVLIAGPKDYVKYTDAYQTRSHINFDDGTITVETIAGTEPAAHLRQAIIKTLLM 108
Cdd:pfam11873   1 FAKDTNALDILVGQFSGNIEKIWGKNEVLVASKKDYVKYTDNYKSRAHIDFDKGIITIETLATKNPKAHLRNAIITTLLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120  109 GDDPGSIDLYSDAdDITISKEPFLYGQVVDQTGQPIRWEGRATKFADYLLQTRLKSRTNGLKVIYSVTINLVPNHLDKRA 188
Cdd:pfam11873  81 PDDPSDVDLYSDK-DIELSGKPFLYGQVLDQDGQPIRWEWRANRFADYLIKNKLKTRKKNGKKVYYVSIPMVANHLDQRA 159


                  ..
gi 489959120  189 HK 190
Cdd:pfam11873 160 YK 161
LT_MltC_MltE cd16893
membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and ...
 194-353 2.75e-97

membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and MltE are periplasmic, outer membrane attached lytic transglycosylases (LTs), which cleave beta-1,4-glycosidic bonds joining N-acetylmuramic acid and N-acetylglucosamine in the cell wall peptidoglycan, yielding 1,6-anhydromuropeptides. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda


Pssm-ID: 381614 [Multi-domain]  Cd Length: 162  Bit Score: 285.61  E-value: 2.75e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120 194 MVRQASRKYGVDESLILAIMQTESSFNPYAVSRSDALGLMQVVQHSAGKDVFR-AQGKSGTPSRSYLFDPQSNIDTGTAY 272
Cdd:cd16893    2 IVEKYAKKYGVDPALILAIIETESSFNPYAVSHSPAYGLMQIVPSTAGRDVYRlLGGKGGLPSKSYLFDPENNIDIGTAY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120 273 LAMLNNVYLGGIDNPTSRRYAVITAYNGGAGSVLRVFSNDKVQAANIINSMAPGDVYATLTTRHPSAESRRYLYKVNTAQ 352
Cdd:cd16893   82 LHILQNRYLKGIKNPKSREYCAIAAYNGGAGNVLRTFSSDRKKAISKINRLSPDEVYQHLTKKLPAAETRNYLKKVLKAK 161


                 .
gi 489959120 353 K 353
Cdd:cd16893  162 K 162
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 186-358 1.37e-44

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: 153.61  E-value: 1.37e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120 186 KRAHKYLGMVRQASRKYGVDESLILAIMQTESSFNPYAVSRSDALGLMQVVqHSAGKDVFRAQGKSgtPSRSYLFDPQSN 265
Cdd:COG0741   98 RRPLPYLPLIEEAAKKYGVDPALVLALIRQESAFNPNAVSPAGARGLMQLM-PATARRLGLKLGLG--PSPDDLFDPETN 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120 266 IDTGTAYLAMLNNVYLGgidnptsRRYAVITAYNGGAGSVLRVFSNDKVQAANIInsmapgdvyatlttrhPSAESRRYL 345
Cdd:COG0741  175 IRAGAAYLRELLDRFDG-------DLVLALAAYNAGPGRVRRWLRRNGDRDGEII----------------PYAETRNYV 231

                        170
                 ....*....|...
gi 489959120 346 YKVNTAQKNYRRR 358
Cdd:COG0741  232 KKVLANYAIYRAG 244
 
Name Accession Description Interval E-value
mltC PRK11671
membrane-bound lytic murein transglycosylase MltC;
16-358 0e+00

membrane-bound lytic murein transglycosylase MltC;


Pssm-ID: 183271 [Multi-domain]  Cd Length: 359  Bit Score: 754.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120  16 SC-SSKKGDEYNEAWVKDTNGFDILMGQFAHNIENIWGFNEVLIAGPKDYVKYTDAYQTRSHINFDDGTITVETIAGTEP 94
Cdd:PRK11671  16 SCsSTKKGDTYNEAWVKDTNGFDILMGQFAHNIENIWGFNEVLIAGPKDYVKYTDQYQTRSHINFDDGTITIETIAGTNP 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120  95 AAHLRQAIIKTLLMGDDPGSIDLYSDADDITISKEPFLYGQVVDQTGQPIRWEGRATKFADYLLQTRLKSRTNGLKVIYS 174
Cdd:PRK11671  96 AAHLRQAIIKTLLMGDDPGSIDLYSDVDDIPISKEPFLYGQVLDNTGQPIRWEGRASNFADYLLQNKLQSRSNGLRIIYS 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120 175 VTINLVPNHLDKRAHKYLGMVRQASRKYGVDESLILAIMQTESSFNPYAVSRSDALGLMQVVQHSAGKDVFRAQGKSGTP 254
Cdd:PRK11671 176 VTINMVPNHLDKRAHKYLPMVRKASRKYGVDESLILAIMQTESSFNPYAVSRSDALGLMQVVQHTAGKDVFRMKGKSGQP 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120 255 SRSYLFDPQSNIDTGTAYLAMLNNVYLGGIDNPTSRRYAVITAYNGGAGSVLRVFSNDKVQAANIINSMAPGDVYATLTT 334
Cdd:PRK11671 256 SRSYLFDPANNIDTGTAYLAILQNVYLGGITNPTSRRYAVITAYNGGAGSVLRVFSNDKIQAANIINTMSPGDVYQTLTT 335

