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Conserved domains on  [gi|874361143|ref|WP_048655241|]
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dienelactone hydrolase family protein [Bacillus subtilis]

Protein Classification

dienelactone hydrolase family protein( domain architecture ID 10785456)

dienelactone hydrolase family protein plays a crucial role in chlorocatechol degradation via the modified ortho cleavage pathway

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  19508187|12369917
SCOP:  3000102

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
38-261 3.29e-28

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


:

Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 108.52  E-value: 3.29e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874361143  38 ETLLLDLNGHEKVPAYFVKPKkTEGPCPAVLFQHSHGGQYDRGKSELiegadylktpsffDELTSLGYGVLAIDHWGFGD 117
Cdd:COG0412    4 ETVTIPTPDGVTLPGYLARPA-GGGPRPGVVVLHEIFGLNPHIRDVA-------------RRLAAAGYVVLAPDLYGRGG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874361143 118 RRGKAEsEIFKemlLTGKVMWGMMIYDSLSALDYMQLRSDVQPDRIGTIGMSMGGLMAWWTAALDDRIKVCVdlcsqvdh 197
Cdd:COG0412   70 PGDDPD-EARA---LMGALDPELLAADLRAALDWLKAQPEVDAGRVGVVGFCFGGGLALLAAARGPDLAAAV-------- 137

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 874361143 198 hvliktqnldrhGFYYYVPSLAKHFSASEIQGliaprPHLSLVGVHDRLTPAEGVDKIEKELTA 261
Cdd:COG0412  138 ------------SFYGGLPADDLLDLAARIKA-----PVLLLYGEKDPLVPPEQVAALEAALAA 184
 
Name Accession Description Interval E-value
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
38-261 3.29e-28

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 108.52  E-value: 3.29e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874361143  38 ETLLLDLNGHEKVPAYFVKPKkTEGPCPAVLFQHSHGGQYDRGKSELiegadylktpsffDELTSLGYGVLAIDHWGFGD 117
Cdd:COG0412    4 ETVTIPTPDGVTLPGYLARPA-GGGPRPGVVVLHEIFGLNPHIRDVA-------------RRLAAAGYVVLAPDLYGRGG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874361143 118 RRGKAEsEIFKemlLTGKVMWGMMIYDSLSALDYMQLRSDVQPDRIGTIGMSMGGLMAWWTAALDDRIKVCVdlcsqvdh 197
Cdd:COG0412   70 PGDDPD-EARA---LMGALDPELLAADLRAALDWLKAQPEVDAGRVGVVGFCFGGGLALLAAARGPDLAAAV-------- 137

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 874361143 198 hvliktqnldrhGFYYYVPSLAKHFSASEIQGliaprPHLSLVGVHDRLTPAEGVDKIEKELTA 261
Cdd:COG0412  138 ------------SFYGGLPADDLLDLAARIKA-----PVLLLYGEKDPLVPPEQVAALEAALAA 184
AXE1 pfam05448
Acetyl xylan esterase (AXE1); This family consists of several bacterial acetyl xylan esterase ...
 46-189 4.68e-07

Acetyl xylan esterase (AXE1); This family consists of several bacterial acetyl xylan esterase proteins. Acetyl xylan esterases are enzymes that hydrolyse the ester linkages of the acetyl groups in position 2 and/or 3 of the xylose moieties of natural acetylated xylan from hardwood. These enzymes are one of the accessory enzymes which are part of the xylanolytic system, together with xylanases, beta-xylosidases, alpha-arabinofuranosidases and methylglucuronidases; these are all required for the complete hydrolysis of xylan.


Pssm-ID: 398876 [Multi-domain]  Cd Length: 316  Bit Score: 50.48  E-value: 4.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874361143   46 GHEKVPAYFVKPKKTEGPCPAVLfqHSHGgqYDRGKSELIEGADYlktpsffdelTSLGYGVLAIDHWGFGDRrGKAESE 125
Cdd:pfam05448  64 GGARIYAWYVVPKESEEKHPAVV--HFHG--YNGRRGDWHDMLHW----------AAHGYAVFVMDVRGQGGL-SEDDPR 128

