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Conserved domains on  [gi|26352958|dbj|BAC40109|]
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unnamed protein product [Mus musculus]

Protein Classification

ribonuclease H family protein( domain architecture ID 10174616)

ribonuclease H family protein may specifically degrade the RNA of RNA-DNA hybrids

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 ...
 8-149 3.48e-81

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: 235.92  E-value: 3.48e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352958   8 IVYTDGCCSSNGRKRARAGIGVYWGPGHPLNVGIRLPGR-QTNQRAEIHAACKAIMQAKAQNISKLVLYTDSMFTINGIT 86
Cdd:cd09280   1 VVYTDGSCLNNGKPGARAGIGVYFGPGDPRNVSEPLPGRkQTNNRAELLAVIHALEQAPEEGIRKLEIRTDSKYAINCIT 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26352958  87 NWVQGWKKNGWRTSTGKDVINKEDFMELDELTQ--GMDIQWMHIPGHSGFVGNEEADRLAREGAK 149
Cdd:cd09280  81 KWIPKWKKNGWKTSKGKPVKNQDLIKELDKLLRkrGIKVKFEHVKGHSGDPGNEEADRLAREGAD 145
 
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 ...
 8-149 3.48e-81

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: 235.92  E-value: 3.48e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352958   8 IVYTDGCCSSNGRKRARAGIGVYWGPGHPLNVGIRLPGR-QTNQRAEIHAACKAIMQAKAQNISKLVLYTDSMFTINGIT 86
Cdd:cd09280   1 VVYTDGSCLNNGKPGARAGIGVYFGPGDPRNVSEPLPGRkQTNNRAELLAVIHALEQAPEEGIRKLEIRTDSKYAINCIT 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26352958  87 NWVQGWKKNGWRTSTGKDVINKEDFMELDELTQ--GMDIQWMHIPGHSGFVGNEEADRLAREGAK 149
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 ...
 5-149 6.74e-62

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: 186.81  E-value: 6.74e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352958     5 ESVIVYTDGCCSSNgRKRARAGIGVYwgPGHPlNVGIRLPGRQTNQRAEIHAACKAIMQAKAQniSKLVLYTDSMFTING 84
Cdd:pfam00075   2 KAVTVYTDGSCLGN-PGPGGAGAVLY--RGHE-NISAPLPGRTTNNRAELQAVIEALKALKSP--SKVNIYTDSQYVIGG 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26352958    85 ITNWVQGWKKNGWR-TSTGKDVINKEDFMELDELTQGMDIQWMHIPGHSGFVGNEEADRLAREGAK 149
Cdd:pfam00075  76 ITQWVHGWKKNGWPtTSEGKPVKNKDLWQLLKALCKKHQVYWQWVKGHAGNPGNEMADRLAKQGAE 141
RnhA COG0328
Ribonuclease HI [Replication, recombination and repair];
7-148 3.56e-38

Ribonuclease HI [Replication, recombination and repair];


Pssm-ID: 440097 [Multi-domain]  Cd Length: 136  Bit Score: 126.50  E-value: 3.56e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352958   7 VIVYTDGCCSSN-GRkrarAGIGV---YWGPGHPLNVGIrlpGRQTNQRAEIHAACKAIMQAKAQNISKLVLYTDSMFTI 82
Cdd:COG0328   3 IEIYTDGACRGNpGP----GGWGAvirYGGEEKELSGGL---GDTTNNRAELTALIAALEALKELGPCEVEIYTDSQYVV 75

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26352958  83 NGITNWVQGWKKNGWrtstgKDVINKEDFMELDELTQGMDIQWMHIPGHSGFVGNEEADRLAREGA 148
Cdd:COG0328  76 NQITGWIHGWKKNGW-----KPVKNPDLWQRLDELLARHKVTFEWVKGHAGHPGNERADALANKAL 136
rnhA PRK00203
ribonuclease H; Reviewed
 6-150 2.64e-29

ribonuclease H; Reviewed


Pssm-ID: 178927 [Multi-domain]  Cd Length: 150  Bit Score: 104.52  E-value: 2.64e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352958    6 SVIVYTDGCCSSNGrkrARAGIGVY----------WGpGHPLNvgirlpgrqTNQRAEIHAAckaIMQAKA-QNISKLVL 74
Cdd:PRK00203   3 QVEIYTDGACLGNP---GPGGWGAIlrykghekelSG-GEALT---------TNNRMELMAA---IEALEAlKEPCEVTL 66

