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Conserved domains on  [gi|1552208978|gb|RVW62672|]
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Retrovirus-related Pol polyprotein from transposon 17.6 [Vitis vinifera]

Protein Classification

pol polyprotein( domain architecture ID 10084787)

retrovirus-related pol polyprotein is a polyprotein supplying protease, reverse transcriptase, RNase H and integrase functions.

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RNase_HI_RT_Ty3 cd09274
Ty3/Gypsy family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) ...
800-919 2.08e-64

Ty3/Gypsy family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes. RNase HI has also been observed as adjunct domains to the reverse transcriptase gene in retroviruses, in long-term repeat (LTR)-bearing retrotransposons and non-LTR retrotransposons. RNase HI in LTR retrotransposons perform degradation of the original RNA template, generation of a polypurine tract (the primer for plus-strand DNA synthesis), and final removal of RNA primers from newly synthesized minus and plus strands. The catalytic residues for RNase H enzymatic activity, three aspartatic acids and one glutamic acid residue (DEDD), are unvaried across all RNase H domains. Phylogenetic patterns of RNase HI of LTR retroelements is classified into five major families, Ty3/Gypsy, Ty1/Copia, Bel/Pao, DIRS1 and the vertebrate retroviruses. Ty3/Gypsy family widely distributed among the genomes of plants, fungi and animals. RNase H inhibitors have been explored as an anti-HIV drug target because RNase H inactivation inhibits reverse transcription.


:

Pssm-ID: 260006 [Multi-domain]  Cd Length: 121  Bit Score: 212.74  E-value: 2.08e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552208978  800 ELMCDASDFAIGAVLGQR-EDGKPYVIYYASKTLNEAQRNYTTTEKELLAVVFALDKFRAYLVGSFIIVFTDHSALKYLL 878
Cdd:cd09274      1 ILETDASDYGIGAVLSQEdDDGKERPIAFFSRKLTPAERNYSTTEKELLAIVWALKKFRHYLLGRPFTVYTDHKALKYLL 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1552208978  879 TKQDAKARLIRWILLLQEFDLQIKDKKGVENVVADHLSRLV 919
Cdd:cd09274     81 TQKDLNGRLARWLLLLSEFDFEIEYRPGKENVVADALSRLP 121
RT_LTR cd01647
RT_LTR: Reverse transcriptases (RTs) from retrotransposons and retroviruses which have long ...
569-706 3.74e-57

RT_LTR: Reverse transcriptases (RTs) from retrotransposons and retroviruses which have long terminal repeats (LTRs) in their DNA copies but not in their RNA template. RT catalyzes DNA replication from an RNA template, and is responsible for the replication of retroelements. An RT gene is usually indicative of a mobile element such as a retrotransposon or retrovirus. RTs are present in a variety of mobile elements, including retrotransposons, retroviruses, group II introns, bacterial msDNAs, hepadnaviruses, and Caulimoviruses.


:

Pssm-ID: 238825  Cd Length: 177  Bit Score: 194.74  E-value: 3.74e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552208978  569 KDHFPLPFIDQVLERVSGHPFYCFF-GYSGYFQIEIDVADQEKTTFTCPFGTYAYRRMPFGLCNAPATFQRCMLSIFSDM 647
Cdd:cd01647     39 KDRYPLPTIDELLEELAGAKVFSKLdLRSGYHQIPLAEESRPKTAFRTPFGLYEYTRMPFGLKNAPATFQRLMNKILGDL 118
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1552208978  648 VERIMEVFMDDITVYGGTFEECLVNLEAVLHRCIEKDLVLNWEKCHFMVRQGIVLGHII 706
Cdd:cd01647    119 LGDFVEVYLDDILVYSKTEEEHLEHLREVLERLREAGLKLNPEKCEFGVPEVEFLGHIV 177
retropepsin_like cd00303
Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate ...
327-400 5.04e-05

