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Conserved domains on  [gi|1907150191|ref|XP_036018941|]
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interferon-stimulated 20 kDa exonuclease-like 2 isoform X1 [Mus musculus]

Protein Classification

3'-5' exonuclease family protein; 3'-5' exonuclease( domain architecture ID 10150278)

3'-5' exonuclease family protein may cleave nucleotides one at a time from the end (exo) of a polynucleotide chain| 3'-5' exonuclease has a fundamental role in reducing polymerase errors and is involved in proofreading activity

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ISG20 cd06149
DEDDh 3'-5' exonuclease domain of Interferon Stimulated Gene product of 20 kDa, and similar ...
 195-351 6.80e-106

DEDDh 3'-5' exonuclease domain of Interferon Stimulated Gene product of 20 kDa, and similar proteins; Interferon (IFN) Stimulated Gene product of 20 kDa (ISG20) is an IFN-induced antiviral exonuclease with a strong preference for single-stranded RNA and minor activity towards single-stranded DNA. It was also independently identified by its response to estrogen and was called HEM45 (human estrogen regulated transcript). ISG20 is a DEDDh-type DnaQ-like 3'-5' exonuclease containing three conserved sequence motifs termed ExoI, ExoII and ExoIII with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. ISG20 may be a major effector of innate immunity against pathogens including viruses, bacteria, and parasites. It is located in promyelocytic leukemia (PML) nuclear bodies, sites for oncogenic DNA viral transcription and replication. It may carry out its function by degrading viral RNAs as part of the IFN-regulated antiviral response.


:

Pssm-ID: 99852  Cd Length: 157  Bit Score: 307.83  E-value: 6.80e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150191 195 VAIDCEMVGTGPKGRVSSLARCSIVNYNGDVLYDEYVLPPCYIVNYRTRWSGIRKCHMVNATPFKTARSQILKILSGKVV 274
Cdd:cd06149     1 VAIDCEMVGTGPGGRESELARCSIVNYHGDVLYDKYIRPEGPVTDYRTRWSGIRRQHLVNATPFAVAQKEILKILKGKVV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907150191 275 IGHAIHNDYKALQYFHPKSLTRDTSRIPLLNRKADCPENVTLSLKHLTKKLLSRDIQVGNTGHSSVEDAQATMELYK 351
Cdd:cd06149    81 VGHAIHNDFKALKYFHPKHMTRDTSTIPLLNRKAGFPENCRVSLKVLAKRLLHRDIQVGRQGHSSVEDARATMELYK 157
 
Name Accession Description Interval E-value
ISG20 cd06149
DEDDh 3'-5' exonuclease domain of Interferon Stimulated Gene product of 20 kDa, and similar ...
 195-351 6.80e-106

DEDDh 3'-5' exonuclease domain of Interferon Stimulated Gene product of 20 kDa, and similar proteins; Interferon (IFN) Stimulated Gene product of 20 kDa (ISG20) is an IFN-induced antiviral exonuclease with a strong preference for single-stranded RNA and minor activity towards single-stranded DNA. It was also independently identified by its response to estrogen and was called HEM45 (human estrogen regulated transcript). ISG20 is a DEDDh-type DnaQ-like 3'-5' exonuclease containing three conserved sequence motifs termed ExoI, ExoII and ExoIII with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. ISG20 may be a major effector of innate immunity against pathogens including viruses, bacteria, and parasites. It is located in promyelocytic leukemia (PML) nuclear bodies, sites for oncogenic DNA viral transcription and replication. It may carry out its function by degrading viral RNAs as part of the IFN-regulated antiviral response.


Pssm-ID: 99852  Cd Length: 157  Bit Score: 307.83  E-value: 6.80e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150191 195 VAIDCEMVGTGPKGRVSSLARCSIVNYNGDVLYDEYVLPPCYIVNYRTRWSGIRKCHMVNATPFKTARSQILKILSGKVV 274
Cdd:cd06149     1 VAIDCEMVGTGPGGRESELARCSIVNYHGDVLYDKYIRPEGPVTDYRTRWSGIRRQHLVNATPFAVAQKEILKILKGKVV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907150191 275 IGHAIHNDYKALQYFHPKSLTRDTSRIPLLNRKADCPENVTLSLKHLTKKLLSRDIQVGNTGHSSVEDAQATMELYK 351
Cdd:cd06149    81 VGHAIHNDFKALKYFHPKHMTRDTSTIPLLNRKAGFPENCRVSLKVLAKRLLHRDIQVGRQGHSSVEDARATMELYK 157
EXOIII smart00479
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ...
 193-358 1.19e-35

exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other exonucleases;


Pssm-ID: 214685 [Multi-domain]  Cd Length: 169  Bit Score: 127.80  E-value: 1.19e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150191  193 KMVAIDCEMVGTGPKGrvSSLARCSIVNYNGD---VLYDEYVLPPCYIVNYRTRWSGIRKCHMVNATPFKTARSQILKIL 269
Cdd:smart00479   1 TLVVIDCETTGLDPGK--DEIIEIAAVDVDGGeiiEVFDTYVKPDRPITDYATEIHGITPEMLDDAPTFEEVLEELLEFL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150191  270 SGKV-VIGHAIHNDYKALQYFHPKSLTRDTSRIPLLN----RKADCPENVTLSLKHLTKKLLSRDIQvgnTGHSSVEDAQ 344
Cdd:smart00479  79 RGRIlVAGNSAHFDLRFLKLEHPRLGIKQPPKLPVIDtlklARATNPGLPKYSLKKLAKRLLLEVIQ---RAHRALDDAR 155

                          170
                   ....*....|....
gi 1907150191  345 ATMELYKLVEVEWE 358
Cdd:smart00479 156 ATAKLFKKLLERLE 169
RNase_T pfam00929
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T ...
 195-350 9.45e-11

Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T and the epsilon subunit of DNA polymerase III.;


Pssm-ID: 395743 [Multi-domain]  Cd Length: 164  Bit Score: 59.67  E-value: 9.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150191 195 VAIDCEMVGTGPKG-RVSSLARCSIVNYNGDVL--YDEYVLP--PCYIVNYRTRWSGIRKCHMVNATPFKTARSQILKIL 269
Cdd:pfam00929   1 VVIDLETTGLDPEKdEIIEIAAVVIDGGENEIGetFHTYVKPtrLPKLTDECTKFTGITQAMLDNKPSFEEVLEEFLEFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150191 270 -SGKVVIGH--------AIHNDYKALQYFHPKSL----TRDTSRIPLLNRKAdcpenvtLSLKHLTKKLlsrDIQVGNTG 336
Cdd:pfam00929  81 rKGNLLVAHnasfdvgfLRYDDKRFLKKPMPKLNpvidTLILDKATYKELPG-------RSLDALAEKL---GLEHIGRA 150

                         170
                  ....*....|....
gi 1907150191 337 HSSVEDAQATMELY 350
Cdd:pfam00929 151 HRALDDARATAKLF 164
DnaQ COG0847
DNA polymerase III, epsilon subunit or related 3'-5' exonuclease [Replication, recombination ...
 193-350 8.75e-10

DNA polymerase III, epsilon subunit or related 3'-5' exonuclease [Replication, recombination and repair];


Pssm-ID: 440608 [Multi-domain]  Cd Length: 163  Bit Score: 57.11  E-value: 8.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150191 193 KMVAIDCEMVGTGP-KGRVSSLArcsIVNYNGDVL---YDEYVLPPCYIVNYRTRWSGIRKCHMVNATPFKTARSQILKI 268
Cdd:COG0847     1 RFVVLDTETTGLDPaKDRIIEIG---AVKVDDGRIvetFHTLVNPERPIPPEATAIHGITDEDVADAPPFAEVLPELLEF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150191 269 LSGKVVIGHAIHNDYKALQ-----YFHPKSLTR--DTSRiplLNRKAdCPENVTLSLKHLTKKLlsrDIQVGNTgHSSVE 341
Cdd:COG0847    78 LGGAVLVAHNAAFDLGFLNaelrrAGLPLPPFPvlDTLR---LARRL-LPGLPSYSLDALCERL---GIPFDER-HRALA 149


                  ....*....
gi 1907150191 342 DAQATMELY 350
Cdd:COG0847   150 DAEATAELF 158
 
Name Accession Description Interval E-value
ISG20 cd06149
DEDDh 3'-5' exonuclease domain of Interferon Stimulated Gene product of 20 kDa, and similar ...
 195-351 6.80e-106

DEDDh 3'-5' exonuclease domain of Interferon Stimulated Gene product of 20 kDa, and similar proteins; Interferon (IFN) Stimulated Gene product of 20 kDa (ISG20) is an IFN-induced antiviral exonuclease with a strong preference for single-stranded RNA and minor activity towards single-stranded DNA. It was also independently identified by its response to estrogen and was called HEM45 (human estrogen regulated transcript). ISG20 is a DEDDh-type DnaQ-like 3'-5' exonuclease containing three conserved sequence motifs termed ExoI, ExoII and ExoIII with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. ISG20 may be a major effector of innate immunity against pathogens including viruses, bacteria, and parasites. It is located in promyelocytic leukemia (PML) nuclear bodies, sites for oncogenic DNA viral transcription and replication. It may carry out its function by degrading viral RNAs as part of the IFN-regulated antiviral response.


Pssm-ID: 99852  Cd Length: 157  Bit Score: 307.83  E-value: 6.80e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150191 195 VAIDCEMVGTGPKGRVSSLARCSIVNYNGDVLYDEYVLPPCYIVNYRTRWSGIRKCHMVNATPFKTARSQILKILSGKVV 274
Cdd:cd06149     1 VAIDCEMVGTGPGGRESELARCSIVNYHGDVLYDKYIRPEGPVTDYRTRWSGIRRQHLVNATPFAVAQKEILKILKGKVV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907150191 275 IGHAIHNDYKALQYFHPKSLTRDTSRIPLLNRKADCPENVTLSLKHLTKKLLSRDIQVGNTGHSSVEDAQATMELYK 351
Cdd:cd06149    81 VGHAIHNDFKALKYFHPKHMTRDTSTIPLLNRKAGFPENCRVSLKVLAKRLLHRDIQVGRQGHSSVEDARATMELYK 157
REX4_like cd06144
DEDDh 3'-5' exonuclease domain of RNA exonuclease 4, XPMC2, Interferon Stimulated Gene product ...
 195-351 9.84e-77

DEDDh 3'-5' exonuclease domain of RNA exonuclease 4, XPMC2, Interferon Stimulated Gene product of 20 kDa, and similar proteins; This subfamily is composed of RNA exonuclease 4 (REX4 or Rex4p), XPMC2, Interferon (IFN) Stimulated Gene product of 20 kDa (ISG20), and similar proteins. REX4 is involved in pre-rRNA processing. It controls the ratio between the two forms of 5.8S rRNA in yeast. XPMC2 is a Xenopus gene which was identified through its ability to correct a mitotic defect in fission yeast. The human homolog of XPMC2 (hPMC2) may be involved in angiotensin II-induced adrenal cell cycle progression and cell proliferation. ISG20 is an IFN-induced antiviral exonuclease with a strong preference for single-stranded RNA and minor activity towards single-stranded DNA. These proteins are DEDDh-type DnaQ-like 3'-5' exonucleases containing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. REX proteins function in the processing and maturation of many RNA species, similar to the function of Escherchia coli RNase T.


Pssm-ID: 99847  Cd Length: 152  Bit Score: 233.18  E-value: 9.84e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150191 195 VAIDCEMVGTGPKGRVSSLARCSIVNYNGDVLYDEYVLPPCYIVNYRTRWSGIRKCHMVNATPFKTARSQILKILSGKVV 274
Cdd:cd06144     1 VALDCEMVGVGPDGSESALARVSIVNEDGNVVYDTYVKPQEPVTDYRTAVSGIRPEHLKDAPDFEEVQKKVAELLKGRIL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907150191 275 IGHAIHNDYKALQYFHPKSLTRDTSRIPLLNRKADCpenVTLSLKHLTKKLLSRDIQVGntGHSSVEDAQATMELYK 351
Cdd:cd06144    81 VGHALKNDLKVLKLDHPKKLIRDTSKYKPLRKTAKG---KSPSLKKLAKQLLGLDIQEG--EHSSVEDARAAMRLYR 152
REX1_like cd06145
DEDDh 3'-5' exonuclease domain of RNA exonuclease 1, -3 and similar eukaryotic proteins; This ...
 195-351 1.72e-47

DEDDh 3'-5' exonuclease domain of RNA exonuclease 1, -3 and similar eukaryotic proteins; This subfamily is composed of RNA exonuclease 1 (REX1 or Rex1p), REX3 (or Rex3p), and similar eukaryotic proteins. In yeast, REX1 and REX3 are required for 5S rRNA and MRP (mitochondrial RNA processing) RNA maturation, respectively. They are DEDDh-type DnaQ-like 3'-5' exonucleases containing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. REX1 is the major exonuclease responsible for pre-tRNA trail trimming and may also be involved in nuclear CCA turnover. REX proteins function in the processing and maturation of many RNA species, similar to the function of Escherichia coli RNase T.


Pssm-ID: 99848  Cd Length: 150  Bit Score: 158.03  E-value: 1.72e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150191 195 VAIDCEMVGTGpKGRVssLARCSIVNYNGDVLYDEYVLPPCYIVNYRTRWSGIRKCHMVNATP-FKTARSQILKILS-GK 272
Cdd:cd06145     1 FALDCEMCYTT-DGLE--LTRVTVVDENGKVVLDELVKPDGEIVDYNTRFSGITEEMLENVTTtLEDVQKKLLSLISpDT 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907150191 273 VVIGHAIHNDYKALQYFHPKSLtrDTSRipLLNRKADCPEnvTLSLKHLTKKLLSRDIQVGNTGHSSVEDAQATMELYK 351
Cdd:cd06145    78 ILVGHSLENDLKALKLIHPRVI--DTAI--LFPHPRGPPY--KPSLKNLAKKYLGRDIQQGEGGHDSVEDARAALELVK 150
DEDDh_RNase cd06137
DEDDh 3'-5' exonuclease domain of the eukaryotic exoribonucleases PAN2, RNA exonuclease (REX) ...
 195-350 5.19e-39

DEDDh 3'-5' exonuclease domain of the eukaryotic exoribonucleases PAN2, RNA exonuclease (REX)-1,-3, and -4, ISG20, and similar proteins; This group is composed of eukaryotic exoribonucleases that include PAN2, RNA exonuclease 1 (REX1 or Rex1p), REX3 (Rex3p), REX4 (or Rex4p), ISG20, and similar proteins. They are DEDDh-type DnaQ-like 3'-5' exonucleases containing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. PAN2 is the catalytic subunit of poly(A) nuclease (PAN), a Pab1p-dependent 3'-5' exoribonuclease which plays an important role in the posttranscriptional maturation of pre-mRNAs. REX proteins are required for the processing and maturation of many RNA species, and ISG20 is an interferon-induced antiviral exonuclease with a strong preference for single-stranded RNA.


Pssm-ID: 99840  Cd Length: 161  Bit Score: 136.64  E-value: 5.19e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150191 195 VAIDCEMVGTGPKGrvSSLARCSIVNYN-GDVLYDEYVLPPCYIVNYRTRWSGIRKCHMVNA-----TPFKT--ARSQIL 266
Cdd:cd06137     1 VALDCEMVGLADGD--SEVVRISAVDVLtGEVLIDSLVRPSVRVTDWRTRFSGVTPADLEEAakagkTIFGWeaARAALW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150191 267 KILSGK-VVIGHAIHNDYKALQYFHPKSLtrDTSRIPLLNRKADCPENvTLSLKHLTKKLLSRDIQVGNTGHSSVEDAQA 345
Cdd:cd06137    79 KFIDPDtILVGHSLQNDLDALRMIHTRVV--DTAILTREAVKGPLAKR-QWSLRTLCRDFLGLKIQGGGEGHDSLEDALA 155


