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Conserved domains on  [gi|1872069013|ref|WP_180048174|]
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metallophosphoesterase [Acinetobacter sp. YH12243]

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];
2-232 1.41e-35

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


:

Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 126.73  E-value: 1.41e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872069013   2 ILHLSDLHF----GTERPECLEAIQQFCRDHALEAVVVSGDLTQRARLGQFFACKRFLEQLNTPYLVIPGNHDIP--LYH 75
Cdd:COG1409     3 FAHISDLHLgapdGSDTAEVLAAALADINAPRPDFVVVTGDLTDDGEPEEYAAAREILARLGVPVYVVPGNHDIRaaMAE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872069013  76 LWNRLFTPFTRYQLFFgelepVLETEHFYLIGVNSIRRRYHTkGHLSLEQIQRIDLKLQQATAsKIKIIVSHQPFYV--P 153
Cdd:COG1409    83 AYREYFGDLPPGGLYY-----SFDYGGVRFIGLDSNVPGRSS-GELGPEQLAWLEEELAAAPA-KPVIVFLHHPPYStgS 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1872069013 154 FQNKRGFKDIPLMAKIalesWSQHGLFAVLHGHLHRTAVYDLNRIfelggnhpVYDVHAGTSASHRLhknqPNSFNAID 232
Cdd:COG1409   156 GSDRIGLRNAEELLAL----LARYGVDLVLSGHVHRYERTRRDGV--------PYIVAGSTGGQVRL----PPGYRVIE 218
 
Name Accession Description Interval E-value
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
2-232 1.41e-35

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 126.73  E-value: 1.41e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872069013   2 ILHLSDLHF----GTERPECLEAIQQFCRDHALEAVVVSGDLTQRARLGQFFACKRFLEQLNTPYLVIPGNHDIP--LYH 75
Cdd:COG1409     3 FAHISDLHLgapdGSDTAEVLAAALADINAPRPDFVVVTGDLTDDGEPEEYAAAREILARLGVPVYVVPGNHDIRaaMAE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872069013  76 LWNRLFTPFTRYQLFFgelepVLETEHFYLIGVNSIRRRYHTkGHLSLEQIQRIDLKLQQATAsKIKIIVSHQPFYV--P 153
Cdd:COG1409    83 AYREYFGDLPPGGLYY-----SFDYGGVRFIGLDSNVPGRSS-GELGPEQLAWLEEELAAAPA-KPVIVFLHHPPYStgS 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1872069013 154 FQNKRGFKDIPLMAKIalesWSQHGLFAVLHGHLHRTAVYDLNRIfelggnhpVYDVHAGTSASHRLhknqPNSFNAID 232
Cdd:COG1409   156 GSDRIGLRNAEELLAL----LARYGVDLVLSGHVHRYERTRRDGV--------PYIVAGSTGGQVRL----PPGYRVIE 218
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 2-214 6.23e-29

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: 106.61  E-value: 6.23e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872069013   2 ILHLSDLHFGTERPECLEAIQ--QFCRDHALEAVVVSGDLTQRARLGQFFACKRFLEQLNT-PYLVIPGNHDIplyhlwn 78
Cdd:cd07400     1 IAHISDLHFGEERKPEVLELNllDEINALKPDLVVVTGDLTQRARPAEFEEAREFLDALEPePVVVVPGNHDA------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872069013  79 rlftpftryqlffgelepvletehfyligvnsirrryhtkghlsleqiqridlklqqataskikIIVSHQPFYVPFQNKR 158
Cdd:cd07400    74 ----------------------------------------------------------------IVALHHPLLPPPDTGR 89

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1872069013 159 GfKDIPLMAKIALESWSQHGLFAVLHGHLHRTAVYDLNRIfelggnHPVYDVHAGT 214
Cdd:cd07400    90 E-RNVLLDAGDALKLLKELGVDLVLHGHKHVPAVWNLGLL------NGIVVVNAGT 138
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 2-94 5.26e-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: 47.21  E-value: 5.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872069013   2 ILHLSDLHFGTERPECLEAIQQFCRDHALEAVVVSGDLTQRARLGQFFAckRFLEQL--NTPYLVIPGNHDI------PL 73
Cdd:pfam00149   3 ILVIGDLHLPGQLDDLLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEVL--ELLERLikYVPVYLVRGNHDFdygeclRL 80

