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Conserved domains on  [gi|521288472|ref|WP_020452740|]
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MULTISPECIES: metallophosphoesterase [Bacillus]

Protein Classification

metallophosphoesterase( domain architecture ID 10003658)

metallophosphoesterase contains an active site consisting of two metal ions (usually manganese, iron, or zinc), similar to Bacillus subtilis YkuE, which is specifically targeted by the Tat pathway to the cell wall

CATH:  3.60.21.10
EC:  3.1.-.-
Gene Ontology:  GO:0046872|GO:0042578|GO:0016311
PubMed:  25837850|8003970

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
4-270 7.18e-72

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


:

Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 221.59  E-value: 7.18e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288472   4 IACLLIILGLMPIFYKANHNTKDVKVNTISVERVQAPALKKKLNILHLSDLHLENISISP--EQILELANKKRVDLIALT 81
Cdd:COG1408    1 LALALLALGLALLAYGLYIEPRRLRVRRYTVPIPKLPPAFDGLRIVQLSDLHLGPFIGGErlERLVEKINALKPDLVVLT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288472  82 GDFLDRKRNipKLANYLKALQKLKPAYGMYAVFGNHDYvlkGEHFRKLKRVLEDNGCITLRNQHVSIEVEGEALNIIGID 161
Cdd:COG1408   81 GDLVDGSVA--ELEALLELLKKLKAPLGVYAVLGNHDY---YAGLEELRAALEEAGVRVLRNEAVTLERGGDRLNLAGVD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288472 162 DYSTKR-SDIAASYKEL-KEGYNLVLTHDPNVVLDMQEFHFDYLLSGHFHGGQIHWPKPYHLLKMGKLVRmNMIKGLHYH 239
Cdd:COG1408  156 DPHAGRfPDLEKALAGVpPDAPRILLAHNPDVFDEAAAAGVDLQLSGHTHGGQIRLPGIGALLTPVRLGR-KYVAGLYRE 234

                        250       260       270
                 ....*....|....*....|....*....|.
gi 521288472 240 HDKPFYISEGLGQTGANIRIGSRPEMTFHHI 270
Cdd:COG1408  235 GGTQLYVSRGLGTSGPPVRFGCPPEITLITL 265
 
Name Accession Description Interval E-value
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
4-270 7.18e-72

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 221.59  E-value: 7.18e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288472   4 IACLLIILGLMPIFYKANHNTKDVKVNTISVERVQAPALKKKLNILHLSDLHLENISISP--EQILELANKKRVDLIALT 81
Cdd:COG1408    1 LALALLALGLALLAYGLYIEPRRLRVRRYTVPIPKLPPAFDGLRIVQLSDLHLGPFIGGErlERLVEKINALKPDLVVLT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288472  82 GDFLDRKRNipKLANYLKALQKLKPAYGMYAVFGNHDYvlkGEHFRKLKRVLEDNGCITLRNQHVSIEVEGEALNIIGID 161
Cdd:COG1408   81 GDLVDGSVA--ELEALLELLKKLKAPLGVYAVLGNHDY---YAGLEELRAALEEAGVRVLRNEAVTLERGGDRLNLAGVD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288472 162 DYSTKR-SDIAASYKEL-KEGYNLVLTHDPNVVLDMQEFHFDYLLSGHFHGGQIHWPKPYHLLKMGKLVRmNMIKGLHYH 239
Cdd:COG1408  156 DPHAGRfPDLEKALAGVpPDAPRILLAHNPDVFDEAAAAGVDLQLSGHTHGGQIRLPGIGALLTPVRLGR-KYVAGLYRE 234

                        250       260       270
                 ....*....|....*....|....*....|.
gi 521288472 240 HDKPFYISEGLGQTGANIRIGSRPEMTFHHI 270
Cdd:COG1408  235 GGTQLYVSRGLGTSGPPVRFGCPPEITLITL 265
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 46-266 1.97e-39

