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Conserved domains on  [gi|297172918|gb|ADI23879|]
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predicted molecular chaperone distantly related to HSP70-fold metalloproteases [uncultured gamma proteobacterium HF4000_48J03]

Protein Classification

anhydro-N-acetylmuramic acid kinase( domain architecture ID 10006420)

anhydro-N-acetylmuramic acid kinase catalyzes hydrolysis of 1,6-anhydro bond of anyhydro-N-acetylmuramic acid (anhMurNAc) and phosphorylates anhMurNAc to produce N-acetyl-muramate-6-phosphate in murein recycling

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AnmK COG2377
1,6-Anhydro-N-acetylmuramate kinase [Cell wall/membrane/envelope biogenesis];
2-365 1.47e-149

1,6-Anhydro-N-acetylmuramate kinase [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 441944  Cd Length: 363  Bit Score: 426.40  E-value: 1.47e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918   2 KSKLYIGVMSGTSMDSMDAALVKIE-NNSWSIINSARREFTPSLREQLL-IFSreSQNISLKDFIVINAKTGIEFSKCIN 79
Cdd:COG2377    1 KPMLVIGLMSGTSLDGIDAALVEFDgEGKVELLAAETVPYPEELRARLLaLCA--PASLSLEELAELDRALGRLFAEAVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918  80 QLIEHQGIKPGDITAVGLHGQTLFHHIESQYSGSLQIGSPSIVAEKTNIAVVADFRNSDIAAGGQGAPLAPVFHSWMFGS 159
Cdd:COG2377   79 ALLAKAGLSAEDIDAIGSHGQTVRHRPEGRPGFTLQIGDGALLAELTGIPVVADFRSRDVAAGGQGAPLVPAFHQALFSD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918 160 NKHKRILINIGGIANISILLNKKSFFGYDIGPGNALLDAWIAKNKQEKYDNKGEWSKSGKPNMKLLKIFKSDPFFKKTPP 239
Cdd:COG2377  159 PGEPRAVLNIGGIANITYLPPGGPVIAFDTGPGNALLDAWVQRHGGKPYDKDGAWAASGKVDEALLARLLADPYFALPPP 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918 240 KSTGSHDFNLEWILSTKKRFGqrLLAKDIQATLTLLTAELIVDAINKCPKDSD-IAFSGGGIKNLSLMALIKNKLSGRHI 318
Cdd:COG2377  239 KSTGRELFNLAWLEQLLAGFG--LSPEDVQATLTELTAASIADAIRRLPPPPDrVLVCGGGAHNPTLMERLQALLPGVPV 316
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 297172918 319 QSTTDWGIAPEWVEAAGFAFLAHQRMQAKPVELTKTTGSKKKSVLGA 365
Cdd:COG2377  317 VTTDELGIDPDAKEALAFAWLAVRTLRGLPGNLPSVTGAKRPVILGA 363
 
Name Accession Description Interval E-value
AnmK COG2377
1,6-Anhydro-N-acetylmuramate kinase [Cell wall/membrane/envelope biogenesis];
2-365 1.47e-149

1,6-Anhydro-N-acetylmuramate kinase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441944  Cd Length: 363  Bit Score: 426.40  E-value: 1.47e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918   2 KSKLYIGVMSGTSMDSMDAALVKIE-NNSWSIINSARREFTPSLREQLL-IFSreSQNISLKDFIVINAKTGIEFSKCIN 79
Cdd:COG2377    1 KPMLVIGLMSGTSLDGIDAALVEFDgEGKVELLAAETVPYPEELRARLLaLCA--PASLSLEELAELDRALGRLFAEAVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918  80 QLIEHQGIKPGDITAVGLHGQTLFHHIESQYSGSLQIGSPSIVAEKTNIAVVADFRNSDIAAGGQGAPLAPVFHSWMFGS 159
Cdd:COG2377   79 ALLAKAGLSAEDIDAIGSHGQTVRHRPEGRPGFTLQIGDGALLAELTGIPVVADFRSRDVAAGGQGAPLVPAFHQALFSD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918 160 NKHKRILINIGGIANISILLNKKSFFGYDIGPGNALLDAWIAKNKQEKYDNKGEWSKSGKPNMKLLKIFKSDPFFKKTPP 239
Cdd:COG2377  159 PGEPRAVLNIGGIANITYLPPGGPVIAFDTGPGNALLDAWVQRHGGKPYDKDGAWAASGKVDEALLARLLADPYFALPPP 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918 240 KSTGSHDFNLEWILSTKKRFGqrLLAKDIQATLTLLTAELIVDAINKCPKDSD-IAFSGGGIKNLSLMALIKNKLSGRHI 318
Cdd:COG2377  239 KSTGRELFNLAWLEQLLAGFG--LSPEDVQATLTELTAASIADAIRRLPPPPDrVLVCGGGAHNPTLMERLQALLPGVPV 316
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 297172918 319 QSTTDWGIAPEWVEAAGFAFLAHQRMQAKPVELTKTTGSKKKSVLGA 365
Cdd:COG2377  317 VTTDELGIDPDAKEALAFAWLAVRTLRGLPGNLPSVTGAKRPVILGA 363
anmK PRK09585
anhydro-N-acetylmuramic acid kinase; Reviewed
3-369 1.01e-142

anhydro-N-acetylmuramic acid kinase; Reviewed


Pssm-ID: 236579  Cd Length: 365  Bit Score: 409.13  E-value: 1.01e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918   3 SKLYIGVMSGTSMDSMDAALVKIENNSWS--IINSARREFTPSLREQLL-IFSREsqNISLKDFIVINAKTGIEFSKCIN 79
Cdd:PRK09585   1 SMRYIGLMSGTSLDGVDAALVEIDGEGTKveLLASATVPYPDELRAALLaLLQGG--ADELERLAELDTALGRLFAEAVN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918  80 QLIEHQGIKPGDITAVGLHGQTLFHhiESQYSGSLQIGSPSIVAEKTNIAVVADFRNSDIAAGGQGAPLAPVFHSWMFGS 159
Cdd:PRK09585  79 ALLAEAGLSPEDIDAIGSHGQTVRH--RPGEGFTLQIGDGALIAELTGITVVADFRRRDVAAGGQGAPLVPAFHQALFGH 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918 160 NKHKRILINIGGIANISILL-NKKSFFGYDIGPGNALLDAWIAKNKQEKYDNKGEWSKSGKPNMKLLKIFKSDPFFKKTP 238
Cdd:PRK09585 157 PDETRAVLNIGGIANITLLPpGGGPVIGFDTGPGNALIDAWIQRHGGKPYDKDGAWAASGKVDEALLARLLAHPYFALPP 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918 239 PKSTGSHDFNLEWILSTKKRFGqrLLAKDIQATLTLLTAELIVDAINKCPKDSD-IAFSGGGIKNLSLMALIKNKLSGRh 317
Cdd:PRK09585 237 PKSTGRELFNLAWLERQLAGFG--LSPEDVQATLTELTAASIARAVRRLPPGPDeLLVCGGGARNPTLMERLAALLPTE- 313
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 297172918 318 IQSTTDWGIAPEWVEAAGFAFLAHQRMQAKPVELTKTTGSKKKSVLGAIYLP 369
Cdd:PRK09585 314 VATTDALGIDGDAKEALAFAWLAVRTLRGLPGNLPSVTGASGPVVLGAIYPA 365
ASKHA_NBD_ANMK cd24050
nucleotide-binding domain (NBD) of anhydro-N-acetylmuramic acid kinase (ANMK) and similar ...
6-368 5.06e-142

nucleotide-binding domain (NBD) of anhydro-N-acetylmuramic acid kinase (ANMK) and similar proteins; ANMK (EC 2.7.1.170), also called AnhMurNAc kinase, catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. It is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling.


