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Conserved domains on  [gi|686531951|gb|AIQ42650|]
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hypothetical protein R50912_23290 [Paenibacillus sp. FSL R5-0912]

Protein Classification

metallophosphoesterase( domain architecture ID 14302878)

metallophosphoesterase similar to Listeria monocytogenes Lmo2642 cyclic nucleotide phosphodiesterase, which may have roles in host-pathogen interactions by changing the cAMP concentration of host cells during L. monocytogenes infection

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
39-291 2.16e-27

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


:

Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 109.40  E-value: 2.16e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686531951  39 LSILTTTDTHYLSQSLRDLGPAFNQFLAagdgkqlgysnemmealgyDIGIRKPDAVIISGDLSNNGEEASHKDLAKHLK 118
Cdd:COG1409    1 FRFAHISDLHLGAPDGSDTAEVLAAALA-------------------DINAPRPDFVVVTGDLTDDGEPEEYAAAREILA 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686531951 119 TIeqetGTRVYVIPGNHDIQNPWARKFKgkrqydtdsvtpkqfrkiydslgydEALLEDEDSLSYLAAPSDDLWLLMLDT 198
Cdd:COG1409   62 RL----GVPVYVVPGNHDIRAAMAEAYR-------------------------EYFGDLPPGGLYYSFDYGGVRFIGLDS 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686531951 199 AQYKNNkilgnpqlEGKVSASTLKWIDTcgEMAAAHDAQIVAVMHHSLLDHSDFIqEGFTVDDNGQVIEALLRNNIHTTL 278
Cdd:COG1409  113 NVPGRS--------SGELGPEQLAWLEE--ELAAAPAKPVIVFLHHPPYSTGSGS-DRIGLRNAEELLALLARYGVDLVL 181

                        250
                 ....*....|...
gi 686531951 279 SGHIHIQDISEYQ 291
Cdd:COG1409  182 SGHVHRYERTRRD 194
CNP_C_terminal super family cl40212
C-terminal domain of cyclic nucleotide phosphodiesterase; This is the C-temrinal domain found ...
 333-434 2.23e-21

C-terminal domain of cyclic nucleotide phosphodiesterase; This is the C-temrinal domain found in Listeria monocytogenes, Lmo2642 cyclic nucleotide phosphodiesterase. The auxiliary C-terminal domain, consists of five alpha-helices forming a long helical bundle, and is connected to the catalytic domain pfam00149 by two loop segments. It is suggested that this auxiliary domain of Lmo2642 might confer functional specificity to the protein through the interactions with unknown factors or involving the substrate recognition.


The actual alignment was detected with superfamily member pfam17839:

Pssm-ID: 465527  Cd Length: 108  Bit Score: 88.87  E-value: 2.23e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686531951  333 MELWAAASGSTDQNLLQFNTYSEANFRKRSATRSYSRLTADtayANYTDTELKAMADVVGRLNEIYFAGTASTDNAAVIN 412
Cdd:pfam17839   2 VEGWARETGQTDENLLNFKTYSKKFLQQITYNQAYDALKAD---AKLSDEQKEEMAKFYADLNIAYFAGTDYEIADEVKE 78

                          90       100
                  ....*....|....*....|...
gi 686531951  413 TEGYRLWQKA-PASGTRSYVLSM 434
Cdd:pfam17839  79 SPGYKLWQRYcYPSFLSDYLESI 101
 
Name Accession Description Interval E-value
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
39-291 2.16e-27

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 109.40  E-value: 2.16e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686531951  39 LSILTTTDTHYLSQSLRDLGPAFNQFLAagdgkqlgysnemmealgyDIGIRKPDAVIISGDLSNNGEEASHKDLAKHLK 118
Cdd:COG1409    1 FRFAHISDLHLGAPDGSDTAEVLAAALA-------------------DINAPRPDFVVVTGDLTDDGEPEEYAAAREILA 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686531951 119 TIeqetGTRVYVIPGNHDIQNPWARKFKgkrqydtdsvtpkqfrkiydslgydEALLEDEDSLSYLAAPSDDLWLLMLDT 198
Cdd:COG1409   62 RL----GVPVYVVPGNHDIRAAMAEAYR-------------------------EYFGDLPPGGLYYSFDYGGVRFIGLDS 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686531951 199 AQYKNNkilgnpqlEGKVSASTLKWIDTcgEMAAAHDAQIVAVMHHSLLDHSDFIqEGFTVDDNGQVIEALLRNNIHTTL 278
Cdd:COG1409  113 NVPGRS--------SGELGPEQLAWLEE--ELAAAPAKPVIVFLHHPPYSTGSGS-DRIGLRNAEELLALLARYGVDLVL 181