                          90       100
                  ....*....|....*....|.
gi 1872069013  74 YHLWNRLFTPFTRYQLFFGEL 94
Cdd:pfam00149  81 YPYLGLLARPWKRFLEVFNFL 101
sbcd TIGR00619
exonuclease SbcD; All proteins in this family for which functions are known are ...
 2-70 5.56e-04

exonuclease SbcD; All proteins in this family for which functions are known are double-stranded DNA exonuclease (as part of a complex with SbcC homologs). This complex functions in the initiation of recombination and recombinational repair and is particularly important in regulating the stability of DNA sections that can form secondary structures. This family is likely homologous to the MRE11 family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273178 [Multi-domain]  Cd Length: 253  Bit Score: 40.48  E-value: 5.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872069013   2 ILHLSDLHFG---------TERPECLEAIQQFCRDHALEAVVVSGDLTQRARLGQ-----FFACKRFLEQLN-TPYLVIP 66
Cdd:TIGR00619   3 ILHTSDWHLGktlegvsrlAEQKAFLDDLLEFAKAEQVDALLVAGDVFDTANPPAeaqelFNAFFVNLSDTGiRPIVVIS 82


                  ....
gi 1872069013  67 GNHD 70
Cdd:TIGR00619  83 GNHD 86
 
Name Accession Description Interval E-value
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
2-232 1.41e-35

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 126.73  E-value: 1.41e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872069013   2 ILHLSDLHF----GTERPECLEAIQQFCRDHALEAVVVSGDLTQRARLGQFFACKRFLEQLNTPYLVIPGNHDIP--LYH 75
Cdd:COG1409     3 FAHISDLHLgapdGSDTAEVLAAALADINAPRPDFVVVTGDLTDDGEPEEYAAAREILARLGVPVYVVPGNHDIRaaMAE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872069013  76 LWNRLFTPFTRYQLFFgelepVLETEHFYLIGVNSIRRRYHTkGHLSLEQIQRIDLKLQQATAsKIKIIVSHQPFYV--P 153
Cdd:COG1409    83 AYREYFGDLPPGGLYY-----SFDYGGVRFIGLDSNVPGRSS-GELGPEQLAWLEEELAAAPA-KPVIVFLHHPPYStgS 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1872069013 154 FQNKRGFKDIPLMAKIalesWSQHGLFAVLHGHLHRTAVYDLNRIfelggnhpVYDVHAGTSASHRLhknqPNSFNAID 232
Cdd:COG1409   156 GSDRIGLRNAEELLAL----LARYGVDLVLSGHVHRYERTRRDGV--------PYIVAGSTGGQVRL----PPGYRVIE 218
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 2-214 6.23e-29

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: 106.61  E-value: 6.23e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872069013   2 ILHLSDLHFGTERPECLEAIQ--QFCRDHALEAVVVSGDLTQRARLGQFFACKRFLEQLNT-PYLVIPGNHDIplyhlwn 78
Cdd:cd07400     1 IAHISDLHFGEERKPEVLELNllDEINALKPDLVVVTGDLTQRARPAEFEEAREFLDALEPePVVVVPGNHDA------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872069013  79 rlftpftryqlffgelepvletehfyligvnsirrryhtkghlsleqiqridlklqqataskikIIVSHQPFYVPFQNKR 158
Cdd:cd07400    74 ----------------------------------------------------------------IVALHHPLLPPPDTGR 89

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1872069013 159 GfKDIPLMAKIALESWSQHGLFAVLHGHLHRTAVYDLNRIfelggnHPVYDVHAGT 214
Cdd:cd07400    90 E-RNVLLDAGDALKLLKELGVDLVLHGHKHVPAVWNLGLL------NGIVVVNAGT 138
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 2-190 9.38e-13

