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Conserved domains on  [gi|1379540447|gb|PUE70020|]
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lytic murein transglycosylase [Xanthomonas vasicola pv. vasculorum]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MltB COG2951
Membrane-bound lytic murein transglycosylase B [Cell wall/membrane/envelope biogenesis];
20-325 2.65e-148

Membrane-bound lytic murein transglycosylase B [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442193 [Multi-domain]  Cd Length: 326  Bit Score: 434.98  E-value: 2.65e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447  20 CADPAFDRCLAGLQSQAAAKGVDAASFQRFTAGLVPDPSVLPLLDAQPEFTTPIWDYLASLVDSQRVTDGQAMLVTHREL 99
Cdd:COG2951    23 AAAADFAAWVAAFRQEAAAAGISRATLDAALAGATPDPRVIELDRRQPEFTKPWWDYLARFVSPARIARGRAFLRQHAAL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 100 LSRLSEQTGVDPATIVAVWGVESDYGRVTGKRPLLVSLATLSCAGRRQPFFRGEFLALLSLLQQGDLSADGLTGSWAGAF 179
Cdd:COG2951   103 LARIEQRYGVPAEIIVAIWGVETNYGRYMGNFPVLDALATLAFDGRRAEFFRGELIAALKILQRGDIDPDQMKGSWAGAM 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 180 GQTQFMPSTYARIAVDGDGDGRRDLVASIPDALASTANYLVKAGWERARPWGMEVTLPRGFDASKAGRTRRQPLQAWQTA 259
Cdd:COG2951   183 GQTQFMPSSYLRYAVDFDGDGRRDLWNSPPDALASTANYLKKHGWQRGQPWGYEVRLPAGFDYALAGLKPRRTLAEWAAL 262
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1379540447 260 GLLGTDGKPlaptgLPAETPAALLLPAGATGPAFLVFRNYDAIYAYNAAESYALSIALLADRLRGG 325
Cdd:COG2951   263 GVRPADGRP-----LPADGPASLLLPAGANGPAFLVTPNFYVITRYNRSDLYALAVGHLADRIAGA 323
YeaD COG0676
D-hexose-6-phosphate mutarotase [Carbohydrate transport and metabolism];
439-720 3.15e-113

D-hexose-6-phosphate mutarotase [Carbohydrate transport and metabolism];


:

Pssm-ID: 440440  Cd Length: 296  Bit Score: 343.77  E-value: 3.15e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 439 TGLTTGDFHGFPSLLIDTPFSTAAISLFGGQLVSFVPKGGQDVMWLSP-SAQQPPTPIRGGAPVCWPYFGRQDQTGDVPA 517
Cdd:COG0676    13 PSVSLRGPGGLPVLRIDNPGARATIALQGAHVLSWQPAGEEPVLWLSPaAAFEPGKAIRGGVPVCWPWFGPHPSDPGLPA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 518 HGFVRTVAWQLTESRrEDDGTVVLTLTPPRLDDL------ALRLRMTLRIGRTLEQRLITENISGASVRFTQALHNYFHV 591
Cdd:COG0676    93 HGFARTRPWQLTEHR-EDDGGVILTLTLTDSEATralwphAFELELTVTLGETLTLELTTTNTGDQPFSFTQALHTYFAV 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 592 GDALNVSVQGLDGLDYLDKYENYATAhRQQGDWSLrdprdPGRSDRIYTNAGGRYTLTDPVLGRRIVIATEGSRSLVVWN 671
Cdd:COG0676   172 GDIEQVRVSGLEGARYIDKLDGGAEK-QQEGPLTF-----TGETDRVYLDPPAPLTIHDPGLKRRIRIAKSGSSSVVVWN 245
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1379540447 672 PGEEAGKKMADVG-DGWRDYVCLEAANAGPDVIELAPGASHTLSQTISVE 720
Cdd:COG0676   246 PWAEKAASMADMPdDGYRTMVCVETANALDDAVTLAPGESHTLSQTISVE 295
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
330-398 3.51e-11

Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 59.15  E-value: 3.51e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1379540447 330 AAWPTDEPGLGRPERRELQQLLLARGHQIGEADGMVGSATRRAIQVEQTRLGLqPADGRPGQRILTALR 398
Cdd:COG3409     1 ASAPTLRLGDSGEDVRELQQRLNALGYYPGPVDGIFGPATEAAVRAFQRANGL-PVDGIVGPATWAALR 68
 
Name Accession Description Interval E-value
MltB COG2951
Membrane-bound lytic murein transglycosylase B [Cell wall/membrane/envelope biogenesis];
20-325 2.65e-148

Membrane-bound lytic murein transglycosylase B [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442193 [Multi-domain]  Cd Length: 326  Bit Score: 434.98  E-value: 2.65e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447  20 CADPAFDRCLAGLQSQAAAKGVDAASFQRFTAGLVPDPSVLPLLDAQPEFTTPIWDYLASLVDSQRVTDGQAMLVTHREL 99
Cdd:COG2951    23 AAAADFAAWVAAFRQEAAAAGISRATLDAALAGATPDPRVIELDRRQPEFTKPWWDYLARFVSPARIARGRAFLRQHAAL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 100 LSRLSEQTGVDPATIVAVWGVESDYGRVTGKRPLLVSLATLSCAGRRQPFFRGEFLALLSLLQQGDLSADGLTGSWAGAF 179
Cdd:COG2951   103 LARIEQRYGVPAEIIVAIWGVETNYGRYMGNFPVLDALATLAFDGRRAEFFRGELIAALKILQRGDIDPDQMKGSWAGAM 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 180 GQTQFMPSTYARIAVDGDGDGRRDLVASIPDALASTANYLVKAGWERARPWGMEVTLPRGFDASKAGRTRRQPLQAWQTA 259
Cdd:COG2951   183 GQTQFMPSSYLRYAVDFDGDGRRDLWNSPPDALASTANYLKKHGWQRGQPWGYEVRLPAGFDYALAGLKPRRTLAEWAAL 262
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1379540447 260 GLLGTDGKPlaptgLPAETPAALLLPAGATGPAFLVFRNYDAIYAYNAAESYALSIALLADRLRGG 325
Cdd:COG2951   263 GVRPADGRP-----LPADGPASLLLPAGANGPAFLVTPNFYVITRYNRSDLYALAVGHLADRIAGA 323
MltB_2 TIGR02283
lytic murein transglycosylase; Members of this family are closely related to the MltB family ...
24-324 2.15e-146