                        250
                 ....*....|...
gi 686531951 279 SGHIHIQDISEYQ 291
Cdd:COG1409  182 SGHVHRYERTRRD 194
CNP_C_terminal pfam17839
C-terminal domain of cyclic nucleotide phosphodiesterase; This is the C-temrinal domain found ...
 333-434 2.23e-21

C-terminal domain of cyclic nucleotide phosphodiesterase; This is the C-temrinal domain found in Listeria monocytogenes, Lmo2642 cyclic nucleotide phosphodiesterase. The auxiliary C-terminal domain, consists of five alpha-helices forming a long helical bundle, and is connected to the catalytic domain pfam00149 by two loop segments. It is suggested that this auxiliary domain of Lmo2642 might confer functional specificity to the protein through the interactions with unknown factors or involving the substrate recognition.


Pssm-ID: 465527  Cd Length: 108  Bit Score: 88.87  E-value: 2.23e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686531951  333 MELWAAASGSTDQNLLQFNTYSEANFRKRSATRSYSRLTADtayANYTDTELKAMADVVGRLNEIYFAGTASTDNAAVIN 412
Cdd:pfam17839   2 VEGWARETGQTDENLLNFKTYSKKFLQQITYNQAYDALKAD---AKLSDEQKEEMAKFYADLNIAYFAGTDYEIADEVKE 78

                          90       100
                  ....*....|....*....|...
gi 686531951  413 TEGYRLWQKA-PASGTRSYVLSM 434
Cdd:pfam17839  79 SPGYKLWQRYcYPSFLSDYLESI 101
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 92-288 3.32e-13

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: 68.84  E-value: 3.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686531951  92 PDAVIISGDLSNNGEEASHKDLAKHLKTIEQetgtRVYVIPGNHDIQNPWARKFKGKrqyDTDSVTPKQFrkIYDSLGYD 171
Cdd:cd07402   40 PDLVVVTGDLSDDGSPESYERLRELLAPLPA----PVYWIPGNHDDRAAMREALPEP---PYDDNGPVQY--VVDFGGWR 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686531951 172 eallededslsylaapsddlwLLMLDTaqyknnkiLGNPQLEGKVSASTLKWIDTcgEMAAAHDAQIVAVMHHSLLD--H 249
Cdd:cd07402  111 ---------------------LILLDT--------SVPGVHHGELSDEQLDWLEA--ALAEAPDRPTLIFLHHPPFPlgI 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 686531951 250 SDFIQEGFtvdDNGQVIEALL--RNNIHTTLSGHIHiQDIS 288
Cdd:cd07402  160 PWMDAIRL---RNSQALFAVLarHPQVKAILCGHIH-RPIS 196
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 39-174 2.26e-04

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: 40.66  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686531951   39 LSILTTTDTHYLSQsLRDLGPAFNQFLAAGdgkqlgysnemmealgydigirKPDAVIISGDLSNNG--EEASHKDLAKH 116
Cdd:pfam00149   1 MRILVIGDLHLPGQ-LDDLLELLKKLLEEG----------------------KPDLVLHAGDLVDRGppSEEVLELLERL 57

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 686531951  117 LKTIeqetgtRVYVIPGNHDIQNPWARKFKGKrqYDTDSVTPKQFRKIYDSLGYDEAL 174
Cdd:pfam00149  58 IKYV------PVYLVRGNHDFDYGECLRLYPY--LGLLARPWKRFLEVFNFLPLAGIL 107
 
Name Accession Description Interval E-value
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
39-291 2.16e-27

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 109.40  E-value: 2.16e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686531951  39 LSILTTTDTHYLSQSLRDLGPAFNQFLAagdgkqlgysnemmealgyDIGIRKPDAVIISGDLSNNGEEASHKDLAKHLK 118
Cdd:COG1409    1 FRFAHISDLHLGAPDGSDTAEVLAAALA-------------------DINAPRPDFVVVTGDLTDDGEPEEYAAAREILA 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686531951 119 TIeqetGTRVYVIPGNHDIQNPWARKFKgkrqydtdsvtpkqfrkiydslgydEALLEDEDSLSYLAAPSDDLWLLMLDT 198
Cdd:COG1409   62 RL----GVPVYVVPGNHDIRAAMAEAYR-------------------------EYFGDLPPGGLYYSFDYGGVRFIGLDS 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686531951 199 AQYKNNkilgnpqlEGKVSASTLKWIDTcgEMAAAHDAQIVAVMHHSLLDHSDFIqEGFTVDDNGQVIEALLRNNIHTTL 278
Cdd:COG1409  113 NVPGRS--------SGELGPEQLAWLEE--ELAAAPAKPVIVFLHHPPYSTGSGS-DRIGLRNAEELLALLARYGVDLVL 181

