Reviewed
Homo Sapiens (Human) [TaxID: 9606]
Gag-pol
♦Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA)
♦ Capsid protein p24 (CA)
♦ Spacer peptide 1 (SP1) (p2)
♦ Nucleocapsid protein p7 (NC)
♦ Transframe peptide (TF)
♦ p6-pol (p6*)
♦ Protease (EC 3.4.23.16) (PR) (Retropepsin)
♦ Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT)
♦ p51 RT
♦ p15
♦ Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
♦ Capsid protein p24 (CA)
♦ Spacer peptide 1 (SP1) (p2)
♦ Nucleocapsid protein p7 (NC)
♦ Transframe peptide (TF)
♦ p6-pol (p6*)
♦ Protease (EC 3.4.23.16) (PR) (Retropepsin)
♦ Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT)
♦ p51 RT
♦ p15
♦ Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
Human Immunodeficiency Virus Type 1 Group M Subtype B (isolate BRU/LAI) (HIV-1)
Viruses> Retro-transcribing Viruses> Retroviridae> Orthoretrovirinae> Lentivirus> Primate Lentivirus Group> Human Immunodeficiency Virus 1> HIV-1 Unknown Group> Human Immunodeficiency Virus Type 1 Group M Subtype B (isolate BRU/LAI) (HIV-1)
Various pathway(s) in which protein is involved
Not Available
Not Available
MGARASVLSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEIKDTKEA
LDKIEEEQNKSKKKAQQAAADTGHSSQVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQM
LKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRF
YKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKARVLAEAMSQVTNSATIMMQRGNFRNQRKIVKCFNCGKEGH
IARNCRAPRKKGCWKCGKEGHQMKDCTERQANFLREDLAFLQGKAREFSSEQTRANSPTISSEQTRANSPTRRELQVWGRDNNSLSEAGADRQGTVSFNF
PQITLWQRPLVTIKIGGQLKEALLDTGADDTVLEEMSLPGRWKPKMIGGIGGFIKVRQYDQILIEICGHKAIGTVLVGPTPVNIIGRNLLTQIGCTLNFP
ISPIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEKEGKISKIGPENPYNTPVFAIKKKDSTKWRKLVDFRELNKRTQDFWEVQLGIPHPAGLK
KKKSVTVLDVGDAYFSVPLDEDFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFRKQNPDIVIYQYMDDLYVGSDLEIGQHRTK
IEELRQHLLRWGLTTPDKKHQKEPPFLWMGYELHPDKWTVQPIVLPEKDSWTVNDIQKLVGKLNWASQIYPGIKVRQLCKLLRGTKALTEVIPLTEEAEL
ELAENREILKEPVHGVYYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLKTGKYARTRGAHTNDVKQLTEAVQKITTESIVIWGKTPKFKLPIQKETWETW
WTEYWQATWIPEWEFVNTPPLVKLWYQLEKEPIVGAETFYVDGAASRETKLGKAGYVTNRGRQKVVTLTDTTNQKTELQAIHLALQDSGLEVNIVTDSQY
ALGIIQAQPDKSESELVNQIIEQLIKKEKVYLAWVPAHKGIGGNEQVDKLVSAGIRKVLFLDGIDKAQDEHEKYHSNWRAMASDFNLPPVVAKEIVASCD
KCQLKGEAMHGQVDCSPGIWQLDCTHLEGKVILVAVHVASGYIEAEVIPAETGQETAYFLLKLAGRWPVKTIHTDNGSNFTSTTVKAACWWAGIKQEFGI
PYNPQSQGVVESMNKELKKIIGQVRDQAEHLKTAVQMAVFIHNFKRKGGIGGYSAGERIVDIIATDIQTKELQKQITKIQNFRVYYRDSRDPLWKGPAKL
LWKGEGAVVIQDNSDIKVVPRRKAKIIRDYGKQMAGDDCVASRQDED
LDKIEEEQNKSKKKAQQAAADTGHSSQVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQM
LKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRF
YKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKARVLAEAMSQVTNSATIMMQRGNFRNQRKIVKCFNCGKEGH
IARNCRAPRKKGCWKCGKEGHQMKDCTERQANFLREDLAFLQGKAREFSSEQTRANSPTISSEQTRANSPTRRELQVWGRDNNSLSEAGADRQGTVSFNF
PQITLWQRPLVTIKIGGQLKEALLDTGADDTVLEEMSLPGRWKPKMIGGIGGFIKVRQYDQILIEICGHKAIGTVLVGPTPVNIIGRNLLTQIGCTLNFP
ISPIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEKEGKISKIGPENPYNTPVFAIKKKDSTKWRKLVDFRELNKRTQDFWEVQLGIPHPAGLK
KKKSVTVLDVGDAYFSVPLDEDFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFRKQNPDIVIYQYMDDLYVGSDLEIGQHRTK
IEELRQHLLRWGLTTPDKKHQKEPPFLWMGYELHPDKWTVQPIVLPEKDSWTVNDIQKLVGKLNWASQIYPGIKVRQLCKLLRGTKALTEVIPLTEEAEL
ELAENREILKEPVHGVYYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLKTGKYARTRGAHTNDVKQLTEAVQKITTESIVIWGKTPKFKLPIQKETWETW
WTEYWQATWIPEWEFVNTPPLVKLWYQLEKEPIVGAETFYVDGAASRETKLGKAGYVTNRGRQKVVTLTDTTNQKTELQAIHLALQDSGLEVNIVTDSQY
ALGIIQAQPDKSESELVNQIIEQLIKKEKVYLAWVPAHKGIGGNEQVDKLVSAGIRKVLFLDGIDKAQDEHEKYHSNWRAMASDFNLPPVVAKEIVASCD
KCQLKGEAMHGQVDCSPGIWQLDCTHLEGKVILVAVHVASGYIEAEVIPAETGQETAYFLLKLAGRWPVKTIHTDNGSNFTSTTVKAACWWAGIKQEFGI
PYNPQSQGVVESMNKELKKIIGQVRDQAEHLKTAVQMAVFIHNFKRKGGIGGYSAGERIVDIIATDIQTKELQKQITKIQNFRVYYRDSRDPLWKGPAKL
LWKGEGAVVIQDNSDIKVVPRRKAKIIRDYGKQMAGDDCVASRQDED
1447
Not Available
Not Available
23-01-2007
Evidence at protein level
Amino Acid | Count | % Frequency | Amino Acid | Count | % Frequency |
---|---|---|---|---|---|
Alanine (A) | Leucine (L) | ||||
Arginine (R) | Lysine (K) | ||||
Asparagine (N) | Methionine (M) | ||||
Aspartic Acid (D) | Phenylalanine (F) | ||||
Cysteine (C) | Proline (P) | ||||
Glutamine (Q) | Serine (S) | ||||
Glutamic Acid (E) | Threonine (T) | ||||
Glycine (G) | Tryptophan (W) | ||||
Histidine (H) | Tyrosine (Y) | ||||
Isoleucine (I) | Valine (V) |
% Number of Residues in Helices | % Number of Residues in Strands | % Number of Residues in Coils |
---|---|---|
♦Gag-Pol polyprotein and Gag polyprotein may regulate their own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, Gag-Pol and Gag would promote translation, whereas at high concentration, the polyproteins encapsidate genomic RNA and then shutt off translation (By similarity).
♦ Matrix protein p17 targets Gag and Gag-pol polyproteins to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus (By similarity). Matrix protein is part of the pre-integration complex. Implicated in the release from host cell mediated by Vpu. Binds to RNA (By similarity).
♦ Capsid protein p24: Forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry (By similarity). Host restriction factors such as TRIM5-alpha or TRIMCyp bind retroviral capsids and cause premature capsid disassembly, leading to blocks in reverse transcription. Capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species. Host PIN1 apparently facilitates the virion uncoating. On the other hand, interactions with PDZD8 or CYPA stabilize the capsid.
♦ Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc fingers. Acts as a nucleic acid chaperone which is involved in rearangement of nucleic acid secondary structure during gRNA retrotranscription. Also facilitates template switch leading to recombination. As part of the polyprotein, participates in gRNA dimerization, packaging, tRNA incorporation and virion assembly.
♦ The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. Also cleaves Nef and Vif, probably concomitantly with viral structural proteins on maturation of virus particles. Hydrolyzes host EIF4GI and PABP1 in order to shut off the capped cellular mRNA translation. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity).
♦ Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that converts the viral RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA(3)-Lys binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for two polypurine tracts (PPTs) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPTs that have not been removed by RNase H as primers. PPTs and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends (By similarity).
♦ Integrase: Catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein, Vpr and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step, the PIC enters cell nucleus. This process is mediated through integrase and Vpr proteins, and allows the virus to infect a non dividing cell. This ability to enter the nucleus is specific of lentiviruses, other retroviruses cannot and rely on cell division to access cell chromosomes. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The 5'-ends are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination intermediate results, with the 5'-ends of the viral DNA strands and the 3' ends of target DNA strands remaining unjoined, flanking a gap of 5 bp. The last step is viral DNA integration into host chromosome. This involves host DNA repair synthesis in which the 5 bp gaps between the unjoined strands are filled in and then ligated. Since this process occurs at both cuts flanking the HIV genome, a 5 bp duplication of host DNA is produced at the ends of HIV-1 integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration.