Pssm-ID: 466900  Cd Length: 369  Bit Score: 407.69  E-value: 5.06e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918   6 YIGVMSGTSMDSMDAALVKIE----NNSWSIINSARREFTPSLREQLLIFSREsQNISLKDFIVINAKTGIEFSKCINQL 81
Cdd:cd24050    1 YIGLMSGTSLDGIDAALVEIDgdgtELRVKLLAFHSVPYPKDLREKLLELCQP-GTDTLDELCRLNFELGELFAEAVLEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918  82 IEHQGIKPGDITAVGLHGQTLFHHIESQYSGS-LQIGSPSIVAEKTNIAVVADFRNSDIAAGGQGAPLAPVFHSWMFGSN 160
Cdd:cd24050   80 LAKSGISPSDIDAIGSHGQTVWHRPEPERVGFtLQIGDPAVIAERTGITVVSDFRRADMAAGGQGAPLVPAFDYALFADP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918 161 KHKRILINIGGIANISILL-NKKSFFGYDIGPGNALLDAWIAKNKQEKYDNKGEWSKSGKPNMKLLKIFKSDPFFKKTPP 239
Cdd:cd24050  160 DETRAVLNIGGIANVTYLPpGSDDVIGFDTGPGNMLIDAWVQRLTGLPYDKDGEIAASGKVDEALLARLLDDPYFALPPP 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918 240 KSTGSHDFNLEWiLSTKKRFGQRLLAKDIQATLTLLTAELIVDAINKC--PKDSDIAFSGGGIKNLSLMALIKNKLSGRH 317
Cdd:cd24050  240 KSTGRELFNLAW-LEELLKRAPGLSPEDIVATLTAFTARSIADAYRKFvpPGPDEVIVCGGGAHNPTLMRRLRELLPGIK 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 297172918 318 IQSTTDWGIAPEWVEAAGFAFLAHQRMQAKPVELTKTTGSKKKSVLGAIYL 368
Cdd:cd24050  319 VKTTDELGISSDAKEAMAFAWLAYRTLNGLPGNLPSVTGASKPVVLGKIYP 369
AnmK pfam03702
Anhydro-N-acetylmuramic acid kinase; Anhydro-N-acetylmuramic acid kinase catalyzes the ...
5-367 2.77e-130

Anhydro-N-acetylmuramic acid kinase; Anhydro-N-acetylmuramic acid kinase catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. It is also required for the utilization of anhMurNAc, either imported from the medium, or derived from its own cell wall murein, and in so doing plays a role in cell wall recycling.


Pssm-ID: 397660  Cd Length: 364  Bit Score: 377.50  E-value: 2.77e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918    5 LYIGVMSGTSMDSMDAALVKIENNSWSIINSARREFTPSLREQLLIFSrESQNISLKDFIVINAKTGIEFSKCINQLIEH 84
Cdd:pfam03702   2 RYIGLMSGTSLDGVDAALVDLDDARVELLASHFSPMPAGLRQQLLDLC-QGGATTLQRLGELDHQLGLLFADAVNALLQK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918   85 QGIKPGDITAVGLHGQTLFHHIESQYSGSLQIGSPSIVAEKTNIAVVADFRNSDIAAGGQGAPLAPVFHSWMFGSNKHKR 164
Cdd:pfam03702  81 QNLSPEQIRAIGCHGQTVRHEPEGAVPFTMQLGDANLIAERTGITVVADFRRRDVAAGGQGAPLVPAFHEALFAAPNETR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918  165 ILINIGGIANISILLNKKSFFGYDIGPGNALLDAWIAKNKQEKYDNKGEWSKSGKPNMKLLKIFKSDPFFKKTPPKSTGS 244
Cdd:pfam03702 161 AVLNIGGIANVSVLPPGAPVLGFDTGPGNMLMDAWIQKHRGEPYDKDGEWAASGKVNPALLAVLLADPYFALPAPKSTGR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918  245 HDFNLEWILSTKKRFgqRLLAKDIQATLTLLTAELIVDAINKC-PKDSDIAFSGGGIKNLSLMALIKNKLSGRHIQSTTD 323
Cdd:pfam03702 241 ELFNLPWLETHLAKH--PVAAADVQATLAELTAVTIVDALLQAqPDCERLLVCGGGARNPLLMARLAALLPGVQVASTDA 318
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 297172918  324 WGIAPEWVEAAGFAFLAHQRMQAKPVELTKTTGSKKKSVLGAIY 367
Cdd:pfam03702 319 YGLDPDYMEAMAFAWLAARTLNGLPGNLPSVTGASRARSLGAIY 362
 
