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Conserved domains on  [gi|1805791173|ref|NP_001365200|]
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ribonuclease H1 isoform 4 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 ...
 141-259 1.21e-63

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: 196.25  E-value: 1.21e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791173 141 VVYTDGCCSSNGRRRPRAGIGVYWGPGHPLNVGIRLPGR-QTNQRAEIHAACKAIEQAKTQNINKLVLYTDSMFTINGIT 219
Cdd:cd09280     1 VVYTDGSCLNNGKPGARAGIGVYFGPGDPRNVSEPLPGRkQTNNRAELLAVIHALEQAPEEGIRKLEIRTDSKYAINCIT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1805791173 220 NWVQGWKKNGWKTSAGKEVINKEDFVALERLTQ--GMDIQWE 259
Cdd:cd09280    81 KWIPKWKKNGWKTSKGKPVKNQDLIKELDKLLRkrGIKVKFE 122
Rnh1 super family cl34588
Ribonuclease HI-related protein, contains viroplasmin and RNaseH domains [General function ...
 28-240 8.19e-27

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


The actual alignment was detected with superfamily member COG3341:

Pssm-ID: 442570 [Multi-domain]  Cd Length: 203  Bit Score: 103.39  E-value: 8.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791173  28 FYAVRRGRKTGVFLTWNECRAQVDRFPAARFKKFATEDEAWAFVRksaspevseghenqhGQESEAKASKRLREPLDGDG 107
Cdd:COG3341     5 FYAVWKGRKPGIYTTWDECKAQVKGFPGAKYKSFKTKEEAEAALN---------------GNYEDYKGKKKKLSEIELDS 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791173 108 hesaepyakhmkpsvepappvsrdtfsymgdfVVVYTDGCCSSNgrrRPRAGIGVYW---GPGHPLNVGIRLPGRQ-TNQ 183
Cdd:COG3341    70 --------------------------------IAVYVDGSCSGN---PGVYEYGGVDtktGKETFSELFHDGPFAEgTNN 114

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1805791173 184 RAEIHAACKAIEQAKTQNInKLVLYTDSMftinGITNWVQG-WKKNGWKTSAGKEVIN 240
Cdd:COG3341   115 AGEFLAAVHALAYLKKKGS-KLPIYSDYR----GAISWVKGkWKTKLERTQAYKELFD 167
 
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 ...
 141-259 1.21e-63

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: 196.25  E-value: 1.21e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791173 141 VVYTDGCCSSNGRRRPRAGIGVYWGPGHPLNVGIRLPGR-QTNQRAEIHAACKAIEQAKTQNINKLVLYTDSMFTINGIT 219
Cdd:cd09280     1 VVYTDGSCLNNGKPGARAGIGVYFGPGDPRNVSEPLPGRkQTNNRAELLAVIHALEQAPEEGIRKLEIRTDSKYAINCIT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1805791173 220 NWVQGWKKNGWKTSAGKEVINKEDFVALERLTQ--GMDIQWE 259
Cdd:cd09280    81 KWIPKWKKNGWKTSKGKPVKNQDLIKELDKLLRkrGIKVKFE 122
RNase_H pfam00075
RNase H; RNase H digests the RNA strand of an RNA/DNA hybrid. Important enzyme in retroviral ...
 140-262 1.52e-41

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: 139.82  E-value: 1.52e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791173 140 VVVYTDGCCSSNGRRRpRAGIGVYwgPGHPlNVGIRLPGRQTNQRAEIHAACKAIEQAKTQNinKLVLYTDSMFTINGIT 219
Cdd:pfam00075   4 VTVYTDGSCLGNPGPG-GAGAVLY--RGHE-NISAPLPGRTTNNRAELQAVIEALKALKSPS--KVNIYTDSQYVIGGIT 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1805791173 220 NWVQGWKKNGWK-TSAGKEVINKEDFVALERLTQGMDIQWENIY 262
Cdd:pfam00075  78 QWVHGWKKNGWPtTSEGKPVKNKDLWQLLKALCKKHQVYWQWVK 121
Rnh1 COG3341
Ribonuclease HI-related protein, contains viroplasmin and RNaseH domains [General function ...
 28-240 8.19e-27

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


Pssm-ID: 442570 [Multi-domain]  Cd Length: 203  Bit Score: 103.39  E-value: 8.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791173  28 FYAVRRGRKTGVFLTWNECRAQVDRFPAARFKKFATEDEAWAFVRksaspevseghenqhGQESEAKASKRLREPLDGDG 107
Cdd:COG3341     5 FYAVWKGRKPGIYTTWDECKAQVKGFPGAKYKSFKTKEEAEAALN---------------GNYEDYKGKKKKLSEIELDS 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791173 108 hesaepyakhmkpsvepappvsrdtfsymgdfVVVYTDGCCSSNgrrRPRAGIGVYW---GPGHPLNVGIRLPGRQ-TNQ 183
Cdd:COG3341    70 --------------------------------IAVYVDGSCSGN---PGVYEYGGVDtktGKETFSELFHDGPFAEgTNN 114

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1805791173 184 RAEIHAACKAIEQAKTQNInKLVLYTDSMftinGITNWVQG-WKKNGWKTSAGKEVIN 240
Cdd:COG3341   115 AGEFLAAVHALAYLKKKGS-KLPIYSDYR----GAISWVKGkWKTKLERTQAYKELFD 167
RnhA COG0328
Ribonuclease HI [Replication, recombination and repair];
140-259 3.59e-23

Ribonuclease HI [Replication, recombination and repair];


Pssm-ID: 440097 [Multi-domain]  Cd Length: 136  Bit Score: 91.83  E-value: 3.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791173 140 VVVYTDGCCSSNgrrrP-RAGIGV---YWGPGHPLNVGIrlpGRQTNQRAEIHAACKAIEQAKTQNINKLVLYTDSMFTI 215
Cdd:COG0328     3 IEIYTDGACRGN----PgPGGWGAvirYGGEEKELSGGL---GDTTNNRAELTALIAALEALKELGPCEVEIYTDSQYVV 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1805791173 216 NGITNWVQGWKKNGWktsagKEVINKEDFVALERLTQGMDIQWE 259
Cdd:COG0328    76 NQITGWIHGWKKNGW-----KPVKNPDLWQRLDELLARHKVTFE 114
Cauli_VI pfam01693
Caulimovirus viroplasmin; This family consists of various caulimovirus viroplasmin proteins. ...
 28-70 2.63e-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: 81.30  E-value: 2.63e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1805791173  28 FYAVRRGRKTGVFLTWNECRAQVDRFPAARFKKFATEDEAWAF 70
Cdd:pfam01693   2 YYAVAKGRKPGIYTTWDECKAQVKGFPGAKYKSFKTREEAEAF 44
rnhA PRK00203
ribonuclease H; Reviewed
 140-258 9.98e-18

ribonuclease H; Reviewed


Pssm-ID: 178927 [Multi-domain]  Cd Length: 150  Bit Score: 77.56  E-value: 9.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791173 140 VVVYTDGCCSSNgrrrP-RAGIGVY----------WGpGHPLNvgirlpgrqTNQRAEIHAACKAIEQAKTQNinKLVLY 208
Cdd:PRK00203    4 VEIYTDGACLGN----PgPGGWGAIlrykghekelSG-GEALT---------TNNRMELMAAIEALEALKEPC--EVTLY 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1805791173 209 TDSMFTINGITNWVQGWKKNGWKTSAGKEVINKEDFVALERLTQGMDIQW 258
Cdd:PRK00203   68 TDSQYVRQGITEWIHGWKKNGWKTADKKPVKNVDLWQRLDAALKRHQIKW 117
 
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 ...
 141-259 1.21e-63

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: 196.25  E-value: 1.21e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791173 141 VVYTDGCCSSNGRRRPRAGIGVYWGPGHPLNVGIRLPGR-QTNQRAEIHAACKAIEQAKTQNINKLVLYTDSMFTINGIT 219
Cdd:cd09280     1 VVYTDGSCLNNGKPGARAGIGVYFGPGDPRNVSEPLPGRkQTNNRAELLAVIHALEQAPEEGIRKLEIRTDSKYAINCIT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1805791173 220 NWVQGWKKNGWKTSAGKEVINKEDFVALERLTQ--GMDIQWE 259
Cdd:cd09280    81 KWIPKWKKNGWKTSKGKPVKNQDLIKELDKLLRkrGIKVKFE 122
RNase_H pfam00075
RNase H; RNase H digests the RNA strand of an RNA/DNA hybrid. Important enzyme in retroviral ...
 140-262 1.52e-41

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: 139.82  E-value: 1.52e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791173 140 VVVYTDGCCSSNGRRRpRAGIGVYwgPGHPlNVGIRLPGRQTNQRAEIHAACKAIEQAKTQNinKLVLYTDSMFTINGIT 219
Cdd:pfam00075   4 VTVYTDGSCLGNPGPG-GAGAVLY--RGHE-NISAPLPGRTTNNRAELQAVIEALKALKSPS--KVNIYTDSQYVIGGIT 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1805791173 220 NWVQGWKKNGWK-TSAGKEVINKEDFVALERLTQGMDIQWENIY 262
Cdd:pfam00075  78 QWVHGWKKNGWPtTSEGKPVKNKDLWQLLKALCKKHQVYWQWVK 121
RNase_H_Dikarya_like cd13934
Fungal (dikarya) Ribonuclease H, uncharacterized; This family contains dikarya RNase H, many ...
 141-258 2.40e-36

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: 126.54  E-value: 2.40e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791173 141 VVYTDGCCSSNGRRRPRAGIGVYWGPGHPLNVGIRLP----GRQTNQRAEIHAACKAIEQAKTQN------INKLVLYTD 210
Cdd:cd13934     1 LVYIDGACRNNGRPDARAGYGVYFGPDSSYNVSGRLEdtggHPQTSQRAELRAAIAALRFRSWIIdpdgegLKTVVIATD 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1805791173 211 SMFTINGITNWVQGWKKNGWKTSAGKEVINKEDFVALERLTQ-----GMDIQW 258
Cdd:cd13934    81 SEYVVKGATEWIPKWKRNGWRTSKGKPVKNRDLFELLLDEIEdleegGVEVQF 133
RNase_HI_prokaryote_like cd09278
RNase HI family found mainly in prokaryotes; Ribonuclease H (RNase H) is classified into two ...
 140-259 1.14e-28

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: 106.41  E-value: 1.14e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791173 140 VVVYTDGCCSSNgrrrPRAG----IGVYWGPGHPLNVGIRlpgRQTNQRAEIHAACKAIEQAKTQNinKLVLYTDSMFTI 215
Cdd:cd09278     2 IVIYTDGACLGN----PGPGgwaaVIRYGDHEKELSGGEP---GTTNNRMELTAAIEALEALKEPC--PVTIYTDSQYVI 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1805791173 216 NGITNWVQGWKKNGWKTSAGKEVINKEDFVALERLTQGMDIQWE 259
Cdd:cd09278    73 NGITKWIKGWKKNGWKTADGKPVKNRDLWQELDALLAGHKVTWE 116
Rnh1 COG3341
Ribonuclease HI-related protein, contains viroplasmin and RNaseH domains [General function ...
 28-240 8.19e-27

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


Pssm-ID: 442570 [Multi-domain]  Cd Length: 203  Bit Score: 103.39  E-value: 8.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791173  28 FYAVRRGRKTGVFLTWNECRAQVDRFPAARFKKFATEDEAWAFVRksaspevseghenqhGQESEAKASKRLREPLDGDG 107
Cdd:COG3341     5 FYAVWKGRKPGIYTTWDECKAQVKGFPGAKYKSFKTKEEAEAALN---------------GNYEDYKGKKKKLSEIELDS 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791173 108 hesaepyakhmkpsvepappvsrdtfsymgdfVVVYTDGCCSSNgrrRPRAGIGVYW---GPGHPLNVGIRLPGRQ-TNQ 183
Cdd:COG3341    70 --------------------------------IAVYVDGSCSGN---PGVYEYGGVDtktGKETFSELFHDGPFAEgTNN 114

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1805791173 184 RAEIHAACKAIEQAKTQNInKLVLYTDSMftinGITNWVQG-WKKNGWKTSAGKEVIN 240
Cdd:COG3341   115 AGEFLAAVHALAYLKKKGS-KLPIYSDYR----GAISWVKGkWKTKLERTQAYKELFD 167
RnhA COG0328
Ribonuclease HI [Replication, recombination and repair];
140-259 3.59e-23

Ribonuclease HI [Replication, recombination and repair];


Pssm-ID: 440097 [Multi-domain]  Cd Length: 136  Bit Score: 91.83  E-value: 3.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791173 140 VVVYTDGCCSSNgrrrP-RAGIGV---YWGPGHPLNVGIrlpGRQTNQRAEIHAACKAIEQAKTQNINKLVLYTDSMFTI 215
Cdd:COG0328     3 IEIYTDGACRGN----PgPGGWGAvirYGGEEKELSGGL---GDTTNNRAELTALIAALEALKELGPCEVEIYTDSQYVV 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1805791173 216 NGITNWVQGWKKNGWktsagKEVINKEDFVALERLTQGMDIQWE 259
Cdd:COG0328    76 NQITGWIHGWKKNGW-----KPVKNPDLWQRLDELLARHKVTFE 114
Cauli_VI pfam01693
Caulimovirus viroplasmin; This family consists of various caulimovirus viroplasmin proteins. ...
 28-70 2.63e-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: 81.30  E-value: 2.63e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1805791173  28 FYAVRRGRKTGVFLTWNECRAQVDRFPAARFKKFATEDEAWAF 70
Cdd:pfam01693   2 YYAVAKGRKPGIYTTWDECKAQVKGFPGAKYKSFKTREEAEAF 44
RNase_H_like cd06222
Ribonuclease H-like superfamily, including RNase H, HI, HII, HIII, and RNase-like domain IV of ...
 142-266 2.27e-18

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: 78.51  E-value: 2.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791173 142 VYTDGCCSSNGRRrprAGIGVYW--GPGHPLNVGIRLPGRQTNQRAEIHAACKAIEQAKTQNINKLVLYTDSMFTINGIT 219
Cdd:cd06222     1 INVDGSCRGNPGP---AGIGGVLrdHEGGWLGGFALKIGAPTALEAELLALLLALELALDLGYLKVIIESDSKYVVDLIN 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1805791173 220 NWVQGWKKNGwktsagkevinKEDFVALERLTQGMDIQWENIY--LNRC 266
Cdd:cd06222    78 SGSFKWSPNI-----------LLIEDILLLLSRFWSVKISHVPreGNQV 115
rnhA PRK00203
ribonuclease H; Reviewed
 140-258 9.98e-18

ribonuclease H; Reviewed


Pssm-ID: 178927 [Multi-domain]  Cd Length: 150  Bit Score: 77.56  E-value: 9.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791173 140 VVVYTDGCCSSNgrrrP-RAGIGVY----------WGpGHPLNvgirlpgrqTNQRAEIHAACKAIEQAKTQNinKLVLY 208
Cdd:PRK00203    4 VEIYTDGACLGN----PgPGGWGAIlrykghekelSG-GEALT---------TNNRMELMAAIEALEALKEPC--EVTLY 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1805791173 209 TDSMFTINGITNWVQGWKKNGWKTSAGKEVINKEDFVALERLTQGMDIQW 258
Cdd:PRK00203   68 TDSQYVRQGITEWIHGWKKNGWKTADKKPVKNVDLWQRLDAALKRHQIKW 117
PRK08719 PRK08719
ribonuclease H; Reviewed
 141-242 4.36e-09

ribonuclease H; Reviewed


Pssm-ID: 236334 [Multi-domain]  Cd Length: 147  Bit Score: 54.10  E-value: 4.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791173 141 VVYTDGCCSSNGRRRPRAGIG--VYWGPGHPLN-VGIRLPGRQTNQRAEIHAACKAIEQAKTQNinklVLYTDSMFTING 217
Cdd:PRK08719    6 SIYIDGAAPNNQHGCVRGGIGlvVYDEAGEIVDeQSITVNRYTDNAELELLALIEALEYARDGD----VIYSDSDYCVRG 81

                          90       100
                  ....*....|....*....|....*
gi 1805791173 218 ITNWVQGWKKNGWKTSAGKEVINKE 242
Cdd:PRK08719   82 FNEWLDTWKQKGWRKSDKKPVANRD 106
RNase_HI_like cd09279
RNAse HI family that includes archaeal, some bacterial as well as plant RNase HI; Ribonuclease ...
 140-219 3.05e-08

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: 51.32  E-value: 3.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791173 140 VVVYTDGccSSNGRRRPrAGIGVYW--GPGHPLNVGIRLPGRQTNQRAEIHAACKAIEQAKTQNINKLVLYTDSMFTING 217
Cdd:cd09279     1 WTLYFDG--ASRGNPGP-AGAGVVIysPGGEVLELSERLGFPATNNEAEYEALIAGLELALELGAEKLEIYGDSQLVVNQ 77


                  ..
gi 1805791173 218 IT 219
Cdd:cd09279    78 LN 79
PRK06548 PRK06548
ribonuclease H; Provisional
 181-262 3.53e-07

ribonuclease H; Provisional


Pssm-ID: 75628 [Multi-domain]  Cd Length: 161  Bit Score: 49.04  E-value: 3.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791173 181 TNQRAEIhAACKAIEQAKTQNINKLVLYTDSMFTINGITNWVQGWKKNGWKTSAGKEVINKEDFVALERLTQGMDIQ--W 258
Cdd:PRK06548   41 TNNIAEL-TAVRELLIATRHTDRPILILSDSKYVINSLTKWVYSWKMRKWRKADGKPVLNQEIIQEIDSLMENRNIRmsW 119


                  ....
gi 1805791173 259 ENIY 262
Cdd:PRK06548  120 VNAH 123
RNase_HI_RT_Bel cd09273
Bel/Pao family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) enzymes ...
 141-252 7.93e-04

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: 38.47  E-value: 7.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791173 141 VVYTDGCCSsngrrrpRAGIGVYWGPGHPLNVGirLPGRQTNQRAEIHAACKAIEQAKTQNINklvLYTDSMFTINGITN 220
Cdd:cd09273     1 TVFTDGSSF-------KAGYAIVSGTEIVEAQP--LPPGTSAQRAELIALIQALELAKGKPVN---IYTDSAYAVHALHL 68

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1805791173 221 WVQGWKKNGWKtsagKEVINKEDFVALERLTQ 252
Cdd:cd09273    69 LETIGIERGFL----KSIKNLSLFLQLLEAVQ 96
 
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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