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Conserved domains on  [gi|42571261|ref|NP_973704|]
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purple acid phosphatase 14 [Arabidopsis thaliana]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 10164588)

metallophosphoesterase family protein may contain an active site consisting of two metal ions (usually manganese, iron, or zinc); similar to Kluyveromyces lactis protein SIA1 that may be involved in the activation of the plasma membrane proton-ATPase by glucose; may be inactive

CATH:  3.60.21.10
Gene Ontology:  GO:0046872
PubMed:  25837850|8003970
SCOP:  3001067

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 44-327 1.60e-62

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: 197.52  E-value: 1.60e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571261  44 GRFKILQVSDMHYGfgketqcSDVSPAEFPYCSDLNTTSFLQRTIASEKPDLIVFSGDNVYGL-CETSDVAKSMDMAFAP 122
Cdd:cd07383   1 GKFKILQFADLHFG-------EGEWTCWEGCEADLKTVEFIESVLDEEKPDLVVLTGDLITGEnTADDNATSYLDKAVSP 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571261 123 AIESGIPWVAILGNHDqesdmtretmmkyimklpnslsqvnppdawlyqidgfgnynlqiegpfgsplffksilnlylld 202
Cdd:cd07383  74 LVERGIPWAATFGNHD---------------------------------------------------------------- 89

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571261 203 ggsytkldgfgyKYDWVKTSQQNWYEHTSKwlEMEHKrwpfpQNSTAPGLVYLHIPMPEF-ALFNKSTEMTGVRQESTCS 281
Cdd:cd07383  90 ------------GYDWIDPSQVEWFESTSA--ALKKK-----YGKNIPSLAFFHIPLPEYrEVWNEKGKLGGINREKVCC 150

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 42571261 282 PPINSGFFTKLVERGEVKGVFSGHDHVNDFCA-ELHGINLCYAGGAG 327
Cdd:cd07383 151 QKTNSGFFKALVKRGDVKAVFCGHDHGNDFCGrWKNGIWLCYGRHTG 197
 
Name Accession Description Interval E-value
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 44-327 1.60e-62

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: 197.52  E-value: 1.60e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571261  44 GRFKILQVSDMHYGfgketqcSDVSPAEFPYCSDLNTTSFLQRTIASEKPDLIVFSGDNVYGL-CETSDVAKSMDMAFAP 122
Cdd:cd07383   1 GKFKILQFADLHFG-------EGEWTCWEGCEADLKTVEFIESVLDEEKPDLVVLTGDLITGEnTADDNATSYLDKAVSP 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571261 123 AIESGIPWVAILGNHDqesdmtretmmkyimklpnslsqvnppdawlyqidgfgnynlqiegpfgsplffksilnlylld 202
Cdd:cd07383  74 LVERGIPWAATFGNHD---------------------------------------------------------------- 89

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571261 203 ggsytkldgfgyKYDWVKTSQQNWYEHTSKwlEMEHKrwpfpQNSTAPGLVYLHIPMPEF-ALFNKSTEMTGVRQESTCS 281
Cdd:cd07383  90 ------------GYDWIDPSQVEWFESTSA--ALKKK-----YGKNIPSLAFFHIPLPEYrEVWNEKGKLGGINREKVCC 150

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 42571261 282 PPINSGFFTKLVERGEVKGVFSGHDHVNDFCA-ELHGINLCYAGGAG 327
Cdd:cd07383 151 QKTNSGFFKALVKRGDVKAVFCGHDHGNDFCGrWKNGIWLCYGRHTG 197
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
46-327 5.82e-16

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 75.88  E-value: 5.82e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571261  46 FKILQVSDMHYGFGKetqcsdvspaefpycsDLNTTSFLQRTIA---SEKPDLIVFSGDNVYglcetSDVAKSMDMAFAP 122
Cdd:COG1409   1 FRFAHISDLHLGAPD----------------GSDTAEVLAAALAdinAPRPDFVVVTGDLTD-----DGEPEEYAAAREI 59

