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Conserved domains on  [gi|498528234|ref|WP_010827760|]
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folylpolyglutamate synthase/dihydrofolate synthase family protein [Enterococcus faecalis]

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

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List of domain hits

 Name Accession Description Interval E-value
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
 4-432 0e+00

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: 562.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234   4 TIEEAIEWIHSRLPFGSRPGLDRINALLEKIDHPENKVPTIHIAGTNGKGSTVTYLRCLLEEMGLKVGTFTSPYIESFNE 83
Cdd:COG0285    3 TYQEALAYLESLHPFGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRFNE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234  84 RIAINGQPISDEQLITYVEKYQPIIKELDKITevagITEFETLTGMALDYFVNEQVDIAVVEVGLGGLLDSTNVVKPLLT 163
Cdd:COG0285   83 RIRINGEPISDEELVEALEEVEPAVEEVDAGP----PTFFEVTTAAAFLYFAEAPVDVAVLEVGLGGRLDATNVIDPLVS 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 164 GITTIGKDHTEILGETIAEIAYQKAGIIKEKVPVVTGNICADALAVIEKVAQEKQSPIFRFGKEYQVEYLHpdtqwGEVF 243
Cdd:COG0285  159 VITSIGLDHTDFLGDTLEEIAREKAGIIKPGVPVVTGDQQPEALEVIEERAAELGAPLYRAGRDFSVEERE-----GAVF 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 244 NFYGEMGKLTKIKVPLLGRHQVENAAVAIQLFDKYCQLqHLPFKERDITQGLAKAQWPARMERLSDEPLIVLDGAHNDHA 323
Cdd:COG0285  234 SYQGPGGEYEDLPLPLLGAHQAENAALALAALEALREL-GLPISEEAIREGLANARWPGRLEVLSRGPLVILDGAHNPAG 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 324 VKRLVENLRKEFPQHTIHILFSALATKDVDEMIQDLKQVPNaHLYLTSFDYPKAIALTEMEKY---EDDLTEIVSLWQFG 400
Cdd:COG0285  313 ARALAETLKELFPFRKLHLVFGMLADKDIEGMLAALAPLAD-EVIVTTPPSPRALDAEELAEAareLGLRVEVAPDVEEA 391

                        410       420       430
                 ....*....|....*....|....*....|..
gi 498528234 401 LGEILEKMSADDLLLVTGSLYFVSQVRELLLT 432
Cdd:COG0285  392 LEAALELADPDDLILVTGSLYLVGEVRALLGR 423
 
Name Accession Description Interval E-value
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
 4-432 0e+00

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: 562.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234   4 TIEEAIEWIHSRLPFGSRPGLDRINALLEKIDHPENKVPTIHIAGTNGKGSTVTYLRCLLEEMGLKVGTFTSPYIESFNE 83
Cdd:COG0285    3 TYQEALAYLESLHPFGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRFNE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234  84 RIAINGQPISDEQLITYVEKYQPIIKELDKITevagITEFETLTGMALDYFVNEQVDIAVVEVGLGGLLDSTNVVKPLLT 163
Cdd:COG0285   83 RIRINGEPISDEELVEALEEVEPAVEEVDAGP----PTFFEVTTAAAFLYFAEAPVDVAVLEVGLGGRLDATNVIDPLVS 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 164 GITTIGKDHTEILGETIAEIAYQKAGIIKEKVPVVTGNICADALAVIEKVAQEKQSPIFRFGKEYQVEYLHpdtqwGEVF 243
Cdd:COG0285  159 VITSIGLDHTDFLGDTLEEIAREKAGIIKPGVPVVTGDQQPEALEVIEERAAELGAPLYRAGRDFSVEERE-----GAVF 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 244 NFYGEMGKLTKIKVPLLGRHQVENAAVAIQLFDKYCQLqHLPFKERDITQGLAKAQWPARMERLSDEPLIVLDGAHNDHA 323
Cdd:COG0285  234 SYQGPGGEYEDLPLPLLGAHQAENAALALAALEALREL-GLPISEEAIREGLANARWPGRLEVLSRGPLVILDGAHNPAG 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 324 VKRLVENLRKEFPQHTIHILFSALATKDVDEMIQDLKQVPNaHLYLTSFDYPKAIALTEMEKY---EDDLTEIVSLWQFG 400
Cdd:COG0285  313 ARALAETLKELFPFRKLHLVFGMLADKDIEGMLAALAPLAD-EVIVTTPPSPRALDAEELAEAareLGLRVEVAPDVEEA 391

