NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|24651315|ref|NP_733350|]
View 

VhaAC45-related protein, isoform A [Drosophila melanogaster]

Protein Classification

V-type proton ATPase subunit S1( domain architecture ID 10530743)

V-type proton ATPase subunit S1 is an accessory subunit of the proton-transporting vacuolar (V)-ATPase protein pump, which is required for luminal acidification of secretory vesicles

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Lamp super family cl46412
Lysosome-associated membrane glycoprotein (Lamp);
242-319 2.59e-08

Lysosome-associated membrane glycoprotein (Lamp);


The actual alignment was detected with superfamily member pfam05827:

Pssm-ID: 480752  Cd Length: 144  Bit Score: 52.49  E-value: 2.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651315   242 TLRFKFSLIRGSWTLRNVEVEYRELKSVLVARGDEYtlpsAPLGFSYRCSaeSVNFLNPA---RNETIQS---LLLSDFQ 315
Cdd:pfam05827  67 SRHFYPVSARGYFTLDNVEIDYNGKAATFNSSRDIS----APAGFSYHCS--SVSFFSDAllvPNSPNNSkwrLTFDDFQ 140


                  ....
gi 24651315   316 VQPW 319
Cdd:pfam05827 141 IQPF 144
 
Name Accession Description Interval E-value
VAS1_LD pfam05827
V-type proton ATPase subunit S1, luminal domain; This entry represents the luminal domain (LD) ...
 242-319 2.59e-08

V-type proton ATPase subunit S1, luminal domain; This entry represents the luminal domain (LD) found in eukaryotic V-type proton ATPase subunit S1 involved in V-ATPase V0 assembly, including Ac45 subunit (ATP6AP1). This domain folds as a globular beta-prism structure which is structurally similar to LAMP1-3, thus, the LD domain of Ac45 is an evolutionarily conserved member of the LAMP family. Ac45 is an ER membrane protein that guides the V-type ATPase into specialized subcellular compartments and is critical for Vo complex assembly as it connects to multiple Vo subunits and phospholipids in the c-ring. Missense mutations in the X-linked ATP6AP1 gene cause immunodeficiency in males that leads to recurrent bacterial infection, hepatopathy, cognitive impairment, and abnormal protein glycosylation.


Pssm-ID: 461752  Cd Length: 144  Bit Score: 52.49  E-value: 2.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651315   242 TLRFKFSLIRGSWTLRNVEVEYRELKSVLVARGDEYtlpsAPLGFSYRCSaeSVNFLNPA---RNETIQS---LLLSDFQ 315
Cdd:pfam05827  67 SRHFYPVSARGYFTLDNVEIDYNGKAATFNSSRDIS----APAGFSYHCS--SVSFFSDAllvPNSPNNSkwrLTFDDFQ 140


                  ....
gi 24651315   316 VQPW 319
Cdd:pfam05827 141 IQPF 144
 
Name Accession Description Interval E-value
VAS1_LD pfam05827
V-type proton ATPase subunit S1, luminal domain; This entry represents the luminal domain (LD) ...
 242-319 2.59e-08

V-type proton ATPase subunit S1, luminal domain; This entry represents the luminal domain (LD) found in eukaryotic V-type proton ATPase subunit S1 involved in V-ATPase V0 assembly, including Ac45 subunit (ATP6AP1). This domain folds as a globular beta-prism structure which is structurally similar to LAMP1-3, thus, the LD domain of Ac45 is an evolutionarily conserved member of the LAMP family. Ac45 is an ER membrane protein that guides the V-type ATPase into specialized subcellular compartments and is critical for Vo complex assembly as it connects to multiple Vo subunits and phospholipids in the c-ring. Missense mutations in the X-linked ATP6AP1 gene cause immunodeficiency in males that leads to recurrent bacterial infection, hepatopathy, cognitive impairment, and abnormal protein glycosylation.


Pssm-ID: 461752  Cd Length: 144  Bit Score: 52.49  E-value: 2.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651315   242 TLRFKFSLIRGSWTLRNVEVEYRELKSVLVARGDEYtlpsAPLGFSYRCSaeSVNFLNPA---RNETIQS---LLLSDFQ 315
Cdd:pfam05827  67 SRHFYPVSARGYFTLDNVEIDYNGKAATFNSSRDIS----APAGFSYHCS--SVSFFSDAllvPNSPNNSkwrLTFDDFQ 140


                  ....
gi 24651315   316 VQPW 319
Cdd:pfam05827 141 IQPF 144
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH