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Conserved domains on  [gi|358349751|emb|CCE73030|]
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Piso0_000041 [Millerozyma farinosa CBS 7064]

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 ...
 129-298 4.84e-62

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: 193.17  E-value: 4.84e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751 129 RVYVDGASRGNGRKGtPISGYGVFYGAGDSRNAAVPLCDIedaaatKPTNQRAELLAMKHALTDIANEIYGgyedaerqs 208
Cdd:cd09280    1 VVYTDGSCLNNGKPG-ARAGIGVYFGPGDPRNVSEPLPGR------KQTNNRAELLAVIHALEQAPEEGIR--------- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751 209 vRYQIYSDSRYAANCITEWCSKWIANGWKNGQGNAVANKDIIEttyPILNYINQyysnhNWGRLEFFHVAGHSGDYGNEM 288
Cdd:cd09280   65 -KLEIRTDSKYAINCITKWIPKWKKNGWKTSKGKPVKNQDLIK---ELDKLLRK-----RGIKVKFEHVKGHSGDPGNEE 135

                        170
                 ....*....|
gi 358349751 289 ADRLANEGAD 298
Cdd:cd09280  136 ADRLAREGAD 145
Cauli_VI pfam01693
Caulimovirus viroplasmin; This family consists of various caulimovirus viroplasmin proteins. ...
 2-45 3.37e-18

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: 76.29  E-value: 3.37e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 358349751    2 PFYAVARGVRPGIYKNWDSCKKNVLGYKGAVYKKFNSSQQAQEF 45
Cdd:pfam01693   1 KYYAVAKGRKPGIYTTWDECKAQVKGFPGAKYKSFKTREEAEAF 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 ...
 129-298 4.84e-62

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: 193.17  E-value: 4.84e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751 129 RVYVDGASRGNGRKGtPISGYGVFYGAGDSRNAAVPLCDIedaaatKPTNQRAELLAMKHALTDIANEIYGgyedaerqs 208
Cdd:cd09280    1 VVYTDGSCLNNGKPG-ARAGIGVYFGPGDPRNVSEPLPGR------KQTNNRAELLAVIHALEQAPEEGIR--------- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751 209 vRYQIYSDSRYAANCITEWCSKWIANGWKNGQGNAVANKDIIEttyPILNYINQyysnhNWGRLEFFHVAGHSGDYGNEM 288
Cdd:cd09280   65 -KLEIRTDSKYAINCITKWIPKWKKNGWKTSKGKPVKNQDLIK---ELDKLLRK-----RGIKVKFEHVKGHSGDPGNEE 135

                        170
                 ....*....|
gi 358349751 289 ADRLANEGAD 298
Cdd:cd09280  136 ADRLAREGAD 145
RNase_H pfam00075
RNase H; RNase H digests the RNA strand of an RNA/DNA hybrid. Important enzyme in retroviral ...
 130-297 9.28e-29

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: 107.46  E-value: 9.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751  130 VYVDGASRGNGRKGtpisGYG-VFYGAGDSRNAAVPLCDiedaaatkpTNQRAELLAMKHALtdianeiyggyEDAERQS 208
Cdd:pfam00075   6 VYTDGSCLGNPGPG----GAGaVLYRGHENISAPLPGRT---------TNNRAELQAVIEAL-----------KALKSPS 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751  209 vRYQIYSDSRYAANCITEWCSKWIANGWKN-GQGNAVANKDIIETTYPILnyinqyySNHNwgrLEFFHVAGHSGDYGNE 287
Cdd:pfam00075  62 -KVNIYTDSQYVIGGITQWVHGWKKNGWPTtSEGKPVKNKDLWQLLKALC-------KKHQ---VYWQWVKGHAGNPGNE 130

                         170
                  ....*....|
gi 358349751  288 MADRLANEGA 297
Cdd:pfam00075 131 MADRLAKQGA 140
RnhA COG0328
Ribonuclease HI [Replication, recombination and repair];
130-297 1.85e-28

Ribonuclease HI [Replication, recombination and repair];


Pssm-ID: 440097 [Multi-domain]  Cd Length: 136  Bit Score: 106.47  E-value: 1.85e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751 130 VYVDGASRGNGRKGtpisGYGVFYGAGDSRnaaVPLCDIEDAAatkpTNQRAELLAMKHALTDIaneiyggyEDAERQSV 209
Cdd:COG0328    5 IYTDGACRGNPGPG----GWGAVIRYGGEE---KELSGGLGDT----TNNRAELTALIAALEAL--------KELGPCEV 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751 210 RyqIYSDSRYAANCITEWCSKWIANGWKngqgnAVANKDIIETtypilnyINQYYSNHNWgrlEFFHVAGHSGDYGNEMA 289
Cdd:COG0328   66 E--IYTDSQYVVNQITGWIHGWKKNGWK-----PVKNPDLWQR-------LDELLARHKV---TFEWVKGHAGHPGNERA 128


                 ....*...
gi 358349751 290 DRLANEGA 297
Cdd:COG0328  129 DALANKAL 136
rnhA PRK00203
ribonuclease H; Reviewed
 127-298 6.64e-22

ribonuclease H; Reviewed


Pssm-ID: 178927 [Multi-domain]  Cd Length: 150  Bit Score: 89.50  E-value: 6.64e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751 127 MKRV--YVDGASRGNGRKGtpisGYGVFYGAGDSRNAavpLCDIEdaAATkpTNQRAELLAMKHALtdianeiyggyeDA 204
Cdd:PRK00203   1 MKQVeiYTDGACLGNPGPG----GWGAILRYKGHEKE---LSGGE--ALT--TNNRMELMAAIEAL------------EA 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751 205 ERQSVRYQIYSDSRYAANCITEWCSKWIANGWKNGQGNAVANKDIiettypilnyinqyysnhnWGRL---------EFF 275
Cdd:PRK00203  58 LKEPCEVTLYTDSQYVRQGITEWIHGWKKNGWKTADKKPVKNVDL-------------------WQRLdaalkrhqiKWH 118

                        170       180
                 ....*....|....*....|...
gi 358349751 276 HVAGHSGDYGNEMADRLANEGAD 298
Cdd:PRK00203 119 WVKGHAGHPENERCDELARAGAE 141
Cauli_VI pfam01693
Caulimovirus viroplasmin; This family consists of various caulimovirus viroplasmin proteins. ...
 2-45 3.37e-18

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: 76.29  E-value: 3.37e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 358349751    2 PFYAVARGVRPGIYKNWDSCKKNVLGYKGAVYKKFNSSQQAQEF 45
Cdd:pfam01693   1 KYYAVAKGRKPGIYTTWDECKAQVKGFPGAKYKSFKTREEAEAF 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 ...
 129-298 4.84e-62

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: 193.17  E-value: 4.84e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751 129 RVYVDGASRGNGRKGtPISGYGVFYGAGDSRNAAVPLCDIedaaatKPTNQRAELLAMKHALTDIANEIYGgyedaerqs 208
Cdd:cd09280    1 VVYTDGSCLNNGKPG-ARAGIGVYFGPGDPRNVSEPLPGR------KQTNNRAELLAVIHALEQAPEEGIR--------- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751 209 vRYQIYSDSRYAANCITEWCSKWIANGWKNGQGNAVANKDIIEttyPILNYINQyysnhNWGRLEFFHVAGHSGDYGNEM 288
Cdd:cd09280   65 -KLEIRTDSKYAINCITKWIPKWKKNGWKTSKGKPVKNQDLIK---ELDKLLRK-----RGIKVKFEHVKGHSGDPGNEE 135

                        170
                 ....*....|
gi 358349751 289 ADRLANEGAD 298
Cdd:cd09280  136 ADRLAREGAD 145
RNase_H_Dikarya_like cd13934
Fungal (dikarya) Ribonuclease H, uncharacterized; This family contains dikarya RNase H, many ...
 130-298 7.81e-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: 126.16  E-value: 7.81e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751 130 VYVDGASRGNGRkGTPISGYGVFYGAGDSRNAAVPLcdiEDAAATKPTNQRAELLAMKHALTDIANEIYGGYEDAerqsV 209
Cdd:cd13934    2 VYIDGACRNNGR-PDARAGYGVYFGPDSSYNVSGRL---EDTGGHPQTSQRAELRAAIAALRFRSWIIDPDGEGL----K 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751 210 RYQIYSDSRYAANCITEWCSKWIANGWKNGQGNAVANKDIIETtypILNYINQYYSNHNwgRLEFFHVAGHSgdygNEMA 289
Cdd:cd13934   74 TVVIATDSEYVVKGATEWIPKWKRNGWRTSKGKPVKNRDLFEL---LLDEIEDLEEGGV--EVQFWHVPREL----NKEA 144


                 ....*....
gi 358349751 290 DRLANEGAD 298
Cdd:cd13934  145 DRLAKAAAE 153
RNase_HI_prokaryote_like cd09278
RNase HI family found mainly in prokaryotes; Ribonuclease H (RNase H) is classified into two ...
 130-298 5.86e-34

