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Conserved domains on  [gi|951232895|ref|NP_001303985|]
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autophagy-related protein 9B [Homo sapiens]

Protein Classification

autophagy-related protein 9( domain architecture ID 10513758)

autophagy-related protein 9 is involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ATG9 pfam04109
Autophagy protein ATG9; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
185-676 1.34e-172

Autophagy protein ATG9; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg9 plays a direct role in the formation of the cytoplasm to vacuole targeting and autophagic vesicles, and it is the sole transmembrane protein in the autophagosome-forming machinery. It colocalizes with Atg2 at the expanding edge of the isolation membrane where Atg2 receives phospholipids from the endoplasmic reticulum (ER). Atg9 is a lipid scramblase that translocates phospholipids between outer and inner leaflets of liposomes. Phospholipids delivered by Atg2 are translocated from the cytoplasmic to the luminal leaflet by Atg9, driving autophagosomal membrane expansion.


:

Pssm-ID: 461177  Cd Length: 478  Bit Score: 509.73  E-value: 1.34e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951232895  185 SWHHIQNLDSFFTKIYSYHQRNGFACILLEDVFQLGQFIFIVTFTTFLLRCVDYNVLFAnqpsnhtrpgpfHSKVTLSDA 264
Cdd:pfam04109   2 RWANVENLDSFLTDVYNYYQGKGFWCILLSRVLELLTLAFVVGFSTFLLLCVDYSKLFN------------PDSVTLSDV 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951232895  265 ILPsaQCAERIrsSPLLVLLLVLAAGFWLVQLLRSVCNLFSYWDIQVFYREALHIPPEELSSVPWAEVQSRLLALQRSGG 344
Cdd:pfam04109  70 IVP--QCTSKI--SGFTKLLLWLFSIYWVLKLLQFFLDLRRLWEIRNFYNYLLNIPDSDLQTISWQEVVERIMALQDENP 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951232895  345 LCVQPRPLTELDIHHRILRYTNYQVALANKGLLPARCPLPWGGSAAFLSRGLALNVDLLLFRGpfsLFRGGWELPHAYKR 424
Cdd:pfam04109 146 LTAHKVRLDAHDIANRIMRKENYLIALFNKDILDLTLPIPFLGNRQFLTKTLEWNLNLCLFDF---VFDENGQIRPEFLK 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951232895  425 SDQRGALAARWGRTVLLLAALNLALSPLVLAWQVLHVFYSHVELLRREPGALGARGWSRLARLQLRHFNELPHELRARLA 504
Cdd:pfam04109 223 DSNRKELAEELRKRFLFAGLLNLLLAPFIVIYFLLYYFFRYFEEYKKNPGSLGSRRWSPLARWKFREFNELPHLFQARLN 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951232895  505 RAYRPAAAFLRTAapPAPLRTLLARQLVFFAGALFAALLVLTVYDEDVL------AVEHVLTAMTALGVTATVARSFIPE 578
Cdd:pfam04109 303 RSYPPASKYLNQF--PSPKTAIIAKFVAFVAGSFAAVLVLLTLLDPELFlnfeitPGRTVLFYITVFGTIWAVARGMIPD 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951232895  579 EQCQGRaPQLLLQTALAHMHYLPEEPgpggRDRA-----YRQMAQLLQYRAVSLLEELLSPLLTPLFLLFWFRPRALEII 653
Cdd:pfam04109 381 ENLVFD-PEQLLREVIQHTHYLPDEW----KGKLhtdevRAEFSELFQLKIVIFLEELLSIILTPFILWFSLPKCSDEII 455
                         490       500
                  ....*....|....*....|...
gi 951232895  654 DFFHHFTVDVAGVGDICSFALMD 676
Cdd:pfam04109 456 DFFREFTVHVDGLGYVCSFAVFD 478
 
Name Accession Description Interval E-value
ATG9 pfam04109
Autophagy protein ATG9; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
185-676 1.34e-172

Autophagy protein ATG9; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg9 plays a direct role in the formation of the cytoplasm to vacuole targeting and autophagic vesicles, and it is the sole transmembrane protein in the autophagosome-forming machinery. It colocalizes with Atg2 at the expanding edge of the isolation membrane where Atg2 receives phospholipids from the endoplasmic reticulum (ER). Atg9 is a lipid scramblase that translocates phospholipids between outer and inner leaflets of liposomes. Phospholipids delivered by Atg2 are translocated from the cytoplasmic to the luminal leaflet by Atg9, driving autophagosomal membrane expansion.


Pssm-ID: 461177  Cd Length: 478  Bit Score: 509.73  E-value: 1.34e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951232895  185 SWHHIQNLDSFFTKIYSYHQRNGFACILLEDVFQLGQFIFIVTFTTFLLRCVDYNVLFAnqpsnhtrpgpfHSKVTLSDA 264
Cdd:pfam04109   2 RWANVENLDSFLTDVYNYYQGKGFWCILLSRVLELLTLAFVVGFSTFLLLCVDYSKLFN------------PDSVTLSDV 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951232895  265 ILPsaQCAERIrsSPLLVLLLVLAAGFWLVQLLRSVCNLFSYWDIQVFYREALHIPPEELSSVPWAEVQSRLLALQRSGG 344
Cdd:pfam04109  70 IVP--QCTSKI--SGFTKLLLWLFSIYWVLKLLQFFLDLRRLWEIRNFYNYLLNIPDSDLQTISWQEVVERIMALQDENP 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951232895  345 LCVQPRPLTELDIHHRILRYTNYQVALANKGLLPARCPLPWGGSAAFLSRGLALNVDLLLFRGpfsLFRGGWELPHAYKR 424
Cdd:pfam04109 146 LTAHKVRLDAHDIANRIMRKENYLIALFNKDILDLTLPIPFLGNRQFLTKTLEWNLNLCLFDF---VFDENGQIRPEFLK 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951232895  425 SDQRGALAARWGRTVLLLAALNLALSPLVLAWQVLHVFYSHVELLRREPGALGARGWSRLARLQLRHFNELPHELRARLA 504
Cdd:pfam04109 223 DSNRKELAEELRKRFLFAGLLNLLLAPFIVIYFLLYYFFRYFEEYKKNPGSLGSRRWSPLARWKFREFNELPHLFQARLN 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951232895  505 RAYRPAAAFLRTAapPAPLRTLLARQLVFFAGALFAALLVLTVYDEDVL------AVEHVLTAMTALGVTATVARSFIPE 578
Cdd:pfam04109 303 RSYPPASKYLNQF--PSPKTAIIAKFVAFVAGSFAAVLVLLTLLDPELFlnfeitPGRTVLFYITVFGTIWAVARGMIPD 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951232895  579 EQCQGRaPQLLLQTALAHMHYLPEEPgpggRDRA-----YRQMAQLLQYRAVSLLEELLSPLLTPLFLLFWFRPRALEII 653
Cdd:pfam04109 381 ENLVFD-PEQLLREVIQHTHYLPDEW----KGKLhtdevRAEFSELFQLKIVIFLEELLSIILTPFILWFSLPKCSDEII 455
                         490       500
                  ....*....|....*....|...
gi 951232895  654 DFFHHFTVDVAGVGDICSFALMD 676
Cdd:pfam04109 456 DFFREFTVHVDGLGYVCSFAVFD 478
COG3903 COG3903
Predicted ATPase [General function prediction only];
297-651 1.20e-04

Predicted ATPase [General function prediction only];


Pssm-ID: 443109 [Multi-domain]  Cd Length: 933  Bit Score: 46.16  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951232895 297 LRSVCNLFSYWDIQVFYREALHIPPEELSSVPWAEVQSRLLALQRSGGLCVQPRPLTELDIHHRILRYTNYQVALANKGL 376
Cdd:COG3903  545 LRLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALL 624
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951232895 377 LPARCPLPWGGSAAFLSRGLALNVDLLLFRGPFSLFRGGWELPHAYKRSDQRGALAARWGRTVLLLAALNLALSPLVLAW 456
Cdd:COG3903  625 LLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALA 704
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951232895 457 QVLHVFYSHVELLRREPGALGARGWSRLARLQLRHFNELPHELRARLARAYRPAAAFLRTAAPPAPLRTLLARQLVFFAG 536
Cdd:COG3903  705 AAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAA 784
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951232895 537 ALFAALLVLTVYDEDVLAVEHVLTAMTALGVTATVARSFIPEEQCQGRAPQLLLQTALAHMHYLPEEPGPGGRDRAYRQM 616
Cdd:COG3903  785 ALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAA 864
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 951232895 617 AQLLQYRAVSLLEELLSPLLTPLFLLFWFRPRALE 651
Cdd:COG3903  865 AAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAA 899
 
Name Accession Description Interval E-value
ATG9 pfam04109
Autophagy protein ATG9; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
185-676 1.34e-172

Autophagy protein ATG9; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg9 plays a direct role in the formation of the cytoplasm to vacuole targeting and autophagic vesicles, and it is the sole transmembrane protein in the autophagosome-forming machinery. It colocalizes with Atg2 at the expanding edge of the isolation membrane where Atg2 receives phospholipids from the endoplasmic reticulum (ER). Atg9 is a lipid scramblase that translocates phospholipids between outer and inner leaflets of liposomes. Phospholipids delivered by Atg2 are translocated from the cytoplasmic to the luminal leaflet by Atg9, driving autophagosomal membrane expansion.


Pssm-ID: 461177  Cd Length: 478  Bit Score: 509.73  E-value: 1.34e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951232895  185 SWHHIQNLDSFFTKIYSYHQRNGFACILLEDVFQLGQFIFIVTFTTFLLRCVDYNVLFAnqpsnhtrpgpfHSKVTLSDA 264
Cdd:pfam04109   2 RWANVENLDSFLTDVYNYYQGKGFWCILLSRVLELLTLAFVVGFSTFLLLCVDYSKLFN------------PDSVTLSDV 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951232895  265 ILPsaQCAERIrsSPLLVLLLVLAAGFWLVQLLRSVCNLFSYWDIQVFYREALHIPPEELSSVPWAEVQSRLLALQRSGG 344
Cdd:pfam04109  70 IVP--QCTSKI--SGFTKLLLWLFSIYWVLKLLQFFLDLRRLWEIRNFYNYLLNIPDSDLQTISWQEVVERIMALQDENP 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951232895  345 LCVQPRPLTELDIHHRILRYTNYQVALANKGLLPARCPLPWGGSAAFLSRGLALNVDLLLFRGpfsLFRGGWELPHAYKR 424
Cdd:pfam04109 146 LTAHKVRLDAHDIANRIMRKENYLIALFNKDILDLTLPIPFLGNRQFLTKTLEWNLNLCLFDF---VFDENGQIRPEFLK 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951232895  425 SDQRGALAARWGRTVLLLAALNLALSPLVLAWQVLHVFYSHVELLRREPGALGARGWSRLARLQLRHFNELPHELRARLA 504
Cdd:pfam04109 223 DSNRKELAEELRKRFLFAGLLNLLLAPFIVIYFLLYYFFRYFEEYKKNPGSLGSRRWSPLARWKFREFNELPHLFQARLN 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951232895  505 RAYRPAAAFLRTAapPAPLRTLLARQLVFFAGALFAALLVLTVYDEDVL------AVEHVLTAMTALGVTATVARSFIPE 578
Cdd:pfam04109 303 RSYPPASKYLNQF--PSPKTAIIAKFVAFVAGSFAAVLVLLTLLDPELFlnfeitPGRTVLFYITVFGTIWAVARGMIPD 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951232895  579 EQCQGRaPQLLLQTALAHMHYLPEEPgpggRDRA-----YRQMAQLLQYRAVSLLEELLSPLLTPLFLLFWFRPRALEII 653
Cdd:pfam04109 381 ENLVFD-PEQLLREVIQHTHYLPDEW----KGKLhtdevRAEFSELFQLKIVIFLEELLSIILTPFILWFSLPKCSDEII 455
                         490       500
                  ....*....|....*....|...
gi 951232895  654 DFFHHFTVDVAGVGDICSFALMD 676
Cdd:pfam04109 456 DFFREFTVHVDGLGYVCSFAVFD 478
COG3903 COG3903
Predicted ATPase [General function prediction only];
297-651 1.20e-04

Predicted ATPase [General function prediction only];


Pssm-ID: 443109 [Multi-domain]  Cd Length: 933  Bit Score: 46.16  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951232895 297 LRSVCNLFSYWDIQVFYREALHIPPEELSSVPWAEVQSRLLALQRSGGLCVQPRPLTELDIHHRILRYTNYQVALANKGL 376
Cdd:COG3903  545 LRLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALL 624
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951232895 377 LPARCPLPWGGSAAFLSRGLALNVDLLLFRGPFSLFRGGWELPHAYKRSDQRGALAARWGRTVLLLAALNLALSPLVLAW 456
Cdd:COG3903  625 LLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALA 704
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951232895 457 QVLHVFYSHVELLRREPGALGARGWSRLARLQLRHFNELPHELRARLARAYRPAAAFLRTAAPPAPLRTLLARQLVFFAG 536
Cdd:COG3903  705 AAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAA 784
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951232895 537 ALFAALLVLTVYDEDVLAVEHVLTAMTALGVTATVARSFIPEEQCQGRAPQLLLQTALAHMHYLPEEPGPGGRDRAYRQM 616
Cdd:COG3903  785 ALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAA 864
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 951232895 617 AQLLQYRAVSLLEELLSPLLTPLFLLFWFRPRALE 651
Cdd:COG3903  865 AAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAA 899
 
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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