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Conserved domains on  [gi|1676323112|dbj|BBD84397|]
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adenylosuccinate synthetase, partial [Drosophila lucipennis]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Adenylsucc_synt super family cl46237
Adenylosuccinate synthetase;
1-103 1.83e-48

Adenylosuccinate synthetase;


The actual alignment was detected with superfamily member pfam00709:

Pssm-ID: 459912  Cd Length: 417  Bit Score: 158.67  E-value: 1.83e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676323112   1 IGPAYSSKATRNGIRVGELLgDFNLFSDKFKSIVATHVRLFPSIN---VDVEAELARYRDYVDKVRPYVKDTICFLHTAL 77
Cdd:pfam00709 129 IGPAYSDKAARRGIRVGDLL-DPEVFREKLEALLELKNKLLEKLYgepLDVEEELEELLEYAERLKPYVVDTSYFLNKAL 207

                          90       100
                  ....*....|....*....|....*.
gi 1676323112  78 RNGKTILVEGANAAMLDIDFGTYPYV 103
Cdd:pfam00709 208 KEGKKILFEGAQGTLLDIDHGTYPYV 233
 
Name Accession Description Interval E-value
Adenylsucc_synt pfam00709
Adenylosuccinate synthetase;
1-103 1.83e-48

Adenylosuccinate synthetase;


Pssm-ID: 459912  Cd Length: 417  Bit Score: 158.67  E-value: 1.83e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676323112   1 IGPAYSSKATRNGIRVGELLgDFNLFSDKFKSIVATHVRLFPSIN---VDVEAELARYRDYVDKVRPYVKDTICFLHTAL 77
Cdd:pfam00709 129 IGPAYSDKAARRGIRVGDLL-DPEVFREKLEALLELKNKLLEKLYgepLDVEEELEELLEYAERLKPYVVDTSYFLNKAL 207

                          90       100
                  ....*....|....*....|....*.
gi 1676323112  78 RNGKTILVEGANAAMLDIDFGTYPYV 103
Cdd:pfam00709 208 KEGKKILFEGAQGTLLDIDHGTYPYV 233
PTZ00350 PTZ00350
adenylosuccinate synthetase; Provisional
 1-103 8.30e-42

adenylosuccinate synthetase; Provisional


Pssm-ID: 240376  Cd Length: 436  Bit Score: 141.70  E-value: 8.30e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676323112   1 IGPAYSSKATRNGIRVGELLgDFNLFSDKFKSIVATHVRLFPSINVDVEAELARYRDYVDKVRPYVKDTICFLHTALRNG 80
Cdd:PTZ00350  146 IGPCYSTKASRTGLRVGDLL-NFETFEKKYRKLVEKLQEQYNIEEYDAEEELERYKGYAEKLKDMIVDTVYFMNKAIKEG 224

                          90       100
                  ....*....|....*....|...
gi 1676323112  81 KTILVEGANAAMLDIDFGTYPYV 103
Cdd:PTZ00350  225 KRVLVEGANATMLDIDFGTYPYV 247
Adenylsucc_synt smart00788
Adenylosuccinate synthetase; Adenylosuccinate synthetase plays an important role in purine ...
 1-103 1.05e-40

Adenylosuccinate synthetase; Adenylosuccinate synthetase plays an important role in purine biosynthesis, by catalyzing the GTP-dependent conversion of IMP and aspartic acid to AMP. Adenylosuccinate synthetase has been characterized from various sources ranging from Escherichia coli (gene purA) to vertebrate tissues. In vertebrates, two isozymes are present - one involved in purine biosynthesis and the other in the purine nucleotide cycle. The crystal structure of adenylosuccinate synthetase from E. coli reveals that the dominant structural element of each monomer of the homodimer is a central beta-sheet of 10 strands. The first nine strands of the sheet are mutually parallel with right-handed crossover connections between the strands. The 10th strand is antiparallel with respect to the first nine strands. In addition, the enzyme has two antiparallel beta-sheets, comprised of two strands and three strands each, 11 alpha-helices and two short 3/10-helices. Further, it has been suggested that the similarities in the GTP-binding domains of the synthetase and the p21ras protein are an example of convergent evolution of two distinct families of GTP-binding proteins. Structures of adenylosuccinate synthetase from Triticum aestivum and Arabidopsis thaliana when compared with the known structures from E. coli reveals that the overall fold is very similar to that of the E. coli protein.


Pssm-ID: 197875  Cd Length: 417  Bit Score: 138.38  E-value: 1.05e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676323112    1 IGPAYSSKATRNGIRVGELLgDFNLFSDKFKSIVATHVRLFPSIN----VDVEAELARYRDYVDKVRPYVKDTICFLHTA 76
Cdd:smart00788 127 IGPAYEDKVARRGIRVGDLF-DEEVLREKLEELLDYKNFLLKKLYgaepVDVEEILEELLEYAERLRPYVTDVSELLNEA 205

                           90       100
                   ....*....|....*....|....*..
gi 1676323112   77 LRNGKTILVEGANAAMLDIDFGTYPYV 103
Cdd:smart00788 206 LKAGKKVLFEGAQGTLLDIDHGTYPYV 232
PurA COG0104
Adenylosuccinate synthase [Nucleotide transport and metabolism]; Adenylosuccinate synthase is ...
 1-103 2.81e-36

Adenylosuccinate synthase [Nucleotide transport and metabolism]; Adenylosuccinate synthase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439874  Cd Length: 423  Bit Score: 126.67  E-value: 2.81e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676323112   1 IGPAYSSKATRNGIRVGELLgDFNLFSDKFKSIVATHVRLFPSIN----VDVEAELARYRDYVDKVRPYVKDTICFLHTA 76
Cdd:COG0104   131 IGPAYEDKVARRGIRVGDLL-DPEVLREKLEELLEYKNFLLEKLYgaepLDFEELLEEYLEYAERLKPYVADTSELLNEA 209

                          90       100
                  ....*....|....*....|....*..
gi 1676323112  77 LRNGKTILVEGANAAMLDIDFGTYPYV 103
Cdd:COG0104   210 LKAGKKVLFEGAQGTLLDIDHGTYPYV 236
purA TIGR00184
adenylosuccinate synthase; Alternate name IMP--aspartate ligase. [Purines, pyrimidines, ...
 1-103 1.13e-28

adenylosuccinate synthase; Alternate name IMP--aspartate ligase. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 272949  Cd Length: 425  Bit Score: 106.48  E-value: 1.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676323112   1 IGPAYSSKATRNGIRVGELLGDfNLFSDKFKSIVATHVRLF----PSINVDVEAELARYRDYVDKVRPYVKDTICFLHTA 76
Cdd:TIGR00184 129 IGPAYEDKVARSGLRVGDLLDD-EAFAEKAKNILEYLNEQLvkyyKDEGVDYEKKLDEYMKYAEELKPFVVDVSVELNEA 207

                          90       100
                  ....*....|....*....|....*..
gi 1676323112  77 LRNGKTILVEGANAAMLDIDFGTYPYV 103
Cdd:TIGR00184 208 LDEGEKVLFEGAQGTMLDIDYGTYPYV 234
AdSS cd03108
adenylosuccinate synthetase; Adenylosuccinate synthetase (AdSS) catalyzes the first step in ...
 1-103 2.54e-24

adenylosuccinate synthetase; Adenylosuccinate synthetase (AdSS) catalyzes the first step in the de novo biosynthesis of AMP. IMP and L-aspartate are conjugated in a two-step reaction accompanied by the hydrolysis of GTP to GDP in the presence of Mg2+. In the first step, the r-phosphate group of GTP is transferred to the 6-oxygen atom of IMP. An aspartate then displaces this 6-phosphate group to form the product adenylosuccinate. Because of its critical role in purine biosynthesis, AdSS is a target of antibiotics, herbicides and antitumor drugs.


