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Conserved domains on  [gi|398365325|ref|NP_014780|]
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Sia1p [Saccharomyces cerevisiae S288C]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 46112)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MPP_superfamily super family cl13995
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
309-575 1.88e-34

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.


The actual alignment was detected with superfamily member cd07383:

Pssm-ID: 472684 [Multi-domain]  Cd Length: 202  Bit Score: 129.72  E-value: 1.88e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365325 309 SFKILQITDFHFKCTDNSMTVINE--IKTVNFIDRVLASENPDLVVITGDLLDSHNTID--YQTCIMKVVQPMISNKIPY 384
Cdd:cd07383    2 KFKILQFADLHFGEGEWTCWEGCEadLKTVEFIESVLDEEKPDLVVLTGDLITGENTADdnATSYLDKAVSPLVERGIPW 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365325 385 AISLGVSDESNLATSAQIrDFIRNLPytfnnvaseeghmaievsfkkkltkntllerdidtedetnpsealffvfdsfap 464
Cdd:cd07383   82 AATFGNHDGYDWIDPSQV-EWFESTS------------------------------------------------------ 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365325 465 vnnflQDYNDLIGKIDFGLAFQYFPLSEYRPHGL--FPIIGQYNERSTltvdtprsrgqvSMTINGKHYKSFLDILslwN 542
Cdd:cd07383  107 -----AALKKKYGKNIPSLAFFHIPLPEYREVWNekGKLGGINREKVC------------CQKTNSGFFKALVKRG---D 166
                        250       260       270
                 ....*....|....*....|....*....|...
gi 398365325 543 IKGVSCGHEHNNDCCLQSKNEMWLCYGGSAGIG 575
Cdd:cd07383  167 VKAVFCGHDHGNDFCGRWKNGIWLCYGRHTGYG 199
 
Name Accession Description Interval E-value
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
309-575 1.88e-34

Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; DCR2 phosphatase (Dosage-dependent Cell Cycle Regulator 2) functions together with DCR1 (Gid8) in a common pathway to accelerate initiation of DNA replication in Saccharomyces cerevisiae. Genetic analysis suggests that DCR1 functions upstream of DCR2. DCR2 interacts with and dephosphorylates Sic1, an inhibitor of mitotic cyclin/cyclin-dependent kinase complexes, which may serve to trigger the initiation of cell division. DCR2 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: 277329 [Multi-domain]  Cd Length: 202  Bit Score: 129.72  E-value: 1.88e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365325 309 SFKILQITDFHFKCTDNSMTVINE--IKTVNFIDRVLASENPDLVVITGDLLDSHNTID--YQTCIMKVVQPMISNKIPY 384
Cdd:cd07383    2 KFKILQFADLHFGEGEWTCWEGCEadLKTVEFIESVLDEEKPDLVVLTGDLITGENTADdnATSYLDKAVSPLVERGIPW 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365325 385 AISLGVSDESNLATSAQIrDFIRNLPytfnnvaseeghmaievsfkkkltkntllerdidtedetnpsealffvfdsfap 464
Cdd:cd07383   82 AATFGNHDGYDWIDPSQV-EWFESTS------------------------------------------------------ 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365325 465 vnnflQDYNDLIGKIDFGLAFQYFPLSEYRPHGL--FPIIGQYNERSTltvdtprsrgqvSMTINGKHYKSFLDILslwN 542
Cdd:cd07383  107 -----AALKKKYGKNIPSLAFFHIPLPEYREVWNekGKLGGINREKVC------------CQKTNSGFFKALVKRG---D 166
                        250       260       270
                 ....*....|....*....|....*....|...
gi 398365325 543 IKGVSCGHEHNNDCCLQSKNEMWLCYGGSAGIG 575
Cdd:cd07383  167 VKAVFCGHDHGNDFCGRWKNGIWLCYGRHTGYG 199
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
294-363 5.09e-09

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 57.50  E-value: 5.09e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365325 294 YKITSPHIqfSRGQRSFKILQITDFHFKctdnsmTVINEIKTVNFIDRVlASENPDLVVITGDLLDSHNT 363
Cdd:COG1408   29 YTVPIPKL--PPAFDGLRIVQLSDLHLG------PFIGGERLERLVEKI-NALKPDLVVLTGDLVDGSVA 89
PRK11148 PRK11148
cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional
306-367 1.95e-04

cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional


Pssm-ID: 182997 [Multi-domain]  Cd Length: 275  Bit Score: 43.77  E-value: 1.95e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365325 306 GQRSFKILQITDFH-FKCTDNSMTVINEIKTVN-FIDRVLASENP-DLVVITGDLLDSHNTIDYQ 367
Cdd:PRK11148  11 GEARVRILQITDTHlFADEHETLLGVNTWESYQaVLEAIRAQQHEfDLIVATGDLAQDHSSEAYQ 75
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
310-389 4.07e-03

