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Conserved domains on  [gi|1890346404|ref|NP_001373140|]
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N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D isoform 2 [Homo sapiens]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 581040)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold super family cl23716
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 129-237 1.74e-50

mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.


The actual alignment was detected with superfamily member cd16283:

Pssm-ID: 451500  Cd Length: 181  Bit Score: 165.14  E-value: 1.74e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346404 129 WLGHATVMVEMDELIFLTDPIFSSRASPSQYMGPKRFRRSPCTISELPPIDAVLISHNHYDHLDYNSVIALNERF----- 203
Cdd:cd16283     1 WIGHATFLIQIEGLNILTDPVFSERASPVSFGGPKRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRPpylvp 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346404 204 -------------------------------------------------------------------GDTGYCPAFEEIG 216
Cdd:cd16283    81 lglkkwflkkgitnvveldwwqsteiggvritfvpaqhwsrrtlfdtneslwggwviegegfriyfaGDTGYFPGFREIG 160

                         170       180
                  ....*....|....*....|.
gi 1890346404 217 KRFGPFDLAAIPIGAYEPRWF 237
Cdd:cd16283   161 RRFGPIDLALLPIGAYEPRWF 181
 
Name Accession Description Interval E-value
RomA-like_MBL-fold cd16283
Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; ...
 129-237 1.74e-50

Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; Derepression of the romA-ramA locus results in a multidrug-resistance phenotype. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293841  Cd Length: 181  Bit Score: 165.14  E-value: 1.74e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346404 129 WLGHATVMVEMDELIFLTDPIFSSRASPSQYMGPKRFRRSPCTISELPPIDAVLISHNHYDHLDYNSVIALNERF----- 203
Cdd:cd16283     1 WIGHATFLIQIEGLNILTDPVFSERASPVSFGGPKRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRPpylvp 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346404 204 -------------------------------------------------------------------GDTGYCPAFEEIG 216
Cdd:cd16283    81 lglkkwflkkgitnvveldwwqsteiggvritfvpaqhwsrrtlfdtneslwggwviegegfriyfaGDTGYFPGFREIG 160

                         170       180
                  ....*....|....*....|.
gi 1890346404 217 KRFGPFDLAAIPIGAYEPRWF 237
Cdd:cd16283   161 RRFGPIDLALLPIGAYEPRWF 181
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 122-290 2.69e-45

L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 153.15  E-value: 2.69e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346404 122 EAGLRVTWLGHATVMVEMDELIFLTDPIFSSRASPsqymgpkrFRRSPCTISELPPIDAVLISHNHYDHLDYNSVIALNE 201
Cdd:COG2220     1 PGGMKITWLGHATFLIETGGKRILIDPVFSGRASP--------VNPLPLDPEDLPKIDAVLVTHDHYDHLDDATLRALKR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346404 202 RF-----------------------------------------------------------------------GDTGYCP 210
Cdd:COG2220    73 TGatvvaplgvaawlrawgfprvteldwgesvelggltvtavparhssgrpdrngglwvgfvietdgktiyhaGDTGYFP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346404 211 AFEEIGKRFgPFDLAAIPIGAYeprwfmkYQHVDPEEAVRIHTDVQTKKSMAIHWGTFALANEhylEPPVKLNEALERYG 290
Cdd:COG2220   153 EMKEIGERF-PIDVALLPIGAY-------PFTMGPEEAAEAARDLKPKVVIPIHYGTFPLLDE---DPLERFAAALAAAG 221
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 144-265 2.61e-20

Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 86.59  E-value: 2.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346404 144 FLTDPIFSSRASPSQYMGPKRFRRSPctiselppIDAVLISHNHYDHL----------------------------DYNS 195
Cdd:pfam12706   3 ILIDPGPDLRQQALPALQPGRLRDDP--------IDAVLLTHDHYDHLaglldlregrprplyaplgvlahlrrnfPYLF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346404 196 V----------IALNERF--------------------------------------------GDTGYCPafEEIGKRFGP 221
Cdd:pfam12706  75 LlehygvrvheIDWGESFtvgdggltvtatparhgsprgldpnpgdtlgfriegpgkrvyyaGDTGYFP--DEIGERLGG 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1890346404 222 FDLAAIPIGAYEPRWFMKYQHVDPEEAVRIHTDVQTKKSMAIHW 265
Cdd:pfam12706 153 ADLLLLDGGAWRDDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 125-226 6.85e-08

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 52.12  E-value: 6.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346404 125 LRVTWLGHATVMVEMDELIFLTDPIFSSRASpsqymgpkrfrrSPCTISELPPiDAVLISHNHYDHLdynsvialnerfG 204
Cdd:PRK00685    1 MKITWLGHSAFLIETGGKKILIDPFITGNPL------------ADLKPEDVKV-DYILLTHGHGDHL------------G 55

                          90       100
                  ....*....|....*....|....*..
gi 1890346404 205 DTgycpafEEIGKR-----FGPFDLAA 226
Cdd:PRK00685   56 DT------VEIAKRtgatvIANAELAN 76
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 175-213 8.37e-03

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 36.76  E-value: 8.37e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1890346404  175 LPPIDAVLISHNHYDHldYNSVIALNERFGDTGYCPAFE 213
Cdd:smart00849  33 PKKIDAIILTHGHPDH--IGGLPELLEAPGAPVYAPEGT 69
 
Name Accession Description Interval E-value
RomA-like_MBL-fold cd16283
Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; ...
 129-237 1.74e-50

Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; Derepression of the romA-ramA locus results in a multidrug-resistance phenotype. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293841  Cd Length: 181  Bit Score: 165.14  E-value: 1.74e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346404 129 WLGHATVMVEMDELIFLTDPIFSSRASPSQYMGPKRFRRSPCTISELPPIDAVLISHNHYDHLDYNSVIALNERF----- 203
Cdd:cd16283     1 WIGHATFLIQIEGLNILTDPVFSERASPVSFGGPKRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRPpylvp 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346404 204 -------------------------------------------------------------------GDTGYCPAFEEIG 216
Cdd:cd16283    81 lglkkwflkkgitnvveldwwqsteiggvritfvpaqhwsrrtlfdtneslwggwviegegfriyfaGDTGYFPGFREIG 160

                         170       180
                  ....*....|....*....|.
gi 1890346404 217 KRFGPFDLAAIPIGAYEPRWF 237
Cdd:cd16283   161 RRFGPIDLALLPIGAYEPRWF 181
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 122-290 2.69e-45

L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 153.15  E-value: 2.69e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346404 122 EAGLRVTWLGHATVMVEMDELIFLTDPIFSSRASPsqymgpkrFRRSPCTISELPPIDAVLISHNHYDHLDYNSVIALNE 201
Cdd:COG2220     1 PGGMKITWLGHATFLIETGGKRILIDPVFSGRASP--------VNPLPLDPEDLPKIDAVLVTHDHYDHLDDATLRALKR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346404 202 RF-----------------------------------------------------------------------GDTGYCP 210
Cdd:COG2220    73 TGatvvaplgvaawlrawgfprvteldwgesvelggltvtavparhssgrpdrngglwvgfvietdgktiyhaGDTGYFP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346404 211 AFEEIGKRFgPFDLAAIPIGAYeprwfmkYQHVDPEEAVRIHTDVQTKKSMAIHWGTFALANEhylEPPVKLNEALERYG 290
Cdd:COG2220   153 EMKEIGERF-PIDVALLPIGAY-------PFTMGPEEAAEAARDLKPKVVIPIHYGTFPLLDE---DPLERFAAALAAAG 221
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 144-265 2.61e-20

Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 86.59  E-value: 2.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346404 144 FLTDPIFSSRASPSQYMGPKRFRRSPctiselppIDAVLISHNHYDHL----------------------------DYNS 195
Cdd:pfam12706   3 ILIDPGPDLRQQALPALQPGRLRDDP--------IDAVLLTHDHYDHLaglldlregrprplyaplgvlahlrrnfPYLF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346404 196 V----------IALNERF--------------------------------------------GDTGYCPafEEIGKRFGP 221
Cdd:pfam12706  75 LlehygvrvheIDWGESFtvgdggltvtatparhgsprgldpnpgdtlgfriegpgkrvyyaGDTGYFP--DEIGERLGG 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1890346404 222 FDLAAIPIGAYEPRWFMKYQHVDPEEAVRIHTDVQTKKSMAIHW 265
Cdd:pfam12706 153 ADLLLLDGGAWRDDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
Lactamase_B_3 pfam13483
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 126-190 3.38e-08

Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.


Pssm-ID: 433247 [Multi-domain]  Cd Length: 160  Bit Score: 52.21  E-value: 3.38e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1890346404 126 RVTWLGHATVMVEMDELIFLTDPifssraspsqymgpkrFRRSPCTISELPPIDAVLISHNHYDH 190
Cdd:pfam13483   1 EITWLGHSSFLIEGGGARILTDP----------------FRATVGYRPPPVTADLVLISHGHDDH 49
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 125-226 6.85e-08

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 52.12  E-value: 6.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346404 125 LRVTWLGHATVMVEMDELIFLTDPIFSSRASpsqymgpkrfrrSPCTISELPPiDAVLISHNHYDHLdynsvialnerfG 204
Cdd:PRK00685    1 MKITWLGHSAFLIETGGKKILIDPFITGNPL------------ADLKPEDVKV-DYILLTHGHGDHL------------G 55

                          90       100
                  ....*....|....*....|....*..
gi 1890346404 205 DTgycpafEEIGKR-----FGPFDLAA 226
Cdd:PRK00685   56 DT------VEIAKRtgatvIANAELAN 76
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 178-252 4.48e-03

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry. Some members of this subgroup are named as octanoyltransferase (also known as lipoate-protein ligase B).


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 37.45  E-value: 4.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346404 178 IDAVLISHNHYDHL----DYNSVIALNERFGDTgYCPAF--EEIGKRFGPFdlAAIPIGAYEPRWFMkyQHVDPEEAVRI 251
Cdd:cd16279    67 LDAVLLTHAHADHIhgldDLRPFNRLQQRPIPV-YASEEtlDDLKRRFPYF--FAATGGGGVPKLDL--HIIEPDEPFTI 141


                  .
gi 1890346404 252 H 252
Cdd:cd16279   142 G 142
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 178-226 5.63e-03

Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Methanocaldococcus jannaschii 7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate synthase (EC 2.5.1.15), a folate biosynthetic enzyme also known as dihydropteroate synthase and 7,8 dihydropteroate synthase. Thermoanaerobacter tengcongensis Tflp is a ferredoxin-like member. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293799  Cd Length: 269  Bit Score: 37.60  E-value: 5.63e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1890346404 178 IDAVLISHNHYDH-------LDYNS---VIALNERFGDTGYCPAFEEIGKRFGPFDLAA 226
Cdd:cd07713    56 IDAVVLSHGHYDHtgglkalLELNPkapVYAHPDAFEPRYSKRGGGKKGIGIGREELEK 114
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 175-213 8.37e-03

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 36.76  E-value: 8.37e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1890346404  175 LPPIDAVLISHNHYDHldYNSVIALNERFGDTGYCPAFE 213
Cdd:smart00849  33 PKKIDAIILTHGHPDH--IGGLPELLEAPGAPVYAPEGT 69
 
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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