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Conserved domains on  [gi|13325281|gb|AAH04456|]
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ERI3 protein [Homo sapiens]

Protein Classification

3'-5' exonuclease( domain architecture ID 10150039)

3'-5' exonuclease catalyzes the excision of nucleoside monophosphates at the DNA or RNA termini in the 3'-5' direction; similar to human ERI1 exoribonuclease 3

CATH:  3.30.420.10
EC:  3.1.-.-
Gene Ontology:  GO:0008408|GO:0003676
PubMed:  11988770|11222749
SCOP:  4000547

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ERI-1_3'hExo_like cd06133
DEDDh 3'-5' exonuclease domain of Caenorhabditis elegans ERI-1, human 3' exonuclease, and ...
 1-114 7.28e-39

DEDDh 3'-5' exonuclease domain of Caenorhabditis elegans ERI-1, human 3' exonuclease, and similar proteins; This subfamily is composed of Caenorhabditis elegans ERI-1, human 3' exonuclease (3'hExo), Drosophila exonuclease snipper (snp), and similar proteins from eukaryotes and bacteria. These 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. ERI-1 has been implicated in the degradation of small interfering RNAs (RNAi). 3'hExo participates in the degradation of histone mRNAs. Snp is a non-essential exonuclease that efficiently degrades structured RNA and DNA substrates as long as there is a minimum of 2 nucleotides in the 3' overhang to initiate degradation. Snp is not a functional homolog of either ERI-1 or 3'hExo.


:

Pssm-ID: 99836 [Multi-domain]  Cd Length: 176  Bit Score: 128.49  E-value: 7.28e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325281   1 MVDGQPSLQQVLERVDEWMAKEGlldpnvKSIFVTCGDWDLKVMLPGQCQYLGLPVADYFKQWINLKKAYSFAMGCWPKN 80
Cdd:cd06133  68 DVDNAPSFPEVLKEFLEWLGKNG------KYAFVTWGDWDLKDLLQNQCKYKIINLPPFFRQWIDLKKEFAKFYGLKKRT 141

                        90       100       110
                ....*....|....*....|....*....|....
gi 13325281  81 GLLDMNKGLSLQHIGRPHSGIDDCKNIANIMKTL 114
Cdd:cd06133 142 GLSKALEYLGLEFEGRHHRGLDDARNIARILKRL 175
 
Name Accession Description Interval E-value
ERI-1_3'hExo_like cd06133
DEDDh 3'-5' exonuclease domain of Caenorhabditis elegans ERI-1, human 3' exonuclease, and ...
 1-114 7.28e-39

DEDDh 3'-5' exonuclease domain of Caenorhabditis elegans ERI-1, human 3' exonuclease, and similar proteins; This subfamily is composed of Caenorhabditis elegans ERI-1, human 3' exonuclease (3'hExo), Drosophila exonuclease snipper (snp), and similar proteins from eukaryotes and bacteria. These 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. ERI-1 has been implicated in the degradation of small interfering RNAs (RNAi). 3'hExo participates in the degradation of histone mRNAs. Snp is a non-essential exonuclease that efficiently degrades structured RNA and DNA substrates as long as there is a minimum of 2 nucleotides in the 3' overhang to initiate degradation. Snp is not a functional homolog of either ERI-1 or 3'hExo.


Pssm-ID: 99836 [Multi-domain]  Cd Length: 176  Bit Score: 128.49  E-value: 7.28e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325281   1 MVDGQPSLQQVLERVDEWMAKEGlldpnvKSIFVTCGDWDLKVMLPGQCQYLGLPVADYFKQWINLKKAYSFAMGCWPKN 80
Cdd:cd06133  68 DVDNAPSFPEVLKEFLEWLGKNG------KYAFVTWGDWDLKDLLQNQCKYKIINLPPFFRQWIDLKKEFAKFYGLKKRT 141

                        90       100       110
                ....*....|....*....|....*....|....
gi 13325281  81 GLLDMNKGLSLQHIGRPHSGIDDCKNIANIMKTL 114
Cdd:cd06133 142 GLSKALEYLGLEFEGRHHRGLDDARNIARILKRL 175
PTZ00315 PTZ00315
2'-phosphotransferase; Provisional
 1-124 3.99e-24

2'-phosphotransferase; Provisional


Pssm-ID: 240356 [Multi-domain]  Cd Length: 582  Bit Score: 96.12  E-value: 3.99e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325281    1 MVDGQPSLQQVLERVDEWMAKEGLLD--PNVKSIFVTCGDWDLKVMLPGQ---CQYLGLPVAdyFKQWINLKKAYS---F 72
Cdd:PTZ00315 123 MVSRADPFPVVYCEALQFLAEAGLGDapPLRSYCVVTCGDWDLKTMLPSQmrvSGQQGTPLS--FQRWCNLKKYMSqlgF 200

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13325281   73 AMGCW---------PKNGLLDMNKGLSLQHIGRPHSGIDDCKNIANIMKTLAYRGFIFKQT 124
Cdd:PTZ00315 201 GNGSGcgggatpplGPSDMPDMLQMLGLPLQGRHHSGIDDCRNIAAVLCELLRRGLVIDPT 261
RNase_T pfam00929
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T ...
 1-111 1.17e-22

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: 87.02  E-value: 1.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325281     1 MVDGQPSLQQVLERVDEWMAKEGLLDPNVKSIFVTCGDWDLKVMLPGQCQylglPVADYFKQWINLKKAYSFAMGcwpkN 80
Cdd:pfam00929  62 MLDNKPSFEEVLEEFLEFLRKGNLLVAHNASFDVGFLRYDDKRFLKKPMP----KLNPVIDTLILDKATYKELPG----R 133

                          90       100       110
                  ....*....|....*....|....*....|.
gi 13325281    81 GLLDMNKGLSLQHIGRPHSGIDDCKNIANIM 111
Cdd:pfam00929 134 SLDALAEKLGLEHIGRAHRALDDARATAKLF 164
EXOIII smart00479
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ...
 1-119 3.03e-17

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


Pssm-ID: 214685 [Multi-domain]  Cd Length: 169  Bit Score: 73.10  E-value: 3.03e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325281      1 MVDGQPSLQQVLERVDEWMAKEGLLDPNVKSIFVTCGDWDLKVMLPGQCQYLglPVADYFKqwinLKKAYSFAmgcWPKN 80
Cdd:smart00479  60 MLDDAPTFEEVLEELLEFLRGRILVAGNSAHFDLRFLKLEHPRLGIKQPPKL--PVIDTLK----LARATNPG---LPKY 130

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 13325281     81 GLLDMNKGLSLQHIGRPHSGIDDCKNIANIMKTLAYRGF 119
Cdd:smart00479 131 SLKKLAKRLLLEVIQRAHRALDDARATAKLFKKLLERLE 169
KapD COG5018
3'-5' exonuclease KapD, inhibitor of KinA-controlled sporulation [Signal transduction ...
 1-114 7.63e-17

3'-5' exonuclease KapD, inhibitor of KinA-controlled sporulation [Signal transduction mechanisms];


Pssm-ID: 444042 [Multi-domain]  Cd Length: 181  Bit Score: 72.20  E-value: 7.63e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325281   1 MVDGQPSLQQVLERVDEWMAKEglldpnvKSIFVTCGDWDLKVMLPgQCQYLGLPVaDYFKQWINLKKAYSFAMGCwpkN 80
Cdd:COG5018  70 DVDSAPSFAEAIEDFKKWIGSE-------DYILCSWGDYDRKQLER-NCRFHGVPY-PFGDRHINLKKLFALYFGL---K 137

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 13325281  81 GLLDMNKGLSLQHI---GRPHSGIDDCKNIANIMKTL 114
Cdd:COG5018 138 KRIGLKKALELLGLefeGTHHRALDDARNTAKLFKKI 174
 
Name Accession Description Interval E-value
ERI-1_3'hExo_like cd06133
DEDDh 3'-5' exonuclease domain of Caenorhabditis elegans ERI-1, human 3' exonuclease, and ...
 1-114 7.28e-39

DEDDh 3'-5' exonuclease domain of Caenorhabditis elegans ERI-1, human 3' exonuclease, and similar proteins; This subfamily is composed of Caenorhabditis elegans ERI-1, human 3' exonuclease (3'hExo), Drosophila exonuclease snipper (snp), and similar proteins from eukaryotes and bacteria. These 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. ERI-1 has been implicated in the degradation of small interfering RNAs (RNAi). 3'hExo participates in the degradation of histone mRNAs. Snp is a non-essential exonuclease that efficiently degrades structured RNA and DNA substrates as long as there is a minimum of 2 nucleotides in the 3' overhang to initiate degradation. Snp is not a functional homolog of either ERI-1 or 3'hExo.


Pssm-ID: 99836 [Multi-domain]  Cd Length: 176  Bit Score: 128.49  E-value: 7.28e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325281   1 MVDGQPSLQQVLERVDEWMAKEGlldpnvKSIFVTCGDWDLKVMLPGQCQYLGLPVADYFKQWINLKKAYSFAMGCWPKN 80
Cdd:cd06133  68 DVDNAPSFPEVLKEFLEWLGKNG------KYAFVTWGDWDLKDLLQNQCKYKIINLPPFFRQWIDLKKEFAKFYGLKKRT 141

                        90       100       110
                ....*....|....*....|....*....|....
gi 13325281  81 GLLDMNKGLSLQHIGRPHSGIDDCKNIANIMKTL 114
Cdd:cd06133 142 GLSKALEYLGLEFEGRHHRGLDDARNIARILKRL 175
PTZ00315 PTZ00315
2'-phosphotransferase; Provisional
 1-124 3.99e-24

2'-phosphotransferase; Provisional


Pssm-ID: 240356 [Multi-domain]  Cd Length: 582  Bit Score: 96.12  E-value: 3.99e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325281    1 MVDGQPSLQQVLERVDEWMAKEGLLD--PNVKSIFVTCGDWDLKVMLPGQ---CQYLGLPVAdyFKQWINLKKAYS---F 72
Cdd:PTZ00315 123 MVSRADPFPVVYCEALQFLAEAGLGDapPLRSYCVVTCGDWDLKTMLPSQmrvSGQQGTPLS--FQRWCNLKKYMSqlgF 200

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13325281   73 AMGCW---------PKNGLLDMNKGLSLQHIGRPHSGIDDCKNIANIMKTLAYRGFIFKQT 124
Cdd:PTZ00315 201 GNGSGcgggatpplGPSDMPDMLQMLGLPLQGRHHSGIDDCRNIAAVLCELLRRGLVIDPT 261
RNase_T pfam00929
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T ...
 1-111 1.17e-22

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: 87.02  E-value: 1.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325281     1 MVDGQPSLQQVLERVDEWMAKEGLLDPNVKSIFVTCGDWDLKVMLPGQCQylglPVADYFKQWINLKKAYSFAMGcwpkN 80
Cdd:pfam00929  62 MLDNKPSFEEVLEEFLEFLRKGNLLVAHNASFDVGFLRYDDKRFLKKPMP----KLNPVIDTLILDKATYKELPG----R 133

                          90       100       110
                  ....*....|....*....|....*....|.
gi 13325281    81 GLLDMNKGLSLQHIGRPHSGIDDCKNIANIM 111
Cdd:pfam00929 134 SLDALAEKLGLEHIGRAHRALDDARATAKLF 164
EXOIII smart00479
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ...
 1-119 3.03e-17

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


Pssm-ID: 214685 [Multi-domain]  Cd Length: 169  Bit Score: 73.10  E-value: 3.03e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325281      1 MVDGQPSLQQVLERVDEWMAKEGLLDPNVKSIFVTCGDWDLKVMLPGQCQYLglPVADYFKqwinLKKAYSFAmgcWPKN 80
Cdd:smart00479  60 MLDDAPTFEEVLEELLEFLRGRILVAGNSAHFDLRFLKLEHPRLGIKQPPKL--PVIDTLK----LARATNPG---LPKY 130

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 13325281     81 GLLDMNKGLSLQHIGRPHSGIDDCKNIANIMKTLAYRGF 119
Cdd:smart00479 131 SLKKLAKRLLLEVIQRAHRALDDARATAKLFKKLLERLE 169
KapD COG5018
3'-5' exonuclease KapD, inhibitor of KinA-controlled sporulation [Signal transduction ...
 1-114 7.63e-17

3'-5' exonuclease KapD, inhibitor of KinA-controlled sporulation [Signal transduction mechanisms];


Pssm-ID: 444042 [Multi-domain]  Cd Length: 181  Bit Score: 72.20  E-value: 7.63e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325281   1 MVDGQPSLQQVLERVDEWMAKEglldpnvKSIFVTCGDWDLKVMLPgQCQYLGLPVaDYFKQWINLKKAYSFAMGCwpkN 80
Cdd:COG5018  70 DVDSAPSFAEAIEDFKKWIGSE-------DYILCSWGDYDRKQLER-NCRFHGVPY-PFGDRHINLKKLFALYFGL---K 137

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 13325281  81 GLLDMNKGLSLQHI---GRPHSGIDDCKNIANIMKTL 114
Cdd:COG5018 138 KRIGLKKALELLGLefeGTHHRALDDARNTAKLFKKI 174
PRK07748 PRK07748
3'-5' exonuclease KapD;
2-112 2.30e-03

3'-5' exonuclease KapD;


Pssm-ID: 236087  Cd Length: 207  Bit Score: 36.20  E-value: 2.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325281    2 VDGQPSLQQVLERVDEwmakeglLDPNVKSIFVTCGDWDLKVmLPGQCQYLGLPVAdyFK-QWINLKKAYSFAMGCWPKN 80
Cdd:PRK07748  73 VDKGISFEELVEKLAE-------YDKRCKPTIVTWGNMDMKV-LKHNCEKAGVPFP--FKgQCRDLSLEYKKFFGERNQT 142

                         90       100       110
                 ....*....|....*....|....*....|..
gi 13325281   81 GLLDMNKGLSLQHIGRPHSGIDDCKNIANIMK 112
Cdd:PRK07748 143 GLWKAIEEYGKEGTGKHHCALDDAMTTYNIFK 174
 
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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