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Conserved domains on  [gi|571512914|ref|XP_006596709|]
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uncharacterized protein LOC102669820 [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 ...
 59-152 6.60e-17

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: 72.37  E-value: 6.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571512914  59 IPCSIDEVTLgKALIDLGASINLMALSMCRRLG-ELEIMPTRMTLQLANRSITRPYGVVEDVLIRVKHMIFPADFVVMDV 137
Cdd:cd00303    1 LKGKINGVPV-RALVDSGASVNFISESLAKKLGlPPRLLPTPLKVKGANGSSVKTLGVILPVTIGIGGKTFTVDFYVLDL 79

                         90
                 ....*....|....*
gi 571512914 138 EedhEVPVILGHPFM 152
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 ...
 59-152 6.60e-17

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: 72.37  E-value: 6.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571512914  59 IPCSIDEVTLgKALIDLGASINLMALSMCRRLG-ELEIMPTRMTLQLANRSITRPYGVVEDVLIRVKHMIFPADFVVMDV 137
Cdd:cd00303    1 LKGKINGVPV-RALVDSGASVNFISESLAKKLGlPPRLLPTPLKVKGANGSSVKTLGVILPVTIGIGGKTFTVDFYVLDL 79

                         90
                 ....*....|....*
gi 571512914 138 EedhEVPVILGHPFM 152
Cdd:cd00303   80 L---SYDVILGRPWL 91
Asp_protease_2 pfam13650
Aspartyl protease; This family consists of predicted aspartic proteases, typically from 180 to ...
 59-151 1.20e-04

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: 39.58  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571512914   59 IPCSIDEVTLgKALIDLGASINLMALSMCRRLG-ELEIMPTRMTLQLANRSITRPYGVVEDVLIRvKHMIFPADFVVMDV 137
Cdd:pfam13650   1 VPVTINGKPV-RFLVDTGASGTVISPSLAERLGlKVRGLAYTVRVSTAGGRVSAARVRLDSLRLG-GLTLENVPALVLDL 78

                          90
                  ....*....|....
gi 571512914  138 EEDHEvpVILGHPF 151
Cdd:pfam13650  79 GDLID--GLLGMDF 90
 
Name Accession Description Interval E-value
retropepsin_like cd00303
Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate ...
 59-152 6.60e-17

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: 72.37  E-value: 6.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571512914  59 IPCSIDEVTLgKALIDLGASINLMALSMCRRLG-ELEIMPTRMTLQLANRSITRPYGVVEDVLIRVKHMIFPADFVVMDV 137
Cdd:cd00303    1 LKGKINGVPV-RALVDSGASVNFISESLAKKLGlPPRLLPTPLKVKGANGSSVKTLGVILPVTIGIGGKTFTVDFYVLDL 79

                         90
                 ....*....|....*
gi 571512914 138 EedhEVPVILGHPFM 152
Cdd:cd00303   80 L---SYDVILGRPWL 91
Asp_protease_2 pfam13650
Aspartyl protease; This family consists of predicted aspartic proteases, typically from 180 to ...
 59-151 1.20e-04

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: 39.58  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571512914   59 IPCSIDEVTLgKALIDLGASINLMALSMCRRLG-ELEIMPTRMTLQLANRSITRPYGVVEDVLIRvKHMIFPADFVVMDV 137
Cdd:pfam13650   1 VPVTINGKPV-RFLVDTGASGTVISPSLAERLGlKVRGLAYTVRVSTAGGRVSAARVRLDSLRLG-GLTLENVPALVLDL 78

                          90
                  ....*....|....
gi 571512914  138 EEDHEvpVILGHPF 151
Cdd:pfam13650  79 GDLID--GLLGMDF 90
gag-asp_proteas pfam13975
gag-polyprotein putative aspartyl protease; This family of putative aspartyl proteases is ...
 59-153 2.13e-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: 38.71  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571512914   59 IPCSIDEVTLgKALIDLGASINLMALSMCRRLG-ELEIMPTRMTLQLANrsitrpyGVVEDVLIRVKHMIFpADFVVMDV 137
Cdd:pfam13975   1 VDVTINGRPV-RFLVDTGASVTVISEALAERLGlDRLVDAYPVTVRTAN-------GTVRAARVRLDSVKI-GGIELRNV 71

                          90       100
                  ....*....|....*....|
gi 571512914  138 E----EDHEVPVILGHPFMS 153
Cdd:pfam13975  72 PavvlPGDLDDVLLGMDFLK 91
Asp_protease pfam09668
Aspartyl protease; This family of eukaryotic aspartyl proteases have a fold similar to ...
 55-160 3.31e-04

Aspartyl protease; This family of eukaryotic aspartyl proteases have a fold similar to retroviral proteases which implies they function proteolytically during regulated protein turnover.


Pssm-ID: 312981  Cd Length: 124  Bit Score: 39.26  E-value: 3.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571512914   55 GSVT---IPCSIDEVTLgKALIDLGASINLMALSMCRRLGELEIMPTRMTLQLANRSITRPYGVVEDVLIRVKHMIFPAD 131
Cdd:pfam09668  20 GRVTmlyINCEINGVPV-KAFVDSGAQTSIMSPRCAERCGIMRLVDTRFAGIAKGVGTARILGRIHMADVKIGGLFLPCS 98

                          90       100
                  ....*....|....*....|....*....
gi 571512914  132 FVVMdveEDHEVPVILGHPFMSTAGYIID 160
Cdd:pfam09668  99 FSVI---EGQDMDLLLGLDMLKRHQCCID 124
RP_DDI cd05479
RP_DDI; retropepsin-like domain of DNA damage inducible protein; The family represents the ...
 59-167 1.43e-03

RP_DDI; retropepsin-like domain of DNA damage inducible protein; The family represents the retropepsin-like domain of DNA damage inducible protein. DNA damage inducible protein has a retropepsin-like domain and an amino-terminal ubiquitin-like domain and/or a UBA (ubiquitin-associated) domain. This CD represents the retropepsin-like domain of DDI.


Pssm-ID: 133146  Cd Length: 124  Bit Score: 37.15  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571512914  59 IPCSIDEVTLgKALIDLGASINLMALSMCRRLGELEIMPTRMTLQLANRSITRPYGVVEDVLIRVKHMIFPADFVVMdve 138
Cdd:cd05479   19 INVEINGVPV-KAFVDSGAQMTIMSKACAEKCGLMRLIDKRFQGIAKGVGTQKILGRIHLAQVKIGNLFLPCSFTVL--- 94

                         90       100
                 ....*....|....*....|....*....
gi 571512914 139 EDHEVPVILGHPFMSTAGYIIDMGRKTLE 167
Cdd:cd05479   95 EDDDVDFLIGLDMLKRHQCVIDLKENVLR 123
 
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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