NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|738887208|ref|WP_036774826|]
View 

ribonuclease T [Photorhabdus australis]

Protein Classification

ribonuclease T( domain architecture ID 10150094)

ribonuclease T is a 3'-5' exonuclease implicated in the 3' maturation of small stable RNAs and 23srRNA, and in the end turnover of tRNA

CATH:  3.30.420.10
EC:  3.1.13.-
Gene Ontology:  GO:0008033|GO:0016896|GO:0003676
PubMed:  11988770|11222749|8506149
SCOP:  4000547

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RNaseT cd06134
DEDDh 3'-5' exonuclease domain of RNase T; RNase T is a DEDDh-type DnaQ-like 3'-5' ...
 13-201 1.82e-130

DEDDh 3'-5' exonuclease domain of RNase T; RNase T is a DEDDh-type DnaQ-like 3'-5' exoribonuclease E implicated in the 3' maturation of small stable RNAs and 23srRNA, and in the end turnover of tRNA. It contains three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. RNase T is related to the proofreading domain of DNA polymerase III. Despite its important role, RNase T is mainly found only in gammaproteobacteria. It is speculated that it might have originated from DNA polymerase III at the time the gamma division of proteobacteria diverged from other bacteria. RNase T is a homodimer with the catalytic residues of one monomer contacting a large basic patch on the other monomer to form a functional active site.


:

Pssm-ID: 99837 [Multi-domain]  Cd Length: 189  Bit Score: 364.69  E-value: 1.82e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208  13 RFRGYYPVVIDVETGGFNAKTDALLEIAAITLKMDDDGWIAPDESLHFHIEPFEGANLEPAALEFTGIDPSNPLRGAVSE 92
Cdd:cd06134    1 RFRGFLPVVVDVETGGFNPQTDALLEIAAVTLEMDEQGNLYPDETFHFHILPFEGANLDPAALEFNGIDPFHPFRFAVDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208  93 YEALHAIFKMVRKGIKNSHCNRAIIVAHNANFDHGFVMAAAERTRLKRNPFHPFATFDTAALSGLVLGQTILAKACITAG 172
Cdd:cd06134   81 KEALKEIFKPIRKALKAQGCTRAILVGHNAHFDLGFLNAAVARCKIKRNPFHPFSTFDTATLAGLAYGQTVLAKACQAAG 160

                        170       180
                 ....*....|....*....|....*....
gi 738887208 173 VSFDNNQAHSALYDTNRTAELFCEMVNRW 201
Cdd:cd06134  161 IEFDNKEAHSALYDTQKTAELFCKIVNRW 189
 
Name Accession Description Interval E-value
RNaseT cd06134
DEDDh 3'-5' exonuclease domain of RNase T; RNase T is a DEDDh-type DnaQ-like 3'-5' ...
 13-201 1.82e-130

DEDDh 3'-5' exonuclease domain of RNase T; RNase T is a DEDDh-type DnaQ-like 3'-5' exoribonuclease E implicated in the 3' maturation of small stable RNAs and 23srRNA, and in the end turnover of tRNA. It contains three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. RNase T is related to the proofreading domain of DNA polymerase III. Despite its important role, RNase T is mainly found only in gammaproteobacteria. It is speculated that it might have originated from DNA polymerase III at the time the gamma division of proteobacteria diverged from other bacteria. RNase T is a homodimer with the catalytic residues of one monomer contacting a large basic patch on the other monomer to form a functional active site.


Pssm-ID: 99837 [Multi-domain]  Cd Length: 189  Bit Score: 364.69  E-value: 1.82e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208  13 RFRGYYPVVIDVETGGFNAKTDALLEIAAITLKMDDDGWIAPDESLHFHIEPFEGANLEPAALEFTGIDPSNPLRGAVSE 92
Cdd:cd06134    1 RFRGFLPVVVDVETGGFNPQTDALLEIAAVTLEMDEQGNLYPDETFHFHILPFEGANLDPAALEFNGIDPFHPFRFAVDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208  93 YEALHAIFKMVRKGIKNSHCNRAIIVAHNANFDHGFVMAAAERTRLKRNPFHPFATFDTAALSGLVLGQTILAKACITAG 172
Cdd:cd06134   81 KEALKEIFKPIRKALKAQGCTRAILVGHNAHFDLGFLNAAVARCKIKRNPFHPFSTFDTATLAGLAYGQTVLAKACQAAG 160

