NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2524451713|ref|WP_286592111|]
View 

metallophosphoesterase [Citrobacter sp. Cpo061]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
202-465 3.00e-21

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


:

Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 92.83  E-value: 3.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524451713 202 IIWLSDIHFDNGKGKHAFPAQDndqqkclssRVVELAdkysNGNKCAGLAISGDLTWQSQVEGFELASKFIKDVssslsl 281
Cdd:COG1409     3 FAHISDLHLGAPDGSDTAEVLA---------AALADI----NAPRPDFVVVTGDLTDDGEPEEYAAAREILARL------ 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524451713 282 tPDDIIICPGNHDVGLVSKEEYFEIMGKPTTDTPWatlaenYHkgskenyikfykdvfqrkpeedlsqgrkFLLGGHKVV 361
Cdd:COG1409    64 -GVPVYVVPGNHDIRAAMAEAYREYFGDLPPGGLY------YS----------------------------FDYGGVRFI 108

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524451713 362 evaALNSCVLQQVKdsflgmGFIGEKQLSnvaesmgWMNKSgeyISKKRGVTRIAMLHHHLTSINEAEDAYldskysVTL 441
Cdd:COG1409   109 ---GLDSNVPGRSS------GELGPEQLA-------WLEEE---LAAAPAKPVIVFLHHPPYSTGSGSDRI------GLR 163

                         250       260
                  ....*....|....*....|....
gi 2524451713 442 DAERLLRWVVKHKVDYILHGHMHR 465
Cdd:COG1409   164 NAEELLALLARYGVDLVLSGHVHR 187
 
Name Accession Description Interval E-value
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
202-465 3.00e-21

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 92.83  E-value: 3.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524451713 202 IIWLSDIHFDNGKGKHAFPAQDndqqkclssRVVELAdkysNGNKCAGLAISGDLTWQSQVEGFELASKFIKDVssslsl 281
Cdd:COG1409     3 FAHISDLHLGAPDGSDTAEVLA---------AALADI----NAPRPDFVVVTGDLTDDGEPEEYAAAREILARL------ 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524451713 282 tPDDIIICPGNHDVGLVSKEEYFEIMGKPTTDTPWatlaenYHkgskenyikfykdvfqrkpeedlsqgrkFLLGGHKVV 361
Cdd:COG1409    64 -GVPVYVVPGNHDIRAAMAEAYREYFGDLPPGGLY------YS----------------------------FDYGGVRFI 108

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524451713 362 evaALNSCVLQQVKdsflgmGFIGEKQLSnvaesmgWMNKSgeyISKKRGVTRIAMLHHHLTSINEAEDAYldskysVTL 441
Cdd:COG1409   109 ---GLDSNVPGRSS------GELGPEQLA-------WLEEE---LAAAPAKPVIVFLHHPPYSTGSGSDRI------GLR 163

                         250       260
                  ....*....|....*....|....
gi 2524451713 442 DAERLLRWVVKHKVDYILHGHMHR 465
Cdd:COG1409   164 NAEELLALLARYGVDLVLSGHVHR 187
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 414-466 5.32e-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: 46.13  E-value: 5.32e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2524451713 414 RIAMLHHHLTSIneaedAYLDSKYSVTLDAERLLRWVVKHKVDYILHGHMHRS 466
Cdd:cd07400    73 AIVALHHPLLPP-----PDTGRERNVLLDAGDALKLLKELGVDLVLHGHKHVP 120
 
Name Accession Description Interval E-value
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
202-465 3.00e-21

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 92.83  E-value: 3.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524451713 202 IIWLSDIHFDNGKGKHAFPAQDndqqkclssRVVELAdkysNGNKCAGLAISGDLTWQSQVEGFELASKFIKDVssslsl 281
Cdd:COG1409     3 FAHISDLHLGAPDGSDTAEVLA---------AALADI----NAPRPDFVVVTGDLTDDGEPEEYAAAREILARL------ 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524451713 282 tPDDIIICPGNHDVGLVSKEEYFEIMGKPTTDTPWatlaenYHkgskenyikfykdvfqrkpeedlsqgrkFLLGGHKVV 361
Cdd:COG1409    64 -GVPVYVVPGNHDIRAAMAEAYREYFGDLPPGGLY------YS----------------------------FDYGGVRFI 108

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524451713 362 evaALNSCVLQQVKdsflgmGFIGEKQLSnvaesmgWMNKSgeyISKKRGVTRIAMLHHHLTSINEAEDAYldskysVTL 441
Cdd:COG1409   109 ---GLDSNVPGRSS------GELGPEQLA-------WLEEE---LAAAPAKPVIVFLHHPPYSTGSGSDRI------GLR 163

                         250       260
                  ....*....|....*....|....
gi 2524451713 442 DAERLLRWVVKHKVDYILHGHMHR 465
Cdd:COG1409   164 NAEELLALLARYGVDLVLSGHVHR 187
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 414-466 5.32e-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: 46.13  E-value: 5.32e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2524451713 414 RIAMLHHHLTSIneaedAYLDSKYSVTLDAERLLRWVVKHKVDYILHGHMHRS 466
Cdd:cd07400    73 AIVALHHPLLPP-----PDTGRERNVLLDAGDALKLLKELGVDLVLHGHKHVP 120
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 202-295 1.11e-04

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: 42.28  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524451713 202 IIWLSDIHFDngkgkhafPAQDNDQ-QKCLSSRVVEL-ADKysngnkcagLAISGDLTWQSQVEGFELASKFIKdvsssl 279
Cdd:cd07400     1 IAHISDLHFG--------EERKPEVlELNLLDEINALkPDL---------VVVTGDLTQRARPAEFEEAREFLD------ 57

                          90
                  ....*....|....*.
gi 2524451713 280 SLTPDDIIICPGNHDV 295
Cdd:cd07400    58 ALEPEPVVVVPGNHDA 73
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 415-473 3.40e-03

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: 38.02  E-value: 3.40e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2524451713 415 IAMLHHHLTSINEAEDayldskYSVTLDAERLLRWVVKHKVDYILHGHMHRSSCITIKK 473
Cdd:cd00838    69 ILVTHGPPYDPLDEGS------PGEDPGSEALLELLDKYGPDLVLSGHTHVPGRREVDK 121
MPP_PF1019 cd07391
Pyrococcus furiosus PF1019 and related proteins, metallophosphatase domain; This family ...
 205-306 7.41e-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: 37.67  E-value: 7.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524451713 205 LSDIH--FDNGKGKH--AFPAQdndQQKCLSSRVVELADKYsngnKCAGLAISGDLtwqsqVEGFELASK--FIKDVSSS 278
Cdd:cd07391     3 IADLHlgYEEELRRQgiNLPRR---QKERLLERLDRLLEEL----GPDRLVILGDL-----KHSFGRVSRqeRREVPFFR 70

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2524451713 279 LSLTPDDIIICPGNHDVGL--------VSKEEYFEI 306
Cdd:cd07391    71 LLAKDVDVILIRGNHDGGLeeilsdvnVVVVEGYLL 106
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH