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Conserved domains on  [gi|571551186|ref|XP_006603263|]
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uncharacterized protein LOC102663351 [Glycine max]

Protein Classification

retropepsin-like aspartic protease( domain architecture ID 10084770)

retropepsin-like (A2 family) peptidase is an aspartic protease that hydrolyzes the peptide bonds of substrates; similar to human retroviral-like aspartic protease 1

CATH:  2.40.70.10
Gene Ontology:  GO:0004190|GO:0006508
MEROPS:  A2
PubMed:  1851433|2194475|7674916

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
retropepsin_like cd00303
Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate ...
 50-143 6.19e-15

Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate proteases from retroviruses, retrotransposons and retroelements, as well as eukaryotic dna-damage-inducible proteins (DDIs), and bacterial aspartate peptidases. While fungal and mammalian pepsins are bilobal proteins with structurally related N and C-terminals, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A.


:

Pssm-ID: 133136  Cd Length: 92  Bit Score: 66.59  E-value: 6.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571551186  50 IPCTIGKETMsKALIDLGASINLMPLSMCKRIGNMKI-NPTKMTLQLADRSITRPYRVVEDVLVKVCHFNFPVDFVIMDI 128
Cdd:cd00303    1 LKGKINGVPV-RALVDSGASVNFISESLAKKLGLPPRlLPTPLKVKGANGSSVKTLGVILPVTIGIGGKTFTVDFYVLDL 79

                         90
                 ....*....|....*
gi 571551186 129 EedtDIPLILGRPFM 143
Cdd:cd00303   80 L---SYDVILGRPWL 91
 
Name Accession Description Interval E-value
retropepsin_like cd00303
Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate ...
 50-143 6.19e-15

Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate proteases from retroviruses, retrotransposons and retroelements, as well as eukaryotic dna-damage-inducible proteins (DDIs), and bacterial aspartate peptidases. While fungal and mammalian pepsins are bilobal proteins with structurally related N and C-terminals, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A.


Pssm-ID: 133136  Cd Length: 92  Bit Score: 66.59  E-value: 6.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571551186  50 IPCTIGKETMsKALIDLGASINLMPLSMCKRIGNMKI-NPTKMTLQLADRSITRPYRVVEDVLVKVCHFNFPVDFVIMDI 128
Cdd:cd00303    1 LKGKINGVPV-RALVDSGASVNFISESLAKKLGLPPRlLPTPLKVKGANGSSVKTLGVILPVTIGIGGKTFTVDFYVLDL 79

                         90
                 ....*....|....*
gi 571551186 129 EedtDIPLILGRPFM 143
Cdd:cd00303   80 L---SYDVILGRPWL 91
Asp_protease_2 pfam13650
Aspartyl protease; This family consists of predicted aspartic proteases, typically from 180 to ...
 50-142 4.78e-05

Aspartyl protease; This family consists of predicted aspartic proteases, typically from 180 to 230 amino acids in length, in MEROPS clan AA. This model describes the well-conserved 121-residue C-terminal region. The poorly conserved, variable length N-terminal region usually contains a predicted transmembrane helix.


Pssm-ID: 433378  Cd Length: 90  Bit Score: 40.35  E-value: 4.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571551186   50 IPCTIGKETMSkALIDLGASINLMPLSMCKRIG-NMKINPTKMTLQLADRSITRPYRVVEDVLVKVCHFNfPVDFVIMDI 128
Cdd:pfam13650   1 VPVTINGKPVR-FLVDTGASGTVISPSLAERLGlKVRGLAYTVRVSTAGGRVSAARVRLDSLRLGGLTLE-NVPALVLDL 78

                          90
                  ....*....|....
gi 571551186  129 EEDTDIplILGRPF 142
Cdd:pfam13650  79 GDLIDG--LLGMDF 90
 
Name Accession Description Interval E-value
retropepsin_like cd00303
Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate ...
 50-143 6.19e-15

Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate proteases from retroviruses, retrotransposons and retroelements, as well as eukaryotic dna-damage-inducible proteins (DDIs), and bacterial aspartate peptidases. While fungal and mammalian pepsins are bilobal proteins with structurally related N and C-terminals, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A.


Pssm-ID: 133136  Cd Length: 92  Bit Score: 66.59  E-value: 6.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571551186  50 IPCTIGKETMsKALIDLGASINLMPLSMCKRIGNMKI-NPTKMTLQLADRSITRPYRVVEDVLVKVCHFNFPVDFVIMDI 128
Cdd:cd00303    1 LKGKINGVPV-RALVDSGASVNFISESLAKKLGLPPRlLPTPLKVKGANGSSVKTLGVILPVTIGIGGKTFTVDFYVLDL 79

                         90
                 ....*....|....*
gi 571551186 129 EedtDIPLILGRPFM 143
Cdd:cd00303   80 L---SYDVILGRPWL 91
Asp_protease_2 pfam13650
Aspartyl protease; This family consists of predicted aspartic proteases, typically from 180 to ...
 50-142 4.78e-05

Aspartyl protease; This family consists of predicted aspartic proteases, typically from 180 to 230 amino acids in length, in MEROPS clan AA. This model describes the well-conserved 121-residue C-terminal region. The poorly conserved, variable length N-terminal region usually contains a predicted transmembrane helix.


Pssm-ID: 433378  Cd Length: 90  Bit Score: 40.35  E-value: 4.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571551186   50 IPCTIGKETMSkALIDLGASINLMPLSMCKRIG-NMKINPTKMTLQLADRSITRPYRVVEDVLVKVCHFNfPVDFVIMDI 128
Cdd:pfam13650   1 VPVTINGKPVR-FLVDTGASGTVISPSLAERLGlKVRGLAYTVRVSTAGGRVSAARVRLDSLRLGGLTLE-NVPALVLDL 78

                          90
                  ....*....|....
gi 571551186  129 EEDTDIplILGRPF 142
Cdd:pfam13650  79 GDLIDG--LLGMDF 90
gag-asp_proteas pfam13975
gag-polyprotein putative aspartyl protease; This family of putative aspartyl proteases is ...
 50-143 8.64e-04

gag-polyprotein putative aspartyl protease; This family of putative aspartyl proteases is found pre-dominantly in retroviral proteins.


Pssm-ID: 464060  Cd Length: 92  Bit Score: 36.79  E-value: 8.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571551186   50 IPCTIGKETMsKALIDLGASINLMPLSMCKRIGNM-KINPTKMTLQLAD-RSITRPYRVVEdvlVKVCHFNFP-VDFVIM 126
Cdd:pfam13975   1 VDVTINGRPV-RFLVDTGASVTVISEALAERLGLDrLVDAYPVTVRTANgTVRAARVRLDS---VKIGGIELRnVPAVVL 76

                          90
                  ....*....|....*..
gi 571551186  127 DIEEDTdipLILGRPFM 143
Cdd:pfam13975  77 PGDLDD---VLLGMDFL 90
 
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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