                        170       180
                 ....*....|....*....|....*....
gi 738887208 173 VSFDNNQAHSALYDTNRTAELFCEMVNRW 201
Cdd:cd06134  161 IEFDNKEAHSALYDTQKTAELFCKIVNRW 189
RNaseT TIGR01298
ribonuclease T; This model describes ribonuclease T, an enzyme found so far only in ...
 10-209 2.07e-127

ribonuclease T; This model describes ribonuclease T, an enzyme found so far only in gamma-subdivision Proteobacteria such as Escherichia coli and Xylella fastidiosa. Ribonuclease T is homologous to the DNA polymerase III alpha chain. It can liberate AMP from the common C-C-A terminus of uncharged tRNA. It appears also to be involved in RNA maturation. It also acts as a 3' to 5' single-strand DNA-specific exonuclease; it is distinctive for its ability to remove residues near a double-stranded stem. Ribonuclease T is a high copy suppressor in E. coli of a uv-repair defect caused by deletion of three other single-stranded DNA exonucleases. [Transcription, RNA processing]


Pssm-ID: 188129 [Multi-domain]  Cd Length: 200  Bit Score: 357.61  E-value: 2.07e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208   10 LSGRFRGYYPVVIDVETGGFNAKTDALLEIAAITLKMDDDGWIAPDESLHFHIEPFEGANLEPAALEFTGIDPSNPLRGA 89
Cdd:TIGR01298   1 LARRFRGYLPVVVDVETGGFNAATDALLEIAAITLKMDEQGFLFPDHTYHFHIEPFEGANIEPEALEFTGIDLDHPLRGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208   90 VSEYEALHAIFKMVRKGIKNSHCNRAIIVAHNANFDHGFVMAAAERTRLKRNPFHPFATFDTAALSGLVLGQTILAKACI 169
Cdd:TIGR01298  81 VQEEAALTEIFRGVRKAMKANGCQRAILVGHNASFDLGFLNAAVARTGIKRNPFHPFSSFDTATLAGLAYGQTVLAKACQ 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 738887208  170 TAGVSFDNNQAHSALYDTNRTAELFCEMVNRWKRLGGWPL 209
Cdd:TIGR01298 161 AAGMDFDNRQAHSALYDTEKTAELFCGIVNRWKELGGWPP 200
DnaQ COG0847
DNA polymerase III, epsilon subunit or related 3'-5' exonuclease [Replication, recombination ...
 20-199 3.59e-42

DNA polymerase III, epsilon subunit or related 3'-5' exonuclease [Replication, recombination and repair];


Pssm-ID: 440608 [Multi-domain]  Cd Length: 163  Bit Score: 139.93  E-value: 3.59e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208  20 VVIDVETGGFNAKTDALLEIAAITLkmdDDGWIApdESLHFHIEPFEgaNLEPAALEFTGIDPSNpLRGAVSEYEALHAI 99
Cdd:COG0847    3 VVLDTETTGLDPAKDRIIEIGAVKV---DDGRIV--ETFHTLVNPER--PIPPEATAIHGITDED-VADAPPFAEVLPEL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208 100 FKMVRKgiknshcnrAIIVAHNANFDHGFVMAAAERTRLKRNPFHpfaTFDTAALSGLV---LGQTILAKACITAGVSFD 176
Cdd:COG0847   75 LEFLGG---------AVLVAHNAAFDLGFLNAELRRAGLPLPPFP---VLDTLRLARRLlpgLPSYSLDALCERLGIPFD 142

                        170       180
                 ....*....|....*....|...
gi 738887208 177 NnqAHSALYDTNRTAELFCEMVN 199
Cdd:COG0847  143 E--RHRALADAEATAELFLALLR 163
RNase_T pfam00929
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T ...
 20-194 2.64e-31

Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T and the epsilon subunit of DNA polymerase III.;


Pssm-ID: 395743 [Multi-domain]  Cd Length: 164  Bit Score: 112.06  E-value: 2.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208   20 VVIDVETGGFNAKTDALLEIAAITLKMDDdgwIAPDESLHFHIEPFEGANLEPAALEFTGIDPSNpLRGAVSEYEALHAI 99
Cdd:pfam00929   1 VVIDLETTGLDPEKDEIIEIAAVVIDGGE---NEIGETFHTYVKPTRLPKLTDECTKFTGITQAM-LDNKPSFEEVLEEF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208  100 FKMVRKGiknshcnrAIIVAHNANFDHGFVMAAAER----TRLKRNPFHPFATFDTAALSGlvLGQTILAKACITAGVSF 175
Cdd:pfam00929  77 LEFLRKG--------NLLVAHNASFDVGFLRYDDKRflkkPMPKLNPVIDTLILDKATYKE--LPGRSLDALAEKLGLEH 146

                         170
                  ....*....|....*....
gi 738887208  176 DNNqAHSALYDTNRTAELF 194
Cdd:pfam00929 147 IGR-AHRALDDARATAKLF 164
EXOIII smart00479
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ...
 18-202 4.06e-29

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


Pssm-ID: 214685 [Multi-domain]  Cd Length: 169  Bit Score: 106.62  E-value: 4.06e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208    18 YPVVIDVETGGFNAKTDALLEIAAITLKMDDdgwiaPDESLHFHIEPFEgaNLEPAALEFTGIDPsNPLRGAVSEYEALH 97
Cdd:smart00479   1 TLVVIDCETTGLDPGKDEIIEIAAVDVDGGE-----IIEVFDTYVKPDR--PITDYATEIHGITP-EMLDDAPTFEEVLE 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208    98 AIFKMVRKGIknshcnraIIVAHNANFDHGFVMAAAERTRLKRNPFHPfaTFDTAALSGLVLGQTI---LAKACITAGVS 174
Cdd:smart00479  73 ELLEFLRGRI--------LVAGNSAHFDLRFLKLEHPRLGIKQPPKLP--VIDTLKLARATNPGLPkysLKKLAKRLLLE 142

                          170       180
                   ....*....|....*....|....*...
gi 738887208   175 FDNNqAHSALYDTNRTAELFCEMVNRWK 202
Cdd:smart00479 143 VIQR-AHRALDDARATAKLFKKLLERLE 169
polC PRK00448
DNA polymerase III PolC; Validated
 20-205 1.43e-18

DNA polymerase III PolC; Validated


Pssm-ID: 234767 [Multi-domain]  Cd Length: 1437  Bit Score: 83.73  E-value: 1.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208   20 VVIDVETGGFNAKTDALLEIAAItlKMDDDGWIapdESLHFHIEPfeGANLEPAALEFTGIDpSNPLRGAVSEYEALhai 99
Cdd:PRK00448  422 VVFDVETTGLSAVYDEIIEIGAV--KIKNGEII---DKFEFFIKP--GHPLSAFTTELTGIT-DDMVKDAPSIEEVL--- 490

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208  100 fKMVRKGIKNShcnraIIVAHNANFDHGFVmaaaeRTRLKRNPFHPFATF--DTaalsgLVLGQTI--------LAKACI 169
Cdd:PRK00448  491 -PKFKEFCGDS-----ILVAHNASFDVGFI-----NTNYEKLGLEKIKNPviDT-----LELSRFLypelkshrLNTLAK 554

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 738887208  170 TAGVSFDNNqaHSALYDTNRTAELFCEMVNRWKRLG 205
Cdd:PRK00448  555 KFGVELEHH--HRADYDAEATAYLLIKFLKDLKEKG 588
 
Name Accession Description Interval E-value
RNaseT cd06134
DEDDh 3'-5' exonuclease domain of RNase T; RNase T is a DEDDh-type DnaQ-like 3'-5' ...
 13-201 1.82e-130

DEDDh 3'-5' exonuclease domain of RNase T; RNase T is a DEDDh-type DnaQ-like 3'-5' exoribonuclease E implicated in the 3' maturation of small stable RNAs and 23srRNA, and in the end turnover of tRNA. It contains three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. RNase T is related to the proofreading domain of DNA polymerase III. Despite its important role, RNase T is mainly found only in gammaproteobacteria. It is speculated that it might have originated from DNA polymerase III at the time the gamma division of proteobacteria diverged from other bacteria. RNase T is a homodimer with the catalytic residues of one monomer contacting a large basic patch on the other monomer to form a functional active site.


Pssm-ID: 99837 [Multi-domain]  Cd Length: 189  Bit Score: 364.69  E-value: 1.82e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208  13 RFRGYYPVVIDVETGGFNAKTDALLEIAAITLKMDDDGWIAPDESLHFHIEPFEGANLEPAALEFTGIDPSNPLRGAVSE 92
Cdd:cd06134    1 RFRGFLPVVVDVETGGFNPQTDALLEIAAVTLEMDEQGNLYPDETFHFHILPFEGANLDPAALEFNGIDPFHPFRFAVDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208  93 YEALHAIFKMVRKGIKNSHCNRAIIVAHNANFDHGFVMAAAERTRLKRNPFHPFATFDTAALSGLVLGQTILAKACITAG 172
Cdd:cd06134   81 KEALKEIFKPIRKALKAQGCTRAILVGHNAHFDLGFLNAAVARCKIKRNPFHPFSTFDTATLAGLAYGQTVLAKACQAAG 160

                        170       180
                 ....*....|....*....|....*....
gi 738887208 173 VSFDNNQAHSALYDTNRTAELFCEMVNRW 201
Cdd:cd06134  161 IEFDNKEAHSALYDTQKTAELFCKIVNRW 189
RNaseT TIGR01298
ribonuclease T; This model describes ribonuclease T, an enzyme found so far only in ...
 10-209 2.07e-127

ribonuclease T; This model describes ribonuclease T, an enzyme found so far only in gamma-subdivision Proteobacteria such as Escherichia coli and Xylella fastidiosa. Ribonuclease T is homologous to the DNA polymerase III alpha chain. It can liberate AMP from the common C-C-A terminus of uncharged tRNA. It appears also to be involved in RNA maturation. It also acts as a 3' to 5' single-strand DNA-specific exonuclease; it is distinctive for its ability to remove residues near a double-stranded stem. Ribonuclease T is a high copy suppressor in E. coli of a uv-repair defect caused by deletion of three other single-stranded DNA exonucleases. [Transcription, RNA processing]


