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Conserved domains on  [gi|1060099385|ref|NP_001317390|]
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atlastin-2 isoform 6 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GBP super family cl46410
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
 1-170 4.68e-88

Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


The actual alignment was detected with superfamily member pfam02263:

Pssm-ID: 460516  Cd Length: 260  Bit Score: 267.70  E-value: 4.68e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099385   1 MDTQGAFD-SQSTIKDCATVFALSTMTSSVQVYNLSQNIQEDDLQHLQLFTE--------YGRLAMEEIYQKPFQTLMFL 71
Cdd:pfam02263  79 LDTEGLGDvEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTEltelssprYGRVADSADFVSFFPDFVWT 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099385  72 IRDWSYPYEHSYGLEGGKQFLEKRLQVKQNQHEELQN---VRKHIHNCFSNLGCFLLPHPGLKVATNPSFDG-RLKDIDE 147
Cdd:pfam02263 159 VRDFSLPLEADGGPITGDEYLENRLKLSQGQHEELQNfnlPRLCIRSFFPKRKCFLFDRPGLKKALNPQFEGlREDELDP 238

                         170       180
                  ....*....|....*....|...
gi 1060099385 148 DFKRELRNLVPLLLApENLVEKE 170
Cdd:pfam02263 239 EFQQQLREFCSYILS-HSLVKTL 260
 
Name Accession Description Interval E-value
GBP pfam02263
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
 1-170 4.68e-88

Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460516  Cd Length: 260  Bit Score: 267.70  E-value: 4.68e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099385   1 MDTQGAFD-SQSTIKDCATVFALSTMTSSVQVYNLSQNIQEDDLQHLQLFTE--------YGRLAMEEIYQKPFQTLMFL 71
Cdd:pfam02263  79 LDTEGLGDvEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTEltelssprYGRVADSADFVSFFPDFVWT 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099385  72 IRDWSYPYEHSYGLEGGKQFLEKRLQVKQNQHEELQN---VRKHIHNCFSNLGCFLLPHPGLKVATNPSFDG-RLKDIDE 147
Cdd:pfam02263 159 VRDFSLPLEADGGPITGDEYLENRLKLSQGQHEELQNfnlPRLCIRSFFPKRKCFLFDRPGLKKALNPQFEGlREDELDP 238

                         170       180
                  ....*....|....*....|...
gi 1060099385 148 DFKRELRNLVPLLLApENLVEKE 170
Cdd:pfam02263 239 EFQQQLREFCSYILS-HSLVKTL 260
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
 1-163 4.46e-45

Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), N-terminal domain. Guanylate-binding proteins (GBPs) define a group of proteins that are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. Furthermore, two unique regions around the base and the phosphate-binding areas, the guanine and the phosphate caps, respectively, give the nucleotide-binding site a unique appearance not found in the canonical GTP-binding proteins. The phosphate cap, which constitutes the region analogous to switch I, completely shields the phosphate-binding site from solvent such that a potential GTPase-activating protein (GAP) cannot approach.


Pssm-ID: 206650  Cd Length: 224  Bit Score: 155.56  E-value: 4.46e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099385   1 MDTQGAFDSQSTI-KDCATVFALSTMTSSVQVYNLSQNIQEDDLQHLQLFTE----YGRLAMEEIYQKPFQTLMFLIRDW 75
Cdd:cd01851    67 LDTEGTDGRERGEfENDARLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKtaleTLGLAGLHNFSKPKPLLLFVVRDF 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099385  76 SYPYEHSYGLEGgkqflekrlQVKQNQHEELQNVRKHIHNCFSNLGCFLLPHPGLKVATNPSfDGRLKDIDEDFKRELRN 155
Cdd:cd01851   147 TGPTPLEGLDVT---------EKSETLIEELNKIWSSIRKPFTPITCFVLPHPGLLHKLLQN-DGRLKDLPPEFRKALKA 216


                  ....*...
gi 1060099385 156 LVPLLLAP 163
Cdd:cd01851   217 LRQRFFSS 224
 
Name Accession Description Interval E-value
GBP pfam02263
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
 1-170 4.68e-88

Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460516  Cd Length: 260  Bit Score: 267.70  E-value: 4.68e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099385   1 MDTQGAFD-SQSTIKDCATVFALSTMTSSVQVYNLSQNIQEDDLQHLQLFTE--------YGRLAMEEIYQKPFQTLMFL 71
Cdd:pfam02263  79 LDTEGLGDvEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTEltelssprYGRVADSADFVSFFPDFVWT 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099385  72 IRDWSYPYEHSYGLEGGKQFLEKRLQVKQNQHEELQN---VRKHIHNCFSNLGCFLLPHPGLKVATNPSFDG-RLKDIDE 147
Cdd:pfam02263 159 VRDFSLPLEADGGPITGDEYLENRLKLSQGQHEELQNfnlPRLCIRSFFPKRKCFLFDRPGLKKALNPQFEGlREDELDP 238

                         170       180
                  ....*....|....*....|...
gi 1060099385 148 DFKRELRNLVPLLLApENLVEKE 170
Cdd:pfam02263 239 EFQQQLREFCSYILS-HSLVKTL 260
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
 1-163 4.46e-45

Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), N-terminal domain. Guanylate-binding proteins (GBPs) define a group of proteins that are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. Furthermore, two unique regions around the base and the phosphate-binding areas, the guanine and the phosphate caps, respectively, give the nucleotide-binding site a unique appearance not found in the canonical GTP-binding proteins. The phosphate cap, which constitutes the region analogous to switch I, completely shields the phosphate-binding site from solvent such that a potential GTPase-activating protein (GAP) cannot approach.


Pssm-ID: 206650  Cd Length: 224  Bit Score: 155.56  E-value: 4.46e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099385   1 MDTQGAFDSQSTI-KDCATVFALSTMTSSVQVYNLSQNIQEDDLQHLQLFTE----YGRLAMEEIYQKPFQTLMFLIRDW 75
Cdd:cd01851    67 LDTEGTDGRERGEfENDARLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKtaleTLGLAGLHNFSKPKPLLLFVVRDF 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099385  76 SYPYEHSYGLEGgkqflekrlQVKQNQHEELQNVRKHIHNCFSNLGCFLLPHPGLKVATNPSfDGRLKDIDEDFKRELRN 155
Cdd:cd01851   147 TGPTPLEGLDVT---------EKSETLIEELNKIWSSIRKPFTPITCFVLPHPGLLHKLLQN-DGRLKDLPPEFRKALKA 216


                  ....*...
gi 1060099385 156 LVPLLLAP 163
Cdd:cd01851   217 LRQRFFSS 224
 
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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