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Conserved domains on  [gi|1040460679|emb|SBO19446|]
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RT-prot, partial [HIV-1 M:G_BA233]

Protein Classification

pol protein( domain architecture ID 20399044)

HIV-1 pol protein containing the pepsin-like aspartate protease, reverse transcriptase (RT), and RT thumb domains; RT catalyzes the conversion of single-stranded RNA into double-stranded DNA for integration into host chromosomes

CATH:  3.10.10.10|2.40.70.10
EC:  2.7.7.49
Gene Ontology:  GO:0003964|GO:0004190|GO:0006508
MEROPS:  A2
PubMed:  1698615|2194475|7674916
SCOP:  4002796|4002288

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ps-ssRNAv_RdRp-like super family cl40470
conserved catalytic core domain of RNA-dependent RNA polymerase (RdRp) from the positive-sense ...
 117-333 1.26e-112

conserved catalytic core domain of RNA-dependent RNA polymerase (RdRp) from the positive-sense single-stranded RNA [(+)ssRNA] viruses and closely related viruses; This family contains the catalytic core domain of RdRp of RNA viruses which belong to Group IV of the Baltimore classification system, and are a group of related viruses that have positive-sense (+), single-stranded (ss) genomes made of ribonucleic acid (RNA). RdRp (also known as RNA replicase) catalyzes the replication of RNA from an RNA template; specifically, it catalyzes the synthesis of the RNA strand complementary to a given RNA template. The Baltimore Classification is divided into 7 classes, 3 of which include RNA viruses: Group IV (+) RNA viruses, Group III double-stranded (ds) RNA viruses, and Group V negative-sense (-) RNA viruses. Baltimore groups of viruses differ with respect to the nature of their genome (i.e., the nucleic acid form that is packaged into virions) and correspond to distinct strategies of genome replication and expression. (+) viral RNA is similar to mRNA and thus can be immediately translated by the host cell. (+)ssRNA viruses can also produce (+) copies of the genome from (-) strands of an intermediate dsRNA genome. This acts as both a transcription and a replication process since the replicated RNA is also mRNA. RdRps belong to the expansive class of polymerases containing so-called palm catalytic domains along with the accessory fingers and thumb domains. All RdRps also have six conserved structural motifs (A-F), located in its majority in the palm subdomain (A-E motifs) and the F motif is located on the finger subdomain. All these motifs have been shown to be implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides. In addition to Group IV viruses, this model also includes Picobirnaviruses (PBVs), members of the family Picobirnaviridae of dsRNA viruses (Baltimore classification Group III), which are bi-segmented dsRNA viruses. The phylogenetic tree of the RdRps of RNA viruses (realm Riboviria) showed that picobirnaviruses are embedded in the branch of diverse (+)RNA viruses; sometimes they are collectively referred to as the picornavirus supergroup. RdRps of members of the family Permutatetraviridae, a distinct group of RNA viruses that encompass a circular permutation within the RdRp palm domain, are not included in this model.


The actual alignment was detected with superfamily member cd01645:

Pssm-ID: 477363 [Multi-domain]  Cd Length: 213  Bit Score: 329.24  E-value: 1.26e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040460679 117 GPKVKQWPLTEEKIKALTEICNDMEKEGKISRIGpeNPYNTP*FAIKKKDStKWRK*VDFRELNKRTQDFWEVQLGIPHP 196
Cdd:cd01645     1 PVWIKQWPLTEEKLEALTELVTEQLKEGHIEPST--SPWNTPVFVIKKKSG-KWRLLHDLRAVNAQTQDMGALQPGLPHP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040460679 197 AGLKKNRSVTVLDVGDAYFSVPLDEEFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMJKILEPFRTKNPE 276
Cdd:cd01645    78 AALPKGWPLIVLDLKDCFFSIPLHPDDRERFAFTVPSINNKGPAKRYQWKVLPQGMKNSPTICQSFVAQALEPFRKQYPD 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1040460679 277 *VICQY*DDLYVGSDLEiGQHRAKIEELRBHLLKWGFTTPDKKYQKEPPFLWMGYEL 333
Cdd:cd01645   158 IVIYHYMDDILIASDLE-GQLREIYEELRQTLLRWGLTIPPEKVQKEPPFQYLGYEL 213
RVP pfam00077
Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, ...
 5-98 8.78e-32

Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, retrotransposons, and badnaviruses (plant dsDNA viruses). These proteases are generally part of a larger polyprotein; usually pol, more rarely gag. Retroviral proteases appear to be homologous to a single domain of the two-domain eukaryotic aspartyl proteases such as pepsins, cathepsins, and renins (pfam00026).


:

Pssm-ID: 425454  Cd Length: 101  Bit Score: 116.70  E-value: 8.78e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040460679   5 LWQRPLVTVKVGGQIIEALLDTGADDTVLEDIDLPGRW----KPKMIGGIGGFIKV*QYDQIPJEISGKRAIGTV--LVG 78
Cdd:pfam00077   1 AEQRPLLTVKIGGKYFTALLDTGADDTVISQNDWPTNWpkqkATTNIQGIGGGINVRQSDQILILIGEDKFRGTVspLIL 80

                          90       100
                  ....*....|....*....|.
gi 1040460679  79 PT-PINIIGRNMLTQIGCTLN 98
Cdd:pfam00077  81 PTcPVNIIGRDLLQQLGGRLT 101
RVT_thumb pfam06817
Reverse transcriptase thumb domain; This domain is known as the thumb domain. It is composed ...
 340-403 5.16e-21

Reverse transcriptase thumb domain; This domain is known as the thumb domain. It is composed of a four helix bundle.


:

Pssm-ID: 429135  Cd Length: 66  Bit Score: 86.22  E-value: 5.16e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1040460679 340 VQPINLPEKDSWTVNDIQKLVGKLNWASQIY*--GIKVKQLCRLLRGTKALTDIVPLT*EAELELA 403
Cdd:pfam06817   1 PQKLQLRKDHLKTLNDFQKLLGDINWIRPYLGitTYDLKPLFSLLRGDSDLTSPRTLTEEAEEALQ 66
 
Name Accession Description Interval E-value
RT_Rtv cd01645
RT_Rtv: Reverse transcriptases (RTs) from retroviruses (Rtvs). RTs catalyze the conversion of ...
 117-333 1.26e-112

RT_Rtv: Reverse transcriptases (RTs) from retroviruses (Rtvs). RTs catalyze the conversion of single-stranded RNA into double-stranded viral DNA for integration into host chromosomes. Proteins in this subfamily contain long terminal repeats (LTRs) and are multifunctional enzymes with RNA-directed DNA polymerase, DNA directed DNA polymerase, and ribonuclease hybrid (RNase H) activities. The viral RNA genome enters the cytoplasm as part of a nucleoprotein complex, and the process of reverse transcription generates in the cytoplasm forming a linear DNA duplex via an intricate series of steps. This duplex DNA is colinear with its RNA template, but contains terminal duplications known as LTRs that are not present in viral RNA. It has been proposed that two specialized template switches, known as strand-transfer reactions or "jumps", are required to generate the LTRs.