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: 136.64  E-value: 1.97e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288472  46 LNILHLSDLHL-ENISIS-PEQILELANKKRVDLIALTGDFLDRkrNIPKLANYLKALQKLKPAYGMYAVFGNHDYvlKG 123
Cdd:cd07385    2 LRIVQLSDIHLgPFVGRTrLQKVVRKVNELNPDLIVITGDLVDG--DVSVLRLLASPLSKLKAPLGVYFVLGNHDY--YS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288472 124 EHFRKLKRVLEDNGCITLRNQHVSIEVEGEALNIIGI--DDYSTKRSDIAASYKELKEG-YNLVLTHDPNVVLDMQEFHF 200
Cdd:cd07385   78 GDVEVWIAALEKAGITVLRNESVELSRDGATIGLAGSgvDDIGGHGEDLEKALKGLDENdPVILLAHNPDAAEEAQRPGV 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521288472 201 DYLLSGHFHGGQIHWPKPYHLLK-MGKLVRmnmikGLHYHHDKPF-YISEGLGQTGANIRIGSRPEMT 266
Cdd:cd07385  158 DLVLSGHTHGGQIFPPNYGVLSKlGFPYDS-----GLYQIGGTTYlYVSRGLGTWGPPIRLGCPPEIT 220
PRK11340 PRK11340
phosphodiesterase YaeI; Provisional
 46-266 4.85e-26

phosphodiesterase YaeI; Provisional


Pssm-ID: 236899  Cd Length: 271  Bit Score: 103.01  E-value: 4.85e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288472  46 LNILHLSDLHLENISISP--EQILELANKKRVDLIALTGDFL--DRKRNIPKLANYLKALQKLKPAYgmyAVFGNHDYVL 121
Cdd:PRK11340  50 FKILFLADLHYSRFVPLSliSDAIALGIEQKPDLILLGGDYVlfDMPLNFSAFSDVLSPLAECAPTF---ACFGNHDRPV 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288472 122 KGEHFRKLKRVLEDNGCITLRNQHVSIEVEGEALNIIGIDDYSTKRsdiAASYKELKEGY-NLVLTHDPNVVLDMQEFHF 200
Cdd:PRK11340 127 GTEKNHLIGETLKSAGITVLFNQATVIATPNRQFELVGTGDLWAGQ---CKPPPASEANLpRLVLAHNPDSKEVMRDEPW 203

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521288472 201 DYLLSGHFHGGQIHWP---KPYhLLKMGKlvrmNMIKGLHYHHDKPFYISEGLGQTGAnIRIGSRPEMT 266
Cdd:PRK11340 204 DLMLCGHTHGGQLRVPlvgEPF-APVEDK----RYVAGLNAFGERQIYTTRGVGSLYG-LRLNCRPEVT 266
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 46-123 6.11e-09

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: 52.60  E-value: 6.11e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521288472   46 LNILHLSDLHLENISISPEQILE-LANKKRVDLIALTGDFLDRKRNIPKLANYLKALQKLKPaygMYAVFGNHDYVLKG 123
Cdd:pfam00149   1 MRILVIGDLHLPGQLDDLLELLKkLLEEGKPDLVLHAGDLVDRGPPSEEVLELLERLIKYVP---VYLVRGNHDFDYGE 76
sbcd TIGR00619
exonuclease SbcD; All proteins in this family for which functions are known are ...
 46-133 1.50e-04

exonuclease SbcD; All proteins in this family for which functions are known are double-stranded DNA exonuclease (as part of a complex with SbcC homologs). This complex functions in the initiation of recombination and recombinational repair and is particularly important in regulating the stability of DNA sections that can form secondary structures. This family is likely homologous to the MRE11 family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273178 [Multi-domain]  Cd Length: 253  Bit Score: 42.02  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288472   46 LNILHLSDLHL----ENISISPEQI------LELANKKRVDLIALTGDFLDRKRNIPK----LANYLKALQKLKPAYgMY 111
Cdd:TIGR00619   1 MRILHTSDWHLgktlEGVSRLAEQKaflddlLEFAKAEQVDALLVAGDVFDTANPPAEaqelFNAFFVNLSDTGIRP-IV 79

                          90       100
                  ....*....|....*....|..
gi 521288472  112 AVFGNHDYVLKGEHFRKLKRVL 133
Cdd:TIGR00619  80 VISGNHDSAQRLSAAKKLLAEL 101
 
Name Accession Description Interval E-value
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
4-270 7.18e-72

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 221.59  E-value: 7.18e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288472   4 IACLLIILGLMPIFYKANHNTKDVKVNTISVERVQAPALKKKLNILHLSDLHLENISISP--EQILELANKKRVDLIALT 81
Cdd:COG1408    1 LALALLALGLALLAYGLYIEPRRLRVRRYTVPIPKLPPAFDGLRIVQLSDLHLGPFIGGErlERLVEKINALKPDLVVLT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288472  82 GDFLDRKRNipKLANYLKALQKLKPAYGMYAVFGNHDYvlkGEHFRKLKRVLEDNGCITLRNQHVSIEVEGEALNIIGID 161
Cdd:COG1408   81 GDLVDGSVA--ELEALLELLKKLKAPLGVYAVLGNHDY---YAGLEELRAALEEAGVRVLRNEAVTLERGGDRLNLAGVD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288472 162 DYSTKR-SDIAASYKEL-KEGYNLVLTHDPNVVLDMQEFHFDYLLSGHFHGGQIHWPKPYHLLKMGKLVRmNMIKGLHYH 239
Cdd:COG1408  156 DPHAGRfPDLEKALAGVpPDAPRILLAHNPDVFDEAAAAGVDLQLSGHTHGGQIRLPGIGALLTPVRLGR-KYVAGLYRE 234

