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Conserved domains on  [gi|736541038|ref|WP_034555536|]
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metallophosphoesterase [Capnocytophaga sp. oral taxon 326]

Protein Classification

metallophosphoesterase( domain architecture ID 10003658)

metallophosphoesterase contains an active site consisting of two metal ions (usually manganese, iron, or zinc), similar to Bacillus subtilis YkuE, which is specifically targeted by the Tat pathway to the cell wall

CATH:  3.60.21.10
EC:  3.1.-.-
Gene Ontology:  GO:0046872|GO:0042578|GO:0016311
PubMed:  25837850|8003970

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
117-403 1.75e-114

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


:

Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 334.84  E-value: 1.75e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 117 LGWGLAAIPFASILYSIFKGKYNYKVWKYTLYFDNLPKAFDGYRITQISDIHCGSFDKYEKIRYGVDLINSQKSDVILFT 196
Cdd:COG1408    1 LALALLALGLALLAYGLYIEPRRLRVRRYTVPIPKLPPAFDGLRIVQLSDLHLGPFIGGERLERLVEKINALKPDLVVLT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 197 GDLVNNLANEVHNWKSLFATLQAPDGVFSIMGNHDYGDysswetpeakqqNLEHLFQLQKQMGWQLLLNEHCYLERNGEK 276
Cdd:COG1408   81 GDLVDGSVAELEALLELLKKLKAPLGVYAVLGNHDYYA------------GLEELRAALEEAGVRVLRNEAVTLERGGDR 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 277 IALIGVENWGHGRFskyGDLNKAMEGVNTEDFKILMSHDPTHWQEIVlpeNKDIQLTLSGHTHGMQCGIEIPGWLkWSPS 356
Cdd:COG1408  149 LNLAGVDDPHAGRF---PDLEKALAGVPPDAPRILLAHNPDVFDEAA---AAGVDLQLSGHTHGGQIRLPGIGAL-LTPV 221

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 736541038 357 QYIYKYWGGMYEEGGKYLNVNRGFGYHAFPGRLGVWPEITVIELKTK 403
Cdd:COG1408  222 RLGRKYVAGLYREGGTQLYVSRGLGTSGPPVRFGCPPEITLITLKSA 268
 
Name Accession Description Interval E-value
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
117-403 1.75e-114

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 334.84  E-value: 1.75e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 117 LGWGLAAIPFASILYSIFKGKYNYKVWKYTLYFDNLPKAFDGYRITQISDIHCGSFDKYEKIRYGVDLINSQKSDVILFT 196
Cdd:COG1408    1 LALALLALGLALLAYGLYIEPRRLRVRRYTVPIPKLPPAFDGLRIVQLSDLHLGPFIGGERLERLVEKINALKPDLVVLT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 197 GDLVNNLANEVHNWKSLFATLQAPDGVFSIMGNHDYGDysswetpeakqqNLEHLFQLQKQMGWQLLLNEHCYLERNGEK 276
Cdd:COG1408   81 GDLVDGSVAELEALLELLKKLKAPLGVYAVLGNHDYYA------------GLEELRAALEEAGVRVLRNEAVTLERGGDR 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 277 IALIGVENWGHGRFskyGDLNKAMEGVNTEDFKILMSHDPTHWQEIVlpeNKDIQLTLSGHTHGMQCGIEIPGWLkWSPS 356
Cdd:COG1408  149 LNLAGVDDPHAGRF---PDLEKALAGVPPDAPRILLAHNPDVFDEAA---AAGVDLQLSGHTHGGQIRLPGIGAL-LTPV 221

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 736541038 357 QYIYKYWGGMYEEGGKYLNVNRGFGYHAFPGRLGVWPEITVIELKTK 403
Cdd:COG1408  222 RLGRKYVAGLYREGGTQLYVSRGLGTSGPPVRFGCPPEITLITLKSA 268
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 158-400 1.81e-58