                        330       340
                 ....*....|....*....|....
gi 489959120 335 RHPSAESRRYLYKVNTAQKNYRRR 358
Cdd:PRK11671 336 RHPSAESRRYLYKVNTAQKSYRRR 359
Mltc_N pfam11873
Membrane-bound lytic murein transglycosylase C, N-terminal domain; This domain is found ...
 29-190 1.70e-98

Membrane-bound lytic murein transglycosylase C, N-terminal domain; This domain is found associated with pfam01464. It is the N-terminal structural domain of MltC (Membrane-bound lytic murein transglycosylase C), one of the seven lytic transglycosylases found in the genome of the Gram-negative bacterium Escherichia coli. The role of the N-terminal domain is suggested to be important not as a mere structural extension of the active site beyond what is seen in other lytic transglycosylases but one that creates a peptide-binding site at position +2.


Pssm-ID: 432150  Cd Length: 161  Bit Score: 288.76  E-value: 1.70e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120   29 WVKDTNGFDILMGQFAHNIENIWGFNEVLIAGPKDYVKYTDAYQTRSHINFDDGTITVETIAGTEPAAHLRQAIIKTLLM 108
Cdd:pfam11873   1 FAKDTNALDILVGQFSGNIEKIWGKNEVLVASKKDYVKYTDNYKSRAHIDFDKGIITIETLATKNPKAHLRNAIITTLLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120  109 GDDPGSIDLYSDAdDITISKEPFLYGQVVDQTGQPIRWEGRATKFADYLLQTRLKSRTNGLKVIYSVTINLVPNHLDKRA 188
Cdd:pfam11873  81 PDDPSDVDLYSDK-DIELSGKPFLYGQVLDQDGQPIRWEWRANRFADYLIKNKLKTRKKNGKKVYYVSIPMVANHLDQRA 159


                  ..
gi 489959120  189 HK 190
Cdd:pfam11873 160 YK 161
LT_MltC_MltE cd16893
membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and ...
 194-353 2.75e-97

membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and MltE are periplasmic, outer membrane attached lytic transglycosylases (LTs), which cleave beta-1,4-glycosidic bonds joining N-acetylmuramic acid and N-acetylglucosamine in the cell wall peptidoglycan, yielding 1,6-anhydromuropeptides. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda


Pssm-ID: 381614 [Multi-domain]  Cd Length: 162  Bit Score: 285.61  E-value: 2.75e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120 194 MVRQASRKYGVDESLILAIMQTESSFNPYAVSRSDALGLMQVVQHSAGKDVFR-AQGKSGTPSRSYLFDPQSNIDTGTAY 272
Cdd:cd16893    2 IVEKYAKKYGVDPALILAIIETESSFNPYAVSHSPAYGLMQIVPSTAGRDVYRlLGGKGGLPSKSYLFDPENNIDIGTAY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120 273 LAMLNNVYLGGIDNPTSRRYAVITAYNGGAGSVLRVFSNDKVQAANIINSMAPGDVYATLTTRHPSAESRRYLYKVNTAQ 352
Cdd:cd16893   82 LHILQNRYLKGIKNPKSREYCAIAAYNGGAGNVLRTFSSDRKKAISKINRLSPDEVYQHLTKKLPAAETRNYLKKVLKAK 161


                 .
gi 489959120 353 K 353
Cdd:cd16893  162 K 162
emtA PRK15470
membrane-bound lytic murein transglycosylase EmtA;
186-351 5.19e-45

membrane-bound lytic murein transglycosylase EmtA;


