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Conserved domains on  [gi|1002257402|ref|XP_015633021|]
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putative metallophosphoesterase At3g03305 isoform X1 [Oryza sativa Japonica Group]

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 ...
 47-262 1.39e-37

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 cd07401:

Pssm-ID: 472684 [Multi-domain]  Cd Length: 254  Bit Score: 140.96  E-value: 1.39e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257402  47 WVVQVSDLHISAYHPDRADDLASILGPALRAIRPHLLLVTGDITDAKNRRK--TTSRQDEREWITYKKAIDAivgiGGID 124
Cdd:cd07401     1 WFVHLTDIHVSSFHDPNRIQDETFCSNFIDVIKPTLVLITGDLTDNKTGNKlpSYQYQEEWQWKYYNILKES----SVIN 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257402 125 KSRIFDIRGNHDTYGVPYRGGKLDFFSTYSVNSQLDrlSTISSILLQGrRNYLFLGIDDTMSIGIRYPANLFGHPTDKRI 204
Cdd:cd07401    77 KEYLFDIRGNHDLFGIVSFDSQNNYYRKYSNTGRDH--SHSFSSTTRF-GNYSFIGFDPTIFPGPKRPFNFFGSLDKKLL 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002257402 205 DAVNSELQYwSNHSNVpitKVVFGHYPMS-FTTSSQK--GQRYESIFAKQSISAYLCGHLH 262
Cdd:cd07401   154 DRLEKELEK-SKNSKY---TIWFGHYPHSlIISPSAKssSKTFKDLLKKYNVTAYLCGHLH 210
 
Name Accession Description Interval E-value
MPP_TMEM62_N cd07401
Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) ...
 47-262 1.39e-37

Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) is an uncharacterized Homo sapiens transmembrane protein with an N-terminal metallophosphatase domain. TMEM62 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: 277346 [Multi-domain]  Cd Length: 254  Bit Score: 140.96  E-value: 1.39e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257402  47 WVVQVSDLHISAYHPDRADDLASILGPALRAIRPHLLLVTGDITDAKNRRK--TTSRQDEREWITYKKAIDAivgiGGID 124
Cdd:cd07401     1 WFVHLTDIHVSSFHDPNRIQDETFCSNFIDVIKPTLVLITGDLTDNKTGNKlpSYQYQEEWQWKYYNILKES----SVIN 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257402 125 KSRIFDIRGNHDTYGVPYRGGKLDFFSTYSVNSQLDrlSTISSILLQGrRNYLFLGIDDTMSIGIRYPANLFGHPTDKRI 204
Cdd:cd07401    77 KEYLFDIRGNHDLFGIVSFDSQNNYYRKYSNTGRDH--SHSFSSTTRF-GNYSFIGFDPTIFPGPKRPFNFFGSLDKKLL 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002257402 205 DAVNSELQYwSNHSNVpitKVVFGHYPMS-FTTSSQK--GQRYESIFAKQSISAYLCGHLH 262
Cdd:cd07401   154 DRLEKELEK-SKNSKY---TIWFGHYPHSlIISPSAKssSKTFKDLLKKYNVTAYLCGHLH 210
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
48-262 1.30e-14

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 73.96  E-value: 1.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257402  48 VVQVSDLHISAYH-PDRADDLASILGpALRAIRPHLLLVTGDITDaknrrkttsRQDEREWITYKKAIDAIvgiggidKS 126
Cdd:COG1409     3 FAHISDLHLGAPDgSDTAEVLAAALA-DINAPRPDFVVVTGDLTD---------DGEPEEYAAAREILARL-------GV 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257402 127 RIFDIRGNHDTYGVPYRggklDFFSTYSVNSQLDRLSTISsillqgRRNYLFLGIDDTmsigirYPANLFGHPTDKRIDA 206
Cdd:COG1409    66 PVYVVPGNHDIRAAMAE----AYREYFGDLPPGGLYYSFD------YGGVRFIGLDSN------VPGRSSGELGPEQLAW 129

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002257402 207 VNSELQywsNHSNVPItkVVFGHYPMsFTTSSQK-------GQRYESIFAKQSISAYLCGHLH 262
Cdd:COG1409   130 LEEELA---AAPAKPV--IVFLHHPP-YSTGSGSdriglrnAEELLALLARYGVDLVLSGHVH 186
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 48-150 2.00e-05

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: 44.13  E-value: 2.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257402  48 VVQVSDLHIsayhPDRADDLASILGPALRAIRPHLLLVTGDITDAKNRRKTTSRQDERewitykkaidaivgigGIDKSR 127
Cdd:pfam00149   3 ILVIGDLHL----PGQLDDLLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEVLELLER----------------LIKYVP 62

                          90       100
                  ....*....|....*....|...
gi 1002257402 128 IFDIRGNHDTYGVPYRGGKLDFF 150
Cdd:pfam00149  63 VYLVRGNHDFDYGECLRLYPYLG 85
 
Name Accession Description Interval E-value
MPP_TMEM62_N cd07401
Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) ...
 47-262 1.39e-37

Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) is an uncharacterized Homo sapiens transmembrane protein with an N-terminal metallophosphatase domain. TMEM62 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: 277346 [Multi-domain]  Cd Length: 254  Bit Score: 140.96  E-value: 1.39e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257402  47 WVVQVSDLHISAYHPDRADDLASILGPALRAIRPHLLLVTGDITDAKNRRK--TTSRQDEREWITYKKAIDAivgiGGID 124
Cdd:cd07401     1 WFVHLTDIHVSSFHDPNRIQDETFCSNFIDVIKPTLVLITGDLTDNKTGNKlpSYQYQEEWQWKYYNILKES----SVIN 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257402 125 KSRIFDIRGNHDTYGVPYRGGKLDFFSTYSVNSQLDrlSTISSILLQGrRNYLFLGIDDTMSIGIRYPANLFGHPTDKRI 204
Cdd:cd07401    77 KEYLFDIRGNHDLFGIVSFDSQNNYYRKYSNTGRDH--SHSFSSTTRF-GNYSFIGFDPTIFPGPKRPFNFFGSLDKKLL 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002257402 205 DAVNSELQYwSNHSNVpitKVVFGHYPMS-FTTSSQK--GQRYESIFAKQSISAYLCGHLH 262
Cdd:cd07401   154 DRLEKELEK-SKNSKY---TIWFGHYPHSlIISPSAKssSKTFKDLLKKYNVTAYLCGHLH 210
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
48-262 1.30e-14

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 73.96  E-value: 1.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257402  48 VVQVSDLHISAYH-PDRADDLASILGpALRAIRPHLLLVTGDITDaknrrkttsRQDEREWITYKKAIDAIvgiggidKS 126
Cdd:COG1409     3 FAHISDLHLGAPDgSDTAEVLAAALA-DINAPRPDFVVVTGDLTD---------DGEPEEYAAAREILARL-------GV 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257402 127 RIFDIRGNHDTYGVPYRggklDFFSTYSVNSQLDRLSTISsillqgRRNYLFLGIDDTmsigirYPANLFGHPTDKRIDA 206
Cdd:COG1409    66 PVYVVPGNHDIRAAMAE----AYREYFGDLPPGGLYYSFD------YGGVRFIGLDSN------VPGRSSGELGPEQLAW 129

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002257402 207 VNSELQywsNHSNVPItkVVFGHYPMsFTTSSQK-------GQRYESIFAKQSISAYLCGHLH 262
Cdd:COG1409   130 LEEELA---AAPAKPV--IVFLHHPP-YSTGSGSdriglrnAEELLALLARYGVDLVLSGHVH 186
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 49-136 2.95e-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: 47.29  E-value: 2.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257402  49 VQVSDLHISAYhPDRADDLASILGPAlRAIRPHLLLVTGDITDaknrrkttsRQDEREWITYKKAIDAivgiggIDKSRI 128
Cdd:cd07400     2 AHISDLHFGEE-RKPEVLELNLLDEI-NALKPDLVVVTGDLTQ---------RARPAEFEEAREFLDA------LEPEPV 64


                  ....*...
gi 1002257402 129 FDIRGNHD 136
Cdd:cd07400    65 VVVPGNHD 72
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 48-150 2.00e-05

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: 44.13  E-value: 2.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257402  48 VVQVSDLHIsayhPDRADDLASILGPALRAIRPHLLLVTGDITDAKNRRKTTSRQDERewitykkaidaivgigGIDKSR 127
Cdd:pfam00149   3 ILVIGDLHL----PGQLDDLLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEVLELLER----------------LIKYVP 62

                          90       100
                  ....*....|....*....|...
gi 1002257402 128 IFDIRGNHDTYGVPYRGGKLDFF 150
Cdd:pfam00149  63 VYLVRGNHDFDYGECLRLYPYLG 85
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
48-139 1.52e-04

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 44.02  E-value: 1.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257402  48 VVQVSDLHISAYhpDRADDLASILGpALRAIRPHLLLVTGDITDaknrrkttSRQDEREWItyKKAIDAIVGIGGidksr 127
Cdd:COG1408    45 IVQLSDLHLGPF--IGGERLERLVE-KINALKPDLVVLTGDLVD--------GSVAELEAL--LELLKKLKAPLG----- 106

                          90
                  ....*....|..
gi 1002257402 128 IFDIRGNHDTYG 139
Cdd:COG1408   107 VYAVLGNHDYYA 118
COG1407 COG1407
Metallophosphoesterase superfamily enzyme [General function prediction only];
51-139 9.94e-03

Metallophosphoesterase superfamily enzyme [General function prediction only];


Pssm-ID: 441017  Cd Length: 224  Bit Score: 38.32  E-value: 9.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257402  51 VSDLHIS-----AYH----P--DRADDLASILGpALRAIRPHLLLVTGDITDAKNRRKTTSRQDEREWITYKKAIDAIVg 119
Cdd:COG1407    28 VADLHLGkesafRRRgiplPpyDTRETLERLEA-LIERTGPDRLIILGDLFHDFGGPSRQEWEELERLLALHAGVEVIL- 105

                          90       100
                  ....*....|....*....|
gi 1002257402 120 iggidksrifdIRGNHDTYG 139
Cdd:COG1407   106 -----------VRGNHDPGL 114
 
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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