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: 190.18  E-value: 1.81e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 158 GYRITQISDIHCGSFDKYEKIRYGVDLINSQKSDVILFTGDLVNNLANEVHNWKSLFATLQAPDGVFSIMGNHDY--GDY 235
Cdd:cd07385    1 GLRIVQLSDIHLGPFVGRTRLQKVVRKVNELNPDLIVITGDLVDGDVSVLRLLASPLSKLKAPLGVYFVLGNHDYysGDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 236 SSWetpeakqqnlehlFQLQKQMGWQLLLNEHCYLERNGEKIALIGVENWGHGRFSKygDLNKAMEGVNTEDFKILMSHD 315
Cdd:cd07385   81 EVW-------------IAALEKAGITVLRNESVELSRDGATIGLAGSGVDDIGGHGE--DLEKALKGLDENDPVILLAHN 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 316 PTHWQEIvlpENKDIQLTLSGHTHGMQcgIEIPGWLKWSPsqYIYKYWGGMYEEG-GKYLNVNRGFGYHAFPGRLGVWPE 394
Cdd:cd07385  146 PDAAEEA---QRPGVDLVLSGHTHGGQ--IFPPNYGVLSK--LGFPYDSGLYQIGgTTYLYVSRGLGTWGPPIRLGCPPE 218


                 ....*.
gi 736541038 395 ITVIEL 400
Cdd:cd07385  219 ITLITL 224
PRK11340 PRK11340
phosphodiesterase YaeI; Provisional
 159-400 6.84e-13

phosphodiesterase YaeI; Provisional


Pssm-ID: 236899  Cd Length: 271  Bit Score: 68.34  E-value: 6.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 159 YRITQISDIHCGSFDKYEKIRYGVDLINSQKSDVILFTGDLVnnLANEVHNWKSLFATLQ-----APdgVFSIMGNHD-- 231
Cdd:PRK11340  50 FKILFLADLHYSRFVPLSLISDAIALGIEQKPDLILLGGDYV--LFDMPLNFSAFSDVLSplaecAP--TFACFGNHDrp 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 232 YGDysswetpeakqqNLEHLFQ-LQKQMGWQLLLNEHCYLERNGEKIALIGVENWGHGRFSKYGDLNKAMEgvntedfKI 310
Cdd:PRK11340 126 VGT------------EKNHLIGeTLKSAGITVLFNQATVIATPNRQFELVGTGDLWAGQCKPPPASEANLP-------RL 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 311 LMSHDPTHwQEIVlpENKDIQLTLSGHTHGMQcgIEIPgwLKWSPSQYI--YKYWGGMYEEGGKYLNVNRGFGYhAFPGR 388
Cdd:PRK11340 187 VLAHNPDS-KEVM--RDEPWDLMLCGHTHGGQ--LRVP--LVGEPFAPVedKRYVAGLNAFGERQIYTTRGVGS-LYGLR 258

                        250
                 ....*....|..
gi 736541038 389 LGVWPEITVIEL 400
Cdd:PRK11340 259 LNCRPEVTMLEL 270
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 159-232 5.78e-08

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: 50.67  E-value: 5.78e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736541038  159 YRITQISDIHC-GSFDKYEKIrygVDLINSQKS-DVILFTGDLVNNLANEvHNWKSLFATLQAPDGVFSIMGNHDY 232
Cdd:pfam00149   1 MRILVIGDLHLpGQLDDLLEL---LKKLLEEGKpDLVLHAGDLVDRGPPS-EEVLELLERLIKYVPVYLVRGNHDF 72
 
Name Accession Description Interval E-value
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
117-403 1.75e-114