Pssm-ID: 349762  Cd Length: 316  Bit Score: 93.33  E-value: 2.54e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676323112   1 IGPAYSSKATRNGIRVGEllgdfnlfsdkfksivathvrlfpsinvdveaelaryrdyvdkvrPYVKDTICFLHTALRNG 80
Cdd:cd03108   132 IGPAYADKAARTGIRVGD---------------------------------------------PYVVDTVELLNEALKAG 166

                          90       100
                  ....*....|....*....|...
gi 1676323112  81 KTILVEGANAAMLDIDFGTYPYV 103
Cdd:cd03108   167 KKVLFEGAQGTLLDIDFGTYPYV 189
 
Name Accession Description Interval E-value
Adenylsucc_synt pfam00709
Adenylosuccinate synthetase;
1-103 1.83e-48

Adenylosuccinate synthetase;


Pssm-ID: 459912  Cd Length: 417  Bit Score: 158.67  E-value: 1.83e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676323112   1 IGPAYSSKATRNGIRVGELLgDFNLFSDKFKSIVATHVRLFPSIN---VDVEAELARYRDYVDKVRPYVKDTICFLHTAL 77
Cdd:pfam00709 129 IGPAYSDKAARRGIRVGDLL-DPEVFREKLEALLELKNKLLEKLYgepLDVEEELEELLEYAERLKPYVVDTSYFLNKAL 207

                          90       100
                  ....*....|....*....|....*.
gi 1676323112  78 RNGKTILVEGANAAMLDIDFGTYPYV 103
Cdd:pfam00709 208 KEGKKILFEGAQGTLLDIDHGTYPYV 233
PTZ00350 PTZ00350
adenylosuccinate synthetase; Provisional
 1-103 8.30e-42

adenylosuccinate synthetase; Provisional


Pssm-ID: 240376  Cd Length: 436  Bit Score: 141.70  E-value: 8.30e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676323112   1 IGPAYSSKATRNGIRVGELLgDFNLFSDKFKSIVATHVRLFPSINVDVEAELARYRDYVDKVRPYVKDTICFLHTALRNG 80
Cdd:PTZ00350  146 IGPCYSTKASRTGLRVGDLL-NFETFEKKYRKLVEKLQEQYNIEEYDAEEELERYKGYAEKLKDMIVDTVYFMNKAIKEG 224

                          90       100
                  ....*....|....*....|...
gi 1676323112  81 KTILVEGANAAMLDIDFGTYPYV 103
Cdd:PTZ00350  225 KRVLVEGANATMLDIDFGTYPYV 247
PLN02513 PLN02513
adenylosuccinate synthase
 1-103 6.54e-41

adenylosuccinate synthase


Pssm-ID: 178129  Cd Length: 427  Bit Score: 139.01  E-value: 6.54e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676323112   1 IGPAYSSKATRNGIRVGELLgDFNLFSDKFKSIVATHVRLFPSINVD---VEAELARYRDYVDKVRPYVKDTICFLHTAL 77
Cdd:PLN02513  135 IGPAYSSKATRNGLRVGDLR-HMDTFAEKLRELLADAAARFEGFEYDasmVEEEVEAYKKFAERLEPFITDTVHYLNEAI 213

                          90       100
                  ....*....|....*....|....*.
gi 1676323112  78 RNGKTILVEGANAAMLDIDFGTYPYV 103
Cdd:PLN02513  214 QAGKKILVEGAQATMLDIDFGTYPFV 239
Adenylsucc_synt smart00788
Adenylosuccinate synthetase; Adenylosuccinate synthetase plays an important role in purine ...
 1-103 1.05e-40

