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Conserved domains on  [gi|259089526|ref|NP_001158563.1|]
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Gamma-aminobutyric acid receptor-associated protein

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List of domain hits

Name Accession Description Interval E-value
GABARAP cd01611
Ubiquitin domain of GABA-receptor-associated protein; GABARAP (GABA-receptor-associated ...
5-116 3.38e-67

Ubiquitin domain of GABA-receptor-associated protein; GABARAP (GABA-receptor-associated protein) belongs ot a large family of proteins that mediate intracellular membrane trafficking and/or fusion. GABARAP binds not only to GABA, type A but also to tubulin, gephrin, and ULK1. Orthologues of GABARAP include Gate-16 (golgi-associated ATPase enhancer), LC3 (microtubule-associated protein light chain 3), and ATG8 (autophagy protein 8). ATG8 is a ubiquitin-like protein that is conjugated to the membrane phospholipid, phosphatidylethanolamine as part of a ubiquitin-like conjugation system essential for autophagosome-formation.


:

Pssm-ID: 176355  Cd Length: 112  Bit Score: 200.54  E-value: 3.38e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259089526   5 YKEEHPFEKRRSEGEKIRKKYPDRVPVIVEKAPKARIGDLDKKKYLVPSDLTVGQFYFLIRKRIHLRAEDALFFFVNNVI 84
Cdd:cd01611    1 FKERHPFEKRKAEVERIRAKYPDRIPVIVERYPKSDLPDLDKKKYLVPSDLTVGQFVYIIRKRIQLRPEKALFLFVNNSL 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 259089526  85 PPTSATMGLLYQEHHEEDFFLYIAYSDESVYG 116
Cdd:cd01611   81 PPTSATMSQLYEEHKDEDGFLYMTYSSEETFG 112
 
Name Accession Description Interval E-value
GABARAP cd01611
Ubiquitin domain of GABA-receptor-associated protein; GABARAP (GABA-receptor-associated ...
5-116 3.38e-67

Ubiquitin domain of GABA-receptor-associated protein; GABARAP (GABA-receptor-associated protein) belongs ot a large family of proteins that mediate intracellular membrane trafficking and/or fusion. GABARAP binds not only to GABA, type A but also to tubulin, gephrin, and ULK1. Orthologues of GABARAP include Gate-16 (golgi-associated ATPase enhancer), LC3 (microtubule-associated protein light chain 3), and ATG8 (autophagy protein 8). ATG8 is a ubiquitin-like protein that is conjugated to the membrane phospholipid, phosphatidylethanolamine as part of a ubiquitin-like conjugation system essential for autophagosome-formation.


Pssm-ID: 176355  Cd Length: 112  Bit Score: 200.54  E-value: 3.38e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259089526   5 YKEEHPFEKRRSEGEKIRKKYPDRVPVIVEKAPKARIGDLDKKKYLVPSDLTVGQFYFLIRKRIHLRAEDALFFFVNNVI 84
Cdd:cd01611    1 FKERHPFEKRKAEVERIRAKYPDRIPVIVERYPKSDLPDLDKKKYLVPSDLTVGQFVYIIRKRIQLRPEKALFLFVNNSL 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 259089526  85 PPTSATMGLLYQEHHEEDFFLYIAYSDESVYG 116
Cdd:cd01611   81 PPTSATMSQLYEEHKDEDGFLYMTYSSEETFG 112
Atg8 pfam02991
Autophagy protein Atg8 ubiquitin like; Light chain 3 is proposed to function primarily as a ...
13-116 1.98e-57

Autophagy protein Atg8 ubiquitin like; Light chain 3 is proposed to function primarily as a subunit of microtubule associated proteins 1A and 1B and that its expression may regulate microtubule binding activity. Autophagy is generally known as a process involved in the degradation of bulk cytoplasmic components that are non-specifically sequestered into an autophagosome, where they are sequestered into double-membrane vesicles and delivered to the degradative organelle, the lysosome/vacuole, for breakdown and eventual recycling of the resulting macromolecules. The yeast proteins are involved in the autophagosome, and Atg8 binds Atg19, via its N-terminus and the C-terminus of Atg19.


Pssm-ID: 111837  Cd Length: 104  Bit Score: 175.62  E-value: 1.98e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259089526   13 KRRSEGEKIRKKYPDRVPVIVEKAPKARIGDLDKKKYLVPSDLTVGQFYFLIRKRIHLRAEDALFFFVNNVIPPTSATMG 92
Cdd:pfam02991   1 KRQAESEKIREKYPDRIPVIIEKASGSDLPDIDKKKYLVPADLTVGQFIYIIRKRIQLRPEKAIFLFVNNTLPPTSATMS 80
                          90       100
                  ....*....|....*....|....
gi 259089526   93 LLYQEHHEEDFFLYIAYSDESVYG 116
Cdd:pfam02991  81 ALYEEEKDEDGFLYMVYSGENTFG 104
PTZ00380 PTZ00380
microtubule-associated protein (MAP); Provisional
5-116 1.39e-10

microtubule-associated protein (MAP); Provisional


Pssm-ID: 173572  Cd Length: 121  Bit Score: 53.97  E-value: 1.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259089526   5 YKEEHPFEKRRSEGEKIRKKYPDRVPVIVEKAPKARigdlDKKKYL-VPSDLTVGQFYFLIRKRIHLRAEDaLFFFVNNV 83
Cdd:PTZ00380   4 YHSSNPVEARRAECARLQAKYPGHVAVVVEAAEKAG----SKVHFLaLPRDATVAELEAAVRQALGTSAKK-VTLAIEGS 78
                         90       100       110
                 ....*....|....*....|....*....|...
gi 259089526  84 IPPTSATMGLLYQEHHEEDFFLYIAYSDESVYG 116
Cdd:PTZ00380  79 TPAVTATVGDIADACKRDDGFLYVSVRTEQAMG 111
 
Name Accession Description Interval E-value
GABARAP cd01611
Ubiquitin domain of GABA-receptor-associated protein; GABARAP (GABA-receptor-associated ...
5-116 3.38e-67

Ubiquitin domain of GABA-receptor-associated protein; GABARAP (GABA-receptor-associated protein) belongs ot a large family of proteins that mediate intracellular membrane trafficking and/or fusion. GABARAP binds not only to GABA, type A but also to tubulin, gephrin, and ULK1. Orthologues of GABARAP include Gate-16 (golgi-associated ATPase enhancer), LC3 (microtubule-associated protein light chain 3), and ATG8 (autophagy protein 8). ATG8 is a ubiquitin-like protein that is conjugated to the membrane phospholipid, phosphatidylethanolamine as part of a ubiquitin-like conjugation system essential for autophagosome-formation.


Pssm-ID: 176355  Cd Length: 112  Bit Score: 200.54  E-value: 3.38e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259089526   5 YKEEHPFEKRRSEGEKIRKKYPDRVPVIVEKAPKARIGDLDKKKYLVPSDLTVGQFYFLIRKRIHLRAEDALFFFVNNVI 84
Cdd:cd01611    1 FKERHPFEKRKAEVERIRAKYPDRIPVIVERYPKSDLPDLDKKKYLVPSDLTVGQFVYIIRKRIQLRPEKALFLFVNNSL 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 259089526  85 PPTSATMGLLYQEHHEEDFFLYIAYSDESVYG 116
Cdd:cd01611   81 PPTSATMSQLYEEHKDEDGFLYMTYSSEETFG 112
Atg8 pfam02991
Autophagy protein Atg8 ubiquitin like; Light chain 3 is proposed to function primarily as a ...
13-116 1.98e-57

Autophagy protein Atg8 ubiquitin like; Light chain 3 is proposed to function primarily as a subunit of microtubule associated proteins 1A and 1B and that its expression may regulate microtubule binding activity. Autophagy is generally known as a process involved in the degradation of bulk cytoplasmic components that are non-specifically sequestered into an autophagosome, where they are sequestered into double-membrane vesicles and delivered to the degradative organelle, the lysosome/vacuole, for breakdown and eventual recycling of the resulting macromolecules. The yeast proteins are involved in the autophagosome, and Atg8 binds Atg19, via its N-terminus and the C-terminus of Atg19.


Pssm-ID: 111837  Cd Length: 104  Bit Score: 175.62  E-value: 1.98e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259089526   13 KRRSEGEKIRKKYPDRVPVIVEKAPKARIGDLDKKKYLVPSDLTVGQFYFLIRKRIHLRAEDALFFFVNNVIPPTSATMG 92
Cdd:pfam02991   1 KRQAESEKIREKYPDRIPVIIEKASGSDLPDIDKKKYLVPADLTVGQFIYIIRKRIQLRPEKAIFLFVNNTLPPTSATMS 80
                          90       100
                  ....*....|....*....|....
gi 259089526   93 LLYQEHHEEDFFLYIAYSDESVYG 116
Cdd:pfam02991  81 ALYEEEKDEDGFLYMVYSGENTFG 104
PTZ00380 PTZ00380
microtubule-associated protein (MAP); Provisional
5-116 1.39e-10

microtubule-associated protein (MAP); Provisional


Pssm-ID: 173572  Cd Length: 121  Bit Score: 53.97  E-value: 1.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259089526   5 YKEEHPFEKRRSEGEKIRKKYPDRVPVIVEKAPKARigdlDKKKYL-VPSDLTVGQFYFLIRKRIHLRAEDaLFFFVNNV 83
Cdd:PTZ00380   4 YHSSNPVEARRAECARLQAKYPGHVAVVVEAAEKAG----SKVHFLaLPRDATVAELEAAVRQALGTSAKK-VTLAIEGS 78
                         90       100       110
                 ....*....|....*....|....*....|...
gi 259089526  84 IPPTSATMGLLYQEHHEEDFFLYIAYSDESVYG 116
Cdd:PTZ00380  79 TPAVTATVGDIADACKRDDGFLYVSVRTEQAMG 111
APG12 pfam04110
Ubiquitin-like autophagy protein Apg12; In yeast, 15 Apg proteins coordinate the formation of ...
37-116 1.08e-05

Ubiquitin-like autophagy protein Apg12; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. The Apg12 system is one of the ubiquitin-like protein conjugation systems conserved in eukaryotes. It was first discovered in yeast during systematic analyses of the apg mutants defective in autophagy. Covalent attachment of Apg12-Apg5 is essential for autophagy.


Pssm-ID: 252381  Cd Length: 87  Bit Score: 39.70  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259089526   37 PKARIGDLDKKKYLVPSDLTVGQFYFLIRKRIHLRAEDALFFFVNNVIPPT-SATMGLLYqEHHEEDFFLYIAYSDESVY 115
Cdd:pfam04110   8 AIGDAPILKKSKFKVNPSQTFASVILFLKKFLKLQASDSLFLYVNNSFAPSpDQIVGNLY-ECFGTDGKLVLNYCISVAW 86

                  .
gi 259089526  116 G 116
Cdd:pfam04110  87 G 87
APG12_C cd01612
Ubiquitin-like domain of APG12; APG12_C The carboxy-terminal ubiquitin-like domain of APG12. ...
31-95 1.75e-04

Ubiquitin-like domain of APG12; APG12_C The carboxy-terminal ubiquitin-like domain of APG12. Autophagy is a process in which cytoplasmic components are delivered to the lysosome/vacuole for degradation. Autophagy requires a ubiquitin-like protein conjugation system, in which APG12 is covalently bound to APG5.


Pssm-ID: 176356  Cd Length: 87  Bit Score: 36.10  E-value: 1.75e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 259089526  31 VIVEKAPKARIGDLDKKKYLVPSDLTVGQFYFLIRKRIHLRAEDALFFFVNNVIPPT-SATMGLLY 95
Cdd:cd01612    2 VTIRFKPIGSAPILKQKVFKISATQSFQAVIDFLRKRLKLKASDSLFLYINNSFAPSpDENVGNLY 67
UBQ cd00196
Ubiquitin-like proteins; Ubiquitin homologs; Includes ubiquitin and ubiquitin-like proteins. ...
38-101 7.95e-03

Ubiquitin-like proteins; Ubiquitin homologs; Includes ubiquitin and ubiquitin-like proteins. Ubiquitin-mediated proteolysis is part of the regulated turnover of proteins required for controlling cell cycle progression. Other family members are protein modifiers that perform a wide range of functions. Ubiquitination usually results in a covalent bond between the C-terminus of ubiquitin and the epsilon-amino group of a substrate lysine. The three-step mechanism requires an activating enzyme (E1) that forms a thiol ester with the C-terminal carboxy group, a conjugating enzyme (E2) that transiently carries the activated ubiquitin molecule as a thiol ester, and a ligase (E3) that transfers the activated ubiquitin from the E2 to the substrate lysine residue. In poly-ubiquitination, ubiquitin itself is the substrate.


Pssm-ID: 176352  Cd Length: 69  Bit Score: 31.73  E-value: 7.95e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 259089526  38 KARIGDLDKKKYLVPSDLTVGQFYFLIRKRIHLRAEDaLFFFVNNVIPPTSATMGLLYQEHHEE 101
Cdd:cd00196    1 KVKLNDGKTVELLVPSGTTVADLKEKLAKKLGLPPEQ-QRLLVNGKILPDSLTLEDYGLQDGDE 63
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.14
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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