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571261 123 AIESGIPWVAILGNHDQESDMTRETMmkyimklpnslsqvnppDAWLYQIDGFGNYNLQIEGpfgsplffksiLNLYLLD 202
Cdd:COG1409  60 LARLGVPVYVVPGNHDIRAAMAEAYR-----------------EYFGDLPPGGLYYSFDYGG-----------VRFIGLD 111

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571261 203 GGSYTKLDGfgykydWVKTSQQNWYEhtsKWLEmehkrwpfpQNSTAPGLVYLHIPMPEFALFNKSTEMTGVRQestcsp 282
Cdd:COG1409 112 SNVPGRSSG------ELGPEQLAWLE---EELA---------AAPAKPVIVFLHHPPYSTGSGSDRIGLRNAEE------ 167

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 42571261 283 pinsgfFTKLVERGEVKGVFSGHDHVNDFcAELHGINLCYAGGAG 327
Cdd:COG1409 168 ------LLALLARYGVDLVLSGHVHRYER-TRRDGVPYIVAGSTG 205
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 46-180 3.68e-07

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: 47.98  E-value: 3.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571261    46 FKILQVSDMHYGFGKETqcsdvspaefpycsdlnTTSFLQRTIASEKPDLIVFSGDNVYGLCETSDVAKSMDMAFApaie 125
Cdd:pfam00149   1 MRILVIGDLHLPGQLDD-----------------LLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEVLELLERLIK---- 59

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 42571261   126 sGIPWVAILGNHDqesDMTRETMMKYimklpnsLSQVNPPDAWLYQIDGFGNYNL 180
Cdd:pfam00149  60 -YVPVYLVRGNHD---FDYGECLRLY-------PYLGLLARPWKRFLEVFNFLPL 103
PRK11340 PRK11340
phosphodiesterase YaeI; Provisional
 1-138 7.45e-04

phosphodiesterase YaeI; Provisional


Pssm-ID: 236899  Cd Length: 271  Bit Score: 40.60  E-value: 7.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571261    1 MEETRRRFV--ISSVLSVSLIYLCLSTCHVSAFDFGRRQLRFNTD--GRFKILQVSDMHYgfgketqcSDVSPaeFPYCS 76
Cdd:PRK11340   1 MMISRRRLLqaAAATIATSSGFGYMHYWEPGWFELIRHRLAFFKDnaAPFKILFLADLHY--------SRFVP--LSLIS 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42571261   77 DLNTTSFLQrtiaseKPDLIVFSGDnvYGLCETSDVAKSMDMAFAPAIESGiPWVAILGNHD 138
Cdd:PRK11340  71 DAIALGIEQ------KPDLILLGGD--YVLFDMPLNFSAFSDVLSPLAECA-PTFACFGNHD 123
 
Name Accession Description Interval E-value
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 44-327 1.60e-62

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: 197.52  E-value: 1.60e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571261  44 GRFKILQVSDMHYGfgketqcSDVSPAEFPYCSDLNTTSFLQRTIASEKPDLIVFSGDNVYGL-CETSDVAKSMDMAFAP 122
Cdd:cd07383   1 GKFKILQFADLHFG-------EGEWTCWEGCEADLKTVEFIESVLDEEKPDLVVLTGDLITGEnTADDNATSYLDKAVSP 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571261 123 AIESGIPWVAILGNHDqesdmtretmmkyimklpnslsqvnppdawlyqidgfgnynlqiegpfgsplffksilnlylld 202
Cdd:cd07383  74 LVERGIPWAATFGNHD---------------------------------------------------------------- 89

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571261 203 ggsytkldgfgyKYDWVKTSQQNWYEHTSKwlEMEHKrwpfpQNSTAPGLVYLHIPMPEF-ALFNKSTEMTGVRQESTCS 281
Cdd:cd07383  90 ------------GYDWIDPSQVEWFESTSA--ALKKK-----YGKNIPSLAFFHIPLPEYrEVWNEKGKLGGINREKVCC 150

