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Conserved domains on  [gi|506351497|ref|WP_015871216|]
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ATP-grasp domain-containing protein [Edwardsiella ictaluri]

Protein Classification

PRK07206 family protein( domain architecture ID 11482629)

PRK07206 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK07206 PRK07206
hypothetical protein; Provisional
 1-413 0e+00

hypothetical protein; Provisional


:

Pssm-ID: 180883 [Multi-domain]  Cd Length: 416  Bit Score: 652.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497   1 MKKIAIVDGFSSGKFIAKELHNMQCKLIHISSSDKLDSYYYNSFDYSIYQENIIHSDLSHTLDFISKFGAECIIAGAESG 80
Cdd:PRK07206   2 MKKVVIVDPFSSGKFLAPAFKKRGIEPIAVTSSCLLDPYYYASFDTSDFIEVIINGDIDDLVEFLRKLGPEAIIAGAESG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497  81 VLLADKLNHTLNLAYSNEYAKTHARRNKFIMLEVLREHGLWPAKQCILSRWDEILTWLEDQPY---PVVLKPIDSAGSDG 157
Cdd:PRK07206  82 VELADRLAEILTPQYSNDPALSSARRNKAEMINALAEAGLPAARQINTADWEEAEAWLRENGLidrPVVIKPLESAGSDG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497 158 VFICHSQDEVRHAFSTLSNKVNKLNLINKTILCQEFLHGTEYVVNFVSLGGHILVSEVVKYHKKRLASGNIVYDIDELID 237
Cdd:PRK07206 162 VFICPAKGDWKHAFNAILGKANKLGLVNETVLVQEYLIGTEYVVNFVSLDGNHLVTEIVRYHKTSLNSGSTVYDYDEFLD 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497 238 YSAPEFNQLVNYVKKVCQCLGIQHGPSHAEVMLTASGPCLVEIAARSDGILRPDVSYLTTGIGQILASAVSIVAPDKFAR 317
Cdd:PRK07206 242 YSEPEYQELVDYTKQALDALGIKNGPAHAEVMLTADGPRLIEIGARLDGGLHPDVARLATGDSQLDATVESLADPDVFRE 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497 318 LVeKPFYHLKNHTFNVGLINDKEAVFTSSKLLVQLKQLASFHRAEFYVDELKSIQQTTDVFSQPGTIYLISKDKAQLWKD 397
Cdd:PRK07206 322 TL-REGYRLKAHVFNVFLISPAAGVFSNVEFLEEIQKLPSFKKSHIYVKEGDYVPQTVDLFSQPGTVYLVHKDKEQLWQD 400

                        410
                 ....*....|....*.
gi 506351497 398 YAAIRHLENTGIYHVT 413
Cdd:PRK07206 401 YEKIRKMESKGVYLLP 416
 
Name Accession Description Interval E-value
PRK07206 PRK07206
hypothetical protein; Provisional
 1-413 0e+00

hypothetical protein; Provisional


Pssm-ID: 180883 [Multi-domain]  Cd Length: 416  Bit Score: 652.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497   1 MKKIAIVDGFSSGKFIAKELHNMQCKLIHISSSDKLDSYYYNSFDYSIYQENIIHSDLSHTLDFISKFGAECIIAGAESG 80
Cdd:PRK07206   2 MKKVVIVDPFSSGKFLAPAFKKRGIEPIAVTSSCLLDPYYYASFDTSDFIEVIINGDIDDLVEFLRKLGPEAIIAGAESG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497  81 VLLADKLNHTLNLAYSNEYAKTHARRNKFIMLEVLREHGLWPAKQCILSRWDEILTWLEDQPY---PVVLKPIDSAGSDG 157
Cdd:PRK07206  82 VELADRLAEILTPQYSNDPALSSARRNKAEMINALAEAGLPAARQINTADWEEAEAWLRENGLidrPVVIKPLESAGSDG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497 158 VFICHSQDEVRHAFSTLSNKVNKLNLINKTILCQEFLHGTEYVVNFVSLGGHILVSEVVKYHKKRLASGNIVYDIDELID 237
Cdd:PRK07206 162 VFICPAKGDWKHAFNAILGKANKLGLVNETVLVQEYLIGTEYVVNFVSLDGNHLVTEIVRYHKTSLNSGSTVYDYDEFLD 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497 238 YSAPEFNQLVNYVKKVCQCLGIQHGPSHAEVMLTASGPCLVEIAARSDGILRPDVSYLTTGIGQILASAVSIVAPDKFAR 317
Cdd:PRK07206 242 YSEPEYQELVDYTKQALDALGIKNGPAHAEVMLTADGPRLIEIGARLDGGLHPDVARLATGDSQLDATVESLADPDVFRE 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497 318 LVeKPFYHLKNHTFNVGLINDKEAVFTSSKLLVQLKQLASFHRAEFYVDELKSIQQTTDVFSQPGTIYLISKDKAQLWKD 397
Cdd:PRK07206 322 TL-REGYRLKAHVFNVFLISPAAGVFSNVEFLEEIQKLPSFKKSHIYVKEGDYVPQTVDLFSQPGTVYLVHKDKEQLWQD 400