Pssm-ID: 185367 [Multi-domain]  Cd Length: 203  Bit Score: 153.20  E-value: 5.19e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120 186 KRAHKYLGMVRQASRKYGVDESLILAIMQTESSFNPYAVSRSDALGLMQVVQHSAGKDVFRAQGKSGTPSRSYLFDPQSN 265
Cdd:PRK15470  34 QRAMQWMPISQKAGAAWGVDPQLITAIIAIESGGNPNAVSKSNAIGLMQLKASTSGRDVYRRMGWSGEPTTSELKNPERN 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120 266 IDTGTAYLAMLNNVYLGGIDNPTSRRYAVITAYNGGAGSVLRVFSNDKVQAANIINSMAPGDVYATLTTRHPSAESRRYL 345
Cdd:PRK15470 114 ISMGAAYLNILETGPLAGIEDPKVLQYALVVSYANGAGALLRTFSSDRKKAISKINDLDADEFLEHVARNHPAPQAPRYI 193


                 ....*.
gi 489959120 346 YKVNTA 351
Cdd:PRK15470 194 YKLEQA 199
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 186-358 1.37e-44

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: 153.61  E-value: 1.37e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120 186 KRAHKYLGMVRQASRKYGVDESLILAIMQTESSFNPYAVSRSDALGLMQVVqHSAGKDVFRAQGKSgtPSRSYLFDPQSN 265
Cdd:COG0741   98 RRPLPYLPLIEEAAKKYGVDPALVLALIRQESAFNPNAVSPAGARGLMQLM-PATARRLGLKLGLG--PSPDDLFDPETN 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120 266 IDTGTAYLAMLNNVYLGgidnptsRRYAVITAYNGGAGSVLRVFSNDKVQAANIInsmapgdvyatlttrhPSAESRRYL 345
Cdd:COG0741  175 IRAGAAYLRELLDRFDG-------DLVLALAAYNAGPGRVRRWLRRNGDRDGEII----------------PYAETRNYV 231

                        170
                 ....*....|...
gi 489959120 346 YKVNTAQKNYRRR 358
Cdd:COG0741  232 KKVLANYAIYRAG 244
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 195-320 2.01e-36

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: 127.81  E-value: 2.01e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120  195 VRQASRKYGVDESLILAIMQTESSFNPYAVSRSDALGLMQVVQHSAGKDVFRaqgksGTPSRSYLFDPQSNIDTGTAYLA 274
Cdd:pfam01464   1 IIKAAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLR-----VNPGVDDLFDPEKNIKAGTKYLK 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 489959120  275 MLNNVYLGgidnptsRRYAVITAYNGGAGSVLRVFSNDKVQAANII 320
Cdd:pfam01464  76 ELYKQYGG-------DLWLALAAYNAGPGRVRKWIKNAGAKDKKLL 114
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
 190-353 1.41e-29

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: 111.06  E-value: 1.41e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120 190 KYLGMVRQASRKYGVDESLILAIMQTESSFNPYAVSRSDALGLMQVVQhSAGKDVFRAQGKSGTpSRSYLFDPQSNIDTG 269
Cdd:cd16896    3 KYREYIEKYAKEYGVDPLLVAAVIKVESNFNPNAVSSKGAIGLMQIMP-ETAEWIAEKLGLEDF-SEDDLYDPETNIRLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120 270 TAYLAMLNNVYLGGIDnptsrryAVITAYNGGAGSVLR-----VFSNDKVQAANIinsmapgdvyatlttrhPSAESRRY 344
Cdd:cd16896   81 TWYLSYLLKEFDGNLV-------LALAAYNAGPGNVDKwlkdgGWSGDGKTLDQI-----------------PFPETRHY 136


                 ....*....
gi 489959120 345 LYKVNTAQK 353
Cdd:cd16896  137 VKKVLKNYK 145
Slt70-like cd13401
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ...
 191-305 5.42e-26

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: 101.40  E-value: 5.42e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120 191 YLGMVRQASRKYGVDESLILAIMQTESSFNPYAVSRSDALGLMQVVQhSAGKDVFRAQGKSgTPSRSYLFDPQSNIDTGT 270
Cdd:cd13401    6 YRDLVERAAKKNGLDPALVYAIIRQESAFDPDAVSPAGALGLMQLMP-ATAKDVAKKLGLP-YYSPRDLFDPEYNIRLGS 83

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489959120 271 AYLAMLNNVYLGgidnptSRRYAVItAYNGGAGSV 305
Cdd:cd13401   84 AYLAELLDRFDG------NPVLALA-AYNAGPGRV 111
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
 206-353 3.51e-21

