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Conserved domains on  [gi|74214487|dbj|BAE31096|]
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unnamed protein product [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 37-333 2.71e-110

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: 326.95  E-value: 2.71e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74214487  37 FWHVTDLHLDPTYHITDDRTkVCASSKGANASNP--------GPFGDVLCDSPYQLILSAFDFIKNSGQEASFMIWTGDS 108
Cdd:cd00842   1 FLHISDIHYDPLYKVGSEYA-NCRSPLCCRDESGpgdvkppaGYWGTYGCDSPWSLVESALEAIKKNHPKPDFILWTGDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74214487 109 PPHVPVPELSTgTVIKVITNMTMTVQNLFPNLQVFPALGNHDYWPQDQLP---IVTSKVYSAVADLWKPWLGEEAISTLK 185
Cdd:cd00842  80 VRHDVDEQTPE-ETVESESNLTNLLKKYFPNVPVYPALGNHDSYPVNQFPphsNSPSWLYDALAELWKPWLPTEAKETFK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74214487 186 KGGFYSQKVasNPGLRIISLNTNLYYGPNIMTL-NKTDPANQFEWLENTLNSSLWNKEKVYIIAHVPVGYLPYAtdtpai 264
Cdd:cd00842 159 KGGYYSVDV--KDGLRVISLNTNLYYKKNFWLYsNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHIPPGLNSYD------ 230

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74214487 265 rQYYNEKLLDIFRRYSSVIAGQFYGHTHRDSLMVLSDKN--GNPLNSVFVAPAVTPVKGvlqketNNPGVR 333
Cdd:cd00842 231 -ADWSERFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDKdtGSPINVAYIAPSVTPYTG------NNPSFR 294
ASMase_C pfam19272
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ...
 305-444 1.39e-89

Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the C-terminal region of the phosphodiesterase domain found in acid sphingomyelin phosphodiesterases. It contains two disulphide bridges.


:

Pssm-ID: 466022  Cd Length: 143  Bit Score: 268.47  E-value: 1.39e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74214487   305 NPLNSVFVAPAVTPVKGVLQKETNNPGVRLFQYKPGDYTLLDMVQYYLNLTEANLKGESNWTLEYVLTQAYSVADLQPKS 384
Cdd:pfam19272   1 NPVNSLFVAPAVTPVKSVLEKESNNPGVRLYQYDPKDYKLLDMLQYYLNLTEANLKGESNWKLEYILTKAYGIEDLQPQS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 74214487   385 LYALVQQFATKDSKQFLKYYHYYFVSYDSSATCDQHCKTLQVCAIMNLDSMSYDDCLKQH 444
Cdd:pfam19272  81 LYGLAKQFAVPHSKQFEKYYNYFFVSYDSSIVCEGGCKALQICAIMYLDYSSYTDCIKQY 140
 
Name Accession Description Interval E-value
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 37-333 2.71e-110

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: 326.95  E-value: 2.71e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74214487  37 FWHVTDLHLDPTYHITDDRTkVCASSKGANASNP--------GPFGDVLCDSPYQLILSAFDFIKNSGQEASFMIWTGDS 108
Cdd:cd00842   1 FLHISDIHYDPLYKVGSEYA-NCRSPLCCRDESGpgdvkppaGYWGTYGCDSPWSLVESALEAIKKNHPKPDFILWTGDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74214487 109 PPHVPVPELSTgTVIKVITNMTMTVQNLFPNLQVFPALGNHDYWPQDQLP---IVTSKVYSAVADLWKPWLGEEAISTLK 185
Cdd:cd00842  80 VRHDVDEQTPE-ETVESESNLTNLLKKYFPNVPVYPALGNHDSYPVNQFPphsNSPSWLYDALAELWKPWLPTEAKETFK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74214487 186 KGGFYSQKVasNPGLRIISLNTNLYYGPNIMTL-NKTDPANQFEWLENTLNSSLWNKEKVYIIAHVPVGYLPYAtdtpai 264
Cdd:cd00842 159 KGGYYSVDV--KDGLRVISLNTNLYYKKNFWLYsNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHIPPGLNSYD------ 230

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74214487 265 rQYYNEKLLDIFRRYSSVIAGQFYGHTHRDSLMVLSDKN--GNPLNSVFVAPAVTPVKGvlqketNNPGVR 333
Cdd:cd00842 231 -ADWSERFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDKdtGSPINVAYIAPSVTPYTG------NNPSFR 294
ASMase_C pfam19272
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ...
 305-444 1.39e-89

Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the C-terminal region of the phosphodiesterase domain found in acid sphingomyelin phosphodiesterases. It contains two disulphide bridges.


Pssm-ID: 466022  Cd Length: 143  Bit Score: 268.47  E-value: 1.39e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74214487   305 NPLNSVFVAPAVTPVKGVLQKETNNPGVRLFQYKPGDYTLLDMVQYYLNLTEANLKGESNWTLEYVLTQAYSVADLQPKS 384
Cdd:pfam19272   1 NPVNSLFVAPAVTPVKSVLEKESNNPGVRLYQYDPKDYKLLDMLQYYLNLTEANLKGESNWKLEYILTKAYGIEDLQPQS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 74214487   385 LYALVQQFATKDSKQFLKYYHYYFVSYDSSATCDQHCKTLQVCAIMNLDSMSYDDCLKQH 444
Cdd:pfam19272  81 LYGLAKQFAVPHSKQFEKYYNYFFVSYDSSIVCEGGCKALQICAIMYLDYSSYTDCIKQY 140
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
37-294 1.38e-09

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 58.16  E-value: 1.38e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74214487  37 FWHVTDLHLDPT--YHITDDRTKVCASskgANASNPgpfgdvlcdspyqlilsafDFIknsgqeasfmIWTGDspphvpv 114
Cdd:COG1409   3 FAHISDLHLGAPdgSDTAEVLAAALAD---INAPRP-------------------DFV----------VVTGD------- 43

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74214487 115 pelstgtvikvITNMTMT-----VQNLFPNLQ--VFPALGNHDYWpqdqlpivtskvySAVADLWKPWLGEEAISTLkkg 187
Cdd:COG1409  44 -----------LTDDGEPeeyaaAREILARLGvpVYVVPGNHDIR-------------AAMAEAYREYFGDLPPGGL--- 96

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74214487 188 gFYSQKVasnPGLRIISLNTNLYYGPNimtlNKTDPAnQFEWLENTLNSSlwNKEKVYIIAHVPVGYLPYATDTPAIRqy 267
Cdd:COG1409  97 -YYSFDY---GGVRFIGLDSNVPGRSS----GELGPE-QLAWLEEELAAA--PAKPVIVFLHHPPYSTGSGSDRIGLR-- 163

                       250       260
                ....*....|....*....|....*..
gi 74214487 268 YNEKLLDIFRRYSsvIAGQFYGHTHRD 294
Cdd:COG1409 164 NAEELLALLARYG--VDLVLSGHVHRY 188
 
Name Accession Description Interval E-value
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 37-333 2.71e-110

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: 326.95  E-value: 2.71e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74214487  37 FWHVTDLHLDPTYHITDDRTkVCASSKGANASNP--------GPFGDVLCDSPYQLILSAFDFIKNSGQEASFMIWTGDS 108
Cdd:cd00842   1 FLHISDIHYDPLYKVGSEYA-NCRSPLCCRDESGpgdvkppaGYWGTYGCDSPWSLVESALEAIKKNHPKPDFILWTGDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74214487 109 PPHVPVPELSTgTVIKVITNMTMTVQNLFPNLQVFPALGNHDYWPQDQLP---IVTSKVYSAVADLWKPWLGEEAISTLK 185
Cdd:cd00842  80 VRHDVDEQTPE-ETVESESNLTNLLKKYFPNVPVYPALGNHDSYPVNQFPphsNSPSWLYDALAELWKPWLPTEAKETFK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74214487 186 KGGFYSQKVasNPGLRIISLNTNLYYGPNIMTL-NKTDPANQFEWLENTLNSSLWNKEKVYIIAHVPVGYLPYAtdtpai 264
Cdd:cd00842 159 KGGYYSVDV--KDGLRVISLNTNLYYKKNFWLYsNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHIPPGLNSYD------ 230

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74214487 265 rQYYNEKLLDIFRRYSSVIAGQFYGHTHRDSLMVLSDKN--GNPLNSVFVAPAVTPVKGvlqketNNPGVR 333
Cdd:cd00842 231 -ADWSERFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDKdtGSPINVAYIAPSVTPYTG------NNPSFR 294
ASMase_C pfam19272
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ...
 305-444 1.39e-89

Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the C-terminal region of the phosphodiesterase domain found in acid sphingomyelin phosphodiesterases. It contains two disulphide bridges.


