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Conserved domains on  [gi|19924103|ref|NP_598328|]
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synapsin-2 isoform IIa [Homo sapiens]

Protein Classification

ATP-grasp domain-containing protein; acetate--CoA ligase family protein( domain architecture ID 10566052)

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; acetate--CoA ligase family protein similar to ADP-forming acetate--CoA ligase that catalyzes the formation of acetate and ATP from acetyl-CoA by using ADP and phosphate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Synapsin_C pfam02750
Synapsin, ATP binding domain; Ca dependent ATP binding in this ATP grasp fold. Function ...
214-416 7.77e-161

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


:

Pssm-ID: 308403  Cd Length: 203  Bit Score: 457.21  E-value: 7.77e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924103   214 NSLESIYNFCDKPWVFAQLVAIYKTLGGEKFPLIEQTYYPNHKEMLTLPTFPVVVKIGHAHSGMGKVKVENHYDFQDIAS 293
Cdd:pfam02750   1 NSLESIYNFCDKPWVFAQLIAIFHSLGGEKFPLIEQTFFPNHKEMLTAPNFPVVIKIGHAHAGMGKIKVENHHDFQDIAS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924103   294 VVALTQTYATAEPFIDSKYDIRVQKIGNNYKAYMRTSISGNWKTNTGSAMLEQIAMSDRYKLWVDTCSEMFGGLDICAVK 373
Cdd:pfam02750  81 VVALAKTYATAEAFIDSKYDIRIQKIGNNYKAYMRTSISGNWKANTGSAMLEQIAMSDRYKLWVDSCSEMFGGLDICAVK 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 19924103   374 AVHGKDGKDYIFEVMDCSMPLIGEHQVEDRQLITELVISKMNQ 416
Cdd:pfam02750 161 AVHGKDGKDYIFEVMDCSMPLIGEHQEEDKQLIADLVISKMNQ 203
Synapsin pfam02078
Synapsin, N-terminal domain; This family is structurally related to the PreATP-grasp domain.
114-212 2.76e-60

Synapsin, N-terminal domain; This family is structurally related to the PreATP-grasp domain.


:

Pssm-ID: 460438  Cd Length: 97  Bit Score: 194.79  E-value: 2.76e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924103   114 KVLLVVDEPHADWAKCFRGKKVLGDYDIKVEQAEFSELNLVAHADGTYAVDMQVLRNGTKVVRSFRPDFVLIRQHAFgmA 193
Cdd:pfam02078   1 KTLLVIDDQHTDWSKYFRGKKIHGDYDIRVEQAEFSELNLTAYADGGCVVDMQVIRNGTKVVRSFRPDFVLVRQHAR--D 78
                          90
                  ....*....|....*....
gi 19924103   194 ENEDFRHLIIGMQYAGLPS 212
Cdd:pfam02078  79 AGEDYRNLLLGLQYGGVPS 97
Synapsin_N super family cl11206
Synapsin N-terminal; This highly conserved domain of synapsin proteins has a serine at ...
2-30 7.01e-13

Synapsin N-terminal; This highly conserved domain of synapsin proteins has a serine at position 9 or 10 which is a phosphorylation site. The domain appears to be the part of the molecule that binds to calmodulin.


The actual alignment was detected with superfamily member pfam10581:

Pssm-ID: 463155  Cd Length: 32  Bit Score: 62.89  E-value: 7.01e-13
                          10        20
                  ....*....|....*....|....*....
gi 19924103     2 MNFLRRRLSDSSFIANLPNGYMTDLQRPE 30
Cdd:pfam10581   1 MNYLRRRLSDSNFMSNLPNGYMSDLQRPD 29
 
Name Accession Description Interval E-value
Synapsin_C pfam02750
Synapsin, ATP binding domain; Ca dependent ATP binding in this ATP grasp fold. Function ...
214-416 7.77e-161

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


Pssm-ID: 308403  Cd Length: 203  Bit Score: 457.21  E-value: 7.77e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924103   214 NSLESIYNFCDKPWVFAQLVAIYKTLGGEKFPLIEQTYYPNHKEMLTLPTFPVVVKIGHAHSGMGKVKVENHYDFQDIAS 293
Cdd:pfam02750   1 NSLESIYNFCDKPWVFAQLIAIFHSLGGEKFPLIEQTFFPNHKEMLTAPNFPVVIKIGHAHAGMGKIKVENHHDFQDIAS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924103   294 VVALTQTYATAEPFIDSKYDIRVQKIGNNYKAYMRTSISGNWKTNTGSAMLEQIAMSDRYKLWVDTCSEMFGGLDICAVK 373
Cdd:pfam02750  81 VVALAKTYATAEAFIDSKYDIRIQKIGNNYKAYMRTSISGNWKANTGSAMLEQIAMSDRYKLWVDSCSEMFGGLDICAVK 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 19924103   374 AVHGKDGKDYIFEVMDCSMPLIGEHQVEDRQLITELVISKMNQ 416
Cdd:pfam02750 161 AVHGKDGKDYIFEVMDCSMPLIGEHQEEDKQLIADLVISKMNQ 203
Synapsin pfam02078
Synapsin, N-terminal domain; This family is structurally related to the PreATP-grasp domain.
114-212 2.76e-60

Synapsin, N-terminal domain; This family is structurally related to the PreATP-grasp domain.


Pssm-ID: 460438  Cd Length: 97  Bit Score: 194.79  E-value: 2.76e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924103   114 KVLLVVDEPHADWAKCFRGKKVLGDYDIKVEQAEFSELNLVAHADGTYAVDMQVLRNGTKVVRSFRPDFVLIRQHAFgmA 193
Cdd:pfam02078   1 KTLLVIDDQHTDWSKYFRGKKIHGDYDIRVEQAEFSELNLTAYADGGCVVDMQVIRNGTKVVRSFRPDFVLVRQHAR--D 78
                          90
                  ....*....|....*....
gi 19924103   194 ENEDFRHLIIGMQYAGLPS 212
Cdd:pfam02078  79 AGEDYRNLLLGLQYGGVPS 97
Synapsin_N pfam10581
Synapsin N-terminal; This highly conserved domain of synapsin proteins has a serine at ...
2-30 7.01e-13

Synapsin N-terminal; This highly conserved domain of synapsin proteins has a serine at position 9 or 10 which is a phosphorylation site. The domain appears to be the part of the molecule that binds to calmodulin.


Pssm-ID: 463155  Cd Length: 32  Bit Score: 62.89  E-value: 7.01e-13
                          10        20
                  ....*....|....*....|....*....
gi 19924103     2 MNFLRRRLSDSSFIANLPNGYMTDLQRPE 30
Cdd:pfam10581   1 MNYLRRRLSDSNFMSNLPNGYMSDLQRPD 29
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
114-387 1.18e-08

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: 56.49  E-value: 1.18e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924103 114 KVLLVVDEPHADWAKCFRgkKVLGDYDIKVEQAEFSELnlvahadgtyAVDMQVLRNGTKVVRSFRPDFVLIRQ----HA 189
Cdd:COG0189   3 KIAILTDPPDKDSTKALI--EAAQRRGHEVEVIDPDDL----------TLDLGRAPELYRGEDLSEFDAVLPRIdppfYG 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924103 190 FGMAENedfrhliigMQYAGLPSINSLESIYNFCDKPWV--FAQLVAIY--KTLGGEKFPLIEQTyypnHKEMltlpTFP 265
Cdd:COG0189  71 LALLRQ---------LEAAGVPVVNDPEAIRRARDKLFTlqLLARAGIPvpPTLVTRDPDDLRAF----LEEL----GGP 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924103 266 VVVKIGHAHSGMGKVKVENHYDFQD-IASVVALTQTYATAEPFIDSK--YDIRVQKIGNNY-KAYMRTSISGNWKTNT-- 339
Cdd:COG0189 134 VVLKPLDGSGGRGVFLVEDEDALESiLEALTELGSEPVLVQEFIPEEdgRDIRVLVVGGEPvAAIRRIPAEGEFRTNLar 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 19924103 340 -GSAmlEQIAMSDRYKLWVDTCSEMFgGLDICAVKAVHGKDGKdYIFEV 387
Cdd:COG0189 214 gGRA--EPVELTDEERELALRAAPAL-GLDFAGVDLIEDDDGP-LVLEV 258
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
114-380 3.19e-05

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: 45.80  E-value: 3.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924103   114 KVLLVVDEPHADwakCFRGKKVLGDYDIKVEQAEFSELNLVAHADGTYAVDMQVLRNgtKVVRSFRPDFVLirqhafgma 193
Cdd:TIGR00768   1 KIAILYDRIRLD---EKMLKEAAEELGIDYKVVTPPAINLTFNEGPRALAELDVVIV--RIVSMFRGLAVL--------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924103   194 enedfRHLiigmQYAGLPSINSLESIYNFCDKPWVFAQLVaiyktlgGEKFPLIEQTYYPNHKEMLTLPT---FPVVVKI 270
Cdd:TIGR00768  67 -----RYL----ESLGVPVINSSDAILNAGDKFLSHQLLA-------KAGIPLPRTGLAGSPEEALKLIEeigFPVVLKP 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924103   271 GHAHSGMGKVKVEnhyDFQDIASVV-ALTQTYATAEPFIDSKY-------DIRVQKIGNNYKAYMRTSISGNWKTNT--- 339
Cdd:TIGR00768 131 VFGSWGRGVSLAR---DRQAAESLLeHFEQLNGPQNLFLVQEYikkpggrDIRVFVVGDEVVAAIYRITSGHWRSNLarg 207
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 19924103   340 GSAMLEQIAMSDRyKLWVDTCSEMfgGLDICAVKAVHGKDG 380
Cdd:TIGR00768 208 GKAEPCSLTEEIE-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 ...
214-416 7.77e-161

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


Pssm-ID: 308403  Cd Length: 203  Bit Score: 457.21  E-value: 7.77e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924103   214 NSLESIYNFCDKPWVFAQLVAIYKTLGGEKFPLIEQTYYPNHKEMLTLPTFPVVVKIGHAHSGMGKVKVENHYDFQDIAS 293
Cdd:pfam02750   1 NSLESIYNFCDKPWVFAQLIAIFHSLGGEKFPLIEQTFFPNHKEMLTAPNFPVVIKIGHAHAGMGKIKVENHHDFQDIAS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924103   294 VVALTQTYATAEPFIDSKYDIRVQKIGNNYKAYMRTSISGNWKTNTGSAMLEQIAMSDRYKLWVDTCSEMFGGLDICAVK 373
Cdd:pfam02750  81 VVALAKTYATAEAFIDSKYDIRIQKIGNNYKAYMRTSISGNWKANTGSAMLEQIAMSDRYKLWVDSCSEMFGGLDICAVK 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 19924103   374 AVHGKDGKDYIFEVMDCSMPLIGEHQVEDRQLITELVISKMNQ 416
Cdd:pfam02750 161 AVHGKDGKDYIFEVMDCSMPLIGEHQEEDKQLIADLVISKMNQ 203
Synapsin pfam02078
Synapsin, N-terminal domain; This family is structurally related to the PreATP-grasp domain.
114-212 2.76e-60

Synapsin, N-terminal domain; This family is structurally related to the PreATP-grasp domain.


Pssm-ID: 460438  Cd Length: 97  Bit Score: 194.79  E-value: 2.76e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924103   114 KVLLVVDEPHADWAKCFRGKKVLGDYDIKVEQAEFSELNLVAHADGTYAVDMQVLRNGTKVVRSFRPDFVLIRQHAFgmA 193
Cdd:pfam02078   1 KTLLVIDDQHTDWSKYFRGKKIHGDYDIRVEQAEFSELNLTAYADGGCVVDMQVIRNGTKVVRSFRPDFVLVRQHAR--D 78
                          90
                  ....*....|....*....
gi 19924103   194 ENEDFRHLIIGMQYAGLPS 212
Cdd:pfam02078  79 AGEDYRNLLLGLQYGGVPS 97
Synapsin_N pfam10581
Synapsin N-terminal; This highly conserved domain of synapsin proteins has a serine at ...
2-30 7.01e-13

Synapsin N-terminal; This highly conserved domain of synapsin proteins has a serine at position 9 or 10 which is a phosphorylation site. The domain appears to be the part of the molecule that binds to calmodulin.


Pssm-ID: 463155  Cd Length: 32  Bit Score: 62.89  E-value: 7.01e-13
                          10        20
                  ....*....|....*....|....*....
gi 19924103     2 MNFLRRRLSDSSFIANLPNGYMTDLQRPE 30
Cdd:pfam10581   1 MNYLRRRLSDSNFMSNLPNGYMSDLQRPD 29
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
114-387 1.18e-08

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: 56.49  E-value: 1.18e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924103 114 KVLLVVDEPHADWAKCFRgkKVLGDYDIKVEQAEFSELnlvahadgtyAVDMQVLRNGTKVVRSFRPDFVLIRQ----HA 189
Cdd:COG0189   3 KIAILTDPPDKDSTKALI--EAAQRRGHEVEVIDPDDL----------TLDLGRAPELYRGEDLSEFDAVLPRIdppfYG 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924103 190 FGMAENedfrhliigMQYAGLPSINSLESIYNFCDKPWV--FAQLVAIY--KTLGGEKFPLIEQTyypnHKEMltlpTFP 265
Cdd:COG0189  71 LALLRQ---------LEAAGVPVVNDPEAIRRARDKLFTlqLLARAGIPvpPTLVTRDPDDLRAF----LEEL----GGP 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924103 266 VVVKIGHAHSGMGKVKVENHYDFQD-IASVVALTQTYATAEPFIDSK--YDIRVQKIGNNY-KAYMRTSISGNWKTNT-- 339
Cdd:COG0189 134 VVLKPLDGSGGRGVFLVEDEDALESiLEALTELGSEPVLVQEFIPEEdgRDIRVLVVGGEPvAAIRRIPAEGEFRTNLar 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 19924103 340 -GSAmlEQIAMSDRYKLWVDTCSEMFgGLDICAVKAVHGKDGKdYIFEV 387
Cdd:COG0189 214 gGRA--EPVELTDEERELALRAAPAL-GLDFAGVDLIEDDDGP-LVLEV 258
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
114-380 3.19e-05

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: 45.80  E-value: 3.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924103   114 KVLLVVDEPHADwakCFRGKKVLGDYDIKVEQAEFSELNLVAHADGTYAVDMQVLRNgtKVVRSFRPDFVLirqhafgma 193
Cdd:TIGR00768   1 KIAILYDRIRLD---EKMLKEAAEELGIDYKVVTPPAINLTFNEGPRALAELDVVIV--RIVSMFRGLAVL--------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924103   194 enedfRHLiigmQYAGLPSINSLESIYNFCDKPWVFAQLVaiyktlgGEKFPLIEQTYYPNHKEMLTLPT---FPVVVKI 270
Cdd:TIGR00768  67 -----RYL----ESLGVPVINSSDAILNAGDKFLSHQLLA-------KAGIPLPRTGLAGSPEEALKLIEeigFPVVLKP 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924103   271 GHAHSGMGKVKVEnhyDFQDIASVV-ALTQTYATAEPFIDSKY-------DIRVQKIGNNYKAYMRTSISGNWKTNT--- 339
Cdd:TIGR00768 131 VFGSWGRGVSLAR---DRQAAESLLeHFEQLNGPQNLFLVQEYikkpggrDIRVFVVGDEVVAAIYRITSGHWRSNLarg 207
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 19924103   340 GSAMLEQIAMSDRyKLWVDTCSEMfgGLDICAVKAVHGKDG 380
Cdd:TIGR00768 208 GKAEPCSLTEEIE-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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