NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1015186530|ref|NP_001308952|]
View 

tartrate-resistant acid phosphatase type 5 precursor [Homo sapiens]

Protein Classification

purple acid phosphatase family protein( domain architecture ID 10164501)

purple acid phosphatase (PAP) family protein is a metallophosphatase containing an active site consisting of two metal ions (usually manganese, iron, or zinc); similar to human tartrate-resistant acid phosphatase type 5 (ACP5) which is involved in osteopontin/bone sialoprotein dephosphorylation in bone matrix

CATH:  3.60.21.10
EC:  3.1.3.2
Gene Ontology:  GO:0046872|GO:0016311|GO:0003993
PubMed:  25837850|8683579|8003970

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 26-311 2.95e-163

Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid phosphatase 5 (ACP5) removes the mannose 6-phosphate recognition marker from lysosomal proteins. The exact site of dephosphorylation is not clear. Evidence suggests dephosphorylation may take place in a prelysosomal compartment as well as in the lysosome. ACP5 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: 277324 [Multi-domain]  Cd Length: 286  Bit Score: 456.40  E-value: 2.95e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530  26 LRFVAVGDWGGVPNaPFHTAREMANAKEIARTVQILGADFILSLGDNFYFTGVQDINDKRFQETFEDVFSDRSLRkVPWY 105
Cdd:cd07378     1 LRFLVLGDWGGKPN-PYTTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSLQ-VPWY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530 106 VLAGNHDHLGNVSAQIAYSKI--SKRWNFPSPFYRLHFKIPQTNVSVAIFMLDTVTLCGNSDDFLSQQPERPRDVKLART 183
Cdd:cd07378    79 LVLGNHDHRGNVSAQIAYTQRpnSKRWNFPNYYYDISFKFPSSDVTVAFIMIDTVLLCGNTDDEASGQPRGPPNKKLAET 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530 184 QLSWLKKQLAAAREDYVLVAGHYPVWSIAEHGPTHCLVKQLRPLLATYGVTAYLCGHDHNLQYLQDENGVGYVLSGAGNF 263
Cdd:cd07378   159 QLAWLEKQLAASKADYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVDESGTYYVISGAGSK 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1015186530 264 MDPSKRHQRKVPNGYLRFHYGTEDSLGGFAYVEISSKEMTVTYIEASG 311
Cdd:cd07378   239 ADPSDIHRDKVPQGYLLFFSGFYSSGGGFAYLEITSSELVIRFVDSDG 286
 
Name Accession Description Interval E-value
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 26-311 2.95e-163

Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid phosphatase 5 (ACP5) removes the mannose 6-phosphate recognition marker from lysosomal proteins. The exact site of dephosphorylation is not clear. Evidence suggests dephosphorylation may take place in a prelysosomal compartment as well as in the lysosome. ACP5 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: 277324 [Multi-domain]  Cd Length: 286  Bit Score: 456.40  E-value: 2.95e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530  26 LRFVAVGDWGGVPNaPFHTAREMANAKEIARTVQILGADFILSLGDNFYFTGVQDINDKRFQETFEDVFSDRSLRkVPWY 105
Cdd:cd07378     1 LRFLVLGDWGGKPN-PYTTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSLQ-VPWY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530 106 VLAGNHDHLGNVSAQIAYSKI--SKRWNFPSPFYRLHFKIPQTNVSVAIFMLDTVTLCGNSDDFLSQQPERPRDVKLART 183
Cdd:cd07378    79 LVLGNHDHRGNVSAQIAYTQRpnSKRWNFPNYYYDISFKFPSSDVTVAFIMIDTVLLCGNTDDEASGQPRGPPNKKLAET 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530 184 QLSWLKKQLAAAREDYVLVAGHYPVWSIAEHGPTHCLVKQLRPLLATYGVTAYLCGHDHNLQYLQDENGVGYVLSGAGNF 263
Cdd:cd07378   159 QLAWLEKQLAASKADYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVDESGTYYVISGAGSK 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1015186530 264 MDPSKRHQRKVPNGYLRFHYGTEDSLGGFAYVEISSKEMTVTYIEASG 311
Cdd:cd07378   239 ADPSDIHRDKVPQGYLLFFSGFYSSGGGFAYLEITSSELVIRFVDSDG 286
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
26-286 4.36e-27

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 106.31  E-value: 4.36e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530  26 LRFVAVGDWGGVPNAPFHTAREMANAkeiARTVQILGADFILSLGDNFYFTGVQDIndKRFQETFEDVfsdrslrKVPWY 105
Cdd:COG1409     1 FRFAHISDLHLGAPDGSDTAEVLAAA---LADINAPRPDFVVVTGDLTDDGEPEEY--AAAREILARL-------GVPVY 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530 106 VLAGNHDHlgnvsaqiayskiskrWNFPSPFYRLHFKIPQTNVS--------VAIFMLDTVTLCGNSDDflsqqperprd 177
Cdd:COG1409    69 VVPGNHDI----------------RAAMAEAYREYFGDLPPGGLyysfdyggVRFIGLDSNVPGRSSGE----------- 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530 178 vkLARTQLSWLKKQLAAAREDYVLVAGHYPVWSIAEHGPTHCLV--KQLRPLLATYGVTAYLCGHDHNlQYLQDENGVGY 255
Cdd:COG1409   122 --LGPEQLAWLEEELAAAPAKPVIVFLHHPPYSTGSGSDRIGLRnaEELLALLARYGVDLVLSGHVHR-YERTRRDGVPY 198

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1015186530 256 VLSGAGNfmdpskrHQRKVPNGYLRFHYGTE 286
Cdd:COG1409   199 IVAGSTG-------GQVRLPPGYRVIEVDGD 222
PTZ00422 PTZ00422
glideosome-associated protein 50; Provisional
 26-325 3.15e-19

glideosome-associated protein 50; Provisional


Pssm-ID: 185607 [Multi-domain]  Cd Length: 394  Bit Score: 87.19  E-value: 3.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530  26 LRFVAVGDWGGVPNApfhtarEMANAKEIARTVQILGADFILSLGDNFyFTGVQDINDKRFQETFEDVFSDRS-LRKVPW 104
Cdd:PTZ00422   27 LRFASLGNWGTGSKQ------QKLVASYLKQYAKNERVTFLVSPGSNF-PGGVDGLNDPKWKHCFENVYSEESgDMQIPF 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530 105 YVLAGNHDHLGNVSAQ----------------IAYSKISK---RWNFPSPFYR--LHF---------KIPQTNVSVAIFM 154
Cdd:PTZ00422  100 FTVLGQADWDGNYNAEllkgqnvylnghgqtdIEYDSNNDiypKWIMPNYWYHyfTHFtdtsgpsllKSGHKDMSVAFIF 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530 155 LDTVTLCGNSDDflsqqperpRDVklarTQLSW--LKKQLAAARE--DYVLVAGHYPVWSIAEHGPTHCLVKQLRPLLAT 230
Cdd:PTZ00422  180 IDTWILSSSFPY---------KKV----SERAWqdLKATLEYAPKiaDYIIVVGDKPIYSSGSSKGDSYLSYYLLPLLKD 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530 231 YGVTAYLCGHDHNLqYLQDENGVGYVLSGAGNfmdpskRHQRKVPNGYLRFHYGTEDSlgGFAYVEISSKEMTVTYIEA- 309
Cdd:PTZ00422  247 AQVDLYISGYDRNM-EVLTDEGTAHINCGSGG------NSGRKSIMKNSKSLFYSEDI--GFCIHELNAEGMVTKFVSGn 317

                         330
                  ....*....|....*.
gi 1015186530 310 SGKSLFKTRLPRRARP 325
Cdd:PTZ00422  318 TGEVLYTHKQPLKKRK 333
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 26-137 6.16e-05

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: 41.82  E-value: 6.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530  26 LRFVAVGDWGGVPNAPfhtaremANAKEIARTVQILGADFILSLGDNFyftgvqdiNDKRFQETFEDVFsDRSLRKVPWY 105
Cdd:pfam00149   1 MRILVIGDLHLPGQLD-------DLLELLKKLLEEGKPDLVLHAGDLV--------DRGPPSEEVLELL-ERLIKYVPVY 64

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1015186530 106 VLAGNHD--HLGNVSAQIAYSKISKRWNFPSPFY 137
Cdd:pfam00149  65 LVRGNHDfdYGECLRLYPYLGLLARPWKRFLEVF 98
 
Name Accession Description Interval E-value
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 26-311 2.95e-163

Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid phosphatase 5 (ACP5) removes the mannose 6-phosphate recognition marker from lysosomal proteins. The exact site of dephosphorylation is not clear. Evidence suggests dephosphorylation may take place in a prelysosomal compartment as well as in the lysosome. ACP5 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: 277324 [Multi-domain]  Cd Length: 286  Bit Score: 456.40  E-value: 2.95e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530  26 LRFVAVGDWGGVPNaPFHTAREMANAKEIARTVQILGADFILSLGDNFYFTGVQDINDKRFQETFEDVFSDRSLRkVPWY 105
Cdd:cd07378     1 LRFLVLGDWGGKPN-PYTTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSLQ-VPWY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530 106 VLAGNHDHLGNVSAQIAYSKI--SKRWNFPSPFYRLHFKIPQTNVSVAIFMLDTVTLCGNSDDFLSQQPERPRDVKLART 183
Cdd:cd07378    79 LVLGNHDHRGNVSAQIAYTQRpnSKRWNFPNYYYDISFKFPSSDVTVAFIMIDTVLLCGNTDDEASGQPRGPPNKKLAET 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530 184 QLSWLKKQLAAAREDYVLVAGHYPVWSIAEHGPTHCLVKQLRPLLATYGVTAYLCGHDHNLQYLQDENGVGYVLSGAGNF 263
Cdd:cd07378   159 QLAWLEKQLAASKADYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVDESGTYYVISGAGSK 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1015186530 264 MDPSKRHQRKVPNGYLRFHYGTEDSLGGFAYVEISSKEMTVTYIEASG 311
Cdd:cd07378   239 ADPSDIHRDKVPQGYLLFFSGFYSSGGGFAYLEITSSELVIRFVDSDG 286
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
26-286 4.36e-27

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 106.31  E-value: 4.36e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530  26 LRFVAVGDWGGVPNAPFHTAREMANAkeiARTVQILGADFILSLGDNFYFTGVQDIndKRFQETFEDVfsdrslrKVPWY 105
Cdd:COG1409     1 FRFAHISDLHLGAPDGSDTAEVLAAA---LADINAPRPDFVVVTGDLTDDGEPEEY--AAAREILARL-------GVPVY 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530 106 VLAGNHDHlgnvsaqiayskiskrWNFPSPFYRLHFKIPQTNVS--------VAIFMLDTVTLCGNSDDflsqqperprd 177
Cdd:COG1409    69 VVPGNHDI----------------RAAMAEAYREYFGDLPPGGLyysfdyggVRFIGLDSNVPGRSSGE----------- 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530 178 vkLARTQLSWLKKQLAAAREDYVLVAGHYPVWSIAEHGPTHCLV--KQLRPLLATYGVTAYLCGHDHNlQYLQDENGVGY 255
Cdd:COG1409   122 --LGPEQLAWLEEELAAAPAKPVIVFLHHPPYSTGSGSDRIGLRnaEELLALLARYGVDLVLSGHVHR-YERTRRDGVPY 198

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1015186530 256 VLSGAGNfmdpskrHQRKVPNGYLRFHYGTE 286
Cdd:COG1409   199 IVAGSTG-------GQVRLPPGYRVIEVDGD 222
PTZ00422 PTZ00422
glideosome-associated protein 50; Provisional
 26-325 3.15e-19

glideosome-associated protein 50; Provisional


Pssm-ID: 185607 [Multi-domain]  Cd Length: 394  Bit Score: 87.19  E-value: 3.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530  26 LRFVAVGDWGGVPNApfhtarEMANAKEIARTVQILGADFILSLGDNFyFTGVQDINDKRFQETFEDVFSDRS-LRKVPW 104
Cdd:PTZ00422   27 LRFASLGNWGTGSKQ------QKLVASYLKQYAKNERVTFLVSPGSNF-PGGVDGLNDPKWKHCFENVYSEESgDMQIPF 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530 105 YVLAGNHDHLGNVSAQ----------------IAYSKISK---RWNFPSPFYR--LHF---------KIPQTNVSVAIFM 154
Cdd:PTZ00422  100 FTVLGQADWDGNYNAEllkgqnvylnghgqtdIEYDSNNDiypKWIMPNYWYHyfTHFtdtsgpsllKSGHKDMSVAFIF 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530 155 LDTVTLCGNSDDflsqqperpRDVklarTQLSW--LKKQLAAARE--DYVLVAGHYPVWSIAEHGPTHCLVKQLRPLLAT 230
Cdd:PTZ00422  180 IDTWILSSSFPY---------KKV----SERAWqdLKATLEYAPKiaDYIIVVGDKPIYSSGSSKGDSYLSYYLLPLLKD 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530 231 YGVTAYLCGHDHNLqYLQDENGVGYVLSGAGNfmdpskRHQRKVPNGYLRFHYGTEDSlgGFAYVEISSKEMTVTYIEA- 309
Cdd:PTZ00422  247 AQVDLYISGYDRNM-EVLTDEGTAHINCGSGG------NSGRKSIMKNSKSLFYSEDI--GFCIHELNAEGMVTKFVSGn 317

                         330
                  ....*....|....*.
gi 1015186530 310 SGKSLFKTRLPRRARP 325
Cdd:PTZ00422  318 TGEVLYTHKQPLKKRK 333
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 26-243 6.62e-12

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: 65.01  E-value: 6.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530  26 LRFVAVGDWGGVPNAPFHTAREMANAKEiartvqilGADFILSLGDNFYFTGvqDINDKR---FQETFEDVFSdrslrKV 102
Cdd:cd00839     5 LKFAVFGDMGQNTNNSTNTLDHLEKELG--------NYDAIIHVGDIAYADG--YNNGSRwdtFMRQIEPLAS-----YV 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530 103 PWYVLAGNHDhlgnvsaqIAY-SKISKRWNFPSPFYRLHFKIPQTNV---SVAIFMLDTVTLCGNSDDFLSQQPERprdv 178
Cdd:cd00839    70 PYMVAPGNHE--------ADYnGSTSKIKFFMPGRGMPPSPSGSTENlwySFDVGPVHFISLSTETDFLKGDNISP---- 137

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1015186530 179 klartQLSWLKKQLAAA---REDYVLVAGHYPvWSIAEHGPTHCLVK-----QLRPLLATYGVTAYLCGHDHN 243
Cdd:cd00839   138 -----QYDWLEADLAKVdrsRTPWIIVMGHRP-MYCSNDDDADCIEGekmreALEDLFYKYGVDLVLSGHVHA 204
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 63-256 7.40e-10

Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known as LOC56985) is an uncharacterized Homo sapiens protein with a domain that 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: 277341 [Multi-domain]  Cd Length: 245  Bit Score: 58.50  E-value: 7.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530  63 ADFILSLGDnfyfTGVQDINDKRFQETFEDVFSDRSLRKVPWYVLAGNHDhLGNVSAQiaYSKISKRWN-FPSPFYrlHF 141
Cdd:cd07396    47 LAFVVQLGD----IIDGYNAKDRSKEALDAVLSILDRLKGPVHHVLGNHE-FYNFPRE--YLNHLKTLNgEDAYYY--SF 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530 142 kipQTNVSVAIFMLDTVTLCGNsddflsqqperprdvkLARTQLSWLKKQL--AAAREDYVLVAGHYPVWSIAEHGptHC 219
Cdd:cd07396   118 ---SPGPGFRFLVLDFVKFNGG----------------IGEEQLAWLRNELtsADANGEKVIVLSHLPIYPEAADP--QC 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1015186530 220 LV---KQLRPLLATYG-VTAYLCGHDHNLQYLQDENGVGYV 256
Cdd:cd07396   177 LLwnyEEVLAILESYPcVKACFSGHNHEGGYEQDSHGVHHV 217
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 139-259 6.52e-07

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: 48.06  E-value: 6.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530 139 LHFKIPQTNVSVAIFMLDTVTlcgnsddflSQQPE------------RPRDVKLARTQLSWLKKqlaaarEDYVLVAG-- 204
Cdd:cd07400     7 LHFGEERKPEVLELNLLDEIN---------ALKPDlvvvtgdltqraRPAEFEEAREFLDALEP------EPVVVVPGnh 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1015186530 205 ------HYPVWSIAEHG---PTHCLVKQLRPLLATYGVTAYLCGHDH--NLQYLQDENGVGYVLSG 259
Cdd:cd07400    72 daivalHHPLLPPPDTGrerNVLLDAGDALKLLKELGVDLVLHGHKHvpAVWNLGLLNGIVVVNAG 137
MPP_TMEM62_N cd07401
Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) ...
 104-245 3.56e-06

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: 47.36  E-value: 3.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530 104 WYVLAGNHDHLGNVSAQIA---YSKISKRwnFPSPFYRLHFKIPQTNVSVAIFmldtvtlcgnsDDFLSQQPERPRDV-- 178
Cdd:cd07401    80 LFDIRGNHDLFGIVSFDSQnnyYRKYSNT--GRDHSHSFSSTTRFGNYSFIGF-----------DPTIFPGPKRPFNFfg 146

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1015186530 179 KLARTQLSWLKKQLAAA-REDYVLVAGHYPVWSIAEHGPTHCLvKQLRPLLATYGVTAYLCGHDHNLQ 245
Cdd:cd07401   147 SLDKKLLDRLEKELEKSkNSKYTIWFGHYPHSLIISPSAKSSS-KTFKDLLKKYNVTAYLCGHLHPLG 213
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 102-243 1.03e-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: 46.12  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530 102 VPWYVLAGNHDHlgnvsaQIAYSKIskrwnFPSPFYRLHFKIpQTNVSVA---IFMLDTVTlCGNSDDFLSQQperprdv 178
Cdd:cd07402    70 APVYWIPGNHDD------RAAMREA-----LPEPPYDDNGPV-QYVVDFGgwrLILLDTSV-PGVHHGELSDE------- 129

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1015186530 179 klartQLSWLKKQLAAAREDYVLVAGHYPVWSIAEHGP-THCLVKQ--LRPLLATY-GVTAYLCGHDHN 243
Cdd:cd07402   130 -----QLDWLEAALAEAPDRPTLIFLHHPPFPLGIPWMdAIRLRNSqaLFAVLARHpQVKAILCGHIHR 193
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 26-137 6.16e-05

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: 41.82  E-value: 6.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530  26 LRFVAVGDWGGVPNAPfhtaremANAKEIARTVQILGADFILSLGDNFyftgvqdiNDKRFQETFEDVFsDRSLRKVPWY 105
Cdd:pfam00149   1 MRILVIGDLHLPGQLD-------DLLELLKKLLEEGKPDLVLHAGDLV--------DRGPPSEEVLELL-ERLIKYVPVY 64

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1015186530 106 VLAGNHD--HLGNVSAQIAYSKISKRWNFPSPFY 137
Cdd:pfam00149  65 LVRGNHDfdYGECLRLYPYLGLLARPWKRFLEVF 98
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 187-257 6.62e-05

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: 41.87  E-value: 6.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530 187 WLKKQLAAAREDYVLVAG-------HYPVWSIAEHG--PTHCLVKQLRPLLATYGVTAYLCGHDHNLQYLQDENGVGYVL 257
Cdd:cd00838    48 LKALRLLLAGIPVYVVPGnhdilvtHGPPYDPLDEGspGEDPGSEALLELLDKYGPDLVLSGHTHVPGRREVDKGGTLVV 127
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
27-259 1.34e-04

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 42.59  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530  27 RFVAVGDW--GgvpnAPFHtAREMANA-----KEIARTVQILGADFILSLGDNFyftgvqDIN--DKRFQETFEDVFSDR 97
Cdd:COG0420     2 RFLHTADWhlG----KPLH-GASRREDqlaalDRLVDLAIEEKVDAVLIAGDLF------DSAnpSPEAVRLLAEALRRL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530  98 SLRKVPWYVLAGNHDHLGnvsaqiayskiskRWNFPSPFYRLHfkipqtNVSV-AIFMLDTVTLCGNSD------DFLsq 170
Cdd:COG0420    71 SEAGIPVVLIAGNHDSPS-------------RLSAGSPLLENL------GVHVfGSVEPEPVELEDGLGvavyglPYL-- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530 171 qpeRPRDVKLARTQLSWLKKQLAAARedYVLVAGHYPVWSIAEHGPTHclVKQLRP-LLATYGVTAYLCGHDHNLQYLQD 249
Cdd:COG0420   130 ---RPSDEEALRDLLERLPRALDPGG--PNILLLHGFVAGASGSRDIY--VAPVPLsALPAAGFDYVALGHIHRPQVLGG 202

                         250
                  ....*....|
gi 1015186530 250 ENGVGYvlSG 259
Cdd:COG0420   203 DPRIRY--SG 210
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
27-243 1.81e-04

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 41.92  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530  27 RFVAVGDWGGvpnapfhtarEMANAKEIARTVQILGADFILSLGDnfyftgvqdINDKRFQETFEDVFSDRSLRKVPWYV 106
Cdd:COG2129     1 KILAVSDLHG----------NFDLLEKLLELARAEDADLVILAGD---------LTDFGTAEEAREVLEELAALGVPVLA 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530 107 LAGNHDHLGnVSAQIAYSKIskrwnfpspfYRLHFKipqtnvsvaIFMLDTVTLCGnsddfLSQQPERPRDVKLARTQlS 186
Cdd:COG2129    62 VPGNHDDPE-VLDALEESGV----------HNLHGR---------VVEIGGLRIAG-----LGGSRPTPFGTPYEYTE-E 115