                        410
                 ....*....|....*.
gi 506351497 398 YAAIRHLENTGIYHVT 413
Cdd:PRK07206 401 YEKIRKMESKGVYLLP 416
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 58-304 4.81e-55

Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440208 [Multi-domain]  Cd Length: 263  Bit Score: 182.76  E-value: 4.81e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497  58 LSHTLDFISKFGAECIIAGAESGVLLADKLNHTLNLAYsNEYAKTHARRNKFIMLEVLREHGLWPAKQCILSRWDEILTW 137
Cdd:COG0439    6 IAAAAELARETGIDAVLSESEFAVETAAELAEELGLPG-PSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497 138 LEDQPYPVVLKPIDSAGSDGVFICHSQDEVRHAFSTLSNKVNKlNLINKTILCQEFLHGTEYVVNFVSLGGHILVSEVVK 217
Cdd:COG0439   85 AEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKA-GSPNGEVLVEEFLEGREYSVEGLVRDGEVVVCSITR 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497 218 YHKKRLASGNIVYDIDELIdySAPEFNQLVNYVKKVCQCLGIQHGPSHAEVMLTASG-PCLVEIAARSDGILRPDVSYLT 296
Cdd:COG0439  164 KHQKPPYFVELGHEAPSPL--PEELRAEIGELVARALRALGYRRGAFHTEFLLTPDGePYLIEINARLGGEHIPPLTELA 241


                 ....*...
gi 506351497 297 TGIGQILA 304
Cdd:COG0439  242 TGVDLVRE 249
ATP-grasp_4 pfam13535
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ...
 142-284 1.71e-14

ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.


Pssm-ID: 316093 [Multi-domain]  Cd Length: 160  Bit Score: 70.78  E-value: 1.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497  142 PYPVVLKPIDSAGSDGVFICHSQDEVRHAFSTLSNKVNKLN-------LINKTILCQEFLHGTEYVVN-FVSLGGHILVS 213
Cdd:pfam13535   2 PYPCVIKPSVGFFSVGVYKINNREEWKAAFAAIREEIEQWKemypeavVDGGSFLVEEYIEGEEFAVDaYFDENGEPVIL 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506351497  214 EVVkyhKKRLASGNivyDIDELIDYSAPE-----FNQLVNYVKKVCQCLGIQHGPSHAEVMLTASGP-CLVEIAARS 284
Cdd:pfam13535  82 NIL---KHDFASSE---DVSDRIYVTSASiiretQAAFTEFLKRINALLGLKNFPVHIELRVDEDGQiIPIEVNPLR 152
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
 106-193 1.27e-03

alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).


Pssm-ID: 273261 [Multi-domain]  Cd Length: 276  Bit Score: 40.41  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497  106 RNKFIMLEVLREHGLWPAKQCILSRWDEILTWLEDQPYPVVLKPIDSAGSDGVFIChsqdEVRHAFSTLSNKVNKLNLIN 185
Cdd:TIGR00768  87 GDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSLA----RDRQAAESLLEHFEQLNGPQ 162