                        410       420       430
                 ....*....|....*....|....*....|..
gi 498528234 401 LGEILEKMSADDLLLVTGSLYFVSQVRELLLT 432
Cdd:COG0285  392 LEAALELADPDDLILVTGSLYLVGEVRALLGR 423
folC TIGR01499
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ...
 24-430 5.60e-178

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: 502.58  E-value: 5.60e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234   24 LDRINALLEKIDHPENKVPTIHIAGTNGKGSTVTYLRCLLEEMGLKVGTFTSPYIESFNERIAINGQPISDEQLITYVEK 103
Cdd:TIGR01499   1 LERMKKLLEALGNPQDLYPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPISDEELAQAFEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234  104 YQPIIKELDKitevaGITEFETLTGMALDYFVNEQVDIAVVEVGLGGLLDSTNVVKPLLTGITTIGKDHTEILGETIAEI 183
Cdd:TIGR01499  81 VRPILESLSQ-----QPTYFELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVIEPLVSVITSIGLDHTEILGDTLEEI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234  184 AYQKAGIIKEKVPVVTGNICADALAVIEKVAQEKQSPIFRFGKEYQVEYLHPDTqwgevFNFYGEMGKLTKIKVPLLGRH 263
Cdd:TIGR01499 156 AWEKAGIIKEGVPIVTGEQEPEALNVLKKKAQEKGAPLFVVGRDFNYSETDENY-----LSFSGANLFLEPLALSLLGDH 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234  264 QVENAAVAIQLFDKYCQlQHLPFKERDITQGLAKAQWPARMERLSDE-PLIVLDGAHNDHAVKRLVENLRKEFPQHTIHI 342
Cdd:TIGR01499 231 QQENAALALAALEVLGK-QNPKLSEEAIRQGLANTIWPGRLEILSEDnPNILLDGAHNPHSAEALAEWFKKRFNGRPITL 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234  343 LFSALATKDVDEMIQDLKQVPNAHLYLTSFDYPKA-IALTEMEKYEDDLTEIVSLWQFGLGEIlEKMSADDLLLVTGSLY 421
Cdd:TIGR01499 310 LFGALADKDAAAMLAPLKPVVDKEVFVTPFDYPRAdDAADLAAFAEETGKSTVEDWREALEEA-LNASAEDDILVTGSLY 388


                  ....*....
gi 498528234  422 FVSQVRELL 430
Cdd:TIGR01499 389 LVGEVRKLL 397
PLN02913 PLN02913
dihydrofolate synthetase
 20-431 1.64e-58

dihydrofolate synthetase


Pssm-ID: 178501 [Multi-domain]  Cd Length: 510  Bit Score: 200.05  E-value: 1.64e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234  20 SRPGLD--RINALLEKIDHPENKVPTIHIAGTNGKGSTVTYLRCLLEEMGLKVGTFTSPYIESFNERIAIN--GQPISDE 95
Cdd:PLN02913  52 SDDGFDlgRMRRLMDRLGNPHSKFKAVHVAGTKGKGSTAAFLSNILRAQGYSVGCYTSPHLRSIRERISVGklGKPVSTN 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234  96 QLITYVEKYQPIIKELDKItEVAGITEFETLTGMALDYFVNEQVDIAVVEVGLGGLLDSTNVVKP--LLTG-ITTIGKDH 172
Cdd:PLN02913 132 TLNDLFHGIKPILDEAIQL-ENGSLTHFEVLTALAFKLFAQENVDIAVIEAGLGGARDATNVIDSsgLAASvITTIGEEH 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 173 TEILGETIAEIAYQKAGIIKEKVPVVTGN-ICADALAVIEKVAQEKQSPIFRF----------------GKEYQVEYLHp 235
Cdd:PLN02913 211 LAALGGSLESIALAKSGIIKQGRPVVLGGpFLPHIESILRDKASSMNSPVVSAsdpgvrssikgiitdnGKPCQSCDIV- 289

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 236 dTQWGEVFNFYGEmgkLTKIKVPLLGRHQVENAA----VAIQLFDKYCQLqhlpfKERDITQGLAKAQWPARMERLSDEP 311
Cdd:PLN02913 290 -IRVEKDDPLFIE---LSDVNLRMLGSHQLQNAVtaacAALCLRDQGWRI-----SDASIRAGLENTNLLGRSQFLTSKE 360

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 312 L---------IVLDGAHNDHAVKRLVENLRKEFPQHTIhILFSALAT-KD----VDEMIQDLKqvpnahlyltsfdyPKA 377
Cdd:PLN02913 361 AevlglpgatVLLDGAHTKESAKALVDTIKTAFPEARL-ALVVAMASdKDhlafASEFLSGLK--------------PEA 425

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 378 IALTEME-------------------KYEDDL-------TEIVSLWQFGLGEILEKMSAD----DLLLVTGSLYFVSQVR 427
Cdd:PLN02913 426 VFLTEADiaggksrstsasalkeawiKAAPELgietllaENNSLLKSLVDASAILRKARTldpsSVVCVTGSLHIVSAVL 505


                 ....
gi 498528234 428 ELLL 431
Cdd:PLN02913 506 ASLQ 509
Mur_ligase_M pfam08245
Mur ligase middle domain;
46-272 3.01e-14

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 71.18  E-value: 3.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234   46 IAGTNGKGSTVTYLRCLLEEMGLKVGT---FTSPYIESFNERIAINgqpisdeqlityvekyqpiikeldkitevagite 122
Cdd:pfam08245   1 VTGTNGKTTTTELIAAILSLAGGVIGTigtYIGKSGNTTNNAIGLP---------------------------------- 46

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234  123 fETLTGMaldyfVNEQVDIAVVEVGLGGLLDS--TNVVKPLLTGITTIGKDHTEILGeTIAEIAYQKAGIIKEKVPVVTG 200
Cdd:pfam08245  47 -LTLAEM-----VEAGAEYAVLEVSSHGLGEGrlSGLLKPDIAVFTNISPDHLDFHG-TMENYAKAKAELFEGLPEDGIA 119

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498528234  201 NICAD--ALAVIEKVAQEKQSPIFRFGKE----YQVEYLHPDTQwGEVFNFYGEMGKLTKIKVPLLGRHQVENAAVAI 272
Cdd:pfam08245 120 VINADdpYGAFLIAKLKKAGVRVITYGIEgeadLRAANIELSSD-GTSFDLFTVPGGELEIEIPLLGRHNVYNALAAI 196
 
Name Accession Description Interval E-value
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
 4-432 0e+00

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: 562.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234   4 TIEEAIEWIHSRLPFGSRPGLDRINALLEKIDHPENKVPTIHIAGTNGKGSTVTYLRCLLEEMGLKVGTFTSPYIESFNE 83
Cdd:COG0285    3 TYQEALAYLESLHPFGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRFNE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234  84 RIAINGQPISDEQLITYVEKYQPIIKELDKITevagITEFETLTGMALDYFVNEQVDIAVVEVGLGGLLDSTNVVKPLLT 163
Cdd:COG0285   83 RIRINGEPISDEELVEALEEVEPAVEEVDAGP----PTFFEVTTAAAFLYFAEAPVDVAVLEVGLGGRLDATNVIDPLVS 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 164 GITTIGKDHTEILGETIAEIAYQKAGIIKEKVPVVTGNICADALAVIEKVAQEKQSPIFRFGKEYQVEYLHpdtqwGEVF 243
Cdd:COG0285  159 VITSIGLDHTDFLGDTLEEIAREKAGIIKPGVPVVTGDQQPEALEVIEERAAELGAPLYRAGRDFSVEERE-----GAVF 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 244 NFYGEMGKLTKIKVPLLGRHQVENAAVAIQLFDKYCQLqHLPFKERDITQGLAKAQWPARMERLSDEPLIVLDGAHNDHA 323
Cdd:COG0285  234 SYQGPGGEYEDLPLPLLGAHQAENAALALAALEALREL-GLPISEEAIREGLANARWPGRLEVLSRGPLVILDGAHNPAG 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 324 VKRLVENLRKEFPQHTIHILFSALATKDVDEMIQDLKQVPNaHLYLTSFDYPKAIALTEMEKY---EDDLTEIVSLWQFG 400
Cdd:COG0285  313 ARALAETLKELFPFRKLHLVFGMLADKDIEGMLAALAPLAD-EVIVTTPPSPRALDAEELAEAareLGLRVEVAPDVEEA 391

                        410       420       430
                 ....*....|....*....|....*....|..
gi 498528234 401 LGEILEKMSADDLLLVTGSLYFVSQVRELLLT 432
Cdd:COG0285  392 LEAALELADPDDLILVTGSLYLVGEVRALLGR 423
folC TIGR01499
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ...
 24-430 5.60e-178

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: 502.58  E-value: 5.60e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234   24 LDRINALLEKIDHPENKVPTIHIAGTNGKGSTVTYLRCLLEEMGLKVGTFTSPYIESFNERIAINGQPISDEQLITYVEK 103
Cdd:TIGR01499   1 LERMKKLLEALGNPQDLYPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPISDEELAQAFEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234  104 YQPIIKELDKitevaGITEFETLTGMALDYFVNEQVDIAVVEVGLGGLLDSTNVVKPLLTGITTIGKDHTEILGETIAEI 183
Cdd:TIGR01499  81 VRPILESLSQ-----QPTYFELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVIEPLVSVITSIGLDHTEILGDTLEEI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234  184 AYQKAGIIKEKVPVVTGNICADALAVIEKVAQEKQSPIFRFGKEYQVEYLHPDTqwgevFNFYGEMGKLTKIKVPLLGRH 263
Cdd:TIGR01499 156 AWEKAGIIKEGVPIVTGEQEPEALNVLKKKAQEKGAPLFVVGRDFNYSETDENY-----LSFSGANLFLEPLALSLLGDH 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234  264 QVENAAVAIQLFDKYCQlQHLPFKERDITQGLAKAQWPARMERLSDE-PLIVLDGAHNDHAVKRLVENLRKEFPQHTIHI 342
Cdd:TIGR01499 231 QQENAALALAALEVLGK-QNPKLSEEAIRQGLANTIWPGRLEILSEDnPNILLDGAHNPHSAEALAEWFKKRFNGRPITL 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234  343 LFSALATKDVDEMIQDLKQVPNAHLYLTSFDYPKA-IALTEMEKYEDDLTEIVSLWQFGLGEIlEKMSADDLLLVTGSLY 421
Cdd:TIGR01499 310 LFGALADKDAAAMLAPLKPVVDKEVFVTPFDYPRAdDAADLAAFAEETGKSTVEDWREALEEA-LNASAEDDILVTGSLY 388


                  ....*....
gi 498528234  422 FVSQVRELL 430
Cdd:TIGR01499 389 LVGEVRKLL 397
PLN02913 PLN02913
dihydrofolate synthetase
 20-431 1.64e-58

dihydrofolate synthetase


Pssm-ID: 178501 [Multi-domain]  Cd Length: 510  Bit Score: 200.05  E-value: 1.64e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234  20 SRPGLD--RINALLEKIDHPENKVPTIHIAGTNGKGSTVTYLRCLLEEMGLKVGTFTSPYIESFNERIAIN--GQPISDE 95
Cdd:PLN02913  52 SDDGFDlgRMRRLMDRLGNPHSKFKAVHVAGTKGKGSTAAFLSNILRAQGYSVGCYTSPHLRSIRERISVGklGKPVSTN 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234  96 QLITYVEKYQPIIKELDKItEVAGITEFETLTGMALDYFVNEQVDIAVVEVGLGGLLDSTNVVKP--LLTG-ITTIGKDH 172
Cdd:PLN02913 132 TLNDLFHGIKPILDEAIQL-ENGSLTHFEVLTALAFKLFAQENVDIAVIEAGLGGARDATNVIDSsgLAASvITTIGEEH 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 173 TEILGETIAEIAYQKAGIIKEKVPVVTGN-ICADALAVIEKVAQEKQSPIFRF----------------GKEYQVEYLHp 235
Cdd:PLN02913 211 LAALGGSLESIALAKSGIIKQGRPVVLGGpFLPHIESILRDKASSMNSPVVSAsdpgvrssikgiitdnGKPCQSCDIV- 289

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 236 dTQWGEVFNFYGEmgkLTKIKVPLLGRHQVENAA----VAIQLFDKYCQLqhlpfKERDITQGLAKAQWPARMERLSDEP 311
Cdd:PLN02913 290 -IRVEKDDPLFIE---LSDVNLRMLGSHQLQNAVtaacAALCLRDQGWRI-----SDASIRAGLENTNLLGRSQFLTSKE 360

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 312 L---------IVLDGAHNDHAVKRLVENLRKEFPQHTIhILFSALAT-KD----VDEMIQDLKqvpnahlyltsfdyPKA 377
Cdd:PLN02913 361 AevlglpgatVLLDGAHTKESAKALVDTIKTAFPEARL-ALVVAMASdKDhlafASEFLSGLK--------------PEA 425

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 378 IALTEME-------------------KYEDDL-------TEIVSLWQFGLGEILEKMSAD----DLLLVTGSLYFVSQVR 427
Cdd:PLN02913 426 VFLTEADiaggksrstsasalkeawiKAAPELgietllaENNSLLKSLVDASAILRKARTldpsSVVCVTGSLHIVSAVL 505


                 ....
gi 498528234 428 ELLL 431
Cdd:PLN02913 506 ASLQ 509
PLN02881 PLN02881
tetrahydrofolylpolyglutamate synthase
 44-319 4.03e-54

tetrahydrofolylpolyglutamate synthase


Pssm-ID: 215476  Cd Length: 530  Bit Score: 188.72  E-value: 4.03e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234  44 IHIAGTNGKGSTVTYLRCLLEEMGLKVGTFTSPYIESFNERIAINGQPISDEQLITYVEKYQPIIKEldKITEVAGI-TE 122
Cdd:PLN02881  64 IHVAGTKGKGSTCTFTESILRNCGFRTGLFTSPHLIDVRERFRLDGVDISEEKFLRYFWWCWDRLKE--KTTEDLPMpAY 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 123 FETLTGMALDYFVNEQVDIAVVEVGLGGLLDSTNVV-KPLLTGITTIGKDHTEILGETIAEIAYQKAGIIKEKVPVVTGN 201
Cdd:PLN02881 142 FRFLTLLAFKIFSAEQVDVAILEVGLGGRLDATNVVqKPVVCGITSLGYDHMEILGDTLGKIAGEKAGIFKPGVPAFTVP 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 202 ICADALAVIEKVAQEKQSPifrfgkeyqVEYLHPDTQWGevfnfygemgkLTKIKVPLLGRHQVENAAVAIQL------- 274
Cdd:PLN02881 222 QPDEAMRVLEERASELGVP---------LQVVEPLDSYG-----------LSGLKLGLAGEHQYLNAGLAVALcstwlqr 281

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 498528234 275 ---FDKYCQLQHLPFKERDITqGLAKAQWPAR---------MERLSDEPLIVLDGAH 319
Cdd:PLN02881 282 tghEEFEALLQAGTLPEQFIK-GLSTASLQGRaqvvpdsyiNSEDSGDLVFYLDGAH 337
PRK10846 PRK10846
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional
 23-430 2.48e-53

bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional


Pssm-ID: 182774 [Multi-domain]  Cd Length: 416  Bit Score: 183.74  E-value: 2.48e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234  23 GLDRINALLEKID--HPENKVPTIhiAGTNGKGSTVTYLRCLLEEMGLKVGTFTSPYIESFNERIAINGQPISdEQLITY 100
Cdd:PRK10846  31 GLERVSQVAARLDllKPAPFVFTV--AGTNGKGTTCRTLESILMAAGYRVGVYSSPHLVRYTERVRIQGQELP-ESAHTA 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 101 VekyqpiIKELDKITEVAGITEFETLTGMALDYFVNEQVDIAVVEVGLGGLLDSTNVVKPLLTGITTIGKDHTEILGETI 180
Cdd:PRK10846 108 S------FAEIEAARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVTSIALDHTDWLGPDR 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 181 AEIAYQKAGIIKEKVPVVTGNicADALAVIEKVAQEKQSPIFRFGKEYQVEylhpdtQWGEVFNFYGEMGKLTKIKVPLL 260
Cdd:PRK10846 182 ESIGREKAGIFRAEKPAVVGE--PDMPSTIADVAQEKGALLQRRGVDWNYS------VTDHDWAFSDGDGTLENLPLPNV 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 261 grhQVENAAVAIQLFdkycQLQHLPFKERDITQGLAKAQWPARMERLSDEPLIVLDGAHNDHAVKRLVENLrKEFPQHT- 339
Cdd:PRK10846 254 ---PLPNAATALAAL----RASGLEVSEQAIRDGIASAILPGRFQIVSESPRVILDVAHNPHAAEYLTGRL-KALPKNGr 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 340 IHILFSALATKDVDEMIQDLKQVPNAhLYLTSFDYPK-------AIALTEMEKYEDdlteIVSLWQfglgEILEKMSADD 412
Cdd:PRK10846 326 VLAVIGMLHDKDIAGTLACLKSVVDD-WYCAPLEGPRgataeqlAEHLGNGKSFDS----VAQAWD----AAMADAKPED 396

                        410
                 ....*....|....*...
gi 498528234 413 LLLVTGSLYFVSQVRELL 430
Cdd:PRK10846 397 TVLVCGSFHTVAHVMEVI 414
murE TIGR01085
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ...
 35-346 1.13e-14

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: 75.82  E-value: 1.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234   35 DHPENKVPTIHIAGTNGKGSTVTYLRCLLEEMGLKVGTFTSPYIESFNERIaingqpisdeqlityvekyqpiikeldkI 114
Cdd:TIGR01085  79 GHPSKKLKVIGVTGTNGKTTTTSLIAQLLRLLGKKTGLIGTIGYRLGGNDL----------------------------I 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234  115 TEVAGITEFETLTGMA-LDYFVNEQVDIAVVEVGLGGL----LDSTNVVKPLLTGITtigKDHTEILGeTIAEIAYQKAG 189
Cdd:TIGR01085 131 KNPAALTTPEALTLQStLAEMVEAGAQYAVMEVSSHALaqgrVRGVRFDAAVFTNLS---RDHLDFHG-TMENYFAAKAS 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234  190 IIKEKVPVVTGNICADALAVIEKVAQEKQsPIFRFGKEYQVEYLHPDTQWGEV-FNFYG------EMGKLTKIKVPLLGR 262
Cdd:TIGR01085 207 LFTELGLKRFAVINLDDEYGAQFVKRLPK-DITVSAITQPADGRAQDIKITDSgYSFEGqqftfeTPAGEGHLHTPLIGR 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234  263 HQVENAAVAIQLfdkYCQLQHLPFKerDITQGLAKAQW-PARMER--LSDEPLIVLDGAHNDHAVKRLVENLRKEFPQHT 339
Cdd:TIGR01085 286 FNVYNLLAALAT---LLHLGGIDLE--DIVAALEKFRGvPGRMELvdGGQKFLVIVDYAHTPDALEKALRTLRKHKDGRL 360


                  ....*..
gi 498528234  340 IhILFSA 346
Cdd:TIGR01085 361 I-VVFGC 366
Mur_ligase_M pfam08245
Mur ligase middle domain;
46-272 3.01e-14

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 71.18  E-value: 3.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234   46 IAGTNGKGSTVTYLRCLLEEMGLKVGT---FTSPYIESFNERIAINgqpisdeqlityvekyqpiikeldkitevagite 122
Cdd:pfam08245   1 VTGTNGKTTTTELIAAILSLAGGVIGTigtYIGKSGNTTNNAIGLP---------------------------------- 46

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234  123 fETLTGMaldyfVNEQVDIAVVEVGLGGLLDS--TNVVKPLLTGITTIGKDHTEILGeTIAEIAYQKAGIIKEKVPVVTG 200
Cdd:pfam08245  47 -LTLAEM-----VEAGAEYAVLEVSSHGLGEGrlSGLLKPDIAVFTNISPDHLDFHG-TMENYAKAKAELFEGLPEDGIA 119

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498528234  201 NICAD--ALAVIEKVAQEKQSPIFRFGKE----YQVEYLHPDTQwGEVFNFYGEMGKLTKIKVPLLGRHQVENAAVAI 272
Cdd:pfam08245 120 VINADdpYGAFLIAKLKKAGVRVITYGIEgeadLRAANIELSSD-GTSFDLFTVPGGELEIEIPLLGRHNVYNALAAI 196
MurE COG0769
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
 35-346 4.31e-11

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: 64.33  E-value: 4.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234  35 DHPENKVPTIHIAGTNGKGSTVTYLRCLLEEMGLKVGTFTSpyiesfneriaiNGQPISDEQLityvekyqpiikeldki 114
Cdd:COG0769   74 GHPSQKLKLIGVTGTNGKTTTTYLLAQILRALGKKTGLIGT------------VGNGIGGELI----------------- 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 115 teVAGITefetlTGMALD------YFVNEQVDIAVVEV---GL-----GGL-LDstnvvkpllTGI-TTIGKDHteiLGE 178
Cdd:COG0769  125 --PSSLT-----TPEALDlqrllaEMVDAGVTHVVMEVsshALdqgrvDGVrFD---------VAVfTNLTRDH---LDY 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 179 --TIAEIAYQKAGIIKEKVPVVTGNICADAlAVIEKVAQEKQSPIFRFGKE----YQVEYLHPDTQwGEVFNFYGEMGKL 252
Cdd:COG0769  186 hgTMEAYFAAKARLFDQLGPGGAAVINADD-PYGRRLAAAAPARVITYGLKadadLRATDIELSAD-GTRFTLVTPGGEV 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 253 tKIKVPLLGRHQVENAAVAIQLfdkycqLQHLPFKERDITQGLAKAQWPA-RMERLS--DEPLIVLDGAHNDHAVKRLVE 329
Cdd:COG0769  264 -EVRLPLIGRFNVYNALAAIAA------ALALGIDLEEILAALEKLKGVPgRMERVDggQGPTVIVDYAHTPDALENVLE 336

                        330
                 ....*....|....*..
gi 498528234 330 NLRkEFPQHTIHILFSA 346
Cdd:COG0769  337 ALR-PHTKGRLIVVFGC 352
MurF COG0770
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
 136-320 3.17e-08

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: 55.49  E-value: 3.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 136 NEQVDIAVVEVG---LGGLLDSTNVVKPLLTGITTIGKDHTEILGeTIAEIAYQKAGIIKekvpvvtgNICADALAVI-- 210
Cdd:COG0770  149 PEDHEFAVLEMGmnhPGEIAYLARIARPDIAVITNIGPAHLEGFG-SLEGIARAKGEIFE--------GLPPGGVAVLna 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 211 -----EKVAQEKQSPIFRFGKE----YQVEYLHPDTQwGEVFNFYGEMGKLTkIKVPLLGRHQVENA----AVAIQLfdk 277
Cdd:COG0770  220 ddpllAALAERAKARVLTFGLSedadVRAEDIELDED-GTRFTLHTPGGELE-VTLPLPGRHNVSNAlaaaAVALAL--- 294

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 498528234 278 ycqlqHLPFKErdITQGLAKAQWPA-RMERLS-DEPLIVLDGAHN 320
Cdd:COG0770  295 -----GLDLEE--IAAGLAAFQPVKgRLEVIEgAGGVTLIDDSYN 332
murE PRK00139
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
 35-344 2.19e-07

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


Pssm-ID: 234660 [Multi-domain]  Cd Length: 460  Bit Score: 52.83  E-value: 2.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234  35 DHPENKVPTIHIAGTNGKGSTVTYLRCLLEEMGLKVGTFTSPYIEsfneriaINGQPISDEqLITyvekyqPIIKELdki 114
Cdd:PRK00139  89 GHPSDKLKLIGVTGTNGKTTTAYLLAQILRLLGEKTALIGTLGNG-------IGGELIPSG-LTT------PDALDL--- 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 115 tevagiteFETLTGMaldyfVNEQVDIAVVEV---GL-----GGLldstnvvkPLLTGI-TTIGKDHteiLGE--TIAEI 183
Cdd:PRK00139 152 --------QRLLAEL-----VDAGVTYAAMEVsshALdqgrvDGL--------KFDVAVfTNLSRDH---LDYhgTMEDY 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 184 AYQKAGIIKEkvPVVTGNICADAlAVIEKVAQEKQSPIFRF-GKEYQVEYLHPDTQwGEVFNFYGEmgkltkIKVPLLGR 262
Cdd:PRK00139 208 LAAKARLFSE--LGLAAVINADD-EVGRRLLALPDAYAVSMaGADLRATDVEYTDS-GQTFTLVTE------VESPLIGR 277

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 263 HQVENAAVAIQLfdkyCQLQHLPFKerDITQGLAKAQW-PARMERLS--DEPLIVLDGAHNDHAVKRLVENLRkEFPQHT 339
Cdd:PRK00139 278 FNVSNLLAALAA----LLALGVPLE--DALAALAKLQGvPGRMERVDagQGPLVIVDYAHTPDALEKVLEALR-PHAKGR 350


                 ....*
gi 498528234 340 IHILF 344
Cdd:PRK00139 351 LICVF 355
PRK11929 PRK11929
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ...
 35-332 6.76e-07

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: 51.63  E-value: 6.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234  35 DHPENKVPTIHIAGTNGKGSTVTYLRCLLEEMGLKVGTftspyiesfnerIAINGQPISDEqlityvekyqpiIKELDKI 114
Cdd:PRK11929 106 GRPSEQLSLVAVTGTNGKTSCAQLLAQLLTRLGKPCGS------------IGTLGARLDGR------------LIPGSLT 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 115 TEVAgITEFETLTGMAldyfvnEQ-VDIAVVEVGLGGL----LDSTNVVkplLTGITTIGKDHTEILGeTIAEIAYQKAG 189
Cdd:PRK11929 162 TPDA-IILHRILARMR------AAgADAVAMEASSHGLeqgrLDGLRIA---VAGFTNLTRDHLDYHG-TMQDYEEAKAA 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 190 IIKEKVPVVTGNICAD-----ALAVIEKVAQEKQSPIFRFGKEYQVEYLHpDTQWGEVFNFYGEMGKLtKIKVPLLGRHQ 264
Cdd:PRK11929 231 LFSKLPGLGAAVINADdpaaaRLLAALPRGLKVGYSPQNAGADVQARDLR-ATAHGQVFTLATPDGSY-QLVTRLLGRFN 308

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498528234 265 VENAAVAIQLFDKycqlqhLPFKERDITQGLAKAQ-WPARMERLSDE-----PLIVLDGAHNDHAVKRLVENLR 332
Cdd:PRK11929 309 VSNLLLVAAALKK------LGLPLAQIARALAAVSpVPGRMERVGPTagaqgPLVVVDYAHTPDALAKALTALR 376
MurC COG0773
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall ...
 165-344 1.18e-04

UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440536 [Multi-domain]  Cd Length: 451  Bit Score: 44.29  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 165 ITTIGKDHTEILGeTIAEI--AYQK-AGIIKEKVPVVtgnICADaLAVIEKVAQEKQSPIFRFGKE----YQVEYLHPDT 237
Cdd:COG0773  177 VTNIEADHLDIYG-DLEAIkeAFHEfARNVPFYGLLV---LCAD-DPGLRELLPRCGRPVITYGFSedadYRAENIRIDG 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498528234 238 QwGEVFNFYGEMGKLTKIKVPLLGRHQVENAAVAIQLfdkycqLQHLPFKERDITQGLAKAQWPA-RMERLSDEPLIVL- 315
Cdd:COG0773  252 G-GSTFDVLRRGEELGEVELNLPGRHNVLNALAAIAV------ALELGVDPEAIAEALASFKGVKrRFELKGEVGGVTVi 324

                        170       180       190
                 ....*....|....*....|....*....|..
gi 498528234 316 -DGAHndH--AVKRLVENLRKEFPQHTIHILF 344
Cdd:COG0773  325 dDYAH--HptEIAATLAAAREKYPDRRLVAVF 354
 
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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