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: 65.76  E-value: 9.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872069013   2 ILHLSDLHFGTER-------------PECLEAIQQfcRDHALEAVVVSGDLTQRARLGQFFACKRFLEQLNTPYLVIPGN 68
Cdd:cd07402     1 IAQISDTHLFAPGegallgvdtaarlAAAVAQVNA--LHPRPDLVVVTGDLSDDGSPESYERLRELLAPLPAPVYWIPGN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872069013  69 HDIPlyhlwnRLFTPF--TRYQLFFGELEPVLETEHFYLIGVNSIRRRYHtKGHLSLEQIQRIDLKLQQATASKIKIIVS 146
Cdd:cd07402    79 HDDR------AAMREAlpEPPYDDNGPVQYVVDFGGWRLILLDTSVPGVH-HGELSDEQLDWLEAALAEAPDRPTLIFLH 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1872069013 147 HQPFYVpfqnkrgfkDIPLMAKIALEswSQHGLFAVLH----------GHLHRT 190
Cdd:cd07402   152 HPPFPL---------GIPWMDAIRLR--NSQALFAVLArhpqvkailcGHIHRP 194
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
1-195 2.41e-11

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 61.57  E-value: 2.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872069013   1 MILHLSDLHFGTERpecLEAIQQFCRDHALEAVVVSGDLTQRARLGQFFACKRFLEQLNTPYLVIPGNHDiplYHLWNRL 80
Cdd:COG2129     1 KILAVSDLHGNFDL---LEKLLELARAEDADLVILAGDLTDFGTAEEAREVLEELAALGVPVLAVPGNHD---DPEVLDA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872069013  81 FTPFTRYqlffgelepVLETEHF-----YLIGVNSIR-RRYHTKGHLSLEQIQRidlKLQQATASKIKIIVSHQPFYVPF 154
Cdd:COG2129    75 LEESGVH---------NLHGRVVeigglRIAGLGGSRpTPFGTPYEYTEEEIEE---RLAKLREKDVDILLTHAPPYGTT 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1872069013 155 QNK------RGFKDIplmAKIALEswsqHGLFAVLHGHLHRTAVYDL 195
Cdd:COG2129   143 LDRvedgphVGSKAL---RELIEE----FQPKLVLHGHIHESRGVDK 182
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
2-189 1.16e-10

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 59.93  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872069013   2 ILHLSDLHFGT---------ERPECLEAIQQFCRDHALEAVVVSGDL----TQRARLGQFFAckRFLEQL---NTPYLVI 65
Cdd:COG0420     3 FLHTADWHLGKplhgasrreDQLAALDRLVDLAIEEKVDAVLIAGDLfdsaNPSPEAVRLLA--EALRRLseaGIPVVLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872069013  66 PGNHDIP----LYHLW--NRLFTPFTRYqlffgELEPVL--ETEHFYLIGVNSIRRRYHTKGHLSLEQIQRidlklqQAT 137
Cdd:COG0420    81 AGNHDSPsrlsAGSPLleNLGVHVFGSV-----EPEPVEleDGLGVAVYGLPYLRPSDEEALRDLLERLPR------ALD 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1872069013 138 ASKIKIIVSHQpFYVPFQNKRGFKDIPLMAKIAleswSQHGLFAVLHGHLHR 189
Cdd:COG0420   150 PGGPNILLLHG-FVAGASGSRDIYVAPVPLSAL----PAAGFDYVALGHIHR 196
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
2-160 1.56e-09

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 56.73  E-value: 1.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872069013   2 ILHLSDLHFGTERPEclEAIQQFCRD-HALEA--VVVSGDLTQRaRLGQFFACKRFLEQLNTPYLV--IPGNHDIplYHL 76
Cdd:COG1408    45 IVQLSDLHLGPFIGG--ERLERLVEKiNALKPdlVVLTGDLVDG-SVAELEALLELLKKLKAPLGVyaVLGNHDY--YAG 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872069013  77 WNRLFTPFTRYQLffgelePVLETEH---------FYLIGVNSirrrYHTKGHLSLEQIqridlkLQQATASKIKIIVSH 147
Cdd:COG1408   120 LEELRAALEEAGV------RVLRNEAvtlerggdrLNLAGVDD----PHAGRFPDLEKA------LAGVPPDAPRILLAH 183

                         170
                  ....*....|...
gi 1872069013 148 QPFYVPFQNKRGF 160
Cdd:COG1408   184 NPDVFDEAAAAGV 196
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 1-189 4.05e-08

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: 51.89  E-value: 4.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872069013   1 MILHLSDLHFG----------TERPECLEAIQQFCRDHALEAVVVSGDLTQRAR-----LGQFFACKRFLEQLNTPYLVI 65
Cdd:cd00840     1 RFLHTADWHLGyplyglsrreEDFFKAFEEIVDLAIEEKVDFVLIAGDLFDSNNpspeaLKLAIEGLRRLCEAGIPVFVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872069013  66 PGNHDIPlyhlwnrlftpfTRYQLFfgelepvletehfyliGVNSIRRRYHTKghlsleQIQRIDLKLQQATASKIKIIV 145
Cdd:cd00840    81 AGNHDSP------------ARVAIY----------------GLPYLRDERLER------LFEDLELRPRLLKPDWFNILL 126

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1872069013 146 SHqpfyvpfQNKRGFKDIPLMAKIALESWSQHGLFAVLHGHLHR 189
Cdd:cd00840   127 LH-------QGVDGAGPSDSERPIVPEDLLPDGFDYVALGHIHK 163
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 2-94 5.26e-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: 47.21  E-value: 5.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872069013   2 ILHLSDLHFGTERPECLEAIQQFCRDHALEAVVVSGDLTQRARLGQFFAckRFLEQL--NTPYLVIPGNHDI------PL 73
Cdd:pfam00149   3 ILVIGDLHLPGQLDDLLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEVL--ELLERLikYVPVYLVRGNHDFdygeclRL 80

                          90       100
                  ....*....|....*....|.
gi 1872069013  74 YHLWNRLFTPFTRYQLFFGEL 94
Cdd:pfam00149  81 YPYLGLLARPWKRFLEVFNFL 101
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 3-75 3.17e-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: 45.34  E-value: 3.17e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1872069013   3 LHLSDLHFGTERPECLEaIQQFCRDHALEAVVVSGDLTQRARLGQF-FACKRFLEQLNTPYLVIPGNHDIPLYH 75
Cdd:cd00838     1 LVISDIHGNLEALEAVL-EAALAKAEKPDLVICLGDLVDYGPDPEEvELKALRLLLAGIPVYVVPGNHDILVTH 73
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 2-214 1.13e-05

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: 45.35  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872069013   2 ILHLSDLHFG-TERPECLEAIQQFCRDHALEAVVVSGDLTQRaRLGQFFACKRFLEQLNTPY--LVIPGNHDIplyhlWN 78
Cdd:cd07385     4 IVQLSDIHLGpFVGRTRLQKVVRKVNELNPDLIVITGDLVDG-DVSVLRLLASPLSKLKAPLgvYFVLGNHDY-----YS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872069013  79 RLFTPFTRyqlffgELEP----VLETEH------FYLIGVNSIRRRYHTKGHLSLEQIqridlkLQQATASKIKIIVSHQ 148
Cdd:cd07385    78 GDVEVWIA------ALEKagitVLRNESvelsrdGATIGLAGSGVDDIGGHGEDLEKA------LKGLDENDPVILLAHN 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1872069013 149 PFYVPFQNKRGFkDIPLmakialeSWSQHG------LFAVLHGHLHRTAVYdlnrIFELGGNHPVYdVHAGT 214
Cdd:cd07385   146 PDAAEEAQRPGV-DLVL-------SGHTHGgqifppNYGVLSKLGFPYDSG----LYQIGGTTYLY-VSRGL 204
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 53-208 1.88e-05

purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; Purple acid phosphatases (PAPs) belong to a diverse family of binuclear metallohydrolases that have been identified and characterized in plants, animals, and fungi. PAPs contain a binuclear metal center and their characteristic pink or purple color derives from a charge-transfer transition between a tyrosine residue and a chromophoric ferric ion within the binuclear center. PAPs catalyze the hydrolysis of a wide range of activated phosphoric acid mono- and di-esters and anhydrides. PAPs are distinguished from the other phosphatases by their insensitivity to L-(+) tartrate inhibition and are therefore also known as tartrate resistant acid phosphatases (TRAPs). While only a few copies of PAP-like genes are present in mammalian and fungal genomes, multiple copies are present in plant genomes. PAPs 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: 277318 [Multi-domain]  Cd Length: 296  Bit Score: 44.98  E-value: 1.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872069013  53 RFLEQLNT--PYLVIPGNHDIplyHLWNRLFTPFTRYQLFFGELEPVLETEHFY---------LIGVNSirrrYH--TKG 119
Cdd:cd00839    60 RQIEPLASyvPYMVAPGNHEA---DYNGSTSKIKFFMPGRGMPPSPSGSTENLWysfdvgpvhFISLST----ETdfLKG 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872069013 120 HLSLEQIQRIDLKLQQATASK---IkIIVSHQPFYVPFQNKRGFKDIPLMaKIALES-WSQHGLFAVLHGHLH---RT-- 190
Cdd:cd00839   133 DNISPQYDWLEADLAKVDRSRtpwI-IVMGHRPMYCSNDDDADCIEGEKM-REALEDlFYKYGVDLVLSGHVHayeRTcp 210

                         170       180
                  ....*....|....*....|..
gi 1872069013 191 ----AVYDLNRIFELGGNHPVY 208
Cdd:cd00839   211 vynnTVANSKDNIYTNPKGPVH 232
MPP_TMEM62_N cd07401
Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) ...
 2-188 4.74e-04

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: 40.43  E-value: 4.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872069013   2 ILHLSDLHFGTERPECLEAIQQFCRDHAL----EAVVVSGDLT--------QRARLGQFFACKrFLEQLNTPY------- 62
Cdd:cd07401     2 FVHLTDIHVSSFHDPNRIQDETFCSNFIDvikpTLVLITGDLTdnktgnklPSYQYQEEWQWK-YYNILKESSvinkeyl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872069013  63 LVIPGNHDiplyhLWNRL-FTPFTRYQLFFGELEPVLETEHFYL--------IGVN-----SIRRRYHTKGHLSLEQIQR 128
Cdd:cd07401    81 FDIRGNHD-----LFGIVsFDSQNNYYRKYSNTGRDHSHSFSSTtrfgnysfIGFDptifpGPKRPFNFFGSLDKKLLDR 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1872069013 129 IDLKLQQATASKIKIIVSHQPF--YVPFQNKRG---FKDIPLMAKIaleswsqhglFAVLHGHLH 188
Cdd:cd07401   156 LEKELEKSKNSKYTIWFGHYPHslIISPSAKSSsktFKDLLKKYNV----------TAYLCGHLH 210
sbcd TIGR00619
exonuclease SbcD; All proteins in this family for which functions are known are ...
 2-70 5.56e-04

exonuclease SbcD; All proteins in this family for which functions are known are double-stranded DNA exonuclease (as part of a complex with SbcC homologs). This complex functions in the initiation of recombination and recombinational repair and is particularly important in regulating the stability of DNA sections that can form secondary structures. This family is likely homologous to the MRE11 family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273178 [Multi-domain]  Cd Length: 253  Bit Score: 40.48  E-value: 5.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872069013   2 ILHLSDLHFG---------TERPECLEAIQQFCRDHALEAVVVSGDLTQRARLGQ-----FFACKRFLEQLN-TPYLVIP 66
Cdd:TIGR00619   3 ILHTSDWHLGktlegvsrlAEQKAFLDDLLEFAKAEQVDALLVAGDVFDTANPPAeaqelFNAFFVNLSDTGiRPIVVIS 82


                  ....
gi 1872069013  67 GNHD 70
Cdd:TIGR00619  83 GNHD 86
 
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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