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Conserved domains on  [gi|2045876397|ref|WP_214057466|]
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alpha/beta hydrolase [Nocardioides aquaticus]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11171394)

alpha/beta hydrolase catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
80-286 2.65e-60

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


:

Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 191.27  E-value: 2.65e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876397  80 VVYAHGGGWCLGSVHAADGPCRRLARAARAVVVSLEYRLAPESPFPAPLADCMAAVDAIVADPGLVGARPTRIVMMGDSA 159
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876397 160 GGNLVLGTALQRRDAGLTSADALVLVYPCVASPHTNARPSMRENAHAPVLTKSTMAWYWDTHLDGRDAD-ARVDILGRTD 238
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDLRTESPSYLAREFADGPLLTRAAMDWFWRLYLPGADRDdPLASPLFASD 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2045876397 239 LTGLPPTLVVAAGLDPLRDEAIELAQTLQEVGVTTSVLHYPGAVHGFW 286
Cdd:pfam07859 161 LSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGFH 208
 
Name Accession Description Interval E-value
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
80-286 2.65e-60

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 191.27  E-value: 2.65e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876397  80 VVYAHGGGWCLGSVHAADGPCRRLARAARAVVVSLEYRLAPESPFPAPLADCMAAVDAIVADPGLVGARPTRIVMMGDSA 159
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876397 160 GGNLVLGTALQRRDAGLTSADALVLVYPCVASPHTNARPSMRENAHAPVLTKSTMAWYWDTHLDGRDAD-ARVDILGRTD 238
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDLRTESPSYLAREFADGPLLTRAAMDWFWRLYLPGADRDdPLASPLFASD 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2045876397 239 LTGLPPTLVVAAGLDPLRDEAIELAQTLQEVGVTTSVLHYPGAVHGFW 286
Cdd:pfam07859 161 LSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGFH 208
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
67-309 1.83e-49

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 163.51  E-value: 1.83e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876397  67 RVYNPAPREE-LPLVVYAHGGGWCLGSVHAADGPCRRLARAARAVVVSLEYRLAPESPFPAPLADCMAAVDAIVADPGLV 145
Cdd:COG0657     2 DVYRPAGAKGpLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876397 146 GARPTRIVMMGDSAGGNLVLGTALQRRDAGLTSADALVLVYPCVasphtnarpsmrenahapvltkstmawywdthldgr 225
Cdd:COG0657    82 GIDPDRIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVL------------------------------------ 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876397 226 daDARVDILgRTDLTGLPPTLVVAAGLDPLRDEAIELAQTLQEVGVTTSVLHYPGAVHGFWSLDGvLEQAAELDGDIANF 305
Cdd:COG0657   126 --DLTASPL-RADLAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAG-LPEARAALAEIAAF 201

                  ....
gi 2045876397 306 MAAL 309
Cdd:COG0657   202 LRRA 205
PRK10162 PRK10162
acetyl esterase;
33-308 3.35e-29

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 113.66  E-value: 3.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876397  33 RRAMEQVTRSQSERAPIALVHDVKITGGDGHIPARVYNPAPREELPLVvYAHGGGWCLGSVHAADGPCRRLARAARAVVV 112
Cdd:PRK10162   38 RQYYTLERRFWNAGAPEMATRAYMVPTPYGQVETRLYYPQPDSQATLF-YLHGGGFILGNLDTHDRIMRLLASYSGCTVI 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876397 113 SLEYRLAPESPFPAPLADCMAAVDAIVADPGLVGARPTRIVMMGDSAGGNLVLGTALQRRDAGLTSAD--ALVLVYpcvA 190
Cdd:PRK10162  117 GIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDYGINMSRIGFAGDSAGAMLALASALWLRDKQIDCGKvaGVLLWY---G 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876397 191 SPHTNARPSMRENAHA-PVLTKSTMAWYWDTHL-DGRDADARVDILGRTDLT-GLPPTLVVAAGLDPLRDEAIELAQTLQ 267
Cdd:PRK10162  194 LYGLRDSVSRRLLGGVwDGLTQQDLQMYEEAYLsNDADRESPYYCLFNNDLTrDVPPCFIAGAEFDPLLDDSRLLYQTLA 273
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2045876397 268 EVGVTTSVLHYPGAVHGFWSLDGVLEQAAELDGDIANFMAA 308
Cdd:PRK10162  274 AHQQPCEFKLYPGTLHAFLHYSRMMDTADDALRDGAQFFTA 314
 
Name Accession Description Interval E-value
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
80-286 2.65e-60