Pssm-ID: 466022  Cd Length: 143  Bit Score: 268.47  E-value: 1.39e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74214487   305 NPLNSVFVAPAVTPVKGVLQKETNNPGVRLFQYKPGDYTLLDMVQYYLNLTEANLKGESNWTLEYVLTQAYSVADLQPKS 384
Cdd:pfam19272   1 NPVNSLFVAPAVTPVKSVLEKESNNPGVRLYQYDPKDYKLLDMLQYYLNLTEANLKGESNWKLEYILTKAYGIEDLQPQS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 74214487   385 LYALVQQFATKDSKQFLKYYHYYFVSYDSSATCDQHCKTLQVCAIMNLDSMSYDDCLKQH 444
Cdd:pfam19272  81 LYGLAKQFAVPHSKQFEKYYNYFFVSYDSSIVCEGGCKALQICAIMYLDYSSYTDCIKQY 140
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
37-294 1.38e-09

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 58.16  E-value: 1.38e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74214487  37 FWHVTDLHLDPT--YHITDDRTKVCASskgANASNPgpfgdvlcdspyqlilsafDFIknsgqeasfmIWTGDspphvpv 114
Cdd:COG1409   3 FAHISDLHLGAPdgSDTAEVLAAALAD---INAPRP-------------------DFV----------VVTGD------- 43

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74214487 115 pelstgtvikvITNMTMT-----VQNLFPNLQ--VFPALGNHDYWpqdqlpivtskvySAVADLWKPWLGEEAISTLkkg 187
Cdd:COG1409  44 -----------LTDDGEPeeyaaAREILARLGvpVYVVPGNHDIR-------------AAMAEAYREYFGDLPPGGL--- 96

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74214487 188 gFYSQKVasnPGLRIISLNTNLYYGPNimtlNKTDPAnQFEWLENTLNSSlwNKEKVYIIAHVPVGYLPYATDTPAIRqy 267
Cdd:COG1409  97 -YYSFDY---GGVRFIGLDSNVPGRSS----GELGPE-QLAWLEEELAAA--PAKPVIVFLHHPPYSTGSGSDRIGLR-- 163

                       250       260
                ....*....|....*....|....*..
gi 74214487 268 YNEKLLDIFRRYSsvIAGQFYGHTHRD 294
Cdd:COG1409 164 NAEELLALLARYG--VDLVLSGHVHRY 188
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 139-293 3.79e-09

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: 56.96  E-value: 3.79e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74214487 139 NLQVFPALGNHDYWpqdqlpiVTSKVYSAvadlwkpwlgeeAISTLKKGGFYSQKVASNPGLRIISLNTNLYYGpnimTL 218
Cdd:cd07396  81 KGPVHHVLGNHEFY-------NFPREYLN------------HLKTLNGEDAYYYSFSPGPGFRFLVLDFVKFNG----GI 137

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74214487 219 NKTdpanQFEWLENTLNSSLWNKEKVYIIAHVPVgyLPYATDTPAIRQYYNEkLLDIFRRYSSVIAgQFYGHTHR 293
Cdd:cd07396 138 GEE----QLAWLRNELTSADANGEKVIVLSHLPI--YPEAADPQCLLWNYEE-VLAILESYPCVKA-CFSGHNHE 204
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 143-292 8.08e-04

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: 41.13  E-value: 8.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74214487 143 FPALGNHDYWPQDQlpivTSKVYSAVADLWKPWLGeeaiSTLKKGGFYSQKVAsnpGLRIISLNTNLYYGPnimtlnKTD 222
Cdd:cd00839  72 MVAPGNHEADYNGS----TSKIKFFMPGRGMPPSP----SGSTENLWYSFDVG---PVHFISLSTETDFLK------GDN 134

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74214487 223 PANQFEWLENTLNSSlwNKEKV-YIIA--HVPvgylPYATDTPAIRQYYNEKLL----DIFRRYSSVIAgqFYGHTH 292
Cdd:cd00839 135 ISPQYDWLEADLAKV--DRSRTpWIIVmgHRP----MYCSNDDDADCIEGEKMRealeDLFYKYGVDLV--LSGHVH 203
 
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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