NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1173275829|ref|WP_081134870|]
View 

MULTISPECIES: DNA repair exonuclease [Enterococcus]

Protein Classification

DNA repair exonuclease( domain architecture ID 12907598)

DNA repair exonuclease similar to DNA double-strand break repair protein Mre11, which is part of the Rad50/Mre11 complex that is involved in the early steps of DNA double-strand break (DSB) repair

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
2-245 1.34e-63

DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];


:

Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 204.38  E-value: 1.34e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275829   2 IQFIHAADLHMDRSFeglvNLDKRVQERLlianlNVLSNIVDEAIKHAVDFVLLAGDSFHQPRPSLKIQKHFVDQMERLN 81
Cdd:COG0420     1 MRFLHTADWHLGKPL----HGASRREDQL-----AALDRLVDLAIEEKVDAVLIAGDLFDSANPSPEAVRLLAEALRRLS 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275829  82 QSNIDVYMIFGNHDYYQQERYWFKFPD--NVHLFTSESVETKKLisKSKEEVAISGFSYLHQWIQQNKVVDF----PLRD 155
Cdd:COG0420    72 EAGIPVVLIAGNHDSPSRLSAGSPLLEnlGVHVFGSVEPEPVEL--EDGLGVAVYGLPYLRPSDEEALRDLLerlpRALD 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275829 156 SVDYHIGMYHGEI--GANEKGNY-APFHVSQMQDKGYDYWALGHIHVPMDLNEHGTINYPGAPQGHTQKETSARSILLVE 232
Cdd:COG0420   150 PGGPNILLLHGFVagASGSRDIYvAPVPLSALPAAGFDYVALGHIHRPQVLGGDPRIRYSGSPEPRSFSEAGGKGVLLVE 229

                         250
                  ....*....|....
gi 1173275829 233 LDQGRS-QIETLEV 245
Cdd:COG0420   230 LDAGGLvSVEFVPL 243
PRK10966 super family cl32618
exonuclease subunit SbcD; Provisional
 190-373 6.67e-05

exonuclease subunit SbcD; Provisional


The actual alignment was detected with superfamily member PRK10966:

Pssm-ID: 182871 [Multi-domain]  Cd Length: 407  Bit Score: 44.93  E-value: 6.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275829 190 DYWALGHIHVPMDLNEHGTINYPGAPQGHTQKET-SARSILLVELDQGR-SQIETLEVAeVYWEEKTISLKLAKTTQdil 267
Cdd:PRK10966  222 DYIALGHIHRAQKVGGTEHIRYSGSPIPLSFDELgKSKSVHLVEFDQGKlQSVTPLPVP-VFQPMAVLKGDLASITA--- 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275829 268 sifktQLET----TSTKLSLLDIKVVDYTHLsHEVIERIQSgelldyLTDKLsanliNIYVWRISIVNEELPNRVS---- 339
Cdd:PRK10966  298 -----QLEQwrdvSQEPPVWLDIEVTTDDYL-HDIQRRIQA------LTESL-----PVEVLLVRRSREQRERSLAseqr 360

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1173275829 340 -----LSVsEDLLEQ--LFETYHSP------EIFQQILNEMYSHSEA 373
Cdd:PRK10966  361 etlseLSV-EEVFERrlALEELDEPqqqrltQLFTQVLHELAEEHEA 406
 
Name Accession Description Interval E-value
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
2-245 1.34e-63

DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 204.38  E-value: 1.34e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275829   2 IQFIHAADLHMDRSFeglvNLDKRVQERLlianlNVLSNIVDEAIKHAVDFVLLAGDSFHQPRPSLKIQKHFVDQMERLN 81
Cdd:COG0420     1 MRFLHTADWHLGKPL----HGASRREDQL-----AALDRLVDLAIEEKVDAVLIAGDLFDSANPSPEAVRLLAEALRRLS 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275829  82 QSNIDVYMIFGNHDYYQQERYWFKFPD--NVHLFTSESVETKKLisKSKEEVAISGFSYLHQWIQQNKVVDF----PLRD 155
Cdd:COG0420    72 EAGIPVVLIAGNHDSPSRLSAGSPLLEnlGVHVFGSVEPEPVEL--EDGLGVAVYGLPYLRPSDEEALRDLLerlpRALD 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275829 156 SVDYHIGMYHGEI--GANEKGNY-APFHVSQMQDKGYDYWALGHIHVPMDLNEHGTINYPGAPQGHTQKETSARSILLVE 232
Cdd:COG0420   150 PGGPNILLLHGFVagASGSRDIYvAPVPLSALPAAGFDYVALGHIHRPQVLGGDPRIRYSGSPEPRSFSEAGGKGVLLVE 229

