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Conserved domains on  [gi|1037179310|emb|SBO15624|]
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RT-prot, partial [HIV-1 M:H_BA201]

Protein Classification

pol protein pepsin-like aspartate protease and reverse transcriptase( domain architecture ID 20398964)

pol protein pepsin-like aspartate protease and reverse transcriptase; the retropepsin-like (A2 family) peptidase is an aspartic protease that hydrolyzes the peptide bonds of substrates

CATH:  2.40.70.10
MEROPS:  A2
PubMed:  2194475|7674916
SCOP:  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 ...
101-294 3.92e-99

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: 289.95  E-value: 3.92e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037179310 101 MEKEGKIS*IGpeNPYNTP*FAIKKKDStKWRKLVDFRELNKRTQDFWEVQLGIPHPAGLKKKKSV*VLDVGDAYFSVPL 180
Cdd:cd01645    24 QLKEGHIEPST--SPWNTPVFVIKKKSG-KWRLLHDLRAVNAQTQDMGALQPGLPHPAALPKGWPLIVLDLKDCFFSIPL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037179310 181 DEBFRKYTAFTIPS*NNETPGIRY*YNVLPQGWKGSPAIFQSSMTKILEPFRKQNP*IVIYQYMDDLYVGSDLEiGQHR* 260
Cdd:cd01645   101 HPDDRERFAFTVPSINNKGPAKRYQWKVLPQGMKNSPTICQSFVAQALEPFRKQYPDIVIYHYMDDILIASDLE-GQLRE 179
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1037179310 261 KIEELR*HLL*WG*TTPDKKHQKEPPFFWKGBEL 294
Cdd:cd01645   180 IYEELRQTLLRWGLTIPPEKVQKEPPFQYLGYEL 213
RVP pfam00077
Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, ...
5-98 2.45e-28

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: 104.76  E-value: 2.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037179310   5 LWQRPLVIVRIGEQLIEALLDTGADDTVLKEIDLTGRW----KPKMIGGIGGFIKVKQYENMTIEIEGKKAVGTV--LIG 78
Cdd:pfam00077   1 AEQRPLLTVKIGGKYFTALLDTGADDTVISQNDWPTNWpkqkATTNIQGIGGGINVRQSDQILILIGEDKFRGTVspLIL 80
                          90       100
                  ....*....|....*....|.
gi 1037179310  79 PT-PVNIIGRNMLTQIGCTLN 98
Cdd:pfam00077  81 PTcPVNIIGRDLLQQLGGRLT 101
 
Name Accession Description Interval E-value
RT_Rtv cd01645
RT_Rtv: Reverse transcriptases (RTs) from retroviruses (Rtvs). RTs catalyze the conversion of ...
101-294 3.92e-99

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: 289.95  E-value: 3.92e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037179310 101 MEKEGKIS*IGpeNPYNTP*FAIKKKDStKWRKLVDFRELNKRTQDFWEVQLGIPHPAGLKKKKSV*VLDVGDAYFSVPL 180
Cdd:cd01645    24 QLKEGHIEPST--SPWNTPVFVIKKKSG-KWRLLHDLRAVNAQTQDMGALQPGLPHPAALPKGWPLIVLDLKDCFFSIPL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037179310 181 DEBFRKYTAFTIPS*NNETPGIRY*YNVLPQGWKGSPAIFQSSMTKILEPFRKQNP*IVIYQYMDDLYVGSDLEiGQHR* 260
Cdd:cd01645   101 HPDDRERFAFTVPSINNKGPAKRYQWKVLPQGMKNSPTICQSFVAQALEPFRKQYPDIVIYHYMDDILIASDLE-GQLRE 179
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1037179310 261 KIEELR*HLL*WG*TTPDKKHQKEPPFFWKGBEL 294
Cdd:cd01645   180 IYEELRQTLLRWGLTIPPEKVQKEPPFQYLGYEL 213
RVT_1 pfam00078
Reverse transcriptase (RNA-dependent DNA polymerase); A reverse transcriptase gene is usually ...
123-282 4.72e-40

