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Conserved domains on  [gi|522003353|ref|WP_020514624|]
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metallophosphoesterase [Paractinoplanes globisporus]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 10005392)

metallophosphoesterase family protein may contain an active site consisting of two metal ions (usually manganese, iron, or zinc)

CATH:  3.60.21.10
EC:  3.1.-.-
Gene Ontology:  GO:0016787|GO:0046872|GO:0042578
PubMed:  25837850|8003970
SCOP:  3001067

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
3-227 2.28e-39

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


:

Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 135.53  E-value: 2.28e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522003353   3 RIAAVGDVHVDKDvlgRFRPALEELPD-RADVLLVAGDLTRHGTVEEARCFATEFGGLGVPVVTVLGNHDHQSdlqsrVT 81
Cdd:COG2129    1 KILAVSDLHGNFD---LLEKLLELARAeDADLVILAGDLTDFGTAEEAREVLEELAALGVPVLAVPGNHDDPE-----VL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522003353  82 EVLTESGITVLEGDatVLELHGHRLGvagvkgfgggfagacasNFGEREMKDFVGTTEVVARKLQDALLS-VQADALVAL 160
Cdd:COG2129   73 DALEESGVHNLHGR--VVEIGGLRIA-----------------GLGGSRPTPFGTPYEYTEEEIEERLAKlREKDVDILL 133

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522003353 161 THYAPVPDTLlgEPLEIYPFLGCYQLGRAIDAAPTALALHGHAHHGAERGRTpGGVPVRNVAHPVIK 227
Cdd:COG2129  134 THAPPYGTTL--DRVEDGPHVGSKALRELIEEFQPKLVLHGHIHESRGVDKI-GGTRVVNPGSLAEG 197
 
Name Accession Description Interval E-value
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
3-227 2.28e-39

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 135.53  E-value: 2.28e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522003353   3 RIAAVGDVHVDKDvlgRFRPALEELPD-RADVLLVAGDLTRHGTVEEARCFATEFGGLGVPVVTVLGNHDHQSdlqsrVT 81
Cdd:COG2129    1 KILAVSDLHGNFD---LLEKLLELARAeDADLVILAGDLTDFGTAEEAREVLEELAALGVPVLAVPGNHDDPE-----VL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522003353  82 EVLTESGITVLEGDatVLELHGHRLGvagvkgfgggfagacasNFGEREMKDFVGTTEVVARKLQDALLS-VQADALVAL 160
Cdd:COG2129   73 DALEESGVHNLHGR--VVEIGGLRIA-----------------GLGGSRPTPFGTPYEYTEEEIEERLAKlREKDVDILL 133

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522003353 161 THYAPVPDTLlgEPLEIYPFLGCYQLGRAIDAAPTALALHGHAHHGAERGRTpGGVPVRNVAHPVIK 227
Cdd:COG2129  134 THAPPYGTTL--DRVEDGPHVGSKALRELIEEFQPKLVLHGHIHESRGVDKI-GGTRVVNPGSLAEG 197
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 2-106 5.47e-08

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: 51.90  E-value: 5.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522003353   2 IRIAAVGDVH----VDKDVLGRFRPALEELPdrADVLLVAGDLTrHGTVEEARCFATEFGGL--GVPVVTVLGNHDHQSD 75
Cdd:cd07385    2 LRIVQLSDIHlgpfVGRTRLQKVVRKVNELN--PDLIVITGDLV-DGDVSVLRLLASPLSKLkaPLGVYFVLGNHDYYSG 78