                        250       260       270
                 ....*....|....*....|....*....|.
gi 521288472 240 HDKPFYISEGLGQTGANIRIGSRPEMTFHHI 270
Cdd:COG1408  235 GGTQLYVSRGLGTSGPPVRFGCPPEITLITL 265
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 46-266 1.97e-39

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: 136.64  E-value: 1.97e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288472  46 LNILHLSDLHL-ENISIS-PEQILELANKKRVDLIALTGDFLDRkrNIPKLANYLKALQKLKPAYGMYAVFGNHDYvlKG 123
Cdd:cd07385    2 LRIVQLSDIHLgPFVGRTrLQKVVRKVNELNPDLIVITGDLVDG--DVSVLRLLASPLSKLKAPLGVYFVLGNHDY--YS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288472 124 EHFRKLKRVLEDNGCITLRNQHVSIEVEGEALNIIGI--DDYSTKRSDIAASYKELKEG-YNLVLTHDPNVVLDMQEFHF 200
Cdd:cd07385   78 GDVEVWIAALEKAGITVLRNESVELSRDGATIGLAGSgvDDIGGHGEDLEKALKGLDENdPVILLAHNPDAAEEAQRPGV 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521288472 201 DYLLSGHFHGGQIHWPKPYHLLK-MGKLVRmnmikGLHYHHDKPF-YISEGLGQTGANIRIGSRPEMT 266
Cdd:cd07385  158 DLVLSGHTHGGQIFPPNYGVLSKlGFPYDS-----GLYQIGGTTYlYVSRGLGTWGPPIRLGCPPEIT 220
PRK11340 PRK11340
phosphodiesterase YaeI; Provisional
 46-266 4.85e-26

phosphodiesterase YaeI; Provisional


Pssm-ID: 236899  Cd Length: 271  Bit Score: 103.01  E-value: 4.85e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288472  46 LNILHLSDLHLENISISP--EQILELANKKRVDLIALTGDFL--DRKRNIPKLANYLKALQKLKPAYgmyAVFGNHDYVL 121
Cdd:PRK11340  50 FKILFLADLHYSRFVPLSliSDAIALGIEQKPDLILLGGDYVlfDMPLNFSAFSDVLSPLAECAPTF---ACFGNHDRPV 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288472 122 KGEHFRKLKRVLEDNGCITLRNQHVSIEVEGEALNIIGIDDYSTKRsdiAASYKELKEGY-NLVLTHDPNVVLDMQEFHF 200
Cdd:PRK11340 127 GTEKNHLIGETLKSAGITVLFNQATVIATPNRQFELVGTGDLWAGQ---CKPPPASEANLpRLVLAHNPDSKEVMRDEPW 203

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521288472 201 DYLLSGHFHGGQIHWP---KPYhLLKMGKlvrmNMIKGLHYHHDKPFYISEGLGQTGAnIRIGSRPEMT 266
Cdd:PRK11340 204 DLMLCGHTHGGQLRVPlvgEPF-APVEDK----RYVAGLNAFGERQIYTTRGVGSLYG-LRLNCRPEVT 266
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
48-222 1.92e-12

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 64.65  E-value: 1.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288472  48 ILHLSDLHLENISIspEQILELANKKRVDLIALTGDFLDrKRNIPKLANYLKALQKL-KPaygMYAVFGNHDYvlkgehf 126
Cdd:COG2129    2 ILAVSDLHGNFDLL--EKLLELARAEDADLVILAGDLTD-FGTAEEAREVLEELAALgVP---VLAVPGNHDD------- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288472 127 RKLKRVLEDNGCITLRNQHVsiEVEGeaLNIIGI---------DDYSTKRSDIAASYKELKEGYNLVL-THDP--NVVLD 194
Cdd:COG2129   69 PEVLDALEESGVHNLHGRVV--EIGG--LRIAGLggsrptpfgTPYEYTEEEIEERLAKLREKDVDILlTHAPpyGTTLD 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 521288472 195 ----------------MQEFHFDYLLSGHfhggqIHWPKPYHLL 222
Cdd:COG2129  145 rvedgphvgskalrelIEEFQPKLVLHGH-----IHESRGVDKI 183
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
48-219 1.45e-11

