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Conserved domains on  [gi|315364768|pdb|3PUF|F]
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Chain F, Ribonuclease H2 subunit C

Protein Classification

ribonuclease H2 subunit C( domain architecture ID 10554357)

ribonuclease H2 subunit C is a non-catalytic subunit of RNase H2, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RNase_H2_suC pfam08615
Ribonuclease H2 non-catalytic subunit (Ylr154p-like); This entry represents the non-catalytic ...
 31-160 1.07e-49

Ribonuclease H2 non-catalytic subunit (Ylr154p-like); This entry represents the non-catalytic subunit of RNase H2, which in S. cerevisiae is Ylr154p/Rnh203p. Whereas bacterial and archaeal RNases H2 are active as single polypeptides, the Saccharomyces cerevisiae homolog, Rnh2Ap, when expressed in Escherichia coli, fails to produce an active RNase H2. For RNase H2 activity three proteins are required [Rnh2Ap (Rnh201p), Ydr279p (Rnh202p) and Ylr154p (Rnh203p)]. Deletion of any one of the proteins or mutations in the catalytic site in Rnh2A leads to loss of RNase H2 activity. RNase H2 ia an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. It participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication.


:

Pssm-ID: 400782  Cd Length: 133  Bit Score: 156.37  E-value: 1.07e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PUF_F         31 TLHLLPCEVAVDGPAPVGRFFTPAIR----QGPEGLEVSFRGRCLRGEEVAVPPGLVGYVMVTEEKKVSMGKPDplRDSG 106
Cdd:pfam08615   1 TVHLLPCHIKHNGPANTDRFFTPYINtvrdDGKEVLRAYFRGRKLIGREVNLPPGYRGFVASTTNKISHTGKGD--AAED 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
3PUF_F        107 TDDQEEEPLERDFDRFIGATANFSRFTLWGLETIP-GPDAKVRGALTWPSLAAAI 160
Cdd:pfam08615  79 EDEEEPEPEEVDVDVKIEPTASFDSFTVWGHDGLPdGSDSFVRGVEEWLGLAEAI 133
 
Name Accession Description Interval E-value
RNase_H2_suC pfam08615
Ribonuclease H2 non-catalytic subunit (Ylr154p-like); This entry represents the non-catalytic ...
 31-160 1.07e-49

Ribonuclease H2 non-catalytic subunit (Ylr154p-like); This entry represents the non-catalytic subunit of RNase H2, which in S. cerevisiae is Ylr154p/Rnh203p. Whereas bacterial and archaeal RNases H2 are active as single polypeptides, the Saccharomyces cerevisiae homolog, Rnh2Ap, when expressed in Escherichia coli, fails to produce an active RNase H2. For RNase H2 activity three proteins are required [Rnh2Ap (Rnh201p), Ydr279p (Rnh202p) and Ylr154p (Rnh203p)]. Deletion of any one of the proteins or mutations in the catalytic site in Rnh2A leads to loss of RNase H2 activity. RNase H2 ia an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. It participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication.


Pssm-ID: 400782  Cd Length: 133  Bit Score: 156.37  E-value: 1.07e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PUF_F         31 TLHLLPCEVAVDGPAPVGRFFTPAIR----QGPEGLEVSFRGRCLRGEEVAVPPGLVGYVMVTEEKKVSMGKPDplRDSG 106
Cdd:pfam08615   1 TVHLLPCHIKHNGPANTDRFFTPYINtvrdDGKEVLRAYFRGRKLIGREVNLPPGYRGFVASTTNKISHTGKGD--AAED 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
3PUF_F        107 TDDQEEEPLERDFDRFIGATANFSRFTLWGLETIP-GPDAKVRGALTWPSLAAAI 160
Cdd:pfam08615  79 EDEEEPEPEEVDVDVKIEPTASFDSFTVWGHDGLPdGSDSFVRGVEEWLGLAEAI 133
RNase_H2-C cd09271
Ribonuclease H2-C is a subunit of the eukaryotic RNase H complex which cleaves RNA-DNA hybrids; ...
 33-138 1.44e-25

Ribonuclease H2-C is a subunit of the eukaryotic RNase H complex which cleaves RNA-DNA hybrids; Ribonuclease H2C is one of the three protein of eukaryotic RNase H2 complex that is required for nucleic acid binding and hydrolysis. RNase H is classified into two families, type I (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type II (prokaryotic RNase HII and HIII, and eukaryotic RNase H2/HII). RNase H endonucleolytically hydrolyzes an RNA strand when it is annealed to a complementary DNA strand in the presence of divalent cations, in DNA replication and repair. The enzyme can be found in bacteria, archaea, and eukaryotes. Most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite a lack of evidence for homology from sequence comparisons, type I and type II RNase H share a common fold and similar steric configurations of the four acidic active-site residues, suggesting identical or very similar catalytic mechanisms. Eukaryotic RNase HII is active during replication and is believed to play a role in removal of Okazaki fragment primers and single ribonucleotides in DNA-DNA duplexes. Eukaryotic RNase HII is functional when it forms a complex with RNase H2B and RNase H2C proteins. It is speculated that the two accessory subunits are required for correct folding of the catalytic subunit of RNase HII. Mutations in the three subunits of human RNase HII cause neurological disorder.


Pssm-ID: 187752  Cd Length: 93  Bit Score: 93.59  E-value: 1.44e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PUF_F       33 HLLPCEVAVDGPAPVGRFFTPAIRQ--GPEGLEVSFRGRCLRGEEVAVPPGLVGYVMVTEEKKVSmgkpdplrdsgtddq 110
Cdd:cd09271   1 HLLPCKIQYDGPANVSEYFKPKTDGdnEEGTLVAYFRGRKLVGKTVSLPEGYSGYVLSKTEKPDS--------------- 65

                        90       100
                ....*....|....*....|....*...
3PUF_F      111 EEEPLERDFDRFIGATANFSRFTLWGLE 138
Cdd:cd09271  66 EEKLEEEEEVRNLEITATFDEVTVWNHD 93
 
Name Accession Description Interval E-value
RNase_H2_suC pfam08615
Ribonuclease H2 non-catalytic subunit (Ylr154p-like); This entry represents the non-catalytic ...
 31-160 1.07e-49

Ribonuclease H2 non-catalytic subunit (Ylr154p-like); This entry represents the non-catalytic subunit of RNase H2, which in S. cerevisiae is Ylr154p/Rnh203p. Whereas bacterial and archaeal RNases H2 are active as single polypeptides, the Saccharomyces cerevisiae homolog, Rnh2Ap, when expressed in Escherichia coli, fails to produce an active RNase H2. For RNase H2 activity three proteins are required [Rnh2Ap (Rnh201p), Ydr279p (Rnh202p) and Ylr154p (Rnh203p)]. Deletion of any one of the proteins or mutations in the catalytic site in Rnh2A leads to loss of RNase H2 activity. RNase H2 ia an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. It participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication.


Pssm-ID: 400782  Cd Length: 133  Bit Score: 156.37  E-value: 1.07e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PUF_F         31 TLHLLPCEVAVDGPAPVGRFFTPAIR----QGPEGLEVSFRGRCLRGEEVAVPPGLVGYVMVTEEKKVSMGKPDplRDSG 106
Cdd:pfam08615   1 TVHLLPCHIKHNGPANTDRFFTPYINtvrdDGKEVLRAYFRGRKLIGREVNLPPGYRGFVASTTNKISHTGKGD--AAED 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
3PUF_F        107 TDDQEEEPLERDFDRFIGATANFSRFTLWGLETIP-GPDAKVRGALTWPSLAAAI 160
Cdd:pfam08615  79 EDEEEPEPEEVDVDVKIEPTASFDSFTVWGHDGLPdGSDSFVRGVEEWLGLAEAI 133
RNase_H2-C cd09271
Ribonuclease H2-C is a subunit of the eukaryotic RNase H complex which cleaves RNA-DNA hybrids; ...
 33-138 1.44e-25

Ribonuclease H2-C is a subunit of the eukaryotic RNase H complex which cleaves RNA-DNA hybrids; Ribonuclease H2C is one of the three protein of eukaryotic RNase H2 complex that is required for nucleic acid binding and hydrolysis. RNase H is classified into two families, type I (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type II (prokaryotic RNase HII and HIII, and eukaryotic RNase H2/HII). RNase H endonucleolytically hydrolyzes an RNA strand when it is annealed to a complementary DNA strand in the presence of divalent cations, in DNA replication and repair. The enzyme can be found in bacteria, archaea, and eukaryotes. Most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite a lack of evidence for homology from sequence comparisons, type I and type II RNase H share a common fold and similar steric configurations of the four acidic active-site residues, suggesting identical or very similar catalytic mechanisms. Eukaryotic RNase HII is active during replication and is believed to play a role in removal of Okazaki fragment primers and single ribonucleotides in DNA-DNA duplexes. Eukaryotic RNase HII is functional when it forms a complex with RNase H2B and RNase H2C proteins. It is speculated that the two accessory subunits are required for correct folding of the catalytic subunit of RNase HII. Mutations in the three subunits of human RNase HII cause neurological disorder.


Pssm-ID: 187752  Cd Length: 93  Bit Score: 93.59  E-value: 1.44e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PUF_F       33 HLLPCEVAVDGPAPVGRFFTPAIRQ--GPEGLEVSFRGRCLRGEEVAVPPGLVGYVMVTEEKKVSmgkpdplrdsgtddq 110
Cdd:cd09271   1 HLLPCKIQYDGPANVSEYFKPKTDGdnEEGTLVAYFRGRKLVGKTVSLPEGYSGYVLSKTEKPDS--------------- 65

                        90       100
                ....*....|....*....|....*...
3PUF_F      111 EEEPLERDFDRFIGATANFSRFTLWGLE 138
Cdd:cd09271  66 EEKLEEEEEVRNLEITATFDEVTVWNHD 93
 
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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