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Conserved domains on  [gi|1720401347|ref|XP_030108119|]
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transmembrane protein 62 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_superfamily super family cl13995
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 28-213 3.91e-43

metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also known as metallophosphoesterases, phosphodiesterases (PDEs), binuclear metallophosphoesterases, and dimetal-containing phosphoesterases (DMPs), represent a diverse superfamily of enzymes with a conserved domain containing an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. This superfamily includes: the phosphoprotein phosphatases (PPPs), Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


The actual alignment was detected with superfamily member cd07401:

Pssm-ID: 472684 [Multi-domain]  Cd Length: 254  Bit Score: 153.68  E-value: 3.91e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401347  28 KYSAVRKDGAFHHIHSTPFGNYSFISVDATQRPGPKRPYNFFGILDEKQMEELVEFSKKSSQSNQTIWFGHFTTSTIMSP 107
Cdd:cd07401   104 KYSNTGRDHSHSFSSTTRFGNYSFIGFDPTIFPGPKRPFNFFGSLDKKLLDRLEKELEKSKNSKYTIWFGHYPHSLIISP 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401347 108 SPGI-------RTVMGSATAYLCGHLHTLGGlMPVLHTRHftgtlelevgdwkdnrryrifafdhdlfsfadvtfdkwPV 180
Cdd:cd07401   184 SAKSssktfkdLLKKYNVTAYLCGHLHPLGG-EPVHYAGH--------------------------------------PI 224

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1720401347 181 VLITNPKSLLYSCakhEPLERLFHSTHIRVLAF 213
Cdd:cd07401   225 AIITNPKPSHLLA---PPSNFNDKSTHIRVLSF 254
Big_7 pfam17957
Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in ...
 208-259 2.61e-06

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: 44.91  E-value: 2.61e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720401347 208 IRVLAFSLSPITSVTVKIDGGDIGQAShlSGPiFILKWNPRNYSNGTHTIEV 259
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) ...
 28-213 3.91e-43

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: 153.68  E-value: 3.91e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401347  28 KYSAVRKDGAFHHIHSTPFGNYSFISVDATQRPGPKRPYNFFGILDEKQMEELVEFSKKSSQSNQTIWFGHFTTSTIMSP 107
Cdd:cd07401   104 KYSNTGRDHSHSFSSTTRFGNYSFIGFDPTIFPGPKRPFNFFGSLDKKLLDRLEKELEKSKNSKYTIWFGHYPHSLIISP 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401347 108 SPGI-------RTVMGSATAYLCGHLHTLGGlMPVLHTRHftgtlelevgdwkdnrryrifafdhdlfsfadvtfdkwPV 180
Cdd:cd07401   184 SAKSssktfkdLLKKYNVTAYLCGHLHPLGG-EPVHYAGH--------------------------------------PI 224

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1720401347 181 VLITNPKSLLYSCakhEPLERLFHSTHIRVLAF 213
Cdd:cd07401   225 AIITNPKPSHLLA---PPSNFNDKSTHIRVLSF 254
Big_7 pfam17957
Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in ...
 208-259 2.61e-06

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: 44.91  E-value: 2.61e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720401347 208 IRVLAFSLSPITSVTVKIDGGDIGQAShlSGPiFILKWNPRNYSNGTHTIEV 259
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) ...
 28-213 3.91e-43

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: 153.68  E-value: 3.91e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401347  28 KYSAVRKDGAFHHIHSTPFGNYSFISVDATQRPGPKRPYNFFGILDEKQMEELVEFSKKSSQSNQTIWFGHFTTSTIMSP 107
Cdd:cd07401   104 KYSNTGRDHSHSFSSTTRFGNYSFIGFDPTIFPGPKRPFNFFGSLDKKLLDRLEKELEKSKNSKYTIWFGHYPHSLIISP 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401347 108 SPGI-------RTVMGSATAYLCGHLHTLGGlMPVLHTRHftgtlelevgdwkdnrryrifafdhdlfsfadvtfdkwPV 180
Cdd:cd07401   184 SAKSssktfkdLLKKYNVTAYLCGHLHPLGG-EPVHYAGH--------------------------------------PI 224

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1720401347 181 VLITNPKSLLYSCakhEPLERLFHSTHIRVLAF 213
Cdd:cd07401   225 AIITNPKPSHLLA---PPSNFNDKSTHIRVLSF 254
Big_7 pfam17957
Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in ...
 208-259 2.61e-06

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: 44.91  E-value: 2.61e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720401347 208 IRVLAFSLSPITSVTVKIDGGDIGQAShlSGPiFILKWNPRNYSNGTHTIEV 259
Cdd:pfam17957  19 ISATASDDGGVSKVEFYVDGTLVGTDT--SAP-YSFTWTTTALANGTHTITV 67
 
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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