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 874361143  126 IFKEMLLTGKVMWGMM---------IY-DSLSALDYMQLRSDVQPDRIGTIGMSMGGLMAWWTAALDDRIKVCV 189
Cdd:pfam05448 129 GPKGNTYKGHITRGLLdretyyyrrVFlDAVRAVEIVMSFPEVDEERIVVTGGSQGGALALAAAALSPRIKAVV 202
 
Name Accession Description Interval E-value
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
38-261 3.29e-28

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 108.52  E-value: 3.29e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874361143  38 ETLLLDLNGHEKVPAYFVKPKkTEGPCPAVLFQHSHGGQYDRGKSELiegadylktpsffDELTSLGYGVLAIDHWGFGD 117
Cdd:COG0412    4 ETVTIPTPDGVTLPGYLARPA-GGGPRPGVVVLHEIFGLNPHIRDVA-------------RRLAAAGYVVLAPDLYGRGG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874361143 118 RRGKAEsEIFKemlLTGKVMWGMMIYDSLSALDYMQLRSDVQPDRIGTIGMSMGGLMAWWTAALDDRIKVCVdlcsqvdh 197
Cdd:COG0412   70 PGDDPD-EARA---LMGALDPELLAADLRAALDWLKAQPEVDAGRVGVVGFCFGGGLALLAAARGPDLAAAV-------- 137

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 874361143 198 hvliktqnldrhGFYYYVPSLAKHFSASEIQGliaprPHLSLVGVHDRLTPAEGVDKIEKELTA 261
Cdd:COG0412  138 ------------SFYGGLPADDLLDLAARIKA-----PVLLLYGEKDPLVPPEQVAALEAALAA 184
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
48-259 8.91e-20

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 85.84  E-value: 8.91e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874361143  48 EKVPAYFVKPKKtEGPCPAVLFQHSHGGQYDRGkseliegadylkTPSFFDELTSLGYGVLAIDHWGFGDRRGKaeseif 127
Cdd:COG1506    8 TTLPGWLYLPAD-GKKYPVVVYVHGGPGSRDDS------------FLPLAQALASRGYAVLAPDYRGYGESAGD------ 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874361143 128 kemlltgkvmWGM-MIYDSLSALDYMQLRSDVQPDRIGTIGMSMGGLMAWWTAALD-DRIKVCVDLCSQVDHHVLIKTQN 205
Cdd:COG1506   69 ----------WGGdEVDDVLAAIDYLAARPYVDPDRIGIYGHSYGGYMALLAAARHpDRFKAAVALAGVSDLRSYYGTTR 138

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 874361143 206 LDRHGFYYYVPSLAKHFSASEIQGLIA--PRPHLSLVGVHDRLTPAEGVDKIEKEL 259
Cdd:COG1506  139 EYTERLMGGPWEDPEAYAARSPLAYADklKTPLLLIHGEADDRVPPEQAERLYEAL 194
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 57-186 3.21e-14

Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 70.71  E-value: 3.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874361143  57 PKKTEGPCPAVLFqhSHGGqydrgkSELIEG-ADYLKTpsffdeLTSLGYGVLAIDHWGFGDRRGKAESEIFKEmlltgk 135
Cdd:COG1073   30 PAGASKKYPAVVV--AHGN------GGVKEQrALYAQR------LAELGFNVLAFDYRGYGESEGEPREEGSPE------ 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 874361143 136 vmwgmmIYDSLSALDYMQLRSDVQPDRIGTIGMSMGGLMAWWTAALDDRIK 186
Cdd:COG1073   90 ------RRDARAAVDYLRTLPGVDPERIGLLGISLGGGYALNAAATDPRVK 134
Axe1 COG3458
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, ...
 37-189 1.08e-09

Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442681 [Multi-domain]  Cd Length: 318  Bit Score: 58.28  E-value: 1.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874361143  37 VETLLLDLNGHEKVP--AYFVKPKKtEGPCPAVLfqHSHGgqYDRGKSELIEGADYlktpsffdelTSLGYGVLAIDHWG 114
Cdd:COG3458   54 VEVYDVTFTGFGGARiyGWLLRPKG-EGPLPAVV--EFHG--YGGGRGLPHEDLDW----------AAAGYAVLVMDTRG 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874361143 115 FGDRRGKAE-SEIFKEMLLTGKVMWGM-----MIY-----DSLSALDYMQLRSDVQPDRIGTIGMSMGGLMAWWTAALDD 183
Cdd:COG3458  119 QGSSWGDTPdPGGYSGGALPGYMTRGIddpdtYYYrrvylDAVRAVDALRSLPEVDGKRIGVTGGSQGGGLALAAAALDP 198