                         250
                  ....*....|....
gi 1173275829 233 LDQGRS-QIETLEV 245
Cdd:COG0420   230 LDAGGLvSVEFVPL 243
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 4-217 2.40e-47

Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia coli) is a subunit of the MRX protein complex. This complex includes: Mre11, Rad50, and Xrs2/Nbs1, and plays a vital role in several nuclear processes including DNA double-strand break repair, telomere length maintenance, cell cycle checkpoint control, and meiotic recombination, in eukaryotes. During double-strand break repair, the MRX complex is required to hold the two ends of a broken chromosome together. In vitro studies show that Mre11 has 3'-5' exonuclease activity on dsDNA templates and endonuclease activity on dsDNA and ssDNA templates. In addition to the N-terminal phosphatase domain, the eukaryotic MRE11 members of this family have a C-terminal DNA binding domain (not included in this alignment model). MRE11-like proteins are found in prokaryotes and archaea was well as in eukaryotes. Mre11 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277319 [Multi-domain]  Cd Length: 186  Bit Score: 160.13  E-value: 2.40e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275829   4 FIHAADLHMDRSFEGLVnldkrvqeRLLIANLNVLSNIVDEAIKHAVDFVLLAGDSFHQPRPSLKIQKHFVDQMERLNQS 83
Cdd:cd00840     2 FLHTADWHLGYPLYGLS--------RREEDFFKAFEEIVDLAIEEKVDFVLIAGDLFDSNNPSPEALKLAIEGLRRLCEA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275829  84 NIDVYMIFGNHDYYQQerywfkfpdnvhlftsesvetkkliskskeeVAISGFSYLHQW----IQQNKVVDFPLRDSVDY 159
Cdd:cd00840    74 GIPVFVIAGNHDSPAR-------------------------------VAIYGLPYLRDErlerLFEDLELRPRLLKPDWF 122

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275829 160 HIGMYHGEI-GANEKGNYAPFHVSQMQDKGYDYWALGHIHVPM-DLNEHGTINYPGAPQG 217
Cdd:cd00840   123 NILLLHQGVdGAGPSDSERPIVPEDLLPDGFDYVALGHIHKPQiIEGGGPPIVYPGSPEP 182
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 4-100 5.83e-05

Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 42.20  E-value: 5.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275829   4 FIHAADLHMDRSFEGLVNLDKRVQErllianlnvlsnivdeaiKHAVDFVLLAGDSFHQPRPSLKiqkhFVDQMERLNqS 83
Cdd:pfam00149   3 ILVIGDLHLPGQLDDLLELLKKLLE------------------EGKPDLVLHAGDLVDRGPPSEE----VLELLERLI-K 59

                          90
                  ....*....|....*..
gi 1173275829  84 NIDVYMIFGNHDYYQQE 100
Cdd:pfam00149  60 YVPVYLVRGNHDFDYGE 76
PRK10966 PRK10966
exonuclease subunit SbcD; Provisional
 190-373 6.67e-05

exonuclease subunit SbcD; Provisional


Pssm-ID: 182871 [Multi-domain]  Cd Length: 407  Bit Score: 44.93  E-value: 6.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275829 190 DYWALGHIHVPMDLNEHGTINYPGAPQGHTQKET-SARSILLVELDQGR-SQIETLEVAeVYWEEKTISLKLAKTTQdil 267
Cdd:PRK10966  222 DYIALGHIHRAQKVGGTEHIRYSGSPIPLSFDELgKSKSVHLVEFDQGKlQSVTPLPVP-VFQPMAVLKGDLASITA--- 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275829 268 sifktQLET----TSTKLSLLDIKVVDYTHLsHEVIERIQSgelldyLTDKLsanliNIYVWRISIVNEELPNRVS---- 339
Cdd:PRK10966  298 -----QLEQwrdvSQEPPVWLDIEVTTDDYL-HDIQRRIQA------LTESL-----PVEVLLVRRSREQRERSLAseqr 360

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1173275829 340 -----LSVsEDLLEQ--LFETYHSP------EIFQQILNEMYSHSEA 373
Cdd:PRK10966  361 etlseLSV-EEVFERrlALEELDEPqqqrltQLFTQVLHELAEEHEA 406
 
Name Accession Description Interval E-value
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
2-245 1.34e-63

DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 204.38  E-value: 1.34e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275829   2 IQFIHAADLHMDRSFeglvNLDKRVQERLlianlNVLSNIVDEAIKHAVDFVLLAGDSFHQPRPSLKIQKHFVDQMERLN 81
Cdd:COG0420     1 MRFLHTADWHLGKPL----HGASRREDQL-----AALDRLVDLAIEEKVDAVLIAGDLFDSANPSPEAVRLLAEALRRLS 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275829  82 QSNIDVYMIFGNHDYYQQERYWFKFPD--NVHLFTSESVETKKLisKSKEEVAISGFSYLHQWIQQNKVVDF----PLRD 155
Cdd:COG0420    72 EAGIPVVLIAGNHDSPSRLSAGSPLLEnlGVHVFGSVEPEPVEL--EDGLGVAVYGLPYLRPSDEEALRDLLerlpRALD 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275829 156 SVDYHIGMYHGEI--GANEKGNY-APFHVSQMQDKGYDYWALGHIHVPMDLNEHGTINYPGAPQGHTQKETSARSILLVE 232
Cdd:COG0420   150 PGGPNILLLHGFVagASGSRDIYvAPVPLSALPAAGFDYVALGHIHRPQVLGGDPRIRYSGSPEPRSFSEAGGKGVLLVE 229

                         250
                  ....*....|....
gi 1173275829 233 LDQGRS-QIETLEV 245
Cdd:COG0420   230 LDAGGLvSVEFVPL 243
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 4-217 2.40e-47

Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia coli) is a subunit of the MRX protein complex. This complex includes: Mre11, Rad50, and Xrs2/Nbs1, and plays a vital role in several nuclear processes including DNA double-strand break repair, telomere length maintenance, cell cycle checkpoint control, and meiotic recombination, in eukaryotes. During double-strand break repair, the MRX complex is required to hold the two ends of a broken chromosome together. In vitro studies show that Mre11 has 3'-5' exonuclease activity on dsDNA templates and endonuclease activity on dsDNA and ssDNA templates. In addition to the N-terminal phosphatase domain, the eukaryotic MRE11 members of this family have a C-terminal DNA binding domain (not included in this alignment model). MRE11-like proteins are found in prokaryotes and archaea was well as in eukaryotes. Mre11 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277319 [Multi-domain]  Cd Length: 186  Bit Score: 160.13  E-value: 2.40e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275829   4 FIHAADLHMDRSFEGLVnldkrvqeRLLIANLNVLSNIVDEAIKHAVDFVLLAGDSFHQPRPSLKIQKHFVDQMERLNQS 83
Cdd:cd00840     2 FLHTADWHLGYPLYGLS--------RREEDFFKAFEEIVDLAIEEKVDFVLIAGDLFDSNNPSPEALKLAIEGLRRLCEA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275829  84 NIDVYMIFGNHDYYQQerywfkfpdnvhlftsesvetkkliskskeeVAISGFSYLHQW----IQQNKVVDFPLRDSVDY 159
Cdd:cd00840    74 GIPVFVIAGNHDSPAR-------------------------------VAIYGLPYLRDErlerLFEDLELRPRLLKPDWF 122

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275829 160 HIGMYHGEI-GANEKGNYAPFHVSQMQDKGYDYWALGHIHVPM-DLNEHGTINYPGAPQG 217
Cdd:cd00840   123 NILLLHQGVdGAGPSDSERPIVPEDLLPDGFDYVALGHIHKPQiIEGGGPPIVYPGSPEP 182
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
6-198 2.87e-06

Predicted phosphohydrolase, MPP superfamily [General function prediction only];


