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Conserved domains on  [gi|518172472|ref|WP_019342680|]
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phosphoribosylamine--glycine ligase [Stutzerimonas stutzeri]

Protein Classification

phosphoribosylamine--glycine ligase( domain architecture ID 11414962)

phosphoribosylamine--glycine ligase catalyzes the second step of the de novo purine biosynthetic pathway; the conversion of phosphoribosylamine, glycine, and ATP to glycinamide ribonucleotide (GAR), ADP, and Pi

CATH:  3.30.1490.20
Gene Ontology:  GO:0005524|GO:0004637|GO:0009113|GO:0006164
PubMed:  2687276

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PurD COG0151
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ...
 1-424 0e+00

Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis


:

Pssm-ID: 439921 [Multi-domain]  Cd Length: 422  Bit Score: 771.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472   1 MNVLIIGSGGREHALAWKVAQDPRVKKVFVAPGNAGTATEAKCenVAIDVLAIEQLADFA-EHNVQLTIVGPEAPLVKGV 79
Cdd:COG0151    1 MKVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAEC--VDIDVTDIEALVAFAkEENIDLVVVGPEAPLVAGI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472  80 VDLFRSRGLDCFGPTAAAAQLEGSKAFTKDFLARHKIPTADYQNFTEVEPALAYLQEKGAPIVIKADGLAAGKGVIVAMT 159
Cdd:COG0151   79 VDAFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAET 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472 160 LTEAEEAVRDMLSGNAFGDAGARVVIEEFLDGEEASFIVMVDGANVLPMATSQDHKRVGDGDTGPNTGGMGAYSPAPVVT 239
Cdd:COG0151  159 LEEALAAVDDMLADGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVT 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472 240 ADVHQRVMDEVIWPTVKGMAAEGNVYTGFLYAGLMIDHHGaPKVIEFNCRFGDPETQPIMLRLQSSLVLLVEAALAKALD 319
Cdd:COG0151  239 EELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADG-PKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRLD 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472 320 KIEAQWDPRPSLGVVMAAGGYPGEYSKGAAIHGLKAAAQLQGKVFHAGTLLADGAVTTSGGRVLCATALGETVSAAQQNA 399
Cdd:COG0151  318 EVELEWDDRAAVCVVLASGGYPGSYEKGDVITGLEEAEAEGVKVFHAGTALEDGKLVTNGGRVLGVTALGDTLEEARERA 397

                        410       420
                 ....*....|....*....|....*
gi 518172472 400 YALAARIDWDGHFYRHDIGYRAIAR 424
Cdd:COG0151  398 YEAVEKIRFEGMFYRRDIGWRALKR 422
 
Name Accession Description Interval E-value
PurD COG0151
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ...
 1-424 0e+00

Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439921 [Multi-domain]  Cd Length: 422  Bit Score: 771.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472   1 MNVLIIGSGGREHALAWKVAQDPRVKKVFVAPGNAGTATEAKCenVAIDVLAIEQLADFA-EHNVQLTIVGPEAPLVKGV 79
Cdd:COG0151    1 MKVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAEC--VDIDVTDIEALVAFAkEENIDLVVVGPEAPLVAGI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472  80 VDLFRSRGLDCFGPTAAAAQLEGSKAFTKDFLARHKIPTADYQNFTEVEPALAYLQEKGAPIVIKADGLAAGKGVIVAMT 159
Cdd:COG0151   79 VDAFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAET 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472 160 LTEAEEAVRDMLSGNAFGDAGARVVIEEFLDGEEASFIVMVDGANVLPMATSQDHKRVGDGDTGPNTGGMGAYSPAPVVT 239
Cdd:COG0151  159 LEEALAAVDDMLADGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVT 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472 240 ADVHQRVMDEVIWPTVKGMAAEGNVYTGFLYAGLMIDHHGaPKVIEFNCRFGDPETQPIMLRLQSSLVLLVEAALAKALD 319
Cdd:COG0151  239 EELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADG-PKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRLD 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472 320 KIEAQWDPRPSLGVVMAAGGYPGEYSKGAAIHGLKAAAQLQGKVFHAGTLLADGAVTTSGGRVLCATALGETVSAAQQNA 399
Cdd:COG0151  318 EVELEWDDRAAVCVVLASGGYPGSYEKGDVITGLEEAEAEGVKVFHAGTALEDGKLVTNGGRVLGVTALGDTLEEARERA 397

                        410       420
                 ....*....|....*....|....*
gi 518172472 400 YALAARIDWDGHFYRHDIGYRAIAR 424
Cdd:COG0151  398 YEAVEKIRFEGMFYRRDIGWRALKR 422
purD TIGR00877
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ...
 1-422 0e+00

phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase (GARS). This enzyme appears as a monofunctional protein in prokaryotes but as part of a larger, multidomain protein in eukaryotes. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273315 [Multi-domain]  Cd Length: 422  Bit Score: 627.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472    1 MNVLIIGSGGREHALAWKVAQDPRVKKVFVAPGNAGTATEAKCENVAIDVLAIEQLADFA-EHNVQLTIVGPEAPLVKGV 79
Cdd:TIGR00877   1 MKVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKNVAIEITDIEALVEFAkKKKIDLAIIGPEAPLVLGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472   80 VDLFRSRGLDCFGPTAAAAQLEGSKAFTKDFLARHKIPTADYQNFTEVEPALAYLQEKGAPIVIKADGLAAGKGVIVAMT 159
Cdd:TIGR00877  81 VDALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPIVVKADGLAAGKGVIVAKT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472  160 LTEAEEAVRDMLSGNaFGDAGARVVIEEFLDGEEASFIVMVDGANVLPMATSQDHKRVGDGDTGPNTGGMGAYSPAPVVT 239
Cdd:TIGR00877 161 NEEAIKAVEDILEQK-FGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472  240 ADVHQRVMDEVIWPTVKGMAAEGNVYTGFLYAGLMIDHHGaPKVIEFNCRFGDPETQPIMLRLQSSLVLLVEAALAKALD 319
Cdd:TIGR00877 240 EEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEG-PKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKLD 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472  320 KIEAQWDPRPSLGVVMAAGGYPGEYSKGAAIHGLKAAAQLQGKVFHAGTLLADGAVTTSGGRVLCATALGETVSAAQQNA 399
Cdd:TIGR00877 319 EVELRFDNRAAVTVVLASEGYPEDYRKGDPITGEPLAEAEGVKVFHAGTKADNGKLVTNGGRVLAVTALGKTLEEARERA 398

                         410       420
                  ....*....|....*....|...
gi 518172472  400 YALAARIDWDGHFYRHDIGYRAI 422
Cdd:TIGR00877 399 YEAVEYIKFEGMFYRKDIGFRAL 421
PLN02257 PLN02257
phosphoribosylamine--glycine ligase
 4-426 0e+00

phosphoribosylamine--glycine ligase


Pssm-ID: 177899 [Multi-domain]  Cd Length: 434  Bit Score: 551.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472   4 LIIGSGGREHALAWKVAQDPRVKKVFVAPGNAGTATEAKCENVA-IDVLAIEQLADFA-EHNVQLTIVGPEAPLVKGVVD 81
Cdd:PLN02257   1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGDATCVPdLDISDSAAVISFCrKWGVGLVVVGPEAPLVAGLAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472  82 LFRSRGLDCFGPTAAAAQLEGSKAFTKDFLARHKIPTADYQNFTEVEPALAYLQEKGAPIVIKADGLAAGKGVIVAMTLT 161
Cdd:PLN02257  81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAPIVVKADGLAAGKGVVVAMTLE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472 162 EAEEAVRDMLSGNAFGDAGARVVIEEFLDGEEASFIVMVDGANVLPMATSQDHKRVGDGDTGPNTGGMGAYSPAPVVTAD 241
Cdd:PLN02257 161 EAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTPE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472 242 VHQRVMDEVIWPTVKGMAAEGNVYTGFLYAGLMIDHH-GAPKVIEFNCRFGDPETQPIMLRLQSSLVLLVEAALAKALDK 320
Cdd:PLN02257 241 LESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKsGLPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELSG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472 321 IEAQWDPRPSLGVVMAAGGYPGEYSKGAAIHGLKAAAQLQG--KVFHAGTLL-ADGAVTTSGGRVLCATALGETVSAAQQ 397
Cdd:PLN02257 321 VSLTWSPDSAMVVVMASNGYPGSYKKGTVIKNLDEAEAVAPgvKVFHAGTALdSDGNVVAAGGRVLGVTAKGKDIAEARA 400

                        410       420
                 ....*....|....*....|....*....
gi 518172472 398 NAYALAARIDWDGHFYRHDIGYRAIAREQ 426
Cdd:PLN02257 401 RAYDAVDQIDWPGGFFRRDIGWRAVARLQ 429
GARS_A pfam01071
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ...
 102-295 4.20e-108

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: 316.92  E-value: 4.20e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472  102 GSKAFTKDFLARHKIPTADYQNFTEVEPALAYLQEKGAPI-VIKADGLAAGKGVIVAMTLTEAEEAVRDMLSGNAFGDAG 180
Cdd:pfam01071   1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAiVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472  181 ARVVIEEFLDGEEASFIVMVDGANVLPMATSQDHKRVGDGDTGPNTGGMGAYSPAPVVTADVHQRVMDEVIWPTVKGMAA 260
Cdd:pfam01071  81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 518172472  261 EGNVYTGFLYAGLMIDHHGaPKVIEFNCRFGDPET 295
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDG-PKVLEFNCRFGDPET 194
 
Name Accession Description Interval E-value
PurD COG0151
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ...
 1-424 0e+00

Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439921 [Multi-domain]  Cd Length: 422  Bit Score: 771.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472   1 MNVLIIGSGGREHALAWKVAQDPRVKKVFVAPGNAGTATEAKCenVAIDVLAIEQLADFA-EHNVQLTIVGPEAPLVKGV 79
Cdd:COG0151    1 MKVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAEC--VDIDVTDIEALVAFAkEENIDLVVVGPEAPLVAGI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472  80 VDLFRSRGLDCFGPTAAAAQLEGSKAFTKDFLARHKIPTADYQNFTEVEPALAYLQEKGAPIVIKADGLAAGKGVIVAMT 159
Cdd:COG0151   79 VDAFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAET 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472 160 LTEAEEAVRDMLSGNAFGDAGARVVIEEFLDGEEASFIVMVDGANVLPMATSQDHKRVGDGDTGPNTGGMGAYSPAPVVT 239
Cdd:COG0151  159 LEEALAAVDDMLADGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVT 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472 240 ADVHQRVMDEVIWPTVKGMAAEGNVYTGFLYAGLMIDHHGaPKVIEFNCRFGDPETQPIMLRLQSSLVLLVEAALAKALD 319
Cdd:COG0151  239 EELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADG-PKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRLD 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472 320 KIEAQWDPRPSLGVVMAAGGYPGEYSKGAAIHGLKAAAQLQGKVFHAGTLLADGAVTTSGGRVLCATALGETVSAAQQNA 399
Cdd:COG0151  318 EVELEWDDRAAVCVVLASGGYPGSYEKGDVITGLEEAEAEGVKVFHAGTALEDGKLVTNGGRVLGVTALGDTLEEARERA 397

                        410       420
                 ....*....|....*....|....*
gi 518172472 400 YALAARIDWDGHFYRHDIGYRAIAR 424
Cdd:COG0151  398 YEAVEKIRFEGMFYRRDIGWRALKR 422
purD TIGR00877
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ...
 1-422 0e+00

phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase (GARS). This enzyme appears as a monofunctional protein in prokaryotes but as part of a larger, multidomain protein in eukaryotes. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273315 [Multi-domain]  Cd Length: 422  Bit Score: 627.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472    1 MNVLIIGSGGREHALAWKVAQDPRVKKVFVAPGNAGTATEAKCENVAIDVLAIEQLADFA-EHNVQLTIVGPEAPLVKGV 79
Cdd:TIGR00877   1 MKVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKNVAIEITDIEALVEFAkKKKIDLAIIGPEAPLVLGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472   80 VDLFRSRGLDCFGPTAAAAQLEGSKAFTKDFLARHKIPTADYQNFTEVEPALAYLQEKGAPIVIKADGLAAGKGVIVAMT 159
Cdd:TIGR00877  81 VDALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPIVVKADGLAAGKGVIVAKT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472  160 LTEAEEAVRDMLSGNaFGDAGARVVIEEFLDGEEASFIVMVDGANVLPMATSQDHKRVGDGDTGPNTGGMGAYSPAPVVT 239
Cdd:TIGR00877 161 NEEAIKAVEDILEQK-FGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472  240 ADVHQRVMDEVIWPTVKGMAAEGNVYTGFLYAGLMIDHHGaPKVIEFNCRFGDPETQPIMLRLQSSLVLLVEAALAKALD 319
Cdd:TIGR00877 240 EEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEG-PKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKLD 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472  320 KIEAQWDPRPSLGVVMAAGGYPGEYSKGAAIHGLKAAAQLQGKVFHAGTLLADGAVTTSGGRVLCATALGETVSAAQQNA 399
Cdd:TIGR00877 319 EVELRFDNRAAVTVVLASEGYPEDYRKGDPITGEPLAEAEGVKVFHAGTKADNGKLVTNGGRVLAVTALGKTLEEARERA 398

                         410       420
                  ....*....|....*....|...
gi 518172472  400 YALAARIDWDGHFYRHDIGYRAI 422
Cdd:TIGR00877 399 YEAVEYIKFEGMFYRKDIGFRAL 421
PLN02257 PLN02257
phosphoribosylamine--glycine ligase
 4-426 0e+00

phosphoribosylamine--glycine ligase


Pssm-ID: 177899 [Multi-domain]  Cd Length: 434  Bit Score: 551.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472   4 LIIGSGGREHALAWKVAQDPRVKKVFVAPGNAGTATEAKCENVA-IDVLAIEQLADFA-EHNVQLTIVGPEAPLVKGVVD 81
Cdd:PLN02257   1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGDATCVPdLDISDSAAVISFCrKWGVGLVVVGPEAPLVAGLAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472  82 LFRSRGLDCFGPTAAAAQLEGSKAFTKDFLARHKIPTADYQNFTEVEPALAYLQEKGAPIVIKADGLAAGKGVIVAMTLT 161
Cdd:PLN02257  81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAPIVVKADGLAAGKGVVVAMTLE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472 162 EAEEAVRDMLSGNAFGDAGARVVIEEFLDGEEASFIVMVDGANVLPMATSQDHKRVGDGDTGPNTGGMGAYSPAPVVTAD 241
Cdd:PLN02257 161 EAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTPE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472 242 VHQRVMDEVIWPTVKGMAAEGNVYTGFLYAGLMIDHH-GAPKVIEFNCRFGDPETQPIMLRLQSSLVLLVEAALAKALDK 320
Cdd:PLN02257 241 LESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKsGLPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELSG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472 321 IEAQWDPRPSLGVVMAAGGYPGEYSKGAAIHGLKAAAQLQG--KVFHAGTLL-ADGAVTTSGGRVLCATALGETVSAAQQ 397
Cdd:PLN02257 321 VSLTWSPDSAMVVVMASNGYPGSYKKGTVIKNLDEAEAVAPgvKVFHAGTALdSDGNVVAAGGRVLGVTAKGKDIAEARA 400

                        410       420
                 ....*....|....*....|....*....
gi 518172472 398 NAYALAARIDWDGHFYRHDIGYRAIAREQ 426
Cdd:PLN02257 401 RAYDAVDQIDWPGGFFRRDIGWRAVARLQ 429
GARS_A pfam01071
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ...
 102-295 4.20e-108

