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Conserved domains on  [gi|15227581|ref|NP_181155|]
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Polynucleotidyl transferase, ribonuclease H-like superfamily protein [Arabidopsis thaliana]

Protein Classification

3'-5' exonuclease( domain architecture ID 10150121)

3'-5' exonuclease catalyzes the excision of nucleoside monophosphates at the DNA or RNA termini in the 3'-5' direction; similar to human exonuclease 3'-5' domain-containing protein 2 that that has both 3'-5' exoribonuclease and exodeoxyribonuclease activities

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
WRN_exo cd06141
DEDDy 3'-5' exonuclease domain of WRN and similar proteins; WRN is a unique RecQ DNA helicase ...
 31-202 1.95e-53

DEDDy 3'-5' exonuclease domain of WRN and similar proteins; WRN is a unique RecQ DNA helicase exhibiting an exonuclease activity. It contains a DEDDy-type DnaQ-like 3'-5' exonuclease domain possessing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D 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. Mutations in the WRN gene cause Werner syndrome, an autosomal recessive disorder associated with premature aging and increased susceptibility to cancer and type II diabetes. WRN interacts with key proteins involved in DNA replication, recombination, and repair. It is believed to maintain genomic stability and life span by participating in DNA processes. WRN is stimulated by Ku70/80, an important regulator of genomic stability.


:

Pssm-ID: 176653 [Multi-domain]  Cd Length: 170  Bit Score: 169.68  E-value: 1.95e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227581  31 THTTSTIRRWIHSIRffsrlrsSHPLVVGLDVQWTPG---GSDPPPDILQLCVGNRCLIIQLSHCKRIPEVLRSFLEDET 107
Cdd:cd06141   1 TDSAQDAEEAVKELL-------GKEKVVGFDTEWRPSfrkGKRNKVALLQLATESRCLLFQLAHMDKLPPSLKQLLEDPS 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227581 108 ITFVGVWNSQDQGKLERfRHQLEIWRLLDIRHYLPTRLLNS---SFEKIVEECLGYKGVrKDKEICMSNWGARSLSHDQI 184
Cdd:cd06141  74 ILKVGVGIKGDARKLAR-DFGIEVRGVVDLSHLAKRVGPRRklvSLARLVEEVLGLPLS-KPKKVRCSNWEARPLSKEQI 151

                       170
                ....*....|....*...
gi 15227581 185 VQASDDVYVCCKLGVKEC 202
Cdd:cd06141 152 LYAATDAYASLELYRKLL 169
 
Name Accession Description Interval E-value
WRN_exo cd06141
DEDDy 3'-5' exonuclease domain of WRN and similar proteins; WRN is a unique RecQ DNA helicase ...
 31-202 1.95e-53

DEDDy 3'-5' exonuclease domain of WRN and similar proteins; WRN is a unique RecQ DNA helicase exhibiting an exonuclease activity. It contains a DEDDy-type DnaQ-like 3'-5' exonuclease domain possessing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D 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. Mutations in the WRN gene cause Werner syndrome, an autosomal recessive disorder associated with premature aging and increased susceptibility to cancer and type II diabetes. WRN interacts with key proteins involved in DNA replication, recombination, and repair. It is believed to maintain genomic stability and life span by participating in DNA processes. WRN is stimulated by Ku70/80, an important regulator of genomic stability.


Pssm-ID: 176653 [Multi-domain]  Cd Length: 170  Bit Score: 169.68  E-value: 1.95e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227581  31 THTTSTIRRWIHSIRffsrlrsSHPLVVGLDVQWTPG---GSDPPPDILQLCVGNRCLIIQLSHCKRIPEVLRSFLEDET 107
Cdd:cd06141   1 TDSAQDAEEAVKELL-------GKEKVVGFDTEWRPSfrkGKRNKVALLQLATESRCLLFQLAHMDKLPPSLKQLLEDPS 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227581 108 ITFVGVWNSQDQGKLERfRHQLEIWRLLDIRHYLPTRLLNS---SFEKIVEECLGYKGVrKDKEICMSNWGARSLSHDQI 184
Cdd:cd06141  74 ILKVGVGIKGDARKLAR-DFGIEVRGVVDLSHLAKRVGPRRklvSLARLVEEVLGLPLS-KPKKVRCSNWEARPLSKEQI 151

                       170
                ....*....|....*...
gi 15227581 185 VQASDDVYVCCKLGVKEC 202
Cdd:cd06141 152 LYAATDAYASLELYRKLL 169
35EXOc smart00474
3'-5' exonuclease; 3\' -5' exonuclease proofreading domain present in DNA polymerase I, Werner ...
 36-206 2.64e-39

