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Conserved domains on  [gi|2431900641|gb|KAJ4622513|]
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hypothetical protein HRR88_005525 [Exophiala dermatitidis]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 11444094)

metallophosphatase family protein containing an active site consisting of two metal ions

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

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];
1-251 1.27e-13

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


:

Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 68.95  E-value: 1.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431900641   1 MRLYAISDIHL-------SYKHNREALDDLKPHPDDSLIICGDVGER--LEHLQEAFEVTTKLFKQVFWVPGNHELYTlp 71
Cdd:COG1409     1 FRFAHISDLHLgapdgsdTAEVLAAALADINAPRPDFVVVTGDLTDDgePEEYAAAREILARLGVPVYVVPGNHDIRA-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431900641  72 gittedDLDKELRGEFKYqeclrvaneygVITPEDEYVKwegEGGPCIICPIFTlYDYSFRPADVTREQaVDWAmeenvy 151
Cdd:COG1409    79 ------AMAEAYREYFGD-----------LPPGGLYYSF---DYGGVRFIGLDS-NVPGRSSGELGPEQ-LAWL------ 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431900641 152 atdeallhsdpyetrdawceqlvkktEERLEAAAARgfPLVIINHWPlrqdLITIPSIPRFSIWCGTKQTDDWHTRFNAK 231
Cdd:COG1409   131 --------------------------EEELAAAPAK--PVIVFLHHP----PYSTGSGSDRIGLRNAEELLALLARYGVD 178

                         250       260
                  ....*....|....*....|
gi 2431900641 232 VVVTGHLHVRRTDWIDGVRF 251
Cdd:COG1409   179 LVLSGHVHRYERTRRDGVPY 198
 
Name Accession Description Interval E-value
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
1-251 1.27e-13

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 68.95  E-value: 1.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431900641   1 MRLYAISDIHL-------SYKHNREALDDLKPHPDDSLIICGDVGER--LEHLQEAFEVTTKLFKQVFWVPGNHELYTlp 71
Cdd:COG1409     1 FRFAHISDLHLgapdgsdTAEVLAAALADINAPRPDFVVVTGDLTDDgePEEYAAAREILARLGVPVYVVPGNHDIRA-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431900641  72 gittedDLDKELRGEFKYqeclrvaneygVITPEDEYVKwegEGGPCIICPIFTlYDYSFRPADVTREQaVDWAmeenvy 151
Cdd:COG1409    79 ------AMAEAYREYFGD-----------LPPGGLYYSF---DYGGVRFIGLDS-NVPGRSSGELGPEQ-LAWL------ 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431900641 152 atdeallhsdpyetrdawceqlvkktEERLEAAAARgfPLVIINHWPlrqdLITIPSIPRFSIWCGTKQTDDWHTRFNAK 231
Cdd:COG1409   131 --------------------------EEELAAAPAK--PVIVFLHHP----PYSTGSGSDRIGLRNAEELLALLARYGVD 178

                         250       260
                  ....*....|....*....|
gi 2431900641 232 VVVTGHLHVRRTDWIDGVRF 251
Cdd:COG1409   179 LVLSGHVHRYERTRRDGVPY 198
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 1-68 4.87e-07

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


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 47.59  E-value: 4.87e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2431900641   1 MRLYAISDIHL--SYKHNREALDDLKPHPD-DSLIICGDV---GERLEHLQEAFEVTTKlFKQVFWVPGNHELY 68
Cdd:pfam00149   1 MRILVIGDLHLpgQLDDLLELLKKLLEEGKpDLVLHAGDLvdrGPPSEEVLELLERLIK-YVPVYLVRGNHDFD 73
MPP_MS158 cd07404
Microscilla MS158 and related proteins, metallophosphatase domain; MS158 is an uncharacterized ...
 7-68 9.40e-07

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: 48.49  E-value: 9.40e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2431900641   7 SDIHLSYKHNREALDDLKPHPD-DSLIICGDVGERLEHLQEA--FEVTTKLFKQVFWVPGNHELY 68
Cdd:cd07404     5 SDLHLEVEQNLAKLKFFPKVPDaDILILAGDIGRLTDAEAWDnfLDLQSFQFEPVYYVPGNHEFY 69
PRK09453 PRK09453
phosphodiesterase; Provisional
 1-37 9.81e-03

phosphodiesterase; Provisional


Pssm-ID: 181869 [Multi-domain]  Cd Length: 182  Bit Score: 36.38  E-value: 9.81e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2431900641   1 MRLYAISDIHLSYKHNREALDDLKPHPDDSLIICGDV 37
Cdd:PRK09453    1 MKLMFASDTHGSLPATEKALELFAQSGADWLVHLGDV 37
 
Name Accession Description Interval E-value
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
1-251 1.27e-13

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 68.95  E-value: 1.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431900641   1 MRLYAISDIHL-------SYKHNREALDDLKPHPDDSLIICGDVGER--LEHLQEAFEVTTKLFKQVFWVPGNHELYTlp 71
Cdd:COG1409     1 FRFAHISDLHLgapdgsdTAEVLAAALADINAPRPDFVVVTGDLTDDgePEEYAAAREILARLGVPVYVVPGNHDIRA-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431900641  72 gittedDLDKELRGEFKYqeclrvaneygVITPEDEYVKwegEGGPCIICPIFTlYDYSFRPADVTREQaVDWAmeenvy 151
Cdd:COG1409    79 ------AMAEAYREYFGD-----------LPPGGLYYSF---DYGGVRFIGLDS-NVPGRSSGELGPEQ-LAWL------ 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431900641 152 atdeallhsdpyetrdawceqlvkktEERLEAAAARgfPLVIINHWPlrqdLITIPSIPRFSIWCGTKQTDDWHTRFNAK 231
Cdd:COG1409   131 --------------------------EEELAAAPAK--PVIVFLHHP----PYSTGSGSDRIGLRNAEELLALLARYGVD 178

                         250       260
                  ....*....|....*....|
gi 2431900641 232 VVVTGHLHVRRTDWIDGVRF 251
Cdd:COG1409   179 LVLSGHVHRYERTRRDGVPY 198
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
2-68 1.86e-10

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 59.64  E-value: 1.86e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2431900641   2 RLYAISDIHLSYKHNREALDDLKPHPDDSLIICGDVGE--RLEHLQEAFEVTTKLFKQVFWVPGNHELY 68
Cdd:COG2129     1 KILAVSDLHGNFDLLEKLLELARAEDADLVILAGDLTDfgTAEEAREVLEELAALGVPVLAVPGNHDDP 69
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 1-68 4.87e-07

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


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 47.59  E-value: 4.87e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2431900641   1 MRLYAISDIHL--SYKHNREALDDLKPHPD-DSLIICGDV---GERLEHLQEAFEVTTKlFKQVFWVPGNHELY 68
Cdd:pfam00149   1 MRILVIGDLHLpgQLDDLLELLKKLLEEGKpDLVLHAGDLvdrGPPSEEVLELLERLIK-YVPVYLVRGNHDFD 73
MPP_MS158 cd07404
Microscilla MS158 and related proteins, metallophosphatase domain; MS158 is an uncharacterized ...
 7-68 9.40e-07

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: 48.49  E-value: 9.40e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2431900641   7 SDIHLSYKHNREALDDLKPHPD-DSLIICGDVGERLEHLQEA--FEVTTKLFKQVFWVPGNHELY 68
Cdd:cd07404     5 SDLHLEVEQNLAKLKFFPKVPDaDILILAGDIGRLTDAEAWDnfLDLQSFQFEPVYYVPGNHEFY 69
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 5-67 1.54e-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: 46.49  E-value: 1.54e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2431900641   5 AISDIHLSYKHNREALD--DLKPHPDDSLIICGDV---GERLEHLQEAFEVTTKLFKQVFWVPGNHEL 67
Cdd:cd00838     2 VISDIHGNLEALEAVLEaaLAKAEKPDLVICLGDLvdyGPDPEEVELKALRLLLAGIPVYVVPGNHDI 69
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 1-86 2.40e-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: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431900641   1 MRLYAISDIHLSYKHNREALDDLKPHPDdsLII-CGDVG--ERLEHLQEAFEVTTklfkqvfwVPGNHELYTLPGITTED 77
Cdd:pfam12850   1 MRIGIISDTHDNLALPEAALERLKGVVD--LIIhAGDIVapEVLEELLELAPVLA--------VRGNNDAAAEFATDLPE 70


                  ....*....
gi 2431900641  78 DLDKELRGE 86
Cdd:pfam12850  71 EAVLELGGV 79
LpxH COG2908
UDP-2,3-diacylglucosamine pyrophosphatase LpxH [Cell wall/membrane/envelope biogenesis];
1-65 3.72e-04

UDP-2,3-diacylglucosamine pyrophosphatase LpxH [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442152 [Multi-domain]  Cd Length: 238  Bit Score: 41.32  E-value: 3.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431900641   1 MRLYAISDIHLSYKHNREA-------LDDLKPHPdDSLIICGD-----VGERLEHLQEAFEVTTKLFK------QVFWVP 62
Cdd:COG2908     1 MRTLFISDLHLGTPGPQAItaalldfLRSIAHDA-DALYLLGDifdfwIGDDDVWPPGHNRVLQKLLEladkgtPVYYIP 79


                  ...
gi 2431900641  63 GNH 65
Cdd:COG2908    80 GNH 82
DR1119 COG1768
Predicted phosphohydrolase, DR1119 family, metallophosphatase superfamily [General function ...
 1-65 1.08e-03

Predicted phosphohydrolase, DR1119 family, metallophosphatase superfamily [General function prediction only];


Pssm-ID: 441374 [Multi-domain]  Cd Length: 230  Bit Score: 39.80  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431900641   1 MRLYAISDIHLSYKHNrealddlKP-----------------------HPDDSLIICGDV--GERLEHLQEAFEVTTKL- 54
Cdd:COG1768     1 MRIYAIGDLHLSFAPD-------KPmdvfgerwenhpekiaenwretvGPDDTVLIPGDIswAMKLEEALPDLDWIDALp 73

                          90
                  ....*....|.
gi 2431900641  55 FKQVFwVPGNH 65
Cdd:COG1768    74 GRKVL-IKGNH 83
MPP_PAE1087 cd07392
Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an ...
 5-76 2.11e-03

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: 38.45  E-value: 2.11e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2431900641   5 AISDIHLSY---KHNREALDDLkphpdDSLIICGDV--GERLEHLQEAFEVTTKLFKQVFWVPGNHELYTLPGITTE 76
Cdd:cd07392     3 AISDVHGDVpklKKIKLKAEEA-----DAVIVAGDIthFGPGEEAIEALNLLLAIGAPVLAVPGNCDTPEVLGELNS 74
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
6-68 2.54e-03

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 38.62  E-value: 2.54e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2431900641   6 ISDIHL----SYKHNREALD---DLKPhpdDSLIICGD-VGERLEHLQEAFEvttkLFKQ------VFWVPGNHELY 68
Cdd:COG1408    48 LSDLHLgpfiGGERLERLVEkinALKP---DLVVLTGDlVDGSVAELEALLE----LLKKlkaplgVYAVLGNHDYY 117
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 6-101 8.92e-03

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: 36.12  E-value: 8.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431900641   6 ISDIHLSYKHNRE-----ALDDLKPHPDDSLIICGDVGERleHLQEAFEVTTKLFKQ-----VFWVPGNHELYTL----- 70
Cdd:cd07400     4 ISDLHFGEERKPEvlelnLLDEINALKPDLVVVTGDLTQR--ARPAEFEEAREFLDAlepepVVVVPGNHDAIVAlhhpl 81

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2431900641  71 --PGITTEDDLDKELRGEFkyqecLRVANEYGV 101
Cdd:cd07400    82 lpPPDTGRERNVLLDAGDA-----LKLLKELGV 109
PRK09453 PRK09453
phosphodiesterase; Provisional
 1-37 9.81e-03

phosphodiesterase; Provisional


Pssm-ID: 181869 [Multi-domain]  Cd Length: 182  Bit Score: 36.38  E-value: 9.81e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2431900641   1 MRLYAISDIHLSYKHNREALDDLKPHPDDSLIICGDV 37
Cdd:PRK09453    1 MKLMFASDTHGSLPATEKALELFAQSGADWLVHLGDV 37
 
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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