Pssm-ID: 238823 [Multi-domain]  Cd Length: 213  Bit Score: 329.24  E-value: 1.26e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040460679 117 GPKVKQWPLTEEKIKALTEICNDMEKEGKISRIGpeNPYNTP*FAIKKKDStKWRK*VDFRELNKRTQDFWEVQLGIPHP 196
Cdd:cd01645     1 PVWIKQWPLTEEKLEALTELVTEQLKEGHIEPST--SPWNTPVFVIKKKSG-KWRLLHDLRAVNAQTQDMGALQPGLPHP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040460679 197 AGLKKNRSVTVLDVGDAYFSVPLDEEFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMJKILEPFRTKNPE 276
Cdd:cd01645    78 AALPKGWPLIVLDLKDCFFSIPLHPDDRERFAFTVPSINNKGPAKRYQWKVLPQGMKNSPTICQSFVAQALEPFRKQYPD 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1040460679 277 *VICQY*DDLYVGSDLEiGQHRAKIEELRBHLLKWGFTTPDKKYQKEPPFLWMGYEL 333
Cdd:cd01645   158 IVIYHYMDDILIASDLE-GQLREIYEELRQTLLRWGLTIPPEKVQKEPPFQYLGYEL 213
RVT_1 pfam00078
Reverse transcriptase (RNA-dependent DNA polymerase); A reverse transcriptase gene is usually ...
 162-333 6.94e-43

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: 148.99  E-value: 6.94e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040460679 162 IKKKDSTKWR----K*VDFRELNKRTQD-------FWEVQLGIPHPAG-LKKNRSVTVLDVGDAYFSVPLDEEFRKYTAF 229
Cdd:pfam00078   1 IPKKGKGKYRpislLSIDYKALNKIIVKrlkpenlDSPPQPGFRPGLAkLKKAKWFLKLDLKKAFDQVPLDELDRKLTAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040460679 230 TIPSINN----ETPGIRYQYNVLPQGWKGSPAIFQSSMJKILEPFRTKnPE*VICQY*DDLYVGSDlEIGQHRAKIEELR 305
Cdd:pfam00078  81 TTPPINInwngELSGGRYEWKGLPQGLVLSPALFQLFMNELLRPLRKR-AGLTLVRYADDILIFSK-SEEEHQEALEEVL 158

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1040460679 306 BHLLKWGFTTPDKK---YQKEPPFLWMGYEL 333
Cdd:pfam00078 159 EWLKESGLKINPEKtqfFLKSKEVKYLGVTL 189
RVP pfam00077
Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, ...
 5-98 8.78e-32

Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, retrotransposons, and badnaviruses (plant dsDNA viruses). These proteases are generally part of a larger polyprotein; usually pol, more rarely gag. Retroviral proteases appear to be homologous to a single domain of the two-domain eukaryotic aspartyl proteases such as pepsins, cathepsins, and renins (pfam00026).


Pssm-ID: 425454  Cd Length: 101  Bit Score: 116.70  E-value: 8.78e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040460679   5 LWQRPLVTVKVGGQIIEALLDTGADDTVLEDIDLPGRW----KPKMIGGIGGFIKV*QYDQIPJEISGKRAIGTV--LVG 78
Cdd:pfam00077   1 AEQRPLLTVKIGGKYFTALLDTGADDTVISQNDWPTNWpkqkATTNIQGIGGGINVRQSDQILILIGEDKFRGTVspLIL 80

                          90       100
                  ....*....|....*....|.
gi 1040460679  79 PT-PINIIGRNMLTQIGCTLN 98
Cdd:pfam00077  81 PTcPVNIIGRDLLQQLGGRLT 101
HIV_retropepsin_like cd05482
Retropepsins, pepsin-like aspartate proteases; This is a subfamily of retropepsins. The family ...
 11-91 6.26e-23

Retropepsins, pepsin-like aspartate proteases; This is a subfamily of retropepsins. The family includes pepsin-like aspartate proteases from retroviruses, retrotransposons and retroelements. While fungal and mammalian pepsins are bilobal proteins with structurally related N- and C-termini, 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: 133149  Cd Length: 87  Bit Score: 91.94  E-value: 6.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040460679  11 VTVKVGGQIIEALLDTGADDTVLEDIDLPGRW----KPKMIGGIGGFIKV*QYDQIPJEISGKRAIGTVLVGP--TPINI 84
Cdd:cd05482     1 LTLYINGKLFEGLLDTGADVSIIAENDWPKNWpiqpAPSNLTGIGGAITPSQSSVLLLEIDGEGHLGTILVYVlsLPVNL 80


                  ....*..
gi 1040460679  85 IGRNMLT 91
Cdd:cd05482    81 WGRDILS 87
RVT_thumb pfam06817
Reverse transcriptase thumb domain; This domain is known as the thumb domain. It is composed ...
 340-403 5.16e-21

Reverse transcriptase thumb domain; This domain is known as the thumb domain. It is composed of a four helix bundle.


