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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SNP_A       20 GPKVKQWPLTEEKIKALVEICTEMEKEGKISKIGpeNPYNTPVFAIKKKDStKWRKLVDFRELNKRTQDFWEVQLGIPHP 99
Cdd:cd01645   1 PVWIKQWPLTEEKLEALTELVTEQLKEGHIEPST--SPWNTPVFVIKKKSG-KWRLLHDLRAVNAQTQDMGALQPGLPHP 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SNP_A      100 AGLKKKKSVTVLDVGDAYFSVPLDEDFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFAAQNPD 179
Cdd:cd01645  78 AALPKGWPLIVLDLKDCFFSIPLHPDDRERFAFTVPSINNKGPAKRYQWKVLPQGMKNSPTICQSFVAQALEPFRKQYPD 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
7SNP_A      180 IVIYQYMDDLYVGSDLEiGQHRTKIEELRQHLLRWGLTTPDKKHQKEPPFLWMGYEL 236
Cdd:cd01645 158 IVIYHYMDDILIASDLE-GQLREIYEELRQTLLRWGLTIPPEKVQKEPPFQYLGYEL 213

Reverse transcriptase connection domain; This domain is known as the connection domain. This domain lies between the thumb and palm domains.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SNP_A        320 YYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLKTGKYARMRGAHTNDVKQLTEAVQKITTESIVIWGKTPKFKLPIQKET 399
Cdd:pfam06815   1 YYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLKTGKYARMRGAHTNDVKQLTEAVQKITTESIVIWGKTPKFKLPIQKET 80

                          90       100
                  ....*....|....*....|..
7SNP_A        400 WETWWTEYWQATWIPEWEFVNT 421
Cdd:pfam06815  81 WETWWTEYWQATWIPEWEFVNT 102

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SNP_A       20 GPKVKQWPLTEEKIKALVEICTEMEKEGKISKIGpeNPYNTPVFAIKKKDStKWRKLVDFRELNKRTQDFWEVQLGIPHP 99
Cdd:cd01645   1 PVWIKQWPLTEEKLEALTELVTEQLKEGHIEPST--SPWNTPVFVIKKKSG-KWRLLHDLRAVNAQTQDMGALQPGLPHP 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SNP_A      100 AGLKKKKSVTVLDVGDAYFSVPLDEDFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFAAQNPD 179
Cdd:cd01645  78 AALPKGWPLIVLDLKDCFFSIPLHPDDRERFAFTVPSINNKGPAKRYQWKVLPQGMKNSPTICQSFVAQALEPFRKQYPD 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
7SNP_A      180 IVIYQYMDDLYVGSDLEiGQHRTKIEELRQHLLRWGLTTPDKKHQKEPPFLWMGYEL 236
Cdd:cd01645 158 IVIYHYMDDILIASDLE-GQLREIYEELRQTLLRWGLTIPPEKVQKEPPFQYLGYEL 213

RNase H; RNase H digests the RNA strand of an RNA/DNA hybrid. Important enzyme in retroviral replication cycle, and often found as a domain associated with reverse transcriptases. Structure is a mixed alpha+beta fold with three a/b/a layers.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SNP_A        439 AETFYVDGAANRETKLGKAGYVTNKGRQ-KVVPLTN-TTNQKTELQAIYLALQD--SGLEVNIVTDSQYALGII------ 508
Cdd:pfam00075   3 AVTVYTDGSCLGNPGPGGAGAVLYRGHEnISAPLPGrTTNNRAELQAVIEALKAlkSPSKVNIYTDSQYVIGGItqwvhg 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
7SNP_A        509 ---QAQPDKSES-ELVNQIIEQL----IKKEKVYLAWVPAHKGIGGNEQVDKLVSAG 557
Cdd:pfam00075  83 wkkNGWPTTSEGkPVKNKDLWQLlkalCKKHQVYWQWVKGHAGNPGNEMADRLAKQG 139

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

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
7SNP_A        243 VQPIVLPEKDSWTVNDIQKLVGKLNWASQIY--PGIKVRQLSKLLRGTKALTEVIPLT 298
Cdd:pfam06817   1 PQKLQLRKDHLKTLNDFQKLLGDINWIRPYLgiTTYDLKPLFSLLRGDSDLTSPRTLT 58

Bel/Pao 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 eukaryote. 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. Bel/Pao family has been described only in metazoan genomes. RNase H inhibitors have been explored as an anti-HIV drug target because RNase H inactivation inhibits reverse transcription.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SNP_A      441 TFYVDGAAnreTKLGKAGYVTNKGRQKVVPLTNTTNQKTELQAIYLALQD-SGLEVNIVTDSQYALGIIQA--------- 510
Cdd:cd09273   1 TVFTDGSS---FKAGYAIVSGTEIVEAQPLPPGTSAQRAELIALIQALELaKGKPVNIYTDSAYAVHALHLletigierg 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
7SNP_A      511 -QPDKSESELVNQIIEQLIKKEKVYLAWVPAHKGIG-----GNEQVDKLV 554
Cdd:cd09273  78 fLKSIKNLSLFLQLLEAVQRPKPVAIIHIRAHSKLPgplaeGNAQADAAA 127

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SNP_A       20 GPKVKQWPLTEEKIKALVEICTEMEKEGKISKIGpeNPYNTPVFAIKKKDStKWRKLVDFRELNKRTQDFWEVQLGIPHP 99
Cdd:cd01645   1 PVWIKQWPLTEEKLEALTELVTEQLKEGHIEPST--SPWNTPVFVIKKKSG-KWRLLHDLRAVNAQTQDMGALQPGLPHP 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SNP_A      100 AGLKKKKSVTVLDVGDAYFSVPLDEDFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFAAQNPD 179
Cdd:cd01645  78 AALPKGWPLIVLDLKDCFFSIPLHPDDRERFAFTVPSINNKGPAKRYQWKVLPQGMKNSPTICQSFVAQALEPFRKQYPD 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
7SNP_A      180 IVIYQYMDDLYVGSDLEiGQHRTKIEELRQHLLRWGLTTPDKKHQKEPPFLWMGYEL 236
Cdd:cd01645 158 IVIYHYMDDILIASDLE-GQLREIYEELRQTLLRWGLTIPPEKVQKEPPFQYLGYEL 213

RNase H; RNase H digests the RNA strand of an RNA/DNA hybrid. Important enzyme in retroviral replication cycle, and often found as a domain associated with reverse transcriptases. Structure is a mixed alpha+beta fold with three a/b/a layers.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SNP_A        439 AETFYVDGAANRETKLGKAGYVTNKGRQ-KVVPLTN-TTNQKTELQAIYLALQD--SGLEVNIVTDSQYALGII------ 508
Cdd:pfam00075   3 AVTVYTDGSCLGNPGPGGAGAVLYRGHEnISAPLPGrTTNNRAELQAVIEALKAlkSPSKVNIYTDSQYVIGGItqwvhg 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
7SNP_A        509 ---QAQPDKSES-ELVNQIIEQL----IKKEKVYLAWVPAHKGIGGNEQVDKLVSAG 557
Cdd:pfam00075  83 wkkNGWPTTSEGkPVKNKDLWQLlkalCKKHQVYWQWVKGHAGNPGNEMADRLAKQG 139

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SNP_A       21 PKVKQWPLTEEKIKALVEICTEMEKEGKIskIGPENPYNTPVFAIKKKDSTKWRKLVDFRELNKRTQDfweVQLGIPHPA 100
Cdd:cd03715   2 VNQKQYPLPREAREGITPHIQELLEAGIL--VPCQSPWNTPILPVKKPGGNDYRMVQDLRLVNQAVLP---IHPAVPNPY 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SNP_A      101 GL-----KKKKSVTVLDVGDAYFSVPLDEDFRKYTAFTIPsinnetpGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFAA 175
Cdd:cd03715  77 TLlsllpPKHQWYTVLDLANAFFSLPLAPDSQPLFAFEWE-------GQQYTFTRLPQGFKNSPTLFHEALARDLAPFPL 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
7SNP_A      176 QNPDIVIYQYMDDLYVGSDLEIGQHRTkIEELRQHLLRWGLTTPDKKHQ 224
Cdd:cd03715 150 EHEGTILLQYVDDLLLAADSEEDCLKG-TDALLTHLGELGYKVSPKKAQ 197

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SNP_A      151 LPQGWKGSPAIFQSSMTKILEPFAAQNPDIVIYQYMDDLYVGSDLEigQHRTKIEELRQHLLRWGLTTPDKKHQ---KEP 227
Cdd:cd00304  12 LPQGSPLSPALANLYMEKLEAPILKQLLDITLIRYVDDLVVIAKSE--QQAVKKRELEEFLARLGLNLSDEKTQfteKEK 89

                ....*....
7SNP_A      228 PFLWMGYEL 236
Cdd:cd00304  90 KFKFLGILV 98

Ribonuclease HI [Replication, recombination and repair];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SNP_A      443 YVDGAANRETklGKAGY---VTNKGRQKVV--PLTNTTNQKTELQAIYLALQ----DSGLEVNIVTDSQYAL----GIIQ 509
Cdd:COG0328   6 YTDGACRGNP--GPGGWgavIRYGGEEKELsgGLGDTTNNRAELTALIAALEalkeLGPCEVEIYTDSQYVVnqitGWIH 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
7SNP_A      510 AQPDKSESELVN----QIIEQLIKKEKVYLAWVPAHKGIGGNEQVDKLVSAG 557
Cdd:COG0328  84 GWKKNGWKPVKNpdlwQRLDELLARHKVTFEWVKGHAGHPGNERADALANKA 135

non-LTR RNase HI domain of reverse transcriptases; Ribonuclease H (RNase H) is classified into two families, type 1 (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type 2 (prokaryotic RNase HII and HIII, and eukaryotic RNase H2). Ribonuclease HI (RNase HI) is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes. RNase HI has also been observed as an adjunct domain to the reverse transcriptase gene in retroviruses, 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. The position of the RNase domain of non-LTR and LTR transposons is at the carboxyl terminal of the reverse transcriptase (RT) domain and their RNase domains group together, indicating a common evolutionary origin. Many non-LTR transposons have lost the RNase domain because their activity is at the nucleus and cellular RNase may suffice; however LTR retrotransposons always encode their own RNase domain because it requires RNase activity in RNA-protein particles in the cytoplasm. RNase H inhibitors have been explored as an anti-HIV drug target because RNase H inactivation inhibits reverse transcription.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SNP_A      441 TFYVDGAANrETKLGkAGYVTNKGRQKVVPLTNTTNQKT----ELQAIYLALQ------DSGLEVNIVTDSQYALGIIQA 510
Cdd:cd09276   1 VIYTDGSKL-EGSVG-AGFVIYRGGEVISRSYRLGTHASvfdaELEAILEALElalataRRARKVTIFTDSQSALQALRN 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
7SNP_A      511 qPDKSESELVNQIIEQLIKKE-----KVYLAWVPAHKGIGGNEQVDKLVSAG 557
Cdd:cd09276  79 -PRRSSGQVILIRILRLLRLLkakgvKVRLRWVPGHVGIEGNEAADRLAKEA 129

RNase HI family found mainly in prokaryotes; Ribonuclease H (RNase H) is classified into two evolutionarily unrelated families, type 1 (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type 2 (prokaryotic RNase HII and HIII, and eukaryotic RNase H2). RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner. RNase H is involved in DNA replication, repair and transcription. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes and most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site (DEDD), residues and have the same catalytic mechanism and functions in cells. One of the important functions of RNase H is to remove Okazaki fragments during DNA replication. Prokaryotic RNase H varies greatly in domain structures and substrate specificities. Prokaryotes and some single-cell eukaryotes do not require RNase H for viability.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SNP_A      473 NTTNQKTELQAIYLALQ--DSGLEVNIVTDSQYAL-GIIQAQPD-------KSESELV-N----QIIEQLIKKEKVYLAW 537
Cdd:cd09278  38 GTTNNRMELTAAIEALEalKEPCPVTIYTDSQYVInGITKWIKGwkkngwkTADGKPVkNrdlwQELDALLAGHKVTWEW 117

                        90       100
                ....*....|....*....|
7SNP_A      538 VPAHKGIGGNEQVDKLVSAG 557
Cdd:cd09278 118 VKGHAGHPGNERADRLANKA 137

Ribonuclease H-like superfamily, including RNase H, HI, HII, HIII, and RNase-like domain IV of spliceosomal protein Prp8; 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. It is widely present in various organisms, including bacteria, archaea, and eukaryotes. Most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site residues and have the same catalytic mechanism and functions in cells. RNase H is involved in DNA replication, repair and transcription. An important RNase H function is to remove Okazaki fragments during DNA replication. RNase H inhibitors have been explored as anti-HIV drug targets since RNase H inactivation inhibits reverse transcription. This model also includes the Prp8 domain IV, which adopts the RNase fold but shows low sequence homology; domain IV is implicated in key spliceosomal interactions.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SNP_A      443 YVDGAANRETKLGKAGYVTNKGRQKVV-----PLTNTTNQKTELQAIYLALQ----DSGLEVNIVTDSQYALGIIQAQPD 513
Cdd:cd06222   2 NVDGSCRGNPGPAGIGGVLRDHEGGWLggfalKIGAPTALEAELLALLLALElaldLGYLKVIIESDSKYVVDLINSGSF 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
7SNP_A      514 KSES--ELVNQIIEQLIKKEKVYLAWVPAHkgigGNEQVDKL 553
Cdd:cd06222  82 KWSPniLLIEDILLLLSRFWSVKISHVPRE----GNQVADAL 119

ribonuclease H; Reviewed

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SNP_A       441 TFYVDGAA-NRETKLGKAGY---VTNKGRQKV----VPLTN-TTNQKTELQAIYLALQDSGLEVNIVTDSQYALGIIQAQ 511
Cdd:PRK08719   6 SIYIDGAApNNQHGCVRGGIglvVYDEAGEIVdeqsITVNRyTDNAELELLALIEALEYARDGDVIYSDSDYCVRGFNEW 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
7SNP_A       512 PD--------KSESELVN-----QIIEQLIKKEKVYLAWVPAHKGIGGNEQVDKLVSA 556
Cdd:PRK08719  86 LDtwkqkgwrKSDKKPVAnrdlwQQVDELRARKYVEVEKVTAHSGIEGNEAADMLAQA 143