Pssm-ID: 188129 [Multi-domain]  Cd Length: 200  Bit Score: 357.61  E-value: 2.07e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208   10 LSGRFRGYYPVVIDVETGGFNAKTDALLEIAAITLKMDDDGWIAPDESLHFHIEPFEGANLEPAALEFTGIDPSNPLRGA 89
Cdd:TIGR01298   1 LARRFRGYLPVVVDVETGGFNAATDALLEIAAITLKMDEQGFLFPDHTYHFHIEPFEGANIEPEALEFTGIDLDHPLRGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208   90 VSEYEALHAIFKMVRKGIKNSHCNRAIIVAHNANFDHGFVMAAAERTRLKRNPFHPFATFDTAALSGLVLGQTILAKACI 169
Cdd:TIGR01298  81 VQEEAALTEIFRGVRKAMKANGCQRAILVGHNASFDLGFLNAAVARTGIKRNPFHPFSSFDTATLAGLAYGQTVLAKACQ 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 738887208  170 TAGVSFDNNQAHSALYDTNRTAELFCEMVNRWKRLGGWPL 209
Cdd:TIGR01298 161 AAGMDFDNRQAHSALYDTEKTAELFCGIVNRWKELGGWPP 200
DnaQ COG0847
DNA polymerase III, epsilon subunit or related 3'-5' exonuclease [Replication, recombination ...
 20-199 3.59e-42

DNA polymerase III, epsilon subunit or related 3'-5' exonuclease [Replication, recombination and repair];


Pssm-ID: 440608 [Multi-domain]  Cd Length: 163  Bit Score: 139.93  E-value: 3.59e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208  20 VVIDVETGGFNAKTDALLEIAAITLkmdDDGWIApdESLHFHIEPFEgaNLEPAALEFTGIDPSNpLRGAVSEYEALHAI 99
Cdd:COG0847    3 VVLDTETTGLDPAKDRIIEIGAVKV---DDGRIV--ETFHTLVNPER--PIPPEATAIHGITDED-VADAPPFAEVLPEL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208 100 FKMVRKgiknshcnrAIIVAHNANFDHGFVMAAAERTRLKRNPFHpfaTFDTAALSGLV---LGQTILAKACITAGVSFD 176
Cdd:COG0847   75 LEFLGG---------AVLVAHNAAFDLGFLNAELRRAGLPLPPFP---VLDTLRLARRLlpgLPSYSLDALCERLGIPFD 142

                        170       180
                 ....*....|....*....|...
gi 738887208 177 NnqAHSALYDTNRTAELFCEMVN 199
Cdd:COG0847  143 E--RHRALADAEATAELFLALLR 163
PolC COG2176
DNA polymerase III, alpha subunit (gram-positive type) [Replication, recombination and repair]; ...
 20-205 2.52e-32

DNA polymerase III, alpha subunit (gram-positive type) [Replication, recombination and repair];


Pssm-ID: 441779 [Multi-domain]  Cd Length: 181  Bit Score: 115.24  E-value: 2.52e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208  20 VVIDVETGGFNAKTDALLEIAAItlKMDDdGWIApdESLHFHIEPfeGANLEPAALEFTGIDPSnPLRGAVSEYEALHAI 99
Cdd:COG2176   11 VVFDLETTGLSPKKDEIIEIGAV--KVEN-GEIV--DRFSTLVNP--GRPIPPFITELTGITDE-MVADAPPFEEVLPEF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208 100 FKMVRKgiknshcnrAIIVAHNANFDHGFVMAAAERTRLK-RNPFhpfatFDTAALSGLVLGQTI---LAKACITAGVSF 175
Cdd:COG2176   83 LEFLGD---------AVLVAHNASFDLGFLNAALKRLGLPfDNPV-----LDTLELARRLLPELKsykLDTLAERLGIPL 148

                        170       180       190
                 ....*....|....*....|....*....|
gi 738887208 176 DNnqAHSALYDTNRTAELFCEMVNRWKRLG 205
Cdd:COG2176  149 ED--RHRALGDAEATAELFLKLLEKLEEKG 176
RNase_T pfam00929
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T ...
 20-194 2.64e-31

Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T and the epsilon subunit of DNA polymerase III.;


Pssm-ID: 395743 [Multi-domain]  Cd Length: 164  Bit Score: 112.06  E-value: 2.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208   20 VVIDVETGGFNAKTDALLEIAAITLKMDDdgwIAPDESLHFHIEPFEGANLEPAALEFTGIDPSNpLRGAVSEYEALHAI 99
Cdd:pfam00929   1 VVIDLETTGLDPEKDEIIEIAAVVIDGGE---NEIGETFHTYVKPTRLPKLTDECTKFTGITQAM-LDNKPSFEEVLEEF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208  100 FKMVRKGiknshcnrAIIVAHNANFDHGFVMAAAER----TRLKRNPFHPFATFDTAALSGlvLGQTILAKACITAGVSF 175
Cdd:pfam00929  77 LEFLRKG--------NLLVAHNASFDVGFLRYDDKRflkkPMPKLNPVIDTLILDKATYKE--LPGRSLDALAEKLGLEH 146