Name Accession Description Interval E-value
AnmK COG2377
1,6-Anhydro-N-acetylmuramate kinase [Cell wall/membrane/envelope biogenesis];
2-365 1.47e-149

1,6-Anhydro-N-acetylmuramate kinase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441944  Cd Length: 363  Bit Score: 426.40  E-value: 1.47e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918   2 KSKLYIGVMSGTSMDSMDAALVKIE-NNSWSIINSARREFTPSLREQLL-IFSreSQNISLKDFIVINAKTGIEFSKCIN 79
Cdd:COG2377    1 KPMLVIGLMSGTSLDGIDAALVEFDgEGKVELLAAETVPYPEELRARLLaLCA--PASLSLEELAELDRALGRLFAEAVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918  80 QLIEHQGIKPGDITAVGLHGQTLFHHIESQYSGSLQIGSPSIVAEKTNIAVVADFRNSDIAAGGQGAPLAPVFHSWMFGS 159
Cdd:COG2377   79 ALLAKAGLSAEDIDAIGSHGQTVRHRPEGRPGFTLQIGDGALLAELTGIPVVADFRSRDVAAGGQGAPLVPAFHQALFSD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918 160 NKHKRILINIGGIANISILLNKKSFFGYDIGPGNALLDAWIAKNKQEKYDNKGEWSKSGKPNMKLLKIFKSDPFFKKTPP 239
Cdd:COG2377  159 PGEPRAVLNIGGIANITYLPPGGPVIAFDTGPGNALLDAWVQRHGGKPYDKDGAWAASGKVDEALLARLLADPYFALPPP 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918 240 KSTGSHDFNLEWILSTKKRFGqrLLAKDIQATLTLLTAELIVDAINKCPKDSD-IAFSGGGIKNLSLMALIKNKLSGRHI 318
Cdd:COG2377  239 KSTGRELFNLAWLEQLLAGFG--LSPEDVQATLTELTAASIADAIRRLPPPPDrVLVCGGGAHNPTLMERLQALLPGVPV 316
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 297172918 319 QSTTDWGIAPEWVEAAGFAFLAHQRMQAKPVELTKTTGSKKKSVLGA 365
Cdd:COG2377  317 VTTDELGIDPDAKEALAFAWLAVRTLRGLPGNLPSVTGAKRPVILGA 363
anmK PRK09585
anhydro-N-acetylmuramic acid kinase; Reviewed
3-369 1.01e-142