♦ Matrix protein p17 targets Gag and Gag-pol polyproteins to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus (By similarity). Matrix protein is part of the pre-integration complex. Implicated in the release from host cell mediated by Vpu. Binds to RNA (By similarity).
♦ Capsid protein p24: Forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry (By similarity). Host restriction factors such as TRIM5-alpha or TRIMCyp bind retroviral capsids and cause premature capsid disassembly, leading to blocks in reverse transcription. Capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species. Host PIN1 apparently facilitates the virion uncoating. On the other hand, interactions with PDZD8 or CYPA stabilize the capsid.
♦ Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc fingers. Acts as a nucleic acid chaperone which is involved in rearangement of nucleic acid secondary structure during gRNA retrotranscription. Also facilitates template switch leading to recombination. As part of the polyprotein, participates in gRNA dimerization, packaging, tRNA incorporation and virion assembly.
♦ The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. Also cleaves Nef and Vif, probably concomitantly with viral structural proteins on maturation of virus particles. Hydrolyzes host EIF4GI and PABP1 in order to shut off the capped cellular mRNA translation. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity).
♦ Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that converts the viral RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA(3)-Lys binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for two polypurine tracts (PPTs) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPTs that have not been removed by RNase H as primers. PPTs and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends (By similarity).
♦ Integrase: Catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein, Vpr and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step, the PIC enters cell nucleus. This process is mediated through integrase and Vpr proteins, and allows the virus to infect a non dividing cell. This ability to enter the nucleus is specific of lentiviruses, other retroviruses cannot and rely on cell division to access cell chromosomes. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The 5'-ends are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination intermediate results, with the 5'-ends of the viral DNA strands and the 3' ends of target DNA strands remaining unjoined, flanking a gap of 5 bp. The last step is viral DNA integration into host chromosome. This involves host DNA repair synthesis in which the 5 bp gaps between the unjoined strands are filled in and then ligated. Since this process occurs at both cuts flanking the HIV genome, a 5 bp duplication of host DNA is produced at the ends of HIV-1 integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration.
3.4.23.16 , 2.7.7.49 , 2.7.7.7 , 3.1.26.13 , 3.1.13.2 , 2.7.7.- , 3.1.-.-
GO:0003677 ; GO:0003723 ; GO:0003887 ; GO:0003964 ; GO:0004190 ;
GO:0004523 ; GO:0004533 ; GO:0005198 ; GO:0006310 ; GO:0008270 ;
GO:0008289 ; GO:0015074 ; GO:0019013 ; GO:0020002 ; GO:0039651 ;
GO:0039657 ; GO:0042025 ; GO:0044826 ; GO:0046718 ; GO:0055036 ;
GO:0072494 ; GO:0075713 ; GO:0075732
GO:0004523 ; GO:0004533 ; GO:0005198 ; GO:0006310 ; GO:0008270 ;
GO:0008289 ; GO:0015074 ; GO:0019013 ; GO:0020002 ; GO:0039651 ;
GO:0039657 ; GO:0042025 ; GO:0044826 ; GO:0046718 ; GO:0055036 ;
GO:0072494 ; GO:0075713 ; GO:0075732
♦ Gag-Pol polyprotein: Host cell membrane
♦ Lipid-anchor. Host endosome, host multivesicular body . Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion assembly. .
♦ Matrix protein p17: Virion membrane
♦ Lipid-anchor . Host nucleus . Host cytoplasm .
♦ Capsid protein p24: Virion .
♦ Nucleocapsid protein p7: Virion .
♦ Reverse transcriptase/ribonuclease H: Virion .
♦ Integrase: Virion . Host nucleus . Host cytoplasm . Note=Nuclear at initial phase, cytoplasmic at assembly. .
♦ Lipid-anchor. Host endosome, host multivesicular body . Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion assembly. .
♦ Matrix protein p17: Virion membrane
♦ Lipid-anchor . Host nucleus . Host cytoplasm .
♦ Capsid protein p24: Virion .
♦ Nucleocapsid protein p7: Virion .
♦ Reverse transcriptase/ribonuclease H: Virion .
♦ Integrase: Virion . Host nucleus . Host cytoplasm . Note=Nuclear at initial phase, cytoplasmic at assembly. .
♦DOMAIN 520 589 Peptidase A2.