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: 429.10  E-value: 2.15e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447  24 AFDRCLAGLQSQAAAKGVDAASFQRFTAGLV-PDPSVLPLLDAQPEFTTPIWDYLASLVDSQRVTDGQAMLVTHRELLSR 102
Cdd:TIGR02283   1 GFDAWLAQLRAEAAAKGISAATFDRAFAGIKePDQSVLNLDRNQPEFTQTFWDYLSRRVSPRRIAIGRAMLQRYAALLAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 103 LSEQTGVDPATIVAVWGVESDYGRVTGKRPLLVSLATLSCAGRRQPFFRGEFLALLSLLQQGDLSADGLTGSWAGAFGQT 182
Cdd:TIGR02283  81 IEKRYGVPAEILLAIWGMESDFGAYQGKFDVIRSLATLAYDGRRKDYFRTELIAALKILQRGDLTRAAMKGSWAGAMGQT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 183 QFMPSTYARIAVDGDGDGRRDLVASIPDALASTANYLVKAGWERARPWGMEVTLPRGFDASKAGRTRRQPLQAWQTAGLL 262
Cdd:TIGR02283 161 QFLPSSYLNYAVDFDGDGRRDIWNSVPDALASTANYLVNGGWKRGEPWGYEVQLPAGFDYALSGSQIKKPIAEWQRLGVT 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1379540447 263 GTDGKPLapTGLPAETPAALLLPAGATGPAFLVFRNYDAIYAYNAAESYALSIALLADRLRG 324
Cdd:TIGR02283 241 RVDGRPL--PASAANAEASLLLPDGRKGPAFLVTPNFRVIKEWNRSDYYALTIGLLADRIAG 300
SLT_2 pfam13406
Transglycosylase SLT domain; This family is related to the SLT domain pfam01464.
24-320 7.21e-134

Transglycosylase SLT domain; This family is related to the SLT domain pfam01464.


Pssm-ID: 404311 [Multi-domain]  Cd Length: 292  Bit Score: 396.54  E-value: 7.21e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447  24 AFDRCLAGLQSQAAAKGVDAASFQRFTAGLVPDPSVLPLLDAQPEFTTPIWDYLASLVDSQRVTDGQAMLVTHRELLSRL 103
Cdd:pfam13406   1 GFDAWVAAFRQEAAAAGISRATLDAAFAGVEPDPRVIELDRRQPEFTKPWWDYLSRFVTPARIARGRAFLQEHAALLARI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 104 SEQTGVDPATIVAVWGVESDYGRVTGKRPLLVSLATLSCAGRRQPFFRGEFLALLSLLQQGDLSADGLTGSWAGAFGQTQ 183
Cdd:pfam13406  81 EKRYGVPPEIIVAIWGVETNYGRYMGNFPVLDALATLAFDGRRSEFFRKELIAALKILDRGDLDPEQLKGSWAGAMGQTQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 184 FMPSTYARIAVDGDGDGRRDLVASIPDALASTANYLVKAGWERARPWGMEVTLPRGFDASKAGRTRRQPLQAWQTAGLLG 263
Cdd:pfam13406 161 FMPSSYLAYAVDFDGDGRRDLWNSPPDALASVANYLKQHGWQPGEPWGREVRLPAGFDYSLAGLGTRKPLAEWAALGVRP 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1379540447 264 TDGKPLAPTGlpaetPAALLLPAGATGPAFLVFRNYDAIYAYNAAESYALSIALLAD 320
Cdd:pfam13406 241 ADGGPPLADA-----EASLLLPAGANGPAFLVYDNFYVITRYNRSDLYALAVGHLAD 292
YeaD COG0676
D-hexose-6-phosphate mutarotase [Carbohydrate transport and metabolism];
439-720 3.15e-113

D-hexose-6-phosphate mutarotase [Carbohydrate transport and metabolism];


Pssm-ID: 440440  Cd Length: 296  Bit Score: 343.77  E-value: 3.15e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 439 TGLTTGDFHGFPSLLIDTPFSTAAISLFGGQLVSFVPKGGQDVMWLSP-SAQQPPTPIRGGAPVCWPYFGRQDQTGDVPA 517
Cdd:COG0676    13 PSVSLRGPGGLPVLRIDNPGARATIALQGAHVLSWQPAGEEPVLWLSPaAAFEPGKAIRGGVPVCWPWFGPHPSDPGLPA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 518 HGFVRTVAWQLTESRrEDDGTVVLTLTPPRLDDL------ALRLRMTLRIGRTLEQRLITENISGASVRFTQALHNYFHV 591
Cdd:COG0676    93 HGFARTRPWQLTEHR-EDDGGVILTLTLTDSEATralwphAFELELTVTLGETLTLELTTTNTGDQPFSFTQALHTYFAV 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 592 GDALNVSVQGLDGLDYLDKYENYATAhRQQGDWSLrdprdPGRSDRIYTNAGGRYTLTDPVLGRRIVIATEGSRSLVVWN 671
Cdd:COG0676   172 GDIEQVRVSGLEGARYIDKLDGGAEK-QQEGPLTF-----TGETDRVYLDPPAPLTIHDPGLKRRIRIAKSGSSSVVVWN 245
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1379540447 672 PGEEAGKKMADVG-DGWRDYVCLEAANAGPDVIELAPGASHTLSQTISVE 720
Cdd:COG0676   246 PWAEKAASMADMPdDGYRTMVCVETANALDDAVTLAPGESHTLSQTISVE 295
D-hex-6-P-epi_like cd09020
D-hexose-6-phosphate epimerase-like; D-Hexose-6-phosphate epimerase Ymr099c from Saccharomyces ...
452-718 5.73e-109

D-hexose-6-phosphate epimerase-like; D-Hexose-6-phosphate epimerase Ymr099c from Saccharomyces cerevisiae belongs to the large superfamily of aldose-1-epimerases. Its active site is very similar to the catalytic site of galactose mutarotase, the best studied member of the superfamily. It also contains the conserved glutamate and histidine residues that have been shown in galactose mutarotase to be critical for catalysis, the glutamate serving as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate, and the histidine as the active site acid to protonate the C-5 ring oxygen. In addition Ymr099c contains 2 conserved arginine residues which are involved in phosphate binding, and exhibits hexose-6-phosphate mutarotase activity on glucose-6-P, galactose-6-P and mannose-6-P.


Pssm-ID: 185697  Cd Length: 269  Bit Score: 331.50  E-value: 5.73e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 452 LLIDTPFSTAAISLFGGQLVSFVPKGGQDVMWLSPSAQ-QPPTPIRGGAPVCWPYFGRQDQTGDVPAHGFVRTVAWQLTE 530
Cdd:cd09020     2 IVLDHPGASAEIALQGAQVLSWKPKGGQDLLWLSPQAPfDGGKAIRGGIPVCWPWFGPHGPNADLPAHGFARTRLWELLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 531 SRREDDGT-VVLTLTPPRLD------DLALRLRMTLRiGRTLEQRLITENISGASVRFTQALHNYFHVGDALNVSVQGLD 603
Cdd:cd09020    82 VSEDEDGVtVSLELDDTDETraiwphAFELRLTVTLG-FDTLELELTVTNTGDKPFSFTAALHTYFRVSDIEQVRVEGLE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 604 GLDYLDKYENYATahRQQGDwslrDPRDPGRSDRIYTNAGGRYTLTDPVLGRRIVIATEGSRSLVVWNPGEEAGKKMADV 683
Cdd:cd09020   161 GATYLDKLTDQRE--KVQGG----AVTFDGEVDRVYLNTPAPLTIDDPAWGRRIRIEKSGSPSAVVWNPWIEKAARMADF 234
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1379540447 684 G-DGWRDYVCLEAANAGpDVIELAPGASHTLSQTIS 718
Cdd:cd09020   235 PdDGYRRMVCVEAANVA-DPVTLAPGESHTLSQTIS 269
Aldose_epim pfam01263
Aldose 1-epimerase;
453-718 4.87e-39

Aldose 1-epimerase;


Pssm-ID: 396013  Cd Length: 300  Bit Score: 146.39  E-value: 4.87e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 453 LIDTPFSTAAISLFGGQLVSFVPKGG-QDVMWLSPS------------AQQPPTPIRG--------GAPVCWPYFGRqdq 511
Cdd:pfam01263   5 LTNGNGLSATISLYGATLLSLKVPGKlREVLLGSDDaegylkdsnyfgATLGPYANRIangrfeldGIPYCLPQNGP--- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 512 tGDVPAHGFVRTVAWQLTESRREDDGTVVLTLTPPRLDDL--ALRLRMTLRIGRTLEQRLITENIS-GASVRFTQALHNY 588
Cdd:pfam01263  82 -GKNPLHGGARGRIWEVEEVKPDDGVTVTLVLDPDGEEGYpgDLEARVTYTLNEDNELTIEYEATNdGKPTPFNLGNHPY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 589 FHVGDALN---VSVQGLDGLDYLDKY-ENYATAHRQQGDWSLRDPR----DPGRSDRIYTNAGGRYTLTDPVLGRRIVIA 660
Cdd:pfam01263 161 FNLSGDIDiheLQIEADEYLEVDDDLiPTGELKDVKGTPFDFRQPTpigeDILGYDHVYLLDPLKAVIIDPDPGSGIVLE 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 661 TEGSR-SLVVWNPGEEAGKKMADVGD-GWRDYVCLEAANAGPDVIELAPGASHTLSQTIS 718
Cdd:pfam01263 241 VSTTQpGLVVYTPNFLKGKYLSDEGFaLETQFLPDEPNHPEFPSIILKPGESYTAETSYS 300
PRK10760 PRK10760
murein hydrolase B; Provisional
58-325 1.74e-29

murein hydrolase B; Provisional


Pssm-ID: 236754 [Multi-domain]  Cd Length: 359  Bit Score: 120.61  E-value: 1.74e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447  58 SVLPLLDAQPEFTTP------IWD-YLASLVDSQRVTDGQAMLVTHRELLSRLSEQTGVDPATIVAVWGVESDYGRVTGK 130
Cdd:PRK10760   90 WVLRLMDRQAPTTRPpsgpngAWLrYRKKFITPDNVQNGVVFWNQYEDALNRAWQVYGVPPEIIVGIIGVETRWGRVMGK 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 131 RPLLVSLATLSCA-GRRQPFFRGEFLALLSLLQQGDLSADGLTGSWAGAFGQTQFMPSTYARIAVDGDGDGRRDLVASIp 209
Cdd:PRK10760  170 TRILDALATLSFNyPRRAEYFSGELETFLLMARDEGDDPLNLRGSFAGAMGYGQFMPSSFKQYAVDFNGDGHINLWDPV- 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 210 DALASTANYLVKAGWERARPW-----GMEVTLPRGFDAskagrtrRQPLQAWQTAGllgtdgkpLAPTG-LPAETPAALL 283
Cdd:PRK10760  249 DAIGSVANYFKAHGWVKGDQVavpanGQAPGLENGFKT-------RYSVSQLAAAG--------LTPQQpLGNHQQASLL 313
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1379540447 284 -LPAGATGPAFLVFRNYDAIYAYNAAESYALSIALLAD---RLRGG 325
Cdd:PRK10760  314 rLDVGTGYQYWYGLPNFYTITRYNHSTHYAMAVWQLGQavaLARVG 359
Slt35-like cd13399
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ...
108-228 1.17e-19