                  ....*...
gi 506351497  186 KTILCQEF 193
Cdd:TIGR00768 163 NLFLVQEY 170
 
Name Accession Description Interval E-value
PRK07206 PRK07206
hypothetical protein; Provisional
 1-413 0e+00

hypothetical protein; Provisional


Pssm-ID: 180883 [Multi-domain]  Cd Length: 416  Bit Score: 652.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497   1 MKKIAIVDGFSSGKFIAKELHNMQCKLIHISSSDKLDSYYYNSFDYSIYQENIIHSDLSHTLDFISKFGAECIIAGAESG 80
Cdd:PRK07206   2 MKKVVIVDPFSSGKFLAPAFKKRGIEPIAVTSSCLLDPYYYASFDTSDFIEVIINGDIDDLVEFLRKLGPEAIIAGAESG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497  81 VLLADKLNHTLNLAYSNEYAKTHARRNKFIMLEVLREHGLWPAKQCILSRWDEILTWLEDQPY---PVVLKPIDSAGSDG 157
Cdd:PRK07206  82 VELADRLAEILTPQYSNDPALSSARRNKAEMINALAEAGLPAARQINTADWEEAEAWLRENGLidrPVVIKPLESAGSDG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497 158 VFICHSQDEVRHAFSTLSNKVNKLNLINKTILCQEFLHGTEYVVNFVSLGGHILVSEVVKYHKKRLASGNIVYDIDELID 237
Cdd:PRK07206 162 VFICPAKGDWKHAFNAILGKANKLGLVNETVLVQEYLIGTEYVVNFVSLDGNHLVTEIVRYHKTSLNSGSTVYDYDEFLD 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497 238 YSAPEFNQLVNYVKKVCQCLGIQHGPSHAEVMLTASGPCLVEIAARSDGILRPDVSYLTTGIGQILASAVSIVAPDKFAR 317
Cdd:PRK07206 242 YSEPEYQELVDYTKQALDALGIKNGPAHAEVMLTADGPRLIEIGARLDGGLHPDVARLATGDSQLDATVESLADPDVFRE 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497 318 LVeKPFYHLKNHTFNVGLINDKEAVFTSSKLLVQLKQLASFHRAEFYVDELKSIQQTTDVFSQPGTIYLISKDKAQLWKD 397
Cdd:PRK07206 322 TL-REGYRLKAHVFNVFLISPAAGVFSNVEFLEEIQKLPSFKKSHIYVKEGDYVPQTVDLFSQPGTVYLVHKDKEQLWQD 400

                        410
                 ....*....|....*.
gi 506351497 398 YAAIRHLENTGIYHVT 413
Cdd:PRK07206 401 YEKIRKMESKGVYLLP 416
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 58-304 4.81e-55

Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440208 [Multi-domain]  Cd Length: 263  Bit Score: 182.76  E-value: 4.81e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497  58 LSHTLDFISKFGAECIIAGAESGVLLADKLNHTLNLAYsNEYAKTHARRNKFIMLEVLREHGLWPAKQCILSRWDEILTW 137
Cdd:COG0439    6 IAAAAELARETGIDAVLSESEFAVETAAELAEELGLPG-PSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497 138 LEDQPYPVVLKPIDSAGSDGVFICHSQDEVRHAFSTLSNKVNKlNLINKTILCQEFLHGTEYVVNFVSLGGHILVSEVVK 217
Cdd:COG0439   85 AEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKA-GSPNGEVLVEEFLEGREYSVEGLVRDGEVVVCSITR 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497 218 YHKKRLASGNIVYDIDELIdySAPEFNQLVNYVKKVCQCLGIQHGPSHAEVMLTASG-PCLVEIAARSDGILRPDVSYLT 296
Cdd:COG0439  164 KHQKPPYFVELGHEAPSPL--PEELRAEIGELVARALRALGYRRGAFHTEFLLTPDGePYLIEINARLGGEHIPPLTELA 241


                 ....*...
gi 506351497 297 TGIGQILA 304
Cdd:COG0439  242 TGVDLVRE 249
PRK02186 PRK02186
argininosuccinate lyase; Provisional
 106-290 2.17e-16

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 81.43  E-value: 2.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497 106 RNKFIMLEVLREHGLWPAKQCILSRWDEILTWLEDQPYPVVLKPIDSAGSDGVFICHSQDEVRHAFSTLsnkvnkLNLIN 185
Cdd:PRK02186 106 RDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAAL------RRAGT 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497 186 KTILCQEFLHGTEYVVNFVSLGGHILVSEVVKYHKKRLASG-NIVYDIDEliDYSAPEFNQLVNYVKKVCQCLGIQHGPS 264
Cdd:PRK02186 180 RAALVQAYVEGDEYSVETLTVARGHQVLGITRKHLGPPPHFvEIGHDFPA--PLSAPQRERIVRTVLRALDAVGYAFGPA 257

                        170       180
                 ....*....|....*....|....*.
gi 506351497 265 HAEVMLTASGPCLVEIAARSDGILRP 290
Cdd:PRK02186 258 HTELRVRGDTVVIIEINPRLAGGMIP 283
ATP-grasp_4 pfam13535
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ...
 142-284 1.71e-14

ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.


Pssm-ID: 316093 [Multi-domain]  Cd Length: 160  Bit Score: 70.78  E-value: 1.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497  142 PYPVVLKPIDSAGSDGVFICHSQDEVRHAFSTLSNKVNKLN-------LINKTILCQEFLHGTEYVVN-FVSLGGHILVS 213
Cdd:pfam13535   2 PYPCVIKPSVGFFSVGVYKINNREEWKAAFAAIREEIEQWKemypeavVDGGSFLVEEYIEGEEFAVDaYFDENGEPVIL 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506351497  214 EVVkyhKKRLASGNivyDIDELIDYSAPE-----FNQLVNYVKKVCQCLGIQHGPSHAEVMLTASGP-CLVEIAARS 284
Cdd:pfam13535  82 NIL---KHDFASSE---DVSDRIYVTSASiiretQAAFTEFLKRINALLGLKNFPVHIELRVDEDGQiIPIEVNPLR 152
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 106-283 1.61e-11

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 64.91  E-value: 1.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497 106 RNKFIMLEVLREHGLWPAKQCILSRWDEILT--WLEDQPYPVVLKPIDSAGSDGVFICHSQDEVRHAFSTLSNkvnklnl 183
Cdd:PRK12767 110 NDKWLTYEFLKENGIPTPKSYLPESLEDFKAalAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYVPN------- 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497 184 inktILCQEFLHGTEYVVN-FVSLGGHILVSEVVKyhKKRLASGN----IVYDIDELIDysapefnqlvnYVKKVCQCLG 258
Cdd:PRK12767 183 ----LIIQEFIEGQEYTVDvLCDLNGEVISIVPRK--RIEVRAGEtskgVTVKDPELFK-----------LAERLAEALG 245

                        170       180
                 ....*....|....*....|....*
gi 506351497 259 iQHGPSHAEVMLTASGPCLVEIAAR 283
Cdd:PRK12767 246 -ARGPLNIQCFVTDGEPYLFEINPR 269
ATP-grasp_3 pfam02655
ATP-grasp domain; No functional information or experimental verification of function is known ...
 107-283 3.24e-10

ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).


Pssm-ID: 396979 [Multi-domain]  Cd Length: 160  Bit Score: 58.55  E-value: 3.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497  107 NKFIMLEVLREHGLwpakQCILSRWDEILTwleDQPYPVVLKPIDSAGSDGVFIChsqDEVRHAFSTLSNkvnklnlink 186
Cdd:pfam02655   3 DKLKTYKALKNAGV----PTPETLQAEELL---REEKKYVVKPRDGCGGEGVRKV---ENGREDEAFIEN---------- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497  187 tILCQEFLHGTEYVVNFVSLGGHILVSEVVKYHKKRLASGnIVYdIDELIDYSAPEFNQLVNYVKKVCQCLGIQHGPSHA 266
Cdd:pfam02655  63 -VLVQEFIEGEPLSVSLLSDGEKALPLSVNRQYIDNGGSG-FVY-AGNVTPSRTELKEEIIELAEEVVECLPGLRGYVGV 139

                         170
                  ....*....|....*..
gi 506351497  267 EVMLTASGPCLVEIAAR 283
Cdd:pfam02655 140 DLVLKDNEPYVIEVNPR 156
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 106-202 3.95e-10

Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 439959 [Multi-domain]  Cd Length: 289  Bit Score: 60.34  E-value: 3.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497 106 RNKFIMLEVLREHGLWPAKQCILSRWDEILTWLEDQPYPVVLKPIDSAGSDGVFICHSQDEVRHAFSTLsnkvnkLNLIN 185
Cdd:COG0189   95 RDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESILEAL------TELGS 168