Adenylosuccinate synthetase; Adenylosuccinate synthetase plays an important role in purine biosynthesis, by catalyzing the GTP-dependent conversion of IMP and aspartic acid to AMP. Adenylosuccinate synthetase has been characterized from various sources ranging from Escherichia coli (gene purA) to vertebrate tissues. In vertebrates, two isozymes are present - one involved in purine biosynthesis and the other in the purine nucleotide cycle. The crystal structure of adenylosuccinate synthetase from E. coli reveals that the dominant structural element of each monomer of the homodimer is a central beta-sheet of 10 strands. The first nine strands of the sheet are mutually parallel with right-handed crossover connections between the strands. The 10th strand is antiparallel with respect to the first nine strands. In addition, the enzyme has two antiparallel beta-sheets, comprised of two strands and three strands each, 11 alpha-helices and two short 3/10-helices. Further, it has been suggested that the similarities in the GTP-binding domains of the synthetase and the p21ras protein are an example of convergent evolution of two distinct families of GTP-binding proteins. Structures of adenylosuccinate synthetase from Triticum aestivum and Arabidopsis thaliana when compared with the known structures from E. coli reveals that the overall fold is very similar to that of the E. coli protein.


Pssm-ID: 197875  Cd Length: 417  Bit Score: 138.38  E-value: 1.05e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676323112    1 IGPAYSSKATRNGIRVGELLgDFNLFSDKFKSIVATHVRLFPSIN----VDVEAELARYRDYVDKVRPYVKDTICFLHTA 76
Cdd:smart00788 127 IGPAYEDKVARRGIRVGDLF-DEEVLREKLEELLDYKNFLLKKLYgaepVDVEEILEELLEYAERLRPYVTDVSELLNEA 205

                           90       100
                   ....*....|....*....|....*..
gi 1676323112   77 LRNGKTILVEGANAAMLDIDFGTYPYV 103
Cdd:smart00788 206 LKAGKKVLFEGAQGTLLDIDHGTYPYV 232
PurA COG0104
Adenylosuccinate synthase [Nucleotide transport and metabolism]; Adenylosuccinate synthase is ...
 1-103 2.81e-36

Adenylosuccinate synthase [Nucleotide transport and metabolism]; Adenylosuccinate synthase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439874  Cd Length: 423  Bit Score: 126.67  E-value: 2.81e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676323112   1 IGPAYSSKATRNGIRVGELLgDFNLFSDKFKSIVATHVRLFPSIN----VDVEAELARYRDYVDKVRPYVKDTICFLHTA 76
Cdd:COG0104   131 IGPAYEDKVARRGIRVGDLL-DPEVLREKLEELLEYKNFLLEKLYgaepLDFEELLEEYLEYAERLKPYVADTSELLNEA 209

                          90       100
                  ....*....|....*....|....*..
gi 1676323112  77 LRNGKTILVEGANAAMLDIDFGTYPYV 103
Cdd:COG0104   210 LKAGKKVLFEGAQGTLLDIDHGTYPYV 236
PRK01117 PRK01117
adenylosuccinate synthetase; Provisional
 1-103 4.92e-35

adenylosuccinate synthetase; Provisional


Pssm-ID: 234904  Cd Length: 430  Bit Score: 123.62  E-value: 4.92e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676323112   1 IGPAYSSKATRNGIRVGELLgDFNLFSDKFKSIVATH----VRLFPSINVDVEAELARYRDYVDKVRPYVKDTICFLHTA 76
Cdd:PRK01117  133 IGPAYEDKVARRGIRVGDLL-DPETFAEKLEENLEYKnfllTKYYGAEAVDFEEILDEYLEYAERLKPYVTDTSLLLNDA 211

                          90       100
                  ....*....|....*....|....*..
gi 1676323112  77 LRNGKTILVEGANAAMLDIDFGTYPYV 103
Cdd:PRK01117  212 LKAGKRVLFEGAQGTLLDIDHGTYPFV 238
purA TIGR00184
adenylosuccinate synthase; Alternate name IMP--aspartate ligase. [Purines, pyrimidines, ...
 1-103 1.13e-28

adenylosuccinate synthase; Alternate name IMP--aspartate ligase. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 272949  Cd Length: 425  Bit Score: 106.48  E-value: 1.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676323112   1 IGPAYSSKATRNGIRVGELLGDfNLFSDKFKSIVATHVRLF----PSINVDVEAELARYRDYVDKVRPYVKDTICFLHTA 76
Cdd:TIGR00184 129 IGPAYEDKVARSGLRVGDLLDD-EAFAEKAKNILEYLNEQLvkyyKDEGVDYEKKLDEYMKYAEELKPFVVDVSVELNEA 207