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: 84.67  E-value: 1.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 108 GVDPATIVAVWGVESDYGRVTGkrpllvslatlscagrrqpffrgeflallsllqqgdlsadgltGSWAGAFGQTQFMPS 187
Cdd:cd13399     2 GVPPGILAAILGVESGFGPNAG-------------------------------------------GSPAGAQGIAQFMPS 38
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1379540447 188 TYARIAVDGDGDGRRDLvASIPDALASTANYLVKAGWERAR 228
Cdd:cd13399    39 TWKAYGVDGNGDGKADP-FNPEDAIASAANYLCRHGWDLNA 78
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
330-398 3.51e-11

Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 59.15  E-value: 3.51e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1379540447 330 AAWPTDEPGLGRPERRELQQLLLARGHQIGEADGMVGSATRRAIQVEQTRLGLqPADGRPGQRILTALR 398
Cdd:COG3409     1 ASAPTLRLGDSGEDVRELQQRLNALGYYPGPVDGIFGPATEAAVRAFQRANGL-PVDGIVGPATWAALR 68
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
341-397 1.48e-08

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 51.36  E-value: 1.48e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1379540447 341 RPERRELQQLLLARGHQIGEADGMVGSATRRAIQVEQTRLGLqPADGRPGQRILTAL 397
Cdd:pfam01471   2 GEDVKELQRYLNRLGYYPGPVDGYFGPSTEAAVKAFQRAFGL-PVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
MltB COG2951
Membrane-bound lytic murein transglycosylase B [Cell wall/membrane/envelope biogenesis];
20-325 2.65e-148

Membrane-bound lytic murein transglycosylase B [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442193 [Multi-domain]  Cd Length: 326  Bit Score: 434.98  E-value: 2.65e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447  20 CADPAFDRCLAGLQSQAAAKGVDAASFQRFTAGLVPDPSVLPLLDAQPEFTTPIWDYLASLVDSQRVTDGQAMLVTHREL 99
Cdd:COG2951    23 AAAADFAAWVAAFRQEAAAAGISRATLDAALAGATPDPRVIELDRRQPEFTKPWWDYLARFVSPARIARGRAFLRQHAAL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 100 LSRLSEQTGVDPATIVAVWGVESDYGRVTGKRPLLVSLATLSCAGRRQPFFRGEFLALLSLLQQGDLSADGLTGSWAGAF 179
Cdd:COG2951   103 LARIEQRYGVPAEIIVAIWGVETNYGRYMGNFPVLDALATLAFDGRRAEFFRGELIAALKILQRGDIDPDQMKGSWAGAM 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 180 GQTQFMPSTYARIAVDGDGDGRRDLVASIPDALASTANYLVKAGWERARPWGMEVTLPRGFDASKAGRTRRQPLQAWQTA 259
Cdd:COG2951   183 GQTQFMPSSYLRYAVDFDGDGRRDLWNSPPDALASTANYLKKHGWQRGQPWGYEVRLPAGFDYALAGLKPRRTLAEWAAL 262
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1379540447 260 GLLGTDGKPlaptgLPAETPAALLLPAGATGPAFLVFRNYDAIYAYNAAESYALSIALLADRLRGG 325
Cdd:COG2951   263 GVRPADGRP-----LPADGPASLLLPAGANGPAFLVTPNFYVITRYNRSDLYALAVGHLADRIAGA 323
MltB_2 TIGR02283
lytic murein transglycosylase; Members of this family are closely related to the MltB family ...
24-324 2.15e-146

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: 429.10  E-value: 2.15e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447  24 AFDRCLAGLQSQAAAKGVDAASFQRFTAGLV-PDPSVLPLLDAQPEFTTPIWDYLASLVDSQRVTDGQAMLVTHRELLSR 102
Cdd:TIGR02283   1 GFDAWLAQLRAEAAAKGISAATFDRAFAGIKePDQSVLNLDRNQPEFTQTFWDYLSRRVSPRRIAIGRAMLQRYAALLAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 103 LSEQTGVDPATIVAVWGVESDYGRVTGKRPLLVSLATLSCAGRRQPFFRGEFLALLSLLQQGDLSADGLTGSWAGAFGQT 182
Cdd:TIGR02283  81 IEKRYGVPAEILLAIWGMESDFGAYQGKFDVIRSLATLAYDGRRKDYFRTELIAALKILQRGDLTRAAMKGSWAGAMGQT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 183 QFMPSTYARIAVDGDGDGRRDLVASIPDALASTANYLVKAGWERARPWGMEVTLPRGFDASKAGRTRRQPLQAWQTAGLL 262
Cdd:TIGR02283 161 QFLPSSYLNYAVDFDGDGRRDIWNSVPDALASTANYLVNGGWKRGEPWGYEVQLPAGFDYALSGSQIKKPIAEWQRLGVT 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1379540447 263 GTDGKPLapTGLPAETPAALLLPAGATGPAFLVFRNYDAIYAYNAAESYALSIALLADRLRG 324
Cdd:TIGR02283 241 RVDGRPL--PASAANAEASLLLPDGRKGPAFLVTPNFRVIKEWNRSDYYALTIGLLADRIAG 300
SLT_2 pfam13406
Transglycosylase SLT domain; This family is related to the SLT domain pfam01464.
24-320 7.21e-134

Transglycosylase SLT domain; This family is related to the SLT domain pfam01464.