anhydro-N-acetylmuramic acid kinase; Reviewed


Pssm-ID: 236579  Cd Length: 365  Bit Score: 409.13  E-value: 1.01e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918   3 SKLYIGVMSGTSMDSMDAALVKIENNSWS--IINSARREFTPSLREQLL-IFSREsqNISLKDFIVINAKTGIEFSKCIN 79
Cdd:PRK09585   1 SMRYIGLMSGTSLDGVDAALVEIDGEGTKveLLASATVPYPDELRAALLaLLQGG--ADELERLAELDTALGRLFAEAVN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918  80 QLIEHQGIKPGDITAVGLHGQTLFHhiESQYSGSLQIGSPSIVAEKTNIAVVADFRNSDIAAGGQGAPLAPVFHSWMFGS 159
Cdd:PRK09585  79 ALLAEAGLSPEDIDAIGSHGQTVRH--RPGEGFTLQIGDGALIAELTGITVVADFRRRDVAAGGQGAPLVPAFHQALFGH 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918 160 NKHKRILINIGGIANISILL-NKKSFFGYDIGPGNALLDAWIAKNKQEKYDNKGEWSKSGKPNMKLLKIFKSDPFFKKTP 238
Cdd:PRK09585 157 PDETRAVLNIGGIANITLLPpGGGPVIGFDTGPGNALIDAWIQRHGGKPYDKDGAWAASGKVDEALLARLLAHPYFALPP 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918 239 PKSTGSHDFNLEWILSTKKRFGqrLLAKDIQATLTLLTAELIVDAINKCPKDSD-IAFSGGGIKNLSLMALIKNKLSGRh 317
Cdd:PRK09585 237 PKSTGRELFNLAWLERQLAGFG--LSPEDVQATLTELTAASIARAVRRLPPGPDeLLVCGGGARNPTLMERLAALLPTE- 313
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 297172918 318 IQSTTDWGIAPEWVEAAGFAFLAHQRMQAKPVELTKTTGSKKKSVLGAIYLP 369
Cdd:PRK09585 314 VATTDALGIDGDAKEALAFAWLAVRTLRGLPGNLPSVTGASGPVVLGAIYPA 365
ASKHA_NBD_ANMK cd24050
nucleotide-binding domain (NBD) of anhydro-N-acetylmuramic acid kinase (ANMK) and similar ...
6-368 5.06e-142

nucleotide-binding domain (NBD) of anhydro-N-acetylmuramic acid kinase (ANMK) and similar proteins; ANMK (EC 2.7.1.170), also called AnhMurNAc kinase, catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. It is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling.


Pssm-ID: 466900  Cd Length: 369  Bit Score: 407.69  E-value: 5.06e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918   6 YIGVMSGTSMDSMDAALVKIE----NNSWSIINSARREFTPSLREQLLIFSREsQNISLKDFIVINAKTGIEFSKCINQL 81
Cdd:cd24050    1 YIGLMSGTSLDGIDAALVEIDgdgtELRVKLLAFHSVPYPKDLREKLLELCQP-GTDTLDELCRLNFELGELFAEAVLEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918  82 IEHQGIKPGDITAVGLHGQTLFHHIESQYSGS-LQIGSPSIVAEKTNIAVVADFRNSDIAAGGQGAPLAPVFHSWMFGSN 160
Cdd:cd24050   80 LAKSGISPSDIDAIGSHGQTVWHRPEPERVGFtLQIGDPAVIAERTGITVVSDFRRADMAAGGQGAPLVPAFDYALFADP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918 161 KHKRILINIGGIANISILL-NKKSFFGYDIGPGNALLDAWIAKNKQEKYDNKGEWSKSGKPNMKLLKIFKSDPFFKKTPP 239
Cdd:cd24050  160 DETRAVLNIGGIANVTYLPpGSDDVIGFDTGPGNMLIDAWVQRLTGLPYDKDGEIAASGKVDEALLARLLDDPYFALPPP 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918 240 KSTGSHDFNLEWiLSTKKRFGQRLLAKDIQATLTLLTAELIVDAINKC--PKDSDIAFSGGGIKNLSLMALIKNKLSGRH 317
Cdd:cd24050  240 KSTGRELFNLAW-LEELLKRAPGLSPEDIVATLTAFTARSIADAYRKFvpPGPDEVIVCGGGAHNPTLMRRLRELLPGIK 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 297172918 318 IQSTTDWGIAPEWVEAAGFAFLAHQRMQAKPVELTKTTGSKKKSVLGAIYL 368
Cdd:cd24050  319 VKTTDELGISSDAKEAMAFAWLAYRTLNGLPGNLPSVTGASKPVVLGKIYP 369
AnmK pfam03702
Anhydro-N-acetylmuramic acid kinase; Anhydro-N-acetylmuramic acid kinase catalyzes the ...
5-367 2.77e-130

Anhydro-N-acetylmuramic acid kinase; Anhydro-N-acetylmuramic acid kinase catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. It is also required for the utilization of anhMurNAc, either imported from the medium, or derived from its own cell wall murein, and in so doing plays a role in cell wall recycling.