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26352958   75 YTDSMFTINGITNWVQGWKKNGWRTSTGKDVINKEDFMELDELTQGMDIQWMHIPGHSGFVGNEEADRLAREGAKQ 150
Cdd:PRK00203  67 YTDSQYVRQGITEWIHGWKKNGWKTADKKPVKNVDLWQRLDAALKRHQIKWHWVKGHAGHPENERCDELARAGAEE 142
 
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 ...
 8-149 3.48e-81

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: 235.92  E-value: 3.48e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352958   8 IVYTDGCCSSNGRKRARAGIGVYWGPGHPLNVGIRLPGR-QTNQRAEIHAACKAIMQAKAQNISKLVLYTDSMFTINGIT 86
Cdd:cd09280   1 VVYTDGSCLNNGKPGARAGIGVYFGPGDPRNVSEPLPGRkQTNNRAELLAVIHALEQAPEEGIRKLEIRTDSKYAINCIT 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26352958  87 NWVQGWKKNGWRTSTGKDVINKEDFMELDELTQ--GMDIQWMHIPGHSGFVGNEEADRLAREGAK 149
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 ...
 5-149 6.74e-62

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: 186.81  E-value: 6.74e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352958     5 ESVIVYTDGCCSSNgRKRARAGIGVYwgPGHPlNVGIRLPGRQTNQRAEIHAACKAIMQAKAQniSKLVLYTDSMFTING 84
Cdd:pfam00075   2 KAVTVYTDGSCLGN-PGPGGAGAVLY--RGHE-NISAPLPGRTTNNRAELQAVIEALKALKSP--SKVNIYTDSQYVIGG 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26352958    85 ITNWVQGWKKNGWR-TSTGKDVINKEDFMELDELTQGMDIQWMHIPGHSGFVGNEEADRLAREGAK 149
Cdd:pfam00075  76 ITQWVHGWKKNGWPtTSEGKPVKNKDLWQLLKALCKKHQVYWQWVKGHAGNPGNEMADRLAKQGAE 141
RNase_H_Dikarya_like cd13934
Fungal (dikarya) Ribonuclease H, uncharacterized; This family contains dikarya RNase H, many ...
 8-149 3.10e-46

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: 147.73  E-value: 3.10e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352958   8 IVYTDGCCSSNGRKRARAGIGVYWGPGHPLNVGIRLP----GRQTNQRAEIHAACKAIMQAK------AQNISKLVLYTD 77
Cdd:cd13934   1 LVYIDGACRNNGRPDARAGYGVYFGPDSSYNVSGRLEdtggHPQTSQRAELRAAIAALRFRSwiidpdGEGLKTVVIATD 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26352958  78 SMFTINGITNWVQGWKKNGWRTSTGKDVINKEDFMELDELTQ-----GMDIQWMHIPGHSgfvgNEEADRLAREGAK 149
Cdd:cd13934  81 SEYVVKGATEWIPKWKRNGWRTSKGKPVKNRDLFELLLDEIEdleegGVEVQFWHVPREL----NKEADRLAKAAAE 153
RNase_HI_prokaryote_like cd09278
RNase HI family found mainly in prokaryotes; Ribonuclease H (RNase H) is classified into two ...
 6-149 2.59e-42

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: 137.23  E-value: 2.59e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352958   6 SVIVYTDGCCSSNGRKRARAGIGVYWGPGHPLNVGIRlpgRQTNQRAEIHAACKAIMQAKaqNISKLVLYTDSMFTINGI 85
Cdd:cd09278   1 EIVIYTDGACLGNPGPGGWAAVIRYGDHEKELSGGEP---GTTNNRMELTAAIEALEALK--EPCPVTIYTDSQYVINGI 75

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26352958  86 TNWVQGWKKNGWRTSTGKDVINKEDFMELDELTQGMDIQWMHIPGHSGFVGNEEADRLAREGAK 149
Cdd:cd09278  76 TKWIKGWKKNGWKTADGKPVKNRDLWQELDALLAGHKVTWEWVKGHAGHPGNERADRLANKAAD 139
RnhA COG0328
Ribonuclease HI [Replication, recombination and repair];
7-148 3.56e-38

Ribonuclease HI [Replication, recombination and repair];


Pssm-ID: 440097 [Multi-domain]  Cd Length: 136  Bit Score: 126.50  E-value: 3.56e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352958   7 VIVYTDGCCSSN-GRkrarAGIGV---YWGPGHPLNVGIrlpGRQTNQRAEIHAACKAIMQAKAQNISKLVLYTDSMFTI 82
Cdd:COG0328   3 IEIYTDGACRGNpGP----GGWGAvirYGGEEKELSGGL---GDTTNNRAELTALIAALEALKELGPCEVEIYTDSQYVV 75

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26352958  83 NGITNWVQGWKKNGWrtstgKDVINKEDFMELDELTQGMDIQWMHIPGHSGFVGNEEADRLAREGA 148
Cdd:COG0328  76 NQITGWIHGWKKNGW-----KPVKNPDLWQRLDELLARHKVTFEWVKGHAGHPGNERADALANKAL 136
rnhA PRK00203
ribonuclease H; Reviewed
 6-150 2.64e-29

ribonuclease H; Reviewed


Pssm-ID: 178927 [Multi-domain]  Cd Length: 150  Bit Score: 104.52  E-value: 2.64e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352958    6 SVIVYTDGCCSSNGrkrARAGIGVY----------WGpGHPLNvgirlpgrqTNQRAEIHAAckaIMQAKA-QNISKLVL 74
Cdd:PRK00203   3 QVEIYTDGACLGNP---GPGGWGAIlrykghekelSG-GEALT---------TNNRMELMAA---IEALEAlKEPCEVTL 66

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26352958   75 YTDSMFTINGITNWVQGWKKNGWRTSTGKDVINKEDFMELDELTQGMDIQWMHIPGHSGFVGNEEADRLAREGAKQ 150
Cdd:PRK00203  67 YTDSQYVRQGITEWIHGWKKNGWKTADKKPVKNVDLWQRLDAALKRHQIKWHWVKGHAGHPENERCDELARAGAEE 142
RNase_H_like cd06222
Ribonuclease H-like superfamily, including RNase H, HI, HII, HIII, and RNase-like domain IV of ...
 9-145 6.62e-24

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: 89.68  E-value: 6.62e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352958   9 VYTDGCCSSNGRkraRAGIGVYW--GPGHPLNVGIRLPGRQTNQRAEIHAACKAIMQAKAQNISKLVLYTDSMFTINGIT 86
Cdd:cd06222   1 INVDGSCRGNPG---PAGIGGVLrdHEGGWLGGFALKIGAPTALEAELLALLLALELALDLGYLKVIIESDSKYVVDLIN 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 26352958  87 NWVQGWKKNGwrtstgkdvinKEDFMELDELTQGMDIQWMHIPGHsgfvGNEEADRLAR 145
Cdd:cd06222  78 SGSFKWSPNI-----------LLIEDILLLLSRFWSVKISHVPRE----GNQVADALAK 121
PRK08719 PRK08719
ribonuclease H; Reviewed
 6-149 7.37e-20

ribonuclease H; Reviewed


Pssm-ID: 236334 [Multi-domain]  Cd Length: 147  Bit Score: 80.29  E-value: 7.37e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352958    6 SVIVYTDGCCSSNGRKRARAGIG--VYWGPGHPLN-VGIRLPGRQTNQRAEIHAACKAIMQAKAQNisklVLYTDSMFTI 82
Cdd:PRK08719   4 SYSIYIDGAAPNNQHGCVRGGIGlvVYDEAGEIVDeQSITVNRYTDNAELELLALIEALEYARDGD----VIYSDSDYCV 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26352958   83 NGITNWVQGWKKNGWRTSTGKDVINKEDFMELDELTQGMDIQWMHIPGHSGFVGNEEADRLAREGAK 149
Cdd:PRK08719  80 RGFNEWLDTWKQKGWRKSDKKPVANRDLWQQVDELRARKYVEVEKVTAHSGIEGNEAADMLAQAAAE 146
PRK06548 PRK06548
ribonuclease H; Provisional
 48-148 2.77e-17

ribonuclease H; Provisional


Pssm-ID: 75628 [Multi-domain]  Cd Length: 161  Bit Score: 74.08  E-value: 2.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352958   48 TNQRAEIhAACKAIMQAKAQNISKLVLYTDSMFTINGITNWVQGWKKNGWRTSTGKDVINKEDFMELDELTQGMDIQWMH 127
Cdd:PRK06548  41 TNNIAEL-TAVRELLIATRHTDRPILILSDSKYVINSLTKWVYSWKMRKWRKADGKPVLNQEIIQEIDSLMENRNIRMSW 119

                         90       100
                 ....*....|....*....|.
gi 26352958  128 IPGHSGFVGNEEADRLAREGA 148
Cdd:PRK06548 120 VNAHTGHPLNEAADSLARQAA 140
RNase_HI_bacteria_like cd09277
Bacterial RNase HI containing a hybrid binding domain (HBD) at the N-terminus; Ribonuclease H ...
 7-147 4.15e-16

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: 69.82  E-value: 4.15e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352958   7 VIVYTDGccS-SNGRKRARAGIGVYWGpghplNVGIRLPGRQTNQRA--------EIHAACKAIMQAKAQNISKLVLYTD 77
Cdd:cd09277   1 VIAYVDG--SyNKETKKYGYGVVIIKN-----GKEEEFSGSGNDPEYasmrnvagEIKGAMKAIKYAIENGIKKITIYYD 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26352958  78 SMftinGITNWVQG-WKKNgwrtstgkDVINKE--DFMelDELTQGMDIQWMHIPGHSGFVGNEEADRLAREG 147
Cdd:cd09277  74 YE----GIEKWATGeWKAN--------KELTKEykEFM--QKYKKKIKIEFVKVKAHSGDKYNELADKLAKKA 132
Rnase_HI_RT_non_LTR cd09276
non-LTR RNase HI domain of reverse transcriptases; Ribonuclease H (RNase H) is classified into ...
 9-149 6.64e-16

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: 69.55  E-value: 6.64e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352958   9 VYTDGccsSNGRKRARAGIGVYWGpGHPLNVGIRLPGRQTNQRAEIHAACKAIMQAKAQ--NISKLVLYTDSMFTINGIT 86
Cdd:cd09276   2 IYTDG---SKLEGSVGAGFVIYRG-GEVISRSYRLGTHASVFDAELEAILEALELALATarRARKVTIFTDSQSALQALR 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26352958  87 NWvqgwkkngwrTSTGKDVINKEDFMELDELTQG---MDIQWmhIPGHSGFVGNEEADRLAREGAK 149
Cdd:cd09276  78 NP----------RRSSGQVILIRILRLLRLLKAKgvkVRLRW--VPGHVGIEGNEAADRLAKEAAS 131
RNase_HI_like cd09279
RNAse HI family that includes archaeal, some bacterial as well as plant RNase HI; Ribonuclease ...
 7-149 4.75e-12

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: 59.41  E-value: 4.75e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352958   7 VIVYTDGCCSSNGRkraRAGIGVYW--GPGHPLNVGIRLPGRQTNQRAEIHAACKAIMQAKAQNISKLVLYTDSMFTING 84
Cdd:cd09279   1 WTLYFDGASRGNPG---PAGAGVVIysPGGEVLELSERLGFPATNNEAEYEALIAGLELALELGAEKLEIYGDSQLVVNQ 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352958  85 ItnwvqgwkkngwrtsTGKDVINKEDFMEL-----DELTQGMDIQWMHIPGHSgfvgNEEADRLAREGAK 149
Cdd:cd09279  78 L---------------NGEYKVKNERLKPLlekvlELLAKFELVELKWIPREQ----NKEADALANQALD 128
RNase_HI_RT_Bel cd09273
Bel/Pao family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) enzymes ...
 9-148 1.32e-08

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: 50.41  E-value: 1.32e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352958   9 VYTDGCCSsngrkraRAGIGVYWGPGHPLNVGirLPGRQTNQRAEIHAACKAIMQAKAQ--NIsklvlYTDSMFTINGIT 86
Cdd:cd09273   2 VFTDGSSF-------KAGYAIVSGTEIVEAQP--LPPGTSAQRAELIALIQALELAKGKpvNI-----YTDSAYAVHALH 67

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26352958  87 NWVQGWKKNGWRtstgKDVINKEDFMELDELTQGMD-IQWMHIPGHS---GFV--GNEEADRLAREGA 148
Cdd:cd09273  68 LLETIGIERGFL----KSIKNLSLFLQLLEAVQRPKpVAIIHIRAHSklpGPLaeGNAQADAAAKQAA 131
flgL PRK08027
flagellar hook-filament junction protein FlgL;
69-110 6.83e-03

flagellar hook-filament junction protein FlgL;


Pssm-ID: 181202 [Multi-domain]  Cd Length: 317  Bit Score: 35.50  E-value: 6.83e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 26352958   69 ISKLVLYTDSMftiNGITNWVQGWKKNGWRTSTGKDVINKED 110
Cdd:PRK08027   3 LSTQMMYQQNM---RGITNSQAEWMKYGEQMSTGKRVVNPSD 41
 
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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