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Conserved domains on  [gi|1045264708|gb|ANU49572|]
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phosphoribosylamine--glycine ligase [Lachnoclostridium sp. YL32]

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]; ...
 1-419 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: 730.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708   1 MKVLIVGGGGREHAIAWKISQSPKVEKLYCAPGNAGIAKVAECVDIGVMDFEKLVAFAGEQAIDLVVVGPDDPLAAGAVD 80
Cdd:COG0151     1 MKVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAECVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIVD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708  81 AFEDAGIRVFGPGKNAAILEASKAFSKDLMKKYNIPSAAYETFDSPEAALTYLETAPMPIVLKADGLALGKGVLICNTRE 160
Cdd:COG0151    81 AFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAETLE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 161 EAKEGVKTLMLDKQFGSAGDRIVIEEFMTGREVSVLSFVDGHTIKIMTSAQDHKRAKDGDQGLNTGGMGTFSPSPFYTDE 240
Cdd:COG0151   161 EALAAVDDMLADGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVTEE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 241 VDAFCRKYVYQPTVDAMKAEGREFKGIIFFGLMLTENGPKVLEYNARFGDPETQVVLPRMKNDIVDVFEACVDGTLDQIE 320
Cdd:COG0151   241 LLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRLDEVE 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 321 LEFEDNAAVCVVLASDGYPEHYEKGYKIDGLDRFDgQDGYYVFHAGSKFdKDGNVVTNGGRVLGVTAKGNTLKEARENAY 400
Cdd:COG0151   321 LEWDDRAAVCVVLASGGYPGSYEKGDVITGLEEAE-AEGVKVFHAGTAL-EDGKLVTNGGRVLGVTALGDTLEEARERAY 398

                         410
                  ....*....|....*....
gi 1045264708 401 KAAEWVEFGNKYMRHDIGK 419
Cdd:COG0151   399 EAVEKIRFEGMFYRRDIGW 417
 
Name Accession Description Interval E-value
PurD COG0151
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ...
 1-419 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: 730.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708   1 MKVLIVGGGGREHAIAWKISQSPKVEKLYCAPGNAGIAKVAECVDIGVMDFEKLVAFAGEQAIDLVVVGPDDPLAAGAVD 80
Cdd:COG0151     1 MKVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAECVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIVD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708  81 AFEDAGIRVFGPGKNAAILEASKAFSKDLMKKYNIPSAAYETFDSPEAALTYLETAPMPIVLKADGLALGKGVLICNTRE 160
Cdd:COG0151    81 AFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAETLE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 161 EAKEGVKTLMLDKQFGSAGDRIVIEEFMTGREVSVLSFVDGHTIKIMTSAQDHKRAKDGDQGLNTGGMGTFSPSPFYTDE 240
Cdd:COG0151   161 EALAAVDDMLADGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVTEE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 241 VDAFCRKYVYQPTVDAMKAEGREFKGIIFFGLMLTENGPKVLEYNARFGDPETQVVLPRMKNDIVDVFEACVDGTLDQIE 320
Cdd:COG0151   241 LLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRLDEVE 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 321 LEFEDNAAVCVVLASDGYPEHYEKGYKIDGLDRFDgQDGYYVFHAGSKFdKDGNVVTNGGRVLGVTAKGNTLKEARENAY 400
Cdd:COG0151   321 LEWDDRAAVCVVLASGGYPGSYEKGDVITGLEEAE-AEGVKVFHAGTAL-EDGKLVTNGGRVLGVTALGDTLEEARERAY 398

