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Conserved domains on  [gi|119580434|gb|EAW60030|]
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synapsin III, isoform CRA_b [Homo sapiens]

Protein Classification

ATP-grasp domain-containing protein; acetate--CoA ligase family protein( domain architecture ID 10301346)

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 pfam02078
Synapsin, N-terminal domain; This family is structurally related to the PreATP-grasp domain.
 92-191 5.95e-62

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


:

Pssm-ID: 460438  Cd Length: 97  Bit Score: 189.01  E-value: 5.95e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580434   92 RILLVIDDAHTDWSKYFHGKKVNGEIEIRVEQAEFSELNLAAYVTGGCMVDMQVVRNGTKVVsRSFKPDFILVRQHAYsm 171
Cdd:pfam02078   1 KTLLVIDDQHTDWSKYFRGKKIHGDYDIRVEQAEFSELNLTAYADGGCVVDMQVIRNGTKVV-RSFRPDFVLVRQHAR-- 77

                          90       100
                  ....*....|....*....|
gi 119580434  172 ALGEDYRSLVIGLQYGGLPA 191
Cdd:pfam02078  78 DAGEDYRNLLLGLQYGGVPS 97
CPSase_L_D2 super family cl17255
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 193-243 2.43e-30

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: 111.69  E-value: 2.43e-30
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 119580434  193 NSLYSVYNFCSKPWVFSQLIKIFHSLGPEKFPLVEQTFFPNHKPMVS-PSLP 243
Cdd:pfam02750   1 NSLESIYNFCDKPWVFAQLIAIFHSLGGEKFPLIEQTFFPNHKEMLTaPNFP 52
Synapsin_N super family cl11206
Synapsin N-terminal; This highly conserved domain of synapsin proteins has a serine at ...
 1-29 4.68e-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: 61.35  E-value: 4.68e-13
                          10        20
                  ....*....|....*....|....*....
gi 119580434    1 MNFLRRRLSDSSFMANLPNGYMTDLQRPD 29
Cdd:pfam10581   1 MNYLRRRLSDSNFMSNLPNGYMSDLQRPD 29
 
Name Accession Description Interval E-value
Synapsin pfam02078
Synapsin, N-terminal domain; This family is structurally related to the PreATP-grasp domain.
 92-191 5.95e-62

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


Pssm-ID: 460438  Cd Length: 97  Bit Score: 189.01  E-value: 5.95e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580434   92 RILLVIDDAHTDWSKYFHGKKVNGEIEIRVEQAEFSELNLAAYVTGGCMVDMQVVRNGTKVVsRSFKPDFILVRQHAYsm 171
Cdd:pfam02078   1 KTLLVIDDQHTDWSKYFRGKKIHGDYDIRVEQAEFSELNLTAYADGGCVVDMQVIRNGTKVV-RSFRPDFVLVRQHAR-- 77

                          90       100
                  ....*....|....*....|
gi 119580434  172 ALGEDYRSLVIGLQYGGLPA 191
Cdd:pfam02078  78 DAGEDYRNLLLGLQYGGVPS 97
Synapsin_C pfam02750
Synapsin, ATP binding domain; Ca dependent ATP binding in this ATP grasp fold. Function ...
 193-243 2.43e-30

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


Pssm-ID: 308403  Cd Length: 203  Bit Score: 111.69  E-value: 2.43e-30
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 119580434  193 NSLYSVYNFCSKPWVFSQLIKIFHSLGPEKFPLVEQTFFPNHKPMVS-PSLP 243
Cdd:pfam02750   1 NSLESIYNFCDKPWVFAQLIAIFHSLGGEKFPLIEQTFFPNHKEMLTaPNFP 52
Synapsin_N pfam10581
Synapsin N-terminal; This highly conserved domain of synapsin proteins has a serine at ...
 1-29 4.68e-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: 61.35  E-value: 4.68e-13
                          10        20
                  ....*....|....*....|....*....
gi 119580434    1 MNFLRRRLSDSSFMANLPNGYMTDLQRPD 29
Cdd:pfam10581   1 MNYLRRRLSDSNFMSNLPNGYMSDLQRPD 29
 
Name Accession Description Interval E-value
Synapsin pfam02078
Synapsin, N-terminal domain; This family is structurally related to the PreATP-grasp domain.
 92-191 5.95e-62

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


Pssm-ID: 460438  Cd Length: 97  Bit Score: 189.01  E-value: 5.95e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580434   92 RILLVIDDAHTDWSKYFHGKKVNGEIEIRVEQAEFSELNLAAYVTGGCMVDMQVVRNGTKVVsRSFKPDFILVRQHAYsm 171
Cdd:pfam02078   1 KTLLVIDDQHTDWSKYFRGKKIHGDYDIRVEQAEFSELNLTAYADGGCVVDMQVIRNGTKVV-RSFRPDFVLVRQHAR-- 77

                          90       100
                  ....*....|....*....|
gi 119580434  172 ALGEDYRSLVIGLQYGGLPA 191
Cdd:pfam02078  78 DAGEDYRNLLLGLQYGGVPS 97
Synapsin_C pfam02750
Synapsin, ATP binding domain; Ca dependent ATP binding in this ATP grasp fold. Function ...
 193-243 2.43e-30

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


Pssm-ID: 308403  Cd Length: 203  Bit Score: 111.69  E-value: 2.43e-30
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 119580434  193 NSLYSVYNFCSKPWVFSQLIKIFHSLGPEKFPLVEQTFFPNHKPMVS-PSLP 243
Cdd:pfam02750   1 NSLESIYNFCDKPWVFAQLIAIFHSLGGEKFPLIEQTFFPNHKEMLTaPNFP 52
Synapsin_N pfam10581
Synapsin N-terminal; This highly conserved domain of synapsin proteins has a serine at ...
 1-29 4.68e-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: 61.35  E-value: 4.68e-13
                          10        20
                  ....*....|....*....|....*....
gi 119580434    1 MNFLRRRLSDSSFMANLPNGYMTDLQRPD 29
Cdd:pfam10581   1 MNYLRRRLSDSNFMSNLPNGYMSDLQRPD 29
 
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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