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1015186530 187 WLKKQLAAAREDY--VLVAgHYPVWSIA---EHGPTHCLVKQLRPLLATYGVTAYLCGHDHN 243
Cdd:COG2129   116 EIEERLAKLREKDvdILLT-HAPPYGTTldrVEDGPHVGSKALRELIEEFQPKLVLHGHIHE 176
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 43-114 2.06e-04

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: 40.71  E-value: 2.06e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1015186530  43 HTAREMANAKEIARTVQILGADFILSLGDNFYFTGVQDINDKRFQEtfedvfsdRSLRKVPWYVLAGNHDHL 114
Cdd:cd00838     7 HGNLEALEAVLEAALAKAEKPDLVICLGDLVDYGPDPEEVELKALR--------LLLAGIPVYVVPGNHDIL 70
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 39-242 2.21e-04

acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase (ASMase) is a ubiquitously expressed phosphodiesterase which hydrolyzes sphingomyelin in acid pH conditions to form ceramide, a bioactive second messenger, as part of the sphingomyelin signaling pathway. ASMase is localized at the noncytosolic leaflet of biomembranes (for example the luminal leaflet of endosomes, lysosomes and phagosomes, and the extracellular leaflet of plasma membranes). ASMase-deficient humans develop Niemann-Pick disease. This disease is characterized by lysosomal storage of sphingomyelin in all tissues. Although ASMase-deficient mice are resistant to stress-induced apoptosis, they have greater susceptibility to bacterial infection. The latter correlates with defective phagolysosomal fusion and antibacterial killing activity in ASMase-deficient macrophages. ASMase 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: 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: 277321 [Multi-domain]  Cd Length: 294  Bit Score: 42.29  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530  39 NAPFHTARE-MANAKEIArtvqiLGADFILSLGDNFYftgvQDINDKRFQETFEDVFS-----DRSLRKVPWYVLAGNHD 112
Cdd:cd00842    50 DSPWSLVESaLEAIKKNH-----PKPDFILWTGDLVR----HDVDEQTPEETVESESNltnllKKYFPNVPVYPALGNHD 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530 113 hlGNVSAQIAYSKISKRWNF------------PSPFYRLH-----FKIPQTNVSVaIFmLDTVtLCGNSDDFLSQQPERP 175
Cdd:cd00842   121 --SYPVNQFPPHSNSPSWLYdalaelwkpwlpTEAKETFKkggyySVDVKDGLRV-IS-LNTN-LYYKKNFWLYSNNTDP 195

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1015186530 176 RDvklartQLSWLKKQLAAARE--DYVLVAGH-YPVWSIAEHGPTHCLVKqlrpLLATYG--VTAYLCGHDH 242
Cdd:cd00842   196 CG------QLQWLEDELEDAEQkgEKVWIIGHiPPGLNSYDADWSERFYQ----IINRYSdtIAGQFFGHTH 257
PhoD COG3540
Phosphodiesterase/alkaline phosphatase D [Inorganic ion transport and metabolism];
19-196 2.86e-03

Phosphodiesterase/alkaline phosphatase D [Inorganic ion transport and metabolism];


Pssm-ID: 442761 [Multi-domain]  Cd Length: 482  Bit Score: 39.13  E-value: 2.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530  19 ADGATPALRFVAVGDWGGvPNAPFHTAREMANAKeiartvqilgADFILSLGDNFYFTGVQDINDKRFQ--------ETF 90
Cdd:COG3540   128 APGAPDRLRFAFASCQNY-EGGYFTAYRAMAEED----------PDFVLHLGDYIYEDGPGPYGLPGLWrpepskeaETL 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015186530  91 ED-------VFSDRSLR----KVPWYVLAGNHDHLGNVSAQIAYSKISKRWNF---------------PSPFY------- 137
Cdd:COG3540   197 ADyrgryaqYRSDPDLQalhaAVPWIATWDDHEVANNWAGGGAEHDRYTEGDFaarraaalqafyeymPIRRPgpdgddg 276

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1015186530 138 RLHFKIPQTNVsVAIFMLDTVTLCGNSDDFLSQQPERPRDVKLARTQLSWLKKQLAAAR 196
Cdd:COG3540   277 RIYRRFRYGDL-ADLFMLDTRSYRDPQPCLQCPEADDPDRTLLGAEQLAWLKDGLAAST 334
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH