|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10829 |
PRK10829 |
ribonuclease D; Provisional |
11-383 |
0e+00 |
|
ribonuclease D; Provisional
Pssm-ID: 236771 [Multi-domain] Cd Length: 373 Bit Score: 771.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 11 YNYQLITSDAQLQSICERAKKHATIALDTEFVRTRTYYPQLGLIQLFDGEQLSLIDPLDISEWQPFRELLTDRDVLKFIH 90
Cdd:PRK10829 1 MNYQMITTDDALASVCEAARAFPAIALDTEFVRTRTYYPQLGLIQLYDGEQLSLIDPLGITDWSPFKALLRDPQVTKFLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 91 AGSEDLEVFWNSFQCLPTPMIDTQVLAAFIGHPMSCGFATLVAQYLHVELDKSESRTDWLARPLSEKQCEYAAADVYYLL 170
Cdd:PRK10829 81 AGSEDLEVFLNAFGELPQPLIDTQILAAFCGRPLSCGFASMVEEYTGVTLDKSESRTDWLARPLSERQCEYAAADVFYLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 171 PLADILMAATEQAGYMGAAQDESYLIAQRRKEILMPECAYKDIGNAWQLRPKQLACLKKLAGWRLNQARERDLAINFVIR 250
Cdd:PRK10829 161 PIAAKLMAETEAAGWLPAALDECRLLCQRRQEVLAPEEAYRDITNAWQLRTRQLACLQLLADWRLRKARERDLAVNFVVR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 251 EENLWQVARYMPTSLGELDALGLSGQEIRCHGRRLLAMVAESRDIPDEACPALITNLIDYPGYRTAFKEIKSLVTQISES 330
Cdd:PRK10829 241 EEHLWQVARYMPGSLGELDSLGLSGSEIRFHGKTLLALVAKAQALPEEALPPPVLNLIDMPGYRKAFKAIKALIQEVSET 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 502753847 331 HQFSVELLASRRQINQLLSSHWKLKSPDYQPELLRGWRGELLAEPVAEILANY 383
Cdd:PRK10829 321 HGLSAELLASRRQINQLLNWHWKLKPQNGLPELISGWRGELLAEALTEILQEY 373
|
|
| Rnd |
COG0349 |
Ribonuclease D [Translation, ribosomal structure and biogenesis]; |
15-383 |
7.12e-166 |
|
Ribonuclease D [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440118 [Multi-domain] Cd Length: 365 Bit Score: 468.58 E-value: 7.12e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 15 LITSDAQLQSICERAKKHATIALDTEFVRTRTYYPQLGLIQLFDGEQLSLIDPLDISEWQPFRELLTDRDVLKFIHAGSE 94
Cdd:COG0349 1 LITTDEELAALCARLAQAPAVAVDTEFMRERTYYPRLCLIQLADGEEVALIDPLAIGDLSPLWELLADPAIVKVFHAARE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 95 DLEVFWNSFQCLPTPMIDTQVLAAFIGHPMSCGFATLVAQYLHVELDKSESRTDWLARPLSEKQCEYAAADVYYLLPLAD 174
Cdd:COG0349 81 DLEILYHLFGILPKPLFDTQIAAALLGYGDSVGYAALVEELLGVELDKSEQRSDWLRRPLSEEQLEYAAADVRYLLPLYE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 175 ILMAATEQAGYMGAAQDESYLIAQRRKEILMPECAYKDIGNAWQLRPKQLACLKKLAGWRLNQARERDLAINFVIREENL 254
Cdd:COG0349 161 KLLEELEREGRLEWAEEECARLLDPATYREDPEEAWLRLKGAWKLNPRQLAVLRELAAWREREARKRDVPRNRVLKDEAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 255 WQVARYMPTSLGELDAL-GLSGQEIRCHGRRLLAMVAESRDIPDEACPALITNLIDYPGYRTAFKEIKSLVTQISESHQF 333
Cdd:COG0349 241 LELARRQPKSLEELARLrGLSPGEIRRHGEELLAAVAEALALPEEELPEPPRRLPLSPGYKALLKLLKALLKEVAEELGV 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 502753847 334 SVELLASRRQINQLLSShwklkSPDYQPELLRGWRGELLAEPVAEILANY 383
Cdd:COG0349 321 APELLASRKDLEALARW-----GELADPPLLSGWRRELFGEELLALLEGE 365
|
|
| rnd |
TIGR01388 |
