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Conserved domains on  [gi|2252660192|ref|NP_001395159|]
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autophagy-related protein 9A isoform c [Mus musculus]

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: 709.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252660192  37 WHHIENLDLFFSRVYNLHQKNGFTCMLIGEMFELMQFLFVVAFTTFLVSCVDYDILFAnkmvnhslhptePVKVTLPDAF 116
Cdd:pfam04109   3 WANVENLDSFLTDVYNYYQGKGFWCILLSRVLELLTLAFVVGFSTFLLLCVDYSKLFN------------PDSVTLSDVI 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252660192 117 LPaqVCSARIqeNGSLITILVIAGVFWIHRLIKFIYNICCYWEIHSFYLHALRIPMSALPYCTWQEVQARIVQTQKEHQI 196
Cdd:pfam04109  71 VP--QCTSKI--SGFTKLLLWLFSIYWVLKLLQFFLDLRRLWEIRNFYNYLLNIPDSDLQTISWQEVVERIMALQDENPL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252660192 197 CIHKRELTELDIYHRILRFQNYMVALVNKSLLPLRFRLPGLGEVVFFTRGLKYNFELILFWGpgsLFLNEWSLKAEYKRG 276
Cdd:pfam04109 147 TAHKVRLDAHDIANRIMRKENYLIALFNKDILDLTLPIPFLGNRQFLTKTLEWNLNLCLFDF---VFDENGQIRPEFLKD 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252660192 277 GQRLELAQRLSNRILWIGIANFLLCPLILIWQILYAFFSYAEVLKREPGALGARCWSLYGRCYLRHFNELEHELQSRLNR 356
Cdd:pfam04109 224 SNRKELAEELRKRFLFAGLLNLLLAPFIVIYFLLYYFFRYFEEYKKNPGSLGSRRWSPLARWKFREFNELPHLFQARLNR 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252660192 357 GYKPASKYMNCFLSPLLTLLAKNGAFFAGSILAVLIALTIYDEDVL------AVEHVLTTVTLLGVTVTVCRSFIPDQHM 430
Cdd:pfam04109 304 SYPPASKYLNQFPSPKTAIIAKFVAFVAGSFAAVLVLLTLLDPELFlnfeitPGRTVLFYITVFGTIWAVARGMIPDENL 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252660192 431 VFCPEQLLRVILAHIHYMPDHWQGNAHRSQTRDEFAQLFQYKAVFILEELLSPIVTPLILIFCLRPRALEIIDFFRNFTV 510
Cdd:pfam04109 384 VFDPEQLLREVIQHTHYLPDEWKGKLHTDEVRAEFSELFQLKIVIFLEELLSIILTPFILWFSLPKCSDEIIDFFREFTV 463
                         490
                  ....*....|....*
gi 2252660192 511 EVVGVGDTCSFAQMD 525
Cdd:pfam04109 464 HVDGLGYVCSFAVFD 478
PHA03247 super family cl33720
large tegument protein UL36; Provisional
657-801 6.97e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.86  E-value: 6.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252660192  657 PLQPGAAPQGRVPStmtgsgstsSRPRLSPSGMCGTAgRVMRVERVPLKRGERVPGPPNPSPARPAIPVLHPGLEH-LRP 735
Cdd:PHA03247  2557 PAAPPAAPDRSVPP---------PRPAPRPSEPAVTS-RARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHaPDP 2626
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2252660192  736 PPCMGASRG--ATGASQILAQCPVAPLTSPGCPwedgqkMASQHQgtQSRCQRRAQRMNSPLKCTRYR 801
Cdd:PHA03247  2627 PPPSPSPAAnePDPHPPPTVPPPERPRDDPAPG------RVSRPR--RARRLGRAAQASSPPQRPRRR 2686
 
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: 709.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252660192  37 WHHIENLDLFFSRVYNLHQKNGFTCMLIGEMFELMQFLFVVAFTTFLVSCVDYDILFAnkmvnhslhptePVKVTLPDAF 116
Cdd:pfam04109   3 WANVENLDSFLTDVYNYYQGKGFWCILLSRVLELLTLAFVVGFSTFLLLCVDYSKLFN------------PDSVTLSDVI 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252660192 117 LPaqVCSARIqeNGSLITILVIAGVFWIHRLIKFIYNICCYWEIHSFYLHALRIPMSALPYCTWQEVQARIVQTQKEHQI 196
Cdd:pfam04109  71 VP--QCTSKI--SGFTKLLLWLFSIYWVLKLLQFFLDLRRLWEIRNFYNYLLNIPDSDLQTISWQEVVERIMALQDENPL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252660192 197 CIHKRELTELDIYHRILRFQNYMVALVNKSLLPLRFRLPGLGEVVFFTRGLKYNFELILFWGpgsLFLNEWSLKAEYKRG 276
Cdd:pfam04109 147 TAHKVRLDAHDIANRIMRKENYLIALFNKDILDLTLPIPFLGNRQFLTKTLEWNLNLCLFDF---VFDENGQIRPEFLKD 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252660192 277 GQRLELAQRLSNRILWIGIANFLLCPLILIWQILYAFFSYAEVLKREPGALGARCWSLYGRCYLRHFNELEHELQSRLNR 356
Cdd:pfam04109 224 SNRKELAEELRKRFLFAGLLNLLLAPFIVIYFLLYYFFRYFEEYKKNPGSLGSRRWSPLARWKFREFNELPHLFQARLNR 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252660192 357 GYKPASKYMNCFLSPLLTLLAKNGAFFAGSILAVLIALTIYDEDVL------AVEHVLTTVTLLGVTVTVCRSFIPDQHM 430
Cdd:pfam04109 304 SYPPASKYLNQFPSPKTAIIAKFVAFVAGSFAAVLVLLTLLDPELFlnfeitPGRTVLFYITVFGTIWAVARGMIPDENL 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252660192 431 VFCPEQLLRVILAHIHYMPDHWQGNAHRSQTRDEFAQLFQYKAVFILEELLSPIVTPLILIFCLRPRALEIIDFFRNFTV 510
Cdd:pfam04109 384 VFDPEQLLREVIQHTHYLPDEWKGKLHTDEVRAEFSELFQLKIVIFLEELLSIILTPFILWFSLPKCSDEIIDFFREFTV 463
                         490
                  ....*....|....*
gi 2252660192 511 EVVGVGDTCSFAQMD 525
Cdd:pfam04109 464 HVDGLGYVCSFAVFD 478
PHA03247 PHA03247
large tegument protein UL36; Provisional
657-801 6.97e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.86  E-value: 6.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252660192  657 PLQPGAAPQGRVPStmtgsgstsSRPRLSPSGMCGTAgRVMRVERVPLKRGERVPGPPNPSPARPAIPVLHPGLEH-LRP 735
Cdd:PHA03247  2557 PAAPPAAPDRSVPP---------PRPAPRPSEPAVTS-RARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHaPDP 2626
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2252660192  736 PPCMGASRG--ATGASQILAQCPVAPLTSPGCPwedgqkMASQHQgtQSRCQRRAQRMNSPLKCTRYR 801
Cdd:PHA03247  2627 PPPSPSPAAnePDPHPPPTVPPPERPRDDPAPG------RVSRPR--RARRLGRAAQASSPPQRPRRR 2686
 
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: 709.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252660192  37 WHHIENLDLFFSRVYNLHQKNGFTCMLIGEMFELMQFLFVVAFTTFLVSCVDYDILFAnkmvnhslhptePVKVTLPDAF 116
Cdd:pfam04109   3 WANVENLDSFLTDVYNYYQGKGFWCILLSRVLELLTLAFVVGFSTFLLLCVDYSKLFN------------PDSVTLSDVI 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252660192 117 LPaqVCSARIqeNGSLITILVIAGVFWIHRLIKFIYNICCYWEIHSFYLHALRIPMSALPYCTWQEVQARIVQTQKEHQI 196
Cdd:pfam04109  71 VP--QCTSKI--SGFTKLLLWLFSIYWVLKLLQFFLDLRRLWEIRNFYNYLLNIPDSDLQTISWQEVVERIMALQDENPL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252660192 197 CIHKRELTELDIYHRILRFQNYMVALVNKSLLPLRFRLPGLGEVVFFTRGLKYNFELILFWGpgsLFLNEWSLKAEYKRG 276
Cdd:pfam04109 147 TAHKVRLDAHDIANRIMRKENYLIALFNKDILDLTLPIPFLGNRQFLTKTLEWNLNLCLFDF---VFDENGQIRPEFLKD 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252660192 277 GQRLELAQRLSNRILWIGIANFLLCPLILIWQILYAFFSYAEVLKREPGALGARCWSLYGRCYLRHFNELEHELQSRLNR 356
Cdd:pfam04109 224 SNRKELAEELRKRFLFAGLLNLLLAPFIVIYFLLYYFFRYFEEYKKNPGSLGSRRWSPLARWKFREFNELPHLFQARLNR 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252660192 357 GYKPASKYMNCFLSPLLTLLAKNGAFFAGSILAVLIALTIYDEDVL------AVEHVLTTVTLLGVTVTVCRSFIPDQHM 430
Cdd:pfam04109 304 SYPPASKYLNQFPSPKTAIIAKFVAFVAGSFAAVLVLLTLLDPELFlnfeitPGRTVLFYITVFGTIWAVARGMIPDENL 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252660192 431 VFCPEQLLRVILAHIHYMPDHWQGNAHRSQTRDEFAQLFQYKAVFILEELLSPIVTPLILIFCLRPRALEIIDFFRNFTV 510
Cdd:pfam04109 384 VFDPEQLLREVIQHTHYLPDEWKGKLHTDEVRAEFSELFQLKIVIFLEELLSIILTPFILWFSLPKCSDEIIDFFREFTV 463
                         490
                  ....*....|....*
gi 2252660192 511 EVVGVGDTCSFAQMD 525
Cdd:pfam04109 464 HVDGLGYVCSFAVFD 478
PHA03247 PHA03247
large tegument protein UL36; Provisional
657-801 6.97e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.86  E-value: 6.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252660192  657 PLQPGAAPQGRVPStmtgsgstsSRPRLSPSGMCGTAgRVMRVERVPLKRGERVPGPPNPSPARPAIPVLHPGLEH-LRP 735
Cdd:PHA03247  2557 PAAPPAAPDRSVPP---------PRPAPRPSEPAVTS-RARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHaPDP 2626
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2252660192  736 PPCMGASRG--ATGASQILAQCPVAPLTSPGCPwedgqkMASQHQgtQSRCQRRAQRMNSPLKCTRYR 801
Cdd:PHA03247  2627 PPPSPSPAAnePDPHPPPTVPPPERPRDDPAPG------RVSRPR--RARRLGRAAQASSPPQRPRRR 2686
Saf_2TM pfam18303
SAVED-fused 2TM effector domain; Predicted pore-forming effector domain directly fused to ...
240-323 8.77e-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: 8.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252660192 240 VVFFTRglKYNFELILFWGPGSLFLN----EWSLKAEYKRGGQRLELAQRLSNRILWIGIANFLLCPLILIWQILYAFFS 315
Cdd:pfam18303  12 IDWFFR--KRSAGMRLFTGGVALLLAgfggNWALKILFPDAGNSVEASFGSAEIPDWILAIILFIGSLLIIVGAVWAWQR 89

                  ....*...
gi 2252660192 316 YAEVLKRE 323
Cdd:pfam18303  90 YVNEQKRQ 97
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
613-769 1.88e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 41.76  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252660192 613 SESEPLsliANVVAGSSCRGPSLSRDLQGSRhRADVASALRSFSPLQPGAAPQGRVPSTMTGsGSTSSRPRLSPSGMCGT 692
Cdd:PRK07003  490 FEPAPR---AAAPSAATPAAVPDARAPAAAS-REDAPAAAAPPAPEARPPTPAAAAPAARAG-GAAAALDVLRNAGMRVS 564
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2252660192 693 AGRvMRVERVPLKRGERVPGPPNPSPARPAIPVLHPGLEHLRP-PPCMGASRGATGASQilaqcpvaPLTSPgcPWED 769
Cdd:PRK07003  565 SDR-GARAAAAAKPAAAPAAAPKPAAPRVAVQVPTPRARAATGdAPPNGAARAEQAAES--------RGAPP--PWED 631
 
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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