                        250
                 ....*....|...
gi 686531951 279 SGHIHIQDISEYQ 291
Cdd:COG1409  182 SGHVHRYERTRRD 194
CNP_C_terminal pfam17839
C-terminal domain of cyclic nucleotide phosphodiesterase; This is the C-temrinal domain found ...
 333-434 2.23e-21

C-terminal domain of cyclic nucleotide phosphodiesterase; This is the C-temrinal domain found in Listeria monocytogenes, Lmo2642 cyclic nucleotide phosphodiesterase. The auxiliary C-terminal domain, consists of five alpha-helices forming a long helical bundle, and is connected to the catalytic domain pfam00149 by two loop segments. It is suggested that this auxiliary domain of Lmo2642 might confer functional specificity to the protein through the interactions with unknown factors or involving the substrate recognition.


Pssm-ID: 465527  Cd Length: 108  Bit Score: 88.87  E-value: 2.23e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686531951  333 MELWAAASGSTDQNLLQFNTYSEANFRKRSATRSYSRLTADtayANYTDTELKAMADVVGRLNEIYFAGTASTDNAAVIN 412
Cdd:pfam17839   2 VEGWARETGQTDENLLNFKTYSKKFLQQITYNQAYDALKAD---AKLSDEQKEEMAKFYADLNIAYFAGTDYEIADEVKE 78

                          90       100
                  ....*....|....*....|...
gi 686531951  413 TEGYRLWQKA-PASGTRSYVLSM 434
Cdd:pfam17839  79 SPGYKLWQRYcYPSFLSDYLESI 101
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 92-288 3.32e-13

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: 68.84  E-value: 3.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686531951  92 PDAVIISGDLSNNGEEASHKDLAKHLKTIEQetgtRVYVIPGNHDIQNPWARKFKGKrqyDTDSVTPKQFrkIYDSLGYD 171
Cdd:cd07402   40 PDLVVVTGDLSDDGSPESYERLRELLAPLPA----PVYWIPGNHDDRAAMREALPEP---PYDDNGPVQY--VVDFGGWR 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686531951 172 eallededslsylaapsddlwLLMLDTaqyknnkiLGNPQLEGKVSASTLKWIDTcgEMAAAHDAQIVAVMHHSLLD--H 249
Cdd:cd07402  111 ---------------------LILLDT--------SVPGVHHGELSDEQLDWLEA--ALAEAPDRPTLIFLHHPPFPlgI 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 686531951 250 SDFIQEGFtvdDNGQVIEALL--RNNIHTTLSGHIHiQDIS 288
Cdd:cd07402  160 PWMDAIRL---RNSQALFAVLarHPQVKAILCGHIH-RPIS 196
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 86-137 2.16e-08

Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the 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: 277345 [Multi-domain]  Cd Length: 138  Bit Score: 52.68  E-value: 2.16e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 686531951  86 DIGIRKPDAVIISGDLSNNGEEASHKDLAKHLKTIEQEtgtRVYVIPGNHDI 137
Cdd:cd07400   25 EINALKPDLVVVTGDLTQRARPAEFEEAREFLDALEPE---PVVVVPGNHDA 73
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
64-136 4.62e-08

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 53.48  E-value: 4.62e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 686531951  64 FLAAGDgkqLGYSNEMMEALGYDIGIRKPDAVIISGDLSNNGEEASHKDLAKHLKTIeqetGTRVYVIPGNHD 136
Cdd:COG2129    2 ILAVSD---LHGNFDLLEKLLELARAEDADLVILAGDLTDFGTAEEAREVLEELAAL----GVPVLAVPGNHD 67
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 90-137 1.65e-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: 47.26  E-value: 1.65e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 686531951  90 RKPDAVIISGDLSNNGEEASHKDLAKhlkTIEQETGTRVYVIPGNHDI 137
Cdd:cd00838   25 EKPDLVICLGDLVDYGPDPEEVELKA---LRLLLAGIPVYVVPGNHDI 69
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 41-137 7.94e-06

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: 46.11  E-value: 7.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686531951  41 ILTTTDTH--YLSQSLRDLGPAFNQFLAagdgkqlgysnemmEALgyDIGI-RKPDAVIISGDL--SNNgeeASHKDLAK 115
Cdd:cd00840    2 FLHTADWHlgYPLYGLSRREEDFFKAFE--------------EIV--DLAIeEKVDFVLIAGDLfdSNN---PSPEALKL 62

                         90       100
                 ....*....|....*....|....
gi 686531951 116 HLKTIEQ--ETGTRVYVIPGNHDI 137
Cdd:cd00840   63 AIEGLRRlcEAGIPVFVIAGNHDS 86
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
90-136 1.93e-05

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 46.06  E-value: 1.93e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 686531951  90 RKPDAVIISGDL--SNNGEEASHKDLAKHLKTIeQETGTRVYVIPGNHD 136
Cdd:COG0420   38 EKVDAVLIAGDLfdSANPSPEAVRLLAEALRRL-SEAGIPVVLIAGNHD 85
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 39-174 2.26e-04

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: 40.66  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686531951   39 LSILTTTDTHYLSQsLRDLGPAFNQFLAAGdgkqlgysnemmealgydigirKPDAVIISGDLSNNG--EEASHKDLAKH 116
Cdd:pfam00149   1 MRILVIGDLHLPGQ-LDDLLELLKKLLEEG----------------------KPDLVLHAGDLVDRGppSEEVLELLERL 57

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 686531951  117 LKTIeqetgtRVYVIPGNHDIQNPWARKFKGKrqYDTDSVTPKQFRKIYDSLGYDEAL 174
Cdd:pfam00149  58 IKYV------PVYLVRGNHDFDYGECLRLYPY--LGLLARPWKRFLEVFNFLPLAGIL 107
MPP_Cdc1_like cd07384
Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also ...
 79-137 4.97e-04

Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also known as XlCdc1 in Xenopus laevis) is an endoplasmic reticulum-localized transmembrane lipid phosphatase with a metallophosphatase domain facing the ER lumen. In budding yeast, the gene encoding CDC1 is essential while nonlethal mutations cause defects in Golgi inheritance and actin polarization. Cdc1 mutant cells accumulate an unidentified phospholipid, suggesting that Cdc1 is a lipid phosphatase. Cdc1 mutant cells also have highly elevated intracellular calcium levels suggesting a possible role for Cdc1 in calcium regulation. The 5' flanking region of Cdc1 is a regulatory region with conserved binding site motifs for AP1, AP2, Sp1, NF-1 and CREB. DNA polymerase delta consists of at least four subunits - Pol3, Cdc1, Cdc27, and Cdm1. This group also contains Saccharomyces cerevisiae TED1 (Trafficking of Emp24p/Erv25p-dependent cargo disrupted 1), which acts together with Emp24p and Erv25p in cargo exit from the ER, and human MPPE1. The human MPPE1 gene is a candidate susceptibility gene for bipolar disorder. These proteins 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: 277330 [Multi-domain]  Cd Length: 172  Bit Score: 40.79  E-value: 4.97e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 686531951  79 MMEALGYDIGIRKPDAVIISGDLSNNG----EEASHKDLAKHLKTIEQETGTR-----VYVIPGNHDI 137
Cdd:cd07384   33 MRRAFDRVQQLLKPDVVLFLGDLFDGGrildSEEWKEYLHRFQKIFFLKSPGSlgsipVIFIPGNHDI 100
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 91-137 8.09e-04

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: 40.73  E-value: 8.09e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 686531951  91 KPDAVIISGDLSNnGEEASHKDLAKHLKTIEQETGtrVYVIPGNHDI 137
Cdd:cd07385   32 NPDLIVITGDLVD-GDVSVLRLLASPLSKLKAPLG--VYFVLGNHDY 75
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
91-136 3.70e-03

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 39.01  E-value: 3.70e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 686531951  91 KPDAVIISGDLSNnGEEASHKDLAKHLKTIEQETGtrVYVIPGNHD 136
Cdd:COG1408   73 KPDLVVLTGDLVD-GSVAELEALLELLKKLKAPLG--VYAVLGNHD 115
MPP_PF1019 cd07391
Pyrococcus furiosus PF1019 and related proteins, metallophosphatase domain; This family ...
 91-147 8.40e-03

Pyrococcus furiosus PF1019 and related proteins, metallophosphatase domain; This family includes bacterial and archeal proteins homologous to PF1019, an uncharacterized Pyrococcus furiosus protein. The domain present in members of this family 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: 277337  Cd Length: 175  Bit Score: 37.29  E-value: 8.40e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 686531951  91 KPDAVIISGDLSNNGEEASHKDLAKHLKTIEQETGTRVYVIPGNHDIQNPWARKFKG 147
Cdd:cd07391   41 GPDRLVILGDLKHSFGRVSRQERREVPFFRLLAKDVDVILIRGNHDGGLEEILSDVN 97
 
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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