Pssm-ID: 404311 [Multi-domain]  Cd Length: 292  Bit Score: 396.54  E-value: 7.21e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447  24 AFDRCLAGLQSQAAAKGVDAASFQRFTAGLVPDPSVLPLLDAQPEFTTPIWDYLASLVDSQRVTDGQAMLVTHRELLSRL 103
Cdd:pfam13406   1 GFDAWVAAFRQEAAAAGISRATLDAAFAGVEPDPRVIELDRRQPEFTKPWWDYLSRFVTPARIARGRAFLQEHAALLARI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 104 SEQTGVDPATIVAVWGVESDYGRVTGKRPLLVSLATLSCAGRRQPFFRGEFLALLSLLQQGDLSADGLTGSWAGAFGQTQ 183
Cdd:pfam13406  81 EKRYGVPPEIIVAIWGVETNYGRYMGNFPVLDALATLAFDGRRSEFFRKELIAALKILDRGDLDPEQLKGSWAGAMGQTQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 184 FMPSTYARIAVDGDGDGRRDLVASIPDALASTANYLVKAGWERARPWGMEVTLPRGFDASKAGRTRRQPLQAWQTAGLLG 263
Cdd:pfam13406 161 FMPSSYLAYAVDFDGDGRRDLWNSPPDALASVANYLKQHGWQPGEPWGREVRLPAGFDYSLAGLGTRKPLAEWAALGVRP 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1379540447 264 TDGKPLAPTGlpaetPAALLLPAGATGPAFLVFRNYDAIYAYNAAESYALSIALLAD 320
Cdd:pfam13406 241 ADGGPPLADA-----EASLLLPAGANGPAFLVYDNFYVITRYNRSDLYALAVGHLAD 292
YeaD COG0676
D-hexose-6-phosphate mutarotase [Carbohydrate transport and metabolism];
439-720 3.15e-113

D-hexose-6-phosphate mutarotase [Carbohydrate transport and metabolism];


Pssm-ID: 440440  Cd Length: 296  Bit Score: 343.77  E-value: 3.15e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 439 TGLTTGDFHGFPSLLIDTPFSTAAISLFGGQLVSFVPKGGQDVMWLSP-SAQQPPTPIRGGAPVCWPYFGRQDQTGDVPA 517
Cdd:COG0676    13 PSVSLRGPGGLPVLRIDNPGARATIALQGAHVLSWQPAGEEPVLWLSPaAAFEPGKAIRGGVPVCWPWFGPHPSDPGLPA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 518 HGFVRTVAWQLTESRrEDDGTVVLTLTPPRLDDL------ALRLRMTLRIGRTLEQRLITENISGASVRFTQALHNYFHV 591
Cdd:COG0676    93 HGFARTRPWQLTEHR-EDDGGVILTLTLTDSEATralwphAFELELTVTLGETLTLELTTTNTGDQPFSFTQALHTYFAV 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 592 GDALNVSVQGLDGLDYLDKYENYATAhRQQGDWSLrdprdPGRSDRIYTNAGGRYTLTDPVLGRRIVIATEGSRSLVVWN 671
Cdd:COG0676   172 GDIEQVRVSGLEGARYIDKLDGGAEK-QQEGPLTF-----TGETDRVYLDPPAPLTIHDPGLKRRIRIAKSGSSSVVVWN 245
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1379540447 672 PGEEAGKKMADVG-DGWRDYVCLEAANAGPDVIELAPGASHTLSQTISVE 720
Cdd:COG0676   246 PWAEKAASMADMPdDGYRTMVCVETANALDDAVTLAPGESHTLSQTISVE 295
D-hex-6-P-epi_like cd09020
D-hexose-6-phosphate epimerase-like; D-Hexose-6-phosphate epimerase Ymr099c from Saccharomyces ...
452-718 5.73e-109

D-hexose-6-phosphate epimerase-like; D-Hexose-6-phosphate epimerase Ymr099c from Saccharomyces cerevisiae belongs to the large superfamily of aldose-1-epimerases. Its active site is very similar to the catalytic site of galactose mutarotase, the best studied member of the superfamily. It also contains the conserved glutamate and histidine residues that have been shown in galactose mutarotase to be critical for catalysis, the glutamate serving as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate, and the histidine as the active site acid to protonate the C-5 ring oxygen. In addition Ymr099c contains 2 conserved arginine residues which are involved in phosphate binding, and exhibits hexose-6-phosphate mutarotase activity on glucose-6-P, galactose-6-P and mannose-6-P.


Pssm-ID: 185697  Cd Length: 269  Bit Score: 331.50  E-value: 5.73e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 452 LLIDTPFSTAAISLFGGQLVSFVPKGGQDVMWLSPSAQ-QPPTPIRGGAPVCWPYFGRQDQTGDVPAHGFVRTVAWQLTE 530
Cdd:cd09020     2 IVLDHPGASAEIALQGAQVLSWKPKGGQDLLWLSPQAPfDGGKAIRGGIPVCWPWFGPHGPNADLPAHGFARTRLWELLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 531 SRREDDGT-VVLTLTPPRLD------DLALRLRMTLRiGRTLEQRLITENISGASVRFTQALHNYFHVGDALNVSVQGLD 603
Cdd:cd09020    82 VSEDEDGVtVSLELDDTDETraiwphAFELRLTVTLG-FDTLELELTVTNTGDKPFSFTAALHTYFRVSDIEQVRVEGLE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 604 GLDYLDKYENYATahRQQGDwslrDPRDPGRSDRIYTNAGGRYTLTDPVLGRRIVIATEGSRSLVVWNPGEEAGKKMADV 683
Cdd:cd09020   161 GATYLDKLTDQRE--KVQGG----AVTFDGEVDRVYLNTPAPLTIDDPAWGRRIRIEKSGSPSAVVWNPWIEKAARMADF 234
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1379540447 684 G-DGWRDYVCLEAANAGpDVIELAPGASHTLSQTIS 718
Cdd:cd09020   235 PdDGYRRMVCVEAANVA-DPVTLAPGESHTLSQTIS 269
MltB TIGR02282
lytic murein transglycosylase B; This family consists of lytic murein transglycosylases ...
35-322 4.96e-53

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: 184.90  E-value: 4.96e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447  35 QAAAKGVDAASFQRFTAGLVPDPSVLPLLDAQPEFTTPiWD-YLASLVDSQRVTDGQAMLVTHRELLSRLSEQTGVDPAT 113
Cdd:TIGR02282   7 LVAKHGFDRAQLEAILAQAKYNDEVIRLIDNPAESAKP-WLeYRGIFITPKRIQDGVEFWKQHEDALNRAEQRYGVPPEI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 114 IVAVWGVESDYGRVTGKRPLLVSLATLSCA-GRRQPFFRGEFLALLSLLQQGDLSADGLTGSWAGAFGQTQFMPSTYARI 192
Cdd:TIGR02282  86 IVAIIGVETNYGRNMGKYRVLDALTTLAFDyPRRATFFRGELGQFLLLAREEQLDPLTLKGSYAGAMGYPQFMPSSYRQY 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 193 AVDGDGDGRRDLVASIPDALASTANYLVKAGWERARPWGMEVTL--PRGFDASKAGRTRrqplqaWQTAGLLGTDGKPLA 270
Cdd:TIGR02282 166 AVDFDGDGHIDLWNSPDDAIGSVANYFHAHGWVRGDPVAVPATGaaPGDQLPNKFAKPH------YSLSQLAAAGLIPQA 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1379540447 271 PtgLPAETPAALL-LPAGATGPAFLVFRNYDAIYAYNAAESYALSIALLADRL 322
Cdd:TIGR02282 240 P--LGNEQKASLVdLDVGGGDQYWLGLPNFYAITRYNRSTFYAMAVYQLSQAL 290
Aldose_epim pfam01263
Aldose 1-epimerase;
453-718 4.87e-39

Aldose 1-epimerase;


Pssm-ID: 396013  Cd Length: 300  Bit Score: 146.39  E-value: 4.87e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 453 LIDTPFSTAAISLFGGQLVSFVPKGG-QDVMWLSPS------------AQQPPTPIRG--------GAPVCWPYFGRqdq 511
Cdd:pfam01263   5 LTNGNGLSATISLYGATLLSLKVPGKlREVLLGSDDaegylkdsnyfgATLGPYANRIangrfeldGIPYCLPQNGP--- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 512 tGDVPAHGFVRTVAWQLTESRREDDGTVVLTLTPPRLDDL--ALRLRMTLRIGRTLEQRLITENIS-GASVRFTQALHNY 588
Cdd:pfam01263  82 -GKNPLHGGARGRIWEVEEVKPDDGVTVTLVLDPDGEEGYpgDLEARVTYTLNEDNELTIEYEATNdGKPTPFNLGNHPY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 589 FHVGDALN---VSVQGLDGLDYLDKY-ENYATAHRQQGDWSLRDPR----DPGRSDRIYTNAGGRYTLTDPVLGRRIVIA 660
Cdd:pfam01263 161 FNLSGDIDiheLQIEADEYLEVDDDLiPTGELKDVKGTPFDFRQPTpigeDILGYDHVYLLDPLKAVIIDPDPGSGIVLE 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 661 TEGSR-SLVVWNPGEEAGKKMADVGD-GWRDYVCLEAANAGPDVIELAPGASHTLSQTIS 718
Cdd:pfam01263 241 VSTTQpGLVVYTPNFLKGKYLSDEGFaLETQFLPDEPNHPEFPSIILKPGESYTAETSYS 300
PRK10760 PRK10760
murein hydrolase B; Provisional
58-325 1.74e-29

murein hydrolase B; Provisional


Pssm-ID: 236754 [Multi-domain]  Cd Length: 359  Bit Score: 120.61  E-value: 1.74e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447  58 SVLPLLDAQPEFTTP------IWD-YLASLVDSQRVTDGQAMLVTHRELLSRLSEQTGVDPATIVAVWGVESDYGRVTGK 130
Cdd:PRK10760   90 WVLRLMDRQAPTTRPpsgpngAWLrYRKKFITPDNVQNGVVFWNQYEDALNRAWQVYGVPPEIIVGIIGVETRWGRVMGK 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 131 RPLLVSLATLSCA-GRRQPFFRGEFLALLSLLQQGDLSADGLTGSWAGAFGQTQFMPSTYARIAVDGDGDGRRDLVASIp 209
Cdd:PRK10760  170 TRILDALATLSFNyPRRAEYFSGELETFLLMARDEGDDPLNLRGSFAGAMGYGQFMPSSFKQYAVDFNGDGHINLWDPV- 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 210 DALASTANYLVKAGWERARPW-----GMEVTLPRGFDAskagrtrRQPLQAWQTAGllgtdgkpLAPTG-LPAETPAALL 283
Cdd:PRK10760  249 DAIGSVANYFKAHGWVKGDQVavpanGQAPGLENGFKT-------RYSVSQLAAAG--------LTPQQpLGNHQQASLL 313
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1379540447 284 -LPAGATGPAFLVFRNYDAIYAYNAAESYALSIALLAD---RLRGG 325
Cdd:PRK10760  314 rLDVGTGYQYWYGLPNFYTITRYNHSTHYAMAVWQLGQavaLARVG 359
Aldose_epim cd01081
aldose 1-epimerase superfamily; Aldose 1-epimerases or mutarotases are key enzymes of ...
459-701 2.57e-20

aldose 1-epimerase superfamily; Aldose 1-epimerases or mutarotases are key enzymes of carbohydrate metabolism; they catalyze the interconversion of the alpha- and beta-anomers of hexose sugars such as glucose and galactose. This interconversion is an important step that allows anomer specific metabolic conversion of sugars. Studies of the catalytic mechanism of the best known member of the family, galactose mutarotase, have shown a glutamate and a histidine residue to be critical for catalysis; the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate and the histidine as the active site acid to protonate the C-5 ring oxygen.


Pssm-ID: 185695 [Multi-domain]  Cd Length: 284  Bit Score: 91.76  E-value: 2.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 459 STAAISLFGGQLVSFVPKGGQDVMWLSPSAQQPPT-PIRGGAPVCWPYFGR---------------QDQTGDVPAHGFVR 522
Cdd:cd01081     1 AVAVIAPRGANIISLKVKGDVDLLWGYPDAEEYPLaPTGGGGAILFPFANRisdgrytfdgkqyplNEDEGGNAIHGFVR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 523 TVAWQLTESrREDDGTVVLTLTPPRLD-----DLALRLRMTLRiGRTLEQRLITENISGASVRFTQALHNYFHVGDA--- 594
Cdd:cd01081    81 NLPWRVVAT-DEEEASVTLSYDLNDGPggypfPLELTVTYTLD-ADTLTITFTVTNLGDEPMPFGLGWHPYFGLPGVaie 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 595 -----LNVSVQGLDGLDYLDKYEnyaTAHRQQGDWSLRDPRDPGRSDRIYTNAGG-----RYTLTDPVLGRRIVIATEGS 664
Cdd:cd01081   159 dlrlrVPASKVLPLDDLLPPTGE---LEVPGEEDFRLGRPLGGGELDDCFLLLGNdagtaEARLEDPDSRISVEFETGWP 235
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1379540447 665 RsLVVWNPgeeagkkmadvGDGWRDYVCLEAANAGPD 701
Cdd:cd01081   236 F-WQVYTG-----------DGGRRGSVAIEPMTSAPD 260
GalM COG2017
Galactose mutarotase or related enzyme [Carbohydrate transport and metabolism];
460-720 9.91e-20

Galactose mutarotase or related enzyme [Carbohydrate transport and metabolism];


Pssm-ID: 441620 [Multi-domain]  Cd Length: 309  Bit Score: 90.72  E-value: 9.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 460 TAAISLFGGQLVSF-VP-KGGQDVMWLSPSAQQPPTPiRGGAPVCWPYFGR--------QDQT-------GDVPAHGFVR 522
Cdd:COG2017    18 RAVIPEYGATLTSLrVPdKDGRDVLLGFDDLEDDPPW-AYGGAILGPYANRiadgrftlDGKTyqlpineGPNALHGGAR 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 523 TVAWQLTEsrrEDDGTVVLTLTPPrlDD------LALRLRMTLRiGRTLEQRLITENISGASVRFTQALHNYFHVGDALN 596
Cdd:COG2017    97 DRPWEVEE---QSEDSVTLSLTSP--DEegypgnLELTVTYTLT-DNGLTITYTATNLGDKPTPFNLGNHPYFNLPGEGG 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 597 VSVQG----LDGLDYLDKYENY----ATAHRQQGDWSLRDPRDPGRS--DRIYT--NAGGRY--TLTDPVLGRRIVIATE 662
Cdd:COG2017   171 GDIDDhrlqIPADEYLPVDEGLiptgELAPVAGTPFDFREPRPLGDGgfDHAFVglDSDGRPaaRLTDPDSGRRLEVSTD 250
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1379540447 663 GSRSLVVWNPgeeagkkmaDVGDGWRDYVCLEA----ANA-----GPDVIELAPGASHTLSQTISVE 720
Cdd:COG2017   251 EFPGLQVYTG---------NFLDPGRDGVCLEPqtgpPDApnhpgFEGLIVLAPGETYSATTRIRFS 308
Slt35-like cd13399
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ...
108-228 1.17e-19

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: 84.67  E-value: 1.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 108 GVDPATIVAVWGVESDYGRVTGkrpllvslatlscagrrqpffrgeflallsllqqgdlsadgltGSWAGAFGQTQFMPS 187
Cdd:cd13399     2 GVPPGILAAILGVESGFGPNAG-------------------------------------------GSPAGAQGIAQFMPS 38
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1379540447 188 TYARIAVDGDGDGRRDLvASIPDALASTANYLVKAGWERAR 228
Cdd:cd13399    39 TWKAYGVDGNGDGKADP-FNPEDAIASAANYLCRHGWDLNA 78
Aldose_epim_Slr1438 cd09025
Aldose 1-epimerase, similar to Synechocystis Slr1438; Proteins similar to Synechocystis ...
466-718 8.34e-19

Aldose 1-epimerase, similar to Synechocystis Slr1438; Proteins similar to Synechocystis Slr1438 are uncharacterized members of aldose-1-epimerase superfamily. Aldose 1-epimerases or mutarotases are key enzymes of carbohydrate metabolism, catalyzing the interconversion of the alpha- and beta-anomers of hexose sugars such as glucose and galactose. This interconversion is an important step that allows anomer specific metabolic conversion of sugars. Studies of the catalytic mechanism of the best known member of the family, galactose mutarotase, have shown a glutamate and a histidine residue to be critical for catalysis; the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate, and the histidine as the active site acid to protonate the C-5 ring oxygen.


Pssm-ID: 185702  Cd Length: 271  Bit Score: 86.92  E-value: 8.34e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 466 FGGQLVSFVpKGGQDVMWLSPSA-QQPPTPIRGGAPVCWPYFGRQD--------QTGDVPAHGFVRTVAWQLTESRREDD 536
Cdd:cd09025    21 RGGLITRWT-VQGRELLYLDEERfADPAKSVRGGIPILFPICGNLPddgyplagQEYTLKQHGFARDLPWEVELLGDGAG 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 537 GTVVLTLTP------PrlddLALRLRMTLRI-GRTLEQRLITENISGASVRFTQALHNYFHVGDALNVSVQGL--DGLDY 607
Cdd:cd09025   100 LTLTLRDNEatravyP----FDFELELTYRLaGNTLEIAQRVHNLGDQPMPFSFGFHPYFAVPDKAKLSLDLPptRCFDQ 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 608 L-DKYENYA--TAHRQQG-DWSLRDprdpgrsdriytnaGGRYTLTDPVLGRRI-VIATEGSRSLVVWN-PGeeagkkma 681
Cdd:cd09025   176 KtDEEANTPgqFDETEEGvDLLFRP--------------LGPASLTDGARGLKItLDHDEPFSNLVVWTdKG-------- 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1379540447 682 dvgdgwRDYVCLE-------AANAGPDVIELAPGASHTLSQTIS 718
Cdd:cd09025   234 ------KDFVCLEpwtgprnALNTGERLLLLPPGETEEASVRIQ 271
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
330-398 3.51e-11

Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 59.15  E-value: 3.51e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1379540447 330 AAWPTDEPGLGRPERRELQQLLLARGHQIGEADGMVGSATRRAIQVEQTRLGLqPADGRPGQRILTALR 398
Cdd:COG3409     1 ASAPTLRLGDSGEDVRELQQRLNALGYYPGPVDGIFGPATEAAVRAFQRANGL-PVDGIVGPATWAALR 68
Aldose_epim_lacX cd09024
Aldose 1-epimerase, similar to Lactococcus lactis lacX; Proteins similar to Lactococcus lactis ...
460-719 5.64e-09

Aldose 1-epimerase, similar to Lactococcus lactis lacX; Proteins similar to Lactococcus lactis lacX are uncharacterized members of aldose-1-epimerase superfamily. Aldose 1-epimerases or mutarotases are key enzymes of carbohydrate metabolism, catalyzing the interconversion of the alpha- and beta-anomers of hexose sugars such as glucose and galactose. This interconversion is an important step that allows anomer specific metabolic conversion of sugars. Studies of the catalytic mechanism of the best known member of the family, galactose mutarotase, have shown a glutamate and a histidine residue to be critical for catalysis; the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate, and the histidine as the active site acid to protonate the C-5 ring oxygen.


Pssm-ID: 185701  Cd Length: 288  Bit Score: 57.94  E-value: 5.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 460 TAAISLFGGQLVSFVPKG-GQDVMWlspsaQQPPTPIRGGAPVCWPYFGR--------QDQTGDVPAHGFVRTVAWQLTE 530
Cdd:cd09024     9 TVTISEHGAELTSIKDKKtGREYLW-----QGDPAYWGRHAPILFPIVGRlkddtytiDGKTYPMPQHGFARDMEFEVVE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 531 srrEDDGTVVLTLTpprlDD---LAL-----RLRMTLRI-GRTLEQRLITENISgasvrfTQALhnYFHVG--DALNVSV 599
Cdd:cd09024    84 ---QSDDSVTFELT----DNeetLKVypfdfELRVTYTLeGNTLKVTYEVKNPD------DKTM--PFSIGghPAFNCPL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 600 -QGLDGLDY---LDKYENYATAHRQQGDWSLRDPRDPGRSDR--------------IYTNAGGR-YTLTDPVLGRRIVIA 660
Cdd:cd09024   149 dEGEKFEDYyleFEPKEELERIPLVGPLGLLGEKKPLLLNEGtlplthdlfdddalIFDNLKSReVTLKSKKTGHGVTVD 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1379540447 661 TEGSRSLVVWNPGEEAgkkmadvgdgwrDYVCLE-----AANAG--------PDVIELAPGASHTLSQTISV 719
Cdd:cd09024   229 FDDFPYLGIWSKPNGA------------PFVCIEpwyglADSVGfdgdledkEGINKLEPGESFEASYSITI 288
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
341-397 1.48e-08

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 51.36  E-value: 1.48e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1379540447 341 RPERRELQQLLLARGHQIGEADGMVGSATRRAIQVEQTRLGLqPADGRPGQRILTAL 397
Cdd:pfam01471   2 GEDVKELQRYLNRLGYYPGPVDGYFGPSTEAAVKAFQRAFGL-PVDGIVDPETLAAL 57
Aldose_epim_Ec_YihR cd09022
Aldose 1-epimerase, similar to Escherichia coli YihR; Proteins similar to Escherichia coli ...
460-717 7.05e-03

Aldose 1-epimerase, similar to Escherichia coli YihR; Proteins similar to Escherichia coli YihR are uncharacterized members of aldose-1-epimerase superfamily. Aldose 1-epimerases or mutarotases are key enzymes of carbohydrate metabolism, catalyzing the interconversion of the alpha- and beta-anomers of hexose sugars such as glucose and galactose. This interconversion is an important step that allows anomer specific metabolic conversion of sugars. Studies of the catalytic mechanism of the best known member of the family, galactose mutarotase, have shown a glutamate and a histidine residue to be critical for catalysis; the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate, and the histidine as the active site acid to protonate the C-5 ring oxygen.


Pssm-ID: 185699  Cd Length: 284  Bit Score: 39.09  E-value: 7.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 460 TAAISLFGGQLVSFVpKGGQDVMWlSPSAQQPPTPIRGGAPVCWP--------YFGRQDQTGDV--PA-----HGFVRTV 524
Cdd:cd09022     2 RAVVTEVGAGLRSLT-VGGRDLVE-PYPADEVPPGAAGQVLAPWPnriadgryTFDGVEHQLPItePErgnaiHGLVRWA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 525 AWQLTEsrrEDDGTVVLTLTPPRLD----DLALRLRMTLRiGRTLEQRLITENISGASVRFTQALHNYFHVGDA------ 594
Cdd:cd09022    80 DWQLVE---HTDSSVTLRTRIPPQPgypfTLELTVTYELD-DDGLTVTLTATNVGDEPAPFGVGFHPYLSAGGApldect 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 595 ---------------LNVSVQGLDGLDYlDKYENYATAHRQQGD-WSLRDPRDPGRSdriytnaggRYTLTDPVLGRRIV 658
Cdd:cd09022   156 ltlpadtwlpvderlLPTGTEPVAGTPY-DFRTGRRLGGTALDTaFTDLTRDADGRA---------RARLTGPDGRGVEL 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1379540447 659 IATEGSRSLVVWNPGEEAgkkmadvGDGWRDYVCLE-------AANAGPDVIELAPGASHTLSQTI 717
Cdd:cd09022   226 WADESFPWVQVFTADTLP-------PPGRRRGLAVEpmtcppnAFNSGTDLIVLAPGETHTASWGI 284
 
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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