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Conserved domains on  [gi|74024917|ref|NP_853629|]
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atlastin-1 isoform b [Homo sapiens]

Protein Classification

atlastin( domain architecture ID 10491594)

membrane-anchored GTPase atlastin couples nucleotide hydrolysis to the catalysis of homotypic membrane fusion to form a branched endoplasmic reticulum network; functions in endoplasmic reticulum tubular network biogenesis; most closely related to the guanylate-binding protein (GBP)subfamily

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GBP pfam02263
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
43-314 3.50e-130

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: 380.18  E-value: 3.50e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74024917    43 DHSFELDETALNRIllseAVRDKEVVAVSVAGAFRKGKSFLMDFMLRymynqesvdwvgdynePLTGFSWRGGSERETTG 122
Cdd:pfam02263   1 DHQLELNEEALEIL----SAITQPVVVVAIAGLYRTGKSFLMNFLAG----------------KLTGFSLGGTVESETKG 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74024917   123 IQIWSEIflinKPDGKKVAVLLMDTQGTFD-SQSTLRDSATVFALSTMISSIQVYNLSQNVQEDDLQHLQLFTE------ 195
Cdd:pfam02263  61 IWMWCVP----HPNKPKHTLVLLDTEGLGDvEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTEltelss 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74024917   196 --YGRLAMEETFLKPFQSLIFLVRDWSFPYEFSYGADGGAKFLEKRLKVSGNQHEELQN---VRKHIHSCFTNISCFLLP 270
Cdd:pfam02263 137 prYGRVADSADFVSFFPDFVWTVRDFSLPLEADGGPITGDEYLENRLKLSQGQHEELQNfnlPRLCIRSFFPKRKCFLFD 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 74024917   271 HPGLKVATNPNFDG-KLKEIDDEFIKNLKILIPWLLSpESLDIKE 314
Cdd:pfam02263 217 RPGLKKALNPQFEGlREDELDPEFQQQLREFCSYILS-HSLVKTL 260
 
Name Accession Description Interval E-value
GBP pfam02263
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
43-314 3.50e-130

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: 380.18  E-value: 3.50e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74024917    43 DHSFELDETALNRIllseAVRDKEVVAVSVAGAFRKGKSFLMDFMLRymynqesvdwvgdynePLTGFSWRGGSERETTG 122
Cdd:pfam02263   1 DHQLELNEEALEIL----SAITQPVVVVAIAGLYRTGKSFLMNFLAG----------------KLTGFSLGGTVESETKG 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74024917   123 IQIWSEIflinKPDGKKVAVLLMDTQGTFD-SQSTLRDSATVFALSTMISSIQVYNLSQNVQEDDLQHLQLFTE------ 195
Cdd:pfam02263  61 IWMWCVP----HPNKPKHTLVLLDTEGLGDvEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTEltelss 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74024917   196 --YGRLAMEETFLKPFQSLIFLVRDWSFPYEFSYGADGGAKFLEKRLKVSGNQHEELQN---VRKHIHSCFTNISCFLLP 270
Cdd:pfam02263 137 prYGRVADSADFVSFFPDFVWTVRDFSLPLEADGGPITGDEYLENRLKLSQGQHEELQNfnlPRLCIRSFFPKRKCFLFD 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 74024917   271 HPGLKVATNPNFDG-KLKEIDDEFIKNLKILIPWLLSpESLDIKE 314
Cdd:pfam02263 217 RPGLKKALNPQFEGlREDELDPEFQQQLREFCSYILS-HSLVKTL 260
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
61-307 1.09e-73

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: 233.75  E-value: 1.09e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74024917  61 AVRDKEVVAVSVAGAFRKGKSFLMDFMLRYMynqesvdwvgdyneplTGFSWRGGSERETTGIQIWSEIFLINkpDGKKV 140
Cdd:cd01851   1 LDVGFPVVVVSVFGSQSSGKSFLLNHLFGTS----------------DGFDVMDTSQQTTKGIWMWSDPFKDT--DGKKH 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74024917 141 AVLLMDTQGTFDSQSTLR-DSATVFALSTMISSIQVYNLSQNVQEDDLQHLQLFTE----YGRLAMEETFLKPFQSLIFL 215
Cdd:cd01851  63 AVLLLDTEGTDGRERGEFeNDARLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKtaleTLGLAGLHNFSKPKPLLLFV 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74024917 216 VRDWSFPYEFSYGADGgakflekrlKVSGNQHEELQNVRKHIHSCFTNISCFLLPHPGLKVATNPNfDGKLKEIDDEFIK 295
Cdd:cd01851 143 VRDFTGPTPLEGLDVT---------EKSETLIEELNKIWSSIRKPFTPITCFVLPHPGLLHKLLQN-DGRLKDLPPEFRK 212
                       250
                ....*....|..
gi 74024917 296 NLKILIPWLLSP 307
Cdd:cd01851 213 ALKALRQRFFSS 224
 
Name Accession Description Interval E-value
GBP pfam02263
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
43-314 3.50e-130

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: 380.18  E-value: 3.50e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74024917    43 DHSFELDETALNRIllseAVRDKEVVAVSVAGAFRKGKSFLMDFMLRymynqesvdwvgdynePLTGFSWRGGSERETTG 122
Cdd:pfam02263   1 DHQLELNEEALEIL----SAITQPVVVVAIAGLYRTGKSFLMNFLAG----------------KLTGFSLGGTVESETKG 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74024917   123 IQIWSEIflinKPDGKKVAVLLMDTQGTFD-SQSTLRDSATVFALSTMISSIQVYNLSQNVQEDDLQHLQLFTE------ 195
Cdd:pfam02263  61 IWMWCVP----HPNKPKHTLVLLDTEGLGDvEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTEltelss 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74024917   196 --YGRLAMEETFLKPFQSLIFLVRDWSFPYEFSYGADGGAKFLEKRLKVSGNQHEELQN---VRKHIHSCFTNISCFLLP 270
Cdd:pfam02263 137 prYGRVADSADFVSFFPDFVWTVRDFSLPLEADGGPITGDEYLENRLKLSQGQHEELQNfnlPRLCIRSFFPKRKCFLFD 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 74024917   271 HPGLKVATNPNFDG-KLKEIDDEFIKNLKILIPWLLSpESLDIKE 314
Cdd:pfam02263 217 RPGLKKALNPQFEGlREDELDPEFQQQLREFCSYILS-HSLVKTL 260
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
61-307 1.09e-73

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: 233.75  E-value: 1.09e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74024917  61 AVRDKEVVAVSVAGAFRKGKSFLMDFMLRYMynqesvdwvgdyneplTGFSWRGGSERETTGIQIWSEIFLINkpDGKKV 140
Cdd:cd01851   1 LDVGFPVVVVSVFGSQSSGKSFLLNHLFGTS----------------DGFDVMDTSQQTTKGIWMWSDPFKDT--DGKKH 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74024917 141 AVLLMDTQGTFDSQSTLR-DSATVFALSTMISSIQVYNLSQNVQEDDLQHLQLFTE----YGRLAMEETFLKPFQSLIFL 215
Cdd:cd01851  63 AVLLLDTEGTDGRERGEFeNDARLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKtaleTLGLAGLHNFSKPKPLLLFV 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74024917 216 VRDWSFPYEFSYGADGgakflekrlKVSGNQHEELQNVRKHIHSCFTNISCFLLPHPGLKVATNPNfDGKLKEIDDEFIK 295
Cdd:cd01851 143 VRDFTGPTPLEGLDVT---------EKSETLIEELNKIWSSIRKPFTPITCFVLPHPGLLHKLLQN-DGRLKDLPPEFRK 212
                       250
                ....*....|..
gi 74024917 296 NLKILIPWLLSP 307
Cdd:cd01851 213 ALKALRQRFFSS 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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