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: 316.92  E-value: 4.20e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472  102 GSKAFTKDFLARHKIPTADYQNFTEVEPALAYLQEKGAPI-VIKADGLAAGKGVIVAMTLTEAEEAVRDMLSGNAFGDAG 180
Cdd:pfam01071   1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAiVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472  181 ARVVIEEFLDGEEASFIVMVDGANVLPMATSQDHKRVGDGDTGPNTGGMGAYSPAPVVTADVHQRVMDEVIWPTVKGMAA 260
Cdd:pfam01071  81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 518172472  261 EGNVYTGFLYAGLMIDHHGaPKVIEFNCRFGDPET 295
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDG-PKVLEFNCRFGDPET 194
GARS_N pfam02844
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes ...
 1-101 3.99e-52

Phosphoribosylglycinamide synthetase, N 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 N-terminal domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam00289). This domain is structurally related to the PreATP-grasp domain.


Pssm-ID: 460723 [Multi-domain]  Cd Length: 102  Bit Score: 169.84  E-value: 3.99e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472    1 MNVLIIGSGGREHALAWKVAQDPRVKKVFVAPGNAGTATEAKCenVAIDVLAIEQLADFA-EHNVQLTIVGPEAPLVKGV 79
Cdd:pfam02844   1 MKVLVIGSGGREHALAWKLAQSPLVEKLYVAPGNGGTAQLAEC--VDIDATDFEALVAFAkENNIDLVVVGPEAPLVAGI 78

                          90       100
                  ....*....|....*....|....
gi 518172472   80 VDLFRSR--GLDCFGPTAAAAQLE 101
Cdd:pfam02844  79 VDALRERaaGIPVFGPSKAAAQLE 102
GARS_C pfam02843
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes ...
 330-420 3.59e-39

Phosphoribosylglycinamide synthetase, C 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 C-terminal domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02787).


Pssm-ID: 460722 [Multi-domain]  Cd Length: 88  Bit Score: 135.65  E-value: 3.59e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472  330 SLGVVMAAGGYPGEYSKGAAIHGLKAAAqlqGKVFHAGTLLADGAVTTSGGRVLCATALGETVSAAQQNAYALAARIDWD 409
Cdd:pfam02843   1 AVCVVLASGGYPGSYEKGDVITGLDEAG---VKVFHAGTKLKDGKLVTSGGRVLAVTALGDTLEEAREKAYEAVEKIDFE 77

                          90
                  ....*....|.
gi 518172472  410 GHFYRHDIGYR 420
Cdd:pfam02843  78 GMFYRKDIGTR 88
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 92-291 6.92e-21

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: 91.47  E-value: 6.92e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472  92 GPTAAAAQLEGSKAFTKDFLARHKIPTADYQNFTEVEPALAYLQEKGAPIVIKADGLAAGKGVIVAMTLTEAEEAVRDML 171
Cdd:COG0439   43 GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEAR 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472 172 SGNAFGDAGARVVIEEFLDGEEASFIVMVDGANVLPMATSQDHKrvgdgdTGPNTGGMGAYSPAPvVTADVHQRVMDEVi 251
Cdd:COG0439  123 AEAKAGSPNGEVLVEEFLEGREYSVEGLVRDGEVVVCSITRKHQ------KPPYFVELGHEAPSP-LPEELRAEIGELV- 194

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 518172472 252 wptVKGMAAEGnVYTGFLYAGLMIDHHGAPKVIEFNCRFG 291
Cdd:COG0439  195 ---ARALRALG-YRRGAFHTEFLLTPDGEPYLIEINARLG 230
PurK COG0026
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ...
 108-198 1.38e-07

Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439797 [Multi-domain]  Cd Length: 353  Bit Score: 53.15  E-value: 1.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472 108 KDFLARHKIPTADYQNFTEVEPALAYLQEKGAPIVIKA-----DglaaGKGVIVAMTLTEAEEAVRDMlsgnafgdAGAR 182
Cdd:COG0026   94 KAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTrrggyD----GKGQVVIKSAADLEAAWAAL--------GGGP 161