                 ....*.
gi 874361143 184 RIKVCV 189
Cdd:COG3458  199 RVKAAA 204
AXE1 pfam05448
Acetyl xylan esterase (AXE1); This family consists of several bacterial acetyl xylan esterase ...
 46-189 4.68e-07

Acetyl xylan esterase (AXE1); This family consists of several bacterial acetyl xylan esterase proteins. Acetyl xylan esterases are enzymes that hydrolyse the ester linkages of the acetyl groups in position 2 and/or 3 of the xylose moieties of natural acetylated xylan from hardwood. These enzymes are one of the accessory enzymes which are part of the xylanolytic system, together with xylanases, beta-xylosidases, alpha-arabinofuranosidases and methylglucuronidases; these are all required for the complete hydrolysis of xylan.


Pssm-ID: 398876 [Multi-domain]  Cd Length: 316  Bit Score: 50.48  E-value: 4.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874361143   46 GHEKVPAYFVKPKKTEGPCPAVLfqHSHGgqYDRGKSELIEGADYlktpsffdelTSLGYGVLAIDHWGFGDRrGKAESE 125
Cdd:pfam05448  64 GGARIYAWYVVPKESEEKHPAVV--HFHG--YNGRRGDWHDMLHW----------AAHGYAVFVMDVRGQGGL-SEDDPR 128

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 874361143  126 IFKEMLLTGKVMWGMM---------IY-DSLSALDYMQLRSDVQPDRIGTIGMSMGGLMAWWTAALDDRIKVCV 189
Cdd:pfam05448 129 GPKGNTYKGHITRGLLdretyyyrrVFlDAVRAVEIVMSFPEVDEERIVVTGGSQGGALALAAAALSPRIKAVV 202
DLH pfam01738
Dienelactone hydrolase family;
98-261 4.97e-06

Dienelactone hydrolase family;


Pssm-ID: 396343 [Multi-domain]  Cd Length: 213  Bit Score: 46.58  E-value: 4.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874361143   98 DELTSLGYGVLAID-HWGFGDRRGKAESEIFKEMLLTgKVMWGMMIYDSLSALDYMQLRSDVQPDRIGTIGMSMGGLMAW 176
Cdd:pfam01738  33 DRLADEGYVALAPDlYFRQGDPNDEADAARAMFELVS-KRVMEKVLDDLEAAVNYLKSQPEVSPKKVGVVGYCMGGALAV 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874361143  177 WTAALDDRIKVCVdlcsqvdhhvliktqnldrhGFYYYVPSLaKHFSASEIQGliaprPHLSLVGVHDRLTPAEGVDKIE 256
Cdd:pfam01738 112 LLAAKGPLVDAAV--------------------GFYGVGPEP-PLIEAPDIKA-----PILFHFGEEDHFVPADSRELIE 165


                  ....*
gi 874361143  257 KELTA 261
Cdd:pfam01738 166 EALKA 170
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
60-299 2.66e-05

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 44.22  E-value: 2.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874361143  60 TEGPCPAVLFQH---SHGGQYDRgkseliegadylktpsFFDELTSLGYGVLAIDHWGFGD---RRGKAESeifkemllt 133
Cdd:COG2267   24 AGSPRGTVVLVHglgEHSGRYAE----------------LAEALAAAGYAVLAFDLRGHGRsdgPRGHVDS--------- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874361143 134 gkvmWGMMIYDSLSALDYMQLRSDvqpDRIGTIGMSMGGLMAWWTAALDDRikvcvdlcsQVDHHVLIKTQNLDRHGFYY 213
Cdd:COG2267   79 ----FDDYVDDLRAALDALRARPG---LPVVLLGHSMGGLIALLYAARYPD---------RVAGLVLLAPAYRADPLLGP 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874361143 214 YVPSLAKHFSASEIQGLIAPRphLSLVGVHDRLTPAEGVDkiekeltAVYAGQGASDCYRVVRSASGHFETAVMRHEAVR 293
Cdd:COG2267  143 SARWLRALRLAEALARIDVPV--LVLHGGADRVVPPEAAR-------RLAARLSPDVELVLLPGARHELLNEPAREEVLA 213


                 ....*.
gi 874361143 294 FLQKWL 299
Cdd:COG2267  214 AILAWL 219
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 63-175 5.62e-04

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 40.66  E-value: 5.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874361143   63 PCPAVLFQH---SHGGQYDRgkseliegadylktpsFFDELTSLGYGVLAIDHWGFGD---RRGKAESeifkemlltgkv 136
Cdd:pfam12146   3 PRAVVVLVHglgEHSGRYAH----------------LADALAAQGFAVYAYDHRGHGRsdgKRGHVPS------------ 54

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 874361143  137 mWGMMIYDSLSALDYMQLRSDVQPdrIGTIGMSMGGLMA 175
Cdd:pfam12146  55 -FDDYVDDLDTFVDKIREEHPGLP--LFLLGHSMGGLIA 90
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 95-214 6.85e-04

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


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 40.18  E-value: 6.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874361143   95 SFFDELTSLGYGVLAIDHWGFG-DRRGKAESEifkemlltgkvmwgmMIYDSLSA-LDYMQLRSDVQPdrIGTIGMSMGG 172
Cdd:pfam00561  18 KLAPALARDGFRVIALDLRGFGkSSRPKAQDD---------------YRTDDLAEdLEYILEALGLEK--VNLVGHSMGG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 874361143  173 LMAWWTAAL-DDRIKVCVDLCSQVDHHVLIKTQNLDRHGFYYY 214
Cdd:pfam00561  81 LIALAYAAKyPDRVKALVLLGALDPPHELDEADRFILALFPGF 123
Abhydrolase_7 pfam12715
Abhydrolase family; This is a family of probable bacterial abhydrolases.
 50-245 8.09e-04

Abhydrolase family; This is a family of probable bacterial abhydrolases.


Pssm-ID: 403805 [Multi-domain]  Cd Length: 387  Bit Score: 40.50  E-value: 8.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874361143   50 VPAYFVKPKKTEGPCPAVLFQHSHGGQydrgKSELI--EGADYLKTPSFFDELTSL-------GYGVLAIDHWGFG---- 116
Cdd:pfam12715  99 STFLVLIPDNLKHPVPAVLCIPGSGGT----KEGLAgePGISPKLTQPYKQPKNAMalnyvkqGYIAVAVDNAAAGeasd 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874361143  117 ----DRRGKAESEIFKEMLLtgKVMWGMMIYDSL---SALDYMQLRSDVQPDRIGTIGMSMGG--LMAwwTAALDDRIKV 187
Cdd:pfam12715 175 lehyTKGSSYDYDVVSRFLL--ELGWSYLGYTSYldqQVLNWMKTQPYIRKDRIIVSGFSLGTepLMV--LGVLDPSIYA 250

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874361143  188 CV--DLCSQVDHHVLIKTQ----------NLDRHgfyyYVPSLAKHFSASEIQGLIAPRPHLSLVGVHDR 245
Cdd:pfam12715 251 FVynDFLCQTQERAIVMTKpdekgrrpfpNSIRH----LIPGFWKYFNFPDIVAALAPRPVILTEGGLDR 316
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
61-179 1.18e-03

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 40.09  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874361143  61 EGPCPAVLFQHSHGGqyDRgkseliEGADYLKTpsffdELTSLGYGVLAIDHWGfgDRRGKAESEIFKEMLLTGKVMWGM 140
Cdd:COG4188   59 GGPFPLVVLSHGLGG--SR------EGYAYLAE-----HLASHGYVVAAPDHPG--SNAADLSAALDGLADALDPEELWE 123

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 874361143 141 MIYDSLSALDYMQLRSD--------VQPDRIGTIGMSMGGlmawWTA 179
Cdd:COG4188  124 RPLDLSFVLDQLLALNKsdpplagrLDLDRIGVIGHSLGG----YTA 166
COG4099 COG4099
Predicted peptidase [General function prediction only];
146-180 3.09e-03

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 38.41  E-value: 3.09e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 874361143 146 LSALDYMQLRSDVQPDRIGTIGMSMGGLMAWWTAA 180
Cdd:COG4099  110 LALLDDLIAEYRIDPDRIYLTGLSMGGYGTWDLAA 144
 
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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