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Conserved domains on  [gi|52851437|ref|NP_079232|]
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transmembrane protein 62 isoform a [Homo sapiens]

Protein Classification

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) ...
 57-345 4.04e-105

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: 318.93  E-value: 4.04e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52851437  57 WGLQISDIHLSRFRDPGRAVDlEKFCSETIDIIQPALVLATGDLTDAKTKEQLGSRQHEVEWQ-TYQGILKKTRVMEKTK 135
Cdd:cd07401   1 WFVHLTDIHVSSFHDPNRIQD-ETFCSNFIDVIKPTLVLITGDLTDNKTGNKLPSYQYQEEWQwKYYNILKESSVINKEY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52851437 136 WLDIKGNHDAFNIPSLDSIKNYYRKYSAVRRDGSFHYVHSTPFGNYSFICVDATVNPGPKRPYNFFGILDKKKMEELLLL 215
Cdd:cd07401  80 LFDIRGNHDLFGIVSFDSQNNYYRKYSNTGRDHSHSFSSTTRFGNYSFIGFDPTIFPGPKRPFNFFGSLDKKLLDRLEKE 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52851437 216 AKESSRSNHTIWFGHFTTSTILSPSPGI-------RSIMSSAIAYLCGHLHTLGGlMPVLHTRHfqgtlelevgdwkdnr 288
Cdd:cd07401 160 LEKSKNSKYTIWFGHYPHSLIISPSAKSssktfkdLLKKYNVTAYLCGHLHPLGG-EPVHYAGH---------------- 222

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 52851437 289 ryrifafdhdlfsfadlifgkwPVVLITNPKSLLYSCGehePLERLLHSTHIRVLAF 345
Cdd:cd07401 223 ----------------------PIAIITNPKPSHLLAP---PSNFNDKSTHIRVLSF 254
Big_7 pfam17957
Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in ...
 340-391 1.36e-04

Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in glycosyl hydrolase enzymes.


:

Pssm-ID: 436171 [Multi-domain]  Cd Length: 67  Bit Score: 40.28  E-value: 1.36e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 52851437   340 IRVLAFSLSSITSVTVKIDGVHLGQAVhvSGPiFVLKWNPRNYSSGTHNIEV 391
Cdd:pfam17957  19 ISATASDDGGVSKVEFYVDGTLVGTDT--SAP-YSFTWTTTALANGTHTITV 67
 
Name Accession Description Interval E-value
MPP_TMEM62_N cd07401
Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) ...
 57-345 4.04e-105

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: 318.93  E-value: 4.04e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52851437  57 WGLQISDIHLSRFRDPGRAVDlEKFCSETIDIIQPALVLATGDLTDAKTKEQLGSRQHEVEWQ-TYQGILKKTRVMEKTK 135
Cdd:cd07401   1 WFVHLTDIHVSSFHDPNRIQD-ETFCSNFIDVIKPTLVLITGDLTDNKTGNKLPSYQYQEEWQwKYYNILKESSVINKEY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52851437 136 WLDIKGNHDAFNIPSLDSIKNYYRKYSAVRRDGSFHYVHSTPFGNYSFICVDATVNPGPKRPYNFFGILDKKKMEELLLL 215
Cdd:cd07401  80 LFDIRGNHDLFGIVSFDSQNNYYRKYSNTGRDHSHSFSSTTRFGNYSFIGFDPTIFPGPKRPFNFFGSLDKKLLDRLEKE 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52851437 216 AKESSRSNHTIWFGHFTTSTILSPSPGI-------RSIMSSAIAYLCGHLHTLGGlMPVLHTRHfqgtlelevgdwkdnr 288
Cdd:cd07401 160 LEKSKNSKYTIWFGHYPHSLIISPSAKSssktfkdLLKKYNVTAYLCGHLHPLGG-EPVHYAGH---------------- 222

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 52851437 289 ryrifafdhdlfsfadlifgkwPVVLITNPKSLLYSCGehePLERLLHSTHIRVLAF 345
Cdd:cd07401 223 ----------------------PIAIITNPKPSHLLAP---PSNFNDKSTHIRVLSF 254
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
59-298 1.88e-12

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 67.41  E-value: 1.88e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52851437  59 LQISDIHLSRFRDPGRAVDLEKFCSEtIDIIQPALVLATGDLTDAKTKEqlgsrqhevEWQTYQGILKKTRVmektKWLD 138
Cdd:COG1409   4 AHISDLHLGAPDGSDTAEVLAAALAD-INAPRPDFVVVTGDLTDDGEPE---------EYAAAREILARLGV----PVYV 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52851437 139 IKGNHDAFNIPSldsikNYYRKYSAVRRDGSFHYVHStpFGNYSFICVDATVnpgpkrPYNFFGILDKkkmEELLLLAKE 218
Cdd:COG1409  70 VPGNHDIRAAMA-----EAYREYFGDLPPGGLYYSFD--YGGVRFIGLDSNV------PGRSSGELGP---EQLAWLEEE 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52851437 219 --SSRSNHTIWFGHFTTSTILSPSPGIRSIMSSAI----------AYLCGHLHtlgglmpVLHTRHFQGTLELEVG---- 282
Cdd:COG1409 134 laAAPAKPVIVFLHHPPYSTGSGSDRIGLRNAEELlallarygvdLVLSGHVH-------RYERTRRDGVPYIVAGstgg 206

                       250
                ....*....|....*.
gi 52851437 283 DWKDNRRYRIFAFDHD 298
Cdd:COG1409 207 QVRLPPGYRVIEVDGD 222
Big_7 pfam17957
Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in ...
 340-391 1.36e-04

Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in glycosyl hydrolase enzymes.


Pssm-ID: 436171 [Multi-domain]  Cd Length: 67  Bit Score: 40.28  E-value: 1.36e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 52851437   340 IRVLAFSLSSITSVTVKIDGVHLGQAVhvSGPiFVLKWNPRNYSSGTHNIEV 391
Cdd:pfam17957  19 ISATASDDGGVSKVEFYVDGTLVGTDT--SAP-YSFTWTTTALANGTHTITV 67
 
Name Accession Description Interval E-value
MPP_TMEM62_N cd07401
Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) ...
 57-345 4.04e-105

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: 318.93  E-value: 4.04e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52851437  57 WGLQISDIHLSRFRDPGRAVDlEKFCSETIDIIQPALVLATGDLTDAKTKEQLGSRQHEVEWQ-TYQGILKKTRVMEKTK 135
Cdd:cd07401   1 WFVHLTDIHVSSFHDPNRIQD-ETFCSNFIDVIKPTLVLITGDLTDNKTGNKLPSYQYQEEWQwKYYNILKESSVINKEY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52851437 136 WLDIKGNHDAFNIPSLDSIKNYYRKYSAVRRDGSFHYVHSTPFGNYSFICVDATVNPGPKRPYNFFGILDKKKMEELLLL 215
Cdd:cd07401  80 LFDIRGNHDLFGIVSFDSQNNYYRKYSNTGRDHSHSFSSTTRFGNYSFIGFDPTIFPGPKRPFNFFGSLDKKLLDRLEKE 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52851437 216 AKESSRSNHTIWFGHFTTSTILSPSPGI-------RSIMSSAIAYLCGHLHTLGGlMPVLHTRHfqgtlelevgdwkdnr 288
Cdd:cd07401 160 LEKSKNSKYTIWFGHYPHSLIISPSAKSssktfkdLLKKYNVTAYLCGHLHPLGG-EPVHYAGH---------------- 222

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 52851437 289 ryrifafdhdlfsfadlifgkwPVVLITNPKSLLYSCGehePLERLLHSTHIRVLAF 345
Cdd:cd07401 223 ----------------------PIAIITNPKPSHLLAP---PSNFNDKSTHIRVLSF 254
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
59-298 1.88e-12

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 67.41  E-value: 1.88e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52851437  59 LQISDIHLSRFRDPGRAVDLEKFCSEtIDIIQPALVLATGDLTDAKTKEqlgsrqhevEWQTYQGILKKTRVmektKWLD 138
Cdd:COG1409   4 AHISDLHLGAPDGSDTAEVLAAALAD-INAPRPDFVVVTGDLTDDGEPE---------EYAAAREILARLGV----PVYV 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52851437 139 IKGNHDAFNIPSldsikNYYRKYSAVRRDGSFHYVHStpFGNYSFICVDATVnpgpkrPYNFFGILDKkkmEELLLLAKE 218
Cdd:COG1409  70 VPGNHDIRAAMA-----EAYREYFGDLPPGGLYYSFD--YGGVRFIGLDSNV------PGRSSGELGP---EQLAWLEEE 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52851437 219 --SSRSNHTIWFGHFTTSTILSPSPGIRSIMSSAI----------AYLCGHLHtlgglmpVLHTRHFQGTLELEVG---- 282
Cdd:COG1409 134 laAAPAKPVIVFLHHPPYSTGSGSDRIGLRNAEELlallarygvdLVLSGHVH-------RYERTRRDGVPYIVAGstgg 206

                       250
                ....*....|....*.
gi 52851437 283 DWKDNRRYRIFAFDHD 298
Cdd:COG1409 207 QVRLPPGYRVIEVDGD 222
Big_7 pfam17957
Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in ...
 340-391 1.36e-04

Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in glycosyl hydrolase enzymes.


Pssm-ID: 436171 [Multi-domain]  Cd Length: 67  Bit Score: 40.28  E-value: 1.36e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 52851437   340 IRVLAFSLSSITSVTVKIDGVHLGQAVhvSGPiFVLKWNPRNYSSGTHNIEV 391
Cdd:pfam17957  19 ISATASDDGGVSKVEFYVDGTLVGTDT--SAP-YSFTWTTTALANGTHTITV 67
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 59-145 1.29e-03

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


Pssm-ID: 277345 [Multi-domain]  Cd Length: 138  Bit Score: 39.58  E-value: 1.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52851437  59 LQISDIHLSRFRDPgraVDLEKFCSETIDIIQPALVLATGDLTDaktkeqlgsRQHEVEWQTYQGILKKtrvMEKTKWLD 138
Cdd:cd07400   2 AHISDLHFGEERKP---EVLELNLLDEINALKPDLVVVTGDLTQ---------RARPAEFEEAREFLDA---LEPEPVVV 66


                ....*..
gi 52851437 139 IKGNHDA 145
Cdd:cd07400  67 VPGNHDA 73
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 59-259 3.51e-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: 39.57  E-value: 3.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52851437  59 LQISDIHL-SRFRDPGRAVDLEKFCSETIDII-----QPALVLATGDLTDaktkeqlgsRQHEVEWQTYQGILKKTRVme 132
Cdd:cd07402   2 AQISDTHLfAPGEGALLGVDTAARLAAAVAQVnalhpRPDLVVVTGDLSD---------DGSPESYERLRELLAPLPA-- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52851437 133 KTKWldIKGNHD-------AFNIPSLDSiknyyrkysavrrDGSFHYVHstPFGNYSFICVDATVNPGPKrpynffGILD 205
Cdd:cd07402  71 PVYW--IPGNHDdraamreALPEPPYDD-------------NGPVQYVV--DFGGWRLILLDTSVPGVHH------GELS 127

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52851437 206 KKKMeELLLLAKESSRSNHTIWFGH---FTTS----------------TILSPSPGIRSImssaiayLCGHLH 259
Cdd:cd07402 128 DEQL-DWLEAALAEAPDRPTLIFLHhppFPLGipwmdairlrnsqalfAVLARHPQVKAI-------LCGHIH 192
 
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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