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 42571261 282 PPINSGFFTKLVERGEVKGVFSGHDHVNDFCA-ELHGINLCYAGGAG 327
Cdd:cd07383 151 QKTNSGFFKALVKRGDVKAVFCGHDHGNDFCGrWKNGIWLCYGRHTG 197
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
46-327 5.82e-16

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 75.88  E-value: 5.82e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571261  46 FKILQVSDMHYGFGKetqcsdvspaefpycsDLNTTSFLQRTIA---SEKPDLIVFSGDNVYglcetSDVAKSMDMAFAP 122
Cdd:COG1409   1 FRFAHISDLHLGAPD----------------GSDTAEVLAAALAdinAPRPDFVVVTGDLTD-----DGEPEEYAAAREI 59

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571261 123 AIESGIPWVAILGNHDQESDMTRETMmkyimklpnslsqvnppDAWLYQIDGFGNYNLQIEGpfgsplffksiLNLYLLD 202
Cdd:COG1409  60 LARLGVPVYVVPGNHDIRAAMAEAYR-----------------EYFGDLPPGGLYYSFDYGG-----------VRFIGLD 111

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571261 203 GGSYTKLDGfgykydWVKTSQQNWYEhtsKWLEmehkrwpfpQNSTAPGLVYLHIPMPEFALFNKSTEMTGVRQestcsp 282
Cdd:COG1409 112 SNVPGRSSG------ELGPEQLAWLE---EELA---------AAPAKPVIVFLHHPPYSTGSGSDRIGLRNAEE------ 167

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 42571261 283 pinsgfFTKLVERGEVKGVFSGHDHVNDFcAELHGINLCYAGGAG 327
Cdd:COG1409 168 ------LLALLARYGVDLVLSGHVHRYER-TRRDGVPYIVAGSTG 205
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 46-148 5.73e-09

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: 55.36  E-value: 5.73e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571261  46 FKILQVSDMHYG-FGKETQCSDVSpaefpycsdlnttsflqRTIASEKPDLIVFSGDNVyglCETSDVAKSMDMAFAPaI 124
Cdd:cd07385   2 LRIVQLSDIHLGpFVGRTRLQKVV-----------------RKVNELNPDLIVITGDLV---DGDVSVLRLLASPLSK-L 60

                        90       100
                ....*....|....*....|....
gi 42571261 125 ESGIPWVAILGNHDQESDMTRETM 148
Cdd:cd07385  61 KAPLGVYFVLGNHDYYSGDVEVWI 84
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
46-142 7.37e-09

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 55.57  E-value: 7.37e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571261  46 FKILQVSDMHYGfgketqcsdvspaefpycsDLNTTSFLQR---TIASEKPDLIVFSGDNVYGlcETSDVAKSMDmAFAP 122
Cdd:COG1408  43 LRIVQLSDLHLG-------------------PFIGGERLERlveKINALKPDLVVLTGDLVDG--SVAELEALLE-LLKK 100

                        90       100
                ....*....|....*....|
gi 42571261 123 aIESGIPWVAILGNHDQESD 142
Cdd:COG1408 101 -LKAPLGVYAVLGNHDYYAG 119
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 46-180 3.68e-07

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: 47.98  E-value: 3.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571261    46 FKILQVSDMHYGFGKETqcsdvspaefpycsdlnTTSFLQRTIASEKPDLIVFSGDNVYGLCETSDVAKSMDMAFApaie 125
Cdd:pfam00149   1 MRILVIGDLHLPGQLDD-----------------LLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEVLELLERLIK---- 59

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 42571261   126 sGIPWVAILGNHDqesDMTRETMMKYimklpnsLSQVNPPDAWLYQIDGFGNYNL 180
Cdd:pfam00149  60 -YVPVYLVRGNHD---FDYGECLRLY-------PYLGLLARPWKRFLEVFNFLPL 103
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 49-138 5.49e-06

metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also known as metallophosphoesterases, phosphodiesterases (PDEs), binuclear metallophosphoesterases, and dimetal-containing phosphoesterases (DMPs), represent a diverse superfamily of enzymes with a conserved domain containing 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. This superfamily includes: the phosphoprotein phosphatases (PPPs), 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: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 45.34  E-value: 5.49e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571261  49 LQVSDMHYGFgketqcsdvspaefpycsDLNTTSFLQRTIASEKPDLIVFSGDNVYGLCETSDVaksmDMAFAPAIESGI 128
Cdd:cd00838   1 LVISDIHGNL------------------EALEAVLEAALAKAEKPDLVICLGDLVDYGPDPEEV----ELKALRLLLAGI 58

                        90
                ....*....|
gi 42571261 129 PWVAILGNHD 138
Cdd:cd00838  59 PVYVVPGNHD 68
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
46-145 4.36e-05

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 44.13  E-value: 4.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571261  46 FKILQVSDMHYGFgkeTQCSDVSPAEFpycsdLNTTSFLQRTIASEKPDLIVFSGDnVYglcETSDV-AKSMDM---AFA 121
Cdd:COG0420   1 MRFLHTADWHLGK---PLHGASRREDQ-----LAALDRLVDLAIEEKVDAVLIAGD-LF---DSANPsPEAVRLlaeALR 68

                        90       100
                ....*....|....*....|....
gi 42571261 122 PAIESGIPWVAILGNHDQESDMTR 145
Cdd:COG0420  69 RLSEAGIPVVLIAGNHDSPSRLSA 92
PRK11340 PRK11340
phosphodiesterase YaeI; Provisional
 1-138 7.45e-04

phosphodiesterase YaeI; Provisional


Pssm-ID: 236899  Cd Length: 271  Bit Score: 40.60  E-value: 7.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571261    1 MEETRRRFV--ISSVLSVSLIYLCLSTCHVSAFDFGRRQLRFNTD--GRFKILQVSDMHYgfgketqcSDVSPaeFPYCS 76
Cdd:PRK11340   1 MMISRRRLLqaAAATIATSSGFGYMHYWEPGWFELIRHRLAFFKDnaAPFKILFLADLHY--------SRFVP--LSLIS 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42571261   77 DLNTTSFLQrtiaseKPDLIVFSGDnvYGLCETSDVAKSMDMAFAPAIESGiPWVAILGNHD 138
Cdd:PRK11340  71 DAIALGIEQ------KPDLILLGGD--YVLFDMPLNFSAFSDVLSPLAECA-PTFACFGNHD 123
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 47-138 5.38e-03

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: 37.25  E-value: 5.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571261  47 KILQVSDMHYGFGKETQcSDVSPAEFpycsdlnttSFLQRTIA---SEKPDLIVFSGD-----NVYglceTSDVAKSMDm 118
Cdd:cd00840   1 RFLHTADWHLGYPLYGL-SRREEDFF---------KAFEEIVDlaiEEKVDFVLIAGDlfdsnNPS----PEALKLAIE- 65

                        90       100
                ....*....|....*....|
gi 42571261 119 AFAPAIESGIPWVAILGNHD 138
Cdd:cd00840  66 GLRRLCEAGIPVFVIAGNHD 85
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
47-138 9.38e-03

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 36.92  E-value: 9.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571261  47 KILQVSDMHYGFGKETQcsdvspaefpycsdlnttsfLQRTIASEKPDLIVFSGDnvygLCETSDvAKSMDMAFAPAIES 126
Cdd:COG2129   1 KILAVSDLHGNFDLLEK--------------------LLELARAEDADLVILAGD----LTDFGT-AEEAREVLEELAAL 55

                        90
                ....*....|..
gi 42571261 127 GIPWVAILGNHD 138
Cdd:COG2129  56 GVPVLAVPGNHD 67
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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