                         410
                  ....*....|....*....
gi 1045264708 401 KAAEWVEFGNKYMRHDIGK 419
Cdd:COG0151   399 EAVEKIRFEGMFYRRDIGW 417
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: 543.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708   1 MKVLIVGGGGREHAIAWKISQSPKVEKLYCAPGNAGIAKVAEC--VDIGVMDFEKLVAFAGEQAIDLVVVGPDDPLAAGA 78
Cdd:TIGR00877   1 MKVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNknVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708  79 VDAFEDAGIRVFGPGKNAAILEASKAFSKDLMKKYNIPSAAYETFDSPEAALTYLETAPMPIVLKADGLALGKGVLICNT 158
Cdd:TIGR00877  81 VDALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPIVVKADGLAAGKGVIVAKT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 159 REEAKEGVKTLMlDKQFGSAGDRIVIEEFMTGREVSVLSFVDGHTIKIMTSAQDHKRAKDGDQGLNTGGMGTFSPSPFYT 238
Cdd:TIGR00877 161 NEEAIKAVEDIL-EQKFGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 239 DEVDAFCRKYVYQPTVDAMKAEGREFKGIIFFGLMLTENGPKVLEYNARFGDPETQVVLPRMKNDIVDVFEACVDGTLDQ 318
Cdd:TIGR00877 240 EEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGPKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKLDE 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 319 IELEFEDNAAVCVVLASDGYPEHYEKGYKIDGLDRFDGQDGyYVFHAGSKFDkDGNVVTNGGRVLGVTAKGNTLKEAREN 398
Cdd:TIGR00877 320 VELRFDNRAAVTVVLASEGYPEDYRKGDPITGEPLAEAEGV-KVFHAGTKAD-NGKLVTNGGRVLAVTALGKTLEEARER 397

                         410       420
                  ....*....|....*....|....*
gi 1045264708 399 AYKAAEWVEFGNKYMRHDIG-KAID 422
Cdd:TIGR00877 398 AYEAVEYIKFEGMFYRKDIGfRALE 422
PLN02257 PLN02257
phosphoribosylamine--glycine ligase
 4-418 1.41e-169

phosphoribosylamine--glycine ligase


Pssm-ID: 177899 [Multi-domain]  Cd Length: 434  Bit Score: 482.32  E-value: 1.41e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708   4 LIVGGGGREHAIAWKISQSPKVEKLYCAPGNAGIAKV--AECV-DIGVMDFEKLVAFAGEQAIDLVVVGPDDPLAAGAVD 80
Cdd:PLN02257    1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSgdATCVpDLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708  81 AFEDAGIRVFGPGKNAAILEASKAFSKDLMKKYNIPSAAYETFDSPEAALTYLETAPMPIVLKADGLALGKGVLICNTRE 160
Cdd:PLN02257   81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAPIVVKADGLAAGKGVVVAMTLE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 161 EAKEGVKTLMLDKQFGSAGDRIVIEEFMTGREVSVLSFVDGHTIKIMTSAQDHKRAKDGDQGLNTGGMGTFSPSPFYTDE 240
Cdd:PLN02257  161 EAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTPE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 241 VDAFCRKYVYQPTVDAMKAEGREFKGIIFFGLMLTENG--PKVLEYNARFGDPETQVVLPRMKNDIVDVFEACVDGTLDQ 318
Cdd:PLN02257  241 LESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKSglPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELSG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 319 IELEFEDNAAVCVVLASDGYPEHYEKGYKIDGLDRFDG-QDGYYVFHAGSKFDKDGNVVTNGGRVLGVTAKGNTLKEARE 397
Cdd:PLN02257  321 VSLTWSPDSAMVVVMASNGYPGSYKKGTVIKNLDEAEAvAPGVKVFHAGTALDSDGNVVAAGGRVLGVTAKGKDIAEARA 400

                         410       420
                  ....*....|....*....|.
gi 1045264708 398 NAYKAAEWVEFGNKYMRHDIG 418
Cdd:PLN02257  401 RAYDAVDQIDWPGGFFRRDIG 421
GARS_A pfam01071
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ...
 101-293 9.37e-94

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: 280.32  E-value: 9.37e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 101 ASKAFSKDLMKKYNIPSAAYETFDSPEAALTYLETAPMPI-VLKADGLALGKGVLICNTREEAKEGVKTLMLDKQFGSAG 179
Cdd:pfam01071   1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAiVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 180 DRIVIEEFMTGREVSVLSFVDGHTIKIMTSAQDHKRAKDGDQGLNTGGMGTFSPSPFYTDEVDAFCRKYVYQPTVDAMKA 259
Cdd:pfam01071  81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1045264708 260 EGREFKGIIFFGLMLTENGPKVLEYNARFGDPET 293
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDGPKVLEFNCRFGDPET 194
 