Pssm-ID: 397660  Cd Length: 364  Bit Score: 377.50  E-value: 2.77e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918    5 LYIGVMSGTSMDSMDAALVKIENNSWSIINSARREFTPSLREQLLIFSrESQNISLKDFIVINAKTGIEFSKCINQLIEH 84
Cdd:pfam03702   2 RYIGLMSGTSLDGVDAALVDLDDARVELLASHFSPMPAGLRQQLLDLC-QGGATTLQRLGELDHQLGLLFADAVNALLQK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918   85 QGIKPGDITAVGLHGQTLFHHIESQYSGSLQIGSPSIVAEKTNIAVVADFRNSDIAAGGQGAPLAPVFHSWMFGSNKHKR 164
Cdd:pfam03702  81 QNLSPEQIRAIGCHGQTVRHEPEGAVPFTMQLGDANLIAERTGITVVADFRRRDVAAGGQGAPLVPAFHEALFAAPNETR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918  165 ILINIGGIANISILLNKKSFFGYDIGPGNALLDAWIAKNKQEKYDNKGEWSKSGKPNMKLLKIFKSDPFFKKTPPKSTGS 244
Cdd:pfam03702 161 AVLNIGGIANVSVLPPGAPVLGFDTGPGNMLMDAWIQKHRGEPYDKDGEWAASGKVNPALLAVLLADPYFALPAPKSTGR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918  245 HDFNLEWILSTKKRFgqRLLAKDIQATLTLLTAELIVDAINKC-PKDSDIAFSGGGIKNLSLMALIKNKLSGRHIQSTTD 323
Cdd:pfam03702 241 ELFNLPWLETHLAKH--PVAAADVQATLAELTAVTIVDALLQAqPDCERLLVCGGGARNPLLMARLAALLPGVQVASTDA 318
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 297172918  324 WGIAPEWVEAAGFAFLAHQRMQAKPVELTKTTGSKKKSVLGAIY 367
Cdd:pfam03702 319 YGLDPDYMEAMAFAWLAARTLNGLPGNLPSVTGASRARSLGAIY 362
ASKHA_NBD_LGK cd24051
nucleotide-binding domain (NBD) of levoglucosan kinase (LGK) and similar proteins; LGK (EC 2.7. ...
7-366 1.23e-56

nucleotide-binding domain (NBD) of levoglucosan kinase (LGK) and similar proteins; LGK (EC 2.7.1.232) catalyzes the transfer of a phosphate group from ATP to levoglucosan (1,6-anhydro-beta-D-glucopyranose, LG) to yield glucose 6-phosphate in the presence of magnesium ion and ATP. In addition to the canonical kinase phosphotransfer reaction, the conversion requires cleavage of the 1,6-anhydro ring to allow ATP-dependent phosphorylation of the sugar O-6 atom.


Pssm-ID: 466901  Cd Length: 409  Bit Score: 190.06  E-value: 1.23e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918   7 IGVMSGTSMDSMDAALVKIENNS------WSIINSARREFTPSLREQLLIFSRESQNiSLKDFIVINAKTGIEFSKCINQ 80
Cdd:cd24051    4 LGLNSGTSMDGIDCALCHFTQKTpdapmeFELIEYGEVPLAQPIKQRVMSMILEDTT-SPSELSEVNVILGETFADAVRQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918  81 LIEHQGIKPGDITAVGLHGQTLFHHI---ESQYSGSLQIGSPSIVAEKTNIAVVADFRNSDIAAGGQGAPLAPVFHSWMF 157
Cdd:cd24051   83 FAAERNVDLSDIDAIASHGQTIWLLSmpeEGQVKSALTMGEGAIIAARTGITSVTDFRISDQAAGRQGAPLIAFFDALLL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918 158 GSNKHKRILINIGGIANISIL-----LNKKSFFGYDIGPGNALLDAWIAK--NKQEKYDNKGEWSKSGKPNMKLLKIFKS 230
Cdd:cd24051  163 HHPTKLRACQNIGGIANVCFIppdndGRTDEYYDFDTGPGNVFIDAVVRHftNGEQEYDKDGAMGKRGKVDQELVDDFLK 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918 231 DPFFKKTPPKSTGSHDFNLEWILSTKKRFGQRLLA-KDIQATLTLLTAELIVDAI---NKCPKDSDIAFSGGGIKNLSLM 306
Cdd:cd24051  243 MPYFQLDPPKTTGREVFRDTLAHDLIRRAEAKGLSpDDIVATTTRITAQSIVDHYrryAPSQEIDEIFMCGGGAFNPNIV 322
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918 307 ALIKNKLSGRHIQSTTDWGIAPEWVEAAGFAFLAHQRMQAKPVELTKTTGSKKKSVLGAI 366
Cdd:cd24051  323 EFIQQSYPGTKIMMLDEAGVPAGAKEAITFAWQGMEALVGRSIPVPTRVETRQHTVLGKV 382
ASKHA_NBD_ANMK-like cd24005
nucleotide-binding domain (NBD) of the anhydro-N-acetylmuramic acid kinase (ANMK)-like domain ...
7-366 2.01e-43

nucleotide-binding domain (NBD) of the anhydro-N-acetylmuramic acid kinase (ANMK)-like domain family; The family includes anhydro-N-acetylmuramic acid kinase (ANMK) and levoglucosan kinase (LGK). ANMK (EC 2.7.1.170), also called AnhMurNAc kinase, catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. It is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. LGK (EC 2.7.1.232) catalyzes the transfer of a phosphate group from ATP to levoglucosan (1,6-anhydro-beta-D-glucopyranose, LG) to yield glucose 6-phosphate in the presence of magnesium ion and ATP. In addition to the canonical kinase phosphotransfer reaction, the conversion requires cleavage of the 1,6-anhydro ring to allow ATP-dependent phosphorylation of the sugar O-6 atom. The ANMK-like family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466855  Cd Length: 358  Bit Score: 154.10  E-value: 2.01e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918   7 IGVMSGTSMDSMDAALVKIENnSWSIINSARREFTPSLREQLLIFSRESQNiSLKDFIVINAKTGIEFSKCINQLIEHQG 86
Cdd:cd24005    2 LGLMSGTSLDGMDIVLIEQGD-RTTLLASHYLPMPAGLREDILALCVPGPD-EIARAAEVEQRWVALAAQGVRELLLQQQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918  87 IKPGDITAVGLHGQTLFhhIESQYSGSLQIGSPSIVAEKTNIAVVADFRNSDIAAGGQGAPLAPVFHSWMFGSNKHKRIL 166
Cdd:cd24005   80 MSPDEVRAIGSHGQTIR--HEPARHFTVQIGNPALLAELTGIDVVADFRRRDVAAGGQGAPLVPAFHQALFGDDDTSRAV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918 167 INIGGIANISILLNKKSFFGYDIGPGNALLDAWIAKNKQEKYDNKGEWSKSGKPNMKLLKIFKSDPFFKKTPPKSTGSHD 246
Cdd:cd24005  158 LNIGGFSNVSLLSPGKPVRGFDCGPGNVLMDAWIHHQRGEHFDRDGAWAASGQVNHALLASLLADEFFAARGPKSTGRER 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297172918 247 FNlEWILSTKKRFGQRLLAKDIQATLTLLTAELIVDAINK-CPKDSDIAFSGGGIKNLSLMALIKNKLSGRHIQSTTDWG 325
Cdd:cd24005  238 FN-LPWLQEHLARHPALPAADIQATLLELSARSISESLLDaQPDCEEVLVCGGGAFNTALMKRLAMLMPEARVASTDEYG 316
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 297172918 326 IAPEWVEAAGFAFLAHQRMQAKPVELTKTTGSKKKSVLGAI 366
Cdd:cd24005  317 IPPAWMEGMAFAWLAHRFLERLPGNCPDVTGALGPRTLGAL 357
 
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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