Protein Domain : IPR001995

Type:  Domain Name:  Peptidase A2A, retrovirus, catalytic
Description:  Aspartic endopeptidases of vertebrate, fungal and retroviral origin have been characterised []. More recently, aspartic endopeptidases associated with the processing of bacterial type 4 prepilin []and archaean preflagellin have been described [, ].Structurally, aspartic endopeptidases are bilobal enzymes, each lobe contributing a catalytic Asp residue, with an extended active site cleft localised between the two lobes of the molecule. One lobe has probably evolved from the other through a gene duplication event in the distant past. In modern-day enzymes, although the three-dimensional structures are very similar, the amino acid sequences are more divergent, except for the catalytic site motif, which is very conserved. The presence and position of disulphide bridges are other conserved features of aspartic peptidases.All or most aspartate peptidases are endopeptidases. These enzymes have been assigned into clans (proteins which are evolutionary related), and further sub-divided into families, largely on the basis of their tertiary structure.This group of aspartic peptidases belong to the MEROPS peptidase family A2 (retropepsin family, clan AA), subfamily A2A. The family includes the single domain aspartic proteases from retroviruses, retrotransposons, and badnaviruses (plant dsDNA viruses).Retroviral aspartyl protease is synthesised as part of the POL polyprotein that contains; an aspartyl protease, a reverse transcriptase, RNase H and integrase. POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. Short Name:  Peptidase_A2_cat

0 Child Features

1 Contains

DB identifier Type Name
IPR001969 Active_site Aspartic peptidase, active site

1 Cross References


2 Found Ins

DB identifier Type Name
IPR021109 Domain Aspartic peptidase domain
IPR018061 Domain Peptidase A2A, retrovirus RVP subgroup

2 GO Annotations

GO Term Gene Name Organism
GO:0004190 IPR001995
GO:0006508 IPR001995

0 Parent Features

102 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
AT3G13235.3 F4JC86 PAC:19664090 Arabidopsis thaliana 413  
AT3G13235.1 Q1EBV4 PAC:19664088 Arabidopsis thaliana 414  
AT3G13235.2 Q1EBV4 PAC:19664089 Arabidopsis thaliana 414  
Thhalv10023188m V4LKM6 PAC:20202415 Eutrema salsugineum 1101  
Thhalv10020839m V4NQ47 PAC:20181450 Eutrema salsugineum 409  
Thhalv10020843m V4LE07 PAC:20181451 Eutrema salsugineum 408  
Thhalv10009827m V4KS84 PAC:20186746 Eutrema salsugineum 772  
Thhalv10005523m V4KTE9 PAC:20198874 Eutrema salsugineum 590  
Carubv10013820m R0G5L0 PAC:20898547 Capsella rubella 414  
Gorai.008G169100.1 A0A0D2T1T3 PAC:26815132 Gossypium raimondii 492  
Gorai.006G078200.1 A0A0D2STQ6 PAC:26832601 Gossypium raimondii 695  
Gorai.003G148300.1 PAC:26798058 Gossypium raimondii 649  
62173 C1FHR6 PAC:27397796 Micromonas sp. RCC299 1601  
Araha.10371s0002.1.p PAC:28857146 Arabidopsis halleri 414  
Cagra.0690s0040.1.p PAC:28893749 Capsella grandiflora 414  
Glyma.20G086500.1.p A0A0R0E8P4 PAC:30520345 Glycine max 884  
Glyma.18G161300.1.p K7MSM0 PAC:30556750 Glycine max 714  
Glyma.15G205000.1.p A0A0R0GC44 PAC:30497743 Glycine max 571  
Glyma.11G160800.1.p A0A0R0HHY3 PAC:30529359 Glycine max 870  
Glyma.09G081300.1.p A0A0R0I5I2 PAC:30486767 Glycine max 611  
Glyma.06G243600.1.p A0A0R0JL94 PAC:30549252 Glycine max 620  
Glyma.05G072900.1.p A0A0R0JZ47 PAC:30523802 Glycine max 871  
Brara.A03272.1.p PAC:30639840 Brassica rapa FPsc 407  
Brara.C03457.1.p PAC:30617283 Brassica rapa FPsc 408  
Brara.C03457.2.p PAC:30617284 Brassica rapa FPsc 407  
Bostr.3640s0108.1.p PAC:30652033 Boechera stricta 415  
Cre10.g447300.t1.2 A8HZC5 PAC:30789776 Chlamydomonas reinhardtii 472  
GRMZM2G450937_P07 K7UBP7 PAC:31049656 Zea mays 989  
ChrSy.fgenesh.mRNA.87 PAC:33149904 Oryza sativa 1235  
LOC_Os01g42170.1 PAC:33120959 Oryza sativa 1634  

4 Publications

First Author Title Year Journal Volume Pages PubMed ID