NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2794512207|ref|WP_372416999|]
View 

folylpolyglutamate synthase/dihydrofolate synthase family protein [Fusobacterium animalis]

Protein Classification

bifunctional folylpolyglutamate synthase/dihydrofolate synthase( domain architecture ID 11416298)

bifunctional folylpolyglutamate synthase (FGPS)/dihydrofolate synthase (DHFS) functions in two distinct reactions of the de novo folate biosynthetic pathway, catalyzing the addition of a glutamate residue to dihydropteroate to form dihydrofolate and the successive additions of L-glutamate to tetrahydrofolate, leading to folylpolyglutamate derivatives

CATH:  3.40.1190.10|3.90.190.20
EC:  6.3.2.-
Gene Ontology:  GO:0004326|GO:0008841|GO:0005524|GO:0006730|GO:0046872
SCOP:  4000353

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
 5-404 1.16e-163

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: 466.50  E-value: 1.16e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207   5 MN-IDALLKELYAYSMFSIRLGLDNIKEICKYLGNPQNSYKVIHITGTNGKGSVSTTVERILLEAGYKVGKYTSPHILEF 83
Cdd:COG0285     1 MTtYQEALAYLESLHPFGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207  84 NERISFNDKYISNEDIAKYYEKVKKIIDEH-NIQATFFEVTTAMMFDYFKDMKADYVILEAGMGGRYDATNICDNIVSVI 162
Cdd:COG0285    81 NERIRINGEPISDEELVEALEEVEPAVEEVdAGPPTFFEVTTAAAFLYFAEAPVDVAVLEVGLGGRLDATNVIDPLVSVI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 163 TNVSLEHTEYLGDTIYKIAKEKAGIIK-NCPyTIFADNNPDVKKAIEEATDKyvnvlekyKNST---YNLDFNTFSTN-- 236
Cdd:COG0285   161 TSIGLDHTDFLGDTLEEIAREKAGIIKpGVP-VVTGDQQPEALEVIEERAAE--------LGAPlyrAGRDFSVEEREga 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 237 -IFINGNKYEY-----SLFGDYQYKNFLCAYEVVKYL-----GIDENIIKEAVKKVVWQCRFEVYSKNPLVIFDGAHNLA 305
Cdd:COG0285   232 vFSYQGPGGEYedlplPLLGAHQAENAALALAALEALrelglPISEEAIREGLANARWPGRLEVLSRGPLVILDGAHNPA 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 306 GVEELTKIVKQHFSKDEVTVLVSILKDKDRVSMFRKLNEISSCIILTSiPDNPRASTAKELYDYVENK-KDFEYEEDPIK 384
Cdd:COG0285   312 GARALAETLKELFPFRKLHLVFGMLADKDIEGMLAALAPLADEVIVTT-PPSPRALDAEELAEAARELgLRVEVAPDVEE 390

                         410       420
                  ....*....|....*....|..
gi 2794512207 385 AYNLALS--KKRKLTVCCGSFY 404
Cdd:COG0285   391 ALEAALElaDPDDLILVTGSLY 412
 
Name Accession Description Interval E-value
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
 5-404 1.16e-163

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: 466.50  E-value: 1.16e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207   5 MN-IDALLKELYAYSMFSIRLGLDNIKEICKYLGNPQNSYKVIHITGTNGKGSVSTTVERILLEAGYKVGKYTSPHILEF 83
Cdd:COG0285     1 MTtYQEALAYLESLHPFGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207  84 NERISFNDKYISNEDIAKYYEKVKKIIDEH-NIQATFFEVTTAMMFDYFKDMKADYVILEAGMGGRYDATNICDNIVSVI 162
Cdd:COG0285    81 NERIRINGEPISDEELVEALEEVEPAVEEVdAGPPTFFEVTTAAAFLYFAEAPVDVAVLEVGLGGRLDATNVIDPLVSVI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 163 TNVSLEHTEYLGDTIYKIAKEKAGIIK-NCPyTIFADNNPDVKKAIEEATDKyvnvlekyKNST---YNLDFNTFSTN-- 236
Cdd:COG0285   161 TSIGLDHTDFLGDTLEEIAREKAGIIKpGVP-VVTGDQQPEALEVIEERAAE--------LGAPlyrAGRDFSVEEREga 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 237 -IFINGNKYEY-----SLFGDYQYKNFLCAYEVVKYL-----GIDENIIKEAVKKVVWQCRFEVYSKNPLVIFDGAHNLA 305
Cdd:COG0285   232 vFSYQGPGGEYedlplPLLGAHQAENAALALAALEALrelglPISEEAIREGLANARWPGRLEVLSRGPLVILDGAHNPA 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 306 GVEELTKIVKQHFSKDEVTVLVSILKDKDRVSMFRKLNEISSCIILTSiPDNPRASTAKELYDYVENK-KDFEYEEDPIK 384
Cdd:COG0285   312 GARALAETLKELFPFRKLHLVFGMLADKDIEGMLAALAPLADEVIVTT-PPSPRALDAEELAEAARELgLRVEVAPDVEE 390

                         410       420
                  ....*....|....*....|..
gi 2794512207 385 AYNLALS--KKRKLTVCCGSFY 404
Cdd:COG0285   391 ALEAALElaDPDDLILVTGSLY 412
folC TIGR01499
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ...
 26-405 1.34e-122

folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of folate pathway proteins. Most examples are bifunctional, active as both folylpolyglutamate synthetase (EC 6.3.2.17) and dihydrofolate synthetase (EC 6.3.2.12). The two activities are similar - ATP + glutamate + dihydropteroate or tetrahydrofolyl-[Glu](n) = ADP + orthophosphate + dihydrofolate or tetrahydrofolyl-[Glu](n+1). A mutation study of the FolC gene of E. coli suggests that both activities belong to the same active site. Because some examples are monofunctional (and these cannot be separated phylogenetically), the model is treated as subfamily, not equivalog. [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]


Pssm-ID: 273659 [Multi-domain]  Cd Length: 397  Bit Score: 360.83  E-value: 1.34e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207  26 LDNIKEICKYLGNPQNSYKVIHITGTNGKGSVSTTVERILLEAGYKVGKYTSPHILEFNERISFNDKYISNEDIAKYYEK 105
Cdd:TIGR01499   1 LERMKKLLEALGNPQDLYPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPISDEELAQAFEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 106 VKKIIDEHNIQATFFEVTTAMMFDYFKDMKADYVILEAGMGGRYDATNICDNIVSVITNVSLEHTEYLGDTIYKIAKEKA 185
Cdd:TIGR01499  81 VRPILESLSQQPTYFELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVIEPLVSVITSIGLDHTEILGDTLEEIAWEKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 186 GIIKNCPYTIFADNNPDV-----KKAIEEAT-----DKYVNVLEKYKNSTYNLDFNTFSTNIFIngnkyeySLFGDYQYK 255
Cdd:TIGR01499 161 GIIKEGVPIVTGEQEPEAlnvlkKKAQEKGAplfvvGRDFNYSETDENYLSFSGANLFLEPLAL-------SLLGDHQQE 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 256 NF---LCAYEVVK--YLGIDENIIKEAVKKVVWQCRFEVYSK-NPLVIFDGAHNLAGVEELTKIVKQHFSKDEVTVLVSI 329
Cdd:TIGR01499 234 NAalaLAALEVLGkqNPKLSEEAIRQGLANTIWPGRLEILSEdNPNILLDGAHNPHSAEALAEWFKKRFNGRPITLLFGA 313

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2794512207 330 LKDKDRVSMFRKLNEISSCIILTSIPDNPRASTAKELYDYVEnKKDFEYEEDPIKAYNLALSKK-RKLTVCCGSFYI 405
Cdd:TIGR01499 314 LADKDAAAMLAPLKPVVDKEVFVTPFDYPRADDAADLAAFAE-ETGKSTVEDWREALEEALNASaEDDILVTGSLYL 389
PRK10846 PRK10846
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional
 21-415 1.51e-50

bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional


Pssm-ID: 182774 [Multi-domain]  Cd Length: 416  Bit Score: 175.65  E-value: 1.51e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207  21 SIRLGLDNIKEICKYLGNPQNSYKVIHITGTNGKGSVSTTVERILLEAGYKVGKYTSPHILEFNERISFNDKYISNEDIA 100
Cdd:PRK10846   27 TIDLGLERVSQVAARLDLLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYRVGVYSSPHLVRYTERVRIQGQELPESAHT 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 101 KYYEKVKKIIDEhnIQATFFEVTTAMMFDYFKDMKADYVILEAGMGGRYDATNICDNIVSVITNVSLEHTEYLGDTIYKI 180
Cdd:PRK10846  107 ASFAEIEAARGD--ISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVTSIALDHTDWLGPDRESI 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 181 AKEKAGIIKNCPYTIFADnnPDVKKAIEE-ATDKYVNVLEKYKNSTYNLDFNTFStniFINGNKYEYSL-FGDYQYKNFL 258
Cdd:PRK10846  185 GREKAGIFRAEKPAVVGE--PDMPSTIADvAQEKGALLQRRGVDWNYSVTDHDWA---FSDGDGTLENLpLPNVPLPNAA 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 259 CAYEVVKY--LGIDENIIKEAVKKVVWQCRFEVYSKNPLVIFDGAHNLAGVEELTKIVKQHFSKDEVTVLVSILKDKDRV 336
Cdd:PRK10846  260 TALAALRAsgLEVSEQAIRDGIASAILPGRFQIVSESPRVILDVAHNPHAAEYLTGRLKALPKNGRVLAVIGMLHDKDIA 339

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 337 SMFRKLNEISSCIILTSIpDNPRASTAKELYDYVENKKDFeyeEDPIKAYNLALS--KKRKLTVCCGSFYILIKLKEGLN 414
Cdd:PRK10846  340 GTLACLKSVVDDWYCAPL-EGPRGATAEQLAEHLGNGKSF---DSVAQAWDAAMAdaKPEDTVLVCGSFHTVAHVMEVID 415


                  .
gi 2794512207 415 G 415
Cdd:PRK10846  416 A 416
Mur_ligase_M pfam08245
Mur ligase middle domain;
48-260 1.07e-11

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 63.48  E-value: 1.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207  48 ITGTNGKGSVSTTVERILLEAGYK---VGKYTSPHILEFNERIsfndkyisnediakyyekvkkiidehNIQATFFEvtt 124
Cdd:pfam08245   1 VTGTNGKTTTTELIAAILSLAGGVigtIGTYIGKSGNTTNNAI--------------------------GLPLTLAE--- 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 125 ammfdyFKDMKADYVILEAGMGGRYDA--TNICDNIVSVITNVSLEHTEYLGdTIYKIAKEKAGIIKNCP----YTIFAD 198
Cdd:pfam08245  52 ------MVEAGAEYAVLEVSSHGLGEGrlSGLLKPDIAVFTNISPDHLDFHG-TMENYAKAKAELFEGLPedgiAVINAD 124

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2794512207 199 nNPDVKKAIEEATDKYVNVL-----EKYKNSTYNLDFNTFSTNIFI---NGNKYEYS--LFGDYQYKNFLCA 260
Cdd:pfam08245 125 -DPYGAFLIAKLKKAGVRVItygieGEADLRAANIELSSDGTSFDLftvPGGELEIEipLLGRHNVYNALAA 195
 
Name Accession Description Interval E-value
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
 5-404 1.16e-163

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: 466.50  E-value: 1.16e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207   5 MN-IDALLKELYAYSMFSIRLGLDNIKEICKYLGNPQNSYKVIHITGTNGKGSVSTTVERILLEAGYKVGKYTSPHILEF 83
Cdd:COG0285     1 MTtYQEALAYLESLHPFGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207  84 NERISFNDKYISNEDIAKYYEKVKKIIDEH-NIQATFFEVTTAMMFDYFKDMKADYVILEAGMGGRYDATNICDNIVSVI 162
Cdd:COG0285    81 NERIRINGEPISDEELVEALEEVEPAVEEVdAGPPTFFEVTTAAAFLYFAEAPVDVAVLEVGLGGRLDATNVIDPLVSVI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 163 TNVSLEHTEYLGDTIYKIAKEKAGIIK-NCPyTIFADNNPDVKKAIEEATDKyvnvlekyKNST---YNLDFNTFSTN-- 236
Cdd:COG0285   161 TSIGLDHTDFLGDTLEEIAREKAGIIKpGVP-VVTGDQQPEALEVIEERAAE--------LGAPlyrAGRDFSVEEREga 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 237 -IFINGNKYEY-----SLFGDYQYKNFLCAYEVVKYL-----GIDENIIKEAVKKVVWQCRFEVYSKNPLVIFDGAHNLA 305
Cdd:COG0285   232 vFSYQGPGGEYedlplPLLGAHQAENAALALAALEALrelglPISEEAIREGLANARWPGRLEVLSRGPLVILDGAHNPA 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 306 GVEELTKIVKQHFSKDEVTVLVSILKDKDRVSMFRKLNEISSCIILTSiPDNPRASTAKELYDYVENK-KDFEYEEDPIK 384
Cdd:COG0285   312 GARALAETLKELFPFRKLHLVFGMLADKDIEGMLAALAPLADEVIVTT-PPSPRALDAEELAEAARELgLRVEVAPDVEE 390