                          90       100
                  ....*....|....*....|....*..
gi 1676323112  77 LRNGKTILVEGANAAMLDIDFGTYPYV 103
Cdd:TIGR00184 208 LDEGEKVLFEGAQGTMLDIDYGTYPYV 234
AdSS cd03108
adenylosuccinate synthetase; Adenylosuccinate synthetase (AdSS) catalyzes the first step in ...
 1-103 2.54e-24

adenylosuccinate synthetase; Adenylosuccinate synthetase (AdSS) catalyzes the first step in the de novo biosynthesis of AMP. IMP and L-aspartate are conjugated in a two-step reaction accompanied by the hydrolysis of GTP to GDP in the presence of Mg2+. In the first step, the r-phosphate group of GTP is transferred to the 6-oxygen atom of IMP. An aspartate then displaces this 6-phosphate group to form the product adenylosuccinate. Because of its critical role in purine biosynthesis, AdSS is a target of antibiotics, herbicides and antitumor drugs.


Pssm-ID: 349762  Cd Length: 316  Bit Score: 93.33  E-value: 2.54e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676323112   1 IGPAYSSKATRNGIRVGEllgdfnlfsdkfksivathvrlfpsinvdveaelaryrdyvdkvrPYVKDTICFLHTALRNG 80
Cdd:cd03108   132 IGPAYADKAARTGIRVGD---------------------------------------------PYVVDTVELLNEALKAG 166

                          90       100
                  ....*....|....*....|...
gi 1676323112  81 KTILVEGANAAMLDIDFGTYPYV 103
Cdd:cd03108   167 KKVLFEGAQGTLLDIDFGTYPYV 189
PRK13788 PRK13788
adenylosuccinate synthetase; Provisional
 1-103 2.47e-18

adenylosuccinate synthetase; Provisional


Pssm-ID: 184326 [Multi-domain]  Cd Length: 404  Bit Score: 77.92  E-value: 2.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676323112   1 IGPAYSSKATRNGIRVGELLgDFNLFSDKFKSIVATHvrlfPSINVDVE--------AELARYRDYVdkvRPYVKDTICF 72
Cdd:PRK13788  125 IGPAYSDRARRVGIRFGDLL-DEAVLRERVERLLEAK----PNSTREAGwdtvekalADLAPMREIL---LPFIADTGSL 196

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1676323112  73 LHTALRNGKTILVEGANAAMLDIDFGTYPYV 103
Cdd:PRK13788  197 LREAIREGKRVLFEGAQATLLDLNYGTYPYV 227
PRK13787 PRK13787
adenylosuccinate synthetase; Provisional
 1-103 6.19e-17

adenylosuccinate synthetase; Provisional


Pssm-ID: 172324  Cd Length: 423  Bit Score: 74.22  E-value: 6.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676323112   1 IGPAYSSKATRNGIRVGELLGdfNLFSDKFKSIVATH----VRLFPSINVDVEAELARYRDYVDKVRPYVKDTICFLHTA 76
Cdd:PRK13787  134 IGICYADKMMRTGLRVGDLLD--KSYKRRLKHLVDEKnrelDKLYGMPPVSYNDINDGLKFFLSKVGKNIINTAYYLDTE 211

                          90       100
                  ....*....|....*....|....*..
gi 1676323112  77 LRNGKTILVEGANAAMLDIDFGTYPYV 103
Cdd:PRK13787  212 LKKGKRVLLEGAQGTGLDVDFGTYPYV 238
PRK13785 PRK13785
adenylosuccinate synthetase; Provisional
 1-103 4.71e-14

adenylosuccinate synthetase; Provisional


Pssm-ID: 237506  Cd Length: 454  Bit Score: 65.94  E-value: 4.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676323112   1 IGPAYSSKATRNGIRVGELLgDFNLFSDKFKSIVATHVRLFPSI----------NVDVEAELARYRDYVDKVRPYVKDTI 70
Cdd:PRK13785  131 IGPTYEDKAGRRGVRVGDLL-DPDVLRDRLEYVVPQKRALAEDVygldasetpeAFDVDALFEEYREYGERLAEEDMTVN 209