Pssm-ID: 429135  Cd Length: 66  Bit Score: 86.22  E-value: 5.16e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1040460679 340 VQPINLPEKDSWTVNDIQKLVGKLNWASQIY*--GIKVKQLCRLLRGTKALTDIVPLT*EAELELA 403
Cdd:pfam06817   1 PQKLQLRKDHLKTLNDFQKLLGDINWIRPYLGitTYDLKPLFSLLRGDSDLTSPRTLTEEAEEALQ 66
COG3577 COG3577
Predicted aspartyl protease [General function prediction only];
1-33 8.21e-03

Predicted aspartyl protease [General function prediction only];


Pssm-ID: 442797  Cd Length: 152  Bit Score: 36.85  E-value: 8.21e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1040460679   1 PQITLWQRP----LVTVKVGGQIIEALLDTGADDTVL 33
Cdd:COG3577    30 GEVVLKRDRdghfVVEGTINGQPVRFLVDTGASTVVL 66
 
Name Accession Description Interval E-value
RT_Rtv cd01645
RT_Rtv: Reverse transcriptases (RTs) from retroviruses (Rtvs). RTs catalyze the conversion of ...
 117-333 1.26e-112

RT_Rtv: Reverse transcriptases (RTs) from retroviruses (Rtvs). RTs catalyze the conversion of single-stranded RNA into double-stranded viral DNA for integration into host chromosomes. Proteins in this subfamily contain long terminal repeats (LTRs) and are multifunctional enzymes with RNA-directed DNA polymerase, DNA directed DNA polymerase, and ribonuclease hybrid (RNase H) activities. The viral RNA genome enters the cytoplasm as part of a nucleoprotein complex, and the process of reverse transcription generates in the cytoplasm forming a linear DNA duplex via an intricate series of steps. This duplex DNA is colinear with its RNA template, but contains terminal duplications known as LTRs that are not present in viral RNA. It has been proposed that two specialized template switches, known as strand-transfer reactions or "jumps", are required to generate the LTRs.


Pssm-ID: 238823 [Multi-domain]  Cd Length: 213  Bit Score: 329.24  E-value: 1.26e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040460679 117 GPKVKQWPLTEEKIKALTEICNDMEKEGKISRIGpeNPYNTP*FAIKKKDStKWRK*VDFRELNKRTQDFWEVQLGIPHP 196
Cdd:cd01645     1 PVWIKQWPLTEEKLEALTELVTEQLKEGHIEPST--SPWNTPVFVIKKKSG-KWRLLHDLRAVNAQTQDMGALQPGLPHP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040460679 197 AGLKKNRSVTVLDVGDAYFSVPLDEEFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMJKILEPFRTKNPE 276
Cdd:cd01645    78 AALPKGWPLIVLDLKDCFFSIPLHPDDRERFAFTVPSINNKGPAKRYQWKVLPQGMKNSPTICQSFVAQALEPFRKQYPD 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1040460679 277 *VICQY*DDLYVGSDLEiGQHRAKIEELRBHLLKWGFTTPDKKYQKEPPFLWMGYEL 333
Cdd:cd01645   158 IVIYHYMDDILIASDLE-GQLREIYEELRQTLLRWGLTIPPEKVQKEPPFQYLGYEL 213
RVT_1 pfam00078
Reverse transcriptase (RNA-dependent DNA polymerase); A reverse transcriptase gene is usually ...
 162-333 6.94e-43