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: 138.20  E-value: 4.72e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037179310 123 IKKKDSTKWRKL----VDFRELNKRTQD-------FWEVQLGIPHPAG-LKKKKSV*VLDVGDAYFSVPLDEBFRKYTAF 190
Cdd:pfam00078   1 IPKKGKGKYRPIsllsIDYKALNKIIVKrlkpenlDSPPQPGFRPGLAkLKKAKWFLKLDLKKAFDQVPLDELDRKLTAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037179310 191 TIPS*NN----ETPGIRY*YNVLPQGWKGSPAIFQSSMTKILEPFRKQnP*IVIYQYMDDLYVGSDlEIGQHR*KIEELR 266
Cdd:pfam00078  81 TTPPINInwngELSGGRYEWKGLPQGLVLSPALFQLFMNELLRPLRKR-AGLTLVRYADDILIFSK-SEEEHQEALEEVL 158
                         170
                  ....*....|....*.
gi 1037179310 267 *HLL*WG*TTPDKKHQ 282
Cdd:pfam00078 159 EWLKESGLKINPEKTQ 174
RVP pfam00077
Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, ...
5-98 2.45e-28

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: 104.76  E-value: 2.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037179310   5 LWQRPLVIVRIGEQLIEALLDTGADDTVLKEIDLTGRW----KPKMIGGIGGFIKVKQYENMTIEIEGKKAVGTV--LIG 78
Cdd:pfam00077   1 AEQRPLLTVKIGGKYFTALLDTGADDTVISQNDWPTNWpkqkATTNIQGIGGGINVRQSDQILILIGEDKFRGTVspLIL 80
                          90       100
                  ....*....|....*....|.
gi 1037179310  79 PT-PVNIIGRNMLTQIGCTLN 98
Cdd:pfam00077  81 PTcPVNIIGRDLLQQLGGRLT 101
HIV_retropepsin_like cd05482
Retropepsins, pepsin-like aspartate proteases; This is a subfamily of retropepsins. The family ...
13-91 8.51e-19

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: 79.23  E-value: 8.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037179310  13 VRIGEQLIEALLDTGADDTVLKEIDLTGRW----KPKMIGGIGGFIKVKQYENMTIEIEGKKAVGTVLIGP--TPVNIIG 86
Cdd:cd05482     3 LYINGKLFEGLLDTGADVSIIAENDWPKNWpiqpAPSNLTGIGGAITPSQSSVLLLEIDGEGHLGTILVYVlsLPVNLWG 82

                  ....*
gi 1037179310  87 RNMLT 91
Cdd:cd05482    83 RDILS 87
 
Name Accession Description Interval E-value
RT_Rtv cd01645
RT_Rtv: Reverse transcriptases (RTs) from retroviruses (Rtvs). RTs catalyze the conversion of ...
101-294 3.92e-99

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: 289.95  E-value: 3.92e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037179310 101 MEKEGKIS*IGpeNPYNTP*FAIKKKDStKWRKLVDFRELNKRTQDFWEVQLGIPHPAGLKKKKSV*VLDVGDAYFSVPL 180
Cdd:cd01645    24 QLKEGHIEPST--SPWNTPVFVIKKKSG-KWRLLHDLRAVNAQTQDMGALQPGLPHPAALPKGWPLIVLDLKDCFFSIPL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037179310 181 DEBFRKYTAFTIPS*NNETPGIRY*YNVLPQGWKGSPAIFQSSMTKILEPFRKQNP*IVIYQYMDDLYVGSDLEiGQHR* 260
Cdd:cd01645   101 HPDDRERFAFTVPSINNKGPAKRYQWKVLPQGMKNSPTICQSFVAQALEPFRKQYPDIVIYHYMDDILIASDLE-GQLRE 179
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1037179310 261 KIEELR*HLL*WG*TTPDKKHQKEPPFFWKGBEL 294
Cdd:cd01645   180 IYEELRQTLLRWGLTIPPEKVQKEPPFQYLGYEL 213
RVT_1 pfam00078
Reverse transcriptase (RNA-dependent DNA polymerase); A reverse transcriptase gene is usually ...
123-282 4.72e-40

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: 138.20  E-value: 4.72e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037179310 123 IKKKDSTKWRKL----VDFRELNKRTQD-------FWEVQLGIPHPAG-LKKKKSV*VLDVGDAYFSVPLDEBFRKYTAF 190
Cdd:pfam00078   1 IPKKGKGKYRPIsllsIDYKALNKIIVKrlkpenlDSPPQPGFRPGLAkLKKAKWFLKLDLKKAFDQVPLDELDRKLTAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037179310 191 TIPS*NN----ETPGIRY*YNVLPQGWKGSPAIFQSSMTKILEPFRKQnP*IVIYQYMDDLYVGSDlEIGQHR*KIEELR 266
Cdd:pfam00078  81 TTPPINInwngELSGGRYEWKGLPQGLVLSPALFQLFMNELLRPLRKR-AGLTLVRYADDILIFSK-SEEEHQEALEEVL 158
                         170
                  ....*....|....*.
gi 1037179310 267 *HLL*WG*TTPDKKHQ 282
Cdd:pfam00078 159 EWLKESGLKINPEKTQ 174
RVP pfam00077
Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, ...
5-98 2.45e-28

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: 104.76  E-value: 2.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037179310   5 LWQRPLVIVRIGEQLIEALLDTGADDTVLKEIDLTGRW----KPKMIGGIGGFIKVKQYENMTIEIEGKKAVGTV--LIG 78
Cdd:pfam00077   1 AEQRPLLTVKIGGKYFTALLDTGADDTVISQNDWPTNWpkqkATTNIQGIGGGINVRQSDQILILIGEDKFRGTVspLIL 80
                          90       100
                  ....*....|....*....|.
gi 1037179310  79 PT-PVNIIGRNMLTQIGCTLN 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 ...
115-252 6.67e-28

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: 107.05  E-value: 6.67e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037179310 115 PYNTP*FAIKKKDSTKWRKLVDFRELNKRTQDfweVQLGIPHPAGL-----KKKKSV*VLDVGDAYFSVPLDEBFRKYTA 189
Cdd:cd03715    36 PWNTPILPVKKPGGNDYRMVQDLRLVNQAVLP---IHPAVPNPYTLlsllpPKHQWYTVLDLANAFFSLPLAPDSQPLFA 112
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1037179310 190 FTIPs*nnetpGIRY*YNVLPQGWKGSPAIFQSSMTKILEPFRKQNP*IVIYQYMDDLYVGSD 252
Cdd:cd03715   113 FEWE-------GQQYTFTRLPQGFKNSPTLFHEALARDLAPFPLEHEGTILLQYVDDLLLAAD 168
RT_LTR cd01647
RT_LTR: Reverse transcriptases (RTs) from retrotransposons and retroviruses which have long ...
115-269 2.06e-23

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: 94.20  E-value: 2.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037179310 115 PYNTP*FAIKKKDStKWRKLVDFRELNKRT-QDFWEvqlgIPHPAG----LKKKKSV*VLDVGDAYFSVPLDEBFRKYTA 189
Cdd:cd01647     9 PYASPVVVVKKKDG-KLRLCVDYRKLNKVTiKDRYP----LPTIDElleeLAGAKVFSKLDLRSGYHQIPLAEESRPKTA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037179310 190 FTips*nneTPGIRY*YNVLPQGWKGSPAIFQSSMTKIlepFRKQNP*IVIyQYMDDLYVGSDleigqhr*KIEELR*HL 269
Cdd:cd01647    84 FR-------TPFGLYEYTRMPFGLKNAPATFQRLMNKI---LGDLLGDFVE-VYLDDILVYSK--------TEEEHLEHL 144
HIV_retropepsin_like cd05482
Retropepsins, pepsin-like aspartate proteases; This is a subfamily of retropepsins. The family ...
13-91 8.51e-19

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: 79.23  E-value: 8.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037179310  13 VRIGEQLIEALLDTGADDTVLKEIDLTGRW----KPKMIGGIGGFIKVKQYENMTIEIEGKKAVGTVLIGP--TPVNIIG 86
Cdd:cd05482     3 LYINGKLFEGLLDTGADVSIIAENDWPKNWpiqpAPSNLTGIGGAITPSQSSVLLLEIDGEGHLGTILVYVlsLPVNLWG 82

                  ....*
gi 1037179310  87 RNMLT 91
Cdd:cd05482    83 RDILS 87
RT_like cd00304
RT_like: Reverse transcriptase (RT, RNA-dependent DNA polymerase)_like family. An RT gene is ...
209-294 2.41e-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: 2.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037179310 209 LPQGWKGSPAIFQSSMTKILEPFRKQNP*IVIYQYMDDLYVGSDLEigQHR*KIEELR*HLL*WG*TTPDKKHQ---KEP 285
Cdd:cd00304    12 LPQGSPLSPALANLYMEKLEAPILKQLLDITLIRYVDDLVVIAKSE--QQAVKKRELEEFLARLGLNLSDEKTQfteKEK 89

                  ....*....
gi 1037179310 286 PFFWKGBEL 294
Cdd:cd00304    90 KFKFLGILV 98
RP_RTVL_H_like cd06095
Retropepsin of the RTVL_H family of human endogenous retrovirus-like elements; This family ...
11-91 2.29e-04

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: 39.24  E-value: 2.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037179310  11 VIVRIGEQLIEALLDTGADDTVLKE-IDLTGRWKPK--MIGGIGGFIK--VKQYENMtIEIEGKKAVGTVLIGPT-PVNI 84
Cdd:cd06095     1 VTITVEGVPIVFLVDTGATHSVLKSdLGPKQELSTTsvLIRGVSGQSQqpVTTYRTL-VDLGGHTVSHSFLVVPNcPDPL 79

                  ....*..
gi 1037179310  85 IGRNMLT 91
Cdd:cd06095    80 LGRDLLS 86
gag-asp_proteas pfam13975
gag-polyprotein putative aspartyl protease; This family of putative aspartyl proteases is ...
13-92 1.01e-03

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: 37.56  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037179310  13 VRIGEQLIEALLDTGADDTVLKE-------IDLTGRWKPKMIGGIGGFIKVKQYENMTIEIEGKKA---VGTVLIGPTPV 82
Cdd:pfam13975   3 VTINGRPVRFLVDTGASVTVISEalaerlgLDRLVDAYPVTVRTANGTVRAARVRLDSVKIGGIELrnvPAVVLPGDLDD 82
                          90
                  ....*....|
gi 1037179310  83 NIIGRNMLTQ 92
Cdd:pfam13975  83 VLLGMDFLKR 92
Asp_protease_2 pfam13650
Aspartyl protease; This family consists of predicted aspartic proteases, typically from 180 to ...
11-88 1.05e-03

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: 37.65  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037179310  11 VIVRIGEQLIEALLDTGADDTVL-----KEIDLTGRWK--PKMIGGIGGFIKVKQYENMTIEIEGKKAVG-TVLI---GP 79
Cdd:pfam13650   1 VPVTINGKPVRFLVDTGASGTVIspslaERLGLKVRGLayTVRVSTAGGRVSAARVRLDSLRLGGLTLENvPALVldlGD 80

                  ....*....
gi 1037179310  80 TPVNIIGRN 88
Cdd:pfam13650  81 LIDGLLGMD 89
 
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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