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 334.84  E-value: 1.75e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 117 LGWGLAAIPFASILYSIFKGKYNYKVWKYTLYFDNLPKAFDGYRITQISDIHCGSFDKYEKIRYGVDLINSQKSDVILFT 196
Cdd:COG1408    1 LALALLALGLALLAYGLYIEPRRLRVRRYTVPIPKLPPAFDGLRIVQLSDLHLGPFIGGERLERLVEKINALKPDLVVLT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 197 GDLVNNLANEVHNWKSLFATLQAPDGVFSIMGNHDYGDysswetpeakqqNLEHLFQLQKQMGWQLLLNEHCYLERNGEK 276
Cdd:COG1408   81 GDLVDGSVAELEALLELLKKLKAPLGVYAVLGNHDYYA------------GLEELRAALEEAGVRVLRNEAVTLERGGDR 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 277 IALIGVENWGHGRFskyGDLNKAMEGVNTEDFKILMSHDPTHWQEIVlpeNKDIQLTLSGHTHGMQCGIEIPGWLkWSPS 356
Cdd:COG1408  149 LNLAGVDDPHAGRF---PDLEKALAGVPPDAPRILLAHNPDVFDEAA---AAGVDLQLSGHTHGGQIRLPGIGAL-LTPV 221

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 736541038 357 QYIYKYWGGMYEEGGKYLNVNRGFGYHAFPGRLGVWPEITVIELKTK 403
Cdd:COG1408  222 RLGRKYVAGLYREGGTQLYVSRGLGTSGPPVRFGCPPEITLITLKSA 268
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 158-400 1.81e-58

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: 190.18  E-value: 1.81e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 158 GYRITQISDIHCGSFDKYEKIRYGVDLINSQKSDVILFTGDLVNNLANEVHNWKSLFATLQAPDGVFSIMGNHDY--GDY 235
Cdd:cd07385    1 GLRIVQLSDIHLGPFVGRTRLQKVVRKVNELNPDLIVITGDLVDGDVSVLRLLASPLSKLKAPLGVYFVLGNHDYysGDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 236 SSWetpeakqqnlehlFQLQKQMGWQLLLNEHCYLERNGEKIALIGVENWGHGRFSKygDLNKAMEGVNTEDFKILMSHD 315
Cdd:cd07385   81 EVW-------------IAALEKAGITVLRNESVELSRDGATIGLAGSGVDDIGGHGE--DLEKALKGLDENDPVILLAHN 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 316 PTHWQEIvlpENKDIQLTLSGHTHGMQcgIEIPGWLKWSPsqYIYKYWGGMYEEG-GKYLNVNRGFGYHAFPGRLGVWPE 394
Cdd:cd07385  146 PDAAEEA---QRPGVDLVLSGHTHGGQ--IFPPNYGVLSK--LGFPYDSGLYQIGgTTYLYVSRGLGTWGPPIRLGCPPE 218


                 ....*.
gi 736541038 395 ITVIEL 400
Cdd:cd07385  219 ITLITL 224
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
159-339 1.20e-14

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 72.80  E-value: 1.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 159 YRITQISDIHCGS---FDKYEKIRYGVDLINSQKSDVILFTGDLVNN-LANEVHNWKSLFATLQAPdgVFSIMGNHDYgd 234
Cdd:COG1409    1 FRFAHISDLHLGApdgSDTAEVLAAALADINAPRPDFVVVTGDLTDDgEPEEYAAAREILARLGVP--VYVVPGNHDI-- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 235 ysswetPEAKQQNLEHLFQLQKQMGWQlllnehcYLERNGEkIALIG----VENWGHGRFSKY------GDLNKAmegvn 304
Cdd:COG1409   77 ------RAAMAEAYREYFGDLPPGGLY-------YSFDYGG-VRFIGldsnVPGRSSGELGPEqlawleEELAAA----- 137

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 736541038 305 TEDFKILMSHDP----THWQEIVLPENKD----------IQLTLSGHTH 339
Cdd:COG1409  138 PAKPVIVFLHHPpystGSGSDRIGLRNAEellallarygVDLVLSGHVH 186
PRK11340 PRK11340
phosphodiesterase YaeI; Provisional
 159-400 6.84e-13

