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Conserved domains on  [gi|442625393|ref|NP_001259919|]
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uncharacterized protein Dmel_CG4267, isoform B [Drosophila melanogaster]

Protein Classification

lipase family protein( domain architecture ID 10091066)

lipase family protein belonging to the alpha/beta hydrolase superfamily may function as a lipase/phospholipase, such as lipase member H that hydrolyzes specifically phosphatidic acid (PA) to produce 2-acyl lysophosphatidic acid

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Pancreat_lipase_like cd00707
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ...
71-347 1.91e-109

Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


:

Pssm-ID: 238363 [Multi-domain]  Cd Length: 275  Bit Score: 321.50  E-value: 1.91e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625393  71 KMQFILFKRDFADCGRELFVGDVENLRNSGFDARHQTRIVIHGWMSQSKGSHIRKVKNAYLSltdpgpngepapYEDFNV 150
Cdd:cd00707    2 DVRFLLYTRENPNCPQLLFADDPSSLKNSNFNPSRPTRFIIHGWTSSGEESWISDLRKAYLS------------RGDYNV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625393 151 IVCDWSKtSTNVNYYEVAKTVEDMGALLAELVRYLNQEANMHYDDVYVIGHSLGAQIAGSAGKQImPYRFNTIYALDPAG 230
Cdd:cd00707   70 IVVDWGR-GANPNYPQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRL-NGKLGRITGLDPAG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625393 231 PQFREKSDEYRIDASDASYVESIQTSVS-FGFEQPVGHATFYPNYGKNQKKCYV-------YGCSHKRSHDYFIESLTSP 302
Cdd:cd00707  148 PLFSGADPEDRLDPSDAQFVDVIHTDGGlLGFSQPIGHADFYPNGGRDQPGCPKdilssdfVACSHQRAVHYFAESILSP 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 442625393 303 AGFWGPRCERHDD--GTWLLLMSDGEFRMGGEPS-IPKNGTFYVKTYS 347
Cdd:cd00707  228 CGFVAYPCSSYDEflAGKCFPCGSGCVRMGYHADrFRREGKFYLKTNA 275
 
Name Accession Description Interval E-value
Pancreat_lipase_like cd00707
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ...
71-347 1.91e-109

Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238363 [Multi-domain]  Cd Length: 275  Bit Score: 321.50  E-value: 1.91e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625393  71 KMQFILFKRDFADCGRELFVGDVENLRNSGFDARHQTRIVIHGWMSQSKGSHIRKVKNAYLSltdpgpngepapYEDFNV 150
Cdd:cd00707    2 DVRFLLYTRENPNCPQLLFADDPSSLKNSNFNPSRPTRFIIHGWTSSGEESWISDLRKAYLS------------RGDYNV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625393 151 IVCDWSKtSTNVNYYEVAKTVEDMGALLAELVRYLNQEANMHYDDVYVIGHSLGAQIAGSAGKQImPYRFNTIYALDPAG 230
Cdd:cd00707   70 IVVDWGR-GANPNYPQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRL-NGKLGRITGLDPAG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625393 231 PQFREKSDEYRIDASDASYVESIQTSVS-FGFEQPVGHATFYPNYGKNQKKCYV-------YGCSHKRSHDYFIESLTSP 302
Cdd:cd00707  148 PLFSGADPEDRLDPSDAQFVDVIHTDGGlLGFSQPIGHADFYPNGGRDQPGCPKdilssdfVACSHQRAVHYFAESILSP 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 442625393 303 AGFWGPRCERHDD--GTWLLLMSDGEFRMGGEPS-IPKNGTFYVKTYS 347
Cdd:cd00707  228 CGFVAYPCSSYDEflAGKCFPCGSGCVRMGYHADrFRREGKFYLKTNA 275
Lipase pfam00151
Lipase;
64-351 3.62e-48

Lipase;


Pssm-ID: 395099  Cd Length: 336  Bit Score: 166.08  E-value: 3.62e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625393   64 PFTSSRGKMQFILFKRDFADCGrELFVGDVENLRNSGFDARHQTRIVIHGWMSQ-SKGSHIRKVKNAYLSLtdpgpngep 142
Cdd:pfam00151  30 PWSPKDIDTRFLLYTNENPNNC-QLITGDPETIRNSNFNTSRKTRFIIHGFIDKgYEESWLSDMCKALFQV--------- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625393  143 apyEDFNVIVCDWSKTSTNvNYYEVAKTVEDMGALLAELVRYLNQEANMHYDDVYVIGHSLGAQIAGSAGKQiMPYRFNT 222
Cdd:pfam00151 100 ---EDVNVICVDWKSGSRT-HYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIGHSLGAHVAGEAGRR-TNGKLGR 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625393  223 IYALDPAGPQFREKSDEYRIDASDASYVESIQTS------VSFGFEQPVGHATFYPNYGKNQKKC--------------- 281
Cdd:pfam00151 175 ITGLDPAGPYFQGTPEEVRLDPGDADFVDAIHTDtrpipgLGFGISQPVGHVDFFPNGGSEQPGCqknilsqiididgiw 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625393  282 ---YVYGCSHKRSHDYFIESLTSPAGFWGPRCERHDD---GTWLLLMSDGEFRMG-------GEPSiPKNGTFYVKTYSK 348
Cdd:pfam00151 255 egtQFVACNHLRSVHYYIDSLLNPRGFPGYPCSSYDAfsqNKCLPCPKGGCPQMGhyadkfpGKTS-KLEQTFYLNTGSS 333

                  ...
gi 442625393  349 PPY 351
Cdd:pfam00151 334 SPF 336
lipo_lipase TIGR03230
lipoprotein lipase; Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a ...
88-299 2.08e-24

lipoprotein lipase; Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a eukaryotic triacylglycerol lipase active in plasma and similar to pancreatic and hepatic triacylglycerol lipases (EC 3.1.1.3). It is also called clearing factor. It cleaves chylomicron and VLDL triacylglycerols; it also has phospholipase A-1 activity.


Pssm-ID: 132274 [Multi-domain]  Cd Length: 442  Bit Score: 103.82  E-value: 2.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625393   88 LFVGDVENLRNSGFDARHQTRIVIHGWMsqskgshirkVKNAYLSLTdpgPNGEPAPYE---DFNVIVCDWSkTSTNVNY 164
Cdd:TIGR03230  24 IVPGQPDSIADCNFNHETKTFIVIHGWT----------VTGMFESWV---PKLVAALYErepSANVIVVDWL-SRAQQHY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625393  165 YEVAKTVEDMGALLAELVRYLNQEANMHYDDVYVIGHSLGAQIAGSAGkQIMPYRFNTIYALDPAGPQFREKSDEYRIDA 244
Cdd:TIGR03230  90 PTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAG-SLTKHKVNRITGLDPAGPTFEYADAPSTLSP 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442625393  245 SDASYVESIQTSV------SFGFEQPVGHATFYPNYGKNQKKC------------------YVYGCSHKRSHDYFIESL 299
Cdd:TIGR03230 169 DDADFVDVLHTNTrgspdrSIGIQRPVGHIDIYPNGGTFQPGCdiqetllviaekglgnmdQLVKCSHERSIHLFIDSL 247
COG4757 COG4757
Predicted alpha/beta hydrolase [General function prediction only];
148-211 1.72e-03

Predicted alpha/beta hydrolase [General function prediction only];


Pssm-ID: 443790 [Multi-domain]  Cd Length: 289  Bit Score: 39.87  E-value: 1.72e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442625393 148 FNVIVCDW-----SKT----STNVNYYEVAktVEDMGALLAELVRylnqeanmHYDD--VYVIGHSLGAQIAGSA 211
Cdd:COG4757   60 FAVLTYDYrgiglSRPgslrGFDAGYRDWG--ELDLPAVLDALRA--------RFPGlpLLLVGHSLGGQLLGLA 124
 
Name Accession Description Interval E-value
Pancreat_lipase_like cd00707
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ...
71-347 1.91e-109

Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238363 [Multi-domain]  Cd Length: 275  Bit Score: 321.50  E-value: 1.91e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625393  71 KMQFILFKRDFADCGRELFVGDVENLRNSGFDARHQTRIVIHGWMSQSKGSHIRKVKNAYLSltdpgpngepapYEDFNV 150
Cdd:cd00707    2 DVRFLLYTRENPNCPQLLFADDPSSLKNSNFNPSRPTRFIIHGWTSSGEESWISDLRKAYLS------------RGDYNV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625393 151 IVCDWSKtSTNVNYYEVAKTVEDMGALLAELVRYLNQEANMHYDDVYVIGHSLGAQIAGSAGKQImPYRFNTIYALDPAG 230
Cdd:cd00707   70 IVVDWGR-GANPNYPQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRL-NGKLGRITGLDPAG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625393 231 PQFREKSDEYRIDASDASYVESIQTSVS-FGFEQPVGHATFYPNYGKNQKKCYV-------YGCSHKRSHDYFIESLTSP 302
Cdd:cd00707  148 PLFSGADPEDRLDPSDAQFVDVIHTDGGlLGFSQPIGHADFYPNGGRDQPGCPKdilssdfVACSHQRAVHYFAESILSP 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 442625393 303 AGFWGPRCERHDD--GTWLLLMSDGEFRMGGEPS-IPKNGTFYVKTYS 347
Cdd:cd00707  228 CGFVAYPCSSYDEflAGKCFPCGSGCVRMGYHADrFRREGKFYLKTNA 275
Lipase pfam00151
Lipase;
64-351 3.62e-48

Lipase;


Pssm-ID: 395099  Cd Length: 336  Bit Score: 166.08  E-value: 3.62e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625393   64 PFTSSRGKMQFILFKRDFADCGrELFVGDVENLRNSGFDARHQTRIVIHGWMSQ-SKGSHIRKVKNAYLSLtdpgpngep 142
Cdd:pfam00151  30 PWSPKDIDTRFLLYTNENPNNC-QLITGDPETIRNSNFNTSRKTRFIIHGFIDKgYEESWLSDMCKALFQV--------- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625393  143 apyEDFNVIVCDWSKTSTNvNYYEVAKTVEDMGALLAELVRYLNQEANMHYDDVYVIGHSLGAQIAGSAGKQiMPYRFNT 222
Cdd:pfam00151 100 ---EDVNVICVDWKSGSRT-HYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIGHSLGAHVAGEAGRR-TNGKLGR 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625393  223 IYALDPAGPQFREKSDEYRIDASDASYVESIQTS------VSFGFEQPVGHATFYPNYGKNQKKC--------------- 281
Cdd:pfam00151 175 ITGLDPAGPYFQGTPEEVRLDPGDADFVDAIHTDtrpipgLGFGISQPVGHVDFFPNGGSEQPGCqknilsqiididgiw 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625393  282 ---YVYGCSHKRSHDYFIESLTSPAGFWGPRCERHDD---GTWLLLMSDGEFRMG-------GEPSiPKNGTFYVKTYSK 348
Cdd:pfam00151 255 egtQFVACNHLRSVHYYIDSLLNPRGFPGYPCSSYDAfsqNKCLPCPKGGCPQMGhyadkfpGKTS-KLEQTFYLNTGSS 333

                  ...
gi 442625393  349 PPY 351
Cdd:pfam00151 334 SPF 336
lipo_lipase TIGR03230
lipoprotein lipase; Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a ...
88-299 2.08e-24

lipoprotein lipase; Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a eukaryotic triacylglycerol lipase active in plasma and similar to pancreatic and hepatic triacylglycerol lipases (EC 3.1.1.3). It is also called clearing factor. It cleaves chylomicron and VLDL triacylglycerols; it also has phospholipase A-1 activity.


Pssm-ID: 132274 [Multi-domain]  Cd Length: 442  Bit Score: 103.82  E-value: 2.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625393   88 LFVGDVENLRNSGFDARHQTRIVIHGWMsqskgshirkVKNAYLSLTdpgPNGEPAPYE---DFNVIVCDWSkTSTNVNY 164
Cdd:TIGR03230  24 IVPGQPDSIADCNFNHETKTFIVIHGWT----------VTGMFESWV---PKLVAALYErepSANVIVVDWL-SRAQQHY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625393  165 YEVAKTVEDMGALLAELVRYLNQEANMHYDDVYVIGHSLGAQIAGSAGkQIMPYRFNTIYALDPAGPQFREKSDEYRIDA 244
Cdd:TIGR03230  90 PTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAG-SLTKHKVNRITGLDPAGPTFEYADAPSTLSP 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442625393  245 SDASYVESIQTSV------SFGFEQPVGHATFYPNYGKNQKKC------------------YVYGCSHKRSHDYFIESL 299
Cdd:TIGR03230 169 DDADFVDVLHTNTrgspdrSIGIQRPVGHIDIYPNGGTFQPGCdiqetllviaekglgnmdQLVKCSHERSIHLFIDSL 247
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
173-282 3.16e-19

Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation", the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238382 [Multi-domain]  Cd Length: 153  Bit Score: 83.32  E-value: 3.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625393 173 DMGALLAELVRYLNQEANMHYDD--VYVIGHSLGAQIAGSAGKQI---MPYRFNTIYALDPAGPQFREKSDEyRIDASDA 247
Cdd:cd00741    5 KAARSLANLVLPLLKSALAQYPDykIHVTGHSLGGALAGLAGLDLrgrGLGRLVRVYTFGPPRVGNAAFAED-RLDPSDA 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 442625393 248 SYVESIQTS------VSF-GFEQPVGHATFYPNYGKNQKKCY 282
Cdd:cd00741   84 LFVDRIVNDndivprLPPgGEGYPHGGAEFYINGGKSQPGCC 125
COG4757 COG4757
Predicted alpha/beta hydrolase [General function prediction only];
148-211 1.72e-03

Predicted alpha/beta hydrolase [General function prediction only];


Pssm-ID: 443790 [Multi-domain]  Cd Length: 289  Bit Score: 39.87  E-value: 1.72e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442625393 148 FNVIVCDW-----SKT----STNVNYYEVAktVEDMGALLAELVRylnqeanmHYDD--VYVIGHSLGAQIAGSA 211
Cdd:COG4757   60 FAVLTYDYrgiglSRPgslrGFDAGYRDWG--ELDLPAVLDALRA--------RFPGlpLLLVGHSLGGQLLGLA 124
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
170-208 4.26e-03

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 38.06  E-value: 4.26e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 442625393 170 TVEDMGALLAELVRYLNqeanmhYDDVYVIGHSLGAQIA 208
Cdd:COG0596   71 TLDDLADDLAALLDALG------LERVVLVGHSMGGMVA 103
Mbeg1-like pfam11187
Mbeg1-like; This family includes a group of uncharacterized proteins from bacteria. Recently, ...
182-241 6.65e-03

Mbeg1-like; This family includes a group of uncharacterized proteins from bacteria. Recently, a member from Gemella sanguinis M325, Mbeg1 (for "microbiome bacteria effector gene") has been identified as the first example of this protein family being associated with a potential effector function in the human microbiome.


Pssm-ID: 402661 [Multi-domain]  Cd Length: 224  Bit Score: 37.67  E-value: 6.65e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442625393  182 VRYLNQEANMHYDDVYVIGHSLGAQIAGSAGKQIMP---YRFNTIYALDpaGPQFREK---SDEYR 241
Cdd:pfam11187  72 AKYLNKILQHYPGKIYLGGHSKGGNLAIYAAMNAEPdlqDRIIKIYSFD--GPGFPKQvleSPGYQ 135
 
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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