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: 43.09  E-value: 5.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552208978  327 DPGSpTISVM-------IGG----KPTAITLSLADRSEN-SKGVIEDVLVQVDNFYYPVDFIVLDTDPtvkeanlVPIIL 394
Cdd:cd00303     15 DSGA-SVNFIseslakkLGLpprlLPTPLKVKGANGSSVkTLGVILPVTIGIGGKTFTVDFYVLDLLS-------YDVIL 86

                   ....*.
gi 1552208978  395 GRPFLA 400
Cdd:cd00303     87 GRPWLE 92
 
Name Accession Description Interval E-value
RNase_HI_RT_Ty3 cd09274
Ty3/Gypsy family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) ...
800-919 2.08e-64

Ty3/Gypsy family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes. RNase HI has also been observed as adjunct domains to the reverse transcriptase gene in retroviruses, in long-term repeat (LTR)-bearing retrotransposons and non-LTR retrotransposons. RNase HI in LTR retrotransposons perform degradation of the original RNA template, generation of a polypurine tract (the primer for plus-strand DNA synthesis), and final removal of RNA primers from newly synthesized minus and plus strands. The catalytic residues for RNase H enzymatic activity, three aspartatic acids and one glutamic acid residue (DEDD), are unvaried across all RNase H domains. Phylogenetic patterns of RNase HI of LTR retroelements is classified into five major families, Ty3/Gypsy, Ty1/Copia, Bel/Pao, DIRS1 and the vertebrate retroviruses. Ty3/Gypsy family widely distributed among the genomes of plants, fungi and animals. RNase H inhibitors have been explored as an anti-HIV drug target because RNase H inactivation inhibits reverse transcription.


Pssm-ID: 260006 [Multi-domain]  Cd Length: 121  Bit Score: 212.74  E-value: 2.08e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552208978  800 ELMCDASDFAIGAVLGQR-EDGKPYVIYYASKTLNEAQRNYTTTEKELLAVVFALDKFRAYLVGSFIIVFTDHSALKYLL 878
Cdd:cd09274      1 ILETDASDYGIGAVLSQEdDDGKERPIAFFSRKLTPAERNYSTTEKELLAIVWALKKFRHYLLGRPFTVYTDHKALKYLL 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1552208978  879 TKQDAKARLIRWILLLQEFDLQIKDKKGVENVVADHLSRLV 919
Cdd:cd09274     81 TQKDLNGRLARWLLLLSEFDFEIEYRPGKENVVADALSRLP 121
RT_LTR cd01647
RT_LTR: Reverse transcriptases (RTs) from retrotransposons and retroviruses which have long ...
569-706 3.74e-57

RT_LTR: Reverse transcriptases (RTs) from retrotransposons and retroviruses which have long terminal repeats (LTRs) in their DNA copies but not in their RNA template. RT catalyzes DNA replication from an RNA template, and is responsible for the replication of retroelements. An RT gene is usually indicative of a mobile element such as a retrotransposon or retrovirus. RTs are present in a variety of mobile elements, including retrotransposons, retroviruses, group II introns, bacterial msDNAs, hepadnaviruses, and Caulimoviruses.


Pssm-ID: 238825  Cd Length: 177  Bit Score: 194.74  E-value: 3.74e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552208978  569 KDHFPLPFIDQVLERVSGHPFYCFF-GYSGYFQIEIDVADQEKTTFTCPFGTYAYRRMPFGLCNAPATFQRCMLSIFSDM 647
Cdd:cd01647     39 KDRYPLPTIDELLEELAGAKVFSKLdLRSGYHQIPLAEESRPKTAFRTPFGLYEYTRMPFGLKNAPATFQRLMNKILGDL 118
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1552208978  648 VERIMEVFMDDITVYGGTFEECLVNLEAVLHRCIEKDLVLNWEKCHFMVRQGIVLGHII 706
Cdd:cd01647    119 LGDFVEVYLDDILVYSKTEEEHLEHLREVLERLREAGLKLNPEKCEFGVPEVEFLGHIV 177
RT_RNaseH pfam17917
RNase H-like domain found in reverse transcriptase; DNA polymerase and ribonuclease H (RNase H) ...
794-896 2.95e-46

RNase H-like domain found in reverse transcriptase; DNA polymerase and ribonuclease H (RNase H) activities allow reverse transcriptases to convert the single-stranded retroviral RNA genome into double-stranded DNA, which is integrated into the host chromosome during infection. This entry represents the RNase H like domain.