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 62.62  E-value: 1.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288472  48 ILHLSDLHLENISISP----------EQILELANKKRVDLIALTGDFLDRkRNIPK--LANYLKALQKLKPAYG-MYAVF 114
Cdd:COG0420    3 FLHTADWHLGKPLHGAsrredqlaalDRLVDLAIEEKVDAVLIAGDLFDS-ANPSPeaVRLLAEALRRLSEAGIpVVLIA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288472 115 GNHDYVLKGEHFRKLKRvledNGCITL----RNQHVSIEvEGEALNIIGIDDYSTKRSD-IAASYKELKE-----GYNLV 184
Cdd:COG0420   82 GNHDSPSRLSAGSPLLE----NLGVHVfgsvEPEPVELE-DGLGVAVYGLPYLRPSDEEaLRDLLERLPRaldpgGPNIL 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 521288472 185 LTH---------DPNVV--LDMQEFH---FDYLLSGHFHGGQIHWPKPY 219
Cdd:COG0420  157 LLHgfvagasgsRDIYVapVPLSALPaagFDYVALGHIHRPQVLGGDPR 205
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 46-123 6.11e-09

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: 52.60  E-value: 6.11e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521288472   46 LNILHLSDLHLENISISPEQILE-LANKKRVDLIALTGDFLDRKRNIPKLANYLKALQKLKPaygMYAVFGNHDYVLKG 123
Cdd:pfam00149   1 MRILVIGDLHLPGQLDDLLELLKkLLEEGKPDLVLHAGDLVDRGPPSEEVLELLERLIKYVP---VYLVRGNHDFDYGE 76
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
46-209 1.35e-08

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 53.93  E-value: 1.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288472  46 LNILHLSDLHLENISISP-----EQILELANKKRVDLIALTGDFLDRKRNiPKLANYLKALQKLKPAYgmYAVFGNHD-Y 119
Cdd:COG1409    1 FRFAHISDLHLGAPDGSDtaevlAAALADINAPRPDFVVVTGDLTDDGEP-EEYAAAREILARLGVPV--YVVPGNHDiR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288472 120 VLKGEHFRKLKRVLEDNGcitlrnQHVSIEVEGeaLNIIGIDDYSTKRSD----------IAASYKELKEGYNLVLTH-- 187
Cdd:COG1409   78 AAMAEAYREYFGDLPPGG------LYYSFDYGG--VRFIGLDSNVPGRSSgelgpeqlawLEEELAAAPAKPVIVFLHhp 149

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 521288472 188 --------DPNVVLDMQEF-------HFDYLLSGHFH 209
Cdd:COG1409  150 pystgsgsDRIGLRNAEELlallaryGVDLVLSGHVH 186
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 48-119 2.35e-07

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: 49.96  E-value: 2.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288472  48 ILHLSDLHL----------ENISISP-EQILELANKKRVDLIALTGDFLDRKRNIPK-LANYLKALQKLK-PAYGMYAVF 114
Cdd:cd00840    2 FLHTADWHLgyplyglsrrEEDFFKAfEEIVDLAIEEKVDFVLIAGDLFDSNNPSPEaLKLAIEGLRRLCeAGIPVFVIA 81


                 ....*
gi 521288472 115 GNHDY 119
Cdd:cd00840   82 GNHDS 86
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 48-121 4.63e-06

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: 45.36  E-value: 4.63e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521288472  48 ILHLSDLHL--ENISISPE-QILELANKKRVDLIALTGDFLDRKR--NIPKLANYLKALQKLKpaygMYAVFGNHDYVL 121
Cdd:cd07400    1 IAHISDLHFgeERKPEVLElNLLDEINALKPDLVVVTGDLTQRARpaEFEEAREFLDALEPEP----VVVVPGNHDAIV 75
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
51-119 8.60e-06

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 45.29  E-value: 8.60e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521288472  51 LSDLH--LENIsispEQILELANKKRVDLIALTGDFLDRKRNIPKLANYLKALqklkpayGMYAVFGNHDY 119
Cdd:COG0622    5 ISDTHgnLPAL----EAVLEDLEREGVDLIVHLGDLVGYGPDPPEVLDLLREL-------PIVAVRGNHDG 64
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 49-121 1.38e-05

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: 43.80  E-value: 1.38e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521288472  49 LHLSDLHLENISISPEQILELANKKRVDLIALTGDFLDRKRniPKLANYLKALQKLKPAYGMYAVFGNHDYVL 121
Cdd:cd00838    1 LVISDIHGNLEALEAVLEAALAKAEKPDLVICLGDLVDYGP--DPEEVELKALRLLLAGIPVYVVPGNHDILV 71
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 47-191 2.30e-05

Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the Calcineurin-like phosphoesterase superfamily.