Name Accession Description Interval E-value
PurD COG0151
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ...
 1-419 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: 730.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708   1 MKVLIVGGGGREHAIAWKISQSPKVEKLYCAPGNAGIAKVAECVDIGVMDFEKLVAFAGEQAIDLVVVGPDDPLAAGAVD 80
Cdd:COG0151     1 MKVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAECVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIVD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708  81 AFEDAGIRVFGPGKNAAILEASKAFSKDLMKKYNIPSAAYETFDSPEAALTYLETAPMPIVLKADGLALGKGVLICNTRE 160
Cdd:COG0151    81 AFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAETLE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 161 EAKEGVKTLMLDKQFGSAGDRIVIEEFMTGREVSVLSFVDGHTIKIMTSAQDHKRAKDGDQGLNTGGMGTFSPSPFYTDE 240
Cdd:COG0151   161 EALAAVDDMLADGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVTEE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 241 VDAFCRKYVYQPTVDAMKAEGREFKGIIFFGLMLTENGPKVLEYNARFGDPETQVVLPRMKNDIVDVFEACVDGTLDQIE 320
Cdd:COG0151   241 LLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRLDEVE 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 321 LEFEDNAAVCVVLASDGYPEHYEKGYKIDGLDRFDgQDGYYVFHAGSKFdKDGNVVTNGGRVLGVTAKGNTLKEARENAY 400
Cdd:COG0151   321 LEWDDRAAVCVVLASGGYPGSYEKGDVITGLEEAE-AEGVKVFHAGTAL-EDGKLVTNGGRVLGVTALGDTLEEARERAY 398

                         410
                  ....*....|....*....
gi 1045264708 401 KAAEWVEFGNKYMRHDIGK 419
Cdd:COG0151   399 EAVEKIRFEGMFYRRDIGW 417
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: 543.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708   1 MKVLIVGGGGREHAIAWKISQSPKVEKLYCAPGNAGIAKVAEC--VDIGVMDFEKLVAFAGEQAIDLVVVGPDDPLAAGA 78
Cdd:TIGR00877   1 MKVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNknVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708  79 VDAFEDAGIRVFGPGKNAAILEASKAFSKDLMKKYNIPSAAYETFDSPEAALTYLETAPMPIVLKADGLALGKGVLICNT 158
Cdd:TIGR00877  81 VDALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPIVVKADGLAAGKGVIVAKT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 159 REEAKEGVKTLMlDKQFGSAGDRIVIEEFMTGREVSVLSFVDGHTIKIMTSAQDHKRAKDGDQGLNTGGMGTFSPSPFYT 238
Cdd:TIGR00877 161 NEEAIKAVEDIL-EQKFGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 239 DEVDAFCRKYVYQPTVDAMKAEGREFKGIIFFGLMLTENGPKVLEYNARFGDPETQVVLPRMKNDIVDVFEACVDGTLDQ 318
Cdd:TIGR00877 240 EEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGPKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKLDE 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 319 IELEFEDNAAVCVVLASDGYPEHYEKGYKIDGLDRFDGQDGyYVFHAGSKFDkDGNVVTNGGRVLGVTAKGNTLKEAREN 398
Cdd:TIGR00877 320 VELRFDNRAAVTVVLASEGYPEDYRKGDPITGEPLAEAEGV-KVFHAGTKAD-NGKLVTNGGRVLAVTALGKTLEEARER 397

                         410       420
                  ....*....|....*....|....*
gi 1045264708 399 AYKAAEWVEFGNKYMRHDIG-KAID 422
Cdd:TIGR00877 398 AYEAVEYIKFEGMFYRKDIGfRALE 422
PLN02257 PLN02257
phosphoribosylamine--glycine ligase
 4-418 1.41e-169

phosphoribosylamine--glycine ligase


Pssm-ID: 177899 [Multi-domain]  Cd Length: 434  Bit Score: 482.32  E-value: 1.41e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708   4 LIVGGGGREHAIAWKISQSPKVEKLYCAPGNAGIAKV--AECV-DIGVMDFEKLVAFAGEQAIDLVVVGPDDPLAAGAVD 80
Cdd:PLN02257    1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSgdATCVpDLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708  81 AFEDAGIRVFGPGKNAAILEASKAFSKDLMKKYNIPSAAYETFDSPEAALTYLETAPMPIVLKADGLALGKGVLICNTRE 160
Cdd:PLN02257   81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAPIVVKADGLAAGKGVVVAMTLE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 161 EAKEGVKTLMLDKQFGSAGDRIVIEEFMTGREVSVLSFVDGHTIKIMTSAQDHKRAKDGDQGLNTGGMGTFSPSPFYTDE 240
Cdd:PLN02257  161 EAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTPE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 241 VDAFCRKYVYQPTVDAMKAEGREFKGIIFFGLMLTENG--PKVLEYNARFGDPETQVVLPRMKNDIVDVFEACVDGTLDQ 318
Cdd:PLN02257  241 LESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKSglPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELSG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 319 IELEFEDNAAVCVVLASDGYPEHYEKGYKIDGLDRFDG-QDGYYVFHAGSKFDKDGNVVTNGGRVLGVTAKGNTLKEARE 397
Cdd:PLN02257  321 VSLTWSPDSAMVVVMASNGYPGSYKKGTVIKNLDEAEAvAPGVKVFHAGTALDSDGNVVAAGGRVLGVTAKGKDIAEARA 400

                         410       420
                  ....*....|....*....|.
gi 1045264708 398 NAYKAAEWVEFGNKYMRHDIG 418
Cdd:PLN02257  401 RAYDAVDQIDWPGGFFRRDIG 421
GARS_A pfam01071
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ...
 101-293 9.37e-94

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: 280.32  E-value: 9.37e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 101 ASKAFSKDLMKKYNIPSAAYETFDSPEAALTYLETAPMPI-VLKADGLALGKGVLICNTREEAKEGVKTLMLDKQFGSAG 179
Cdd:pfam01071   1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAiVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 180 DRIVIEEFMTGREVSVLSFVDGHTIKIMTSAQDHKRAKDGDQGLNTGGMGTFSPSPFYTDEVDAFCRKYVYQPTVDAMKA 259
Cdd:pfam01071  81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1045264708 260 EGREFKGIIFFGLMLTENGPKVLEYNARFGDPET 293
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDGPKVLEFNCRFGDPET 194
GARS_N pfam02844
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes ...
 1-100 3.31e-60

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: 190.65  E-value: 3.31e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708   1 MKVLIVGGGGREHAIAWKISQSPKVEKLYCAPGNAGIAKVAECVDIGVMDFEKLVAFAGEQAIDLVVVGPDDPLAAGAVD 80
Cdd:pfam02844   1 MKVLVIGSGGREHALAWKLAQSPLVEKLYVAPGNGGTAQLAECVDIDATDFEALVAFAKENNIDLVVVGPEAPLVAGIVD 80

                          90       100
                  ....*....|....*....|..
gi 1045264708  81 AF--EDAGIRVFGPGKNAAILE 100
Cdd:pfam02844  81 ALreRAAGIPVFGPSKAAAQLE 102
GARS_C pfam02843
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes ...
 328-419 1.29e-40

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: 139.50  E-value: 1.29e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 328 AVCVVLASDGYPEHYEKGYKIDGLDrfdgQDGYYVFHAGSKFdKDGNVVTNGGRVLGVTAKGNTLKEARENAYKAAEWVE 407
Cdd:pfam02843   1 AVCVVLASGGYPGSYEKGDVITGLD----EAGVKVFHAGTKL-KDGKLVTSGGRVLAVTALGDTLEEAREKAYEAVEKID 75