                         90       100
                 ....*....|....*....|...
gi 506351497 186 KTILCQEFL---HGTEY---VVN 202
Cdd:COG0189  169 EPVLVQEFIpeeDGRDIrvlVVG 191
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 107-280 1.16e-07

D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440794 [Multi-domain]  Cd Length: 303  Bit Score: 52.80  E-value: 1.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497 107 NKFIMLEVLREHGLwP-AKQCILSR--WDEILTWLEDQPYPVVLKPIDSAGSDGVFICHSQDE----VRHAFStlsnkvn 179
Cdd:COG1181   95 DKALTKRVLAAAGL-PtPPYVVLRRgeLADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEElaaaLEEAFK------- 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497 180 klnlINKTILCQEFLHGTEY---VVNfvslGGHILVSEVVK---------YHKKRLAsGNIVYDIDEliDYSAPEFNQLV 247
Cdd:COG1181  167 ----YDDKVLVEEFIDGREVtvgVLG----NGGPRALPPIEivpengfydYEAKYTD-GGTEYICPA--RLPEELEERIQ 235

                        170       180       190
                 ....*....|....*....|....*....|....
gi 506351497 248 NYVKKVCQCLGIQhGPSHAEVMLTASG-PCLVEI 280
Cdd:COG1181  236 ELALKAFRALGCR-GYARVDFRLDEDGePYLLEV 268
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
62-283 1.55e-07

Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 53.01  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497  62 LDFISKFGAECIIAGAESGVLL----ADKLNHTLNLAYSNeyAKTHAR-RNKFIMLEVLREHGLwPA-KQCILSRWDEIL 135
Cdd:COG3919   69 LELAERHGPDVLIPTGDEYVELlsrhRDELEEHYRLPYPD--ADLLDRlLDKERFYELAEELGV-PVpKTVVLDSADDLD 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497 136 TWLEDQPYPVVLKPIDSA--------GSDGVFICHSQDEVRHAFSTLSNKVNKLnlinktiLCQEFLHG---TEYVVN-F 203
Cdd:COG3919  146 ALAEDLGFPVVVKPADSVgydelsfpGKKKVFYVDDREELLALLRRIAAAGYEL-------IVQEYIPGddgEMRGLTaY 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497 204 VSLGGHILVSEVvkyHKKRLAS----GNIVY----DIDELIDYSApEFNQLVNYvkkvcqclgiqHGPSHAEVMLTASG- 274
Cdd:COG3919  219 VDRDGEVVATFT---GRKLRHYppagGNSAAresvDDPELEEAAR-RLLEALGY-----------HGFANVEFKRDPRDg 283

                        250
                 ....*....|
gi 506351497 275 -PCLVEIAAR 283
Cdd:COG3919  284 eYKLIEINPR 293
PRK14571 PRK14571
D-alanyl-alanine synthetase A; Provisional
 133-223 3.58e-05

D-alanyl-alanine synthetase A; Provisional


Pssm-ID: 184751 [Multi-domain]  Cd Length: 299  Bit Score: 45.20  E-value: 3.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497 133 EILTWLEDQP--YPVVLKPIDSAGSDGVFICHSQDEVRHAFStlsnkvNKLNLINKTILcQEFLHGTEYVVNFVSLGGHI 210
Cdd:PRK14571 114 EIKEFMKTSPlgYPCVVKPRREGSSIGVFICESDEEFQHALK------EDLPRYGSVIV-QEYIPGREMTVSILETEKGF 186

                         90
                 ....*....|...
gi 506351497 211 LVSEVVKYHKKRL 223
Cdd:PRK14571 187 EVLPILELRPKRR 199
ddl PRK01372
D-alanine--D-alanine ligase; Reviewed
 114-280 5.38e-05

D-alanine--D-alanine ligase; Reviewed


Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 44.72  E-value: 5.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497 114 VLREHGLWPAKQCILSRWDEILTWLEDQPYPVVLKPIdSAGSD-GVFICHSQDEVRHAFSTLSNkvnklnlINKTILCQE 192
Cdd:PRK01372 105 VWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKPA-REGSSvGVSKVKEEDELQAALELAFK-------YDDEVLVEK 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497 193 FLHGTEYVVNFvsLGGHIL-VSEVV----------KYhkkrlASGNIVYDI-DELidySAPEFNQLVNYVKKVCQCLGIQ 260
Cdd:PRK01372 177 YIKGRELTVAV--LGGKALpVIEIVpagefydyeaKY-----LAGGTQYICpAGL---PAEIEAELQELALKAYRALGCR 246

