NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2569584919|ref|WP_306823530|]
View 

alpha/beta hydrolase [Qipengyuania flava]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11429202)

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
PubMed:  37582413|12369917|19508187

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
32-253 7.88e-40

Acetyl esterase/lipase [Lipid transport and metabolism];


:

Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 137.31  E-value: 7.88e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569584919  32 MAVFRPDR--PTGAAVLLIPGGGYRHVVVDKEGFEMGRWLSRRGITAFVLFYRLPGDgwaAGANVALSDAQRATRIIRAD 109
Cdd:COG0657     1 MDVYRPAGakGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPE---HPFPAALEDAYAALRWLRAN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569584919 110 ADRFTIDPQRVSAMGFSAGGHLCADLATRfalhtydahdAADTLSARPDGAACIYPVISMDpeiahagsrrlligehass 189
Cdd:COG0657    78 AAELGIDPDRIAVAGDSAGGHLAAALALR----------ARDRGGPRPAAQVLIYPVLDLT------------------- 128

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2569584919 190 qreraHSPDHNVTPDTPPMFLLHPEDDgsVPVENSLRMRAALRAQGIPVETHLFASGGHGFGLR 253
Cdd:COG0657   129 -----ASPLRADLAGLPPTLIVTGEAD--PLVDESEALAAALRAAGVPVELHVYPGGGHGFGLL 185
 
Name Accession Description Interval E-value
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
32-253 7.88e-40

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 137.31  E-value: 7.88e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569584919  32 MAVFRPDR--PTGAAVLLIPGGGYRHVVVDKEGFEMGRWLSRRGITAFVLFYRLPGDgwaAGANVALSDAQRATRIIRAD 109
Cdd:COG0657     1 MDVYRPAGakGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPE---HPFPAALEDAYAALRWLRAN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569584919 110 ADRFTIDPQRVSAMGFSAGGHLCADLATRfalhtydahdAADTLSARPDGAACIYPVISMDpeiahagsrrlligehass 189
Cdd:COG0657    78 AAELGIDPDRIAVAGDSAGGHLAAALALR----------ARDRGGPRPAAQVLIYPVLDLT------------------- 128

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2569584919 190 qreraHSPDHNVTPDTPPMFLLHPEDDgsVPVENSLRMRAALRAQGIPVETHLFASGGHGFGLR 253
Cdd:COG0657   129 -----ASPLRADLAGLPPTLIVTGEAD--PLVDESEALAAALRAAGVPVELHVYPGGGHGFGLL 185
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 44-231 6.82e-15

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: 71.83  E-value: 6.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569584919  44 AVLLIPGGGYRHVvvDKEGF-----EMGRWLSRRGitaFVLF---YRLPGDgwaAGANVALSDAQRATRIIRADADRFTI 115
Cdd:pfam20434  15 VVIWIHGGGWNSG--DKEADmgfmtNTVKALLKAG---YAVAsinYRLSTD---AKFPAQIQDVKAAIRFLRANAAKYGI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569584919 116 DPQRVSAMGFSAGGHLCADLATRFALHTYDAH-DAADTLSARPDG--AACI--YP---VISMDPEIAHAGSR---RLLIG 184
Cdd:pfam20434  87 DTNKIALMGFSAGGHLALLAGLSNNNKEFEGNvGDYTPESSKESFkvNAVVdfYGptdLLDMDSCGTHNDAKspeTLLLG 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2569584919 185 EHASSQRERAH--SPDHNVTPDTPPMFLLHPEDDGSVPVENSLRMRAAL 231
Cdd:pfam20434 167 APPLENPDLAKsaSPITYVDKNDPPFLIIHGDKDPLVPYCQSVLLHEKL 215
 
Name Accession Description Interval E-value
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
32-253 7.88e-40

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 137.31  E-value: 7.88e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569584919  32 MAVFRPDR--PTGAAVLLIPGGGYRHVVVDKEGFEMGRWLSRRGITAFVLFYRLPGDgwaAGANVALSDAQRATRIIRAD 109
Cdd:COG0657     1 MDVYRPAGakGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPE---HPFPAALEDAYAALRWLRAN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569584919 110 ADRFTIDPQRVSAMGFSAGGHLCADLATRfalhtydahdAADTLSARPDGAACIYPVISMDpeiahagsrrlligehass 189
Cdd:COG0657    78 AAELGIDPDRIAVAGDSAGGHLAAALALR----------ARDRGGPRPAAQVLIYPVLDLT------------------- 128

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2569584919 190 qreraHSPDHNVTPDTPPMFLLHPEDDgsVPVENSLRMRAALRAQGIPVETHLFASGGHGFGLR 253
Cdd:COG0657   129 -----ASPLRADLAGLPPTLIVTGEAD--PLVDESEALAAALRAAGVPVELHVYPGGGHGFGLL 185
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
34-273 1.47e-20

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 87.76  E-value: 1.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569584919  34 VFRPDRPTGA-AVLLIPGGGYRHvvvDKEGFEMGRWLSRRGITAFVLFYRLPGDGWAAGANVALSDAQRATRIIRADADr 112
Cdd:COG1506    14 LYLPADGKKYpVVVYVHGGPGSR---DDSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDEVDDVLAAIDYLAARPY- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569584919 113 ftIDPQRVSAMGFSAGGHLCADLATRFalhtydahdaadtlSARPDGAACIYPVISMDP--EIAHAGSRRLLIGEHASSQ 190
Cdd:COG1506    90 --VDPDRIGIYGHSYGGYMALLAAARH--------------PDRFKAAVALAGVSDLRSyyGTTREYTERLMGGPWEDPE 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569584919 191 RERAHSPDHNVTPDTPPMFLLHPEDDGSVPVENSLRMRAALRAQGIPVETHLFASGGHGFglrkaVGKPVEDWPALWLAW 270
Cdd:COG1506   154 AYAARSPLAYADKLKTPLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLVYPGEGHGF-----SGAGAPDYLERILDF 228


                  ...
gi 2569584919 271 AER 273
Cdd:COG1506   229 LDR 231
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 44-231 6.82e-15

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: 71.83  E-value: 6.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569584919  44 AVLLIPGGGYRHVvvDKEGF-----EMGRWLSRRGitaFVLF---YRLPGDgwaAGANVALSDAQRATRIIRADADRFTI 115
Cdd:pfam20434  15 VVIWIHGGGWNSG--DKEADmgfmtNTVKALLKAG---YAVAsinYRLSTD---AKFPAQIQDVKAAIRFLRANAAKYGI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569584919 116 DPQRVSAMGFSAGGHLCADLATRFALHTYDAH-DAADTLSARPDG--AACI--YP---VISMDPEIAHAGSR---RLLIG 184
Cdd:pfam20434  87 DTNKIALMGFSAGGHLALLAGLSNNNKEFEGNvGDYTPESSKESFkvNAVVdfYGptdLLDMDSCGTHNDAKspeTLLLG 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2569584919 185 EHASSQRERAH--SPDHNVTPDTPPMFLLHPEDDGSVPVENSLRMRAAL 231
Cdd:pfam20434 167 APPLENPDLAKsaSPITYVDKNDPPFLIIHGDKDPLVPYCQSVLLHEKL 215
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
34-250 9.09e-14

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 68.84  E-value: 9.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569584919  34 VFRPDRPTGA-AVLLIPG-GGYRHVVVDkegfeMGRWLSRRGITAFV--LFYRLPGDGWAAGANV---------ALSDAQ 100
Cdd:COG0412    20 LARPAGGGPRpGVVVLHEiFGLNPHIRD-----VARRLAAAGYVVLApdLYGRGGPGDDPDEARAlmgaldpelLAADLR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569584919 101 RATRIIRADADrftIDPQRVSAMGFSAGGHLCADLATRFalhtydahdaadtlsARPDGAACIYPVISMDPEIAHAGSRR 180
Cdd:COG0412    95 AALDWLKAQPE---VDAGRVGVVGFCFGGGLALLAAARG---------------PDLAAAVSFYGGLPADDLLDLAARIK 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569584919 181 lligehassqrerahspdhnvtpdtPPMFLLHPEDDGSVPVENSLRMRAALRAQGIPVETHLFASGGHGF 250
Cdd:COG0412   157 -------------------------APVLLLYGEKDPLVPPEQVAALEAALAAAGVDVELHVYPGAGHGF 201
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
110-251 5.23e-12

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 63.40  E-value: 5.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569584919 110 ADRFTIDPQRVSAMGFSAGGHLcadlatrfalhtydahdAADTLSARPD---GAACIYPVISMdpeIAHAGSRRLLIGE- 185
Cdd:pfam00326  56 IEQGYTDPDRLAIWGGSYGGYL-----------------TGAALNQRPDlfkAAVAHVPVVDW---LAYMSDTSLPFTEr 115

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2569584919 186 ---HASSQRERAH-------SPDHNVTpDTPPMFLLHPEDDGSVPVENSLRMRAALRAQGIPVETHLFASGGHGFG 251
Cdd:pfam00326 116 ymeWGNPWDNEEGydylspySPADNVK-VYPPLLLIHGLLDDRVPPWQSLKLVAALQRKGVPFLLLIFPDEGHGIG 190
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
31-248 1.76e-10

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 59.25  E-value: 1.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569584919  31 RMAVFRPDRPTGAAVLLIPGGGYRHVVVDkegfEMGRWLSRRGITafVLFYRLPGDGWAAGANVALSDAQRATRIIRADA 110
Cdd:COG2267    17 RGRRWRPAGSPRGTVVLVHGLGEHSGRYA----ELAEALAAAGYA--VLAFDLRGHGRSDGPRGHVDSFDDYVDDLRAAL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569584919 111 DRFTIDP-QRVSAMGFSAGGHLCADLATRFAlhtydahdaadtlsARPDGAACIYPVISMDPEIahAGSRRLLIGEHASS 189
Cdd:COG2267    91 DALRARPgLPVVLLGHSMGGLIALLYAARYP--------------DRVAGLVLLAPAYRADPLL--GPSARWLRALRLAE 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2569584919 190 QRERAhspdhnvtpdTPPMFLLHPEDDGSVPVENSLRMRAALRAQgipVETHLFASGGH 248
Cdd:COG2267   155 ALARI----------DVPVLVLHGGADRVVPPEAARRLAARLSPD---VELVLLPGARH 200
YpfH COG0400
Predicted esterase [General function prediction only];
80-249 1.64e-09

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 56.07  E-value: 1.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569584919  80 FYRLPGDGWAAGANVALSDAQRATRIIRADADRFTIDPQRVSAMGFSAGghlcADLATRFALHtydahdaadtlsaRPDG 159
Cdd:COG0400    51 WFDLSFLEGREDEEGLAAAAEALAAFIDELEARYGIDPERIVLAGFSQG----AAMALSLALR-------------RPEL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569584919 160 AACIypvismdpeIAHAGsrrLLIGEHASSQRERAHSpdhnvtpdTPPMFLLHPEDDGSVPVENSLRMRAALRAQGIPVE 239
Cdd:COG0400   114 LAGV---------VALSG---YLPGEEALPAPEAALA--------GTPVFLAHGTQDPVIPVERAREAAEALEAAGADVT 173

                         170
                  ....*....|
gi 2569584919 240 THLFAsGGHG 249
Cdd:COG0400   174 YREYP-GGHE 182
COG4099 COG4099
Predicted peptidase [General function prediction only];
76-249 5.95e-09

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 54.97  E-value: 5.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569584919  76 AFVLFYRLP-GDGWAAGanvalSDAQRATRIIRADADRFTIDPQRVSAMGFSAGGHLCADLATRfalhtydahdaadtls 154
Cdd:COG4099    87 AIVLAPQCPeDDYWSDT-----KALDAVLALLDDLIAEYRIDPDRIYLTGLSMGGYGTWDLAAR---------------- 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569584919 155 aRPDGAACIYPVISM-DPEIAhagsRRLligehassqrerahspdHNVtpdtpPMFLLHPEDDGSVPVENSLRMRAALRA 233
Cdd:COG4099   146 -YPDLFAAAVPICGGgDPANA----ANL-----------------KKV-----PVWIFHGAKDDVVPVEESRAMVEALKA 198

                         170
                  ....*....|....*.
gi 2569584919 234 QGIPVETHLFASGGHG 249
Cdd:COG4099   199 AGADVKYTEYPGVGHN 214
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 95-250 3.07e-08

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: 52.60  E-value: 3.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569584919  95 ALSDAQRATRIIRADADRFTIDPQRVSAMGFSAGGHLcadlatrfALHTydAHDAADTLSARPDGAACIYPVISMDPE-- 172
Cdd:pfam07859  48 AYDDAYAALRWLAEQAAELGADPSRIAVAGDSAGGNL--------AAAV--ALRARDEGLPKPAGQVLIYPGTDLRTEsp 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569584919 173 --IAHAGSRRLLIGEHASSQRERAHSPDHNVtpDTPPMFLLHPEDDGSVP------------VENSLRMRAALRAQGIPV 238
Cdd:pfam07859 118 syLAREFADGPLLTRAAMDWFWRLYLPGADR--DDPLASPLFASDLSGLPpalvvvaefdplRDEGEAYAERLRAAGVPV 195

                         170
                  ....*....|..
gi 2569584919 239 ETHLFASGGHGF 250
Cdd:pfam07859 196 ELIEYPGMPHGF 207
DLH pfam01738
Dienelactone hydrolase family;
34-271 2.21e-04

Dienelactone hydrolase family;


Pssm-ID: 396343 [Multi-domain]  Cd Length: 213  Bit Score: 41.57  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569584919  34 VFRPDRPTGAAVLLIP--GGgyrhvvVDKEGFEMGRWLSRRGITAFV--LFYRLPGDGWAAGANVALSDAQRATRIIRAD 109
Cdd:pfam01738   4 LATPKNPPWPVVVVFQeiFG------VNDNIREIADRLADEGYVALApdLYFRQGDPNDEADAARAMFELVSKRVMEKVL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569584919 110 ADRF----------TIDPQRVSAMGFSAGGHLCADLATRFAlhtydahdaadtlsaRPDGAACIYPViSMDPEIAHAgsr 179
Cdd:pfam01738  78 DDLEaavnylksqpEVSPKKVGVVGYCMGGALAVLLAAKGP---------------LVDAAVGFYGV-GPEPPLIEA--- 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569584919 180 rlligehassqrerahsPDHNVtpdtpPMFLLHPEDDGSVPVENSLRMRAALRAQGIPVETHLFASGGHGFGLRKAvgkP 259
Cdd:pfam01738 139 -----------------PDIKA-----PILFHFGEEDHFVPADSRELIEEALKAANVDHQIHSYPGAGHAFANDSR---P 193

                         250
                  ....*....|..
gi 2569584919 260 VEDWPALWLAWA 271
Cdd:pfam01738 194 SYNAAAAEDAWE 205
 
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