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Conserved domains on  [gi|571468646|ref|XP_006584380|]
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uncharacterized protein LOC102660337 [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 ...
 166-259 9.87e-13

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: 63.89  E-value: 9.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571468646 166 IPFTIWNVSVRkALIDLGAHINLMPLSMCRRIGNLKI-DPTKMTLQLTDQSIIRPYGVVKDVFVKVRHFTLPVDFVIMDI 244
Cdd:cd00303    1 LKGKINGVPVR-ALVDSGASVNFISESLAKKLGLPPRlLPTPLKVKGANGSSVKTLGVILPVTIGIGGKTFTVDFYVLDL 79

                         90
                 ....*....|....*
gi 571468646 245 EEdtkIPLILGRPFM 259
Cdd:cd00303   80 LS---YDVILGRPWL 91
 
Name Accession Description Interval E-value
retropepsin_like cd00303
Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate ...
 166-259 9.87e-13

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: 63.89  E-value: 9.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571468646 166 IPFTIWNVSVRkALIDLGAHINLMPLSMCRRIGNLKI-DPTKMTLQLTDQSIIRPYGVVKDVFVKVRHFTLPVDFVIMDI 244
Cdd:cd00303    1 LKGKINGVPVR-ALVDSGASVNFISESLAKKLGLPPRlLPTPLKVKGANGSSVKTLGVILPVTIGIGGKTFTVDFYVLDL 79

                         90
                 ....*....|....*
gi 571468646 245 EEdtkIPLILGRPFM 259
Cdd:cd00303   80 LS---YDVILGRPWL 91
Asp_protease_2 pfam13650
Aspartyl protease; This family consists of predicted aspartic proteases, typically from 180 to ...
 166-258 6.52e-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: 38.81  E-value: 6.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571468646  166 IPFTIWNVSVRkALIDLGAHINLMPLSMCRRIGnLKIDPTKMTLQLTDqsiirPYGVVKDVFVKVRHFTL------PVDF 239
Cdd:pfam13650   1 VPVTINGKPVR-FLVDTGASGTVISPSLAERLG-LKVRGLAYTVRVST-----AGGRVSAARVRLDSLRLggltleNVPA 73

                          90
                  ....*....|....*....
gi 571468646  240 VIMDIEEdtKIPLILGRPF 258
Cdd:pfam13650  74 LVLDLGD--LIDGLLGMDF 90
 
Name Accession Description Interval E-value
retropepsin_like cd00303
Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate ...
 166-259 9.87e-13

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: 63.89  E-value: 9.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571468646 166 IPFTIWNVSVRkALIDLGAHINLMPLSMCRRIGNLKI-DPTKMTLQLTDQSIIRPYGVVKDVFVKVRHFTLPVDFVIMDI 244
Cdd:cd00303    1 LKGKINGVPVR-ALVDSGASVNFISESLAKKLGLPPRlLPTPLKVKGANGSSVKTLGVILPVTIGIGGKTFTVDFYVLDL 79

                         90
                 ....*....|....*
gi 571468646 245 EEdtkIPLILGRPFM 259
Cdd:cd00303   80 LS---YDVILGRPWL 91
Asp_protease_2 pfam13650
Aspartyl protease; This family consists of predicted aspartic proteases, typically from 180 to ...
 166-258 6.52e-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: 38.81  E-value: 6.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571468646  166 IPFTIWNVSVRkALIDLGAHINLMPLSMCRRIGnLKIDPTKMTLQLTDqsiirPYGVVKDVFVKVRHFTL------PVDF 239
Cdd:pfam13650   1 VPVTINGKPVR-FLVDTGASGTVISPSLAERLG-LKVRGLAYTVRVST-----AGGRVSAARVRLDSLRLggltleNVPA 73

                          90
                  ....*....|....*....
gi 571468646  240 VIMDIEEdtKIPLILGRPF 258
Cdd:pfam13650  74 LVLDLGD--LIDGLLGMDF 90
retropepsin_like_LTR_1 cd05481
Retropepsins_like_LTR; pepsin-like aspartate protease from retrotransposons with long terminal ...
 177-257 1.13e-03

Retropepsins_like_LTR; pepsin-like aspartate protease from retrotransposons with long terminal repeats; Retropepsin of retrotransposons with long terminal repeats are pepsin-like aspartate proteases. 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: 133148  Cd Length: 93  Bit Score: 38.01  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571468646 177 KALIDLGAHINLMPLSMCRRI---GNLKIDPTKMTLQLTDQSIIRPYGVVKdvfVKVRHF--TLPVDFVIMdieeDTKIP 251
Cdd:cd05481   12 KFQLDTGATCNVLPLRWLKSLtpdKDPELRPSPVRLTAYGGSTIPVEGGVK---LKCRYRnpKYNLTFQVV----KEEGP 84


                 ....*.
gi 571468646 252 LILGRP 257
Cdd:cd05481   85 PLLGAK 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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