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Conserved domains on  [gi|28572965|ref|NP_650715|]
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WRN exonuclease, isoform A [Drosophila melanogaster]

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 ...
 141-313 4.61e-60

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: 190.87  E-value: 4.61e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572965 141 SADDVLQWVEKQKDEVVPMAFDMEWPFSFQTG-PGKSAVIQICVdEKCCYIYQLTNVKKLPAALVALINHPKVRLHGVNI 219
Cdd:cd06141   3 SAQDAEEAVKELLGKEKVVGFDTEWRPSFRKGkRNKVALLQLAT-ESRCLLFQLAHMDKLPPSLKQLLEDPSILKVGVGI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572965 220 KNDFRKLARDFPEVtaeplIEKCVDLGLWCNEVCETGGRWSLERLTNFIAKKAMDKSKKVRMSKWHVIPLDENQLMYAAI 299
Cdd:cd06141  82 KGDARKLARDFGIE-----VRGVVDLSHLAKRVGPRRKLVSLARLVEEVLGLPLSKPKKVRCSNWEARPLSKEQILYAAT 156

                       170
                ....*....|....
gi 28572965 300 DVYIGQVIYRELER 313
Cdd:cd06141 157 DAYASLELYRKLLA 170
PLN02967 super family cl30538
kinase
 16-113 4.70e-03

kinase


The actual alignment was detected with superfamily member PLN02967:

Pssm-ID: 215521 [Multi-domain]  Cd Length: 581  Bit Score: 38.87  E-value: 4.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572965   16 EVPKEEAGVKKETPKVARKATKKDTPKELKDKENAG-------DDNTPKQTKGRPGRpaaKRKNLDTPDVTEklaMEEEN 88
Cdd:PLN02967  60 EEPDENGAVSKKKPTRSVKRATKKTVVEISEPLEEGselvvneDAALDKESKKTPRR---TRRKAAAASSDV---EEEKT 133

                         90       100
                 ....*....|....*....|....*
gi 28572965   89 PPKRRSSRLTRSTRSMAEDGSPSPE 113
Cdd:PLN02967 134 EKKVRKRRKVKKMDEDVEDQGSESE 158
 
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 ...
 141-313 4.61e-60

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: 190.87  E-value: 4.61e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572965 141 SADDVLQWVEKQKDEVVPMAFDMEWPFSFQTG-PGKSAVIQICVdEKCCYIYQLTNVKKLPAALVALINHPKVRLHGVNI 219
Cdd:cd06141   3 SAQDAEEAVKELLGKEKVVGFDTEWRPSFRKGkRNKVALLQLAT-ESRCLLFQLAHMDKLPPSLKQLLEDPSILKVGVGI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572965 220 KNDFRKLARDFPEVtaeplIEKCVDLGLWCNEVCETGGRWSLERLTNFIAKKAMDKSKKVRMSKWHVIPLDENQLMYAAI 299
Cdd:cd06141  82 KGDARKLARDFGIE-----VRGVVDLSHLAKRVGPRRKLVSLARLVEEVLGLPLSKPKKVRCSNWEARPLSKEQILYAAT 156

                       170
                ....*....|....
gi 28572965 300 DVYIGQVIYRELER 313
Cdd:cd06141 157 DAYASLELYRKLLA 170
35EXOc smart00474
3'-5' exonuclease; 3\' -5' exonuclease proofreading domain present in DNA polymerase I, Werner ...
 142-314 2.78e-12

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: 64.30  E-value: 2.78e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572965    142 ADDVLQWVEKQKDEVVPMAFDMEWPfSFQTGPGKSAVIQICVDEKCCYIYQLTNVKKLPAALVALINHPKVRLHGVNIKN 221
Cdd:smart00474   7 SETLEELLEKLRAAGGEVALDTETT-GLDSYSGKLVLIQISVTGEGAFIIDPLALGDDLEILKDLLEDETITKVGHNAKF 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572965    222 DFRKLARDFPEVtaepliEKCVDLGLWCNEVCETGGRWSLERLTNFIAKKAMDKSKKvrMSKWHVIPLDENQLMYAAIDV 301
Cdd:smart00474  86 DLHVLARFGIEL------ENIFDTMLAAYLLLGGPSKHGLATLLLGYLGVELDKEEQ--KSDWGARPLSEEQLEYAAEDA 157

                          170
                   ....*....|...
gi 28572965    302 YIGQVIYRELERR 314
Cdd:smart00474 158 DALLRLYEKLEKE 170
DNA_pol_A_exo1 pfam01612
3'-5' exonuclease; This domain is responsible for the 3'-5' exonuclease proofreading activity ...
 158-314 8.39e-12

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: 63.09  E-value: 8.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572965   158 PMAFDMEWPfSFQTGPGKS--AVIQICVDEKCCYIYQLTNVKKLPAALVALINHPKVRLHGVNIKNDFRKLARDFPEVTa 235
Cdd:pfam01612  22 YVAVDTETT-SLDTYSYYLrgALIQIGTGEGAYIIDPLALGDDVLSALKRLLEDPNITKVGHNAKFDLEVLARDFGIKL- 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28572965   236 EPLIEKCVDlglwcNEVCETGGRWSLERLTNFIAKKAMDKSKkvRMSKWHVIPLDENQLMYAAIDVYIGQVIYRELERR 314
Cdd:pfam01612 100 RNLFDTMLA-----AYLLGYDRSHSLADLAEKYLGVELDKEE--QCSDWQARPLSEEQLRYAALDADYLLRLYDKLRKE 171
PLN02967 PLN02967
kinase
 16-113 4.70e-03

kinase


Pssm-ID: 215521 [Multi-domain]  Cd Length: 581  Bit Score: 38.87  E-value: 4.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572965   16 EVPKEEAGVKKETPKVARKATKKDTPKELKDKENAG-------DDNTPKQTKGRPGRpaaKRKNLDTPDVTEklaMEEEN 88
Cdd:PLN02967  60 EEPDENGAVSKKKPTRSVKRATKKTVVEISEPLEEGselvvneDAALDKESKKTPRR---TRRKAAAASSDV---EEEKT 133

                         90       100
                 ....*....|....*....|....*
gi 28572965   89 PPKRRSSRLTRSTRSMAEDGSPSPE 113
Cdd:PLN02967 134 EKKVRKRRKVKKMDEDVEDQGSESE 158
 
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 ...
 141-313 4.61e-60

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: 190.87  E-value: 4.61e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572965 141 SADDVLQWVEKQKDEVVPMAFDMEWPFSFQTG-PGKSAVIQICVdEKCCYIYQLTNVKKLPAALVALINHPKVRLHGVNI 219
Cdd:cd06141   3 SAQDAEEAVKELLGKEKVVGFDTEWRPSFRKGkRNKVALLQLAT-ESRCLLFQLAHMDKLPPSLKQLLEDPSILKVGVGI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572965 220 KNDFRKLARDFPEVtaeplIEKCVDLGLWCNEVCETGGRWSLERLTNFIAKKAMDKSKKVRMSKWHVIPLDENQLMYAAI 299
Cdd:cd06141  82 KGDARKLARDFGIE-----VRGVVDLSHLAKRVGPRRKLVSLARLVEEVLGLPLSKPKKVRCSNWEARPLSKEQILYAAT 156

                       170
                ....*....|....
gi 28572965 300 DVYIGQVIYRELER 313
Cdd:cd06141 157 DAYASLELYRKLLA 170
DEDDy_polA_RNaseD_like_exo cd09018
DEDDy 3'-5' exonuclease domain of family-A DNA polymerases, RNase D, WRN, and similar proteins; ...
 159-312 1.18e-20

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: 86.91  E-value: 1.18e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572965 159 MAFDMEWPfSFQTGPGKSAVIQICVDEKCCYIYQLTNVKKLPAALVALINHPKVRLHGVNIKNDFRKLARDFPEvtaepL 238
Cdd:cd09018   2 FAFDTETD-SLDNISANLVLIQLAIEPGVAALIPVAHDYLALELLKPLLEDEKALKVGQNLKYDRGILLNYFIE-----L 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28572965 239 IEKCVDLGLWCNEVCETGGRWSLERLTNFIAKKAMDKSKKVRMSKWHVIPLDENQLMYAAIDVYIGQVIYRELE 312
Cdd:cd09018  76 RGIAFDTMLEAYILNSVAGRWDMDSLVERWLGHKLIKFESIAGKLWFNQPLTEEQGRYAAEDADVTLQIHLKLW 149
RNaseD_like cd06129
DEDDy 3'-5' exonuclease domain of RNase D, WRN, and similar proteins; The RNase D-like group ...
 159-312 2.71e-18

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: 81.02  E-value: 2.71e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572965 159 MAFDMEWPFSFQTGpGKSAVIQICVDEKCCYIYQLTNVKKLPAALVALINHPKVRLHGVNIKNDFRKLARDFPEvtaepL 238
Cdd:cd06129  16 IAFDMEWPPGRRYY-GEVALIQLCVSEEKCYLFDPLSLSVDWQGLKMLLENPSIVKALHGIEGDLWKLLRDFGE-----K 89

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28572965 239 IEKCVDLGLWCNEvCETGGRWSLERLTNFIAKKAMDKSkkVRMSKWHVIPLDENQLMYAAIDVYIGQVIYRELE 312
Cdd:cd06129  90 LQRLFDTTIAANL-KGLPERWSLASLVEHFLGKTLDKS--ISCADWSYRPLTEDQKLYAAADVYALLIIYTKLR 160
35EXOc smart00474
3'-5' exonuclease; 3\' -5' exonuclease proofreading domain present in DNA polymerase I, Werner ...
 142-314 2.78e-12

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: 64.30  E-value: 2.78e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572965    142 ADDVLQWVEKQKDEVVPMAFDMEWPfSFQTGPGKSAVIQICVDEKCCYIYQLTNVKKLPAALVALINHPKVRLHGVNIKN 221
Cdd:smart00474   7 SETLEELLEKLRAAGGEVALDTETT-GLDSYSGKLVLIQISVTGEGAFIIDPLALGDDLEILKDLLEDETITKVGHNAKF 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572965    222 DFRKLARDFPEVtaepliEKCVDLGLWCNEVCETGGRWSLERLTNFIAKKAMDKSKKvrMSKWHVIPLDENQLMYAAIDV 301
Cdd:smart00474  86 DLHVLARFGIEL------ENIFDTMLAAYLLLGGPSKHGLATLLLGYLGVELDKEEQ--KSDWGARPLSEEQLEYAAEDA 157

                          170
                   ....*....|...
gi 28572965    302 YIGQVIYRELERR 314
Cdd:smart00474 158 DALLRLYEKLEKE 170
mut-7_like_exo cd06146
DEDDy 3'-5' exonuclease domain of Caenorhabditis elegans mut-7 and similar proteins; The mut-7 ...
 138-313 4.30e-12

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: 64.24  E-value: 4.30e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572965 138 IAASADDVLQWVEKQKDEVVPM-AFDMEWPFSFQTGPG-KSAVIQICVDEK-----CCYIYQLTNvKKLPAALVALINHP 210
Cdd:cd06146   3 IVDSEEELEALLLALSLEAGRVvGIDSEWKPSFLGDSDpRVAILQLATEDEvflldLLALENLES-EDWDRLLKRLFEDP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572965 211 KVRLHGVNIKNDFRKLARDFPevTAEPLIEKC---VDLGLWCNEVCETGGRWSLE-------RLTNFIAK---KAMDKSK 277
Cdd:cd06146  82 DVLKLGFGFKQDLKALSASYP--ALKCMFERVqnvLDLQNLAKELQKSDMGRLKGnlpsktkGLADLVQEvlgKPLDKSE 159

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 28572965 278 kvRMSKWHVIPLDENQLMYAAIDVYIGQVIYRELER 313
Cdd:cd06146 160 --QCSNWERRPLREEQILYAALDAYCLLEVFDKLLE 193
DNA_pol_A_exo1 pfam01612
3'-5' exonuclease; This domain is responsible for the 3'-5' exonuclease proofreading activity ...
 158-314 8.39e-12

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: 63.09  E-value: 8.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572965   158 PMAFDMEWPfSFQTGPGKS--AVIQICVDEKCCYIYQLTNVKKLPAALVALINHPKVRLHGVNIKNDFRKLARDFPEVTa 235
Cdd:pfam01612  22 YVAVDTETT-SLDTYSYYLrgALIQIGTGEGAYIIDPLALGDDVLSALKRLLEDPNITKVGHNAKFDLEVLARDFGIKL- 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28572965   236 EPLIEKCVDlglwcNEVCETGGRWSLERLTNFIAKKAMDKSKkvRMSKWHVIPLDENQLMYAAIDVYIGQVIYRELERR 314
Cdd:pfam01612 100 RNLFDTMLA-----AYLLGYDRSHSLADLAEKYLGVELDKEE--QCSDWQARPLSEEQLRYAALDADYLLRLYDKLRKE 171
RNaseD_exo cd06142
DEDDy 3'-5' exonuclease domain of Ribonuclease D and similar proteins; Ribonuclease (RNase) D ...
 177-326 3.34e-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: 40.98  E-value: 3.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572965 177 AVIQICVDEKCcYIYQLTNVKKLPAaLVALINHPKVR--LHGVNikNDFRKLARDFPEVTAepliekcvdlGLWCNEV-- 252
Cdd:cd06142  32 CLIQISTGGEV-YLIDPLAIGDLSP-LKELLADPNIVkvFHAAR--EDLELLKRDFGILPQ----------NLFDTQIaa 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572965 253 --CETGGRWSLERLTNFIAKKAMDKSKKVrmSKWHVIPLDENQLMYAAIDVYIGQVIYRELerREKVKIKN-----EEEF 325
Cdd:cd06142  98 rlLGLGDSVGLAALVEELLGVELDKGEQR--SDWSKRPLTDEQLEYAALDVRYLLPLYEKL--KEELEEEGrlewaEEEC 173


                .
gi 28572965 326 K 326
Cdd:cd06142 174 E 174
PLN02967 PLN02967
kinase
 16-113 4.70e-03

kinase


Pssm-ID: 215521 [Multi-domain]  Cd Length: 581  Bit Score: 38.87  E-value: 4.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572965   16 EVPKEEAGVKKETPKVARKATKKDTPKELKDKENAG-------DDNTPKQTKGRPGRpaaKRKNLDTPDVTEklaMEEEN 88
Cdd:PLN02967  60 EEPDENGAVSKKKPTRSVKRATKKTVVEISEPLEEGselvvneDAALDKESKKTPRR---TRRKAAAASSDV---EEEKT 133

                         90       100
                 ....*....|....*....|....*
gi 28572965   89 PPKRRSSRLTRSTRSMAEDGSPSPE 113
Cdd:PLN02967 134 EKKVRKRRKVKKMDEDVEDQGSESE 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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