phosphodiesterase YaeI; Provisional


Pssm-ID: 236899  Cd Length: 271  Bit Score: 68.34  E-value: 6.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 159 YRITQISDIHCGSFDKYEKIRYGVDLINSQKSDVILFTGDLVnnLANEVHNWKSLFATLQ-----APdgVFSIMGNHD-- 231
Cdd:PRK11340  50 FKILFLADLHYSRFVPLSLISDAIALGIEQKPDLILLGGDYV--LFDMPLNFSAFSDVLSplaecAP--TFACFGNHDrp 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 232 YGDysswetpeakqqNLEHLFQ-LQKQMGWQLLLNEHCYLERNGEKIALIGVENWGHGRFSKYGDLNKAMEgvntedfKI 310
Cdd:PRK11340 126 VGT------------EKNHLIGeTLKSAGITVLFNQATVIATPNRQFELVGTGDLWAGQCKPPPASEANLP-------RL 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 311 LMSHDPTHwQEIVlpENKDIQLTLSGHTHGMQcgIEIPgwLKWSPSQYI--YKYWGGMYEEGGKYLNVNRGFGYhAFPGR 388
Cdd:PRK11340 187 VLAHNPDS-KEVM--RDEPWDLMLCGHTHGGQ--LRVP--LVGEPFAPVedKRYVAGLNAFGERQIYTTRGVGS-LYGLR 258

                        250
                 ....*....|..
gi 736541038 389 LGVWPEITVIEL 400
Cdd:PRK11340 259 LNCRPEVTMLEL 270
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 164-231 3.08e-09

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: 54.97  E-value: 3.08e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 736541038 164 ISDIHcGSFDKYEKIrYGVDLINSQKSDVILFTGDLVNNLANEVHNWKSLFATLQAPDGVFSIMGNHD 231
Cdd:cd00838    3 ISDIH-GNLEALEAV-LEAALAKAEKPDLVICLGDLVDYGPDPEEVELKALRLLLAGIPVYVVPGNHD 68
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 159-232 5.78e-08

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: 50.67  E-value: 5.78e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736541038  159 YRITQISDIHC-GSFDKYEKIrygVDLINSQKS-DVILFTGDLVNNLANEvHNWKSLFATLQAPDGVFSIMGNHDY 232
Cdd:pfam00149   1 MRILVIGDLHLpGQLDDLLEL---LKKLLEEGKpDLVLHAGDLVDRGPPS-EEVLELLERLIKYVPVYLVRGNHDF 72
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
164-339 3.09e-07

Predicted phosphodiesterase, calcineurin family [General function prediction only];


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 50.30  E-value: 3.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 164 ISDIHcGSFDKYEKIrygVDLINSQKSDVILFTGDLVNNLANEvhnwKSLFATLQApDGVFSIMGNHDYGDYsswetpea 243
Cdd:COG0622    5 ISDTH-GNLPALEAV---LEDLEREGVDLIVHLGDLVGYGPDP----PEVLDLLRE-LPIVAVRGNHDGAVL-------- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 244 kqQNLEHlfqlqkqmgwqllLNEHCYLERNGEKIALIgvenwgHGRFSKYGdlnkamegvntedfkilmshDPTHWQEIV 323
Cdd:COG0622   68 --RGLRS-------------LPETLRLELEGVRILLV------HGSPNEYL--------------------LPDTPAERL 106

                        170
                 ....*....|....*...
gi 736541038 324 --LPENKDIQLTLSGHTH 339
Cdd:COG0622  107 raLAAEGDADVVVCGHTH 124
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
160-339 6.54e-07

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 49.63  E-value: 6.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 160 RITQISDIHcGSFDKYEKIrygVDLINSQKSDVILFTGDLVNN-LANEVHNWKSLFATLQAPdgVFSIMGNHDYgdyssw 238
Cdd:COG2129    1 KILAVSDLH-GNFDLLEKL---LELARAEDADLVILAGDLTDFgTAEEAREVLEELAALGVP--VLAVPGNHDD------ 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 239 etpeakqqnlEHLFQLQKQMGWQLLLNEHCYLERngekIALIGVenwGHGRFSKYG--------DLNKAMEGVNTEDFKI 310
Cdd:COG2129   69 ----------PEVLDALEESGVHNLHGRVVEIGG----LRIAGL---GGSRPTPFGtpyeyteeEIEERLAKLREKDVDI 131

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 736541038 311 LMSHDPTHWQEIVLPEN---------------KDIQLTLSGHTH 339
Cdd:COG2129  132 LLTHAPPYGTTLDRVEDgphvgskalrelieeFQPKLVLHGHIH 175
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 161-232 1.59e-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: 1.59e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 736541038 161 ITQISDIHCGSFDKYEKIRY-GVDLINSQKSDVILFTGDLVNN-LANEVHNWKSLFATLQAPDgVFSIMGNHDY 232
Cdd:cd07400    1 IAHISDLHFGEERKPEVLELnLLDEINALKPDLVVVTGDLTQRaRPAEFEEAREFLDALEPEP-VVVVPGNHDA 73
UshA COG0737
2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family ...
 160-349 8.41e-06

2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms];


Pssm-ID: 440500 [Multi-domain]  Cd Length: 471  Bit Score: 47.54  E-value: 8.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 160 RITQISDIHC------GSFDKYEKiRYGVD----LINSQKS---DVILF-TGDLVNNlanevhnwkSLFATLQAPDGVFS 225
Cdd:COG0737    6 TILHTNDLHGhlepydYFDDKYGK-AGGLArlatLIKQLRAenpNTLLLdAGDTIQG---------SPLSTLTKGEPMIE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 226 IM----------GNHDYgDYSswetpeakqqnLEHLFQLQKQM-------------GWQLLLNEHCYLERNGEKIALIGV 282
Cdd:COG0737   76 AMnalgydaatlGNHEF-DYG-----------LDVLLELLDGAnfpvlsanvydkdTGEPLFKPYTIKEVGGVKVGVIGL 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 283 -----ENWGHGRFSK---YGDLNKAM---------EGVnteDFKILMSHDPTHWQEIVL-PENKDIQLTLSGHTH-GMQC 343
Cdd:COG0737  144 ttpdtPTWSSPGNIGgltFTDPVEAAqkyvdelraEGA---DVVVLLSHLGLDGEDRELaKEVPGIDVILGGHTHtLLPE 220


                 ....*.
gi 736541038 344 GIEIPG 349
Cdd:COG0737  221 PVVVNG 226
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 161-232 1.86e-05

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: 45.73  E-value: 1.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 161 ITQISDIH--------CGSFDKYEKIRYGVDLIN--SQKSDVILFTGDLVNN-LANEVHNWKSLFATLQAPdgVFSIMGN 229
Cdd:cd07402    1 IAQISDTHlfapgegaLLGVDTAARLAAAVAQVNalHPRPDLVVVTGDLSDDgSPESYERLRELLAPLPAP--VYWIPGN 78


                 ...
gi 736541038 230 HDY 232
Cdd:cd07402   79 HDD 81
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 160-257 9.59e-05

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: 43.03  E-value: 9.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 160 RITQISDIHCGS----FDKYEKIRYG-----VDLINSQKSDVILFTGDLVNnlanevHNWKSLFATLQAPDG-------- 222
Cdd:cd00840    1 RFLHTADWHLGYplygLSRREEDFFKafeeiVDLAIEEKVDFVLIAGDLFD------SNNPSPEALKLAIEGlrrlceag 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 736541038 223 --VFSIMGNHD-------YGD-YSSWETPEAKQQNLEHLFQLQKQ 257
Cdd:cd00840   75 ipVFVIAGNHDsparvaiYGLpYLRDERLERLFEDLELRPRLLKP 119
MPP_NostocDevT-like cd07397
Nostoc DevT and similar proteins, metallophosphatase domain; DevT (Alr4674) is a putative ...
 159-314 5.82e-04

