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Conserved domains on  [gi|502820730|ref|WP_013055706|]
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MULTISPECIES: poly-gamma-glutamate synthase PgsB [Priestia]

Protein Classification

poly_gGlu_PgsB family protein( domain architecture ID 11499291)

poly_gGlu_PgsB family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
poly_gGlu_PgsB TIGR04012
poly-gamma-glutamate synthase PgsB/CapB; Of four genes commonly found to be involved in ...
16-383 0e+00

poly-gamma-glutamate synthase PgsB/CapB; Of four genes commonly found to be involved in biosynthesis and export of poly-gamma-glutamate, pgsB(capB) and pgsC(capC) are found to be involved in the synthesis per se. Members of this family are designated PgsB, a nomeclature that covers both cases in which the poly-gamma-glutamate is secreted and those in which it is retained to form capsular material.PgsB has been shown to have poly-gamma-glutamate activity by itself but is bound tightly by PgsC (TIGR04011). [Cell envelope, Other]


:

Pssm-ID: 188527 [Multi-domain]  Cd Length: 366  Bit Score: 567.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820730   16 VWEYRRHLRKLHSIPVRVNVNGIRGKSTVTRLITGIVKEAGYKTVGKTTGTQARMIYWhTSEEEPIIRrKEGPNIGEQRR 95
Cdd:TIGR04012   1 IFEKIRHDKNLKKIPIRIHVNGTRGKSTVTRLITAGLREGGYKVVGKTTGTDARMIYP-DGSEFPIFR-PGGANIGEQKR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820730   96 VVNEVADIGAEALICECMAVQPDYQITFQNQLIQAKVGVIVNVLEDHMDVMGPTLDEVAQAFTATIPYDGHLVTIEGPYL 175
Cdd:TIGR04012  79 VVKKAVKLKADALVLECMAVQPDYQIVFELKLVKANIGVITNVREDHMDVMGPTLDDVAEAFTATIPYNGDLFTAEDDYL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820730  176 EYYKKIAAERNTKVIVADNDKVSEEYLREFDYMVFPDNASIGLAVAEALGIDAETAMRGMLNAQPDPGAMRITTFGDEKN 255
Cdd:TIGR04012 159 DFFKEAAKDRNTKLIVADAEEISDDILRKFGYIVFPENVALALAVAEALGVDREIALRGMLNAPPDPGAMKILYLNDKNK 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820730  256 PAFLVNGFAANDASSTLRIWERVDSMNYSEKLPIVIMNCRPDRVDRTEQFAEDVMPYIEADVMIAIGQTTSPIAAAYQRG 335
Cdd:TIGR04012 239 RIFFVNAFAANDPVSTERIWDRVCAKGYPTDKPVLIMNCRADRVDRTKQFAEDVLPWSPADKLVLIGEGTELFTSVYKKG 318
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 502820730  336 ELPTKEFWDMEGASTEEILERMKPYLKDRIVYGVGNIHGSAEPLVEAI 383
Cdd:TIGR04012 319 KIPPNKYLNLENKSTIEIVEMILEESSSALIFGVGNIHGGGEELVEYI 366
 
Name Accession Description Interval E-value
poly_gGlu_PgsB TIGR04012
poly-gamma-glutamate synthase PgsB/CapB; Of four genes commonly found to be involved in ...
16-383 0e+00

poly-gamma-glutamate synthase PgsB/CapB; Of four genes commonly found to be involved in biosynthesis and export of poly-gamma-glutamate, pgsB(capB) and pgsC(capC) are found to be involved in the synthesis per se. Members of this family are designated PgsB, a nomeclature that covers both cases in which the poly-gamma-glutamate is secreted and those in which it is retained to form capsular material.PgsB has been shown to have poly-gamma-glutamate activity by itself but is bound tightly by PgsC (TIGR04011). [Cell envelope, Other]


Pssm-ID: 188527 [Multi-domain]  Cd Length: 366  Bit Score: 567.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820730   16 VWEYRRHLRKLHSIPVRVNVNGIRGKSTVTRLITGIVKEAGYKTVGKTTGTQARMIYWhTSEEEPIIRrKEGPNIGEQRR 95
Cdd:TIGR04012   1 IFEKIRHDKNLKKIPIRIHVNGTRGKSTVTRLITAGLREGGYKVVGKTTGTDARMIYP-DGSEFPIFR-PGGANIGEQKR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820730   96 VVNEVADIGAEALICECMAVQPDYQITFQNQLIQAKVGVIVNVLEDHMDVMGPTLDEVAQAFTATIPYDGHLVTIEGPYL 175
Cdd:TIGR04012  79 VVKKAVKLKADALVLECMAVQPDYQIVFELKLVKANIGVITNVREDHMDVMGPTLDDVAEAFTATIPYNGDLFTAEDDYL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820730  176 EYYKKIAAERNTKVIVADNDKVSEEYLREFDYMVFPDNASIGLAVAEALGIDAETAMRGMLNAQPDPGAMRITTFGDEKN 255
Cdd:TIGR04012 159 DFFKEAAKDRNTKLIVADAEEISDDILRKFGYIVFPENVALALAVAEALGVDREIALRGMLNAPPDPGAMKILYLNDKNK 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820730  256 PAFLVNGFAANDASSTLRIWERVDSMNYSEKLPIVIMNCRPDRVDRTEQFAEDVMPYIEADVMIAIGQTTSPIAAAYQRG 335
Cdd:TIGR04012 239 RIFFVNAFAANDPVSTERIWDRVCAKGYPTDKPVLIMNCRADRVDRTKQFAEDVLPWSPADKLVLIGEGTELFTSVYKKG 318
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 502820730  336 ELPTKEFWDMEGASTEEILERMKPYLKDRIVYGVGNIHGSAEPLVEAI 383
Cdd:TIGR04012 319 KIPPNKYLNLENKSTIEIVEMILEESSSALIFGVGNIHGGGEELVEYI 366
Mur_ligase_M pfam08245
Mur ligase middle domain;
40-238 4.39e-07

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 50.00  E-value: 4.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820730   40 GKSTVTRLITGIVKEAGYKTvgKTTGTQARMIYWHTSEEepiirrkegpnIGEQRrVVNEVADIGAEALICE-CMAVQPD 118
Cdd:pfam08245   6 GKTTTTELIAAILSLAGGVI--GTIGTYIGKSGNTTNNA-----------IGLPL-TLAEMVEAGAEYAVLEvSSHGLGE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820730  119 YQItfqNQLIQAKVGVIVNVLEDHMDVMGpTLDEVAQA---FTATIPYDGHLVT-IEGPYLEYYKKIAAERNTKVIVADN 194
Cdd:pfam08245  72 GRL---SGLLKPDIAVFTNISPDHLDFHG-TMENYAKAkaeLFEGLPEDGIAVInADDPYGAFLIAKLKKAGVRVITYGI 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 502820730  195 DKvsEEYLREFDYMVFPDNASIGLAVAEALGIDAETAMRGMLNA 238
Cdd:pfam08245 148 EG--EADLRAANIELSSDGTSFDLFTVPGGELEIEIPLLGRHNV 189
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
128-239 1.40e-05

Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; Folylpolyglutamate synthase/Dihydropteroate synthase is part of the Pathway/BioSystem: Folate biosynthesis


Pssm-ID: 440054 [Multi-domain]  Cd Length: 423  Bit Score: 47.02  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820730 128 IQAKVGVIVNVLEDHMDVMGPTLDEVAQ----AFTATIPydghLVT--IEGPYLEYYKKIAAERNTKVIVADND-KVSEE 200
Cdd:COG0285  153 IDPLVSVITSIGLDHTDFLGDTLEEIARekagIIKPGVP----VVTgdQQPEALEVIEERAAELGAPLYRAGRDfSVEER 228
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820730 201 YLREFDY----MVFPD------------NASIGLAVAEAL-----GIDAETAMRGMLNAQ 239
Cdd:COG0285  229 EGAVFSYqgpgGEYEDlplpllgahqaeNAALALAALEALrelglPISEEAIREGLANAR 288
PRK14016 PRK14016
cyanophycin synthetase; Provisional
27-64 7.37e-03

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 38.60  E-value: 7.37e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 502820730  27 HSIPVrVNVNGIRGKSTVTRLITGIVKEAGYKtVGKTT 64
Cdd:PRK14016 478 GRIPI-VAVTGTNGKTTTTRLIAHILKLSGKR-VGMTT 513
 
Name Accession Description Interval E-value
poly_gGlu_PgsB TIGR04012
poly-gamma-glutamate synthase PgsB/CapB; Of four genes commonly found to be involved in ...
16-383 0e+00

poly-gamma-glutamate synthase PgsB/CapB; Of four genes commonly found to be involved in biosynthesis and export of poly-gamma-glutamate, pgsB(capB) and pgsC(capC) are found to be involved in the synthesis per se. Members of this family are designated PgsB, a nomeclature that covers both cases in which the poly-gamma-glutamate is secreted and those in which it is retained to form capsular material.PgsB has been shown to have poly-gamma-glutamate activity by itself but is bound tightly by PgsC (TIGR04011). [Cell envelope, Other]


Pssm-ID: 188527 [Multi-domain]  Cd Length: 366  Bit Score: 567.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820730   16 VWEYRRHLRKLHSIPVRVNVNGIRGKSTVTRLITGIVKEAGYKTVGKTTGTQARMIYWhTSEEEPIIRrKEGPNIGEQRR 95
Cdd:TIGR04012   1 IFEKIRHDKNLKKIPIRIHVNGTRGKSTVTRLITAGLREGGYKVVGKTTGTDARMIYP-DGSEFPIFR-PGGANIGEQKR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820730   96 VVNEVADIGAEALICECMAVQPDYQITFQNQLIQAKVGVIVNVLEDHMDVMGPTLDEVAQAFTATIPYDGHLVTIEGPYL 175
Cdd:TIGR04012  79 VVKKAVKLKADALVLECMAVQPDYQIVFELKLVKANIGVITNVREDHMDVMGPTLDDVAEAFTATIPYNGDLFTAEDDYL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820730  176 EYYKKIAAERNTKVIVADNDKVSEEYLREFDYMVFPDNASIGLAVAEALGIDAETAMRGMLNAQPDPGAMRITTFGDEKN 255
Cdd:TIGR04012 159 DFFKEAAKDRNTKLIVADAEEISDDILRKFGYIVFPENVALALAVAEALGVDREIALRGMLNAPPDPGAMKILYLNDKNK 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820730  256 PAFLVNGFAANDASSTLRIWERVDSMNYSEKLPIVIMNCRPDRVDRTEQFAEDVMPYIEADVMIAIGQTTSPIAAAYQRG 335
Cdd:TIGR04012 239 RIFFVNAFAANDPVSTERIWDRVCAKGYPTDKPVLIMNCRADRVDRTKQFAEDVLPWSPADKLVLIGEGTELFTSVYKKG 318
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 502820730  336 ELPTKEFWDMEGASTEEILERMKPYLKDRIVYGVGNIHGSAEPLVEAI 383
Cdd:TIGR04012 319 KIPPNKYLNLENKSTIEIVEMILEESSSALIFGVGNIHGGGEELVEYI 366
Mur_ligase_M pfam08245
Mur ligase middle domain;
40-238 4.39e-07

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 50.00  E-value: 4.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820730   40 GKSTVTRLITGIVKEAGYKTvgKTTGTQARMIYWHTSEEepiirrkegpnIGEQRrVVNEVADIGAEALICE-CMAVQPD 118
Cdd:pfam08245   6 GKTTTTELIAAILSLAGGVI--GTIGTYIGKSGNTTNNA-----------IGLPL-TLAEMVEAGAEYAVLEvSSHGLGE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820730  119 YQItfqNQLIQAKVGVIVNVLEDHMDVMGpTLDEVAQA---FTATIPYDGHLVT-IEGPYLEYYKKIAAERNTKVIVADN 194
Cdd:pfam08245  72 GRL---SGLLKPDIAVFTNISPDHLDFHG-TMENYAKAkaeLFEGLPEDGIAVInADDPYGAFLIAKLKKAGVRVITYGI 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 502820730  195 DKvsEEYLREFDYMVFPDNASIGLAVAEALGIDAETAMRGMLNA 238
Cdd:pfam08245 148 EG--EADLRAANIELSSDGTSFDLFTVPGGELEIEIPLLGRHNV 189
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
128-239 1.40e-05

Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; Folylpolyglutamate synthase/Dihydropteroate synthase is part of the Pathway/BioSystem: Folate biosynthesis


Pssm-ID: 440054 [Multi-domain]  Cd Length: 423  Bit Score: 47.02  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820730 128 IQAKVGVIVNVLEDHMDVMGPTLDEVAQ----AFTATIPydghLVT--IEGPYLEYYKKIAAERNTKVIVADND-KVSEE 200
Cdd:COG0285  153 IDPLVSVITSIGLDHTDFLGDTLEEIARekagIIKPGVP----VVTgdQQPEALEVIEERAAELGAPLYRAGRDfSVEER 228
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820730 201 YLREFDY----MVFPD------------NASIGLAVAEAL-----GIDAETAMRGMLNAQ 239
Cdd:COG0285  229 EGAVFSYqgpgGEYEDlplpllgahqaeNAALALAALEALrelglPISEEAIREGLANAR 288
murD TIGR01087
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation ...
33-359 1.15e-03

UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273436 [Multi-domain]  Cd Length: 433  Bit Score: 40.79  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820730   33 VNVNGIRGKSTVTRLITGIVKEAGYKTVgkttgtqarmiywhtseeepiirrkEGPNIGEQrrVVNEVADIGAEALICEC 112
Cdd:TIGR01087 105 VAITGTNGKTTTTSLLYHLLKAAGLKAF-------------------------LGGNIGTP--ALEVLDQEGAELYVLEL 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820730  113 MAVQPDYQITFqnqliQAKVGVIVNVLEDHMDVMGpTLDEVAQA----FTATIPYDGHLVTIEGPYLEYYKKiAAERNTK 188
Cdd:TIGR01087 158 SSFQLETTESL-----RPEIALILNISEDHLDWHG-SFEDYVAAklkiFARQTEGDVAVLNADDPRFARLAQ-KSKAQVI 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820730  189 VIVADNDKVSEEYLREFDYMVFPDNASIGL-------------AVAEALGIDAETAMRGMLNAQPDPGamRITTFGDEKN 255
Cdd:TIGR01087 231 WFSVEKDAERGLCIRDGGLYLKPNDLEGSLlglhnaenilaaiALAKSLGLNLEAILEALRSFKGLPH--RLEYVGQKNG 308
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820730  256 PAFlVNGFAANDASSTLRIWERVDsmnyseKLPIVIMNCRPDRVDRTEQFAEDVMPYIEAdvmIAIGQTTSPIAAAYQRG 335
Cdd:TIGR01087 309 VHF-YNDSKATNVHATLAALSAFD------NPVILIVGGDDKGADFSPLAPAAAGKVKAV---LAIGEDAAKIAPLLKEA 378
                         330       340
                  ....*....|....*....|....
gi 502820730  336 ELPTKEFWDMEGAsTEEILERMKP 359
Cdd:TIGR01087 379 GLSVYLVESLEEA-VQAAREVASP 401
PRK14016 PRK14016
cyanophycin synthetase; Provisional
27-64 7.37e-03

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 38.60  E-value: 7.37e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 502820730  27 HSIPVrVNVNGIRGKSTVTRLITGIVKEAGYKtVGKTT 64
Cdd:PRK14016 478 GRIPI-VAVTGTNGKTTTTRLIAHILKLSGKR-VGMTT 513
 
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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