                  ....*
gi 1907150191 346 TMELY 350
Cdd:cd06137   156 AREVV 160
EXOIII smart00479
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ...
 193-358 1.19e-35

exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other exonucleases;


Pssm-ID: 214685 [Multi-domain]  Cd Length: 169  Bit Score: 127.80  E-value: 1.19e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150191  193 KMVAIDCEMVGTGPKGrvSSLARCSIVNYNGD---VLYDEYVLPPCYIVNYRTRWSGIRKCHMVNATPFKTARSQILKIL 269
Cdd:smart00479   1 TLVVIDCETTGLDPGK--DEIIEIAAVDVDGGeiiEVFDTYVKPDRPITDYATEIHGITPEMLDDAPTFEEVLEELLEFL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150191  270 SGKV-VIGHAIHNDYKALQYFHPKSLTRDTSRIPLLN----RKADCPENVTLSLKHLTKKLLSRDIQvgnTGHSSVEDAQ 344
Cdd:smart00479  79 RGRIlVAGNSAHFDLRFLKLEHPRLGIKQPPKLPVIDtlklARATNPGLPKYSLKKLAKRLLLEVIQ---RAHRALDDAR 155

                          170
                   ....*....|....
gi 1907150191  345 ATMELYKLVEVEWE 358
Cdd:smart00479 156 ATAKLFKKLLERLE 169
PAN2_exo cd06143
DEDDh 3'-5' exonuclease domain of the eukaryotic exoribonuclease PAN2; PAN2 is the catalytic ...
 195-351 8.19e-21

DEDDh 3'-5' exonuclease domain of the eukaryotic exoribonuclease PAN2; PAN2 is the catalytic subunit of poly(A) nuclease (PAN), a Pab1p-dependent 3'-5' exoribonuclease which plays an important role in the posttranscriptional maturation of pre-mRNAs. PAN catalyzes the deadenylation of poly(A) tails, which are initially synthesized to default lengths of 70 to 90, to mRNA-specific lengths of 55 to 71. Pab1p and PAN also play a role in the export and decay of mRNA. PAN2 contains a DEDDh-type DnaQ-like 3'-5' exonuclease domain with three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis.


Pssm-ID: 99846  Cd Length: 174  Bit Score: 88.44  E-value: 8.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150191 195 VAIDCEMVGTGP--------------KGRVSSLARCSIVNYNGD---VLY-DEYVLPPCYIVNYRTRWSGIRKCHMVNAT 256
Cdd:cd06143     1 VAIDAEFVKLKPeeteirsdgtkstiRPSQMSLARVSVVRGEGElegVPFiDDYISTTEPVVDYLTRFSGIKPGDLDPKT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150191 257 PFK--TARSQILKILS-----GKVVIGHAIHNDYKALQYFHPKSLTRDTSRIPLLnrkadcPENVTLSLKHLTKKLLSRD 329
Cdd:cd06143    81 SSKnlTTLKSAYLKLRllvdlGCIFVGHGLAKDFRVINIQVPKEQVIDTVELFHL------PGQRKLSLRFLAWYLLGEK 154

                         170       180
                  ....*....|....*....|..
gi 1907150191 330 IQVGNtgHSSVEDAQATMELYK 351
Cdd:cd06143   155 IQSET--HDSIEDARTALKLYR 174
DEDDh cd06127
DEDDh 3'-5' exonuclease domain family; DEDDh exonucleases, part of the DnaQ-like (or DEDD) ...
 195-351 6.56e-12

DEDDh 3'-5' exonuclease domain family; DEDDh exonucleases, part of the DnaQ-like (or DEDD) exonuclease superfamily, catalyze the excision of nucleoside monophosphates at the DNA or RNA termini in the 3'-5' direction. These proteins contain four invariant acidic residues in three conserved sequence motifs termed ExoI, ExoII and ExoIII. DEDDh exonucleases are classified as such because of the presence of specific Hx(4)D conserved pattern at the ExoIII motif. The four conserved acidic residues are clustered around the active site and serve as ligands for the two metal ions required for catalysis. Most DEDDh exonucleases are the proofreading subunits (epsilon) or domains of bacterial DNA polymerase III, the main replicating enzyme in bacteria, which functions as the chromosomal replicase. Other members include other DNA and RNA exonucleases such as RNase T, Oligoribonuclease, and RNA exonuclease (REX), among others.


Pssm-ID: 176648 [Multi-domain]  Cd Length: 159  Bit Score: 63.09  E-value: 6.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150191 195 VAIDCEMVGTGPKG-RVSSLArcsIVNYNGDVL----YDEYVLPPCYIVNYRTRWSGIRKCHMVNATPFKTARSQILKIL 269
Cdd:cd06127     1 VVFDTETTGLDPKKdRIIEIG---AVKVDGGIEiverFETLVNPGRPIPPEATAIHGITDEMLADAPPFEEVLPEFLEFL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150191 270 SGKVVIGHAIHNDYKALQYFhpkslTRDTSRIPLLNRKADcpenvTLSL---------KHLTKKLLSRDIQVGNTG-HSS 339
Cdd:cd06127    78 GGRVLVAHNASFDLRFLNRE-----LRRLGGPPLPNPWID-----TLRLarrllpglrSHRLGLLLAERYGIPLEGaHRA 147

                         170
                  ....*....|..
gi 1907150191 340 VEDAQATMELYK 351
Cdd:cd06127   148 LADALATAELLL 159
RNase_T pfam00929
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T ...
 195-350 9.45e-11

Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T and the epsilon subunit of DNA polymerase III.;


Pssm-ID: 395743 [Multi-domain]  Cd Length: 164  Bit Score: 59.67  E-value: 9.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150191 195 VAIDCEMVGTGPKG-RVSSLARCSIVNYNGDVL--YDEYVLP--PCYIVNYRTRWSGIRKCHMVNATPFKTARSQILKIL 269
Cdd:pfam00929   1 VVIDLETTGLDPEKdEIIEIAAVVIDGGENEIGetFHTYVKPtrLPKLTDECTKFTGITQAMLDNKPSFEEVLEEFLEFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150191 270 -SGKVVIGH--------AIHNDYKALQYFHPKSL----TRDTSRIPLLNRKAdcpenvtLSLKHLTKKLlsrDIQVGNTG 336
Cdd:pfam00929  81 rKGNLLVAHnasfdvgfLRYDDKRFLKKPMPKLNpvidTLILDKATYKELPG-------RSLDALAEKL---GLEHIGRA 150

                         170
                  ....*....|....
gi 1907150191 337 HSSVEDAQATMELY 350
Cdd:pfam00929 151 HRALDDARATAKLF 164
DnaQ COG0847
DNA polymerase III, epsilon subunit or related 3'-5' exonuclease [Replication, recombination ...
 193-350 8.75e-10

DNA polymerase III, epsilon subunit or related 3'-5' exonuclease [Replication, recombination and repair];


Pssm-ID: 440608 [Multi-domain]  Cd Length: 163  Bit Score: 57.11  E-value: 8.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150191 193 KMVAIDCEMVGTGP-KGRVSSLArcsIVNYNGDVL---YDEYVLPPCYIVNYRTRWSGIRKCHMVNATPFKTARSQILKI 268
Cdd:COG0847     1 RFVVLDTETTGLDPaKDRIIEIG---AVKVDDGRIvetFHTLVNPERPIPPEATAIHGITDEDVADAPPFAEVLPELLEF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150191 269 LSGKVVIGHAIHNDYKALQ-----YFHPKSLTR--DTSRiplLNRKAdCPENVTLSLKHLTKKLlsrDIQVGNTgHSSVE 341
Cdd:COG0847    78 LGGAVLVAHNAAFDLGFLNaelrrAGLPLPPFPvlDTLR---LARRL-LPGLPSYSLDALCERL---GIPFDER-HRALA 149


                  ....*....
gi 1907150191 342 DAQATMELY 350
Cdd:COG0847   150 DAEATAELF 158
 
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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