                         170
                  ....*....|....*....
gi 738887208  176 DNNqAHSALYDTNRTAELF 194
Cdd:pfam00929 147 IGR-AHRALDDARATAKLF 164
EXOIII smart00479
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ...
 18-202 4.06e-29

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


Pssm-ID: 214685 [Multi-domain]  Cd Length: 169  Bit Score: 106.62  E-value: 4.06e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208    18 YPVVIDVETGGFNAKTDALLEIAAITLKMDDdgwiaPDESLHFHIEPFEgaNLEPAALEFTGIDPsNPLRGAVSEYEALH 97
Cdd:smart00479   1 TLVVIDCETTGLDPGKDEIIEIAAVDVDGGE-----IIEVFDTYVKPDR--PITDYATEIHGITP-EMLDDAPTFEEVLE 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208    98 AIFKMVRKGIknshcnraIIVAHNANFDHGFVMAAAERTRLKRNPFHPfaTFDTAALSGLVLGQTI---LAKACITAGVS 174
Cdd:smart00479  73 ELLEFLRGRI--------LVAGNSAHFDLRFLKLEHPRLGIKQPPKLP--VIDTLKLARATNPGLPkysLKKLAKRLLLE 142

                          170       180
                   ....*....|....*....|....*...
gi 738887208   175 FDNNqAHSALYDTNRTAELFCEMVNRWK 202
Cdd:smart00479 143 VIQR-AHRALDDARATAKLFKKLLERLE 169
DEDDh cd06127
DEDDh 3'-5' exonuclease domain family; DEDDh exonucleases, part of the DnaQ-like (or DEDD) ...
 20-194 5.18e-24

DEDDh 3'-5' exonuclease domain family; DEDDh 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. These proteins contain four invariant acidic residues in three conserved sequence motifs termed ExoI, ExoII and ExoIII. DEDDh exonucleases are classified as such because of the presence of specific Hx(4)D conserved pattern at the ExoIII motif. The four conserved acidic residues are clustered around the active site and serve as ligands for the two metal ions required for catalysis. Most DEDDh exonucleases are the proofreading subunits (epsilon) or domains of bacterial DNA polymerase III, the main replicating enzyme in bacteria, which functions as the chromosomal replicase. Other members include other DNA and RNA exonucleases such as RNase T, Oligoribonuclease, and RNA exonuclease (REX), among others.


Pssm-ID: 176648 [Multi-domain]  Cd Length: 159  Bit Score: 93.13  E-value: 5.18e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208  20 VVIDVETGGFNAKTDALLEIAAItlKMDDDGWIApdESLHFHIEPfeGANLEPAALEFTGIDPSnPLRGAVSEYEALHAI 99
Cdd:cd06127    1 VVFDTETTGLDPKKDRIIEIGAV--KVDGGIEIV--ERFETLVNP--GRPIPPEATAIHGITDE-MLADAPPFEEVLPEF 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208 100 FKMvrkgiknshCNRAIIVAHNANFDHGFVMAAAERTRLkrnPFHPFATFDTAALSGLVLGQT--ILAKACITAGVSFDN 177
Cdd:cd06127   74 LEF---------LGGRVLVAHNASFDLRFLNRELRRLGG---PPLPNPWIDTLRLARRLLPGLrsHRLGLLLAERYGIPL 141

                        170
                 ....*....|....*..
gi 738887208 178 NQAHSALYDTNRTAELF 194
Cdd:cd06127  142 EGAHRALADALATAELL 158
polC PRK00448
DNA polymerase III PolC; Validated
 20-205 1.43e-18

DNA polymerase III PolC; Validated


Pssm-ID: 234767 [Multi-domain]  Cd Length: 1437  Bit Score: 83.73  E-value: 1.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208   20 VVIDVETGGFNAKTDALLEIAAItlKMDDDGWIapdESLHFHIEPfeGANLEPAALEFTGIDpSNPLRGAVSEYEALhai 99
Cdd:PRK00448  422 VVFDVETTGLSAVYDEIIEIGAV--KIKNGEII---DKFEFFIKP--GHPLSAFTTELTGIT-DDMVKDAPSIEEVL--- 490

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208  100 fKMVRKGIKNShcnraIIVAHNANFDHGFVmaaaeRTRLKRNPFHPFATF--DTaalsgLVLGQTI--------LAKACI 169
Cdd:PRK00448  491 -PKFKEFCGDS-----ILVAHNASFDVGFI-----NTNYEKLGLEKIKNPviDT-----LELSRFLypelkshrLNTLAK 554

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 738887208  170 TAGVSFDNNqaHSALYDTNRTAELFCEMVNRWKRLG 205
Cdd:PRK00448  555 KFGVELEHH--HRADYDAEATAYLLIKFLKDLKEKG 588
PRK08074 PRK08074
bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated
 20-211 1.21e-10

bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated


Pssm-ID: 236148 [Multi-domain]  Cd Length: 928  Bit Score: 60.35  E-value: 1.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208  20 VVIDVETGGfNA--KTDALLEIAAITLkmdDDGWIAPDESLHFH----IEPFeganLEpaalEFTGIDPSNplrgaVSEY 93
Cdd:PRK08074   6 VVVDLETTG-NSpkKGDKIIQIAAVVV---EDGEILERFSSFVNperpIPPF----IT----ELTGISEEM-----VKQA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208  94 EALHAIFKMVRKGIKNshcnrAIIVAHNANFDHGFVMAAaertrLKRNPFHPFA--TFDTAALSGLV--------LGQti 163
Cdd:PRK08074  69 PLFEDVAPEIVELLEG-----AYFVAHNVHFDLNFLNEE-----LERAGYTEIHcpKLDTVELARILlptaesykLRD-- 136

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 738887208 164 LAKAcitagVSFDNNQAHSALYDTNRTAELFCEMVNRWKRLggwPLTT 211
Cdd:PRK08074 137 LSEE-----LGLEHDQPHRADSDAEVTAELFLQLLNKLERL---PLVT 176
DNA_pol_III_epsilon_Ecoli_like cd06131
DEDDh 3'-5' exonuclease domain of the epsilon subunit of Escherichia coli DNA polymerase III ...
 20-197 3.79e-09

DEDDh 3'-5' exonuclease domain of the epsilon subunit of Escherichia coli DNA polymerase III and similar proteins; This subfamily is composed of the epsilon subunit of Escherichia coli DNA polymerase III (Pol III) and similar proteins. Pol III is the main DNA replicating enzyme in bacteria, functioning as the chromosomal replicase. It is a holoenzyme complex of ten different subunits, three of which (alpha, epsilon, and theta) compose the catalytic core. The Pol III epsilon subunit, encoded by the dnaQ gene, is a DEDDh-type 3'-5' exonuclease which is responsible for the proofreading activity of the polymerase, increasing the fidelity of DNA synthesis. It contains three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. The epsilon subunit of Pol III also functions as a stabilizer of the holoenzyme complex.


Pssm-ID: 99835 [Multi-domain]  Cd Length: 167  Bit Score: 53.69  E-value: 3.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208  20 VVIDVETGGFNAKT-DALLEIAAItlKMDDDgwIAPDESLHFHIEPfeGANLEPAALEFTGIDpsnplrgavSEYEALHA 98
Cdd:cd06131    2 IVLDTETTGLDPREgHRIIEIGCV--ELINR--RLTGNTFHVYINP--ERDIPEEAFKVHGIT---------DEFLADKP 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208  99 IFKMVRKGIKNsHCNRAIIVAHNANFDHGFVMAAAERTRLKRNPFHPFATFDTAALS-GLVLGQTI-LAKACITAGVSFD 176
Cdd:cd06131   67 KFAEIADEFLD-FIRGAELVIHNASFDVGFLNAELSLLGLGKKIIDFCRVIDTLALArKKFPGKPNsLDALCKRFGIDNS 145

                        170       180
                 ....*....|....*....|.
gi 738887208 177 NNQAHSALYDTNRTAELFCEM 197
Cdd:cd06131  146 HRTLHGALLDAELLAEVYLEL 166
PRK08517 PRK08517
3'-5' exonuclease;
20-194 4.33e-08

3'-5' exonuclease;


Pssm-ID: 236281 [Multi-domain]  Cd Length: 257  Bit Score: 51.95  E-value: 4.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208  20 VVIDVETGGFNAKTDALLEIAAITLKmddDGWIapdeslhfhIEPFEG----ANLEPAALEFTGIDPSNpLRGAVSeyea 95
Cdd:PRK08517  71 CFVDIETNGSKPKKHQIIEIGAVKVK---NGEI---------IDRFESfvkaKEVPEYITELTGITYED-LENAPS---- 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208  96 LHAIFKMVRKGIKNShcnraIIVAHNANFDHGFVMAAAERTRLKR--NPfhPFATFDtaalsglvlgqtiLAKACITA-- 171
Cdd:PRK08517 134 LKEVLEEFRLFLGDS-----VFVAHNVNFDYNFISRSLEEIGLGPllNR--KLCTID-------------LAKRTIESpr 193

                        170       180       190
                 ....*....|....*....|....*....|.
gi 738887208 172 -GVSF-------DNNQAHSALYDTNRTAELF 194
Cdd:PRK08517 194 yGLSFlkellgiEIEVHHRAYADALAAYEIF 224
dnaq TIGR00573
exonuclease, DNA polymerase III, epsilon subunit family; All proteins in this family for which ...
 20-197 7.42e-08

exonuclease, DNA polymerase III, epsilon subunit family; All proteins in this family for which functions are known are components of the DNA polymerase III complex (epsilon subunit). There is, however, an outgroup that includes paralogs in some gamma-proteobacteria and the n-terminal region of DinG from some low GC gram positive bacteria. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, Degradation of DNA]


Pssm-ID: 129663 [Multi-domain]  Cd Length: 217  Bit Score: 50.91  E-value: 7.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208   20 VVIDVETGGFNAKTDaLLEIAAITlKMDDDGWIApdeslHFHIEPFEGANLEPAALEFTGIDPSNpLRGAVSEYEalhaI 99
Cdd:TIGR00573  10 TTGDNETTGLYAGHD-IIEIGAVE-IINRRITGN-----KFHTYIKPDRPIDPDAIKIHGITDDM-LKDKPDFKE----I 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208  100 FKMVRKGIKNshcnrAIIVAHNANFDHGFVMAAAERTRLKRNPFHPFA-TFDTA--ALSGLVLGQTILAKACITAGVSFD 176
Cdd:TIGR00573  78 AEDFADYIRG-----AELVIHNASFDVGFLNYEFSKLYKVEPKTNDVIdTTDTLqyARPEFPGKRNTLDALCKRYEITNS 152

                         170       180
                  ....*....|....*....|.
gi 738887208  177 NNQAHSALYDTNRTAELFCEM 197
Cdd:TIGR00573 153 HRALHGALADAFILAKLYLVM 173
PRK07740 PRK07740
hypothetical protein; Provisional
 1-205 7.25e-07

hypothetical protein; Provisional


Pssm-ID: 236085 [Multi-domain]  Cd Length: 244  Bit Score: 48.51  E-value: 7.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208   1 MSDKKEPNVLSGRFRGYYPVVIDVETGGFN-AKTDALLEIAAITLKmdddGWIAPDESLHFHIEPfeGANLEPAALEFTG 79
Cdd:PRK07740  43 QKEAKRDDVLDIPLTDLPFVVFDLETTGFSpQQGDEILSIGAVKTK----GGEVETDTFYSLVKP--KRPIPEHILELTG 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208  80 I-----DPSNPLRgavseyEALHAIFKMVrkgiknshcNRAIIVAHNANFDHGFVMAAAERTrlKRNPF-HPFatFDTAA 153
Cdd:PRK07740 117 ItaedvAFAPPLA------EVLHRFYAFI---------GAGVLVAHHAGHDKAFLRHALWRT--YRQPFtHRL--IDTMF 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 738887208 154 LSGLVLGQTI---LAKACITAGVsfDNNQAHSALYDTNRTAELFCEMVNRWKRLG 205
Cdd:PRK07740 178 LTKLLAHERDfptLDDALAYYGI--PIPRRHHALGDALMTAKLWAILLVEAQQRG 230
PRK09182 PRK09182
DNA polymerase III subunit epsilon; Validated
 20-129 3.39e-06

DNA polymerase III subunit epsilon; Validated


Pssm-ID: 236397 [Multi-domain]  Cd Length: 294  Bit Score: 46.51  E-value: 3.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208  20 VVIDVETGGFNAKTDALLEIAAITLKMDDDGWI-APDESLHFHIEPFEGANLEPAALefTGIDPSNpLRGAVSEYEALHA 98
Cdd:PRK09182  40 VILDTETTGLDPRKDEIIEIGMVAFEYDDDGRIgDVLDTFGGLQQPSRPIPPEITRL--TGITDEM-VAGQTIDPAAVDA 116

                         90       100       110
                 ....*....|....*....|....*....|.
gi 738887208  99 IFKMVrkgiknshcnrAIIVAHNANFDHGFV 129
Cdd:PRK09182 117 LIAPA-----------DLIIAHNAGFDRPFL 136
PRK06195 PRK06195
DNA polymerase III subunit epsilon; Validated
 20-134 1.39e-04

DNA polymerase III subunit epsilon; Validated


Pssm-ID: 235735 [Multi-domain]  Cd Length: 309  Bit Score: 41.69  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208  20 VVIDVETGgfNAKTDALLEIAAITLKmddDGWIApdESLHFHIEPFEgANLEPAALEFTGIDPsnplrGAVSEYEALHAI 99
Cdd:PRK06195   4 VAIDFETA--NEKRNSPCSIGIVVVK---DGEIV--EKVHYLIKPKE-MRFMPINIGIHGIRP-----HMVEDELEFDKI 70

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 738887208 100 FKMVRkgiknSHCNRAIIVAHNANFDHGFVMAAAE 134
Cdd:PRK06195  71 WEKIK-----HYFNNNLVIAHNASFDISVLRKTLE 100
DnaQ_like_exo cd06125
DnaQ-like (or DEDD) 3'-5' exonuclease domain superfamily; The DnaQ-like exonuclease ...
 115-154 6.78e-04

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: 37.80  E-value: 6.78e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 738887208 115 AIIVAHNANFDHGFVMAAAERTRLKrNPFHPFATFDTAAL 154
Cdd:cd06125   45 AILVGHNGSFDLPFLNNRCAELGLK-YPLLAGSWIDTIKL 83
DNA_pol_III_epsilon_like cd06130
an uncharacterized bacterial subgroup of the DEDDh 3'-5' exonuclease domain family with ...
 20-196 1.15e-03

an uncharacterized bacterial subgroup of the DEDDh 3'-5' exonuclease domain family with similarity to the epsilon subunit of DNA polymerase III; This subfamily is composed of uncharacterized bacterial proteins with similarity to the epsilon subunit of DNA polymerase III (Pol III), a multisubunit polymerase which is the main DNA replicating enzyme in bacteria, functioning as the chromosomal replicase. The Pol III holoenzyme is a complex of ten different subunits, three of which (alpha, epsilon, and theta) compose the catalytic core. The Pol III epsilon subunit, encoded by the dnaQ gene, is a DEDDh-type 3'-5' exonuclease which is responsible for the proofreading activity of the polymerase, increasing the fidelity of DNA synthesis. It contains three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. The epsilon subunit of Pol III also functions as a stabilizer of the holoenzyme complex.


Pssm-ID: 99834 [Multi-domain]  Cd Length: 156  Bit Score: 38.26  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208  20 VVIDVETGgfNAKTDALLEIAAITLKmddDGWIApdESLHFHIEPFEgaNLEPAALEFTGIDPSNpLRGAVSEYEALHAI 99
Cdd:cd06130    2 VAIDFETA--NADRASACSIGLVKVR---DGQIV--DTFYTLIRPPT--RFDPFNIAIHGITPED-VADAPTFPEVWPEI 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208 100 FKMVrkgiknshcNRAIIVAHNANFDHGFVMAAAERTRLkrnPFHPFATFDTAALSGLV---LGQTILAKACITAGVSFD 176
Cdd:cd06130   72 KPFL---------GGSLVVAHNASFDRSVLRAALEAYGL---PPPPYQYLCTVRLARRVwplLPNHKLNTVAEHLGIELN 139

                        170       180
                 ....*....|....*....|
gi 738887208 177 NnqaHSALYDTNRTAELFCE 196
Cdd:cd06130  140 H---HDALEDARACAEILLA 156
PRK09145 PRK09145
3'-5' exonuclease;
20-98 1.31e-03

3'-5' exonuclease;


Pssm-ID: 236391 [Multi-domain]  Cd Length: 202  Bit Score: 38.34  E-value: 1.31e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738887208  20 VVIDVETGGFNAKTDALLEIAAITLKmddDGWIAPDESLHFHIEPfeGANLEPAALEFTGIDPSNpLRGAVSEYEALHA 98
Cdd:PRK09145  32 VALDCETTGLDPRRAEIVSIAAVKIR---GNRILTSERLELLVRP--PQSLSAESIKIHRLRHQD-LEDGLSEEEALRQ 104
ExoI_N cd06138
N-terminal DEDDh 3'-5' exonuclease domain of Escherichia coli exonuclease I and similar ...
 23-147 6.54e-03

N-terminal DEDDh 3'-5' exonuclease domain of Escherichia coli exonuclease I and similar proteins; This subfamily is composed of the N-terminal domain of Escherichia coli exonuclease I (ExoI) and similar proteins. ExoI is a monomeric enzyme that hydrolyzes single stranded DNA in the 3' to 5' direction. It plays a role in DNA recombination and repair. It primarily functions in repairing frameshift mutations. The N-terminal domain of ExoI is a DEDDh-type DnaQ-like 3'-5 exonuclease containing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. The ExoI structure is unique among DnaQ family enzymes in that there is a large distance between the two metal ions required for catalysis and the catalytic histidine is oriented away from the active site.


Pssm-ID: 99841 [Multi-domain]  Cd Length: 183  Bit Score: 36.09  E-value: 6.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738887208  23 DVETGGFNAKTDALLEIAAITLKMDddgwIAPDESLHFHIEPFEGANLEPAALEFTGIDPSNPLRGAVSEYEA---LHAI 99
Cdd:cd06138    4 DYETFGLNPSFDQILQFAAIRTDEN----FNEIEPFNIFCRLPPDVLPSPEALIVTGITPQQLLKEGLSEYEFiakIHRL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 738887208 100 FKmvRKGiknshcnrAIIVAHNA-NFDHGFVmaaaeRTRLKRNPFHPFA 147
Cdd:cd06138   80 FN--TPG--------TCIVGYNNiRFDDEFL-----RFAFYRNLYDPYT 113
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH