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Conserved domains on  [gi|116089282|ref|NP_001070666|]
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autophagy-related protein 9A [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. ...
37-525 0e+00

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: 711.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116089282   37 WHHIENLDLFFSRVYNLHQKNGFTCMLIGEIFELMQFLFVVAFTTFLVSCVDYDILFAnkmvnhslhptePVKVTLPDAF 116
Cdd:pfam04109   3 WANVENLDSFLTDVYNYYQGKGFWCILLSRVLELLTLAFVVGFSTFLLLCVDYSKLFN------------PDSVTLSDVI 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116089282  117 LPaqVCSARIqeNGSLITILVIAGVFWIHRLIKFIYNICCYWEIHSFYLHALRIPMSALPYCTWQEVQARIVQTQKEHQI 196
Cdd:pfam04109  71 VP--QCTSKI--SGFTKLLLWLFSIYWVLKLLQFFLDLRRLWEIRNFYNYLLNIPDSDLQTISWQEVVERIMALQDENPL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116089282  197 CIHKRELTELDIYHRILRFQNYMVALVNKSLLPLRFRLPGLGEAVFFTRGLKYNFELILFWGpgsLFLNEWSLKAEYKRG 276
Cdd:pfam04109 147 TAHKVRLDAHDIANRIMRKENYLIALFNKDILDLTLPIPFLGNRQFLTKTLEWNLNLCLFDF---VFDENGQIRPEFLKD 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116089282  277 GQRLELAQRLSNRILWIGIANFLLCPLILIWQILYAFFSYAEVLKREPGALGARCWSLYGRCYLRHFNELEHELQSRLNR 356
Cdd:pfam04109 224 SNRKELAEELRKRFLFAGLLNLLLAPFIVIYFLLYYFFRYFEEYKKNPGSLGSRRWSPLARWKFREFNELPHLFQARLNR 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116089282  357 GYKPASKYMNCFLSPLLTLLAKNGAFFAGSILAVLIALTIYDEDVL------AVEHVLTTVTLLGVTVTVCRSFIPDQHM 430
Cdd:pfam04109 304 SYPPASKYLNQFPSPKTAIIAKFVAFVAGSFAAVLVLLTLLDPELFlnfeitPGRTVLFYITVFGTIWAVARGMIPDENL 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116089282  431 VFCPEQLLRVILAHIHYMPDHWQGNAHRSQTRDEFAQLFQYKAVFILEELLSPIVTPLILIFCLRPRALEIIDFFRNFTV 510
Cdd:pfam04109 384 VFDPEQLLREVIQHTHYLPDEWKGKLHTDEVRAEFSELFQLKIVIFLEELLSIILTPFILWFSLPKCSDEIIDFFREFTV 463
                         490
                  ....*....|....*
gi 116089282  511 EVVGVGDTCSFAQMD 525
Cdd:pfam04109 464 HVDGLGYVCSFAVFD 478
 
Name Accession Description Interval E-value
ATG9 pfam04109
Autophagy protein ATG9; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
37-525 0e+00

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: 711.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116089282   37 WHHIENLDLFFSRVYNLHQKNGFTCMLIGEIFELMQFLFVVAFTTFLVSCVDYDILFAnkmvnhslhptePVKVTLPDAF 116
Cdd:pfam04109   3 WANVENLDSFLTDVYNYYQGKGFWCILLSRVLELLTLAFVVGFSTFLLLCVDYSKLFN------------PDSVTLSDVI 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116089282  117 LPaqVCSARIqeNGSLITILVIAGVFWIHRLIKFIYNICCYWEIHSFYLHALRIPMSALPYCTWQEVQARIVQTQKEHQI 196
Cdd:pfam04109  71 VP--QCTSKI--SGFTKLLLWLFSIYWVLKLLQFFLDLRRLWEIRNFYNYLLNIPDSDLQTISWQEVVERIMALQDENPL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116089282  197 CIHKRELTELDIYHRILRFQNYMVALVNKSLLPLRFRLPGLGEAVFFTRGLKYNFELILFWGpgsLFLNEWSLKAEYKRG 276
Cdd:pfam04109 147 TAHKVRLDAHDIANRIMRKENYLIALFNKDILDLTLPIPFLGNRQFLTKTLEWNLNLCLFDF---VFDENGQIRPEFLKD 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116089282  277 GQRLELAQRLSNRILWIGIANFLLCPLILIWQILYAFFSYAEVLKREPGALGARCWSLYGRCYLRHFNELEHELQSRLNR 356
Cdd:pfam04109 224 SNRKELAEELRKRFLFAGLLNLLLAPFIVIYFLLYYFFRYFEEYKKNPGSLGSRRWSPLARWKFREFNELPHLFQARLNR 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116089282  357 GYKPASKYMNCFLSPLLTLLAKNGAFFAGSILAVLIALTIYDEDVL------AVEHVLTTVTLLGVTVTVCRSFIPDQHM 430
Cdd:pfam04109 304 SYPPASKYLNQFPSPKTAIIAKFVAFVAGSFAAVLVLLTLLDPELFlnfeitPGRTVLFYITVFGTIWAVARGMIPDENL 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116089282  431 VFCPEQLLRVILAHIHYMPDHWQGNAHRSQTRDEFAQLFQYKAVFILEELLSPIVTPLILIFCLRPRALEIIDFFRNFTV 510
Cdd:pfam04109 384 VFDPEQLLREVIQHTHYLPDEWKGKLHTDEVRAEFSELFQLKIVIFLEELLSIILTPFILWFSLPKCSDEIIDFFREFTV 463
                         490
                  ....*....|....*
gi 116089282  511 EVVGVGDTCSFAQMD 525
Cdd:pfam04109 464 HVDGLGYVCSFAVFD 478
 
Name Accession Description Interval E-value
ATG9 pfam04109
Autophagy protein ATG9; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
37-525 0e+00

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: 711.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116089282   37 WHHIENLDLFFSRVYNLHQKNGFTCMLIGEIFELMQFLFVVAFTTFLVSCVDYDILFAnkmvnhslhptePVKVTLPDAF 116
Cdd:pfam04109   3 WANVENLDSFLTDVYNYYQGKGFWCILLSRVLELLTLAFVVGFSTFLLLCVDYSKLFN------------PDSVTLSDVI 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116089282  117 LPaqVCSARIqeNGSLITILVIAGVFWIHRLIKFIYNICCYWEIHSFYLHALRIPMSALPYCTWQEVQARIVQTQKEHQI 196
Cdd:pfam04109  71 VP--QCTSKI--SGFTKLLLWLFSIYWVLKLLQFFLDLRRLWEIRNFYNYLLNIPDSDLQTISWQEVVERIMALQDENPL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116089282  197 CIHKRELTELDIYHRILRFQNYMVALVNKSLLPLRFRLPGLGEAVFFTRGLKYNFELILFWGpgsLFLNEWSLKAEYKRG 276
Cdd:pfam04109 147 TAHKVRLDAHDIANRIMRKENYLIALFNKDILDLTLPIPFLGNRQFLTKTLEWNLNLCLFDF---VFDENGQIRPEFLKD 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116089282  277 GQRLELAQRLSNRILWIGIANFLLCPLILIWQILYAFFSYAEVLKREPGALGARCWSLYGRCYLRHFNELEHELQSRLNR 356
Cdd:pfam04109 224 SNRKELAEELRKRFLFAGLLNLLLAPFIVIYFLLYYFFRYFEEYKKNPGSLGSRRWSPLARWKFREFNELPHLFQARLNR 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116089282  357 GYKPASKYMNCFLSPLLTLLAKNGAFFAGSILAVLIALTIYDEDVL------AVEHVLTTVTLLGVTVTVCRSFIPDQHM 430
Cdd:pfam04109 304 SYPPASKYLNQFPSPKTAIIAKFVAFVAGSFAAVLVLLTLLDPELFlnfeitPGRTVLFYITVFGTIWAVARGMIPDENL 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116089282  431 VFCPEQLLRVILAHIHYMPDHWQGNAHRSQTRDEFAQLFQYKAVFILEELLSPIVTPLILIFCLRPRALEIIDFFRNFTV 510
Cdd:pfam04109 384 VFDPEQLLREVIQHTHYLPDEWKGKLHTDEVRAEFSELFQLKIVIFLEELLSIILTPFILWFSLPKCSDEIIDFFREFTV 463
                         490
                  ....*....|....*
gi 116089282  511 EVVGVGDTCSFAQMD 525
Cdd:pfam04109 464 HVDGLGYVCSFAVFD 478
Saf_2TM pfam18303
SAVED-fused 2TM effector domain; Predicted pore-forming effector domain directly fused to ...
240-323 9.32e-04

SAVED-fused 2TM effector domain; Predicted pore-forming effector domain directly fused to predicted SAVED sensor domain. Binding of a ligand via the SAVED sensor is predicted to activate the Saf-2TM and initiate a cell suicide response. Component of a class of conflict systems reliant on the production of second messenger nucleotide or nucleotide derivative.


Pssm-ID: 408111  Cd Length: 152  Bit Score: 40.43  E-value: 9.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116089282  240 AVFFTRglKYNFELILFWGPGSLFLN----EWSLKAEYKRGGQRLELAQRLSNRILWIGIANFLLCPLILIWQILYAFFS 315
Cdd:pfam18303  12 IDWFFR--KRSAGMRLFTGGVALLLAgfggNWALKILFPDAGNSVEASFGSAEIPDWILAIILFIGSLLIIVGAVWAWQR 89

                  ....*...
gi 116089282  316 YAEVLKRE 323
Cdd:pfam18303  90 YVNEQKRQ 97
 
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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