                         90       100       110
                 ....*....|....*....|....*....|.
gi 522003353  76 LQSRVTEVLTESGITVLEGDATVLELHGHRL 106
Cdd:cd07385   79 DVEVWIAALEKAGITVLRNESVELSRDGATI 109
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 2-71 1.10e-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: 49.13  E-value: 1.10e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522003353    2 IRIAAVGDVHVDKDvLGRFRPALEEL--PDRADVLLVAGDLTRHGTVEEARCFATEFGGLGVPVVTVLGNHD 71
Cdd:pfam00149   1 MRILVIGDLHLPGQ-LDDLLELLKKLleEGKPDLVLHAGDLVDRGPPSEEVLELLERLIKYVPVYLVRGNHD 71
PRK11340 PRK11340
phosphodiesterase YaeI; Provisional
 2-99 6.89e-03

phosphodiesterase YaeI; Provisional


Pssm-ID: 236899  Cd Length: 271  Bit Score: 37.14  E-value: 6.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522003353   2 IRIAAVGDVHVDKDV-LGRFRPALEE-LPDRADVLLVAGDLTRHGTVEEARCFATEFGGLG--VPVVTVLGNHDHQ--SD 75
Cdd:PRK11340  50 FKILFLADLHYSRFVpLSLISDAIALgIEQKPDLILLGGDYVLFDMPLNFSAFSDVLSPLAecAPTFACFGNHDRPvgTE 129

                         90       100
                 ....*....|....*....|....
gi 522003353  76 LQSRVTEVLTESGITVLEGDATVL 99
Cdd:PRK11340 130 KNHLIGETLKSAGITVLFNQATVI 153
 
Name Accession Description Interval E-value
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
3-227 2.28e-39

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 135.53  E-value: 2.28e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522003353   3 RIAAVGDVHVDKDvlgRFRPALEELPD-RADVLLVAGDLTRHGTVEEARCFATEFGGLGVPVVTVLGNHDHQSdlqsrVT 81
Cdd:COG2129    1 KILAVSDLHGNFD---LLEKLLELARAeDADLVILAGDLTDFGTAEEAREVLEELAALGVPVLAVPGNHDDPE-----VL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522003353  82 EVLTESGITVLEGDatVLELHGHRLGvagvkgfgggfagacasNFGEREMKDFVGTTEVVARKLQDALLS-VQADALVAL 160
Cdd:COG2129   73 DALEESGVHNLHGR--VVEIGGLRIA-----------------GLGGSRPTPFGTPYEYTEEEIEERLAKlREKDVDILL 133

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522003353 161 THYAPVPDTLlgEPLEIYPFLGCYQLGRAIDAAPTALALHGHAHHGAERGRTpGGVPVRNVAHPVIK 227
Cdd:COG2129  134 THAPPYGTTL--DRVEDGPHVGSKALRELIEEFQPKLVLHGHIHESRGVDKI-GGTRVVNPGSLAEG 197
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
2-246 4.04e-13

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 66.64  E-value: 4.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522003353   2 IRIAAVGDVHVD----KDVLGRFRPALEELPD-RADVLLVAGDLTRHGTVEEARCFATEFGGLGVPVVTVLGNHDHQSDL 76
Cdd:COG1409    1 FRFAHISDLHLGapdgSDTAEVLAAALADINApRPDFVVVTGDLTDDGEPEEYAAAREILARLGVPVYVVPGNHDIRAAM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522003353  77 QSRVTEVLtesGITVLEGDATVLELHGHRLgvagvkgfgggfagACASNFGEREMKDFVGTTEVvaRKLQDALLSVQADA 156
Cdd:COG1409   81 AEAYREYF---GDLPPGGLYYSFDYGGVRF--------------IGLDSNVPGRSSGELGPEQL--AWLEEELAAAPAKP 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522003353 157 LVALTHYAPVPDtllGEPLEIYPFLGCYQLGRAIDAAPTALALHGHAHHgaERGRTPGGVPV---RNVAHPV-IKQAYNV 232
Cdd:COG1409  142 VIVFLHHPPYST---GSGSDRIGLRNAEELLALLARYGVDLVLSGHVHR--YERTRRDGVPYivaGSTGGQVrLPPGYRV 216

                        250
                 ....*....|....
gi 522003353 233 YQLLSEDVDLELVA 246
Cdd:COG1409  217 IEVDGDGLTVEVRR 230
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
2-106 4.58e-10

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 58.27  E-value: 4.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522003353   2 IRIAAVGDVHVDKDVLGRF-RPALEELPD-RADVLLVAGDLTRHGTVEEARcFATEFGGL--GVPVVTVLGNHDHQSDLQ 77
Cdd:COG1408   43 LRIVQLSDLHLGPFIGGERlERLVEKINAlKPDLVVLTGDLVDGSVAELEA-LLELLKKLkaPLGVYAVLGNHDYYAGLE 121