ribonuclease D; This model describes ribonuclease D, a 3'-exonuclease shown to act on tRNA ... |
15-374 |
8.00e-163 |
|
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: 460.78 E-value: 8.00e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 15 LITSDAQLQSICERAKKHATIALDTEFVRTRTYYPQLGLIQLFDGEQLSLIDPLDISEWQPFRELLTDRDVLKFIHAGSE 94
Cdd:TIGR01388 1 WITTDDELATVCEAVRTFPFVALDTEFVRERTFWPQLGLIQVADGEQLALIDPLVIIDWSPLKELLRDESVVKVLHAASE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 95 DLEVFWNSFQCLPTPMIDTQVLAAFIGHPMSCGFATLVAQYLHVELDKSESRTDWLARPLSEKQCEYAAADVYYLLPLAD 174
Cdd:TIGR01388 81 DLEVFLNLFGELPQPLFDTQIAAAFCGFGMSMGYAKLVQEVLGVELDKSESRTDWLARPLTDAQLEYAAADVTYLLPLYA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 175 ILMAATEQAGYMGAAQDESYLIAQRRKEILMPECAYKDIGNAWQLRPKQLACLKKLAGWRLNQARERDLAINFVIREENL 254
Cdd:TIGR01388 161 KLMERLEESGRLAWLEEECTLLTDRRTYVVNPEDAWRDIKNAWQLRPQQLAVLQALAAWREREARERDLPRNFVLKEEAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 255 WQVARYMPTSLGELDALGLSGQEIRCHGRRLLAMVAESRDIPDEACPALITNLIDYPGYRTAFKEIKSLVTQISESHQFS 334
Cdd:TIGR01388 241 WELARQAPGNLTELASLGPKGSEIRKHGDTLLALVKTALALPEDALPQAPLNLMPPPGYKALFKLLKVLVKDVSETLGLA 320
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 502753847 335 VELLASRRQINQLLSSHWKLKsPDYQPELLRGWRGELLAE 374
Cdd:TIGR01388 321 SELLASRRQLEQLLAWGWKLK-PNALPPLLQGWRRELGEE 359
|
|
| RNaseD_exo |
cd06142 |
DEDDy 3'-5' exonuclease domain of Ribonuclease D and similar proteins; Ribonuclease (RNase) D ... |
21-192 |
4.22e-73 |
|
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: 225.49 E-value: 4.22e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 21 QLQSICERAKKHATIALDTEFVRTRTYYPQLGLIQLFDGEQLSLIDPLDISEWQPFRELLTDRDVLKFIHAGSEDLEVFW 100
Cdd:cd06142 1 ELEDLCERLASAGVIAVDTEFMRLNTYYPRLCLIQISTGGEVYLIDPLAIGDLSPLKELLADPNIVKVFHAAREDLELLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 101 NSFQCLPTPMIDTQVLAAFIGHPMSCGFATLVAQYLHVELDKSESRTDWLARPLSEKQCEYAAADVYYLLPLADILMAAT 180
Cdd:cd06142 81 RDFGILPQNLFDTQIAARLLGLGDSVGLAALVEELLGVELDKGEQRSDWSKRPLTDEQLEYAALDVRYLLPLYEKLKEEL 160
|
170
....*....|..
gi 502753847 181 EQAGYMGAAQDE 192
Cdd:cd06142 161 EEEGRLEWAEEE 172
|
|
| DNA_pol_A_exo1 |
pfam01612 |
3'-5' exonuclease; This domain is responsible for the 3'-5' exonuclease proofreading activity ... |
13-177 |
3.19e-46 |
|
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: 155.92 E-value: 3.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 13 YQLITSDAQLQSICERAKKHATIALDTEF--VRTRTYYPQLGLIQLFDGEQLSLIDPLDISEW--QPFRELLTDRDVLKF 88
Cdd:pfam01612 1 YRIVTTEDELEDLIEELLNAPYVAVDTETtsLDTYSYYLRGALIQIGTGEGAYIIDPLALGDDvlSALKRLLEDPNITKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 89 IHAGSEDLEVFWNSFQCLPTPMIDTQVLAAFIGHPMSCGFATLVAQYLHVELDKSESRTDWLARPLSEKQCEYAAADVYY 168
Cdd:pfam01612 81 GHNAKFDLEVLARDFGIKLRNLFDTMLAAYLLGYDRSHSLADLAEKYLGVELDKEEQCSDWQARPLSEEQLRYAALDADY 160
|
....*....
gi 502753847 169 LLPLADILM 177
Cdd:pfam01612 161 LLRLYDKLR 169
|
|
| 35EXOc |
smart00474 |
3'-5' exonuclease; 3\' -5' exonuclease proofreading domain present in DNA polymerase I, Werner ... |
13-178 |
2.21e-32 |
|
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: 119.77 E-value: 2.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 13 YQLITSDAQLQSICERAKKHAT-IALDTEFVRTRTYYPQLGLIQL-FDGEQLSLIDPLDI-SEWQPFRELLTDRDVLKFI 89
Cdd:smart00474 1 VIVVTDSETLEELLEKLRAAGGeVALDTETTGLDSYSGKLVLIQIsVTGEGAFIIDPLALgDDLEILKDLLEDETITKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 90 HAGSEDLEVFwNSFQCLPTPMIDTQVLAA-FIGHPMSCGFATLVAQYLHVELDKSESRTDWLARPLSEKQCEYAAADVYY 168
Cdd:smart00474 81 HNAKFDLHVL-ARFGIELENIFDTMLAAYlLLGGPSKHGLATLLLGYLGVELDKEEQKSDWGARPLSEEQLEYAAEDADA 159
|
170
....*....|
gi 502753847 169 LLPLADILMA 178
Cdd:smart00474 160 LLRLYEKLEK 169
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10829 |
PRK10829 |
ribonuclease D; Provisional |
11-383 |
0e+00 |
|
ribonuclease D; Provisional
Pssm-ID: 236771 [Multi-domain] Cd Length: 373 Bit Score: 771.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 11 YNYQLITSDAQLQSICERAKKHATIALDTEFVRTRTYYPQLGLIQLFDGEQLSLIDPLDISEWQPFRELLTDRDVLKFIH 90
Cdd:PRK10829 1 MNYQMITTDDALASVCEAARAFPAIALDTEFVRTRTYYPQLGLIQLYDGEQLSLIDPLGITDWSPFKALLRDPQVTKFLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 91 AGSEDLEVFWNSFQCLPTPMIDTQVLAAFIGHPMSCGFATLVAQYLHVELDKSESRTDWLARPLSEKQCEYAAADVYYLL 170
Cdd:PRK10829 81 AGSEDLEVFLNAFGELPQPLIDTQILAAFCGRPLSCGFASMVEEYTGVTLDKSESRTDWLARPLSERQCEYAAADVFYLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 171 PLADILMAATEQAGYMGAAQDESYLIAQRRKEILMPECAYKDIGNAWQLRPKQLACLKKLAGWRLNQARERDLAINFVIR 250
Cdd:PRK10829 161 PIAAKLMAETEAAGWLPAALDECRLLCQRRQEVLAPEEAYRDITNAWQLRTRQLACLQLLADWRLRKARERDLAVNFVVR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 251 EENLWQVARYMPTSLGELDALGLSGQEIRCHGRRLLAMVAESRDIPDEACPALITNLIDYPGYRTAFKEIKSLVTQISES 330
Cdd:PRK10829 241 EEHLWQVARYMPGSLGELDSLGLSGSEIRFHGKTLLALVAKAQALPEEALPPPVLNLIDMPGYRKAFKAIKALIQEVSET 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 502753847 331 HQFSVELLASRRQINQLLSSHWKLKSPDYQPELLRGWRGELLAEPVAEILANY 383
Cdd:PRK10829 321 HGLSAELLASRRQINQLLNWHWKLKPQNGLPELISGWRGELLAEALTEILQEY 373
|
|
| Rnd |
COG0349 |
Ribonuclease D [Translation, ribosomal structure and biogenesis]; |
15-383 |
7.12e-166 |
|
Ribonuclease D [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440118 [Multi-domain] Cd Length: 365 Bit Score: 468.58 E-value: 7.12e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 15 LITSDAQLQSICERAKKHATIALDTEFVRTRTYYPQLGLIQLFDGEQLSLIDPLDISEWQPFRELLTDRDVLKFIHAGSE 94
Cdd:COG0349 1 LITTDEELAALCARLAQAPAVAVDTEFMRERTYYPRLCLIQLADGEEVALIDPLAIGDLSPLWELLADPAIVKVFHAARE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 95 DLEVFWNSFQCLPTPMIDTQVLAAFIGHPMSCGFATLVAQYLHVELDKSESRTDWLARPLSEKQCEYAAADVYYLLPLAD 174
Cdd:COG0349 81 DLEILYHLFGILPKPLFDTQIAAALLGYGDSVGYAALVEELLGVELDKSEQRSDWLRRPLSEEQLEYAAADVRYLLPLYE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 175 ILMAATEQAGYMGAAQDESYLIAQRRKEILMPECAYKDIGNAWQLRPKQLACLKKLAGWRLNQARERDLAINFVIREENL 254
Cdd:COG0349 161 KLLEELEREGRLEWAEEECARLLDPATYREDPEEAWLRLKGAWKLNPRQLAVLRELAAWREREARKRDVPRNRVLKDEAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 255 WQVARYMPTSLGELDAL-GLSGQEIRCHGRRLLAMVAESRDIPDEACPALITNLIDYPGYRTAFKEIKSLVTQISESHQF 333
Cdd:COG0349 241 LELARRQPKSLEELARLrGLSPGEIRRHGEELLAAVAEALALPEEELPEPPRRLPLSPGYKALLKLLKALLKEVAEELGV 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 502753847 334 SVELLASRRQINQLLSShwklkSPDYQPELLRGWRGELLAEPVAEILANY 383
Cdd:COG0349 321 APELLASRKDLEALARW-----GELADPPLLSGWRRELFGEELLALLEGE 365
|
|
| rnd |
TIGR01388 |
ribonuclease D; This model describes ribonuclease D, a 3'-exonuclease shown to act on tRNA ... |
15-374 |
8.00e-163 |
|
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: 460.78 E-value: 8.00e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 15 LITSDAQLQSICERAKKHATIALDTEFVRTRTYYPQLGLIQLFDGEQLSLIDPLDISEWQPFRELLTDRDVLKFIHAGSE 94
Cdd:TIGR01388 1 WITTDDELATVCEAVRTFPFVALDTEFVRERTFWPQLGLIQVADGEQLALIDPLVIIDWSPLKELLRDESVVKVLHAASE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 95 DLEVFWNSFQCLPTPMIDTQVLAAFIGHPMSCGFATLVAQYLHVELDKSESRTDWLARPLSEKQCEYAAADVYYLLPLAD 174
Cdd:TIGR01388 81 DLEVFLNLFGELPQPLFDTQIAAAFCGFGMSMGYAKLVQEVLGVELDKSESRTDWLARPLTDAQLEYAAADVTYLLPLYA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 175 ILMAATEQAGYMGAAQDESYLIAQRRKEILMPECAYKDIGNAWQLRPKQLACLKKLAGWRLNQARERDLAINFVIREENL 254
Cdd:TIGR01388 161 KLMERLEESGRLAWLEEECTLLTDRRTYVVNPEDAWRDIKNAWQLRPQQLAVLQALAAWREREARERDLPRNFVLKEEAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 255 WQVARYMPTSLGELDALGLSGQEIRCHGRRLLAMVAESRDIPDEACPALITNLIDYPGYRTAFKEIKSLVTQISESHQFS 334
Cdd:TIGR01388 241 WELARQAPGNLTELASLGPKGSEIRKHGDTLLALVKTALALPEDALPQAPLNLMPPPGYKALFKLLKVLVKDVSETLGLA 320
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 502753847 335 VELLASRRQINQLLSSHWKLKsPDYQPELLRGWRGELLAE 374
Cdd:TIGR01388 321 SELLASRRQLEQLLAWGWKLK-PNALPPLLQGWRRELGEE 359
|
|
| RNaseD_exo |
cd06142 |
DEDDy 3'-5' exonuclease domain of Ribonuclease D and similar proteins; Ribonuclease (RNase) D ... |
21-192 |
4.22e-73 |
|
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: 225.49 E-value: 4.22e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 21 QLQSICERAKKHATIALDTEFVRTRTYYPQLGLIQLFDGEQLSLIDPLDISEWQPFRELLTDRDVLKFIHAGSEDLEVFW 100
Cdd:cd06142 1 ELEDLCERLASAGVIAVDTEFMRLNTYYPRLCLIQISTGGEVYLIDPLAIGDLSPLKELLADPNIVKVFHAAREDLELLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 101 NSFQCLPTPMIDTQVLAAFIGHPMSCGFATLVAQYLHVELDKSESRTDWLARPLSEKQCEYAAADVYYLLPLADILMAAT 180
Cdd:cd06142 81 RDFGILPQNLFDTQIAARLLGLGDSVGLAALVEELLGVELDKGEQRSDWSKRPLTDEQLEYAALDVRYLLPLYEKLKEEL 160
|
170
....*....|..