                        170       180
                 ....*....|....*....|.
gi 506351497 261 hGPSHAEVMLTASG-PCLVEI 280
Cdd:PRK01372 247 -GWGRVDFMLDEDGkPYLLEV 266
GARS_A pfam01071
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ...
 107-283 3.21e-04

Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the ATP-grasp domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02786).


Pssm-ID: 395851 [Multi-domain]  Cd Length: 194  Bit Score: 41.50  E-value: 3.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497  107 NKFIMLEVLREHGLWPAKQCILSRWDEILTWLEDQPYPV-VLKPIDSAGSDGVFICHSQDE-VRHAFSTLSNKvnKLNLI 184
Cdd:pfam01071   2 SKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAiVVKADGLAAGKGVIVASSNEEaIKAVDEILEQK--KFGEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497  185 NKTILCQEFLHGTEYVVNFVSLGGHILVSEVVKYHkKRLASGN--------------------IVYDIDELIDYSAPEfn 244
Cdd:pfam01071  80 GETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDH-KRAGEGDtgpntggmgayspapvitpeLLERIKETIVEPTVD-- 156

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 506351497  245 qlvNYVKKVCQCLGIQhgpsHAEVMLTASGPCLVEIAAR 283
Cdd:pfam01071 157 ---GLRKEGIPFKGVL----YAGLMLTKDGPKVLEFNCR 188
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
 106-193 1.27e-03

alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).


Pssm-ID: 273261 [Multi-domain]  Cd Length: 276  Bit Score: 40.41  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497  106 RNKFIMLEVLREHGLWPAKQCILSRWDEILTWLEDQPYPVVLKPIDSAGSDGVFIChsqdEVRHAFSTLSNKVNKLNLIN 185
Cdd:TIGR00768  87 GDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSLA----RDRQAAESLLEHFEQLNGPQ 162


                  ....*...
gi 506351497  186 KTILCQEF 193
Cdd:TIGR00768 163 NLFLVQEY 170
Dala_Dala_lig_C pfam07478
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ...
 113-280 1.32e-03

D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).


Pssm-ID: 429483 [Multi-domain]  Cd Length: 204  Bit Score: 39.61  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497  113 EVLREHGLWPAKQCILSRWDEILTwledqpYPVVLKPIDSAGSDGVFICHSQDEVRHAFSTLSNKVNKlnlinktILCQE 192
Cdd:pfam07478  13 VTFTRADWKLNPKEWCAQVEEALG------YPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDEK-------VLVEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497  193 FLHGTEYVV-------NFVSLGGHILVS-EVVKYHKKRLaSGNIVYDIDELIDysAPEFNQLVNYVKKVCQCLGIQhGPS 264
Cdd:pfam07478  80 GIEGREIECavlgnedPEVSPVGEIVPSgGFYDYEAKYI-DDSAQIVVPADLE--EEQEEQIQELALKAYKALGCR-GLA 155

                         170
                  ....*....|....*..
gi 506351497  265 HAEVMLTASG-PCLVEI 280
Cdd:pfam07478 156 RVDFFLTEDGeIVLNEV 172
RimK pfam08443
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ...
 106-194 3.98e-03

RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification enzyme RimK.


Pssm-ID: 369879 [Multi-domain]  Cd Length: 188  Bit Score: 38.25  E-value: 3.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351497  106 RNKFIMLEVLREHGLWPAKQCILSRWDEILTWLE--DQPYPVVLKPIDSAGSDGVFICHSQDEVRHAFSTLsnkvnklnl 183
Cdd:pfam08443   2 RDKAKSHQLLAKHGIGPPNTRLAWYPEDAEQFIEqiKRQFPVIVKSIYGSQGIGVFLAEDEQKLRQTLSAT--------- 72

                          90
                  ....*....|.
gi 506351497  184 iNKTILCQEFL 194
Cdd:pfam08443  73 -NEQILVQEFI 82
 
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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