                         90       100
                 ....*....|....*....|....*....
gi 522003353  78 sRVTEVLTESGITVLEGDATVLELHGHRL 106
Cdd:COG1408  122 -ELRAALEEAGVRVLRNEAVTLERGGDRL 149
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 2-106 5.47e-08

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: 51.90  E-value: 5.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522003353   2 IRIAAVGDVH----VDKDVLGRFRPALEELPdrADVLLVAGDLTrHGTVEEARCFATEFGGL--GVPVVTVLGNHDHQSD 75
Cdd:cd07385    2 LRIVQLSDIHlgpfVGRTRLQKVVRKVNELN--PDLIVITGDLV-DGDVSVLRLLASPLSKLkaPLGVYFVLGNHDYYSG 78

                         90       100       110
                 ....*....|....*....|....*....|.
gi 522003353  76 LQSRVTEVLTESGITVLEGDATVLELHGHRL 106
Cdd:cd07385   79 DVEVWIAALEKAGITVLRNESVELSRDGATI 109
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 5-71 7.23e-08

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: 49.96  E-value: 7.23e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522003353   5 AAVGDVHVDKDVLGRFRPALEELPDRADVLLVAGDLTRHGTV-EEARCFATEFGGLGVPVVTVLGNHD 71
Cdd:cd00838    1 LVISDIHGNLEALEAVLEAALAKAEKPDLVICLGDLVDYGPDpEEVELKALRLLLAGIPVYVVPGNHD 68
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 15-88 1.01e-07

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: 51.12  E-value: 1.01e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522003353  15 DVLGRFRPALEELP---DRADVLLVAGDLTRHGTVEEARCFATEFGGLGVPVVTVLGNHDHQSDLQSRVTEVLTESG 88
Cdd:cd07402   21 DTAARLAAAVAQVNalhPRPDLVVVTGDLSDDGSPESYERLRELLAPLPAPVYWIPGNHDDRAAMREALPEPPYDDN 97
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 2-71 1.10e-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: 49.13  E-value: 1.10e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522003353    2 IRIAAVGDVHVDKDvLGRFRPALEEL--PDRADVLLVAGDLTRHGTVEEARCFATEFGGLGVPVVTVLGNHD 71
Cdd:pfam00149   1 MRILVIGDLHLPGQ-LDDLLELLKKLleEGKPDLVLHAGDLVDRGPPSEEVLELLERLIKYVPVYLVRGNHD 71
MPP_PAE1087 cd07392
Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an ...
 4-91 2.45e-06

Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an uncharacterized Pyrobaculum aerophilum protein with a metallophosphatase domain. 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: 277338 [Multi-domain]  Cd Length: 190  Bit Score: 46.54  E-value: 2.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522003353   4 IAAVGDVHvdkdvlGRFRPALEELP--DRADVLLVAGDLTRHGTVEEARCFATEFGGLGVPVVTVLGNHDHqsdlqSRVT 81
Cdd:cd07392    1 ILAISDVH------GDVPKLKKIKLkaEEADAVIVAGDITHFGPGEEAIEALNLLLAIGAPVLAVPGNCDT-----PEVL 69

                         90
                 ....*....|
gi 522003353  82 EVLTESGITV 91
Cdd:cd07392   70 GELNSAGLNI 79
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
2-92 4.00e-06

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 46.44  E-value: 4.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522003353   2 IRIAAVGDVHVDKDVLGRFRP-----ALEELPDRA-----DVLLVAGDLTRHG-----TVEEARCFATEFGGLGVPVVTV 66
Cdd:COG0420    1 MRFLHTADWHLGKPLHGASRRedqlaALDRLVDLAieekvDAVLIAGDLFDSAnpspeAVRLLAEALRRLSEAGIPVVLI 80

                         90       100
                 ....*....|....*....|....*.
gi 522003353  67 LGNHDHQSDLqSRVTEVLTESGITVL 92
Cdd:COG0420   81 AGNHDSPSRL-SAGSPLLENLGVHVF 105
MPP_239FB cd07379
Homo sapiens 239FB and related proteins, metallophosphatase domain; 239FB (Fetal brain protein ...
 27-71 9.80e-05

Homo sapiens 239FB and related proteins, metallophosphatase domain; 239FB (Fetal brain protein 239) is thought to play a role in central nervous system development, but its specific role in unknown. 239FB is expressed predominantly in human fetal brain from a gene located in the chromosome 11p13 region associated with the mental retardation component of the WAGR (Wilms tumor, Aniridia, Genitourinary anomalies, Mental retardation) syndrome. Orthologous brp-like (brain protein 239-like) proteins have been identified in the invertebrate amphioxus group and in vertebrates. 239FB 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: 277325 [Multi-domain]  Cd Length: 135  Bit Score: 41.08  E-value: 9.80e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 522003353  27 LPDrADVLLVAGDLTRHGTVEEARCFATEFGGLGVPV-VTVLGNHD 71
Cdd:cd07379   17 IPD-GDVLIHAGDFTEGGTPDEVKKFLDWLKSLPHPHkIVIAGNHD 61
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 3-106 1.80e-04

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: 40.76  E-value: 1.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522003353    3 RIAAVGDVHvdkDVLGRFRPALEELPDRADVLLVAGDLTRHGTVEEARCFAtefgglgvPVVTVLGNHDHQSDlqsrVTE 82
Cdd:pfam12850   2 RIGIISDTH---DNLALPEAALERLKGVVDLIIHAGDIVAPEVLEELLELA--------PVLAVRGNNDAAAE----FAT 66

                          90       100
                  ....*....|....*....|....
gi 522003353   83 VLTESGITVLEGDaTVLELHGHRL 106
Cdd:pfam12850  67 DLPEEAVLELGGV-KILLTHGHGV 89
MPP_YfcE cd00841
Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a ...
 3-106 3.14e-04

Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a manganase-dependent metallophosphatase, found in bacteria and archaea, that cleaves bis-p-nitrophenyl phosphate, thymidine 5'-monophosphate-p-nitrophenyl ester, and p-nitrophenyl phosphorylcholine, but is unable to hydrolyze 2',3 ' or 3',5' cyclic nucleic phosphodiesters, and various phosphomonoesters, including p-nitrophenyl phosphate. This family also includes the Bacilus subtilis YsnB and Methanococcus jannaschii MJ0936 proteins. This domain 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: 277320 [Multi-domain]  Cd Length: 156  Bit Score: 39.95  E-value: 3.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522003353   3 RIAAVGDVHVDKDVLGRfrpALEELPDRADVLLVAGDLTRHGTVEEARCfatefggLGVPVVTVLGNHDHQSDLQSRVTE 82
Cdd:cd00841    1 KIGVISDTHGNLEAIEK---ALELFEDGVDAVIHAGDFVSPFVLNALLE-------LKAPLIAVRGNNDGEVDQLLGRPI 70

                         90       100
                 ....*....|....*....|....
gi 522003353  83 VLTESGITVleGDATVLELHGHRL 106
Cdd:cd00841   71 LPEFLTLEI--GGLRILLTHGHLF 92
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
3-104 6.08e-04

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 39.51  E-value: 6.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522003353   3 RIAAVGDVHvdkDVLGRFRPALEELPDR-ADVLLVAGDLTRHG-----TVEEARcfatefgglGVPVVTVLGNHDHQSDl 76
Cdd:COG0622    1 KIAVISDTH---GNLPALEAVLEDLEREgVDLIVHLGDLVGYGpdppeVLDLLR---------ELPIVAVRGNHDGAVL- 67

                         90       100
                 ....*....|....*....|....*...
gi 522003353  77 qsRVTEVLTESGITVLEGDaTVLELHGH 104
Cdd:COG0622   68 --RGLRSLPETLRLELEGV-RILLVHGS 92
MPP_MS158 cd07404
Microscilla MS158 and related proteins, metallophosphatase domain; MS158 is an uncharacterized ...
 27-205 1.70e-03

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: 38.47  E-value: 1.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522003353  27 LPDRADVLLVAGDLtrhGTVEEARCFATEFGGLG---VPVVTVLGNH-------DHQSDLQSRVTEVLteSGITVLEGDA 96
Cdd:cd07404   23 KVPDADILILAGDI---GRLTDAEAWDNFLDLQSfqfEPVYYVPGNHefyggslDITLDALRMAAQDL--SNVHYLNNQE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522003353  97 TVLE--------LHGHrlgvagvkgfgggfagacASNFGERE----MKDFVGTTEVVarklqdallsvqadalvalTHYA 164
Cdd:cd07404   98 VVLDdvrilgctLWSD------------------FDPDGEDIvqrkLNDFRGATVVV-------------------THHA 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 522003353 165 PVPDTLLGEPLEIYPFLGCYQLGRA--IDAAPTALALHGHAHH 205
Cdd:cd07404  141 PSPRSTSDNYADGLPKNAAFHVDLKdlILAPPIDLWIHGHTHF 183
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 3-77 2.49e-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: 37.63  E-value: 2.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522003353   3 RIAAVGDVHVDK------DVLGRFRPALEELPDRA-----DVLLVAGDL--TRHGTVEEARCFATEFGGL---GVPVVTV 66
Cdd:cd00840    1 RFLHTADWHLGYplyglsRREEDFFKAFEEIVDLAieekvDFVLIAGDLfdSNNPSPEALKLAIEGLRRLceaGIPVFVI 80

                         90
                 ....*....|.
gi 522003353  67 LGNHDHQSDLQ 77
Cdd:cd00840   81 AGNHDSPARVA 91
MPP_NostocDevT-like cd07397
Nostoc DevT and similar proteins, metallophosphatase domain; DevT (Alr4674) is a putative ...
 2-71 2.50e-03

Nostoc DevT and similar proteins, metallophosphatase domain; DevT (Alr4674) is a putative protein phosphatase from Nostoc PCC 7120 (Anabaena PCC 7120). DevT mutants form mature heterocysts, but they are unable to fix N(2) and must be supplied with a source of combined nitrogen in order to survive. Anabaena DevT shows homology to phosphatases of the PPP family and displays a Mn(2+)-dependent phosphatase activity. DevT is constitutively expressed in both vegetative cells and heterocysts, and is not regulated by NtcA. The heterocyst regulator HetR may exert a certain inhibition on the expression of devT. Under diazotrophic growth conditions, DevT protein accumulates specifically in mature heterocysts. The role that DevT plays in a late essential step of heterocyst differentiation is still unknown. 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: 277342 [Multi-domain]  Cd Length: 245  Bit Score: 38.04  E-value: 2.50e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522003353   2 IRIAAVGDVHVDKDVLGRfrPALEELpdRADVLLVAGDLTrHGTVEEARCFATefggLGVPVVTVLGNHD 71
Cdd:cd07397    1 VRIAIVGDVHGQWDAEDE--RALRLL--QPDLVLFVGDFG-NENVQLVRRIAS----LDLPKAVILGNHD 61
PRK11340 PRK11340
phosphodiesterase YaeI; Provisional
 2-99 6.89e-03

phosphodiesterase YaeI; Provisional


Pssm-ID: 236899  Cd Length: 271  Bit Score: 37.14  E-value: 6.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522003353   2 IRIAAVGDVHVDKDV-LGRFRPALEE-LPDRADVLLVAGDLTRHGTVEEARCFATEFGGLG--VPVVTVLGNHDHQ--SD 75
Cdd:PRK11340  50 FKILFLADLHYSRFVpLSLISDAIALgIEQKPDLILLGGDYVLFDMPLNFSAFSDVLSPLAecAPTFACFGNHDRPvgTE 129

                         90       100
                 ....*....|....*....|....
gi 522003353  76 LQSRVTEVLTESGITVLEGDATVL 99
Cdd:PRK11340 130 KNHLIGETLKSAGITVLFNQATVI 153
 
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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