gi 502753847 181 EQAGYMGAAQDE 192
Cdd:cd06142 161 EEEGRLEWAEEE 172
|
|
| RNaseD_like |
cd06129 |
DEDDy 3'-5' exonuclease domain of RNase D, WRN, and similar proteins; The RNase D-like group ... |
22-178 |
7.73e-52 |
|
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: 170.39 E-value: 7.73e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 22 LQSICER-AKKHATIALDTEFVRTRTYYPQLGLIQLF-DGEQLSLIDPLDISE-WQPFRELLTDRDVLKFIHAGSEDLEV 98
Cdd:cd06129 2 LSSLCEDlSMDGDVIAFDMEWPPGRRYYGEVALIQLCvSEEKCYLFDPLSLSVdWQGLKMLLENPSIVKALHGIEGDLWK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 99 FWNSFQCLPTPMIDTQVLAAFIGHPMSCGFATLVAQYLHVELDKSESRTDWLARPLSEKQCEYAAADVYYLLPLADILMA 178
Cdd:cd06129 82 LLRDFGEKLQRLFDTTIAANLKGLPERWSLASLVEHFLGKTLDKSISCADWSYRPLTEDQKLYAAADVYALLIIYTKLRN 161
|
|
| DNA_pol_A_exo1 |
pfam01612 |
3'-5' exonuclease; This domain is responsible for the 3'-5' exonuclease proofreading activity ... |
13-177 |
3.19e-46 |
|
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: 155.92 E-value: 3.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 13 YQLITSDAQLQSICERAKKHATIALDTEF--VRTRTYYPQLGLIQLFDGEQLSLIDPLDISEW--QPFRELLTDRDVLKF 88
Cdd:pfam01612 1 YRIVTTEDELEDLIEELLNAPYVAVDTETtsLDTYSYYLRGALIQIGTGEGAYIIDPLALGDDvlSALKRLLEDPNITKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 89 IHAGSEDLEVFWNSFQCLPTPMIDTQVLAAFIGHPMSCGFATLVAQYLHVELDKSESRTDWLARPLSEKQCEYAAADVYY 168
Cdd:pfam01612 81 GHNAKFDLEVLARDFGIKLRNLFDTMLAAYLLGYDRSHSLADLAEKYLGVELDKEEQCSDWQARPLSEEQLRYAALDADY 160
|
....*....