                          90
                  ....*....|..
gi 1045264708 408 FGNKYMRHDIGK 419
Cdd:pfam02843  76 FEGMFYRKDIGT 87
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 50-289 3.26e-20

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: 89.55  E-value: 3.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708  50 DFEKLVAFAGEQA----IDLVVVGPDD--PLAAGAVDAFedaGIrvfgPGKNAAILEA--SKAFSKDLMKKYNIPSAAYE 121
Cdd:COG0439     1 DIDAIIAAAAELAretgIDAVLSESEFavETAAELAEEL---GL----PGPSPEAIRAmrDKVLMREALAAAGVPVPGFA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 122 TFDSPEAALTYLETAPMPIVLKADGLALGKGVLICNTREEAKEGVKTLMLDKQFGSAGDRIVIEEFMTGREVSVLSFVDG 201
Cdd:COG0439    74 LVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEGREYSVEGLVRD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 202 HTIKImTSAQDhkRAKDGDQGLNTGGMgtfSPSPFyTDEVDAFCRKYVyqptVDAMKAEGREFkGIIFFGLMLTENG-PK 280
Cdd:COG0439   154 GEVVV-CSITR--KHQKPPYFVELGHE---APSPL-PEELRAEIGELV----ARALRALGYRR-GAFHTEFLLTPDGePY 221


                  ....*....
gi 1045264708 281 VLEYNARFG 289
Cdd:COG0439   222 LIEINARLG 230
PurK COG0026
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ...
 61-196 1.78e-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: 52.77  E-value: 1.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708  61 QAIDLVVVGP-DDPLA----AGAVDA----FE----------DAGIRVFgPGknAAILEAS--KAFSKDLMKKYNIPSAA 119
Cdd:COG0026    30 QVADEHIVADyDDEEAlrefAERCDVvtfeFEnvpaealealEAEVPVR-PG--PEALEIAqdRLLEKAFLAELGIPVAP 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 120 YETFDSPEAALTYLETAPMPIVLKA-----DglalGKGVLICNTREEAKEGVKTLmldkqfgsAGDRIVIEEFMT-GREV 193
Cdd:COG0026   107 FAAVDSLEDLEAAIAELGLPAVLKTrrggyD----GKGQVVIKSAADLEAAWAAL--------GGGPCILEEFVPfEREL 174


                  ...
gi 1045264708 194 SVL 196
Cdd:COG0026   175 SVI 177
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 103-195 8.35e-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: 50.49  E-value: 8.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 103 KAFSKDLMKKYNIPSAAYETFDSPEAALTYLETAPM--PIVLKAdgLALG--KGVLICNTREEAKEGVKTLMldkqfgSA 178
Cdd:COG1181    96 KALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEELglPLFVKP--AREGssVGVSKVKNAEELAAALEEAF------KY 167

                          90
                  ....*....|....*..
gi 1045264708 179 GDRIVIEEFMTGREVSV 195
Cdd:COG1181   168 DDKVLVEEFIDGREVTV 184
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 1-289 1.02e-06

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 50.27  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708   1 MKVLIVGGGGREHAI-AWKISQSP-KVEKLYCAPGNAGIAKVAECV------DIGVMDFekLVAFAGEQAIDLVVVG--P 70
Cdd:PRK12767    2 MNILVTSAGRRVQLVkALKKSLLKgRVIGADISELAPALYFADKFYvvpkvtDPNYIDR--LLDICKKEKIDLLIPLidP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708  71 DDPLAAGAVDAFEDAGIRVFGPGKNAAileaSKAFSKDLMKKY----NIPSAAYETFDSPEAALTYLETAPM--PIVLKA 144
Cdd:PRK12767   80 ELPLLAQNRDRFEEIGVKVLVSSKEVI----EICNDKWLTYEFlkenGIPTPKSYLPESLEDFKAALAKGELqfPLFVKP 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 145 DGLALGKGVLICNTREEakegvktLMLDKQFGSAgdrIVIEEFMTGRE--VSVLSFVDGHTIKIMTSAQDHKRAKDGDQG 222
Cdd:PRK12767  156 RDGSASIGVFKVNDKEE-------LEFLLEYVPN---LIIQEFIEGQEytVDVLCDLNGEVISIVPRKRIEVRAGETSKG 225

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1045264708 223 LntggmgTFsPSPFYTDEVDAFCRKYvyqptvdamkaegrEFKGIIFFGLMLTENGPKVLEYNARFG 289
Cdd:PRK12767  226 V------TV-KDPELFKLAERLAEAL--------------GARGPLNIQCFVTDGEPYLFEINPRFG 271
PRK07206 PRK07206
hypothetical protein; Provisional
 124-287 7.72e-05

hypothetical protein; Provisional


Pssm-ID: 180883 [Multi-domain]  Cd Length: 416  Bit Score: 44.63  E-value: 7.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 124 DSPEAALTYLETAPM---PIVLKADGLALGKGVLICNTREEAKEGVKTLMLDK-QFGSAGDRIVIEEFMTGREVSVLSF- 198
Cdd:PRK07206  130 ADWEEAEAWLRENGLidrPVVIKPLESAGSDGVFICPAKGDWKHAFNAILGKAnKLGLVNETVLVQEYLIGTEYVVNFVs 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 199 VDG-HTIKIM-----TSAQDHKRAKDGDQGLntggmgtfspsPFYTDEVDAFCrKYVYQptvdAMKAEGrefkgiIFFG- 271
Cdd:PRK07206  210 LDGnHLVTEIvryhkTSLNSGSTVYDYDEFL-----------DYSEPEYQELV-DYTKQ----ALDALG------IKNGp 267

                         170       180
                  ....*....|....*....|
gi 1045264708 272 ----LMLTENGPKVLEYNAR 287
Cdd:PRK07206  268 ahaeVMLTADGPRLIEIGAR 287
ddl PRK01966
D-alanine--D-alanine ligase;
82-195 3.70e-04

D-alanine--D-alanine ligase;


Pssm-ID: 234993 [Multi-domain]  Cd Length: 333  Bit Score: 42.42  E-value: 3.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708  82 FEDAGIRVFGPGknaaiLEASKA-FSKDLMKKY----NIPSAAYETFDSPEAALTYLETAP----MPIVLKAdgLALGK- 151
Cdd:PRK01966  103 LELLGIPYVGCG-----VLASALsMDKILTKRLlaaaGIPVAPYVVLTRGDWEEASLAEIEaklgLPVFVKP--ANLGSs 175

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1045264708 152 -GVLICNTREEAKEGvktlmLDKQFGSAgDRIVIEEFMTGREVSV 195
Cdd:PRK01966  176 vGISKVKNEEELAAA-----LDLAFEYD-RKVLVEQGIKGREIEC 214
PRK06019 PRK06019
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
 58-196 5.35e-04

phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed


Pssm-ID: 235674 [Multi-domain]  Cd Length: 372  Bit Score: 42.06  E-value: 5.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708  58 AGEQAIDLVVVGPDDPLA----AGAVDA----FE----------DAGIRVFgPGKNA-AILeASKAFSKDLMKKYNIPSA 118
Cdd:PRK06019   39 AAQVADEVIVADYDDVAAlrelAEQCDVityeFEnvpaealdalAARVPVP-PGPDAlAIA-QDRLTEKQFLDKLGIPVA 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 119 AYETFDSPEAALTYLETAPMPIVLKA-----DglalGKGVLICNTREEAKEGVKTLmldkqfgsAGDRIVIEEFMT-GRE 192
Cdd:PRK06019  117 PFAVVDSAEDLEAALADLGLPAVLKTrrggyD----GKGQWVIRSAEDLEAAWALL--------GSVPCILEEFVPfERE 184


                  ....
gi 1045264708 193 VSVL 196
Cdd:PRK06019  185 VSVI 188
ATP-grasp_2 pfam08442
ATP-grasp domain;
106-186 1.41e-03

ATP-grasp domain;


Pssm-ID: 400651 [Multi-domain]  Cd Length: 202  Bit Score: 39.55  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 106 SKDLMKKYNIPSAAYETFDSPEAAltyLETAPM----PIVLKADGLALGK----GVLICNTREEAKEGVKTL----MLDK 173
Cdd:pfam08442   7 AKEIFAKYGIPVPRGEVATSPEEA---EEIAKKlggkVYVVKAQVLAGGRgkagGVKLAKSPEEAKEVAKEMlgknLVTK 83

                          90
                  ....*....|....*.
gi 1045264708 174 QFGSAG---DRIVIEE 186
Cdd:pfam08442  84 QTGPDGqpvNKVLVEE 99
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 74-287 2.08e-03

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 40.37  E-value: 2.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708   74 LAAGAVDAFEDAGIRVFG-PGKNAAILEASKAFSKdLMKKYNIPSAAYETFDSPEAALTYLETAPMPIVLKADGLALGKG 152
Cdd:TIGR01369  641 TPLNLAKALEEAGVPILGtSPESIDRAEDREKFSE-LLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRA 719

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708  153 VLICNTREEakegVKTLMLDKQFGSAGDRIVIEEFMT-GREVSVLSFVDGHTIKIMTSAQDHKRAkdgdqGLNTGGMGTF 231
Cdd:TIGR01369  720 MEIVYNEEE----LRRYLEEAVAVSPEHPVLIDKYLEdAVEVDVDAVSDGEEVLIPGIMEHIEEA-----GVHSGDSTCV 790

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1045264708  232 SPSPFYTDEVDAFCRKYVYQptvdamKAEGREFKGIIFFGLMLTENGPKVLEYNAR 287
Cdd:TIGR01369  791 LPPQTLSAEIVDRIKDIVRK------IAKELNVKGLMNIQFAVKDGEVYVIEVNPR 840
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
80-204 3.67e-03

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 39.58  E-value: 3.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708  80 DAFEDAGIRVFGPGKNAAILEASKAFSKDLMKKYNIP--SAAYETFDSPEAALTYLETAPMPIVLKADGLALGKGVLICN 157
Cdd:PRK08654   93 KACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPvlPGTEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVY 172

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1045264708 158 TREEAKEGVKTLMldKQFGSA-GDRIV-IEEFMTG-R--EVSVLSFVDGHTI 204
Cdd:PRK08654  173 SEEELEDAIESTQ--SIAQSAfGDSTVfIEKYLEKpRhiEIQILADKHGNVI 222
ddl PRK01372
D-alanine--D-alanine ligase; Reviewed
 103-195 4.16e-03

D-alanine--D-alanine ligase; Reviewed


Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 38.94  E-value: 4.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708 103 KAFSKDLMKKYNIPSAAYETFDSPEAALTYLETAPMPIVLK--ADGLALgkGVLICNTREEAKEGvktLMLDKQFgsaGD 180
Cdd:PRK01372   99 KLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKpaREGSSV--GVSKVKEEDELQAA---LELAFKY---DD 170

                          90
                  ....*....|....*
gi 1045264708 181 RIVIEEFMTGREVSV 195
Cdd:PRK01372  171 EVLVEKYIKGRELTV 185
PRK05586 PRK05586
acetyl-CoA carboxylase biotin carboxylase subunit;
83-188 5.66e-03

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180150 [Multi-domain]  Cd Length: 447  Bit Score: 38.92  E-value: 5.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045264708  83 EDAGIRVFGPGKNAAILEASKAFSKDLMKKYNIPSA-AYE-TFDSPEAALTYLETAPMPIVLKADGLALGKGVLICNTRE 160
Cdd:PRK05586   96 KECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVpGSEgEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEE 175

                          90       100
                  ....*....|....*....|....*...
gi 1045264708 161 EAKEGVKTLMLDKQFGSAGDRIVIEEFM 188
Cdd:PRK05586  176 ELIKAFNTAKSEAKAAFGDDSMYIEKFI 203
 
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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