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Conserved domains on  [gi|1370467303|ref|XP_024305840|]
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transmembrane protein 62 isoform X7 [Homo sapiens]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 10164708)

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_TMEM62_N cd07401
Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) ...
 57-341 3.01e-108

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: 317.39  E-value: 3.01e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370467303  57 WGLQISDIHLSRFRDPGRAVDlEKFCSETIDIIQPALVLATGDLTDAKTKEQLGSRQHEVEWQ-TYQGILKKTRVMEKTK 135
Cdd:cd07401     1 WFVHLTDIHVSSFHDPNRIQD-ETFCSNFIDVIKPTLVLITGDLTDNKTGNKLPSYQYQEEWQwKYYNILKESSVINKEY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370467303 136 WLDIKGNHDAFNIPSLDSIKNYYRKYSAVRRDGSFHYVHSTPFGNYSFICVDATVNPGPKRPYNFFGILDKKKMEELLLL 215
Cdd:cd07401    80 LFDIRGNHDLFGIVSFDSQNNYYRKYSNTGRDHSHSFSSTTRFGNYSFIGFDPTIFPGPKRPFNFFGSLDKKLLDRLEKE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370467303 216 AKESSRSNHTIWFGHFTTSTILSPSPGI-------RSIMSSAIAYLCGHLHTLGGlMPVLHTRHfqgtlelevgdwkdnr 288
Cdd:cd07401   160 LEKSKNSKYTIWFGHYPHSLIISPSAKSssktfkdLLKKYNVTAYLCGHLHPLGG-EPVHYAGH---------------- 222

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370467303 289 ryrifafdhdlfsfadlifgkwPVVLITNPKSLLYSCGehePLERLLHSTHIR 341
Cdd:cd07401   223 ----------------------PIAIITNPKPSHLLAP---PSNFNDKSTHIR 250
 
Name Accession Description Interval E-value
MPP_TMEM62_N cd07401
Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) ...
 57-341 3.01e-108

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: 317.39  E-value: 3.01e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370467303  57 WGLQISDIHLSRFRDPGRAVDlEKFCSETIDIIQPALVLATGDLTDAKTKEQLGSRQHEVEWQ-TYQGILKKTRVMEKTK 135
Cdd:cd07401     1 WFVHLTDIHVSSFHDPNRIQD-ETFCSNFIDVIKPTLVLITGDLTDNKTGNKLPSYQYQEEWQwKYYNILKESSVINKEY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370467303 136 WLDIKGNHDAFNIPSLDSIKNYYRKYSAVRRDGSFHYVHSTPFGNYSFICVDATVNPGPKRPYNFFGILDKKKMEELLLL 215
Cdd:cd07401    80 LFDIRGNHDLFGIVSFDSQNNYYRKYSNTGRDHSHSFSSTTRFGNYSFIGFDPTIFPGPKRPFNFFGSLDKKLLDRLEKE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370467303 216 AKESSRSNHTIWFGHFTTSTILSPSPGI-------RSIMSSAIAYLCGHLHTLGGlMPVLHTRHfqgtlelevgdwkdnr 288
Cdd:cd07401   160 LEKSKNSKYTIWFGHYPHSLIISPSAKSssktfkdLLKKYNVTAYLCGHLHPLGG-EPVHYAGH---------------- 222

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370467303 289 ryrifafdhdlfsfadlifgkwPVVLITNPKSLLYSCGehePLERLLHSTHIR 341
Cdd:cd07401   223 ----------------------PIAIITNPKPSHLLAP---PSNFNDKSTHIR 250
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
59-298 7.49e-13

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 67.41  E-value: 7.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370467303  59 LQISDIHLSRFRDPGRAVDLEKFCSEtIDIIQPALVLATGDLTDAKTKEqlgsrqhevEWQTYQGILKKTRVmektKWLD 138
Cdd:COG1409     4 AHISDLHLGAPDGSDTAEVLAAALAD-INAPRPDFVVVTGDLTDDGEPE---------EYAAAREILARLGV----PVYV 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370467303 139 IKGNHDAFNIPSldsikNYYRKYSAVRRDGSFHYVHStpFGNYSFICVDATVnpgpkrPYNFFGILDKkkmEELLLLAKE 218
Cdd:COG1409    70 VPGNHDIRAAMA-----EAYREYFGDLPPGGLYYSFD--YGGVRFIGLDSNV------PGRSSGELGP---EQLAWLEEE 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370467303 219 --SSRSNHTIWFGHFTTSTILSPSPGIRSIMSSAI----------AYLCGHLHtlgglmpVLHTRHFQGTLELEVG---- 282
Cdd:COG1409   134 laAAPAKPVIVFLHHPPYSTGSGSDRIGLRNAEELlallarygvdLVLSGHVH-------RYERTRRDGVPYIVAGstgg 206

                         250
                  ....*....|....*.
gi 1370467303 283 DWKDNRRYRIFAFDHD 298
Cdd:COG1409   207 QVRLPPGYRVIEVDGD 222
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 59-159 6.38e-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: 36.04  E-value: 6.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370467303  59 LQISDIHLsrfrdPGRAVDLEKFCSETIDIIQPALVLATGDLTDaktkeqlgsrqHEVEWQTYQGILKktRVMEKTKWLD 138
Cdd:pfam00149   4 LVIGDLHL-----PGQLDDLLELLKKLLEEGKPDLVLHAGDLVD-----------RGPPSEEVLELLE--RLIKYVPVYL 65

                          90       100
                  ....*....|....*....|.
gi 1370467303 139 IKGNHDAFNIPSLDSIKNYYR 159
Cdd:pfam00149  66 VRGNHDFDYGECLRLYPYLGL 86
 
Name Accession Description Interval E-value
MPP_TMEM62_N cd07401
Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) ...
 57-341 3.01e-108

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: 317.39  E-value: 3.01e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370467303  57 WGLQISDIHLSRFRDPGRAVDlEKFCSETIDIIQPALVLATGDLTDAKTKEQLGSRQHEVEWQ-TYQGILKKTRVMEKTK 135
Cdd:cd07401     1 WFVHLTDIHVSSFHDPNRIQD-ETFCSNFIDVIKPTLVLITGDLTDNKTGNKLPSYQYQEEWQwKYYNILKESSVINKEY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370467303 136 WLDIKGNHDAFNIPSLDSIKNYYRKYSAVRRDGSFHYVHSTPFGNYSFICVDATVNPGPKRPYNFFGILDKKKMEELLLL 215
Cdd:cd07401    80 LFDIRGNHDLFGIVSFDSQNNYYRKYSNTGRDHSHSFSSTTRFGNYSFIGFDPTIFPGPKRPFNFFGSLDKKLLDRLEKE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370467303 216 AKESSRSNHTIWFGHFTTSTILSPSPGI-------RSIMSSAIAYLCGHLHTLGGlMPVLHTRHfqgtlelevgdwkdnr 288
Cdd:cd07401   160 LEKSKNSKYTIWFGHYPHSLIISPSAKSssktfkdLLKKYNVTAYLCGHLHPLGG-EPVHYAGH---------------- 222

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370467303 289 ryrifafdhdlfsfadlifgkwPVVLITNPKSLLYSCGehePLERLLHSTHIR 341
Cdd:cd07401   223 ----------------------PIAIITNPKPSHLLAP---PSNFNDKSTHIR 250
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
59-298 7.49e-13

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 67.41  E-value: 7.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370467303  59 LQISDIHLSRFRDPGRAVDLEKFCSEtIDIIQPALVLATGDLTDAKTKEqlgsrqhevEWQTYQGILKKTRVmektKWLD 138
Cdd:COG1409     4 AHISDLHLGAPDGSDTAEVLAAALAD-INAPRPDFVVVTGDLTDDGEPE---------EYAAAREILARLGV----PVYV 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370467303 139 IKGNHDAFNIPSldsikNYYRKYSAVRRDGSFHYVHStpFGNYSFICVDATVnpgpkrPYNFFGILDKkkmEELLLLAKE 218
Cdd:COG1409    70 VPGNHDIRAAMA-----EAYREYFGDLPPGGLYYSFD--YGGVRFIGLDSNV------PGRSSGELGP---EQLAWLEEE 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370467303 219 --SSRSNHTIWFGHFTTSTILSPSPGIRSIMSSAI----------AYLCGHLHtlgglmpVLHTRHFQGTLELEVG---- 282
Cdd:COG1409   134 laAAPAKPVIVFLHHPPYSTGSGSDRIGLRNAEELlallarygvdLVLSGHVH-------RYERTRRDGVPYIVAGstgg 206

                         250
                  ....*....|....*.
gi 1370467303 283 DWKDNRRYRIFAFDHD 298
Cdd:COG1409   207 QVRLPPGYRVIEVDGD 222
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 59-145 8.33e-04

Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277345 [Multi-domain]  Cd Length: 138  Bit Score: 39.20  E-value: 8.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370467303  59 LQISDIHLSRFRDPgraVDLEKFCSETIDIIQPALVLATGDLTDaktkeqlgsRQHEVEWQTYQGILKKtrvMEKTKWLD 138
Cdd:cd07400     2 AHISDLHFGEERKP---EVLELNLLDEINALKPDLVVVTGDLTQ---------RARPAEFEEAREFLDA---LEPEPVVV 66


                  ....*..
gi 1370467303 139 IKGNHDA 145
Cdd:cd07400    67 VPGNHDA 73
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 59-259 3.60e-03

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: 38.41  E-value: 3.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370467303  59 LQISDIHL-SRFRDPGRAVDLEKFCSETIDII-----QPALVLATGDLTDaktkeqlgsRQHEVEWQTYQGILKKTRVme 132
Cdd:cd07402     2 AQISDTHLfAPGEGALLGVDTAARLAAAVAQVnalhpRPDLVVVTGDLSD---------DGSPESYERLRELLAPLPA-- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370467303 133 KTKWldIKGNHD-------AFNIPSLDSiknyyrkysavrrDGSFHYVHstPFGNYSFICVDATVNPGPKrpynffGILD 205
Cdd:cd07402    71 PVYW--IPGNHDdraamreALPEPPYDD-------------NGPVQYVV--DFGGWRLILLDTSVPGVHH------GELS 127

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370467303 206 KKKMeELLLLAKESSRSNHTIWFGH---FTTS----------------TILSPSPGIRSImssaiayLCGHLH 259
Cdd:cd07402   128 DEQL-DWLEAALAEAPDRPTLIFLHhppFPLGipwmdairlrnsqalfAVLARHPQVKAI-------LCGHIH 192
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
59-107 5.13e-03

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 38.24  E-value: 5.13e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1370467303  59 LQISDIHLSRFRDPGRavdLEKFCsETIDIIQPALVLATGDLTDAKTKE 107
Cdd:COG1408    46 VQLSDLHLGPFIGGER---LERLV-EKINALKPDLVVLTGDLVDGSVAE 90
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 59-159 6.38e-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: 36.04  E-value: 6.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370467303  59 LQISDIHLsrfrdPGRAVDLEKFCSETIDIIQPALVLATGDLTDaktkeqlgsrqHEVEWQTYQGILKktRVMEKTKWLD 138
Cdd:pfam00149   4 LVIGDLHL-----PGQLDDLLELLKKLLEEGKPDLVLHAGDLVD-----------RGPPSEEVLELLE--RLIKYVPVYL 65

                          90       100
                  ....*....|....*....|.
gi 1370467303 139 IKGNHDAFNIPSLDSIKNYYR 159
Cdd:pfam00149  66 VRGNHDFDYGECLRLYPYLGL 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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