Pssm-ID: 465565  Cd Length: 104  Bit Score: 160.75  E-value: 2.95e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552208978  794 NWQLPFELMCDASDFAIGAVLGQR-EDGKPYVIYYASKTLNEAQRNYTTTEKELLAVVFALDKFRAYLVGSFIIVFTDHS 872
Cdd:pfam17917    1 DPSKPFILETDASDYGIGAVLSQKdEDGKERPIAYASRKLTPAERNYSTTEKELLAIVWALKKFRHYLLGRKFTVYTDHK 80
                           90       100
                   ....*....|....*....|....
gi 1552208978  873 ALKYLLTKQDAKARLIRWILLLQE 896
Cdd:pfam17917   81 PLKYLFTPKELNGRLARWALFLQE 104
RVT_1 pfam00078
Reverse transcriptase (RNA-dependent DNA polymerase); A reverse transcriptase gene is usually ...
552-706 1.33e-20

Reverse transcriptase (RNA-dependent DNA polymerase); A reverse transcriptase gene is usually indicative of a mobile element such as a retrotransposon or retrovirus. Reverse transcriptases occur in a variety of mobile elements, including retrotransposons, retroviruses, group II introns, bacterial msDNAs, hepadnaviruses, and caulimoviruses.


Pssm-ID: 395031 [Multi-domain]  Cd Length: 189  Bit Score: 90.44  E-value: 1.33e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552208978  552 LKLLQAsLFTLYLIALGKDHFPLPFIDQVLERVSGHPFYCFFG-YSGYFQIEIDVADQEKTTFTCP-----------FGT 619
Cdd:pfam00078   19 YKALNK-IIVKRLKPENLDSPPQPGFRPGLAKLKKAKWFLKLDlKKAFDQVPLDELDRKLTAFTTPpininwngelsGGR 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552208978  620 YAYRRMPFGLCNAPATFQRCMLSIFSDMVERI---MEVFMDDITVYGGTFEECLVNLEAVLHRCIEKDLVLNWEKCHFMV 696
Cdd:pfam00078   98 YEWKGLPQGLVLSPALFQLFMNELLRPLRKRAgltLVRYADDILIFSKSEEEHQEALEEVLEWLKESGLKINPEKTQFFL 177
                          170
                   ....*....|..
gi 1552208978  697 RQGIV--LGHII 706
Cdd:pfam00078  178 KSKEVkyLGVTL 189
retropepsin_like cd00303
Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate ...
327-400 5.04e-05

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: 43.09  E-value: 5.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552208978  327 DPGSpTISVM-------IGG----KPTAITLSLADRSEN-SKGVIEDVLVQVDNFYYPVDFIVLDTDPtvkeanlVPIIL 394
Cdd:cd00303     15 DSGA-SVNFIseslakkLGLpprlLPTPLKVKGANGSSVkTLGVILPVTIGIGGKTFTVDFYVLDLLS-------YDVIL 86

                   ....*.
gi 1552208978  395 GRPFLA 400
Cdd:cd00303     87 GRPWLE 92
 
Name Accession Description Interval E-value
RNase_HI_RT_Ty3 cd09274
Ty3/Gypsy family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) ...
800-919 2.08e-64

Ty3/Gypsy family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes. RNase HI has also been observed as adjunct domains to the reverse transcriptase gene in retroviruses, in long-term repeat (LTR)-bearing retrotransposons and non-LTR retrotransposons. RNase HI in LTR retrotransposons perform degradation of the original RNA template, generation of a polypurine tract (the primer for plus-strand DNA synthesis), and final removal of RNA primers from newly synthesized minus and plus strands. The catalytic residues for RNase H enzymatic activity, three aspartatic acids and one glutamic acid residue (DEDD), are unvaried across all RNase H domains. Phylogenetic patterns of RNase HI of LTR retroelements is classified into five major families, Ty3/Gypsy, Ty1/Copia, Bel/Pao, DIRS1 and the vertebrate retroviruses. Ty3/Gypsy family widely distributed among the genomes of plants, fungi and animals. RNase H inhibitors have been explored as an anti-HIV drug target because RNase H inactivation inhibits reverse transcription.


Pssm-ID: 260006 [Multi-domain]  Cd Length: 121  Bit Score: 212.74  E-value: 2.08e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552208978  800 ELMCDASDFAIGAVLGQR-EDGKPYVIYYASKTLNEAQRNYTTTEKELLAVVFALDKFRAYLVGSFIIVFTDHSALKYLL 878
Cdd:cd09274      1 ILETDASDYGIGAVLSQEdDDGKERPIAFFSRKLTPAERNYSTTEKELLAIVWALKKFRHYLLGRPFTVYTDHKALKYLL 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1552208978  879 TKQDAKARLIRWILLLQEFDLQIKDKKGVENVVADHLSRLV 919
Cdd:cd09274     81 TQKDLNGRLARWLLLLSEFDFEIEYRPGKENVVADALSRLP 121
RT_LTR cd01647
RT_LTR: Reverse transcriptases (RTs) from retrotransposons and retroviruses which have long ...
569-706 3.74e-57

RT_LTR: Reverse transcriptases (RTs) from retrotransposons and retroviruses which have long terminal repeats (LTRs) in their DNA copies but not in their RNA template. RT catalyzes DNA replication from an RNA template, and is responsible for the replication of retroelements. An RT gene is usually indicative of a mobile element such as a retrotransposon or retrovirus. RTs are present in a variety of mobile elements, including retrotransposons, retroviruses, group II introns, bacterial msDNAs, hepadnaviruses, and Caulimoviruses.


Pssm-ID: 238825  Cd Length: 177  Bit Score: 194.74  E-value: 3.74e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552208978  569 KDHFPLPFIDQVLERVSGHPFYCFF-GYSGYFQIEIDVADQEKTTFTCPFGTYAYRRMPFGLCNAPATFQRCMLSIFSDM 647
Cdd:cd01647     39 KDRYPLPTIDELLEELAGAKVFSKLdLRSGYHQIPLAEESRPKTAFRTPFGLYEYTRMPFGLKNAPATFQRLMNKILGDL 118
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1552208978  648 VERIMEVFMDDITVYGGTFEECLVNLEAVLHRCIEKDLVLNWEKCHFMVRQGIVLGHII 706
Cdd:cd01647    119 LGDFVEVYLDDILVYSKTEEEHLEHLREVLERLREAGLKLNPEKCEFGVPEVEFLGHIV 177
RT_RNaseH pfam17917
RNase H-like domain found in reverse transcriptase; DNA polymerase and ribonuclease H (RNase H) ...
794-896 2.95e-46

RNase H-like domain found in reverse transcriptase; DNA polymerase and ribonuclease H (RNase H) activities allow reverse transcriptases to convert the single-stranded retroviral RNA genome into double-stranded DNA, which is integrated into the host chromosome during infection. This entry represents the RNase H like domain.


Pssm-ID: 465565  Cd Length: 104  Bit Score: 160.75  E-value: 2.95e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552208978  794 NWQLPFELMCDASDFAIGAVLGQR-EDGKPYVIYYASKTLNEAQRNYTTTEKELLAVVFALDKFRAYLVGSFIIVFTDHS 872
Cdd:pfam17917    1 DPSKPFILETDASDYGIGAVLSQKdEDGKERPIAYASRKLTPAERNYSTTEKELLAIVWALKKFRHYLLGRKFTVYTDHK 80
                           90       100
                   ....*....|....*....|....
gi 1552208978  873 ALKYLLTKQDAKARLIRWILLLQE 896
Cdd:pfam17917   81 PLKYLFTPKELNGRLARWALFLQE 104
RT_RNaseH_2 pfam17919
RNase H-like domain found in reverse transcriptase;
769-867 6.01e-41

RNase H-like domain found in reverse transcriptase;


Pssm-ID: 465567 [Multi-domain]  Cd Length: 100  Bit Score: 145.72  E-value: 6.01e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552208978  769 WDERCQNSFDQLKKFLTTTPIVRAPNWQLPFELMCDASDFAIGAVLGQR-EDGKPYVIYYASKTLNEAQRNYTTTEKELL 847
Cdd:pfam17919    1 WTEECQKAFEKLKQALTSAPVLAHPDPDKPFILETDASDYGIGAVLSQEdDDGGERPIAYASRKLSPAERNYSTTEKELL 80
                           90       100
                   ....*....|....*....|
gi 1552208978  848 AVVFALDKFRAYLVGSFIIV 867
Cdd:pfam17919   81 AIVFALKKFRHYLLGRKFTV 100
RVT_1 pfam00078
Reverse transcriptase (RNA-dependent DNA polymerase); A reverse transcriptase gene is usually ...
552-706 1.33e-20

Reverse transcriptase (RNA-dependent DNA polymerase); A reverse transcriptase gene is usually indicative of a mobile element such as a retrotransposon or retrovirus. Reverse transcriptases occur in a variety of mobile elements, including retrotransposons, retroviruses, group II introns, bacterial msDNAs, hepadnaviruses, and caulimoviruses.


Pssm-ID: 395031 [Multi-domain]  Cd Length: 189  Bit Score: 90.44  E-value: 1.33e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552208978  552 LKLLQAsLFTLYLIALGKDHFPLPFIDQVLERVSGHPFYCFFG-YSGYFQIEIDVADQEKTTFTCP-----------FGT 619
Cdd:pfam00078   19 YKALNK-IIVKRLKPENLDSPPQPGFRPGLAKLKKAKWFLKLDlKKAFDQVPLDELDRKLTAFTTPpininwngelsGGR 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552208978  620 YAYRRMPFGLCNAPATFQRCMLSIFSDMVERI---MEVFMDDITVYGGTFEECLVNLEAVLHRCIEKDLVLNWEKCHFMV 696
Cdd:pfam00078   98 YEWKGLPQGLVLSPALFQLFMNELLRPLRKRAgltLVRYADDILIFSKSEEEHQEALEEVLEWLKESGLKINPEKTQFFL 177
                          170
                   ....*....|..
gi 1552208978  697 RQGIV--LGHII 706
Cdd:pfam00078  178 KSKEVkyLGVTL 189
RNase_HI_RT_DIRS1 cd09275
DIRS1 family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) enzymes ...
800-918 3.00e-11

DIRS1 family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes. RNase HI has also been observed as adjunct domains to the reverse transcriptase gene in retroviruses, in long-term repeat (LTR)-bearing retrotransposons and non-LTR retrotransposons. RNase HI in LTR retrotransposons perform degradation of the original RNA template, generation of a polypurine tract (the primer for plus-strand DNA synthesis), and final removal of RNA primers from newly synthesized minus and plus strands. The catalytic residues for RNase H enzymatic activity, three aspartatic acids and one glutamic acid residue (DEDD), are unvaried across all RNase H domains. Phylogenetic patterns of RNase HI of LTR retroelements is classified into five major families, Ty3/Gypsy, Ty1/Copia, Bel/Pao, DIRS1 and the vertebrate retroviruses. The structural features of DIRS1-group elements are different from typical LTR elements. RNase H inhibitors have been explored as an anti-HIV drug target because RNase H inactivation inhibits reverse transcription.


Pssm-ID: 260007  Cd Length: 120  Bit Score: 61.53  E-value: 3.00e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552208978  800 ELMCDASDFAIGAVLGQREDGKPYviyyasktlNEAQRNYTTTEKELLAVVFALDKFRAYLVGSFIIVFTDH-SALKYLL 878
Cdd:cd09275      1 VLFTDASLSGWGAYLLNSRAHGPW---------SADERNKHINLLELKAVLLALQHFAAELKNRKILIRTDNtTAVAYIN 71
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1552208978  879 ----TKQDAKARLIRWILLL-QEFDLQIKDK--KGVENVVADHLSRL 918
Cdd:cd09275     72 kqggTSSPPLLALARQILLWcEQRNIWLRAShiPGVLNTEADRLSRL 118
retropepsin_like cd00303
Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate ...
327-400 5.04e-05

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: 43.09  E-value: 5.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552208978  327 DPGSpTISVM-------IGG----KPTAITLSLADRSEN-SKGVIEDVLVQVDNFYYPVDFIVLDTDPtvkeanlVPIIL 394
Cdd:cd00303     15 DSGA-SVNFIseslakkLGLpprlLPTPLKVKGANGSSVkTLGVILPVTIGIGGKTFTVDFYVLDLLS-------YDVIL 86

                   ....*.
gi 1552208978  395 GRPFLA 400
Cdd:cd00303     87 GRPWLE 92
RT_DIRS1 cd03714
RT_DIRS1: Reverse transcriptases (RTs) occurring in the DIRS1 group of retransposons. Members ...
596-706 6.67e-05

RT_DIRS1: Reverse transcriptases (RTs) occurring in the DIRS1 group of retransposons. Members of the subfamily include the Dictyostelium DIRS-1, Volvox carteri kangaroo, and Panagrellus redivivus PAT elements. These elements differ from LTR and conventional non-LTR retrotransposons. They contain split direct repeat (SDR) termini, and have been proposed to integrate via double-stranded closed-circle DNA intermediates assisted by an encoded recombinase which is similar to gamma-site-specific integrase.


Pssm-ID: 239684 [Multi-domain]  Cd Length: 119  Bit Score: 43.49  E-value: 6.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552208978  596 SGYFQIEIDvaDQEKTTFTCPFG--TYAYRRMPFGLCNAPATFQRCMLSIFSDMVERIMEVF--MDDITVYGGTFEEClv 671
Cdd:cd03714      5 DAYFHIPIL--PRSRDLLGFAWQgeTYQFKALPFGLSLAPRVFTKVVEALLAPLRLLGVRIFsyLDDLLIIASSIKTS-- 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1552208978  672 nlEAVL-----HRCIEKDLVLNWEKCHFMVRQGIVLGHII 706
Cdd:cd03714     81 --EAVLrhlraTLLANLGFTLNLEKSKLGPTQRITFLGLE 118
RT_like cd00304
RT_like: Reverse transcriptase (RT, RNA-dependent DNA polymerase)_like family. An RT gene is ...
624-706 9.60e-03

RT_like: Reverse transcriptase (RT, RNA-dependent DNA polymerase)_like family. An RT gene is usually indicative of a mobile element such as a retrotransposon or retrovirus. RTs occur in a variety of mobile elements, including retrotransposons, retroviruses, group II introns, bacterial msDNAs, hepadnaviruses, and caulimoviruses. These elements can be divided into two major groups. One group contains retroviruses and DNA viruses whose propagation involves an RNA intermediate. They are grouped together with transposable elements containing long terminal repeats (LTRs). The other group, also called poly(A)-type retrotransposons, contain fungal mitochondrial introns and transposable elements that lack LTRs.


Pssm-ID: 238185 [Multi-domain]  Cd Length: 98  Bit Score: 36.56  E-value: 9.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552208978  624 RMPFGLCNAPATFQRCMLSIFSDMVERIMEVFM----DDItVYGGTFEECLVNLEAVLHRCIEKDLVLNWEKCHFMVRQG 699
Cdd:cd00304     11 PLPQGSPLSPALANLYMEKLEAPILKQLLDITLiryvDDL-VVIAKSEQQAVKKRELEEFLARLGLNLSDEKTQFTEKEK 89

                   ....*....
gi 1552208978  700 IV--LGHII 706
Cdd:cd00304     90 KFkfLGILV 98
 
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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