DB code: M00206

RLCP classification	1.13.200.966 : Hydrolysis
CATH domain	-.-.-.- :
	2.40.70.10 : Cathepsin D, subunit A; domain 1	Catalytic domain
	3.10.10.10 : HIV Type 1 Reverse Transcriptase; Chain A, domain 1
	3.30.70.270 : Alpha-Beta Plaits
	3.30.70.270 : Alpha-Beta Plaits
	3.30.70.270 : Alpha-Beta Plaits
	3.30.420.10 : Nucleotidyltransferase; domain 5
	2.70.40.10 : Deoxyuridine 5'-Triphosphate Nucleotidohydrolase; Chain A	Catalytic domain
	1.10.10.200 : Arc Repressor Mutant, subunit A
	3.30.420.10 : Nucleotidyltransferase; domain 5
	2.30.30.10 : SH3 type barrels.
E.C.	3.4.23.- 2.7.7.49 3.1.26.4 3.6.1.23
CSA
M-CSA
MACiE

CATH domain	Related DB codes (homologues)
1.10.10.200 : Arc Repressor Mutant, subunit A	M00166
2.30.30.10 : SH3 type barrels.	M00135 M00146
2.40.70.10 : Cathepsin D, subunit A; domain 1	D00471 D00436 D00438 D00439 D00440 D00441 D00442 D00443 D00437 D00444 D00423 D00445 D00484 M00166 D00231 D00529
2.70.40.10 : Deoxyuridine 5'-Triphosphate Nucleotidohydrolase; Chain A	T00231
3.10.10.10 : HIV Type 1 Reverse Transcriptase; Chain A, domain 1	M00135 M00146 M00166
3.30.420.10 : Nucleotidyltransferase; domain 5	T00252 M00019 M00020 M00055 M00135 M00146 M00166 M00173 M00175 M00186
3.30.70.270 : Alpha-Beta Plaits	M00019 M00135 M00146 M00166 M00209

Uniprot Enzyme Name
UniprotKB	Protein name	Synonyms	Contains	Pfam
P16088	Pol polyprotein	None	Protease Retropepsin EC 3.4.23.- Reverse transcriptase/ribonuclease H (RT) EC 2.7.7.49 EC 3.1.26.4 Deoxyuridine 5''-triphosphate nucleotidohydrolase (dUTPase) EC 3.6.1.23 Integrase (IN)	PF00692 (dUTPase) PF00552 (IN_DBD_C) PF02022 (Integrase_Zn) PF00075 (RNase_H) PF00665 (rve) PF00077 (RVP) PF00078 (RVT_1) PF06815 (RVT_connect) PF06817 (RVT_thumb) [Graphical View]

KEGG enzyme name
RNA-directed DNA polymerase (EC 2.7.7.49 ) DNA nucleotidyltransferase (RNA-directed) (EC 2.7.7.49 ) reverse transcriptase (EC 2.7.7.49 ) revertase (EC 2.7.7.49 ) RNA-dependent deoxyribonucleate nucleotidyltransferase (EC 2.7.7.49 ) RNA revertase (EC 2.7.7.49 ) RNA-dependent DNA polymerase (EC 2.7.7.49 ) RNA-instructed DNA polymerase (EC 2.7.7.49 ) RT (EC 2.7.7.49 ) calf thymus ribonuclease H (EC 3.1.26.4 ) endoribonuclease H (calf thymus) (EC 3.1.26.4 ) RNase H (EC 3.1.26.4 ) RNA*DNA hybrid ribonucleotidohydrolase (EC 3.1.26.4 ) hybrid ribonuclease (EC 3.1.26.4 ) hybridase (EC 3.1.26.4 ) hybridase (ribonuclease H) (EC 3.1.26.4 ) ribonuclease H (EC 3.1.26.4 ) hybrid nuclease (EC 3.1.26.4 ) dUTP diphosphatase (EC 3.6.1.23 ) deoxyuridine-triphosphatase (EC 3.6.1.23 ) dUTPase (EC 3.6.1.23 ) dUTP pyrophosphatase (EC 3.6.1.23 ) desoxyuridine 5'-triphosphate nucleotidohydrolase (EC 3.6.1.23 ) desoxyuridine 5'-triphosphatase (EC 3.6.1.23 )

KEGG enzyme name

RNA-directed DNA polymerase
(EC 2.7.7.49 )
DNA nucleotidyltransferase (RNA-directed)
(EC 2.7.7.49 )
reverse transcriptase
(EC 2.7.7.49 )
revertase
(EC 2.7.7.49 )
RNA-dependent deoxyribonucleate nucleotidyltransferase
(EC 2.7.7.49 )
RNA revertase
(EC 2.7.7.49 )
RNA-dependent DNA polymerase
(EC 2.7.7.49 )
RNA-instructed DNA polymerase
(EC 2.7.7.49 )
RT
(EC 2.7.7.49 )
calf thymus ribonuclease H
(EC 3.1.26.4 )
endoribonuclease H (calf thymus)
(EC 3.1.26.4 )
RNase H
(EC 3.1.26.4 )
RNA*DNA hybrid ribonucleotidohydrolase
(EC 3.1.26.4 )
hybrid ribonuclease
(EC 3.1.26.4 )
hybridase
(EC 3.1.26.4 )
hybridase (ribonuclease H)
(EC 3.1.26.4 )
ribonuclease H
(EC 3.1.26.4 )
hybrid nuclease
(EC 3.1.26.4 )
dUTP diphosphatase
(EC 3.6.1.23 )
deoxyuridine-triphosphatase
(EC 3.6.1.23 )
dUTPase
(EC 3.6.1.23 )
dUTP pyrophosphatase
(EC 3.6.1.23 )
desoxyuridine 5'-triphosphate nucleotidohydrolase
(EC 3.6.1.23 )
desoxyuridine 5'-triphosphatase
(EC 3.6.1.23 )

UniprotKB: Accession Number	Entry name	Activity	Subunit	Subcellular location	Cofactor
P16088	POL_FIVPE	Endonucleolytic cleavage to 5''- phosphomonoester. dUTP + H(2)O = dUMP + diphosphate. Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

KEGG Pathways
Map code	Pathways	E.C.
MAP00240	Pyrimidine metabolism	3.6.1.23

Compound table
	Cofactors	Substrates							Products						Intermediates
KEGG-id	C00305	C00017	C00012	C00677	C00039	C00046	C00460	C00001	C00017	C00012	C00039	C00960	C00365	C00013	I00136
E.C.		3.4.23.-	3.4.23.-	2.7.7.49	2.7.7.49	3.1.26.4	3.6.1.23	3.4.23.- 3.1.26.4 3.6.1.23	3.4.23.-	3.4.23.-	2.7.7.49	3.1.26.4	3.6.1.23	2.7.7.49 3.6.1.23	3.4.23.-
Compound	Magnesium	Protein	Peptide	Deoxynucleoside triphosphate	DNA(n)	RNA	dUTP	H2O	Protein	Peptide	DNA(n+1)	RNA 5'-phosphate	dUMP	Pyrophosphate	Amino-diol-tetrahedral intermediate
Type	divalent metal (Ca2+, Mg2+)	peptide/protein	peptide/protein	nucleotide	nucleic acids	nucleic acids	amide group,nucleotide	H2O	peptide/protein	peptide/protein	nucleic acids	nucleic acids,phosphate group/phosphate ion	amide group,nucleotide	phosphate group/phosphate ion
ChEBI	18420 18420						17625 17625	15377 15377					17622 17622	29888 29888
PubChem	888 888						65070 65070	22247451 962 22247451 962					65063 65063	1023 21961011 1023 21961011

1b11A	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound		Unbound	Analogue:INT	Unbound	Unbound	Unbound	Unbound	Unbound
1fivA	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound		Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Transition-state-analogue:ACE-ALN-VAL-STA-GLU-ALN
2fivA	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound		Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Transition-state-analogue:ACE-ALN-VAL-STA-GLU-ALN-NH2
3fivA	Unbound	Unbound	Analogue:ACE-ALN-VAL-LEU-ALA-GLU-ALN-NH2 (chain I, J)	Unbound	Unbound	Unbound	Unbound		Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound
4fivA	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound		Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Transition-state-analogue:LP1
5fivA	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound		Unbound	Analogue:INT	Unbound	Unbound	Unbound	Unbound	Unbound
6fivA	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound		Unbound	Analogue:INT	Unbound	Unbound	Unbound	Unbound	Unbound
2fivB	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound		Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound
3fivB	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound		Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound
1dutA	Bound:_MG	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound		Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound
1dutB	Bound:_MG	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound		Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound
1f7dA	Bound:_MG	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound		Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound
1f7dB	Bound:_MG	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound		Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound
1f7kA	Bound:_MG	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound		Unbound	Unbound	Unbound	Unbound	Bound:UMP	Unbound	Unbound
1f7kB	Bound:_MG	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound		Unbound	Unbound	Unbound	Unbound	Bound:UMP	Unbound	Unbound
1f7nA	Bound:_MG	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound		Unbound	Unbound	Unbound	Unbound	Bound:UMP	Unbound	Unbound
1f7nB	Bound:_MG	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound		Unbound	Unbound	Unbound	Unbound	Bound:UMP	Unbound	Unbound
1f7oA	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound		Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound
1f7oB	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound		Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound
1f7oC	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound		Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound
1f7pA	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Analogue:UDP		Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound
1f7pB	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound		Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound
1f7pC	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Analogue:UDP		Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound
1f7qA	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Bound:DUT	Bound:HOH_658	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound
1f7qB	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound		Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound
1f7qC	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Bound:DUT	Bound:HOH_646	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound
1f7rA	Bound:_MG	Unbound	Unbound	Unbound	Unbound	Unbound	Analogue:UDP		Unbound	Unbound	Unbound	Unbound	Unbound	Unbound	Unbound

