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Conserved domains on  [gi|1805791167|ref|NP_001365202|]
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ribonuclease H1 isoform 6 precursor [Homo sapiens]

Protein Classification

ribonuclease H family protein( domain architecture ID 10483817)

ribonuclease H (RNaseH) family protein containing a reverse transcriptase (RT)-like domain; may be an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner

EC:  3.1.26.4
Gene Ontology:  GO:0003723|GO:0004523

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RNase_HI_eukaryote_like cd09280
Eukaryotic RNase H is essential and is longer and more complex than their prokaryotic ...
 141-277 2.21e-77

Eukaryotic RNase H is essential and is longer and more complex than their prokaryotic counterparts; 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). 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. One of the important functions of RNase H is to remove Okazaki fragments during DNA replication. RNase H is widely present in various organisms, including bacteria, archaea and eukaryote 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. Eukaryotic RNase H is longer and more complex than in prokaryotes. Almost all eukaryotic RNase HI have highly conserved regions at their N-termini called hybrid binding domain (HBD). It is speculated that the HBD contributes to binding the RNA/DNA hybrid. Prokaryotes and some single-cell eukaryotes do not require RNase H for viability, but RNase H is essential in higher eukaryotes. RNase H knockout mice lack mitochondrial DNA replication and die as embryos.


:

Pssm-ID: 260012 [Multi-domain]  Cd Length: 145  Bit Score: 231.30  E-value: 2.21e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791167 141 VVYTDGCCSSNGRRRPRAGIGVYWGPGHPL-----LPGR-QTNQRAEIHAACKAIEQAKTQNINKLVLYTDSMFTINGIT 214
Cdd:cd09280     1 VVYTDGSCLNNGKPGARAGIGVYFGPGDPRnvsepLPGRkQTNNRAELLAVIHALEQAPEEGIRKLEIRTDSKYAINCIT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1805791167 215 NWVQGWKKNGWKTSAGKEVINKEDFVALERLTQ--GMDIQWMHVPGHSGFIGNEEADRLAREGAK 277
Cdd:cd09280    81 KWIPKWKKNGWKTSKGKPVKNQDLIKELDKLLRkrGIKVKFEHVKGHSGDPGNEEADRLAREGAD 145
Cauli_VI pfam01693
Caulimovirus viroplasmin; This family consists of various caulimovirus viroplasmin proteins. ...
 28-70 5.44e-20

Caulimovirus viroplasmin; This family consists of various caulimovirus viroplasmin proteins. The viroplasmin protein is encoded by gene VI and is the main component of viral inclusion bodies or viroplasms. Inclusions are the site of viral assembly, DNA synthesis and accumulation. Two domains exist within gene VI corresponding approximately to the 5' third and middle third of gene VI, these influence systemic infection in a light-dependent manner.


:

Pssm-ID: 460297 [Multi-domain]  Cd Length: 44  Bit Score: 80.91  E-value: 5.44e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1805791167  28 FYAVRRGRKTGVFLTWNECRAQVDRFPAARFKKFATEDEAWAF 70
Cdd:pfam01693   2 YYAVAKGRKPGIYTTWDECKAQVKGFPGAKYKSFKTREEAEAF 44
 
Name Accession Description Interval E-value
RNase_HI_eukaryote_like cd09280
Eukaryotic RNase H is essential and is longer and more complex than their prokaryotic ...
 141-277 2.21e-77

Eukaryotic RNase H is essential and is longer and more complex than their prokaryotic counterparts; 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). 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. One of the important functions of RNase H is to remove Okazaki fragments during DNA replication. RNase H is widely present in various organisms, including bacteria, archaea and eukaryote 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. Eukaryotic RNase H is longer and more complex than in prokaryotes. Almost all eukaryotic RNase HI have highly conserved regions at their N-termini called hybrid binding domain (HBD). It is speculated that the HBD contributes to binding the RNA/DNA hybrid. Prokaryotes and some single-cell eukaryotes do not require RNase H for viability, but RNase H is essential in higher eukaryotes. RNase H knockout mice lack mitochondrial DNA replication and die as embryos.


Pssm-ID: 260012 [Multi-domain]  Cd Length: 145  Bit Score: 231.30  E-value: 2.21e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791167 141 VVYTDGCCSSNGRRRPRAGIGVYWGPGHPL-----LPGR-QTNQRAEIHAACKAIEQAKTQNINKLVLYTDSMFTINGIT 214
Cdd:cd09280     1 VVYTDGSCLNNGKPGARAGIGVYFGPGDPRnvsepLPGRkQTNNRAELLAVIHALEQAPEEGIRKLEIRTDSKYAINCIT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1805791167 215 NWVQGWKKNGWKTSAGKEVINKEDFVALERLTQ--GMDIQWMHVPGHSGFIGNEEADRLAREGAK 277
Cdd:cd09280    81 KWIPKWKKNGWKTSKGKPVKNQDLIKELDKLLRkrGIKVKFEHVKGHSGDPGNEEADRLAREGAD 145
RNase_H pfam00075
RNase H; RNase H digests the RNA strand of an RNA/DNA hybrid. Important enzyme in retroviral ...
 140-277 6.13e-57

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.


Pssm-ID: 395028 [Multi-domain]  Cd Length: 141  Bit Score: 179.50  E-value: 6.13e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791167 140 VVVYTDGCCSSNGRRRpRAGIGVYWGP---GHPLlPGRQTNQRAEIHAACKAIEQAKTQNinKLVLYTDSMFTINGITNW 216
Cdd:pfam00075   4 VTVYTDGSCLGNPGPG-GAGAVLYRGHeniSAPL-PGRTTNNRAELQAVIEALKALKSPS--KVNIYTDSQYVIGGITQW 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1805791167 217 VQGWKKNGWK-TSAGKEVINKEDFVALERLTQGMDIQWMHVPGHSGFIGNEEADRLAREGAK 277
Cdd:pfam00075  80 VHGWKKNGWPtTSEGKPVKNKDLWQLLKALCKKHQVYWQWVKGHAGNPGNEMADRLAKQGAE 141
RnhA COG0328
Ribonuclease HI [Replication, recombination and repair];
140-276 3.74e-36

Ribonuclease HI [Replication, recombination and repair];


Pssm-ID: 440097 [Multi-domain]  Cd Length: 136  Bit Score: 125.73  E-value: 3.74e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791167 140 VVVYTDGCCSSNgrrrP-RAGIGVYWGPGHPLLP-----GRQTNQRAEIHAACKAIEQAKTQNINKLVLYTDSMFTINGI 213
Cdd:COG0328     3 IEIYTDGACRGN----PgPGGWGAVIRYGGEEKElsgglGDTTNNRAELTALIAALEALKELGPCEVEIYTDSQYVVNQI 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1805791167 214 TNWVQGWKKNGWktsagKEVINKEDFVALERLTQGMDIQWMHVPGHSGFIGNEEADRLAREGA 276
Cdd:COG0328    79 TGWIHGWKKNGW-----KPVKNPDLWQRLDELLARHKVTFEWVKGHAGHPGNERADALANKAL 136
rnhA PRK00203
ribonuclease H; Reviewed
 140-278 2.13e-29

ribonuclease H; Reviewed


Pssm-ID: 178927 [Multi-domain]  Cd Length: 150  Bit Score: 108.76  E-value: 2.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791167 140 VVVYTDGCCSSNgrrrP-RAGIGVY----------WGpGHPLlpgrQTNQRAEIHAACKAIEQAKTQNinKLVLYTDSMF 208
Cdd:PRK00203    4 VEIYTDGACLGN----PgPGGWGAIlrykghekelSG-GEAL----TTNNRMELMAAIEALEALKEPC--EVTLYTDSQY 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791167 209 TINGITNWVQGWKKNGWKTSAGKEVINKEDFVALERLTQGMDIQWMHVPGHSGFIGNEEADRLAREGAKQ 278
Cdd:PRK00203   73 VRQGITEWIHGWKKNGWKTADKKPVKNVDLWQRLDAALKRHQIKWHWVKGHAGHPENERCDELARAGAEE 142
Cauli_VI pfam01693
Caulimovirus viroplasmin; This family consists of various caulimovirus viroplasmin proteins. ...
 28-70 5.44e-20

Caulimovirus viroplasmin; This family consists of various caulimovirus viroplasmin proteins. The viroplasmin protein is encoded by gene VI and is the main component of viral inclusion bodies or viroplasms. Inclusions are the site of viral assembly, DNA synthesis and accumulation. Two domains exist within gene VI corresponding approximately to the 5' third and middle third of gene VI, these influence systemic infection in a light-dependent manner.


Pssm-ID: 460297 [Multi-domain]  Cd Length: 44  Bit Score: 80.91  E-value: 5.44e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1805791167  28 FYAVRRGRKTGVFLTWNECRAQVDRFPAARFKKFATEDEAWAF 70
Cdd:pfam01693   2 YYAVAKGRKPGIYTTWDECKAQVKGFPGAKYKSFKTREEAEAF 44
 
Name Accession Description Interval E-value
RNase_HI_eukaryote_like cd09280
Eukaryotic RNase H is essential and is longer and more complex than their prokaryotic ...
 141-277 2.21e-77

Eukaryotic RNase H is essential and is longer and more complex than their prokaryotic counterparts; 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). 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. One of the important functions of RNase H is to remove Okazaki fragments during DNA replication. RNase H is widely present in various organisms, including bacteria, archaea and eukaryote 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. Eukaryotic RNase H is longer and more complex than in prokaryotes. Almost all eukaryotic RNase HI have highly conserved regions at their N-termini called hybrid binding domain (HBD). It is speculated that the HBD contributes to binding the RNA/DNA hybrid. Prokaryotes and some single-cell eukaryotes do not require RNase H for viability, but RNase H is essential in higher eukaryotes. RNase H knockout mice lack mitochondrial DNA replication and die as embryos.


Pssm-ID: 260012 [Multi-domain]  Cd Length: 145  Bit Score: 231.30  E-value: 2.21e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791167 141 VVYTDGCCSSNGRRRPRAGIGVYWGPGHPL-----LPGR-QTNQRAEIHAACKAIEQAKTQNINKLVLYTDSMFTINGIT 214
Cdd:cd09280     1 VVYTDGSCLNNGKPGARAGIGVYFGPGDPRnvsepLPGRkQTNNRAELLAVIHALEQAPEEGIRKLEIRTDSKYAINCIT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1805791167 215 NWVQGWKKNGWKTSAGKEVINKEDFVALERLTQ--GMDIQWMHVPGHSGFIGNEEADRLAREGAK 277
Cdd:cd09280    81 KWIPKWKKNGWKTSKGKPVKNQDLIKELDKLLRkrGIKVKFEHVKGHSGDPGNEEADRLAREGAD 145
RNase_H pfam00075
RNase H; RNase H digests the RNA strand of an RNA/DNA hybrid. Important enzyme in retroviral ...
 140-277 6.13e-57

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.


Pssm-ID: 395028 [Multi-domain]  Cd Length: 141  Bit Score: 179.50  E-value: 6.13e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791167 140 VVVYTDGCCSSNGRRRpRAGIGVYWGP---GHPLlPGRQTNQRAEIHAACKAIEQAKTQNinKLVLYTDSMFTINGITNW 216
Cdd:pfam00075   4 VTVYTDGSCLGNPGPG-GAGAVLYRGHeniSAPL-PGRTTNNRAELQAVIEALKALKSPS--KVNIYTDSQYVIGGITQW 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1805791167 217 VQGWKKNGWK-TSAGKEVINKEDFVALERLTQGMDIQWMHVPGHSGFIGNEEADRLAREGAK 277
Cdd:pfam00075  80 VHGWKKNGWPtTSEGKPVKNKDLWQLLKALCKKHQVYWQWVKGHAGNPGNEMADRLAKQGAE 141
RNase_HI_prokaryote_like cd09278
RNase HI family found mainly in prokaryotes; Ribonuclease H (RNase H) is classified into two ...
 140-277 5.84e-41

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.


Pssm-ID: 260010 [Multi-domain]  Cd Length: 139  Bit Score: 138.38  E-value: 5.84e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791167 140 VVVYTDGCCSSNgrrrPRAG----IGVYWGPGHPLLPG--RQTNQRAEIHAACKAIEQAKTQNinKLVLYTDSMFTINGI 213
Cdd:cd09278     2 IVIYTDGACLGN----PGPGgwaaVIRYGDHEKELSGGepGTTNNRMELTAAIEALEALKEPC--PVTIYTDSQYVINGI 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1805791167 214 TNWVQGWKKNGWKTSAGKEVINKEDFVALERLTQGMDIQWMHVPGHSGFIGNEEADRLAREGAK 277
Cdd:cd09278    76 TKWIKGWKKNGWKTADGKPVKNRDLWQELDALLAGHKVTWEWVKGHAGHPGNERADRLANKAAD 139
RNase_H_Dikarya_like cd13934
Fungal (dikarya) Ribonuclease H, uncharacterized; This family contains dikarya RNase H, many ...
 141-277 2.84e-39

Fungal (dikarya) Ribonuclease H, uncharacterized; This family contains dikarya RNase H, many of which are uncharacterized. 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.


Pssm-ID: 260014 [Multi-domain]  Cd Length: 153  Bit Score: 134.25  E-value: 2.84e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791167 141 VVYTDGCCSSNGRRRPRAGIGVYWGPGHPL---------LPGRQTNQRAEIHAACKAIEQAKTQN------INKLVLYTD 205
Cdd:cd13934     1 LVYIDGACRNNGRPDARAGYGVYFGPDSSYnvsgrledtGGHPQTSQRAELRAAIAALRFRSWIIdpdgegLKTVVIATD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1805791167 206 SMFTINGITNWVQGWKKNGWKTSAGKEVINKEDFVALERLTQ-----GMDIQWMHVPGHSgfigNEEADRLAREGAK 277
Cdd:cd13934    81 SEYVVKGATEWIPKWKRNGWRTSKGKPVKNRDLFELLLDEIEdleegGVEVQFWHVPREL----NKEADRLAKAAAE 153
RnhA COG0328
Ribonuclease HI [Replication, recombination and repair];
140-276 3.74e-36

Ribonuclease HI [Replication, recombination and repair];


Pssm-ID: 440097 [Multi-domain]  Cd Length: 136  Bit Score: 125.73  E-value: 3.74e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791167 140 VVVYTDGCCSSNgrrrP-RAGIGVYWGPGHPLLP-----GRQTNQRAEIHAACKAIEQAKTQNINKLVLYTDSMFTINGI 213
Cdd:COG0328     3 IEIYTDGACRGN----PgPGGWGAVIRYGGEEKElsgglGDTTNNRAELTALIAALEALKELGPCEVEIYTDSQYVVNQI 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1805791167 214 TNWVQGWKKNGWktsagKEVINKEDFVALERLTQGMDIQWMHVPGHSGFIGNEEADRLAREGA 276
Cdd:COG0328    79 TGWIHGWKKNGW-----KPVKNPDLWQRLDELLARHKVTFEWVKGHAGHPGNERADALANKAL 136
Rnh1 COG3341
Ribonuclease HI-related protein, contains viroplasmin and RNaseH domains [General function ...
 28-277 1.71e-33

Ribonuclease HI-related protein, contains viroplasmin and RNaseH domains [General function prediction only];


Pssm-ID: 442570 [Multi-domain]  Cd Length: 203  Bit Score: 121.11  E-value: 1.71e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791167  28 FYAVRRGRKTGVFLTWNECRAQVDRFPAARFKKFATEDEAWAFVRksaspevseghenqhGQESEAKASKRLREPLDGDG 107
Cdd:COG3341     5 FYAVWKGRKPGIYTTWDECKAQVKGFPGAKYKSFKTKEEAEAALN---------------GNYEDYKGKKKKLSEIELDS 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791167 108 hesaepyakhmkpsvepappvsrdtfsymgdfVVVYTDGCCSSNgrrrP----------RAGIGVYWGPGH--PLLPGRq 175
Cdd:COG3341    70 --------------------------------IAVYVDGSCSGN----PgvyeyggvdtKTGKETFSELFHdgPFAEGT- 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791167 176 tNQRAEIHAACKAIEQAKTQNInKLVLYTDSMftinGITNWVQG-WKKNGWKTSAGKEvinkedFVALERLTQGMDIQWM 254
Cdd:COG3341   113 -NNAGEFLAAVHALAYLKKKGS-KLPIYSDYR----GAISWVKGkWKTKLERTQAYKE------LFDLIEKKNTYENPFV 180

                         250       260
                  ....*....|....*....|...
gi 1805791167 255 HVPGHSGFIGNEEADRLAREGAK 277
Cdd:COG3341   181 KVKTHSGDKWNEIPDDLARKALG 203
rnhA PRK00203
ribonuclease H; Reviewed
 140-278 2.13e-29

ribonuclease H; Reviewed


Pssm-ID: 178927 [Multi-domain]  Cd Length: 150  Bit Score: 108.76  E-value: 2.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791167 140 VVVYTDGCCSSNgrrrP-RAGIGVY----------WGpGHPLlpgrQTNQRAEIHAACKAIEQAKTQNinKLVLYTDSMF 208
Cdd:PRK00203    4 VEIYTDGACLGN----PgPGGWGAIlrykghekelSG-GEAL----TTNNRMELMAAIEALEALKEPC--EVTLYTDSQY 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791167 209 TINGITNWVQGWKKNGWKTSAGKEVINKEDFVALERLTQGMDIQWMHVPGHSGFIGNEEADRLAREGAKQ 278
Cdd:PRK00203   73 VRQGITEWIHGWKKNGWKTADKKPVKNVDLWQRLDAALKRHQIKWHWVKGHAGHPENERCDELARAGAEE 142
RNase_H_like cd06222
Ribonuclease H-like superfamily, including RNase H, HI, HII, HIII, and RNase-like domain IV of ...
 142-273 6.60e-23

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.


Pssm-ID: 259998 [Multi-domain]  Cd Length: 121  Bit Score: 90.84  E-value: 6.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791167 142 VYTDGCCSSNGRRrprAGIGVYW--GPGHPL-----LPGRQTNQRAEIHAACKAIEQAKTQNINKLVLYTDSMFTINGIT 214
Cdd:cd06222     1 INVDGSCRGNPGP---AGIGGVLrdHEGGWLggfalKIGAPTALEAELLALLLALELALDLGYLKVIIESDSKYVVDLIN 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1805791167 215 NWVQGWKKNGwktsagkevinKEDFVALERLTQGMDIQWMHVPGHsgfiGNEEADRLAR 273
Cdd:cd06222    78 SGSFKWSPNI-----------LLIEDILLLLSRFWSVKISHVPRE----GNQVADALAK 121
Cauli_VI pfam01693
Caulimovirus viroplasmin; This family consists of various caulimovirus viroplasmin proteins. ...
 28-70 5.44e-20

Caulimovirus viroplasmin; This family consists of various caulimovirus viroplasmin proteins. The viroplasmin protein is encoded by gene VI and is the main component of viral inclusion bodies or viroplasms. Inclusions are the site of viral assembly, DNA synthesis and accumulation. Two domains exist within gene VI corresponding approximately to the 5' third and middle third of gene VI, these influence systemic infection in a light-dependent manner.


Pssm-ID: 460297 [Multi-domain]  Cd Length: 44  Bit Score: 80.91  E-value: 5.44e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1805791167  28 FYAVRRGRKTGVFLTWNECRAQVDRFPAARFKKFATEDEAWAF 70
Cdd:pfam01693   2 YYAVAKGRKPGIYTTWDECKAQVKGFPGAKYKSFKTREEAEAF 44
RNase_HI_bacteria_like cd09277
Bacterial RNase HI containing a hybrid binding domain (HBD) at the N-terminus; Ribonuclease H ...
 181-275 3.81e-17

Bacterial RNase HI containing a hybrid binding domain (HBD) at the N-terminus; 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 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. Some bacteria distinguished from other bacterial RNase HI in the presence of a hybrid binding domain (HBD) at the N-terminus which is commonly present at the N-termini of eukaryotic RNase HI. It has been reported that this domain is required for dimerization and processivity of RNase HI upon binding to RNA-DNA hybrids.


Pssm-ID: 260009 [Multi-domain]  Cd Length: 133  Bit Score: 75.98  E-value: 3.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791167 181 EIHAACKAIEQAKTQNINKLVLYTDSMftinGITNWVQG-WKKNGWKTSAGKEVINKedfvalerLTQGMDIQWMHVPGH 259
Cdd:cd09277    49 EIKGAMKAIKYAIENGIKKITIYYDYE----GIEKWATGeWKANKELTKEYKEFMQK--------YKKKIKIEFVKVKAH 116

                          90
                  ....*....|....*.
gi 1805791167 260 SGFIGNEEADRLAREG 275
Cdd:cd09277   117 SGDKYNELADKLAKKA 132
PRK08719 PRK08719
ribonuclease H; Reviewed
 141-277 4.44e-16

ribonuclease H; Reviewed


Pssm-ID: 236334 [Multi-domain]  Cd Length: 147  Bit Score: 73.36  E-value: 4.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791167 141 VVYTDGCCSSNGRRRPRAGIG--VYWGPGHPL------LPGRQTNQRAEIHAACKAIEQAKTQNinklVLYTDSMFTING 212
Cdd:PRK08719    6 SIYIDGAAPNNQHGCVRGGIGlvVYDEAGEIVdeqsitVNRYTDNAELELLALIEALEYARDGD----VIYSDSDYCVRG 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1805791167 213 ITNWVQGWKKNGWKTSAGKEVINKEDFVALERLTQGMDIQWMHVPGHSGFIGNEEADRLAREGAK 277
Cdd:PRK08719   82 FNEWLDTWKQKGWRKSDKKPVANRDLWQQVDELRARKYVEVEKVTAHSGIEGNEAADMLAQAAAE 146
Rnase_HI_RT_non_LTR cd09276
non-LTR RNase HI domain of reverse transcriptases; Ribonuclease H (RNase H) is classified into ...
 141-277 5.40e-14

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.


Pssm-ID: 260008 [Multi-domain]  Cd Length: 131  Bit Score: 67.24  E-value: 5.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791167 141 VVYTDGccSSNGRRrprAGIGVYWGPGHPL------LPGRQTNQRAEIHAACKAIEQAKTQ--NINKLVLYTDSMFTING 212
Cdd:cd09276     1 VIYTDG--SKLEGS---VGAGFVIYRGGEVisrsyrLGTHASVFDAELEAILEALELALATarRARKVTIFTDSQSALQA 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1805791167 213 ITNWvqgwkkngwkTSAGKEVINKEDFVALERLTQG---MDIQWmhVPGHSGFIGNEEADRLAREGAK 277
Cdd:cd09276    76 LRNP----------RRSSGQVILIRILRLLRLLKAKgvkVRLRW--VPGHVGIEGNEAADRLAKEAAS 131
PRK06548 PRK06548
ribonuclease H; Provisional
 176-276 4.67e-13

ribonuclease H; Provisional


Pssm-ID: 75628 [Multi-domain]  Cd Length: 161  Bit Score: 65.61  E-value: 4.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791167 176 TNQRAEIhAACKAIEQAKTQNINKLVLYTDSMFTINGITNWVQGWKKNGWKTSAGKEVINKEDFVALERLTQGMDIQWMH 255
Cdd:PRK06548   41 TNNIAEL-TAVRELLIATRHTDRPILILSDSKYVINSLTKWVYSWKMRKWRKADGKPVLNQEIIQEIDSLMENRNIRMSW 119

                          90       100
                  ....*....|....*....|.
gi 1805791167 256 VPGHSGFIGNEEADRLAREGA 276
Cdd:PRK06548  120 VNAHTGHPLNEAADSLARQAA 140
RNase_HI_like cd09279
RNAse HI family that includes archaeal, some bacterial as well as plant RNase HI; Ribonuclease ...
 140-277 1.90e-11

RNAse HI family that includes archaeal, some bacterial as well as plant RNase HI; 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. Most archaeal genomes contain only type 2 RNase H (RNase HII); however, a few contain RNase HI as well. Although archaeal RNase HI sequences conserve the DEDD active-site motif, they lack other common features important for catalytic function, such as the basic protrusion region. Archaeal RNase HI homologs are more closely related to retroviral RNase HI than bacterial and eukaryotic type I RNase H in enzymatic properties.


Pssm-ID: 260011 [Multi-domain]  Cd Length: 128  Bit Score: 60.18  E-value: 1.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791167 140 VVVYTDGccSSNGRRRPrAGIGVYW-GPGHPL------LPGRQTNQRAEIHAACKAIEQAKTQNINKLVLYTDSMFTING 212
Cdd:cd09279     1 WTLYFDG--ASRGNPGP-AGAGVVIySPGGEVlelserLGFPATNNEAEYEALIAGLELALELGAEKLEIYGDSQLVVNQ 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791167 213 ITnwvqgwkkngwktsaGKEVINKEDFV-----ALERLTQGMDIQWMHVPGHSgfigNEEADRLAREGAK 277
Cdd:cd09279    78 LN---------------GEYKVKNERLKpllekVLELLAKFELVELKWIPREQ----NKEADALANQALD 128
RNase_HI_RT_Bel cd09273
Bel/Pao family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) enzymes ...
 141-276 3.80e-09

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.


Pssm-ID: 260005 [Multi-domain]  Cd Length: 131  Bit Score: 53.88  E-value: 3.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791167 141 VVYTDGCCSsngrrrpRAGIGVYWGPGH---PLLPGRQTNQRAEIHAACKAIEQAKTQNINklvLYTDSMFTINGITNWV 217
Cdd:cd09273     1 TVFTDGSSF-------KAGYAIVSGTEIveaQPLPPGTSAQRAELIALIQALELAKGKPVN---IYTDSAYAVHALHLLE 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1805791167 218 QGWKKNGWKtsagKEVINKEDFVALERLTQGMD-IQWMHVPGHS---GFI--GNEEADRLAREGA 276
Cdd:cd09273    71 TIGIERGFL----KSIKNLSLFLQLLEAVQRPKpVAIIHIRAHSklpGPLaeGNAQADAAAKQAA 131
 
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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