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Conserved domains on  [gi|1370514688|ref|XP_024303356|]
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exonuclease mut-7 homolog isoform X5 [Homo sapiens]

Protein Classification

exonuclease mut-7 family protein; 3'-5' exonuclease( domain architecture ID 10150257)

exonuclease mut-7 family protein belonging to the DnaQ-like (or DEDD) 3'-5' exonuclease superfamily may catalyze the excision of nucleoside monophosphates at the DNA or RNA termini in the 3'-5' direction| 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
mut-7_like_exo cd06146
DEDDy 3'-5' exonuclease domain of Caenorhabditis elegans mut-7 and similar proteins; The mut-7 ...
 325-521 1.95e-74

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: 241.43  E-value: 1.95e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 325 VHLLASWEDLTRHEGAL-LQCHQVVGVDVEWTPVFVAGGRPRPSLLQVAVEGHVFLLDVLALSQpptgQGAQAFSRLVAQ 403
Cdd:cd06146     1 IHIVDSEEELEALLLALsLEAGRVVGIDSEWKPSFLGDSDPRVAILQLATEDEVFLLDLLALEN----LESEDWDRLLKR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 404 LLSDPSITKLGYGMVGDLQKLGTSCPALAHVEKQILGGMDLLLVHRQqMRVASVPAPAVDRARELRGLSLLVQQVLGTAL 483
Cdd:cd06146    77 LFEDPDVLKLGFGFKQDLKALSASYPALKCMFERVQNVLDLQNLAKE-LQKSDMGRLKGNLPSKTKGLADLVQEVLGKPL 155

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1370514688 484 DKTQQLSNWDRRPLCEEQVIYAAADAYCLLEVHQALCR 521
Cdd:cd06146   156 DKSEQCSNWERRPLREEQILYAALDAYCLLEVFDKLLE 193
Mut7-C super family cl19501
Mut7-C RNAse domain; RNAse domain of the PIN fold with an inserted Zinc Ribbon at the C ...
 584-680 9.58e-13

Mut7-C RNAse domain; RNAse domain of the PIN fold with an inserted Zinc Ribbon at the C terminus.


The actual alignment was detected with superfamily member pfam01927:

Pssm-ID: 473177  Cd Length: 146  Bit Score: 66.51  E-value: 9.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 584 RVVCDNMLQGLARSLRCLGVDARmLGNGEDHRRAAEVARQEGRIILTSGQPFHKlRAQVgAGRCLSvdCSLKAQQQAKAV 663
Cdd:pfam01927   2 RFLLDAMLGKLARYLRMLGYDTL-YDNDYEDDELLRIAAKEGRILLTRDRGLLK-RREL-THGVYV--RSLDPEEQLREV 76

                          90
                  ....*....|....*..
gi 1370514688 664 LKHFNVRVTHADIFSRC 680
Cdd:pfam01927  77 IARLGLALSLKPEFSRC 93
 
Name Accession Description Interval E-value
mut-7_like_exo cd06146
DEDDy 3'-5' exonuclease domain of Caenorhabditis elegans mut-7 and similar proteins; The mut-7 ...
 325-521 1.95e-74

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: 241.43  E-value: 1.95e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 325 VHLLASWEDLTRHEGAL-LQCHQVVGVDVEWTPVFVAGGRPRPSLLQVAVEGHVFLLDVLALSQpptgQGAQAFSRLVAQ 403
Cdd:cd06146     1 IHIVDSEEELEALLLALsLEAGRVVGIDSEWKPSFLGDSDPRVAILQLATEDEVFLLDLLALEN----LESEDWDRLLKR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 404 LLSDPSITKLGYGMVGDLQKLGTSCPALAHVEKQILGGMDLLLVHRQqMRVASVPAPAVDRARELRGLSLLVQQVLGTAL 483
Cdd:cd06146    77 LFEDPDVLKLGFGFKQDLKALSASYPALKCMFERVQNVLDLQNLAKE-LQKSDMGRLKGNLPSKTKGLADLVQEVLGKPL 155

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1370514688 484 DKTQQLSNWDRRPLCEEQVIYAAADAYCLLEVHQALCR 521
Cdd:cd06146   156 DKSEQCSNWERRPLREEQILYAALDAYCLLEVFDKLLE 193
DNA_pol_A_exo1 pfam01612
3'-5' exonuclease; This domain is responsible for the 3'-5' exonuclease proofreading activity ...
 342-522 4.37e-22

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: 93.91  E-value: 4.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 342 LQCHQVVGVDVEWTPVFVAGGRPRPSLLQVAVEGHVFLLDVLALsqpptgqgAQAFSRLVAQLLSDPSITKLGYGMVGDL 421
Cdd:pfam01612  17 LLNAPYVAVDTETTSLDTYSYYLRGALIQIGTGEGAYIIDPLAL--------GDDVLSALKRLLEDPNITKVGHNAKFDL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 422 qklgtscPALAHVEKQILGGM-DLLLVHRqqmrvasvpapAVDRARElRGLSLLVQQVLGTALDKTQQLSNWDRRPLCEE 500
Cdd:pfam01612  89 -------EVLARDFGIKLRNLfDTMLAAY-----------LLGYDRS-HSLADLAEKYLGVELDKEEQCSDWQARPLSEE 149

                         170       180
                  ....*....|....*....|..
gi 1370514688 501 QVIYAAADAYCLLEVHQALCRE 522
Cdd:pfam01612 150 QLRYAALDADYLLRLYDKLRKE 171
35EXOc smart00474
3'-5' exonuclease; 3\' -5' exonuclease proofreading domain present in DNA polymerase I, Werner ...
 325-519 1.12e-17

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: 81.25  E-value: 1.12e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688  325 VHLLASWEDLTRHEGALLQCHQVVGVDVEWTPVFVAGGRPRpsLLQVAVEG-HVFLLDVLALSQPPTgqgaqafsrLVAQ 403
Cdd:smart00474   1 VIVVTDSETLEELLEKLRAAGGEVALDTETTGLDSYSGKLV--LIQISVTGeGAFIIDPLALGDDLE---------ILKD 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688  404 LLSDPSITKLGYGMVGDLQKLgtscpALAHVEkqiLGGM-DLLLVHRQqmrvasvpapaVDRARELRGLSLLVQQVLGTA 482
Cdd:smart00474  70 LLEDETITKVGHNAKFDLHVL-----ARFGIE---LENIfDTMLAAYL-----------LLGGPSKHGLATLLLGYLGVE 130

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1370514688  483 LDKTQQLSNWDRRPLCEEQVIYAAADAYCLLEVHQAL 519
Cdd:smart00474 131 LDKEEQKSDWGARPLSEEQLEYAAEDADALLRLYEKL 167
Rnd COG0349
Ribonuclease D [Translation, ribosomal structure and biogenesis];
332-522 2.58e-16

Ribonuclease D [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440118 [Multi-domain]  Cd Length: 365  Bit Score: 81.46  E-value: 2.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 332 EDLTRHEGALLQcHQVVGVDVEwtpvFVAG--GRPRPSLLQVAVEGHVFLLDVLALsqpptgqgaQAFSRLvAQLLSDPS 409
Cdd:COG0349     6 EELAALCARLAQ-APAVAVDTE----FMRErtYYPRLCLIQLADGEEVALIDPLAI---------GDLSPL-WELLADPA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 410 ITKLGYGMVGDLQKLGTSCPALAH------VEKQILGgmdlllvHRQQMrvasvpapavdrarelrGLSLLVQQVLGTAL 483
Cdd:COG0349    71 IVKVFHAAREDLEILYHLFGILPKplfdtqIAAALLG-------YGDSV-----------------GYAALVEELLGVEL 126

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1370514688 484 DKTQQLSNWDRRPLCEEQVIYAAADAYCLLEVHQALCRE 522
Cdd:COG0349   127 DKSEQRSDWLRRPLSEEQLEYAAADVRYLLPLYEKLLEE 165
Mut7-C pfam01927
Mut7-C RNAse domain; RNAse domain of the PIN fold with an inserted Zinc Ribbon at the C ...
 584-680 9.58e-13

Mut7-C RNAse domain; RNAse domain of the PIN fold with an inserted Zinc Ribbon at the C terminus.


Pssm-ID: 426515  Cd Length: 146  Bit Score: 66.51  E-value: 9.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 584 RVVCDNMLQGLARSLRCLGVDARmLGNGEDHRRAAEVARQEGRIILTSGQPFHKlRAQVgAGRCLSvdCSLKAQQQAKAV 663
Cdd:pfam01927   2 RFLLDAMLGKLARYLRMLGYDTL-YDNDYEDDELLRIAAKEGRILLTRDRGLLK-RREL-THGVYV--RSLDPEEQLREV 76

                          90
                  ....*....|....*..
gi 1370514688 664 LKHFNVRVTHADIFSRC 680
Cdd:pfam01927  77 IARLGLALSLKPEFSRC 93
Mut7-C COG1656
Uncharacterized conserved protein, contains PIN-related Mut7-C RNAse domain [General function ...
 584-847 1.14e-10

Uncharacterized conserved protein, contains PIN-related Mut7-C RNAse domain [General function prediction only];


Pssm-ID: 441262  Cd Length: 155  Bit Score: 60.65  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 584 RVVCDNMLQGLARSLRCLGVDARMLGNGEDhRRAAEVARQEGRIILTSGQPFHKlRAQVGAGRCLSvdcSLKAQQQAKAV 663
Cdd:COG1656     2 RFLLDVMLGKLARWLRMLGFDTLYANDIDD-DELLAIAREEGRILLTRDRGLLK-RAEVTRGVLLR---STDPEEQLAEV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 664 LKHFNVRVTHADIFSRCqtqsfeeraegwgmghpekPRlglstpsgpqaCNcdqylkvsrdmmkqlmwlsshqegprssg 743
Cdd:COG1656    77 LRRFGLDLELDRPFTRC-------------------LR-----------CN----------------------------- 97

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 744 deatqsqavqepgpapdaapegctydrpcrwlqmADLRAETPDMLADGtrlqlagVPVGVLRTPglRCFYCCTGCGKVFW 823
Cdd:COG1656    98 ----------------------------------GPLEPVDKEEVADR-------VPPYVRERY--DEFWRCPKCGKVYW 134

                         250       260
                  ....*....|....*....|....
gi 1370514688 824 DGSHLGRVathfRDMLESAPSPCE 847
Cdd:COG1656   135 RGSHWRRM----RERLERLLKRSA 154
rnd TIGR01388
ribonuclease D; This model describes ribonuclease D, a 3'-exonuclease shown to act on tRNA ...
 364-531 3.09e-10

ribonuclease D; This model describes ribonuclease D, a 3'-exonuclease shown to act on tRNA both in vitro and when overexpressed in vivo. Trusted members of this family are restricted to the Proteobacteria; Aquifex, Mycobacterial, and eukaryotic homologs are not full-length homologs. Ribonuclease D is not essential in E. coli and is deleterious when overexpressed. Its precise biological role is still unknown. [Transcription, RNA processing]


Pssm-ID: 130455 [Multi-domain]  Cd Length: 367  Bit Score: 62.86  E-value: 3.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 364 PRPSLLQVAVEGHVFLLDVLALsqpptgqgaQAFSRLVAqLLSDPSITKLGYGMVGDLQKLGTSCPALAH--VEKQILGg 441
Cdd:TIGR01388  35 PQLGLIQVADGEQLALIDPLVI---------IDWSPLKE-LLRDESVVKVLHAASEDLEVFLNLFGELPQplFDTQIAA- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 442 mdLLLVHRQQMrvasvpapavdrarelrGLSLLVQQVLGTALDKTQQLSNWDRRPLCEEQVIYAAADAYCLLEVHQALCR 521
Cdd:TIGR01388 104 --AFCGFGMSM-----------------GYAKLVQEVLGVELDKSESRTDWLARPLTDAQLEYAAADVTYLLPLYAKLME 164

                         170
                  ....*....|...
gi 1370514688 522 EPA---RFHLSED 531
Cdd:TIGR01388 165 RLEesgRLAWLEE 177
PRK10829 PRK10829
ribonuclease D; Provisional
 470-522 1.35e-05

ribonuclease D; Provisional


Pssm-ID: 236771 [Multi-domain]  Cd Length: 373  Bit Score: 48.46  E-value: 1.35e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370514688 470 GLSLLVQQVLGTALDKTQQLSNWDRRPLCEEQVIYAAADAYCLLEVHQALCRE 522
Cdd:PRK10829  117 GFASMVEEYTGVTLDKSESRTDWLARPLSERQCEYAAADVFYLLPIAAKLMAE 169
 
Name Accession Description Interval E-value
mut-7_like_exo cd06146
DEDDy 3'-5' exonuclease domain of Caenorhabditis elegans mut-7 and similar proteins; The mut-7 ...
 325-521 1.95e-74

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: 241.43  E-value: 1.95e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 325 VHLLASWEDLTRHEGAL-LQCHQVVGVDVEWTPVFVAGGRPRPSLLQVAVEGHVFLLDVLALSQpptgQGAQAFSRLVAQ 403
Cdd:cd06146     1 IHIVDSEEELEALLLALsLEAGRVVGIDSEWKPSFLGDSDPRVAILQLATEDEVFLLDLLALEN----LESEDWDRLLKR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 404 LLSDPSITKLGYGMVGDLQKLGTSCPALAHVEKQILGGMDLLLVHRQqMRVASVPAPAVDRARELRGLSLLVQQVLGTAL 483
Cdd:cd06146    77 LFEDPDVLKLGFGFKQDLKALSASYPALKCMFERVQNVLDLQNLAKE-LQKSDMGRLKGNLPSKTKGLADLVQEVLGKPL 155

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1370514688 484 DKTQQLSNWDRRPLCEEQVIYAAADAYCLLEVHQALCR 521
Cdd:cd06146   156 DKSEQCSNWERRPLREEQILYAALDAYCLLEVFDKLLE 193
WRN_exo cd06141
DEDDy 3'-5' exonuclease domain of WRN and similar proteins; WRN is a unique RecQ DNA helicase ...
 340-521 7.68e-40

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: 144.64  E-value: 7.68e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 340 ALLQCHQVVGVDVEWTPVFVAGGRPRPSLLQVAVEGHVFLLDVLALsqpptgqgaQAFSRLVAQLLSDPSITKLGYGMVG 419
Cdd:cd06141    13 ELLGKEKVVGFDTEWRPSFRKGKRNKVALLQLATESRCLLFQLAHM---------DKLPPSLKQLLEDPSILKVGVGIKG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 420 DLQKLGTSCPAlahvekQILGGMDLLLVHRQqmrvasvpapaVDRARELRGLSLLVQQVLGTALDK--TQQLSNWDRRPL 497
Cdd:cd06141    84 DARKLARDFGI------EVRGVVDLSHLAKR-----------VGPRRKLVSLARLVEEVLGLPLSKpkKVRCSNWEARPL 146

                         170       180
                  ....*....|....*....|....
gi 1370514688 498 CEEQVIYAAADAYCLLEVHQALCR 521
Cdd:cd06141   147 SKEQILYAATDAYASLELYRKLLA 170
DNA_pol_A_exo1 pfam01612
3'-5' exonuclease; This domain is responsible for the 3'-5' exonuclease proofreading activity ...
 342-522 4.37e-22

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: 93.91  E-value: 4.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 342 LQCHQVVGVDVEWTPVFVAGGRPRPSLLQVAVEGHVFLLDVLALsqpptgqgAQAFSRLVAQLLSDPSITKLGYGMVGDL 421
Cdd:pfam01612  17 LLNAPYVAVDTETTSLDTYSYYLRGALIQIGTGEGAYIIDPLAL--------GDDVLSALKRLLEDPNITKVGHNAKFDL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 422 qklgtscPALAHVEKQILGGM-DLLLVHRqqmrvasvpapAVDRARElRGLSLLVQQVLGTALDKTQQLSNWDRRPLCEE 500
Cdd:pfam01612  89 -------EVLARDFGIKLRNLfDTMLAAY-----------LLGYDRS-HSLADLAEKYLGVELDKEEQCSDWQARPLSEE 149

                         170       180
                  ....*....|....*....|..
gi 1370514688 501 QVIYAAADAYCLLEVHQALCRE 522
Cdd:pfam01612 150 QLRYAALDADYLLRLYDKLRKE 171
RNaseD_exo cd06142
DEDDy 3'-5' exonuclease domain of Ribonuclease D and similar proteins; Ribonuclease (RNase) D ...
 340-522 3.99e-20

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: 88.74  E-value: 3.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 340 ALLQCHQVVGVDVE--WTPVFvaggRPRPSLLQVAVEGHVFLLDVLALSQPPtgqgaqafsrLVAQLLSDPSITKLGYGm 417
Cdd:cd06142     7 ERLASAGVIAVDTEfmRLNTY----YPRLCLIQISTGGEVYLIDPLAIGDLS----------PLKELLADPNIVKVFHA- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 418 vgdlqklgtscpalahvekqilGGMDLLLVHRQQMRVasvPAPAVDR---ARELR-----GLSLLVQQVLGTALDKTQQL 489
Cdd:cd06142    72 ----------------------AREDLELLKRDFGIL---PQNLFDTqiaARLLGlgdsvGLAALVEELLGVELDKGEQR 126

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1370514688 490 SNWDRRPLCEEQVIYAAADAYCLLEVHQALCRE 522
Cdd:cd06142   127 SDWSKRPLTDEQLEYAALDVRYLLPLYEKLKEE 159
RNaseD_like cd06129
DEDDy 3'-5' exonuclease domain of RNase D, WRN, and similar proteins; The RNase D-like group ...
 345-519 2.03e-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: 83.33  E-value: 2.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 345 HQVVGVDVEWTPVFVAGGRPrpSLLQVAVEG-HVFLLDVLALSQPPTGqgaqafsrlVAQLLSDPSITKLGYGMVGDLQK 423
Cdd:cd06129    13 GDVIAFDMEWPPGRRYYGEV--ALIQLCVSEeKCYLFDPLSLSVDWQG---------LKMLLENPSIVKALHGIEGDLWK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 424 LgtscpaLAHVEKQILGGMDLLLVHRQQMRvasvpapavdraRELRGLSLLVQQVLGTALDKTQQLSNWDRRPLCEEQVI 503
Cdd:cd06129    82 L------LRDFGEKLQRLFDTTIAANLKGL------------PERWSLASLVEHFLGKTLDKSISCADWSYRPLTEDQKL 143

                         170
                  ....*....|....*.
gi 1370514688 504 YAAADAYCLLEVHQAL 519
Cdd:cd06129   144 YAAADVYALLIIYTKL 159
35EXOc smart00474
3'-5' exonuclease; 3\' -5' exonuclease proofreading domain present in DNA polymerase I, Werner ...
 325-519 1.12e-17

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: 81.25  E-value: 1.12e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688  325 VHLLASWEDLTRHEGALLQCHQVVGVDVEWTPVFVAGGRPRpsLLQVAVEG-HVFLLDVLALSQPPTgqgaqafsrLVAQ 403
Cdd:smart00474   1 VIVVTDSETLEELLEKLRAAGGEVALDTETTGLDSYSGKLV--LIQISVTGeGAFIIDPLALGDDLE---------ILKD 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688  404 LLSDPSITKLGYGMVGDLQKLgtscpALAHVEkqiLGGM-DLLLVHRQqmrvasvpapaVDRARELRGLSLLVQQVLGTA 482
Cdd:smart00474  70 LLEDETITKVGHNAKFDLHVL-----ARFGIE---LENIfDTMLAAYL-----------LLGGPSKHGLATLLLGYLGVE 130

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1370514688  483 LDKTQQLSNWDRRPLCEEQVIYAAADAYCLLEVHQAL 519
Cdd:smart00474 131 LDKEEQKSDWGARPLSEEQLEYAAEDADALLRLYEKL 167
Rnd COG0349
Ribonuclease D [Translation, ribosomal structure and biogenesis];
332-522 2.58e-16

Ribonuclease D [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440118 [Multi-domain]  Cd Length: 365  Bit Score: 81.46  E-value: 2.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 332 EDLTRHEGALLQcHQVVGVDVEwtpvFVAG--GRPRPSLLQVAVEGHVFLLDVLALsqpptgqgaQAFSRLvAQLLSDPS 409
Cdd:COG0349     6 EELAALCARLAQ-APAVAVDTE----FMRErtYYPRLCLIQLADGEEVALIDPLAI---------GDLSPL-WELLADPA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 410 ITKLGYGMVGDLQKLGTSCPALAH------VEKQILGgmdlllvHRQQMrvasvpapavdrarelrGLSLLVQQVLGTAL 483
Cdd:COG0349    71 IVKVFHAAREDLEILYHLFGILPKplfdtqIAAALLG-------YGDSV-----------------GYAALVEELLGVEL 126

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1370514688 484 DKTQQLSNWDRRPLCEEQVIYAAADAYCLLEVHQALCRE 522
Cdd:COG0349   127 DKSEQRSDWLRRPLSEEQLEYAAADVRYLLPLYEKLLEE 165
DEDDy_polA_RNaseD_like_exo cd09018
DEDDy 3'-5' exonuclease domain of family-A DNA polymerases, RNase D, WRN, and similar proteins; ...
 347-519 2.36e-13

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: 68.42  E-value: 2.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 347 VVGVDVEWTPVFVAggRPRPSLLQVAV-EGHVFLLDVLALSQPPTGqgaqafsrlVAQLLSDPSITKLGYGMVGDLQKLg 425
Cdd:cd09018     1 VFAFDTETDSLDNI--SANLVLIQLAIePGVAALIPVAHDYLALEL---------LKPLLEDEKALKVGQNLKYDRGIL- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 426 tscpalAHVEKQILG-GMDLLLVHRQQMRVAsvpapavdrarELRGLSLLVQQVLGTALDKTQQL--SNWDRRPLCEEQV 502
Cdd:cd09018    69 ------LNYFIELRGiAFDTMLEAYILNSVA-----------GRWDMDSLVERWLGHKLIKFESIagKLWFNQPLTEEQG 131

                         170
                  ....*....|....*..
gi 1370514688 503 IYAAADAYCLLEVHQAL 519
Cdd:cd09018   132 RYAAEDADVTLQIHLKL 148
Mut7-C pfam01927
Mut7-C RNAse domain; RNAse domain of the PIN fold with an inserted Zinc Ribbon at the C ...
 584-680 9.58e-13

Mut7-C RNAse domain; RNAse domain of the PIN fold with an inserted Zinc Ribbon at the C terminus.


Pssm-ID: 426515  Cd Length: 146  Bit Score: 66.51  E-value: 9.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 584 RVVCDNMLQGLARSLRCLGVDARmLGNGEDHRRAAEVARQEGRIILTSGQPFHKlRAQVgAGRCLSvdCSLKAQQQAKAV 663
Cdd:pfam01927   2 RFLLDAMLGKLARYLRMLGYDTL-YDNDYEDDELLRIAAKEGRILLTRDRGLLK-RREL-THGVYV--RSLDPEEQLREV 76

                          90
                  ....*....|....*..
gi 1370514688 664 LKHFNVRVTHADIFSRC 680
Cdd:pfam01927  77 IARLGLALSLKPEFSRC 93
Mut7-C COG1656
Uncharacterized conserved protein, contains PIN-related Mut7-C RNAse domain [General function ...
 584-847 1.14e-10

Uncharacterized conserved protein, contains PIN-related Mut7-C RNAse domain [General function prediction only];


Pssm-ID: 441262  Cd Length: 155  Bit Score: 60.65  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 584 RVVCDNMLQGLARSLRCLGVDARMLGNGEDhRRAAEVARQEGRIILTSGQPFHKlRAQVGAGRCLSvdcSLKAQQQAKAV 663
Cdd:COG1656     2 RFLLDVMLGKLARWLRMLGFDTLYANDIDD-DELLAIAREEGRILLTRDRGLLK-RAEVTRGVLLR---STDPEEQLAEV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 664 LKHFNVRVTHADIFSRCqtqsfeeraegwgmghpekPRlglstpsgpqaCNcdqylkvsrdmmkqlmwlsshqegprssg 743
Cdd:COG1656    77 LRRFGLDLELDRPFTRC-------------------LR-----------CN----------------------------- 97

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 744 deatqsqavqepgpapdaapegctydrpcrwlqmADLRAETPDMLADGtrlqlagVPVGVLRTPglRCFYCCTGCGKVFW 823
Cdd:COG1656    98 ----------------------------------GPLEPVDKEEVADR-------VPPYVRERY--DEFWRCPKCGKVYW 134

                         250       260
                  ....*....|....*....|....
gi 1370514688 824 DGSHLGRVathfRDMLESAPSPCE 847
Cdd:COG1656   135 RGSHWRRM----RERLERLLKRSA 154
rnd TIGR01388
ribonuclease D; This model describes ribonuclease D, a 3'-exonuclease shown to act on tRNA ...
 364-531 3.09e-10

ribonuclease D; This model describes ribonuclease D, a 3'-exonuclease shown to act on tRNA both in vitro and when overexpressed in vivo. Trusted members of this family are restricted to the Proteobacteria; Aquifex, Mycobacterial, and eukaryotic homologs are not full-length homologs. Ribonuclease D is not essential in E. coli and is deleterious when overexpressed. Its precise biological role is still unknown. [Transcription, RNA processing]


Pssm-ID: 130455 [Multi-domain]  Cd Length: 367  Bit Score: 62.86  E-value: 3.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 364 PRPSLLQVAVEGHVFLLDVLALsqpptgqgaQAFSRLVAqLLSDPSITKLGYGMVGDLQKLGTSCPALAH--VEKQILGg 441
Cdd:TIGR01388  35 PQLGLIQVADGEQLALIDPLVI---------IDWSPLKE-LLRDESVVKVLHAASEDLEVFLNLFGELPQplFDTQIAA- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514688 442 mdLLLVHRQQMrvasvpapavdrarelrGLSLLVQQVLGTALDKTQQLSNWDRRPLCEEQVIYAAADAYCLLEVHQALCR 521
Cdd:TIGR01388 104 --AFCGFGMSM-----------------GYAKLVQEVLGVELDKSESRTDWLARPLTDAQLEYAAADVTYLLPLYAKLME 164

                         170
                  ....*....|...
gi 1370514688 522 EPA---RFHLSED 531
Cdd:TIGR01388 165 RLEesgRLAWLEE 177
Rrp6p_like_exo cd06147
DEDDy 3'-5' exonuclease domain of yeast Rrp6p, human polymyositis/scleroderma autoantigen ...
 464-519 5.66e-06

DEDDy 3'-5' exonuclease domain of yeast Rrp6p, human polymyositis/scleroderma autoantigen 100kDa, and similar proteins; Yeast Rrp6p and its human homolog, the polymyositis/scleroderma autoantigen 100kDa (PM/Scl-100), are exosome-associated proteins involved in the degradation and processing of precursors to stable RNAs. Both proteins contain 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. The 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. PM/Scl-100, an autoantigen present in the nucleolar compartment of the cell, reacts with autoantibodies produced by about 50% of patients with polymyositis-scleroderma overlap syndrome.


Pssm-ID: 99850 [Multi-domain]  Cd Length: 192  Bit Score: 47.98  E-value: 5.66e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370514688 464 RARELRGLSL--LVQQVLGTALDKTQQLSNWDRRPLCEEQVIYAAADAYCLLEVHQAL 519
Cdd:cd06147   111 RVLNLPRHSLayLLQKYCNVDADKKYQLADWRIRPLPEEMIKYAREDTHYLLYIYDRL 168
PRK10829 PRK10829
ribonuclease D; Provisional
 470-522 1.35e-05

ribonuclease D; Provisional


Pssm-ID: 236771 [Multi-domain]  Cd Length: 373  Bit Score: 48.46  E-value: 1.35e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370514688 470 GLSLLVQQVLGTALDKTQQLSNWDRRPLCEEQVIYAAADAYCLLEVHQALCRE 522
Cdd:PRK10829  117 GFASMVEEYTGVTLDKSESRTDWLARPLSERQCEYAAADVFYLLPIAAKLMAE 169
 
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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