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: 87.27  E-value: 3.51e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120 206 ESLILAIMQTESSFNPYAVSRSDALGLMQVVQHSAGKDVFRAQgksgtpsrSYLFDPQSNIDTGTAYLAMLNNVYLGGId 285
Cdd:cd00254    1 PALVLAVIRVESGFNPRAVSPAGARGLMQLMPGTARDLGRRGV--------DDLFDPEENIRAGARYLRELLDRFGGDL- 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489959120 286 nptsrrYAVITAYNGGAGSVlrvfsnDKVQAANIInsmapgdvyatlttrhPSAESRRYLYKVNTAQK 353
Cdd:cd00254   72 ------ELALAAYNAGPGAV------DRWGGGEVP----------------PYKETRNYVQRVLAYYQ 111
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
 182-307 5.75e-18

Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 84.34  E-value: 5.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120 182 NHLDKRAHKYLGMVRQASRKYGVDESLILAIMQTESSFNPYAVSRSDALGLMQVVQhSAGKDVfraqgksGTPSRsylFD 261
Cdd:COG4623  255 RRIEGRLPPYDPLFEKYAEEYGLDWRLLAALAYQESHWNPRARSPTGARGLMQLMP-ATAKEL-------GVDDR---LD 323

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 489959120 262 PQSNIDTGTAYLAMLNNVYLGGIDNPTsRRYAVITAYNGGAGSVLR 307
Cdd:COG4623  324 PEQSIRAGAKYLRWLYDRFPEAIDEPD-RWWFALAAYNAGPGHVQD 368
MLTF-like cd13403
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily ...
 195-307 1.16e-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: 70.64  E-value: 1.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120 195 VRQASRKYGVDESLILAIMQTESSFNPYAVSRSDALGLMQVvqhsagkdvfraqgksgTPS--RSY----LFDPQSNIDT 268
Cdd:cd13403    1 FKKYAEKYGFDWRLLAAQAYQESRFNPNARSPAGARGLMQL-----------------MPStaRELgvndRLDPEQNIHA 63

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489959120 269 GTAYLAMLNNVYLGGIDnPTSRRYAVITAYNGGAGSVLR 307
Cdd:cd13403   64 GAKYLRYLRDRFPPDID-EPDRLKFALAAYNAGPGHVRD 101
PRK11619 PRK11619
lytic murein transglycosylase; Provisional
 182-348 3.57e-11

lytic murein transglycosylase; Provisional


Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 64.31  E-value: 3.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120 182 NHLDKR---AHKYLgmVRQASRKYGVDESLILAIMQTESSFNPYAVSRSDALGLMQVVQHSAGKDVfRAQGKSGTPSRSY 258
Cdd:PRK11619 469 DHLEERfplAWNDE--FRRYTSGKGIPQSYAMAIARQESAWNPKARSPVGASGLMQIMPGTATHTV-KMFSIPGYSSSSQ 545

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120 259 LFDPQSNIDTGTAYlamLNNVYLGGIDNptsrRYAVITAYNGGAGSVLRVFSN--DKVQAANIINSMapgdvyatlttrh 336
Cdd:PRK11619 546 LLDPETNINIGTSY---LEYVYQQFGNN----RILASAAYNAGPGRVRTWLGNsaGRIDAVAFVESI------------- 605

                        170
                 ....*....|..
gi 489959120 337 PSAESRRYLYKV 348
Cdd:PRK11619 606 PFSETRGYVKNV 617
LT_IagB-like cd13400
Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like ...
 202-275 2.03e-09

Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like protein, similar to Escherichia coli invasion protein IagB. IagB is encoded within a pathogenicity island in Salmonella enterica and has been shown to degrade polymeric peptidoglycan. IagB-like invasion proteins are implicated in the invasion of eukaryotic host cells by bacteria. 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. Members of this family resemble the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda.


Pssm-ID: 381603 [Multi-domain]  Cd Length: 109  Bit Score: 54.46  E-value: 2.03e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489959120 202 YGVDESLILAIMQTESSFNPYAVSR----SDALGLMQV-VQHsagkdvFRAQGKSGTPSRSYLFDPQSNIDTGTAYLAM 275
Cdd:cd13400    1 YGVPPRLLRAIAKVESGFNPNAINRnkngSYDIGLMQInSIW------LPELARYGITREELLNDPCTNIYVGAWILAR 73
PHA00368 PHA00368
internal virion protein D
 189-282 2.52e-07

internal virion protein D


Pssm-ID: 222785 [Multi-domain]  Cd Length: 1315  Bit Score: 52.48  E-value: 2.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120  189 HKYLGMVRQASRKYGVDESLILAIMQTESSFNPYAVSRSDALGLMQVvqhsaGKDVFRAQGKSGTPSRSYlfDPQSNIDT 268
Cdd:PHA00368    9 SEYDGLFQKAADAHGVSYDLLRKVGWDESRFNPTAKSPTGPKGLMQF-----TKATAKALGLIVDDDDRL--DPELAIDA 81

                          90
                  ....*....|....
gi 489959120  269 GTAYLAMLNNVYLG 282
Cdd:PHA00368   82 GARYLADLVGKYDG 95
PRK15328 PRK15328
type III secretion system invasion protein IagB;
197-301 3.18e-05

type III secretion system invasion protein IagB;


Pssm-ID: 185228 [Multi-domain]  Cd Length: 160  Bit Score: 43.70  E-value: 3.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120 197 QASRKYGVDESLILAIMQTESSFNPYAVSR----SDALGLMQVvqHSAGkdvFRAQGKSGTPSRSYLFDPQSNIDTGTAY 272
Cdd:PRK15328  24 QAEKMFNIESELLYAIAQQESAMKPGAIGHnrdgSTDLGLMQI--NSFH---MKRLKKMGISEKQLLQDPCISVIVGASI 98

                         90       100
                 ....*....|....*....|....*....
gi 489959120 273 LAMLNNVYlggidnptSRRYAVITAYNGG 301
Cdd:PRK15328  99 LSDMMKIY--------GYSWEAVGAYNAG 119
Slt35-like cd13399
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ...
 202-234 4.48e-05

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: 42.30  E-value: 4.48e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 489959120 202 YGVDESLILAIMQTESSFNPYAV-SRSDALGLMQ 234
Cdd:cd13399    1 YGVPPGILAAILGVESGFGPNAGgSPAGAQGIAQ 34
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 200-347 6.26e-05

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: 42.12  E-value: 6.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120 200 RKYGVDESLI-LAImqTESSFNPYAVSRSDALGLMQvvqhsagkdvF-RAQGKS-GTPSRSYL---FDPQSNIDTGTAYL 273
Cdd:cd16894    2 LKEGLPEELKyLAL--VESGFNPDAVSSAGAAGLWQ----------FmPATAREyGLRVDSWVderRDPEKSTRAAARYL 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489959120 274 ----AMLNNVYLggidnptsrryaVITAYNGGAGSVLRVFSNDKVQAANIINSMapgdvyatlttrHPSAESRRYLYK 347
Cdd:cd16894   70 kdlyKRFGDWLL------------ALAAYNAGEGRVRRAIKRAGTDKWEDYYRL------------YLPAETRRYVPK 123
Lyz-like cd00442
lysozyme-like domains; This family contains several members, including soluble lytic ...
 209-272 3.61e-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: 38.16  E-value: 3.61e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489959120 209 ILAIMQTESSFNP--YAVSRSDALGLMQVVQhsagkDVFRAQGKSgtpSRSYLFDPQSNIDTGTAY 272
Cdd:cd00442    2 LAAIIGQESGGNKpaNAGSGSGAAGLFQFMP-----GTWKAYGKN---SSSDLNDPEASIEAAAKY 59
GEWL cd01021
Goose egg-white lysozyme; Eukaryotic goose-type or G-type lysozyme (goose egg-white lysozyme; ...
 186-305 6.28e-04

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: 40.28  E-value: 6.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120 186 KRAHKYLGMVRQASRKYGVDESLILAIMQTESSF-----NPYAVSRSDALGLMQVvqhsagkDVfRAQGKSGTPsrsylf 260
Cdd:cd01021   32 NRLNKYKDCIKQVGKKLCIDPALIAAIISRESRAgaaldKNGWGDHGNGFGLMQV-------DK-RYHPPKGAW------ 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489959120 261 DPQSNIDTGTAYLAmlnnVYLGGIDN--PT-SRRYAV---ITAYNGGAGSV 305
Cdd:cd01021   98 DSEEHIEQATGILI----DFIKTVQRkhPSwSPEQQLkggIAAYNAGVGNV 144
LT_TF-like cd13402
lytic transglycosylase-like domain of tail fiber-like proteins and similar domains; These tail ...
 208-305 1.20e-03

lytic transglycosylase-like domain of tail fiber-like proteins and similar domains; These tail fiber-like proteins are multi-domain proteins that include a lytic transglycosylase (LT) domain. Members of the LT family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, and the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL). 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: 381605 [Multi-domain]  Cd Length: 117  Bit Score: 38.33  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120 208 LILAIMQTESSFNPYAVSRSD--------ALGLMQVVQHSagkdvFRAQGKSGtpsrsY--LFDPQSNIdtgtayLAMLN 277
Cdd:cd13402    3 ALLRQIQTESGGNPNAINNWDsnakaghpSKGLMQVIPPT-----FAAYAPPG-----HgnILNPLDNI------LAAIN 66

                         90       100
                 ....*....|....*....|....*...
gi 489959120 278 NvylggidnpTSRRYAVITAYNGGAGSV 305
Cdd:cd13402   67 Y---------AKARYGSGFALAAGGGGG 85
LT_VirB1-like cd16892
VirB1-like subfamily; This subfamily includes VirB1 protein, one of twelve proteins making up ...
 203-317 1.29e-03

VirB1-like subfamily; This subfamily includes VirB1 protein, one of twelve proteins making up type IV secretion systems (T4SS). T4SS are macromolecular assemblies generally composed of VirB1-11 and VirD4 proteins, and are used by bacteria to transport material across their membranes. VirB1 acts as a lytic transglycosylase (LT), and is important with respect to piercing the peptidoglycan layer in the periplasm. 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, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).


Pssm-ID: 381613 [Multi-domain]  Cd Length: 143  Bit Score: 38.68  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120 203 GVDESLILAIMQTESSFNPYAV------------SRSDA---------------LGLMQV-VQHsagkdvFRAQGKSGtp 254
Cdd:cd16892    8 GVHPETLAAIVQVESGGNPYAIgvnggklsrqpkTKAEAiatarqliaaghnfdVGLGQInSRN------LARLGLTV-- 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489959120 255 srSYLFDPQSNIDTGTAYLAMLNNVYLGGIDNPTSRRYAVITAYNggAGSVLRVFSN---DKVQAA 317
Cdd:cd16892   80 --EDVFDPCTNLKAGATILTECYARAKKTGGDGQAALRAALSCYN--TGNFTRGFSNgyvQKVVAA 141
CwlT-like cd16891
CwlT-like N-terminal lysozyme domain and similar domains; CwlT is a bifunctional cell wall ...
 191-303 1.55e-03

CwlT-like N-terminal lysozyme domain and similar domains; CwlT is a bifunctional cell wall hydrolase containing an N-terminal lysozyme domain and a C-terminal NlpC/P60 endopeptidase domain (gamma-d-D-glutamyl-L-diamino acid endopeptidase), and has been implicated in the spread of transposons. 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: 381612 [Multi-domain]  Cd Length: 151  Bit Score: 38.74  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120 191 YLGMVRQASRKYGVDE--SLILAIMQTESSFNpyavsrsdalglmqvvqhsaGKDVFRAQGKSGTPSRSYLfDPQSNIDT 268
Cdd:cd16891    1 YRPLVEKEAKKYGIPEyvPLILAIIMQESGGK--------------------GPDIMQSSESAGLPPNTIT-DPEESIEQ 59

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489959120 269 GTAYLA-MLN--NVYLGGIDnptsrryAVITAYNGGAG 303
Cdd:cd16891   60 GVKYFAdVLKkaKGKGVDIW-------TAVQAYNFGGG 90
PRK10859 PRK10859
membrane-bound lytic murein transglycosylase MltF;
182-306 4.98e-03

membrane-bound lytic murein transglycosylase MltF;


Pssm-ID: 236778 [Multi-domain]  Cd Length: 482  Bit Score: 38.70  E-value: 4.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959120 182 NHLDKRAHKYLGMVRQASRkyGVDESLILAIMQTESSFNPYAVSRSDALGLMQVVQHSAgKDVfraqgksGTPSRsylFD 261
Cdd:PRK10859 281 RAIDNRLPKYQPLFEKYAG--ELDWRLLAAIAYQESHWNPQATSPTGVRGLMMLTRNTA-QSM-------GVTDR---LD 347

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489959120 262 PQSNIDTGTAYLAMLNNVYLGGIDNPTSRRYAvITAYNGGAGSVL 306
Cdd:PRK10859 348 PEQSIRGGARYLQDLMERLPESIPEPERIWFA-LAAYNIGYGHML 391
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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