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1676323112  71 C--FLHTALRNGKTILVEGANAAMLDIDFGTYPYV 103
Cdd:PRK13785  210 AgdFLAERIDDGDNVMLEGAQGTSIDIDHGNYPYV 244
PRK13783 PRK13783
adenylosuccinate synthetase; Provisional
 1-103 2.53e-13

adenylosuccinate synthetase; Provisional


Pssm-ID: 237505  Cd Length: 404  Bit Score: 63.97  E-value: 2.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676323112   1 IGPAYSSKATRNGIRVGELlGDFNLFSDKFKSIVATHVRLFpSINVDVEAELARYRDYVDKVRPYVKDTIcFLHTALRNg 80
Cdd:PRK13783  131 IGPAYADKVMRVGVRLADL-FDEEKLREFLEKILSLYKKLY-GIEFDVEKMMEDLLTFYEKIKDLVVSPV-EIKRILEE- 206

                          90       100
                  ....*....|....*....|...
gi 1676323112  81 KTILVEGANAAMLDIDFGTYPYV 103
Cdd:PRK13783  207 KSVLFEGTQGVLLDLDVGTYPYV 229
PRK13784 PRK13784
adenylosuccinate synthetase; Provisional
 1-103 6.80e-12

adenylosuccinate synthetase; Provisional


Pssm-ID: 172322  Cd Length: 428  Bit Score: 60.03  E-value: 6.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676323112   1 IGPAYSSKATRNGIRVGELLgDFNLFSDKFKSIVATHVRLFPSINV----DVEAELARYRDYVDKVRPYVKDTICFLHTA 76
Cdd:PRK13784  133 IGPAYEDKVSRKGIKFKHLF-DKDLLRSRLAISLAEKETLFRDLYKveypTLEQEFDKLFALGQKLKQYAADTFSIIDQA 211

                          90       100
                  ....*....|....*....|....*..
gi 1676323112  77 LRNGKTILVEGANAAMLDIDFGTYPYV 103
Cdd:PRK13784  212 IAAGKNVVYEGAQGVLLDVDYGTYPFV 238
PRK13786 PRK13786
adenylosuccinate synthetase; Provisional
 1-103 2.58e-08

adenylosuccinate synthetase; Provisional


Pssm-ID: 184325  Cd Length: 424  Bit Score: 49.80  E-value: 2.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676323112   1 IGPAYSSKATRNGIRVGELLgDFNLFSDKFKSIVATHVRLF------PSINVDvEAELARYRDYVDKVRPYVKDTICFLH 74
Cdd:PRK13786  131 IGFAYIDKIARDEVRMSDLV-DKERLMRRLEELAPQKEKEIkelggdPSIVRD-EALIDKYLELGRQLAPYITDVSYEIN 208

                          90       100
                  ....*....|....*....|....*....
gi 1676323112  75 TALRNGKTILVEGANAAMLDIDFGTYPYV 103
Cdd:PRK13786  209 KALDEGKSVLAEGAQGTHLDVIHGTQKFV 237
PRK04293 PRK04293
adenylosuccinate synthetase; Provisional
 59-103 1.58e-05

adenylosuccinate synthetase; Provisional


Pssm-ID: 179812  Cd Length: 333  Bit Score: 41.79  E-value: 1.58e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1676323112  59 VDKVRPYVKDTICFLHTALRNGKTILVEGANAAMLDIDFGTYPYV 103
Cdd:PRK04293  146 VEELEKYLTDVPEEVNEALDRGENVLIEGTQGFGLSLYYGTYPYV 190
 
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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