                         90
                 ....*....|....*..
gi 518172472 183 VVIEEFLDGE-EASFIV 198
Cdd:COG0026  162 CILEEFVPFErELSVIV 178
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 104-193 2.09e-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: 52.42  E-value: 2.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472 104 KAFTKDFLARHKIPTADYQNFT--EVEPALAYLQEKGAPIVIKADGLAAGKGVIVAMTLTEAEEAVRDMLsgnAFGDaga 181
Cdd:COG1181   96 KALTKRVLAAAGLPTPPYVVLRrgELADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAF---KYDD--- 169

                         90
                 ....*....|..
gi 518172472 182 RVVIEEFLDGEE 193
Cdd:COG1181  170 KVLVEEFIDGRE 181
PRK02471 PRK02471
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB;
104-220 6.50e-06

bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB;


Pssm-ID: 179427 [Multi-domain]  Cd Length: 752  Bit Score: 48.38  E-value: 6.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472 104 KAFTKDFLARHKIPTADYQNFTEVEPALAYLQE-KGAPIVIKADGLAAGKGVIV---AMTLTEAEEAVRdmlsgNAFGDA 179
Cdd:PRK02471 489 KVVTKKILAEAGFPVPAGDEFTSLEEALADYSLfADKAIVVKPKSTNFGLGISIfkePASLEDYEKALE-----IAFRED 563

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 518172472 180 GArVVIEEFLDGEEASFIVMvDG----------ANVlpmatsqdhkrVGDG 220
Cdd:PRK02471 564 SS-VLVEEFIVGTEYRFFVL-DGkveavllrvpANV-----------VGDG 601
PRK06019 PRK06019
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
 108-198 1.19e-05

phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed


Pssm-ID: 235674 [Multi-domain]  Cd Length: 372  Bit Score: 47.07  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472 108 KDFLARHKIPTADYQNFTEVEPALAYLQEKGAPIVIKA-----DglaaGKGVIVAMTLTEAEEAVRDMLSGNAfgdagar 182
Cdd:PRK06019 105 KQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLKTrrggyD----GKGQWVIRSAEDLEAAWALLGSVPC------- 173

                         90
                 ....*....|....*..
gi 518172472 183 vVIEEFLDGE-EASFIV 198
Cdd:PRK06019 174 -ILEEFVPFErEVSVIV 189
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 78-287 2.32e-05

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: 45.70  E-value: 2.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472  78 GVVDLFRSRGLDCFGPtAAAAQLEGSKAFTKDFLARHKIPTADyqnfTEV----EPALAYLQEKGAPIVIK-ADGlAAGK 152
Cdd:COG0189   72 ALLRQLEAAGVPVVND-PEAIRRARDKLFTLQLLARAGIPVPP----TLVtrdpDDLRAFLEELGGPVVLKpLDG-SGGR 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472 153 GVIVAMTLTEAEEAVRDMlsgnaFGDAGARVVIEEFLDGEEASF--IVMVDGANVLPMA--TSQDHKRVgdgdtgpNTGG 228
Cdd:COG0189  146 GVFLVEDEDALESILEAL-----TELGSEPVLVQEFIPEEDGRDirVLVVGGEPVAAIRriPAEGEFRT-------NLAR 213

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472 229 MGAYSPAPvvtadvhqrVMDEVIWPTVKGMAAegnvyTGFLYAGL-MIDHHGAPKVIEFN 287
Cdd:COG0189  214 GGRAEPVE---------LTDEERELALRAAPA-----LGLDFAGVdLIEDDDGPLVLEVN 259
ddl PRK01372
D-alanine--D-alanine ligase; Reviewed
 104-193 5.08e-05

D-alanine--D-alanine ligase; Reviewed


Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 44.72  E-value: 5.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472 104 KAFTKDFLARHKIPTADYQNFTEVEPALAYLQEKGAPIVIKadglAAGKGVIVAMTLTEAEEAVRDMLSgNAFGDaGARV 183
Cdd:PRK01372  99 KLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVK----PAREGSSVGVSKVKEEDELQAALE-LAFKY-DDEV 172

                         90
                 ....*....|
gi 518172472 184 VIEEFLDGEE 193
Cdd:PRK01372 173 LVEKYIKGRE 182
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
104-291 4.02e-04

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


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 42.22  E-value: 4.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472 104 KAFTKDFLARHKIPTADYQNFTEVEPALAYLQEKGAPIVIK-ADGLAA-------GKGVIVAMTLTEAEEAVRDMLsgna 175
Cdd:COG3919  118 KERFYELAEELGVPVPKTVVLDSADDLDALAEDLGFPVVVKpADSVGYdelsfpgKKKVFYVDDREELLALLRRIA---- 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472 176 fgDAGARVVIEEFL---DGEEASFIVMVDGA-NVLpmATSQDHKRVGDgdtgPNTGGMGAYspapVVTADvhqrvmDEVI 251
Cdd:COG3919  194 --AAGYELIVQEYIpgdDGEMRGLTAYVDRDgEVV--ATFTGRKLRHY----PPAGGNSAA----RESVD------DPEL 255

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 518172472 252 WPTVKGMAAEGNvYTGFLYAGLMIDH-HGAPKVIEFNCRFG 291
Cdd:COG3919  256 EEAARRLLEALG-YHGFANVEFKRDPrDGEYKLIEINPRFW 295
ATP-grasp pfam02222
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ...
 112-198 5.21e-04

ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.


Pssm-ID: 396689 [Multi-domain]  Cd Length: 169  Bit Score: 40.70  E-value: 5.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472  112 ARHKIPTADYQNFTEVEPALAYLQEKGAPIVIKADGLA-AGKGVIVAMTLTEAEEAVRDMLSGnafgdagaRVVIEEFLD 190
Cdd:pfam02222   1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADLPQAWEELGDG--------PVIVEEFVP 72


                  ....*....
gi 518172472  191 GE-EASFIV 198
Cdd:pfam02222  73 FDrELSVLV 81
PRK06111 PRK06111
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 87-190 2.13e-03

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 180406 [Multi-domain]  Cd Length: 450  Bit Score: 40.01  E-value: 2.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472  87 GLDCFGPTAAAAQLEGSKAFTKDFLARHKIPT--ADYQNFTEVEPALAYLQEKGAPIVIKAdglAAGKGVIvAMTLTEAE 164
Cdd:PRK06111  99 GIVFIGPSADIIAKMGSKIEARRAMQAAGVPVvpGITTNLEDAEEAIAIARQIGYPVMLKA---SAGGGGI-GMQLVETE 174

                         90       100       110
                 ....*....|....*....|....*....|..
gi 518172472 165 EAVRDMLSGN------AFGDagARVVIEEFLD 190
Cdd:PRK06111 175 QELTKAFESNkkraanFFGN--GEMYIEKYIE 204
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 92-190 3.79e-03

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 39.40  E-value: 3.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472  92 GPTAAAAQLEGSKAFTKDFLARHKIPT---ADYQNFTEVEpALAYLQEKGAPIVIKADGLAAGKGVIVAMTLTEAEEAVR 168
Cdd:PRK08591 104 GPSAETIRLMGDKVTAKATMKKAGVPVvpgSDGPVDDEEE-ALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFS 182

                         90       100
                 ....*....|....*....|....*
gi 518172472 169 dMLSGNA---FGDAGarVVIEEFLD 190
Cdd:PRK08591 183 -MARAEAkaaFGNPG--VYMEKYLE 204
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 127-204 9.99e-03

Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.


Pssm-ID: 397079 [Multi-domain]  Cd Length: 209  Bit Score: 37.28  E-value: 9.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172472  127 VEPALAYLQEKGAPIVIKADGLAAGKGVIVAMTLTEAEEAVRDML--SGNAFGDAgaRVVIEEFLDG-EEASFIVMVDGA 203
Cdd:pfam02786  27 EEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALaeAPAAFGNP--QVLVEKSLKGpKHIEYQVLRDAH 104


                  .
gi 518172472  204 N 204
Cdd:pfam02786 105 G 105
 
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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