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 191.27  E-value: 2.65e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876397  80 VVYAHGGGWCLGSVHAADGPCRRLARAARAVVVSLEYRLAPESPFPAPLADCMAAVDAIVADPGLVGARPTRIVMMGDSA 159
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876397 160 GGNLVLGTALQRRDAGLTSADALVLVYPCVASPHTNARPSMRENAHAPVLTKSTMAWYWDTHLDGRDAD-ARVDILGRTD 238
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDLRTESPSYLAREFADGPLLTRAAMDWFWRLYLPGADRDdPLASPLFASD 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2045876397 239 LTGLPPTLVVAAGLDPLRDEAIELAQTLQEVGVTTSVLHYPGAVHGFW 286
Cdd:pfam07859 161 LSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGFH 208
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
67-309 1.83e-49

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 163.51  E-value: 1.83e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876397  67 RVYNPAPREE-LPLVVYAHGGGWCLGSVHAADGPCRRLARAARAVVVSLEYRLAPESPFPAPLADCMAAVDAIVADPGLV 145
Cdd:COG0657     2 DVYRPAGAKGpLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876397 146 GARPTRIVMMGDSAGGNLVLGTALQRRDAGLTSADALVLVYPCVasphtnarpsmrenahapvltkstmawywdthldgr 225
Cdd:COG0657    82 GIDPDRIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVL------------------------------------ 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876397 226 daDARVDILgRTDLTGLPPTLVVAAGLDPLRDEAIELAQTLQEVGVTTSVLHYPGAVHGFWSLDGvLEQAAELDGDIANF 305
Cdd:COG0657   126 --DLTASPL-RADLAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAG-LPEARAALAEIAAF 201

                  ....
gi 2045876397 306 MAAL 309
Cdd:COG0657   202 LRRA 205
PRK10162 PRK10162
acetyl esterase;
33-308 3.35e-29

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 113.66  E-value: 3.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876397  33 RRAMEQVTRSQSERAPIALVHDVKITGGDGHIPARVYNPAPREELPLVvYAHGGGWCLGSVHAADGPCRRLARAARAVVV 112
Cdd:PRK10162   38 RQYYTLERRFWNAGAPEMATRAYMVPTPYGQVETRLYYPQPDSQATLF-YLHGGGFILGNLDTHDRIMRLLASYSGCTVI 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876397 113 SLEYRLAPESPFPAPLADCMAAVDAIVADPGLVGARPTRIVMMGDSAGGNLVLGTALQRRDAGLTSAD--ALVLVYpcvA 190
Cdd:PRK10162  117 GIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDYGINMSRIGFAGDSAGAMLALASALWLRDKQIDCGKvaGVLLWY---G 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876397 191 SPHTNARPSMRENAHA-PVLTKSTMAWYWDTHL-DGRDADARVDILGRTDLT-GLPPTLVVAAGLDPLRDEAIELAQTLQ 267
Cdd:PRK10162  194 LYGLRDSVSRRLLGGVwDGLTQQDLQMYEEAYLsNDADRESPYYCLFNNDLTrDVPPCFIAGAEFDPLLDDSRLLYQTLA 273
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2045876397 268 EVGVTTSVLHYPGAVHGFWSLDGVLEQAAELDGDIANFMAA 308
Cdd:PRK10162  274 AHQQPCEFKLYPGTLHAFLHYSRMMDTADDALRDGAQFFTA 314
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
68-169 6.38e-14

BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, previously known as bifunctional carbohydrate esterase (CE)), which is active on complex natural xylans and was identified as the basis of a monophyletic clade gathering all homologs identified in PULs (polysaccharide utilization loci) predicted to act on xylan. It adopts an alpha-beta-hydrolase fold with the catalytic triad Ser-Asp-His. This new family of proteins is a new candidate for biomass processing due to its capacity to remove ferulic acid and acetic acid from natural corn and birchwood xylan substrates.


Pssm-ID: 466583 [Multi-domain]  Cd Length: 215  Bit Score: 69.52  E-value: 6.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876397  68 VYNPAPRE-ELPLVVYAHGGGWCLGSVHAADGPCRRLARAARAV---VVSLEYRLAPESPFPAPLADCMAAVDAIVADPG 143
Cdd:pfam20434   3 IYLPKNAKgPYPVVIWIHGGGWNSGDKEADMGFMTNTVKALLKAgyaVASINYRLSTDAKFPAQIQDVKAAIRFLRANAA 82
                          90       100
                  ....*....|....*....|....*.
gi 2045876397 144 LVGARPTRIVMMGDSAGGNLVLGTAL 169
Cdd:pfam20434  83 KYGIDTNKIALMGFSAGGHLALLAGL 108
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
57-285 9.62e-13

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 66.58  E-value: 9.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876397  57 ITGGDGH-IPARVYNPAPREELPLVVYAHGggwclgsvhaadGPCRRLARAARAVVV---------SLEYRLAPESP--- 123
Cdd:COG1506     2 FKSADGTtLPGWLYLPADGKKYPVVVYVHG------------GPGSRDDSFLPLAQAlasrgyavlAPDYRGYGESAgdw 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876397 124 FPAPLADCMAAVDAIVADPglvGARPTRIVMMGDSAGGNLVLGTALQRRDAgltsADALVLVYPcVASPHTNARpsmren 203
Cdd:COG1506    70 GGDEVDDVLAAIDYLAARP---YVDPDRIGIYGHSYGGYMALLAAARHPDR----FKAAVALAG-VSDLRSYYG------ 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876397 204 ahapvLTKSTMAWYWDTHLDGRDADARVDILGRTD-LTGlpPTLVVAAGLDPL--RDEAIELAQTLQEVGVTTSVLHYPG 280
Cdd:COG1506   136 -----TTREYTERLMGGPWEDPEAYAARSPLAYADkLKT--PLLLIHGEADDRvpPEQAERLYEALKKAGKPVELLVYPG 208

                  ....*
gi 2045876397 281 AVHGF 285
Cdd:COG1506   209 EGHGF 213
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
127-299 2.40e-06

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 47.61  E-value: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876397 127 PLADCMAAVDAIVADpGLVGarPTRIVMMGDSAGGNLVLGTALQRRDagltsadalvlVYPCVAsphtnarpsmrenAHA 206
Cdd:pfam00326  44 EFDDFIAAAEYLIEQ-GYTD--PDRLAIWGGSYGGYLTGAALNQRPD-----------LFKAAV-------------AHV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876397 207 PVLtkSTMAWYWDTHLD-----------GRDADARVDILGRTDLTGL---PPTLVVAAGLDP--LRDEAIELAQTLQEVG 270
Cdd:pfam00326  97 PVV--DWLAYMSDTSLPfterymewgnpWDNEEGYDYLSPYSPADNVkvyPPLLLIHGLLDDrvPPWQSLKLVAALQRKG 174
                         170       180       190
                  ....*....|....*....|....*....|
gi 2045876397 271 VTTSVLHYPGAVHGFWS-LDGVLEQAAELD 299
Cdd:pfam00326 175 VPFLLLIFPDEGHGIGKpRNKVEEYARELA 204
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
53-308 1.60e-05

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 44.99  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876397  53 HDVKITGGDGH-IPARVYNPAPREElPLVVYAHGGGWCLGS--------------VHAADGPCRRLARAARAVVVSleyr 117
Cdd:COG2267     4 RLVTLPTRDGLrLRGRRWRPAGSPR-GTVVLVHGLGEHSGRyaelaealaaagyaVLAFDLRGHGRSDGPRGHVDS---- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876397 118 lapespFPAPLADCMAAVDAIVADPGLvgarptRIVMMGDSAGGNLVLGTALQRRDAgltsADALVLVypcvaSPHTNAR 197
Cdd:COG2267    79 ------FDDYVDDLRAALDALRARPGL------PVVLLGHSMGGLIALLYAARYPDR----VAGLVLL-----APAYRAD 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876397 198 PsmrenahapvLTKSTMAWYWDTHLdgRDADARVDIlgrtdltglpPTLVVAAGLDPLRDEAiELAQTLQEVGVTTSVLH 277
Cdd:COG2267   138 P----------LLGPSARWLRALRL--AEALARIDV----------PVLVLHGGADRVVPPE-AARRLAARLSPDVELVL 194
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2045876397 278 YPGAVHGFwSLDGVLEQAAEldgDIANFMAA 308
Cdd:COG2267   195 LPGARHEL-LNEPAREEVLA---AILAWLER 221
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
53-285 3.10e-05

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 44.19  E-value: 3.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876397  53 HDVKITGGDGH-IPARVYNPAPREELPLVVYAHGGG--------WC-----LG-SVHAADGPCRRLARAARAVVVSLEYR 117
Cdd:COG0412     4 ETVTIPTPDGVtLPGYLARPAGGGPRPGVVVLHEIFglnphirdVArrlaaAGyVVLAPDLYGRGGPGDDPDEARALMGA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876397 118 LAPEspfpAPLADCMAAVDAIVADPglvGARPTRIVMMGDSAGGNLVLGTALQRRDagltsADALVLVYPcvasphtnar 197
Cdd:COG0412    84 LDPE----LLAADLRAALDWLKAQP---EVDAGRVGVVGFCFGGGLALLAAARGPD-----LAAAVSFYG---------- 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876397 198 psmrenahapvltkstmawywdthldGRDADARVDILGRTDltglPPTLVVAAGLDPL--RDEAIELAQTLQEVGVTTSV 275
Cdd:COG0412   142 --------------------------GLPADDLLDLAARIK----APVLLLYGEKDPLvpPEQVAALEAALAAAGVDVEL 191
                         250
                  ....*....|
gi 2045876397 276 LHYPGAVHGF 285
Cdd:COG0412   192 HVYPGAGHGF 201
 
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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