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 48.25  E-value: 2.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275829   6 HAADLHMDRSFEGlvnldKRVQErllianlnvlsnIVDEAIKHAVDFVLLAGDSFHQPRPSLKiqkHFVDQMERLnQSNI 85
Cdd:COG1408    47 QLSDLHLGPFIGG-----ERLER------------LVEKINALKPDLVVLTGDLVDGSVAELE---ALLELLKKL-KAPL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275829  86 DVYMIFGNHDYYQQERYWFKFPD--NVHLFTSESVEtkklISKSKEEVAISGFSYLHqwiqQNKVVDFPL----RDSVDY 159
Cdd:COG1408   106 GVYAVLGNHDYYAGLEELRAALEeaGVRVLRNEAVT----LERGGDRLNLAGVDDPH----AGRFPDLEKalagVPPDAP 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1173275829 160 HIGMYHgeiganekgnyAPFHVSQMQDKGYDyWAL-GHIH 198
Cdd:COG1408   178 RILLAH-----------NPDVFDEAAAAGVD-LQLsGHTH 205
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
29-255 1.72e-05

Predicted phosphodiesterase, calcineurin family [General function prediction only];


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 44.91  E-value: 1.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275829  29 RLLI-----ANLNVLSNIVDEAIKHAVDFVLLAGDS-FHQPRPSlkiqkhFVdqMERLNQsnIDVYMIFGNHDYYQqERY 102
Cdd:COG0622     1 KIAVisdthGNLPALEAVLEDLEREGVDLIVHLGDLvGYGPDPP------EV--LDLLRE--LPIVAVRGNHDGAV-LRG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275829 103 WFKFPDnvhlftsesvetkklisksKEEVAISGFSylhqwiqqnkvvdfplrdsvdyhIGMYHGEIGANEKGNYAPFHVS 182
Cdd:COG0622    70 LRSLPE-------------------TLRLELEGVR-----------------------ILLVHGSPNEYLLPDTPAERLR 107

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1173275829 183 QM-QDKGYDYWALGHIHVPMDLNEHGT--INyPGAPqghTQKETS-ARSILLVELDQGRSQIETLEVAevYWEEKTI 255
Cdd:COG0622   108 ALaAEGDADVVVCGHTHIPFVRRVGGVllVN-PGSV---GQPRDGdPASYAILDIDDGEWSVEFVRVP--YDIEAAI 178
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 4-100 5.83e-05

Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 42.20  E-value: 5.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275829   4 FIHAADLHMDRSFEGLVNLDKRVQErllianlnvlsnivdeaiKHAVDFVLLAGDSFHQPRPSLKiqkhFVDQMERLNqS 83
Cdd:pfam00149   3 ILVIGDLHLPGQLDDLLELLKKLLE------------------EGKPDLVLHAGDLVDRGPPSEE----VLELLERLI-K 59

                          90
                  ....*....|....*..
gi 1173275829  84 NIDVYMIFGNHDYYQQE 100
Cdd:pfam00149  60 YVPVYLVRGNHDFDYGE 76
PRK10966 PRK10966
exonuclease subunit SbcD; Provisional
 190-373 6.67e-05

exonuclease subunit SbcD; Provisional


Pssm-ID: 182871 [Multi-domain]  Cd Length: 407  Bit Score: 44.93  E-value: 6.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275829 190 DYWALGHIHVPMDLNEHGTINYPGAPQGHTQKET-SARSILLVELDQGR-SQIETLEVAeVYWEEKTISLKLAKTTQdil 267
Cdd:PRK10966  222 DYIALGHIHRAQKVGGTEHIRYSGSPIPLSFDELgKSKSVHLVEFDQGKlQSVTPLPVP-VFQPMAVLKGDLASITA--- 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275829 268 sifktQLET----TSTKLSLLDIKVVDYTHLsHEVIERIQSgelldyLTDKLsanliNIYVWRISIVNEELPNRVS---- 339
Cdd:PRK10966  298 -----QLEQwrdvSQEPPVWLDIEVTTDDYL-HDIQRRIQA------LTESL-----PVEVLLVRRSREQRERSLAseqr 360

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1173275829 340 -----LSVsEDLLEQ--LFETYHSP------EIFQQILNEMYSHSEA 373
Cdd:PRK10966  361 etlseLSV-EEVFERrlALEELDEPqqqrltQLFTQVLHELAEEHEA 406
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
4-97 1.28e-04

3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 43.14  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275829   4 FIHAADLHMDRSfEGLVNLDkrvqerllianlnVLSNIVDEAIKHAVDFVLLAGDSFHQPRPSlkiqkHFVDQMERLNQS 83
Cdd:COG1409     3 FAHISDLHLGAP-DGSDTAE-------------VLAAALADINAPRPDFVVVTGDLTDDGEPE-----EYAAAREILARL 63

                          90
                  ....*....|....
gi 1173275829  84 NIDVYMIFGNHDYY 97
Cdd:COG1409    64 GVPVYVVPGNHDIR 77
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
34-102 6.22e-04

Predicted phosphoesterase, related to the Icc protein [General function prediction only];


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 40.77  E-value: 6.22e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1173275829  34 NLNVLSNIVDEAIKHAVDFVLLAGDsFHQPRPSLKIQKHFvdqmERLNQSNIDVYMIFGNHDYYQQERY 102
Cdd:COG2129    11 NFDLLEKLLELARAEDADLVILAGD-LTDFGTAEEAREVL----EELAALGVPVLAVPGNHDDPEVLDA 74
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 4-96 9.87e-04

Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ (glycerophosphodiesterase Q, also known as Rv0805 in Mycobacterium tuberculosis) is a binuclear metallophosphoesterase from Enterobacter aerogenes that catalyzes the hydrolysis of mono-, di-, and triester substrates, including some organophosphate pesticides and products of the degradation of nerve agents. The GpdQ homolog, Rv0805, has 2',3'-cyclic nucleotide phosphodiesterase activity. GpdQ and Rv0805 belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277347 [Multi-domain]  Cd Length: 240  Bit Score: 40.34  E-value: 9.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275829   4 FIHAADLHMDRSFEGLVN-LDKRVQERLLIANLNvlsnivdeAIKHAVDFVLLAGDSFHQPRP-SLkiqKHFVDQMERLn 81
Cdd:cd07402     1 IAQISDTHLFAPGEGALLgVDTAARLAAAVAQVN--------ALHPRPDLVVVTGDLSDDGSPeSY---ERLRELLAPL- 68

                          90
                  ....*....|....*
gi 1173275829  82 qsNIDVYMIFGNHDY 96
Cdd:cd07402    69 --PAPVYWIPGNHDD 81
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 4-105 1.06e-03

Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an uncharacterized Bacillus subtilis protein with a C-terminal metallophosphatase domain and an N-terminal twin-arginine (RR) motif. An RR-signal peptide derived from the Bacillus subtilis YkuE protein can direct Tat-dependent secretion of agarase in Streptomyces lividans. This is an indication that YkuE is transported by the Bacillus subtilis Tat (Twin-arginine translocation) pathway machinery. YkuE belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277331 [Multi-domain]  Cd Length: 224  Bit Score: 40.34  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275829   4 FIHAADLHMdrsfeGLVNLDKRVQErllianlnvlsnIVDEAIKHAVDFVLLAGDSFHQPRPSLKiqkHFVDQMERLNqS 83
Cdd:cd07385     4 IVQLSDIHL-----GPFVGRTRLQK------------VVRKVNELNPDLIVITGDLVDGDVSVLR---LLASPLSKLK-A 62

                          90       100
                  ....*....|....*....|..
gi 1173275829  84 NIDVYMIFGNHDYYQQERYWFK 105
Cdd:cd07385    63 PLGVYFVLGNHDYYSGDVEVWI 84
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 2-105 7.03e-03

Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; DCR2 phosphatase (Dosage-dependent Cell Cycle Regulator 2) functions together with DCR1 (Gid8) in a common pathway to accelerate initiation of DNA replication in Saccharomyces cerevisiae. Genetic analysis suggests that DCR1 functions upstream of DCR2. DCR2 interacts with and dephosphorylates Sic1, an inhibitor of mitotic cyclin/cyclin-dependent kinase complexes, which may serve to trigger the initiation of cell division. DCR2 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277329 [Multi-domain]  Cd Length: 202  Bit Score: 37.66  E-value: 7.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275829   2 IQFihaADLHMdrsfeGLVNLDKRVQERLLIANLNVLSNIVDEAikhAVDFVLLAGDSFHQPRPSLKIQKHFVDQM-ERL 80
Cdd:cd07383     6 LQF---ADLHF-----GEGEWTCWEGCEADLKTVEFIESVLDEE---KPDLVVLTGDLITGENTADDNATSYLDKAvSPL 74

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1173275829  81 NQSNIDVYMIFGNHDYY------QQEryWFK 105
Cdd:cd07383    75 VERGIPWAATFGNHDGYdwidpsQVE--WFE 103
 
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