Nostoc DevT and similar proteins, metallophosphatase domain; DevT (Alr4674) is a putative protein phosphatase from Nostoc PCC 7120 (Anabaena PCC 7120). DevT mutants form mature heterocysts, but they are unable to fix N(2) and must be supplied with a source of combined nitrogen in order to survive. Anabaena DevT shows homology to phosphatases of the PPP family and displays a Mn(2+)-dependent phosphatase activity. DevT is constitutively expressed in both vegetative cells and heterocysts, and is not regulated by NtcA. The heterocyst regulator HetR may exert a certain inhibition on the expression of devT. Under diazotrophic growth conditions, DevT protein accumulates specifically in mature heterocysts. The role that DevT plays in a late essential step of heterocyst differentiation is still unknown. 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: 277342 [Multi-domain]  Cd Length: 245  Bit Score: 41.12  E-value: 5.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 159 YRITQISDIHcGSFDKYEKirygvDLINSQKSDVILFTGDLVN---NLANEVhnwkslfATLQAPDGVfsIMGNHDYG-D 234
Cdd:cd07397    1 VRIAIVGDVH-GQWDAEDE-----RALRLLQPDLVLFVGDFGNenvQLVRRI-------ASLDLPKAV--ILGNHDAWyT 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 235 YSSWETPEAKQQNLEHlfqLQKQMgwQLLLNEHCYLER---NGEKIALIGV-------ENWGHGRF--SKYG-------- 294
Cdd:cd07397   66 ATRWGRCPYDRSKGDR---VQQQL--EILGDEHVGYGRldfPSLKLSVVGGrpfskggGRWLSKRFlsAVYGvisleesa 140

                        170       180
                 ....*....|....*....|.
gi 736541038 295 -DLNKAMEGVNTEDFKILMSH 314
Cdd:cd07397  141 qRIADAAKAAPEDHPLIFLAH 161
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 159-338 1.42e-03

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: 39.58  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 159 YRITQISDIHCGSFDKYEKIRYGVDL---------INSQKSDVILFTGDLVN----NLANEVHNWKSLFATLQAPDGVF- 224
Cdd:cd07383    3 FKILQFADLHFGEGEWTCWEGCEADLktvefiesvLDEEKPDLVVLTGDLITgentADDNATSYLDKAVSPLVERGIPWa 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 225 SIMGNHDYGDY---SSWETPEAKQQNLEHLFQL-QKQMGWQ---------LLLNEHCYLERNGEKIALIGVENWGhgrFS 291
Cdd:cd07383   83 ATFGNHDGYDWidpSQVEWFESTSAALKKKYGKnIPSLAFFhiplpeyreVWNEKGKLGGINREKVCCQKTNSGF---FK 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 736541038 292 KYgdlnkamegVNTEDFK-ILMSHDptHWQEIVLPENKDIQLTLSGHT 338
Cdd:cd07383  160 AL---------VKRGDVKaVFCGHD--HGNDFCGRWKNGIWLCYGRHT 196
MPP_TMEM62_N cd07401
Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) ...
 161-339 2.88e-03

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: 39.27  E-value: 2.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 161 ITQISDIHCGSFDKYEKIRYG---VDLINSQKSDVILFTGDLVNNL-------ANEVHNWKS-LFATLQAPDGV-----F 224
Cdd:cd07401    2 FVHLTDIHVSSFHDPNRIQDEtfcSNFIDVIKPTLVLITGDLTDNKtgnklpsYQYQEEWQWkYYNILKESSVInkeylF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736541038 225 SIMGNHDYGDYSSWETpeakQQNLEHLFQLQKQMGwqlllNEHCYLERNGEKIALIGV----ENWGHGRFSKYGDLNKAM 300
Cdd:cd07401   82 DIRGNHDLFGIVSFDS----QNNYYRKYSNTGRDH-----SHSFSSTTRFGNYSFIGFdptiFPGPKRPFNFFGSLDKKL 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736541038 301 --------EGVNTEDFKILMSHDPThwqEIVLPENK--------------DIQLTLSGHTH 339
Cdd:cd07401  153 ldrlekelEKSKNSKYTIWFGHYPH---SLIISPSAksssktfkdllkkyNVTAYLCGHLH 210
 
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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