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: 37.58  E-value: 4.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365325  310 FKILQITDFHFKCTDNSmtvineikTVNFIDRVLASENPDLVVITGDLLDSHNTIDYqtcIMKVVQPMIsNKIPYAISLG 389
Cdd:pfam00149   1 MRILVIGDLHLPGQLDD--------LLELLKKLLEEGKPDLVLHAGDLVDRGPPSEE---VLELLERLI-KYVPVYLVRG 68
 
Name Accession Description Interval E-value
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
309-575 1.88e-34

Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; DCR2 phosphatase (Dosage-dependent Cell Cycle Regulator 2) functions together with DCR1 (Gid8) in a common pathway to accelerate initiation of DNA replication in Saccharomyces cerevisiae. Genetic analysis suggests that DCR1 functions upstream of DCR2. DCR2 interacts with and dephosphorylates Sic1, an inhibitor of mitotic cyclin/cyclin-dependent kinase complexes, which may serve to trigger the initiation of cell division. DCR2 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: 277329 [Multi-domain]  Cd Length: 202  Bit Score: 129.72  E-value: 1.88e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365325 309 SFKILQITDFHFKCTDNSMTVINE--IKTVNFIDRVLASENPDLVVITGDLLDSHNTID--YQTCIMKVVQPMISNKIPY 384
Cdd:cd07383    2 KFKILQFADLHFGEGEWTCWEGCEadLKTVEFIESVLDEEKPDLVVLTGDLITGENTADdnATSYLDKAVSPLVERGIPW 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365325 385 AISLGVSDESNLATSAQIrDFIRNLPytfnnvaseeghmaievsfkkkltkntllerdidtedetnpsealffvfdsfap 464
Cdd:cd07383   82 AATFGNHDGYDWIDPSQV-EWFESTS------------------------------------------------------ 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365325 465 vnnflQDYNDLIGKIDFGLAFQYFPLSEYRPHGL--FPIIGQYNERSTltvdtprsrgqvSMTINGKHYKSFLDILslwN 542
Cdd:cd07383  107 -----AALKKKYGKNIPSLAFFHIPLPEYREVWNekGKLGGINREKVC------------CQKTNSGFFKALVKRG---D 166
                        250       260       270
                 ....*....|....*....|....*....|...
gi 398365325 543 IKGVSCGHEHNNDCCLQSKNEMWLCYGGSAGIG 575
Cdd:cd07383  167 VKAVFCGHDHGNDFCGRWKNGIWLCYGRHTGYG 199
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
294-363 5.09e-09

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 57.50  E-value: 5.09e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365325 294 YKITSPHIqfSRGQRSFKILQITDFHFKctdnsmTVINEIKTVNFIDRVlASENPDLVVITGDLLDSHNT 363
Cdd:COG1408   29 YTVPIPKL--PPAFDGLRIVQLSDLHLG------PFIGGERLERLVEKI-NALKPDLVVLTGDLVDGSVA 89
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
309-365 1.81e-06

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: 49.20  E-value: 1.81e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 398365325 309 SFKILQITDFHFKCTDNSMTVINEIKTVNfidrvlaSENPDLVVITGDLLDSHNTID 365
Cdd:cd07385    1 GLRIVQLSDIHLGPFVGRTRLQKVVRKVN-------ELNPDLIVITGDLVDGDVSVL 50
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
310-367 1.61e-05

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 46.61  E-value: 1.61e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365325 310 FKILQITDFHFKCTDNSmtvineiKTVNFIDRVLA---SENPDLVVITGDLLDSHNTIDYQ 367
Cdd:COG1409    1 FRFAHISDLHLGAPDGS-------DTAEVLAAALAdinAPRPDFVVVTGDLTDDGEPEEYA 54
PRK11148 PRK11148
cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional
306-367 1.95e-04

cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional


Pssm-ID: 182997 [Multi-domain]  Cd Length: 275  Bit Score: 43.77  E-value: 1.95e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365325 306 GQRSFKILQITDFH-FKCTDNSMTVINEIKTVN-FIDRVLASENP-DLVVITGDLLDSHNTIDYQ 367
Cdd:PRK11148  11 GEARVRILQITDTHlFADEHETLLGVNTWESYQaVLEAIRAQQHEfDLIVATGDLAQDHSSEAYQ 75
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
312-359 1.58e-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: 39.20  E-value: 1.58e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 398365325 312 ILQITDFHFKCTDNSMTVinEIKTVNFIDrvlaSENPDLVVITGDLLD 359
Cdd:cd07400    1 IAHISDLHFGEERKPEVL--ELNLLDEIN----ALKPDLVVVTGDLTQ 42
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
310-389 4.07e-03

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: 37.58  E-value: 4.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365325  310 FKILQITDFHFKCTDNSmtvineikTVNFIDRVLASENPDLVVITGDLLDSHNTIDYqtcIMKVVQPMIsNKIPYAISLG 389
Cdd:pfam00149   1 MRILVIGDLHLPGQLDD--------LLELLKKLLEEGKPDLVLHAGDLVDRGPPSEE---VLELLERLI-KYVPVYLVRG 68
 
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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