3'-5' exonuclease; 3\' -5' exonuclease proofreading domain present in DNA polymerase I, Werner syndrome helicase, RNase D and other enzymes


Pssm-ID: 214681 [Multi-domain]  Cd Length: 172  Bit Score: 133.64  E-value: 2.64e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227581     36 TIRRWIHSIRFFSRLRSsHPLVVGLDVQWTPGGS-DPPPDILQLCV-GNRCLIIQLSHCKRIPEVLRSFLEDETITFVGV 113
Cdd:smart00474   3 VVTDSETLEELLEKLRA-AGGEVALDTETTGLDSySGKLVLIQISVtGEGAFIIDPLALGDDLEILKDLLEDETITKVGH 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227581    114 WNSQDQGKLERFRHQLEIwrLLDIRHYLPTRLLNSSFEKIVEECLGYKGVRKDKEICMSNWGARSLSHDQIVQASDDVYV 193
Cdd:smart00474  82 NAKFDLHVLARFGIELEN--IFDTMLAAYLLLGGPSKHGLATLLLGYLGVELDKEEQKSDWGARPLSEEQLEYAAEDADA 159

                          170
                   ....*....|...
gi 15227581    194 CCKLgvKECIWKE 206
Cdd:smart00474 160 LLRL--YEKLEKE 170
DNA_pol_A_exo1 pfam01612
3'-5' exonuclease; This domain is responsible for the 3'-5' exonuclease proofreading activity ...
 46-193 9.92e-09

3'-5' exonuclease; This domain is responsible for the 3'-5' exonuclease proofreading activity of E. coli DNA polymerase I (polI) and other enzymes, it catalyzes the hydrolysis of unpaired or mismatched nucleotides. This domain consists of the amino-terminal half of the Klenow fragment in E. coli polI it is also found in the Werner syndrome helicase (WRN), focus forming activity 1 protein (FFA-1) and ribonuclease D (RNase D). Werner syndrome is a human genetic disorder causing premature aging; the WRN protein has helicase activity in the 3'-5' direction. The FFA-1 protein is required for formation of a replication foci and also has helicase activity; it is a homolog of the WRN protein. RNase D is a 3'-5' exonuclease involved in tRNA processing. Also found in this family is the autoantigen PM/Scl thought to be involved in polymyositis-scleroderma overlap syndrome.


Pssm-ID: 396266 [Multi-domain]  Cd Length: 173  Bit Score: 53.07  E-value: 9.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227581    46 FFSRLRSSHPlvVGLDVQWTPGgsDPPPD-----ILQLCVGNRCLIIQLSHCKRIP-EVLRSFLEDETITFVGVWNSQDQ 119
Cdd:pfam01612  13 LIEELLNAPY--VAVDTETTSL--DTYSYylrgaLIQIGTGEGAYIIDPLALGDDVlSALKRLLEDPNITKVGHNAKFDL 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15227581   120 GKLERfRHQLEIWRLLDIR--HYLPTRLLNSSFEKIVEECLGYKgvrKDKEICMSNWGARSLSHDQIVQASDDVYV 193
Cdd:pfam01612  89 EVLAR-DFGIKLRNLFDTMlaAYLLGYDRSHSLADLAEKYLGVE---LDKEEQCSDWQARPLSEEQLRYAALDADY 160
Rnd COG0349
Ribonuclease D [Translation, ribosomal structure and biogenesis];
76-192 3.03e-04

Ribonuclease D [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440118 [Multi-domain]  Cd Length: 365  Bit Score: 41.40  E-value: 3.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227581  76 LQLCVGNRCLIIQlshCKRIPEV--LRSFLEDETITFV---GvwnSQDqgkLERFRHQLEIwrlldirhyLPTRL----- 145
Cdd:COG0349  40 IQLADGEEVALID---PLAIGDLspLWELLADPAIVKVfhaA---RED---LEILYHLFGI---------LPKPLfdtqi 101

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15227581 146 --------LNSSFEKIVEECLGykgVRKDKEICMSNWGARSLSHDQIVQASDDVY 192
Cdd:COG0349 102 aaallgygDSVGYAALVEELLG---VELDKSEQRSDWLRRPLSEEQLEYAAADVR 153
 
Name Accession Description Interval E-value
WRN_exo cd06141
DEDDy 3'-5' exonuclease domain of WRN and similar proteins; WRN is a unique RecQ DNA helicase ...
 31-202 1.95e-53

DEDDy 3'-5' exonuclease domain of WRN and similar proteins; WRN is a unique RecQ DNA helicase exhibiting an exonuclease activity. It contains a DEDDy-type DnaQ-like 3'-5' exonuclease domain possessing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D 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. Mutations in the WRN gene cause Werner syndrome, an autosomal recessive disorder associated with premature aging and increased susceptibility to cancer and type II diabetes. WRN interacts with key proteins involved in DNA replication, recombination, and repair. It is believed to maintain genomic stability and life span by participating in DNA processes. WRN is stimulated by Ku70/80, an important regulator of genomic stability.


Pssm-ID: 176653 [Multi-domain]  Cd Length: 170  Bit Score: 169.68  E-value: 1.95e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227581  31 THTTSTIRRWIHSIRffsrlrsSHPLVVGLDVQWTPG---GSDPPPDILQLCVGNRCLIIQLSHCKRIPEVLRSFLEDET 107
Cdd:cd06141   1 TDSAQDAEEAVKELL-------GKEKVVGFDTEWRPSfrkGKRNKVALLQLATESRCLLFQLAHMDKLPPSLKQLLEDPS 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227581 108 ITFVGVWNSQDQGKLERfRHQLEIWRLLDIRHYLPTRLLNS---SFEKIVEECLGYKGVrKDKEICMSNWGARSLSHDQI 184
Cdd:cd06141  74 ILKVGVGIKGDARKLAR-DFGIEVRGVVDLSHLAKRVGPRRklvSLARLVEEVLGLPLS-KPKKVRCSNWEARPLSKEQI 151

                       170
                ....*....|....*...
gi 15227581 185 VQASDDVYVCCKLGVKEC 202
Cdd:cd06141 152 LYAATDAYASLELYRKLL 169
35EXOc smart00474
3'-5' exonuclease; 3\' -5' exonuclease proofreading domain present in DNA polymerase I, Werner ...
 36-206 2.64e-39

3'-5' exonuclease; 3\' -5' exonuclease proofreading domain present in DNA polymerase I, Werner syndrome helicase, RNase D and other enzymes


Pssm-ID: 214681 [Multi-domain]  Cd Length: 172  Bit Score: 133.64  E-value: 2.64e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227581     36 TIRRWIHSIRFFSRLRSsHPLVVGLDVQWTPGGS-DPPPDILQLCV-GNRCLIIQLSHCKRIPEVLRSFLEDETITFVGV 113
Cdd:smart00474   3 VVTDSETLEELLEKLRA-AGGEVALDTETTGLDSySGKLVLIQISVtGEGAFIIDPLALGDDLEILKDLLEDETITKVGH 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227581    114 WNSQDQGKLERFRHQLEIwrLLDIRHYLPTRLLNSSFEKIVEECLGYKGVRKDKEICMSNWGARSLSHDQIVQASDDVYV 193
Cdd:smart00474  82 NAKFDLHVLARFGIELEN--IFDTMLAAYLLLGGPSKHGLATLLLGYLGVELDKEEQKSDWGARPLSEEQLEYAAEDADA 159

                          170
                   ....*....|...
gi 15227581    194 CCKLgvKECIWKE 206
Cdd:smart00474 160 LLRL--YEKLEKE 170
mut-7_like_exo cd06146
DEDDy 3'-5' exonuclease domain of Caenorhabditis elegans mut-7 and similar proteins; The mut-7 ...
 57-197 7.06e-13

DEDDy 3'-5' exonuclease domain of Caenorhabditis elegans mut-7 and similar proteins; The mut-7 subfamily is composed of Caenorhabditis elegans mut-7 and similar proteins found in plants and metazoans. Mut-7 is implicated in posttranscriptional gene silencing. It contains a DEDDy-type DnaQ-like 3'-5' exonuclease domain possessing three conserved sequence motifs, termed ExoI, ExoII and ExoIII, with a specific YX(3)D 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: 176655  Cd Length: 193  Bit Score: 65.01  E-value: 7.06e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227581  57 VVGLDVQWTP---GGSDPPPDILQLCVGNR-----CLIIQLSHCKRIPEVLRSFLEDETITFVGVWNSQDQGKLER---- 124
Cdd:cd06146  24 VVGIDSEWKPsflGDSDPRVAILQLATEDEvflldLLALENLESEDWDRLLKRLFEDPDVLKLGFGFKQDLKALSAsypa 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227581 125 FRHQLE-IWRLLDIRH---YL-------PTRLLNS---SFEKIVEECLGykgVRKDKEICMSNWGARSLSHDQIVQASDD 190
Cdd:cd06146 104 LKCMFErVQNVLDLQNlakELqksdmgrLKGNLPSktkGLADLVQEVLG---KPLDKSEQCSNWERRPLREEQILYAALD 180


                ....*..
gi 15227581 191 VYVCCKL 197
Cdd:cd06146 181 AYCLLEV 187
DEDDy_polA_RNaseD_like_exo cd09018
DEDDy 3'-5' exonuclease domain of family-A DNA polymerases, RNase D, WRN, and similar proteins; ...
 57-193 5.05e-12

DEDDy 3'-5' exonuclease domain of family-A DNA polymerases, RNase D, WRN, and similar proteins; DEDDy 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. They contain four invariant acidic residues in three conserved sequence motifs termed ExoI, ExoII and ExoIII. DEDDy exonucleases are classified as such because of the presence of a specific YX(3)D pattern at ExoIII. The four conserved acidic residues serve as ligands for the two metal ions required for catalysis. This family of DEDDy exonucleases includes the proofreading domains of family A DNA polymerases, as well as RNases such as RNase D and yeast Rrp6p. The Egalitarian (Egl) and Bacillus-like DNA Polymerase I subfamilies do not possess a completely conserved YX(3)D pattern at the ExoIII motif. In addition, the Bacillus-like DNA polymerase I subfamily has inactive 3'-5' exonuclease domains which do not possess the metal-binding residues necessary for activity.


Pssm-ID: 176656 [Multi-domain]  Cd Length: 150  Bit Score: 61.87  E-value: 5.05e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227581  57 VVGLDVQWTPGGSDPPP-DILQLCVG-NRCLIIQLSHCKRIPEVLRSFLEDETITFVGVWNSQDQGKLER-FRHQLEIWR 133
Cdd:cd09018   1 VFAFDTETDSLDNISANlVLIQLAIEpGVAALIPVAHDYLALELLKPLLEDEKALKVGQNLKYDRGILLNyFIELRGIAF 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15227581 134 LLDIRHYLPTRLLNS-SFEKIVEECLGYKgVRKDKEICMSNWGARSLSHDQIVQASDDVYV 193
Cdd:cd09018  81 DTMLEAYILNSVAGRwDMDSLVERWLGHK-LIKFESIAGKLWFNQPLTEEQGRYAAEDADV 140
RNaseD_like cd06129
DEDDy 3'-5' exonuclease domain of RNase D, WRN, and similar proteins; The RNase D-like group ...
 48-192 7.49e-12

DEDDy 3'-5' exonuclease domain of RNase D, WRN, and similar proteins; The RNase D-like group is composed of RNase D, WRN, and similar proteins. They contain a DEDDy-type, DnaQ-like, 3'-5' exonuclease domain that contains three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D 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. RNase D is involved in the 3'-end processing of tRNA precursors. RNase D-like proteins in eukaryotes include yeast Rrp6p, human PM/Scl-100 and Drosophila melanogaster egalitarian (Egl) protein. WRN is a unique DNA helicase possessing exonuclease activity. Mutation in the WRN gene is implicated in Werner syndrome, a disease associated with premature aging and increased predisposition to cancer. Yeast Rrp6p and the human Polymyositis/scleroderma autoantigen 100kDa (PM/Scl-100) are exosome-associated proteins involved in the degradation and processing of precursors to stable RNAs. Egl is a component of an mRNA-binding complex which is required for oocyte specification. The Egl subfamily does not possess a completely conserved YX(3)D pattern at the ExoIII motif.


Pssm-ID: 176650 [Multi-domain]  Cd Length: 161  Bit Score: 61.38  E-value: 7.49e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227581  48 SRLRSSHPlVVGLDVQWTPGGSDPPPDIL-QLCV-GNRCLIIQLSHCKRIPEVLRSFLEDETITFVGVWNSQDQGKLER- 124
Cdd:cd06129   7 EDLSMDGD-VIAFDMEWPPGRRYYGEVALiQLCVsEEKCYLFDPLSLSVDWQGLKMLLENPSIVKALHGIEGDLWKLLRd 85

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15227581 125 FRHQLEiwRLLDIRHY-----LPTRLlnsSFEKIVEEclgYKGVRKDKEICMSNWGARSLSHDQIVQASDDVY 192
Cdd:cd06129  86 FGEKLQ--RLFDTTIAanlkgLPERW---SLASLVEH---FLGKTLDKSISCADWSYRPLTEDQKLYAAADVY 150
DNA_pol_A_exo1 pfam01612
3'-5' exonuclease; This domain is responsible for the 3'-5' exonuclease proofreading activity ...
 46-193 9.92e-09

3'-5' exonuclease; This domain is responsible for the 3'-5' exonuclease proofreading activity of E. coli DNA polymerase I (polI) and other enzymes, it catalyzes the hydrolysis of unpaired or mismatched nucleotides. This domain consists of the amino-terminal half of the Klenow fragment in E. coli polI it is also found in the Werner syndrome helicase (WRN), focus forming activity 1 protein (FFA-1) and ribonuclease D (RNase D). Werner syndrome is a human genetic disorder causing premature aging; the WRN protein has helicase activity in the 3'-5' direction. The FFA-1 protein is required for formation of a replication foci and also has helicase activity; it is a homolog of the WRN protein. RNase D is a 3'-5' exonuclease involved in tRNA processing. Also found in this family is the autoantigen PM/Scl thought to be involved in polymyositis-scleroderma overlap syndrome.


Pssm-ID: 396266 [Multi-domain]  Cd Length: 173  Bit Score: 53.07  E-value: 9.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227581    46 FFSRLRSSHPlvVGLDVQWTPGgsDPPPD-----ILQLCVGNRCLIIQLSHCKRIP-EVLRSFLEDETITFVGVWNSQDQ 119
Cdd:pfam01612  13 LIEELLNAPY--VAVDTETTSL--DTYSYylrgaLIQIGTGEGAYIIDPLALGDDVlSALKRLLEDPNITKVGHNAKFDL 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15227581   120 GKLERfRHQLEIWRLLDIR--HYLPTRLLNSSFEKIVEECLGYKgvrKDKEICMSNWGARSLSHDQIVQASDDVYV 193
Cdd:pfam01612  89 EVLAR-DFGIKLRNLFDTMlaAYLLGYDRSHSLADLAEKYLGVE---LDKEEQCSDWQARPLSEEQLRYAALDADY 160
RNaseD_exo cd06142
DEDDy 3'-5' exonuclease domain of Ribonuclease D and similar proteins; Ribonuclease (RNase) D ...
 76-191 2.61e-04

DEDDy 3'-5' exonuclease domain of Ribonuclease D and similar proteins; Ribonuclease (RNase) D is a bacterial enzyme involved in the maturation of small stable RNAs and the 3' maturation of tRNA. It contains a DEDDy-type DnaQ-like 3'-5' exonuclease domain possessing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D 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. In vivo, RNase D only becomes essential upon removal of other ribonucleases. Eukaryotic RNase D homologs include yeast Rrp6p, human PM/Scl-100, and the Drosophila melanogaster egalitarian protein.


Pssm-ID: 176654 [Multi-domain]  Cd Length: 178  Bit Score: 40.59  E-value: 2.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227581  76 LQLCVGNRCLIIQlshCKRIP--EVLRSFLEDETITFV---GvwnSQDqgkLERFRHQLEIW--RLLDIrhYLPTRLLNS 148
Cdd:cd06142  34 IQISTGGEVYLID---PLAIGdlSPLKELLADPNIVKVfhaA---RED---LELLKRDFGILpqNLFDT--QIAARLLGL 102

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15227581 149 ----SFEKIVEECLGykgVRKDKEICMSNWGARSLSHDQIVQASDDV 191
Cdd:cd06142 103 gdsvGLAALVEELLG---VELDKGEQRSDWSKRPLTDEQLEYAALDV 146
Rnd COG0349
Ribonuclease D [Translation, ribosomal structure and biogenesis];
76-192 3.03e-04

Ribonuclease D [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440118 [Multi-domain]  Cd Length: 365  Bit Score: 41.40  E-value: 3.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227581  76 LQLCVGNRCLIIQlshCKRIPEV--LRSFLEDETITFV---GvwnSQDqgkLERFRHQLEIwrlldirhyLPTRL----- 145
Cdd:COG0349  40 IQLADGEEVALID---PLAIGDLspLWELLADPAIVKVfhaA---RED---LEILYHLFGI---------LPKPLfdtqi 101

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15227581 146 --------LNSSFEKIVEECLGykgVRKDKEICMSNWGARSLSHDQIVQASDDVY 192
Cdd:COG0349 102 aaallgygDSVGYAALVEELLG---VELDKSEQRSDWLRRPLSEEQLEYAAADVR 153
 
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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