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: 121.05  E-value: 5.86e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751 130 VYVDGASRGNGRKGtpisGYGVFYGAGDSRNAavpLCDIEDAAatkpTNQRAELLAMKHALTDIAneiyggyedaERQSV 209
Cdd:cd09278    4 IYTDGACLGNPGPG----GWAAVIRYGDHEKE---LSGGEPGT----TNNRMELTAAIEALEALK----------EPCPV 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751 210 RyqIYSDSRYAANCITEWCSKWIANGWKNGQGNAVANKDIIETtypilnyINQYYSNHNwgrLEFFHVAGHSGDYGNEMA 289
Cdd:cd09278   63 T--IYTDSQYVINGITKWIKGWKKNGWKTADGKPVKNRDLWQE-------LDALLAGHK---VTWEWVKGHAGHPGNERA 130


                 ....*....
gi 358349751 290 DRLANEGAD 298
Cdd:cd09278  131 DRLANKAAD 139
RNase_H pfam00075
RNase H; RNase H digests the RNA strand of an RNA/DNA hybrid. Important enzyme in retroviral ...
 130-297 9.28e-29

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: 107.46  E-value: 9.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751  130 VYVDGASRGNGRKGtpisGYG-VFYGAGDSRNAAVPLCDiedaaatkpTNQRAELLAMKHALtdianeiyggyEDAERQS 208
Cdd:pfam00075   6 VYTDGSCLGNPGPG----GAGaVLYRGHENISAPLPGRT---------TNNRAELQAVIEAL-----------KALKSPS 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751  209 vRYQIYSDSRYAANCITEWCSKWIANGWKN-GQGNAVANKDIIETTYPILnyinqyySNHNwgrLEFFHVAGHSGDYGNE 287
Cdd:pfam00075  62 -KVNIYTDSQYVIGGITQWVHGWKKNGWPTtSEGKPVKNKDLWQLLKALC-------KKHQ---VYWQWVKGHAGNPGNE 130

                         170
                  ....*....|
gi 358349751  288 MADRLANEGA 297
Cdd:pfam00075 131 MADRLAKQGA 140
RnhA COG0328
Ribonuclease HI [Replication, recombination and repair];
130-297 1.85e-28

Ribonuclease HI [Replication, recombination and repair];


Pssm-ID: 440097 [Multi-domain]  Cd Length: 136  Bit Score: 106.47  E-value: 1.85e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751 130 VYVDGASRGNGRKGtpisGYGVFYGAGDSRnaaVPLCDIEDAAatkpTNQRAELLAMKHALTDIaneiyggyEDAERQSV 209
Cdd:COG0328    5 IYTDGACRGNPGPG----GWGAVIRYGGEE---KELSGGLGDT----TNNRAELTALIAALEAL--------KELGPCEV 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751 210 RyqIYSDSRYAANCITEWCSKWIANGWKngqgnAVANKDIIETtypilnyINQYYSNHNWgrlEFFHVAGHSGDYGNEMA 289
Cdd:COG0328   66 E--IYTDSQYVVNQITGWIHGWKKNGWK-----PVKNPDLWQR-------LDELLARHKV---TFEWVKGHAGHPGNERA 128


                 ....*...
gi 358349751 290 DRLANEGA 297
Cdd:COG0328  129 DALANKAL 136
Rnh1 COG3341
Ribonuclease HI-related protein, contains viroplasmin and RNaseH domains [General function ...
 1-297 1.10e-24

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


Pssm-ID: 442570 [Multi-domain]  Cd Length: 203  Bit Score: 98.39  E-value: 1.10e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751   1 MPFYAVARGVRPGIYKNWDSCKKNVLGYKGAVYKKFNSSQQAQEFiLANRSRRYQPRDDESSDSDIETPSvspmgpfvve 80
Cdd:COG3341    3 KKFYAVWKGRKPGIYTTWDECKAQVKGFPGAKYKSFKTKEEAEAA-LNGNYEDYKGKKKKLSEIELDSIA---------- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751  81 kqtvsppvvvelarhamsqlrfrlderylgipkafmrteakhpptqmkrVYVDGASRGNgrkgTPISGYGVFYGAGDSRN 160
Cdd:COG3341   72 -------------------------------------------------VYVDGSCSGN----PGVYEYGGVDTKTGKET 98

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751 161 AAVPLCDIEDAAAtkpTNQRAELLAMKHALtdianeiyggyEDAERQSVRYQIYSDSRYAAncitewcsKWIANGWKngq 240
Cdd:COG3341   99 FSELFHDGPFAEG---TNNAGEFLAAVHAL-----------AYLKKKGSKLPIYSDYRGAI--------SWVKGKWK--- 153

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 358349751 241 gnavANKDIIETTYPilnYINQYYSNHNWgRLEFFHVAGHSGDYGNEMADRLANEGA 297
Cdd:COG3341  154 ----TKLERTQAYKE---LFDLIEKKNTY-ENPFVKVKTHSGDKWNEIPDDLARKAL 202
rnhA PRK00203
ribonuclease H; Reviewed
 127-298 6.64e-22

ribonuclease H; Reviewed


Pssm-ID: 178927 [Multi-domain]  Cd Length: 150  Bit Score: 89.50  E-value: 6.64e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751 127 MKRV--YVDGASRGNGRKGtpisGYGVFYGAGDSRNAavpLCDIEdaAATkpTNQRAELLAMKHALtdianeiyggyeDA 204
Cdd:PRK00203   1 MKQVeiYTDGACLGNPGPG----GWGAILRYKGHEKE---LSGGE--ALT--TNNRMELMAAIEAL------------EA 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751 205 ERQSVRYQIYSDSRYAANCITEWCSKWIANGWKNGQGNAVANKDIiettypilnyinqyysnhnWGRL---------EFF 275
Cdd:PRK00203  58 LKEPCEVTLYTDSQYVRQGITEWIHGWKKNGWKTADKKPVKNVDL-------------------WQRLdaalkrhqiKWH 118

                        170       180
                 ....*....|....*....|...
gi 358349751 276 HVAGHSGDYGNEMADRLANEGAD 298
Cdd:PRK00203 119 WVKGHAGHPENERCDELARAGAE 141
Cauli_VI pfam01693
Caulimovirus viroplasmin; This family consists of various caulimovirus viroplasmin proteins. ...
 2-45 3.37e-18

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: 76.29  E-value: 3.37e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 358349751    2 PFYAVARGVRPGIYKNWDSCKKNVLGYKGAVYKKFNSSQQAQEF 45
Cdd:pfam01693   1 KYYAVAKGRKPGIYTTWDECKAQVKGFPGAKYKSFKTREEAEAF 44
RNase_H_like cd06222
Ribonuclease H-like superfamily, including RNase H, HI, HII, HIII, and RNase-like domain IV of ...
 130-294 3.18e-12

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: 62.33  E-value: 3.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751 130 VYVDGASRGNGRKGtpisGYGVFYGagDSRNAAVplcdiedAAATK----PTNQRAELLAMKHALtdianeiyggyEDAE 205
Cdd:cd06222    1 INVDGSCRGNPGPA----GIGGVLR--DHEGGWL-------GGFALkigaPTALEAELLALLLAL-----------ELAL 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751 206 RQSVRY-QIYSDSRYAANCITEWCSKWIANGwkngqgnavankdiiettypILNYINQYYSNHNWgRLEFFHVAGHsgdy 284
Cdd:cd06222   57 DLGYLKvIIESDSKYVVDLINSGSFKWSPNI--------------------LLIEDILLLLSRFW-SVKISHVPRE---- 111

                        170
                 ....*....|
gi 358349751 285 GNEMADRLAN 294
Cdd:cd06222  112 GNQVADALAK 121
PRK08719 PRK08719
ribonuclease H; Reviewed
 130-299 1.33e-11

ribonuclease H; Reviewed


Pssm-ID: 236334 [Multi-domain]  Cd Length: 147  Bit Score: 61.42  E-value: 1.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751 130 VYVDGASrGNGRKGTPISGYG-VFYgagDSRNAAVPLCDIEDAAATkpTNQRAELLAMKHALTdianeiYGGYEDAerqs 208
Cdd:PRK08719   7 IYIDGAA-PNNQHGCVRGGIGlVVY---DEAGEIVDEQSITVNRYT--DNAELELLALIEALE------YARDGDV---- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751 209 vryqIYSDSRYAANCITEWCSKWIANGWKNGQGNAVANKDIIETtypilnyINQYYSNHnwgRLEFFHVAGHSGDYGNEM 288
Cdd:PRK08719  71 ----IYSDSDYCVRGFNEWLDTWKQKGWRKSDKKPVANRDLWQQ-------VDELRARK---YVEVEKVTAHSGIEGNEA 136

                        170
                 ....*....|.
gi 358349751 289 ADRLANEGADL 299
Cdd:PRK08719 137 ADMLAQAAAEL 147
PRK06548 PRK06548
ribonuclease H; Provisional
 177-298 2.45e-08

ribonuclease H; Provisional


Pssm-ID: 75628 [Multi-domain]  Cd Length: 161  Bit Score: 52.51  E-value: 2.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751 177 TNQRAELLAMKHALTdianeiyggyedAERQSVR-YQIYSDSRYAANCITEWCSKWIANGWKNGQGNAVANKDIIETtyp 255
Cdd:PRK06548  41 TNNIAELTAVRELLI------------ATRHTDRpILILSDSKYVINSLTKWVYSWKMRKWRKADGKPVLNQEIIQE--- 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 358349751 256 ilnyINQYYSNHNwgrLEFFHVAGHSGDYGNEMADRLANEGAD 298
Cdd:PRK06548 106 ----IDSLMENRN---IRMSWVNAHTGHPLNEAADSLARQAAN 141
RNase_HI_bacteria_like cd09277
Bacterial RNase HI containing a hybrid binding domain (HBD) at the N-terminus; Ribonuclease H ...
 229-293 8.41e-08

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: 50.18  E-value: 8.41e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 358349751 229 SKWiANG-WKngqgnavANKDIIETTYpilNYINQYYSNHNwgrLEFFHVAGHSGDYGNEMADRLA 293
Cdd:cd09277   78 EKW-ATGeWK-------ANKELTKEYK---EFMQKYKKKIK---IEFVKVKAHSGDKYNELADKLA 129
Rnase_HI_RT_non_LTR cd09276
non-LTR RNase HI domain of reverse transcriptases; Ribonuclease H (RNase H) is classified into ...
 181-297 4.74e-05

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: 42.20  E-value: 4.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751 181 AELLAMKHALTDIAneiyggyEDAERQSvRYQIYSDSRYAANCItewcskwiANGWKNGQGNAVANKdiiettypILNYI 260
Cdd:cd09276   41 AELEAILEALELAL-------ATARRAR-KVTIFTDSQSALQAL--------RNPRRSSGQVILIRI--------LRLLR 96

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 358349751 261 NQYYSNHnwgRLEFFHVAGHSGDYGNEMADRLANEGA 297
Cdd:cd09276   97 LLKAKGV---KVRLRWVPGHVGIEGNEAADRLAKEAA 130
RNase_HI_RT_Bel cd09273
Bel/Pao family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) enzymes ...
 130-293 2.61e-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: 40.40  E-value: 2.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751 130 VYVDGASRGNGRkgtpisgygvfygagdsrnAAVPLCDIEDAAATKPTN--QRAELLAMKHALtdianeiyggyEDAERQ 207
Cdd:cd09273    2 VFTDGSSFKAGY-------------------AIVSGTEIVEAQPLPPGTsaQRAELIALIQAL-----------ELAKGK 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751 208 SVryQIYSDSRYAANCITEWCSKWIANGWKNGQGNAVANKDIIETTypilnyinqyysnhnWGRLEFF--HVAGHSG--- 282
Cdd:cd09273   52 PV--NIYTDSAYAVHALHLLETIGIERGFLKSIKNLSLFLQLLEAV---------------QRPKPVAiiHIRAHSKlpg 114

                        170
                 ....*....|...
gi 358349751 283 --DYGNEMADRLA 293
Cdd:cd09273  115 plAEGNAQADAAA 127
RNase_HI_like cd09279
RNAse HI family that includes archaeal, some bacterial as well as plant RNase HI; Ribonuclease ...
 129-298 1.23e-03

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: 38.22  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751 129 RVYVDGASRGNGRkgtpISGYGV--FYGAGDSRNAAVPLCDIEdaaatkpTNQRAELLAMKHALTDIaneiyggyedAER 206
Cdd:cd09279    2 TLYFDGASRGNPG----PAGAGVviYSPGGEVLELSERLGFPA-------TNNEAEYEALIAGLELA----------LEL 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358349751 207 QSVRYQIYSDSRYAANCIT-EWcskwiangwkngqgnAVANKDIIettyPILNYINQYYSNHnwGRLEFFHVAGHSgdyg 285
Cdd:cd09279   61 GAEKLEIYGDSQLVVNQLNgEY---------------KVKNERLK----PLLEKVLELLAKF--ELVELKWIPREQ---- 115

                        170
                 ....*....|...
gi 358349751 286 NEMADRLANEGAD 298
Cdd:cd09279  116 NKEADALANQALD 128
 
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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