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: 148.99  E-value: 6.94e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040460679 162 IKKKDSTKWR----K*VDFRELNKRTQD-------FWEVQLGIPHPAG-LKKNRSVTVLDVGDAYFSVPLDEEFRKYTAF 229
Cdd:pfam00078   1 IPKKGKGKYRpislLSIDYKALNKIIVKrlkpenlDSPPQPGFRPGLAkLKKAKWFLKLDLKKAFDQVPLDELDRKLTAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040460679 230 TIPSINN----ETPGIRYQYNVLPQGWKGSPAIFQSSMJKILEPFRTKnPE*VICQY*DDLYVGSDlEIGQHRAKIEELR 305
Cdd:pfam00078  81 TTPPINInwngELSGGRYEWKGLPQGLVLSPALFQLFMNELLRPLRKR-AGLTLVRYADDILIFSK-SEEEHQEALEEVL 158

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1040460679 306 BHLLKWGFTTPDKK---YQKEPPFLWMGYEL 333
Cdd:pfam00078 159 EWLKESGLKINPEKtqfFLKSKEVKYLGVTL 189
RVP pfam00077
Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, ...
 5-98 8.78e-32

Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, retrotransposons, and badnaviruses (plant dsDNA viruses). These proteases are generally part of a larger polyprotein; usually pol, more rarely gag. Retroviral proteases appear to be homologous to a single domain of the two-domain eukaryotic aspartyl proteases such as pepsins, cathepsins, and renins (pfam00026).


Pssm-ID: 425454  Cd Length: 101  Bit Score: 116.70  E-value: 8.78e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040460679   5 LWQRPLVTVKVGGQIIEALLDTGADDTVLEDIDLPGRW----KPKMIGGIGGFIKV*QYDQIPJEISGKRAIGTV--LVG 78
Cdd:pfam00077   1 AEQRPLLTVKIGGKYFTALLDTGADDTVISQNDWPTNWpkqkATTNIQGIGGGINVRQSDQILILIGEDKFRGTVspLIL 80

                          90       100
                  ....*....|....*....|.
gi 1040460679  79 PT-PINIIGRNMLTQIGCTLN 98
Cdd:pfam00077  81 PTcPVNIIGRDLLQQLGGRLT 101
RT_ZFREV_like cd03715
RT_ZFREV_like: A subfamily of reverse transcriptases (RTs) found in sequences similar to the ...
 118-321 8.95e-30

RT_ZFREV_like: A subfamily of reverse transcriptases (RTs) found in sequences similar to the intact endogenous retrovirus ZFERV from zebrafish and to Moloney murine leukemia virus RT. 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. Phylogenetic analysis suggests that ZFERV belongs to a distinct group of retroviruses.


Pssm-ID: 239685 [Multi-domain]  Cd Length: 210  Bit Score: 114.75  E-value: 8.95e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040460679 118 PKVKQWPLTEEKIKALTEICNDMEKEGKIsrIGPENPYNTP*FAIKKKDSTKWRK*VDFRELNKRTQDfweVQLGIPHPA 197
Cdd:cd03715     2 VNQKQYPLPREAREGITPHIQELLEAGIL--VPCQSPWNTPILPVKKPGGNDYRMVQDLRLVNQAVLP---IHPAVPNPY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040460679 198 GL-----KKNRSVTVLDVGDAYFSVPLDEEFRKYTAFTIpsinnetPGIRYQYNVLPQGWKGSPAIFQSSMJKILEPFRT 272
Cdd:cd03715    77 TLlsllpPKHQWYTVLDLANAFFSLPLAPDSQPLFAFEW-------EGQQYTFTRLPQGFKNSPTLFHEALARDLAPFPL 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1040460679 273 KNPE*VICQY*DDLYVGSDLEIGQHRAKIEELRbHLLKWGFTTPDKKYQ 321
Cdd:cd03715   150 EHEGTILLQYVDDLLLAADSEEDCLKGTDALLT-HLGELGYKVSPKKAQ 197
RT_LTR cd01647
RT_LTR: Reverse transcriptases (RTs) from retrotransposons and retroviruses which have long ...
 154-310 9.97e-25

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: 99.98  E-value: 9.97e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040460679 154 PYNTP*FAIKKKDStKWRK*VDFRELNKRT-QDFWEvqlgIPHPAG----LKKNRSVTVLDVGDAYFSVPLDEEFRKYTA 228
Cdd:cd01647     9 PYASPVVVVKKKDG-KLRLCVDYRKLNKVTiKDRYP----LPTIDElleeLAGAKVFSKLDLRSGYHQIPLAEESRPKTA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040460679 229 FTipsinneTPGIRYQYNVLPQGWKGSPAIFQSSMJKILEPFRtknPE*VICqY*DDLYVGSDlEIGQHRAKIEE----L 304
Cdd:cd01647    84 FR-------TPFGLYEYTRMPFGLKNAPATFQRLMNKILGDLL---GDFVEV-YLDDILVYSK-TEEEHLEHLREvlerL 151


                  ....*.
gi 1040460679 305 RBHLLK 310
Cdd:cd01647   152 REAGLK 157
HIV_retropepsin_like cd05482
Retropepsins, pepsin-like aspartate proteases; This is a subfamily of retropepsins. The family ...
 11-91 6.26e-23

Retropepsins, pepsin-like aspartate proteases; This is a subfamily of retropepsins. The family includes pepsin-like aspartate proteases from retroviruses, retrotransposons and retroelements. While fungal and mammalian pepsins are bilobal proteins with structurally related N- and C-termini, 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: 133149  Cd Length: 87  Bit Score: 91.94  E-value: 6.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040460679  11 VTVKVGGQIIEALLDTGADDTVLEDIDLPGRW----KPKMIGGIGGFIKV*QYDQIPJEISGKRAIGTVLVGP--TPINI 84
Cdd:cd05482     1 LTLYINGKLFEGLLDTGADVSIIAENDWPKNWpiqpAPSNLTGIGGAITPSQSSVLLLEIDGEGHLGTILVYVlsLPVNL 80


                  ....*..
gi 1040460679  85 IGRNMLT 91
Cdd:cd05482    81 WGRDILS 87
RVT_thumb pfam06817
Reverse transcriptase thumb domain; This domain is known as the thumb domain. It is composed ...
 340-403 5.16e-21

Reverse transcriptase thumb domain; This domain is known as the thumb domain. It is composed of a four helix bundle.


Pssm-ID: 429135  Cd Length: 66  Bit Score: 86.22  E-value: 5.16e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1040460679 340 VQPINLPEKDSWTVNDIQKLVGKLNWASQIY*--GIKVKQLCRLLRGTKALTDIVPLT*EAELELA 403
Cdd:pfam06817   1 PQKLQLRKDHLKTLNDFQKLLGDINWIRPYLGitTYDLKPLFSLLRGDSDLTSPRTLTEEAEEALQ 66
RT_like cd00304
RT_like: Reverse transcriptase (RT, RNA-dependent DNA polymerase)_like family. An RT gene is ...
 248-333 5.27e-14

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: 67.38  E-value: 5.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040460679 248 LPQGWKGSPAIFQSSMJKILEPFRTKNPE*VICQY*DDLYVGSDLEigQHRAKIEELRBHLLKWGFTTPDKKYQ---KEP 324
Cdd:cd00304    12 LPQGSPLSPALANLYMEKLEAPILKQLLDITLIRYVDDLVVIAKSE--QQAVKKRELEEFLARLGLNLSDEKTQfteKEK 89


                  ....*....
gi 1040460679 325 PFLWMGYEL 333
Cdd:cd00304    90 KFKFLGILV 98
RT_DIRS1 cd03714
RT_DIRS1: Reverse transcriptases (RTs) occurring in the DIRS1 group of retransposons. Members ...
 208-324 2.91e-06

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: 46.18  E-value: 2.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040460679 208 LDVGDAYFSVPLDEEFRKYTAFtIPSinnetpGIRYQYNVLPQGWKGSPAIFQSSMJKILEPFRTKNpe*VICQY*DD-L 286
Cdd:cd03714     1 VDLKDAYFHIPILPRSRDLLGF-AWQ------GETYQFKALPFGLSLAPRVFTKVVEALLAPLRLLG--VRIFSYLDDlL 71

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1040460679 287 YVGSDLEIGQHRAKieELRBHLL-KWGFTTPDKKYQKEP 324
Cdd:cd03714    72 IIASSIKTSEAVLR--HLRATLLaNLGFTLNLEKSKLGP 108
RP_RTVL_H_like cd06095
Retropepsin of the RTVL_H family of human endogenous retrovirus-like elements; This family ...
 11-91 4.57e-06

Retropepsin of the RTVL_H family of human endogenous retrovirus-like elements; This family includes aspartate proteases from retroelements with LTR (long terminal repeats) including the RTVL_H family of human endogenous retrovirus-like elements. While fungal and mammalian pepsins are bilobal proteins with structurally related N- and C-termini, 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: 133159  Cd Length: 86  Bit Score: 44.63  E-value: 4.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040460679  11 VTVKVGGQIIEALLDTGADDTVL-EDIDLPGRWKPKMIGGIGgfikV*QYDQIPJE-------ISGKRAIGTVLVGPT-P 81
Cdd:cd06095     1 VTITVEGVPIVFLVDTGATHSVLkSDLGPKQELSTTSVLIRG----VSGQSQQPVTtyrtlvdLGGHTVSHSFLVVPNcP 76

                          90
                  ....*....|
gi 1040460679  82 INIIGRNMLT 91
Cdd:cd06095    77 DPLLGRDLLS 86
gag-asp_proteas pfam13975
gag-polyprotein putative aspartyl protease; This family of putative aspartyl proteases is ...
 11-92 2.11e-05

gag-polyprotein putative aspartyl protease; This family of putative aspartyl proteases is found pre-dominantly in retroviral proteins.


Pssm-ID: 464060  Cd Length: 92  Bit Score: 42.95  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040460679  11 VTVKVGGQIIEALLDTGADDTVL-------EDIDLPGRWKPKMIGGIGGFIKV*QY--DQI---PJEISGKRAigTVLVG 78
Cdd:pfam13975   1 VDVTINGRPVRFLVDTGASVTVIsealaerLGLDRLVDAYPVTVRTANGTVRAARVrlDSVkigGIELRNVPA--VVLPG 78

                          90
                  ....*....|....
gi 1040460679  79 PTPINIIGRNMLTQ 92
Cdd:pfam13975  79 DLDDVLLGMDFLKR 92
Asp_protease_2 pfam13650
Aspartyl protease; This family consists of predicted aspartic proteases, typically from 180 to ...
 11-88 4.50e-05

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: 41.89  E-value: 4.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040460679  11 VTVKVGGQIIEALLDTGADDTVL-----EDIDLPGRWK--PKMIGGIGGFIKV*QYDQIPJEISGKRAIG-TVLV---GP 79
Cdd:pfam13650   1 VPVTINGKPVRFLVDTGASGTVIspslaERLGLKVRGLayTVRVSTAGGRVSAARVRLDSLRLGGLTLENvPALVldlGD 80


                  ....*....
gi 1040460679  80 TPINIIGRN 88
Cdd:pfam13650  81 LIDGLLGMD 89
COG3577 COG3577
Predicted aspartyl protease [General function prediction only];
1-33 8.21e-03

Predicted aspartyl protease [General function prediction only];


Pssm-ID: 442797  Cd Length: 152  Bit Score: 36.85  E-value: 8.21e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1040460679   1 PQITLWQRP----LVTVKVGGQIIEALLDTGADDTVL 33
Cdd:COG3577    30 GEVVLKRDRdghfVVEGTINGQPVRFLVDTGASTVVL 66
 
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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