Reference for Active-site residues
resource	references	E.C.
Swiss-prot;P16088

Active-site residues
PDB	Catalytic residues	Cofactor-binding residues	Modified residues	Main-chain involved in catalysis	Comment

1b11A	ASP 30				(EC 3.4.23.-)
1fivA	ASP 30				(EC 3.4.23.-)
2fivA					(EC 3.4.23.-) mutant D30N
3fivA					(EC 3.4.23.-) mutant D30N
4fivA	ASP 30				(EC 3.4.23.-)
5fivA	ASP 30				(EC 3.4.23.-)
6fivA	ASP 30				(EC 3.4.23.-)
2fivB					(EC 3.4.23.-) mutant D30N
3fivB					(EC 3.4.23.-) mutant D30N
1dutA	LYS 55;ASP 71;LYS 97;GLN 100	ASP 64(magnesium binding)		SER 56;SER 57	(EC 3.6.1.23)
1dutB	LYS 55;ASP 71;LYS 97;GLN 100	ASP 64(magnesium binding)		SER 56;SER 57	(EC 3.6.1.23)
1f7dA	LYS 55;ASP 71;LYS 97;GLN 100	ASP 64(magnesium binding)		SER 56;SER 57	(EC 3.6.1.23)
1f7dB	LYS 255;ASP 271;LYS 297;GLN 300	ASP 264(magnesium binding)		SER 256;SER 257	(EC 3.6.1.23)
1f7kA	LYS 55;ASP 71;LYS 97;GLN 100	ASP 64(magnesium binding)		SER 56;SER 57	(EC 3.6.1.23)
1f7kB	LYS 255;ASP 271;LYS 297;GLN 300	ASP 264(magnesium binding)		SER 256;SER 257	(EC 3.6.1.23)
1f7nA	LYS 55;ASP 71;LYS 97;GLN 100	ASP 64(magnesium binding)		SER 56;SER 57	(EC 3.6.1.23)
1f7nB	LYS 255;ASP 271;LYS 297;GLN 300	ASP 264(magnesium binding)		SER 256;SER 257	(EC 3.6.1.23)
1f7oA	LYS 55;ASP 71;LYS 97;GLN 100	ASP 64(magnesium binding)		SER 56;SER 57	(EC 3.6.1.23)
1f7oB	LYS 255;ASP 271;LYS 297;GLN 300	ASP 264(magnesium binding)		SER 256;SER 257	(EC 3.6.1.23)
1f7oC	LYS 455;ASP 471;LYS 497;GLN 500	ASP 464(magnesium binding)		SER 456;SER 457	(EC 3.6.1.23)
1f7pA	LYS 55;ASP 71;LYS 97;GLN 100	ASP 64(magnesium binding)		SER 56;SER 57	(EC 3.6.1.23)
1f7pB	LYS 255;ASP 271;LYS 297;GLN 300	ASP 264(magnesium binding)		SER 256;SER 257	(EC 3.6.1.23)
1f7pC	LYS 455;ASP 471;LYS 497;GLN 500	ASP 464(magnesium binding)		SER 456;SER 457	(EC 3.6.1.23)
1f7qA	LYS 55;ASP 71;LYS 97;GLN 100	ASP 64(magnesium binding)		SER 56;SER 57	(EC 3.6.1.23)
1f7qB	LYS 255;ASP 271;LYS 297;GLN 300	ASP 264(magnesium binding)		SER 256;SER 257	(EC 3.6.1.23)
1f7qC	LYS 455;ASP 471;LYS 497;GLN 500	ASP 464(magnesium binding)		SER 456;SER 457	(EC 3.6.1.23)
1f7rA	LYS 55;ASP 71;LYS 97;GLN 100	ASP 64(magnesium binding)		SER 56;SER 57	(EC 3.6.1.23)

References for Catalytic Mechanism
References	Sections	No. of steps in catalysis
[2]	Fig.1
[4]	Fig.8, p.10705-10707

References
[1]
Resource
Comments	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 42-154. Retropepsin (3.4.23.-)
Medline ID	95393228
PubMed ID	7664111
Journal	Nat Struct Biol
Year	1995
Volume	2
Pages	480-8
Authors	Wlodawer A, Gustchina A, Reshetnikova L, Lubkowski J, Zdanov A, Hui KY, Angleton EL, Farmerie WG, Goodenow MM, Bhatt D, et al
Title	Structure of an inhibitor complex of the proteinase from feline immunodeficiency virus.
Related PDB	1fiv
Related UniProtKB	P16088
[2]
Resource
Comments	Retropepsin (3.4.23.-)
Medline ID
PubMed ID	9022971
Journal	Bioorg Med Chem
Year	1996
Volume	4
Pages	2055-69
Authors	Qian X, Moris-Varas F, Fitzgerald MC, Wong CH
Title	C2-symmetrical tetrahydroxyazepanes as inhibitors of glycosidases and HIV/FIV proteases.
Related PDB
Related UniProtKB
[3]
Resource
Comments	dUTP pyrophosphatase (3.6.1.23)
Medline ID
PubMed ID	8976551
Journal	Protein Sci
Year	1996
Volume	5
Pages	2429-37
Authors	Prasad GS, Stura EA, McRee DE, Laco GS, Hasselkus-Light C, Elder JH, Stout CD
Title	Crystal structure of dUTP pyrophosphatase from feline immunodeficiency virus.
Related PDB	1dut
Related UniProtKB
[4]
Resource
Comments	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 42-154. Retropepsin (3.4.23.-)
Medline ID	97419133
PubMed ID	9271500
Journal	Biochemistry
Year	1997
Volume	36
Pages	10696-708
Authors	Laco GS, Schalk-Hihi C, Lubkowski J, Morris G, Zdanov A, Olson A, Elder JH, Wlodawer A, Gustchina A
Title	Crystal structures of the inactive D30N mutant of feline immunodeficiency virus protease complexed with a substrate and an inhibitor.
Related PDB	2fiv 3fiv
Related UniProtKB	P16088
[5]
Resource
Comments	X-ray crystallography. Retropepsin (3.4.23.-)
Medline ID
PubMed ID	9827997
Journal	Protein Sci
Year	1998
Volume	7
Pages	2314-23
Authors	Kervinen J, Lubkowski J, Zdanov A, Bhatt D, Dunn BM, Hui KY, Powell DJ, Kay J, Wlodawer A, Gustchina A
Title	Toward a universal inhibitor of retroviral proteases: comparative analysis of the interactions of LP-130 complexed with proteases from HIV-1, FIV, and EIAV.
Related PDB	4fiv
Related UniProtKB
[6]
Resource
Comments	Retropepsin (3.4.23.-)
Medline ID
PubMed ID	10380354
Journal	Biopolymers
Year	1999
Volume	51
Pages	69-77
Authors	Dunn BM, Pennington MW, Frase DC, Nash K
Title	Comparison of inhibitor binding to feline and human immunodeficiency virus proteases: structure-based drug design and the resistance problem.
Related PDB
Related UniProtKB
[7]
Resource
Comments	Retropepsin (3.4.23.-)
Medline ID
PubMed ID	10409825
Journal	Proteins
Year	1999
Volume	36
Pages	318-31
Authors	Dominy BN, Brooks CL 3rd
Title	Methodology for protein-ligand binding studies: application to a model for drug resistance, the HIV/FIV protease system.
Related PDB
Related UniProtKB
[8]
Resource
Comments	dUTP pyrophosphatase (3.6.1.23)
Medline ID
PubMed ID	10329142
Journal	J Mol Biol
Year	1999
Volume	288
Pages	275-87
Authors	Harris JM, McIntosh EM, Muscat GE
Title	Structure/function analysis of a dUTPase: catalytic mechanism of a potential chemotherapeutic target.
Related PDB
Related UniProtKB
[9]
Resource
Comments	X-ray crystallography. Retropepsin (3.4.23.-)
Medline ID
PubMed ID	10651036
Journal	Proteins
Year	2000
Volume	38
Pages	29-40
Authors	Li M, Morris GM, Lee T, Laco GS, Wong CH, Olson AJ, Elder JH, Wlodawer A, Gustchina A
Title	Structural studies of FIV and HIV-1 proteases complexed with an efficient inhibitor of FIV protease.
Related PDB	1b11 5fiv 6fiv
Related UniProtKB
[10]
Resource
Comments	dUTP pyrophosphatase (3.6.1.23)
Medline ID
PubMed ID	10957629
Journal	Acta Crystallogr D Biol Crystallogr
Year	2000
Volume	56
Pages	1100-9
Authors	Prasad GS, Stura EA, Elder JH, Stout CD
Title	Structures of feline immunodeficiency virus dUTP pyrophosphatase and its nucleotide complexes in three crystal forms.
Related PDB	1f7d 1f7k 1f7n 1f7o 1f7p 1f7q 1f7r
Related UniProtKB
[11]
Resource
Comments	Retropepsin (3.4.23.-)
Medline ID
PubMed ID	11206463
Journal	Bioorg Med Chem Lett
Year	2001
Volume	11
Pages	219-22
Authors	Mak CC, Le VD, Lin YC, Elder JH, Wong CH
Title	Design, synthesis, and biological evaluation of HIV/FIV protease inhibitors incorporating a conformationally constrained macrocycle with a small P3' residue.
Related PDB
Related UniProtKB
[12]
Resource
Comments	Retropepsin (3.4.23.-)
Medline ID
PubMed ID	12767979
Journal	J Virol
Year	2003
Volume	77
Pages	6589-600
Authors	Lin YC, Beck Z, Morris GM, Olson AJ, Elder JH
Title	Structural basis for distinctions between substrate and inhibitor specificities for feline immunodeficiency virus and human immunodeficiency virus proteases.
Related PDB
Related UniProtKB
[13]
Resource
Comments	Retropepsin (3.4.23.-)
Medline ID
PubMed ID	15289598
Journal	Proc Natl Acad Sci U S A
Year	2004
Volume	101
Pages	11640-5
Authors	Fernandez A, Rogale K, Scott R, Scheraga HA
Title	Inhibitor design by wrapping packing defects in HIV-1 proteins.
Related PDB
Related UniProtKB
[14]
Resource
Comments	dUTP pyrophosphatase (3.6.1.23)
Medline ID
PubMed ID	16154087
Journal	Structure
Year	2005
Volume	13
Pages	1299-310
Authors	Tarbouriech N, Buisson M, Seigneurin JM, Cusack S, Burmeister WP
Title	The monomeric dUTPase from Epstein-Barr virus mimics trimeric dUTPases.
Related PDB
Related UniProtKB

Comments
This enzyme is composed of retropepsin (EC 3.4.23.-), RNA-directed DNA polymerase (EC 2.7.7.49), RNase H (EC 3.1.26.4), dUTP pyrophosphatase (EC 3.6.1.23), and integrase. The tertiary structures have been solved only for retropepsin (EC 3.4.23.-) and dUTP pyrophosphatase (EC 3.6.1.23). The dUTP pyrophosphatase domain (EC 3.6.1.23) forms a trimer, which binds one Mg2+ ion (see PDB;1dut). The domains which corresponds to protease domain (EC 3.4.23.-) belong to the peptidase family-A2. Although this domain has a catalytic aspartic residue, it forms a homodimer with a single active site with a typical catalytic dyad, composed of two aspartic acid residues. According to the literature [4], the catalytic mechanism is very similar to that of pepsin (see D00436 in EzCatDB).

Comments

This enzyme is composed of retropepsin (EC 3.4.23.-), RNA-directed DNA polymerase (EC 2.7.7.49), RNase H (EC 3.1.26.4), dUTP pyrophosphatase (EC 3.6.1.23), and integrase.
The tertiary structures have been solved only for retropepsin (EC 3.4.23.-) and dUTP pyrophosphatase (EC 3.6.1.23). The dUTP pyrophosphatase domain (EC 3.6.1.23) forms a trimer, which binds one Mg2+ ion (see PDB;1dut).
The domains which corresponds to protease domain (EC 3.4.23.-) belong to the peptidase family-A2.
Although this domain has a catalytic aspartic residue, it forms a homodimer with a single active site with a typical catalytic dyad, composed of two aspartic acid residues. According to the literature [4], the catalytic mechanism is very similar to that of pepsin (see D00436 in EzCatDB).

Created	Updated
2004-03-19	2012-06-28