♦ DOMAIN 643 833 Reverse transcriptase.
♦ DOMAIN 1033 1156 RNase H.
♦ DOMAIN 1213 1363 Integrase catalytic.
♦ DOMAIN 643 833 Reverse transcriptase.
♦ DOMAIN 1033 1156 RNase H.
♦ DOMAIN 1213 1363 Integrase catalytic.
MOTIF 16 22 Nuclear export signal. ; MOTIF 26 32 Nuclear localization signal. ; MOTIF 997 1013 Tryptophan repeat motif.
Model (1); X-ray crystallography (149); Neutron diffraction (1)
1A8G 1A8K 1A94 1AAQ 1D4S 1D4Y 1DAZ 1DIF 1FQX 1HHP 1HNI 1HPO 1HPX 1HSG 1HVL
1IIQ 1IZI 1LZQ 1M0B 1MRW 1MRX 1MSM 1MSN 1NH0 1RL8 1SDT 1SDU 1SDV 1SGU 1SH9
1SP5 1U8G 1UPJ 1XL2 1XL5 1Z8C 1ZBG 1ZJ7 1ZLF 1ZPK 1ZTZ 2A1E 2AZ8 2AZ9 2AZB
2AZC 2B7Z 2BB9 2FDE 2FND 2HB2 2HB4 2HC0 2HND 2HNY 2IEN 2O4K 2O4L 2O4N 2O4P
2O4S 2P3B 2PK5 2PK6 2PQZ 2PWC 2PWR 2PYM 2PYN 2Q63 2Q64 2QAK 2QCI 2QD6 2QD7
2QD8 2QHC 2QNN 2QNP 2QNQ 2R43 2UPJ 2Z4O 2ZGA 2ZYE 3A2O 3BHE 3BVA 3BVB 3CKT
3DJK 3DK1 3FX5 3GGU 3H5B 3I6O 3I8W 3JVW 3JVY 3JW2 3KDB 3KDC 3KDD 3NDU 3NDW
3NDX 3NLS 3PWM 3PWR 3QBF 3QIH 3QN8 3QP0 3QPJ 3QRM 3QRO 3QRS 3ST5 3T11 3T3C
3TOF 3TOG 3TOH 3TTP 3U7S 3UCB 3UF3 3UFN 3UHL 3VF5 3VF7 3VFB 4DFG 4FAF 4FE6
4FL8 4FLG 4FM6 4GB2 4HDB 4HDF 4HDP 4HE9 4HEG 4HLA 4J54 4J55 4J5J 4JEC 4LL3
5E5K 6BSH 7UPJ
1IIQ 1IZI 1LZQ 1M0B 1MRW 1MRX 1MSM 1MSN 1NH0 1RL8 1SDT 1SDU 1SDV 1SGU 1SH9
1SP5 1U8G 1UPJ 1XL2 1XL5 1Z8C 1ZBG 1ZJ7 1ZLF 1ZPK 1ZTZ 2A1E 2AZ8 2AZ9 2AZB
2AZC 2B7Z 2BB9 2FDE 2FND 2HB2 2HB4 2HC0 2HND 2HNY 2IEN 2O4K 2O4L 2O4N 2O4P
2O4S 2P3B 2PK5 2PK6 2PQZ 2PWC 2PWR 2PYM 2PYN 2Q63 2Q64 2QAK 2QCI 2QD6 2QD7
2QD8 2QHC 2QNN 2QNP 2QNQ 2R43 2UPJ 2Z4O 2ZGA 2ZYE 3A2O 3BHE 3BVA 3BVB 3CKT
3DJK 3DK1 3FX5 3GGU 3H5B 3I6O 3I8W 3JVW 3JVY 3JW2 3KDB 3KDC 3KDD 3NDU 3NDW
3NDX 3NLS 3PWM 3PWR 3QBF 3QIH 3QN8 3QP0 3QPJ 3QRM 3QRO 3QRS 3ST5 3T11 3T3C
3TOF 3TOG 3TOH 3TTP 3U7S 3UCB 3UF3 3UFN 3UHL 3VF5 3VF7 3VFB 4DFG 4FAF 4FE6
4FL8 4FLG 4FM6 4GB2 4HDB 4HDF 4HDP 4HE9 4HEG 4HLA 4J54 4J55 4J5J 4JEC 4LL3
5E5K 6BSH 7UPJ
♦ACT_SITE 525 525 For protease activity
♦ shared with dimeric partner.
♦ shared with dimeric partner.
Protein couldn't be modeled using I-Tasser and Raptor X because of length constraints of the software.