Pssm-ID: 432832 [Multi-domain]  Cd Length: 150  Bit Score: 43.46  E-value: 2.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288472   47 NILHLSDLHlENISIsPEQILELAnKKRVDLIALTGDFLDrkrnipklANYLKALQKLKPaygMYAVFGNHDYVlkGEHF 126
Cdd:pfam12850   2 RIGIISDTH-DNLAL-PEAALERL-KGVVDLIIHAGDIVA--------PEVLEELLELAP---VLAVRGNNDAA--AEFA 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521288472  127 RKLKRVLEdngcitlrnqhvsIEVEGEALNIIGIDDYstkRSDIAASYKELKEGYNLVL---THDPNV 191
Cdd:pfam12850  66 TDLPEEAV-------------LELGGVKILLTHGHGV---KDALARLLRRAEEGVAVVVyghTHVPGV 117
MPP_MS158 cd07404
Microscilla MS158 and related proteins, metallophosphatase domain; MS158 is an uncharacterized ...
 48-149 1.20e-04

Microscilla MS158 and related proteins, metallophosphatase domain; MS158 is an uncharacterized Microscilla protein with a metallophosphatase domain. Microscilla proteins MS152, and MS153 are also included in this family. 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: 277349 [Multi-domain]  Cd Length: 201  Bit Score: 41.94  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288472  48 ILHLSDLHLENISiSPEQILELANKKRVDLIALTGDfLDRKRNIPKLANYLKALqkLKPAYGMYAVFGNHDYVLK----G 123
Cdd:cd07404    1 LQIASDLHLEVEQ-NLAKLKFFPKVPDADILILAGD-IGRLTDAEAWDNFLDLQ--SFQFEPVYYVPGNHEFYGGsldiT 76

                         90       100
                 ....*....|....*....|....*.
gi 521288472 124 EHFRKLKRVLEDNgCITLRNQHVSIE 149
Cdd:cd07404   77 LDALRMAAQDLSN-VHYLNNQEVVLD 101
sbcd TIGR00619
exonuclease SbcD; All proteins in this family for which functions are known are ...
 46-133 1.50e-04

exonuclease SbcD; All proteins in this family for which functions are known are double-stranded DNA exonuclease (as part of a complex with SbcC homologs). This complex functions in the initiation of recombination and recombinational repair and is particularly important in regulating the stability of DNA sections that can form secondary structures. This family is likely homologous to the MRE11 family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273178 [Multi-domain]  Cd Length: 253  Bit Score: 42.02  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288472   46 LNILHLSDLHL----ENISISPEQI------LELANKKRVDLIALTGDFLDRKRNIPK----LANYLKALQKLKPAYgMY 111
Cdd:TIGR00619   1 MRILHTSDWHLgktlEGVSRLAEQKaflddlLEFAKAEQVDALLVAGDVFDTANPPAEaqelFNAFFVNLSDTGIRP-IV 79

                          90       100
                  ....*....|....*....|..
gi 521288472  112 AVFGNHDYVLKGEHFRKLKRVL 133
Cdd:TIGR00619  80 VISGNHDSAQRLSAAKKLLAEL 101
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 48-209 1.73e-03

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: 38.80  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288472  48 ILHLSDLHLEN------ISISPEQILELANKK------RVDLIALTGDFLDRKRNiPKLANYLKALQKLKPAYgmYAVFG 115
Cdd:cd07402    1 IAQISDTHLFApgegalLGVDTAARLAAAVAQvnalhpRPDLVVVTGDLSDDGSP-ESYERLRELLAPLPAPV--YWIPG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288472 116 NHDYVlkgehfRKLKRVLEDNGCITlrNQHVSIEVEGEALNIIGID---------DYSTKRSD-IAASYKELKEGYNLVL 185
Cdd:cd07402   78 NHDDR------AAMREALPEPPYDD--NGPVQYVVDFGGWRLILLDtsvpgvhhgELSDEQLDwLEAALAEAPDRPTLIF 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 521288472 186 TH-----------DPNVVLDMQEF--------HFDYLLSGHFH 209
Cdd:cd07402  150 LHhppfplgipwmDAIRLRNSQALfavlarhpQVKAILCGHIH 192
 
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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