                         410       420
                  ....*....|....*....|..
gi 2794512207 385 AYNLALS--KKRKLTVCCGSFY 404
Cdd:COG0285   391 ALEAALElaDPDDLILVTGSLY 412
folC TIGR01499
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ...
 26-405 1.34e-122

folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of folate pathway proteins. Most examples are bifunctional, active as both folylpolyglutamate synthetase (EC 6.3.2.17) and dihydrofolate synthetase (EC 6.3.2.12). The two activities are similar - ATP + glutamate + dihydropteroate or tetrahydrofolyl-[Glu](n) = ADP + orthophosphate + dihydrofolate or tetrahydrofolyl-[Glu](n+1). A mutation study of the FolC gene of E. coli suggests that both activities belong to the same active site. Because some examples are monofunctional (and these cannot be separated phylogenetically), the model is treated as subfamily, not equivalog. [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]


Pssm-ID: 273659 [Multi-domain]  Cd Length: 397  Bit Score: 360.83  E-value: 1.34e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207  26 LDNIKEICKYLGNPQNSYKVIHITGTNGKGSVSTTVERILLEAGYKVGKYTSPHILEFNERISFNDKYISNEDIAKYYEK 105
Cdd:TIGR01499   1 LERMKKLLEALGNPQDLYPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPISDEELAQAFEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 106 VKKIIDEHNIQATFFEVTTAMMFDYFKDMKADYVILEAGMGGRYDATNICDNIVSVITNVSLEHTEYLGDTIYKIAKEKA 185
Cdd:TIGR01499  81 VRPILESLSQQPTYFELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVIEPLVSVITSIGLDHTEILGDTLEEIAWEKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 186 GIIKNCPYTIFADNNPDV-----KKAIEEAT-----DKYVNVLEKYKNSTYNLDFNTFSTNIFIngnkyeySLFGDYQYK 255
Cdd:TIGR01499 161 GIIKEGVPIVTGEQEPEAlnvlkKKAQEKGAplfvvGRDFNYSETDENYLSFSGANLFLEPLAL-------SLLGDHQQE 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 256 NF---LCAYEVVK--YLGIDENIIKEAVKKVVWQCRFEVYSK-NPLVIFDGAHNLAGVEELTKIVKQHFSKDEVTVLVSI 329
Cdd:TIGR01499 234 NAalaLAALEVLGkqNPKLSEEAIRQGLANTIWPGRLEILSEdNPNILLDGAHNPHSAEALAEWFKKRFNGRPITLLFGA 313

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2794512207 330 LKDKDRVSMFRKLNEISSCIILTSIPDNPRASTAKELYDYVEnKKDFEYEEDPIKAYNLALSKK-RKLTVCCGSFYI 405
Cdd:TIGR01499 314 LADKDAAAMLAPLKPVVDKEVFVTPFDYPRADDAADLAAFAE-ETGKSTVEDWREALEEALNASaEDDILVTGSLYL 389
PRK10846 PRK10846
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional
 21-415 1.51e-50

bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional


Pssm-ID: 182774 [Multi-domain]  Cd Length: 416  Bit Score: 175.65  E-value: 1.51e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207  21 SIRLGLDNIKEICKYLGNPQNSYKVIHITGTNGKGSVSTTVERILLEAGYKVGKYTSPHILEFNERISFNDKYISNEDIA 100
Cdd:PRK10846   27 TIDLGLERVSQVAARLDLLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYRVGVYSSPHLVRYTERVRIQGQELPESAHT 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 101 KYYEKVKKIIDEhnIQATFFEVTTAMMFDYFKDMKADYVILEAGMGGRYDATNICDNIVSVITNVSLEHTEYLGDTIYKI 180
Cdd:PRK10846  107 ASFAEIEAARGD--ISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVTSIALDHTDWLGPDRESI 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 181 AKEKAGIIKNCPYTIFADnnPDVKKAIEE-ATDKYVNVLEKYKNSTYNLDFNTFStniFINGNKYEYSL-FGDYQYKNFL 258
Cdd:PRK10846  185 GREKAGIFRAEKPAVVGE--PDMPSTIADvAQEKGALLQRRGVDWNYSVTDHDWA---FSDGDGTLENLpLPNVPLPNAA 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 259 CAYEVVKY--LGIDENIIKEAVKKVVWQCRFEVYSKNPLVIFDGAHNLAGVEELTKIVKQHFSKDEVTVLVSILKDKDRV 336
Cdd:PRK10846  260 TALAALRAsgLEVSEQAIRDGIASAILPGRFQIVSESPRVILDVAHNPHAAEYLTGRLKALPKNGRVLAVIGMLHDKDIA 339

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 337 SMFRKLNEISSCIILTSIpDNPRASTAKELYDYVENKKDFeyeEDPIKAYNLALS--KKRKLTVCCGSFYILIKLKEGLN 414
Cdd:PRK10846  340 GTLACLKSVVDDWYCAPL-EGPRGATAEQLAEHLGNGKSF---DSVAQAWDAAMAdaKPEDTVLVCGSFHTVAHVMEVID 415


                  .
gi 2794512207 415 G 415
Cdd:PRK10846  416 A 416
PLN02913 PLN02913
dihydrofolate synthetase
 36-342 4.26e-40

dihydrofolate synthetase


Pssm-ID: 178501 [Multi-domain]  Cd Length: 510  Bit Score: 149.58  E-value: 4.26e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207  36 LGNPQNSYKVIHITGTNGKGSVSTTVERILLEAGYKVGKYTSPHILEFNERISFND--KYISNEDIAKYYEKVKKIIDE- 112
Cdd:PLN02913   68 LGNPHSKFKAVHVAGTKGKGSTAAFLSNILRAQGYSVGCYTSPHLRSIRERISVGKlgKPVSTNTLNDLFHGIKPILDEa 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 113 ---HNIQATFFEVTTAMMFDYFKDMKADYVILEAGMGGRYDATNICDN---IVSVITNVSLEHTEYLGDTIYKIAKEKAG 186
Cdd:PLN02913  148 iqlENGSLTHFEVLTALAFKLFAQENVDIAVIEAGLGGARDATNVIDSsglAASVITTIGEEHLAALGGSLESIALAKSG 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 187 IIKN-CPYTIFADNNPDVKKAIEE-----------ATDKYVNVLEKyknSTYNLDFNTFST-----------NIFINGNK 243
Cdd:PLN02913  228 IIKQgRPVVLGGPFLPHIESILRDkassmnspvvsASDPGVRSSIK---GIITDNGKPCQScdivirvekddPLFIELSD 304

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 244 YEYSLFGDYQYKNFL---CAYEVVKYLG--IDENIIKEAVKKVVWQCRFEVYSKNPL---------VIFDGAHNLAGVEE 309
Cdd:PLN02913  305 VNLRMLGSHQLQNAVtaaCAALCLRDQGwrISDASIRAGLENTNLLGRSQFLTSKEAevlglpgatVLLDGAHTKESAKA 384

                         330       340       350
                  ....*....|....*....|....*....|...
gi 2794512207 310 LTKIVKQHFSKDEVTVLVSILKDKDRVSMFRKL 342
Cdd:PLN02913  385 LVDTIKTAFPEARLALVVAMASDKDHLAFASEF 417
PLN02881 PLN02881
tetrahydrofolylpolyglutamate synthase
 44-189 4.87e-35

tetrahydrofolylpolyglutamate synthase


Pssm-ID: 215476  Cd Length: 530  Bit Score: 135.56  E-value: 4.87e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207  44 KVIHITGTNGKGSVSTTVERILLEAGYKVGKYTSPHILEFNERISFNDKYISNEDIAKY----YEKVKKIIDEHNIQATF 119
Cdd:PLN02881   62 KVIHVAGTKGKGSTCTFTESILRNCGFRTGLFTSPHLIDVRERFRLDGVDISEEKFLRYfwwcWDRLKEKTTEDLPMPAY 141

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2794512207 120 FEVTTAMMFDYFKDMKADYVILEAGMGGRYDATNICDN-IVSVITNVSLEHTEYLGDTIYKIAKEKAGIIK 189
Cdd:PLN02881  142 FRFLTLLAFKIFSAEQVDVAILEVGLGGRLDATNVVQKpVVCGITSLGYDHMEILGDTLGKIAGEKAGIFK 212
murE TIGR01085
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ...
 35-359 9.09e-16

UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase. An exception is Staphylococcus aureus, in which diaminopimelate is replaced by lysine in the peptidoglycan and MurE is EC 6.3.2.7. The Mycobacteria, part of the closest neighboring branch outside of the low-GC Gram-positive bacteria, use diaminopimelate. A close homolog, scoring just below the trusted cutoff, is found (with introns) in Arabidopsis thaliana. Its role is unknown. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273435 [Multi-domain]  Cd Length: 464  Bit Score: 78.90  E-value: 9.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207  35 YLGNPQNSYKVIHITGTNGKGSVSTTVERILLEAGYKVGKY-TSPHILEFNERISFNDKyisnediakyyekvkkiideh 113
Cdd:TIGR01085  77 FYGHPSKKLKVIGVTGTNGKTTTTSLIAQLLRLLGKKTGLIgTIGYRLGGNDLIKNPAA--------------------- 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 114 niQATFFEVTTAMMFDYFKDMKADYVILEA---GMG-GRYDAtniCDNIVSVITNVSLEHTEYLGdTI--YKIAKEK--- 184
Cdd:TIGR01085 136 --LTTPEALTLQSTLAEMVEAGAQYAVMEVsshALAqGRVRG---VRFDAAVFTNLSRDHLDFHG-TMenYFAAKASlft 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 185 -------AGIIKNCPYTifADNNPDVKKAIeeaTDKYVNVLEKYK-------NSTYNLDFNTFsTNIFINGN-KYEYSLF 249
Cdd:TIGR01085 210 elglkrfAVINLDDEYG--AQFVKRLPKDI---TVSAITQPADGRaqdikitDSGYSFEGQQF-TFETPAGEgHLHTPLI 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 250 GDYQYKNFLCAYEVVKYLG-IDENIIKEAVKKVVWQC-RFEV--YSKNPLVIFDGAHNLAGVEELTKIVKQHfSKDEVTV 325
Cdd:TIGR01085 284 GRFNVYNLLAALATLLHLGgIDLEDIVAALEKFRGVPgRMELvdGGQKFLVIVDYAHTPDALEKALRTLRKH-KDGRLIV 362

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 2794512207 326 LVSILKDKDRVSMFrKLNEISS----CIILTSipDNPR 359
Cdd:TIGR01085 363 VFGCGGDRDRGKRP-LMGAIAEqladLVILTS--DNPR 397
murE PRK00139
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
 35-359 4.35e-13

UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional


Pssm-ID: 234660 [Multi-domain]  Cd Length: 460  Bit Score: 70.55  E-value: 4.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207  35 YLGNPQNSYKVIHITGTNGKGSVSTTVERILLEAGYKVGkytsphiLefnerisfndkyISNEDIakyyekvkkIIDEHN 114
Cdd:PRK00139   87 FYGHPSDKLKLIGVTGTNGKTTTAYLLAQILRLLGEKTA-------L------------IGTLGN---------GIGGEL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 115 IQATFfevTT-------AMMFDyFKDMKADYVILEA---GMG-GRYDATNICdniVSVITNVSLEHTEYLGdTI--YKIA 181
Cdd:PRK00139  139 IPSGL---TTpdaldlqRLLAE-LVDAGVTYAAMEVsshALDqGRVDGLKFD---VAVFTNLSRDHLDYHG-TMedYLAA 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 182 KEKagiikncpytIFADNNPdvkKAIEEATDKY-VNVLE-------KYKNSTY---NLDFNTFSTNIFINGnKYEYSLFG 250
Cdd:PRK00139  211 KAR----------LFSELGL---AAVINADDEVgRRLLAlpdayavSMAGADLratDVEYTDSGQTFTLVT-EVESPLIG 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 251 DYQYKNFLCAYEVVKYLGIDENIIKEAVKKVVWQC-RFEVYS--KNPLVIFDGAHNLAGVEELTKIVKQHFSKDevtvLV 327
Cdd:PRK00139  277 RFNVSNLLAALAALLALGVPLEDALAALAKLQGVPgRMERVDagQGPLVIVDYAHTPDALEKVLEALRPHAKGR----LI 352

