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Conserved domains on  [gi|578806514|ref|XP_006713376|]
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synapsin-2 isoform X4 [Homo sapiens]

Protein Classification

ATP-grasp domain-containing protein( domain architecture ID 106900)

ATP-grasp domain-containing protein may be related to carbamoyl phosphate synthetase and predicted to be involved in the biosynthesis of a ribonucleoside involved in stress response

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CPSase_L_D2 super family cl17255
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 1-159 1.46e-125

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.


The actual alignment was detected with superfamily member pfam02750:

Pssm-ID: 473076  Cd Length: 203  Bit Score: 357.83  E-value: 1.46e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806514    1 MLTLPTFPVVVKIGHAHSGMGKVKVENHYDFQDIASVVALTQTYATAEPFIDSKYDIRVQKIGNNYKAYMRTSISGNWKT 80
Cdd:pfam02750  45 MLTAPNFPVVIKIGHAHAGMGKIKVENHHDFQDIASVVALAKTYATAEAFIDSKYDIRIQKIGNNYKAYMRTSISGNWKA 124

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578806514   81 NTGSAMLEQIAMSDRYKLWVDTCSEMFGGLDICAVKAVHGKDGKDYIFEVMDCSMPLIGEHQVEDRQLITELVISKMNQ 159
Cdd:pfam02750 125 NTGSAMLEQIAMSDRYKLWVDSCSEMFGGLDICAVKAVHGKDGKDYIFEVMDCSMPLIGEHQEEDKQLIADLVISKMNQ 203
 
Name Accession Description Interval E-value
Synapsin_C pfam02750
Synapsin, ATP binding domain; Ca dependent ATP binding in this ATP grasp fold. Function ...
 1-159 1.46e-125

Synapsin, ATP binding domain; Ca dependent ATP binding in this ATP grasp fold. Function unknown.


Pssm-ID: 308403  Cd Length: 203  Bit Score: 357.83  E-value: 1.46e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806514    1 MLTLPTFPVVVKIGHAHSGMGKVKVENHYDFQDIASVVALTQTYATAEPFIDSKYDIRVQKIGNNYKAYMRTSISGNWKT 80
Cdd:pfam02750  45 MLTAPNFPVVIKIGHAHAGMGKIKVENHHDFQDIASVVALAKTYATAEAFIDSKYDIRIQKIGNNYKAYMRTSISGNWKA 124

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578806514   81 NTGSAMLEQIAMSDRYKLWVDTCSEMFGGLDICAVKAVHGKDGKDYIFEVMDCSMPLIGEHQVEDRQLITELVISKMNQ 159
Cdd:pfam02750 125 NTGSAMLEQIAMSDRYKLWVDSCSEMFGGLDICAVKAVHGKDGKDYIFEVMDCSMPLIGEHQEEDKQLIADLVISKMNQ 203
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 7-130 1.15e-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: 46.09  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806514   7 FPVVVKIGHAHSGMGKVKVENHYDFQD-IASVVALTQTYATAEPFIDSK--YDIRVQKIGNNY-KAYMRTSISGNWKTNT 82
Cdd:COG0189  132 GPVVLKPLDGSGGRGVFLVEDEDALESiLEALTELGSEPVLVQEFIPEEdgRDIRVLVVGGEPvAAIRRIPAEGEFRTNL 211

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578806514  83 ---GSAmlEQIAMSDRYKLWVDTCSEMFgGLDICAVKAVHGKDGKdYIFEV 130
Cdd:COG0189  212 argGRA--EPVELTDEERELALRAAPAL-GLDFAGVDLIEDDDGP-LVLEV 258
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
 7-123 2.36e-03

alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).


Pssm-ID: 273261 [Multi-domain]  Cd Length: 276  Bit Score: 38.87  E-value: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806514    7 FPVVVKIGHAHSGMGKVKVEnhyDFQDIASVV-ALTQTYATAEPFIDSKY-------DIRVQKIGNNYKAYMRTSISGNW 78
Cdd:TIGR00768 124 FPVVLKPVFGSWGRGVSLAR---DRQAAESLLeHFEQLNGPQNLFLVQEYikkpggrDIRVFVVGDEVVAAIYRITSGHW 200

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 578806514   79 KTNT---GSAMLEQIAMSDRyKLWVDTCSEMfgGLDICAVKAVHGKDG 123
Cdd:TIGR00768 201 RSNLargGKAEPCSLTEEIE-ELAIKAAKAL--GLDVAGVDLLESEDG 245
 
Name Accession Description Interval E-value
Synapsin_C pfam02750
Synapsin, ATP binding domain; Ca dependent ATP binding in this ATP grasp fold. Function ...
 1-159 1.46e-125

Synapsin, ATP binding domain; Ca dependent ATP binding in this ATP grasp fold. Function unknown.


Pssm-ID: 308403  Cd Length: 203  Bit Score: 357.83  E-value: 1.46e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806514    1 MLTLPTFPVVVKIGHAHSGMGKVKVENHYDFQDIASVVALTQTYATAEPFIDSKYDIRVQKIGNNYKAYMRTSISGNWKT 80
Cdd:pfam02750  45 MLTAPNFPVVIKIGHAHAGMGKIKVENHHDFQDIASVVALAKTYATAEAFIDSKYDIRIQKIGNNYKAYMRTSISGNWKA 124

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578806514   81 NTGSAMLEQIAMSDRYKLWVDTCSEMFGGLDICAVKAVHGKDGKDYIFEVMDCSMPLIGEHQVEDRQLITELVISKMNQ 159
Cdd:pfam02750 125 NTGSAMLEQIAMSDRYKLWVDSCSEMFGGLDICAVKAVHGKDGKDYIFEVMDCSMPLIGEHQEEDKQLIADLVISKMNQ 203
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 7-130 1.15e-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: 46.09  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806514   7 FPVVVKIGHAHSGMGKVKVENHYDFQD-IASVVALTQTYATAEPFIDSK--YDIRVQKIGNNY-KAYMRTSISGNWKTNT 82
Cdd:COG0189  132 GPVVLKPLDGSGGRGVFLVEDEDALESiLEALTELGSEPVLVQEFIPEEdgRDIRVLVVGGEPvAAIRRIPAEGEFRTNL 211

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578806514  83 ---GSAmlEQIAMSDRYKLWVDTCSEMFgGLDICAVKAVHGKDGKdYIFEV 130
Cdd:COG0189  212 argGRA--EPVELTDEERELALRAAPAL-GLDFAGVDLIEDDDGP-LVLEV 258
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
 7-123 2.36e-03

alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).


Pssm-ID: 273261 [Multi-domain]  Cd Length: 276  Bit Score: 38.87  E-value: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806514    7 FPVVVKIGHAHSGMGKVKVEnhyDFQDIASVV-ALTQTYATAEPFIDSKY-------DIRVQKIGNNYKAYMRTSISGNW 78
Cdd:TIGR00768 124 FPVVLKPVFGSWGRGVSLAR---DRQAAESLLeHFEQLNGPQNLFLVQEYikkpggrDIRVFVVGDEVVAAIYRITSGHW 200

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 578806514   79 KTNT---GSAMLEQIAMSDRyKLWVDTCSEMfgGLDICAVKAVHGKDG 123
Cdd:TIGR00768 201 RSNLargGKAEPCSLTEEIE-ELAIKAAKAL--GLDVAGVDLLESEDG 245
 
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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