gi 502753847 169 LLPLADILM 177
Cdd:pfam01612 161 LLRLYDKLR 169
|
|
| DEDDy_polA_RNaseD_like_exo |
cd09018 |
DEDDy 3'-5' exonuclease domain of family-A DNA polymerases, RNase D, WRN, and similar proteins; ... |
35-177 |
4.99e-43 |
|
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: 147.00 E-value: 4.99e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 35 IALDTEFVRTRTYYPQLGLIQLFDGEQ-LSLIDPLDIS-EWQPFRELLTDRDVLKFIHAGSEDLEVFWNSFQCLPTPMID 112
Cdd:cd09018 2 FAFDTETDSLDNISANLVLIQLAIEPGvAALIPVAHDYlALELLKPLLEDEKALKVGQNLKYDRGILLNYFIELRGIAFD 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502753847 113 TQVLAAFIGHP-MSCGFATLVAQYLHVELDKSESRTD--WLARPLSEKQCEYAAADVYYLLPLADILM 177
Cdd:cd09018 82 TMLEAYILNSVaGRWDMDSLVERWLGHKLIKFESIAGklWFNQPLTEEQGRYAAEDADVTLQIHLKLW 149
|
|
| 35EXOc |
smart00474 |
3'-5' exonuclease; 3\' -5' exonuclease proofreading domain present in DNA polymerase I, Werner ... |
13-178 |
2.21e-32 |
|
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: 119.77 E-value: 2.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 13 YQLITSDAQLQSICERAKKHAT-IALDTEFVRTRTYYPQLGLIQL-FDGEQLSLIDPLDI-SEWQPFRELLTDRDVLKFI 89
Cdd:smart00474 1 VIVVTDSETLEELLEKLRAAGGeVALDTETTGLDSYSGKLVLIQIsVTGEGAFIIDPLALgDDLEILKDLLEDETITKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 90 HAGSEDLEVFwNSFQCLPTPMIDTQVLAA-FIGHPMSCGFATLVAQYLHVELDKSESRTDWLARPLSEKQCEYAAADVYY 168
Cdd:smart00474 81 HNAKFDLHVL-ARFGIELENIFDTMLAAYlLLGGPSKHGLATLLLGYLGVELDKEEQKSDWGARPLSEEQLEYAAEDADA 159
|
170
....*....|
gi 502753847 169 LLPLADILMA 178
Cdd:smart00474 160 LLRLYEKLEK 169
|
|
| WRN_exo |
cd06141 |
DEDDy 3'-5' exonuclease domain of WRN and similar proteins; WRN is a unique RecQ DNA helicase ... |
16-167 |
7.01e-15 |
|
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: 71.84 E-value: 7.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 16 ITSDAQLQSICERAKKHAT-IALDTEFV--RTRTYYPQLGLIQLFDGE-----QLSLIDPLDisewQPFRELLTDRDVLK 87
Cdd:cd06141 1 TDSAQDAEEAVKELLGKEKvVGFDTEWRpsFRKGKRNKVALLQLATESrcllfQLAHMDKLP----PSLKQLLEDPSILK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 88 FIHAGSEDLEVFWNSFQCLPTPMIDTQVLAAFIGHPMS-CGFATLVAQYLHVELDKSES--RTDWLARPLSEKQCEYAAA 164
Cdd:cd06141 77 VGVGIKGDARKLARDFGIEVRGVVDLSHLAKRVGPRRKlVSLARLVEEVLGLPLSKPKKvrCSNWEARPLSKEQILYAAT 156
|
...
gi 502753847 165 DVY 167
Cdd:cd06141 157 DAY 159
|
|
| mut-7_like_exo |
cd06146 |
DEDDy 3'-5' exonuclease domain of Caenorhabditis elegans mut-7 and similar proteins; The mut-7 ... |
35-176 |
1.15e-14 |
|
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: 71.94 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 35 IALDTEF--VRTRTYYPQLGLIQLFDGEQLSLIDPLDISE------WQPFRELLTDRDVLKFIHAGSEDLEVFWNSF--- 103
Cdd:cd06146 25 VGIDSEWkpSFLGDSDPRVAILQLATEDEVFLLDLLALENlesedwDRLLKRLFEDPDVLKLGFGFKQDLKALSASYpal 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 104 QCL---PTPMIDTQVLA-AFIGHPM----------SCGFATLVAQYLHVELDKSESRTDWLARPLSEKQCEYAAADVYYL 169
Cdd:cd06146 105 KCMferVQNVLDLQNLAkELQKSDMgrlkgnlpskTKGLADLVQEVLGKPLDKSEQCSNWERRPLREEQILYAALDAYCL 184
|
....*..
gi 502753847 170 LPLADIL 176
Cdd:cd06146 185 LEVFDKL 191
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
220-299 |
5.55e-14 |
|
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the HRDC domain cause human disease.
Pssm-ID: 128635 [Multi-domain] Cd Length: 81 Bit Score: 66.55 E-value: 5.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 220 RPKQLACLKKLAGWRLNQARERDLAINFVIREENLWQVARYMPTSLGELDALGLSGQEIRCH-GRRLLAMVAESRDIPDE 298
Cdd:smart00341 1 RERQLRLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRyGKDLLAVIQEASDSPSE 80
|
.
gi 502753847 299 A 299
Cdd:smart00341 81 A 81
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
223-289 |
1.11e-13 |
|
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic acid binding. Mutations in the HRDC domain cause human disease. It is interesting to note that the RecQ helicase in Deinococcus radiodurans has three tandem HRDC domains.
Pssm-ID: 425755 [Multi-domain] Cd Length: 68 Bit Score: 65.25 E-value: 1.11e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502753847 223 QLACLKKLAGWRLNQARERDLAINFVIREENLWQVARYMPTSLGELDAL-GLSGQEIRCHGRRLLAMV 289
Cdd:pfam00570 1 QLALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIpGVGPRKVERYGEEILAAI 68
|
|
| Rrp6p_like_exo |
cd06147 |
DEDDy 3'-5' exonuclease domain of yeast Rrp6p, human polymyositis/scleroderma autoantigen ... |
13-176 |
2.39e-13 |
|
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: 68.01 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 13 YQLITSDAQLQSICERAKKHATIALDTEFVRTRTYYPQLGLIQLFDGEQLSLIDPLDI-SEWQPFRELLTDRDVLKFIHA 91
Cdd:cd06147 5 LTFVDTEEKLEELVEKLKNCKEIAVDLEHHSYRSYLGFTCLMQISTREEDYIVDTLKLrDDMHILNEVFTDPNILKVFHG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 92 GSEDLEVFWNSFQCLPTPMIDTQVLAAFIGHPmSCGFATLVAQYLHVELDKSESRTDWLARPLSEKQCEYAAADVYYLLP 171
Cdd:cd06147 85 ADSDIIWLQRDFGLYVVNLFDTGQAARVLNLP-RHSLAYLLQKYCNVDADKKYQLADWRIRPLPEEMIKYAREDTHYLLY 163
|
....*
gi 502753847 172 LADIL 176
Cdd:cd06147 164 IYDRL 168
|
|
| DnaQ_like_exo |
cd06125 |
DnaQ-like (or DEDD) 3'-5' exonuclease domain superfamily; The DnaQ-like exonuclease ... |
35-118 |
1.26e-08 |
|
DnaQ-like (or DEDD) 3'-5' exonuclease domain superfamily; The DnaQ-like exonuclease superfamily is a structurally conserved group of 3'-5' exonucleases, which catalyze the excision of nucleoside monophosphates at the DNA or RNA termini in the 3'-5' direction. It is also called the DEDD superfamily, after the four invariant acidic residues present in the catalytic site of its members. The superfamily consists of DNA- and RNA-processing enzymes such as the proofreading domains of DNA polymerases, other DNA exonucleases, RNase D, RNase T, Oligoribonuclease and RNA exonucleases (REX). The DnaQ-like exonuclease domain contains three conserved sequence motifs termed ExoI, ExoII and ExoIII, which are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. The conservation patterns of the three motifs may vary among different subfamilies. DnaQ-like exonucleases are classified as DEDDy or DEDDh exonucleases depending on the variation of motif III as YX(3)D or HX(4)D, respectively. The significance of the motif differences is still unclear. Almost all RNase families in this superfamily are present only in eukaryotes and bacteria, but not in archaea, suggesting a later origin, which in some cases are accompanied by horizontal gene transfer.
Pssm-ID: 176647 [Multi-domain] Cd Length: 96 Bit Score: 52.06 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 35 IALDTEFVRTRTYYPQLGLIQLFDG--EQLSLIDPLDISEWQPfrelltdrDVLKFIHAGSEDLEVFWNSFQ-------C 105
Cdd:cd06125 1 IAIDTEATGLDGAVHEIIEIALADVnpEDTAVIDLKDILRDKP--------LAILVGHNGSFDLPFLNNRCAelglkypL 72
|
90
....*....|...
gi 502753847 106 LPTPMIDTQVLAA 118
Cdd:cd06125 73 LAGSWIDTIKLAA 85
|
|
| Egl_like_exo |
cd06148 |
DEDDy 3'-5' exonuclease domain of Drosophila Egalitarian (Egl) and similar proteins; The ... |
27-177 |
9.53e-08 |
|
DEDDy 3'-5' exonuclease domain of Drosophila Egalitarian (Egl) and similar proteins; The Egalitarian (Egl) protein subfamily is composed of Drosophila Egl and similar proteins. Egl is a component of an mRNA-binding complex which is required for oocyte specification. Egl 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. 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. The conservation of this subfamily throughout eukaryotes suggests that its members may be part of ancient RNA processing complexes that are likely to participate in the regulated processing of specific mRNAs. Some members of this subfamily do not have a completely conserved YX(3)D pattern at the ExoIII motif.
Pssm-ID: 99851 Cd Length: 197 Bit Score: 51.90 E-value: 9.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 27 ERAKKHATIALDTEFVRTRTYyPQLGLIQL-FDGEQLSLIDPL---DISEWQPFRELLTDRDVLKFIHAGSEDLEVFWNS 102
Cdd:cd06148 5 IHLKKQKVIGLDCEGVNLGRK-GKLCLVQIaTRTGQIYLFDILklgSIVFINGLKDILESKKILKVIHDCRRDSDALYHQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 103 FQCLPTPMIDTQVLAAFIGH-------PM-SCGFATLVAQYL-----HVELDKSESRTD---WLARPLSEKQCEYAAADV 166
Cdd:cd06148 84 YGIKLNNVFDTQVADALLQEqetggfnPDrVISLVQLLDKYLyisisLKEDVKKLMREDpkfWALRPLTEDMIRYAALDV 163
|
170
....*....|.
gi 502753847 167 YYLLPLADILM 177
Cdd:cd06148 164 LCLLPLYYAML 174
|
|
| PRK05755 |
PRK05755 |
DNA polymerase I; Provisional |
12-183 |
2.16e-07 |
|
DNA polymerase I; Provisional
Pssm-ID: 235591 [Multi-domain] Cd Length: 880 Bit Score: 52.79 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 12 NYQLITSDAQLQSICERAKKHATIALDTEfvrTRTYYPQ----LGLIQLFDGEQLSLIDPLDISEWQ--PFRELLTDRDV 85
Cdd:PRK05755 295 DYETILDEEELEAWLAKLKAAGLFAFDTE---TTSLDPMqaelVGLSFAVEPGEAAYIPLDQLDREVlaALKPLLEDPAI 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502753847 86 LKFIHAGSEDLEVFWNSFQCLPTPMIDTQvLAAFIGHP-MSCGFATLVAQYLHVELDKSESRT---DWLARPLSEKQCEY 161
Cdd:PRK05755 372 KKVGQNLKYDLHVLARYGIELRGIAFDTM-LASYLLDPgRRHGLDSLAERYLGHKTISFEEVAgkqLTFAQVDLEEAAEY 450
|
170 180
....*....|....*....|..
gi 502753847 162 AAADVYYLLPLADILMAATEQA 183
Cdd:PRK05755 451 AAEDADVTLRLHEVLKPKLLEE 472
|
|
| PRK14975 |
PRK14975 |
bifunctional 3'-5' exonuclease/DNA polymerase; Provisional |
111-172 |
4.17e-03 |
|
bifunctional 3'-5' exonuclease/DNA polymerase; Provisional
Pssm-ID: 237876 [Multi-domain] Cd Length: 553 Bit Score: 39.20 E-value: 4.17e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502753847 111 IDTQVLAAFIGH---PMSCGFATLVAQYLHVELDKSESRTDWLArPLSEKQCEYAAADVYYLLPL 172
Cdd:PRK14975 73 HDLMLASQLLLGsegRAGSSLSAAAARALGEGLDKPPQTSALSD-PPDEEQLLYAAADADVLLEL 136
|
|
| |