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 2794512207 328 SIL-----KDKDRvsmfRKL-----NEISSCIILTSipDNPR 359
Cdd:PRK00139  353 CVFgcggdRDKGK----RPLmgaiaERLADVVIVTS--DNPR 388
Mur_ligase_M pfam08245
Mur ligase middle domain;
48-260 1.07e-11

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 63.48  E-value: 1.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207  48 ITGTNGKGSVSTTVERILLEAGYK---VGKYTSPHILEFNERIsfndkyisnediakyyekvkkiidehNIQATFFEvtt 124
Cdd:pfam08245   1 VTGTNGKTTTTELIAAILSLAGGVigtIGTYIGKSGNTTNNAI--------------------------GLPLTLAE--- 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 125 ammfdyFKDMKADYVILEAGMGGRYDA--TNICDNIVSVITNVSLEHTEYLGdTIYKIAKEKAGIIKNCP----YTIFAD 198
Cdd:pfam08245  52 ------MVEAGAEYAVLEVSSHGLGEGrlSGLLKPDIAVFTNISPDHLDFHG-TMENYAKAKAELFEGLPedgiAVINAD 124

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2794512207 199 nNPDVKKAIEEATDKYVNVL-----EKYKNSTYNLDFNTFSTNIFI---NGNKYEYS--LFGDYQYKNFLCA 260
Cdd:pfam08245 125 -DPYGAFLIAKLKKAGVRVItygieGEADLRAANIELSSDGTSFDLftvPGGELEIEipLLGRHNVYNALAA 195
MurE COG0769
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
 37-359 2.27e-10

UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramyl tripeptide synthase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440532 [Multi-domain]  Cd Length: 459  Bit Score: 62.02  E-value: 2.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207  37 GNPQNSYKVIHITGTNGKGSVSTTVERILLEAGYKVGkytsphilefnerisfndkYISNediakyyekVKKIIDEHNIQ 116
Cdd:COG0769    74 GHPSQKLKLIGVTGTNGKTTTTYLLAQILRALGKKTG-------------------LIGT---------VGNGIGGELIP 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 117 ATFfevTT------AMMFDYFKDMKADYVILEA-GMG---GRYDATNICdniVSVITNVSLEHTEYLGdTI--YKIAKEK 184
Cdd:COG0769   126 SSL---TTpealdlQRLLAEMVDAGVTHVVMEVsSHAldqGRVDGVRFD---VAVFTNLTRDHLDYHG-TMeaYFAAKAR 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 185 agiikncpytIFADNNPDvKKAIEEATDKYVNVL-EKYKNS--TY-----------NLDFNTFSTNIFIN--GNKYEYS- 247
Cdd:COG0769   199 ----------LFDQLGPG-GAAVINADDPYGRRLaAAAPARviTYglkadadlratDIELSADGTRFTLVtpGGEVEVRl 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 248 -LFGDYQYKNFLCAYEVVKYLGIDENIIKEAVKKVVWQC-RFEVYS--KNPLVIFDGAHNLAGVEELTKIVKQHfSKDEV 323
Cdd:COG0769   268 pLIGRFNVYNALAAIAAALALGIDLEEILAALEKLKGVPgRMERVDggQGPTVIVDYAHTPDALENVLEALRPH-TKGRL 346

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 2794512207 324 TVLVSILKDKDRVsmFRKLN-----EISSCIILTSipDNPR 359
Cdd:COG0769   347 IVVFGCGGDRDRG--KRPLMgeiaaRLADVVIVTS--DNPR 383
MurF COG0770
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
 137-281 3.25e-10

UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramyl pentapeptide synthase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440533 [Multi-domain]  Cd Length: 451  Bit Score: 61.66  E-value: 3.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 137 DYVILEAGMGGRYDATNICDnI----VSVITNVSLEHTEYLGdTIYKIAKEKAGIIKNCPYT----IFADNnPDVKKAIE 208
Cdd:COG0770   153 EFAVLEMGMNHPGEIAYLAR-IarpdIAVITNIGPAHLEGFG-SLEGIARAKGEIFEGLPPGgvavLNADD-PLLAALAE 229

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2794512207 209 EATDKYVNV-LEKY-----KNSTYNLDFNTFSTNIFINGNKYEYSLFGDYQYKNFLCAYEVVKYLGIDENIIKEAVKKV 281
Cdd:COG0770   230 RAKARVLTFgLSEDadvraEDIELDEDGTRFTLHTPGGELEVTLPLPGRHNVSNALAAAAVALALGLDLEEIAAGLAAF 308
PRK11929 PRK11929
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ...
 35-371 8.03e-09

bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE/UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase MurF;


Pssm-ID: 237025 [Multi-domain]  Cd Length: 958  Bit Score: 57.79  E-value: 8.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207  35 YLGNPQNSYKVIHITGTNGKGSVSTTVERILLEAGYKVGKytsphilefnerISFNDKYISNEDIAKYYekvkKIIDEHN 114
Cdd:PRK11929  104 WYGRPSEQLSLVAVTGTNGKTSCAQLLAQLLTRLGKPCGS------------IGTLGARLDGRLIPGSL----TTPDAII 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 115 IQATFfevttAMMfdyfKDMKADYVILEAGMGG----RYDATNIcdnIVSVITNVSLEHTEYLGdTIYKIAKEKAGIIKN 190
Cdd:PRK11929  168 LHRIL-----ARM----RAAGADAVAMEASSHGleqgRLDGLRI---AVAGFTNLTRDHLDYHG-TMQDYEEAKAALFSK 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 191 CPYTIFADNNPDVK-----KAIEEATDKYVNVLEKYKNSTYNLDFNTFSTNIFI----NGNKYEY--SLFGDYQYKNFLC 259
Cdd:PRK11929  235 LPGLGAAVINADDPaaarlLAALPRGLKVGYSPQNAGADVQARDLRATAHGQVFtlatPDGSYQLvtRLLGRFNVSNLLL 314

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 260 AYEVVKYLGIDENIIKEAVKKVV-----WQCRFEVYSKN-PLVIFDGAHN---LAGVEELTKIVKQHFSKDevtvLVSIL 330
Cdd:PRK11929  315 VAAALKKLGLPLAQIARALAAVSpvpgrMERVGPTAGAQgPLVVVDYAHTpdaLAKALTALRPVAQARNGR----LVCVF 390

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 2794512207 331 -----KDKD-RVSMFRKLNEISSCIILTSipDNPRASTAKELYDYVE 371
Cdd:PRK11929  391 gcggdRDKGkRPEMGRIAAELADRVVVTS--DNPRSEAPEAIIDQIL 435
Mur_ligase_C pfam02875
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ...
 286-360 4.41e-05

Mur ligase family, glutamate ligase domain; This family contains a number of related ligase enzymes which have EC numbers 6.3.2.*. This family includes: MurC, MurD, MurE, MurF, Mpl and FolC. MurC, MurD, Mure and MurF catalyze consecutive steps in the synthesis of peptidoglycan. Peptidoglycan consists of a sheet of two sugar derivatives, with one of these N-acetylmuramic acid attaching to a small pentapeptide. The pentapeptide is is made of L-alanine, D-glutamic acid, Meso-diaminopimelic acid and D-alanyl alanine. The peptide moiety is synthesized by successively adding these amino acids to UDP-N-acetylmuramic acid. MurC transfers the L-alanine, MurD transfers the D-glutamate, MurE transfers the diaminopimelic acid, and MurF transfers the D-alanyl alanine. This family also includes Folylpolyglutamate synthase that transfers glutamate to folylpolyglutamate.


Pssm-ID: 460731 [Multi-domain]  Cd Length: 87  Bit Score: 41.95  E-value: 4.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794512207 286 RFEV--YSKNPLVIFDGAHNLAGVEELTKIVKQHFSKDeVTVLVSILKDKD---RVSMFRKLNEISSCIILTsiPDNPRA 360
Cdd:pfam02875   4 RLEVvgENNGVLVIDDYAHNPDAMEAALRALRNLFPGR-LILVFGGMGDRDaefHALLGRLAAALADVVILT--GDYPRA 80
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
 44-73 3.92e-03

UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440534 [Multi-domain]  Cd Length: 445  Bit Score: 39.29  E-value: 3.92e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2794512207  44 KVIHITGTNGKGSVSTTVERILLEAGYKVG 73
Cdd:COG0771   106 PIIAITGTNGKTTTTTLIGHILKAAGLRVA 135
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH