NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|502860886|ref|WP_013095862|]
View 

MULTISPECIES: YbgC/FadM family acyl-CoA thioesterase [Enterobacter]

Protein Classification

YbgC/FadM family acyl-CoA thioesterase( domain architecture ID 10794435)

YbgC/FadM family acyl-CoA thioesterase similar to Escherichia coli long-chain acyl-CoA thioesterase FadM and Bacillus subtilis acyl-CoA thioesterase YneP

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
TIGR00051 TIGR00051
acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related ...
 4-120 1.51e-49

acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related acyl-CoA thioesterases that include several at least partially characterized proteins. YbgC is an acyl-CoA thioesterase associated with the Tol-Pal system. YbaW is part of the FadM regulon. [Unknown function, General]


:

Pssm-ID: 129161 [Multi-domain]  Cd Length: 117  Bit Score: 154.11  E-value: 1.51e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860886    4 KIKVRGFHLDVYQHVNNARYLEFLEEARWDGLENSESFQWLTAHN-IAFVVVNININYRRPAVLGDVLTVTSQVQQLNGK 82
Cdd:TIGR00051   1 PVRVYYEDTDAQGIVYHANYLRYCERARTEFLRSLGFPQSVLRAEgVAFVVVNINIEYKKPARLDDVLEIRTQIEELNGF 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 502860886   83 SGVLSQIVTLDPEGQVVADALITFvCIDLKTQKALPLE 120
Cdd:TIGR00051  81 SFVFSQEIFNEDEALLKAATVIVV-CVDPKKQKPVAIP 117
 
Name Accession Description Interval E-value
TIGR00051 TIGR00051
acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related ...
 4-120 1.51e-49

acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related acyl-CoA thioesterases that include several at least partially characterized proteins. YbgC is an acyl-CoA thioesterase associated with the Tol-Pal system. YbaW is part of the FadM regulon. [Unknown function, General]


Pssm-ID: 129161 [Multi-domain]  Cd Length: 117  Bit Score: 154.11  E-value: 1.51e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860886    4 KIKVRGFHLDVYQHVNNARYLEFLEEARWDGLENSESFQWLTAHN-IAFVVVNININYRRPAVLGDVLTVTSQVQQLNGK 82
Cdd:TIGR00051   1 PVRVYYEDTDAQGIVYHANYLRYCERARTEFLRSLGFPQSVLRAEgVAFVVVNINIEYKKPARLDDVLEIRTQIEELNGF 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 502860886   83 SGVLSQIVTLDPEGQVVADALITFvCIDLKTQKALPLE 120
Cdd:TIGR00051  81 SFVFSQEIFNEDEALLKAATVIVV-CVDPKKQKPVAIP 117
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 2-128 2.32e-41

Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440586 [Multi-domain]  Cd Length: 139  Bit Score: 133.87  E-value: 2.32e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860886   2 QTKIKVRGFHLDVYQHVNNARYLEFLEEARWDGL-ENSESFQWLTAHNIAFVVVNININYRRPAVLGDVLTVTSQVQQLN 80
Cdd:COG0824    7 ETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLrALGLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTVETRVVRLG 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 502860886  81 GKSGVLSQIVTLDPEGQVVADALITFVCIDLKTQKALPLEGELREKLE 128
Cdd:COG0824   87 GSSLTFEYEIFRADDGELLATGETVLVFVDLETGRPVPLPDELRAALE 134
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 3-110 2.48e-31

4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate degradation pathway in which 4-chlorobenzoate is converted to 4-hydroxybenzoate in certain soil-dwelling bacteria. 4HBT forms a homotetramer with four active sites. There is no evidence to suggest that 4HBT is related to the type I thioesterases functioning in primary or secondary metabolic pathways. Each subunit of the 4HBT tetramer adopts a so-called hot-dog fold similar to those of beta-hydroxydecanoyl-ACP dehydratase, (R)-specific enoyl-CoA hydratase, and type II, thioesterase (TEII).


Pssm-ID: 238329 [Multi-domain]  Cd Length: 110  Bit Score: 107.69  E-value: 2.48e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860886   3 TKIKVRGFHLDVYQHVNNARYLEFLEEARWDGLEN-SESFQWLTAHNIAFVVVNININYRRPAVLGDVLTVTSQVQQLNG 81
Cdd:cd00586    3 LEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRElGLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRLGR 82

                         90       100
                 ....*....|....*....|....*....
gi 502860886  82 KSGVLSQIVTlDPEGQVVADALITFVCID 110
Cdd:cd00586   83 KSFTFEQEIF-REDGELLATAETVLVCVD 110
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 11-127 4.06e-22

Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally thioesterases. These enzymes are part of the Hotdog fold superfamily.


Pssm-ID: 463826  Cd Length: 121  Bit Score: 84.31  E-value: 4.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860886   11 HLDVYQHVNNARYLEFLEEARWDGLE-NSESFQWLTAHNIAFVVVNININYRRPAVLGDVLTVTSQVQQLNGKSGVLSQI 89
Cdd:pfam13279   5 DIDANGHMNNARYLRYFEEARDRFLErLGLDLAYREALGIGLILAEAHVRYRRELKLGDELTVETRLIDWDAKRFHLEHR 84

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 502860886   90 VtLDPEGQVVADALITFVCIDLKTQKALPLEGELREKL 127
Cdd:pfam13279  85 F-LSPDGKLVATAETRLVFVDYETRKPAPIPEELLEAL 121
PRK10800 PRK10800
acyl-CoA thioesterase YbgC; Provisional
 18-118 2.07e-13

acyl-CoA thioesterase YbgC; Provisional


Pssm-ID: 182742  Cd Length: 130  Bit Score: 62.45  E-value: 2.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860886  18 VNNARYLEFLEEARWDGL-ENSESFQWLTAHNIAFVVVNININYRRPAVLGDVLTVTSQVQQLNGKSGVLSQIVtLDPEG 96
Cdd:PRK10800  20 VYHASYVAFYERARTEMLrHHHFSQQALLAERVAFVVRKMTVEYYAPARLDDMLEVQSEITSMRGTSLTFTQRI-VNAEG 98

                         90       100
                 ....*....|....*....|....
gi 502860886  97 QVVADALITFVCIDLKTQK--ALP 118
Cdd:PRK10800  99 TLLNEAEVLIVCVDPLKMKprALP 122
 
Name Accession Description Interval E-value
TIGR00051 TIGR00051
acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related ...
 4-120 1.51e-49

acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related acyl-CoA thioesterases that include several at least partially characterized proteins. YbgC is an acyl-CoA thioesterase associated with the Tol-Pal system. YbaW is part of the FadM regulon. [Unknown function, General]


Pssm-ID: 129161 [Multi-domain]  Cd Length: 117  Bit Score: 154.11  E-value: 1.51e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860886    4 KIKVRGFHLDVYQHVNNARYLEFLEEARWDGLENSESFQWLTAHN-IAFVVVNININYRRPAVLGDVLTVTSQVQQLNGK 82
Cdd:TIGR00051   1 PVRVYYEDTDAQGIVYHANYLRYCERARTEFLRSLGFPQSVLRAEgVAFVVVNINIEYKKPARLDDVLEIRTQIEELNGF 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 502860886   83 SGVLSQIVTLDPEGQVVADALITFvCIDLKTQKALPLE 120
Cdd:TIGR00051  81 SFVFSQEIFNEDEALLKAATVIVV-CVDPKKQKPVAIP 117
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 2-128 2.32e-41

Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440586 [Multi-domain]  Cd Length: 139  Bit Score: 133.87  E-value: 2.32e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860886   2 QTKIKVRGFHLDVYQHVNNARYLEFLEEARWDGL-ENSESFQWLTAHNIAFVVVNININYRRPAVLGDVLTVTSQVQQLN 80
Cdd:COG0824    7 ETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLrALGLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTVETRVVRLG 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 502860886  81 GKSGVLSQIVTLDPEGQVVADALITFVCIDLKTQKALPLEGELREKLE 128
Cdd:COG0824   87 GSSLTFEYEIFRADDGELLATGETVLVFVDLETGRPVPLPDELRAALE 134
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 3-110 2.48e-31

4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate degradation pathway in which 4-chlorobenzoate is converted to 4-hydroxybenzoate in certain soil-dwelling bacteria. 4HBT forms a homotetramer with four active sites. There is no evidence to suggest that 4HBT is related to the type I thioesterases functioning in primary or secondary metabolic pathways. Each subunit of the 4HBT tetramer adopts a so-called hot-dog fold similar to those of beta-hydroxydecanoyl-ACP dehydratase, (R)-specific enoyl-CoA hydratase, and type II, thioesterase (TEII).


Pssm-ID: 238329 [Multi-domain]  Cd Length: 110  Bit Score: 107.69  E-value: 2.48e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860886   3 TKIKVRGFHLDVYQHVNNARYLEFLEEARWDGLEN-SESFQWLTAHNIAFVVVNININYRRPAVLGDVLTVTSQVQQLNG 81
Cdd:cd00586    3 LEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRElGLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRLGR 82

                         90       100
                 ....*....|....*....|....*....
gi 502860886  82 KSGVLSQIVTlDPEGQVVADALITFVCID 110
Cdd:cd00586   83 KSFTFEQEIF-REDGELLATAETVLVCVD 110
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 11-127 4.06e-22

Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally thioesterases. These enzymes are part of the Hotdog fold superfamily.


Pssm-ID: 463826  Cd Length: 121  Bit Score: 84.31  E-value: 4.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860886   11 HLDVYQHVNNARYLEFLEEARWDGLE-NSESFQWLTAHNIAFVVVNININYRRPAVLGDVLTVTSQVQQLNGKSGVLSQI 89
Cdd:pfam13279   5 DIDANGHMNNARYLRYFEEARDRFLErLGLDLAYREALGIGLILAEAHVRYRRELKLGDELTVETRLIDWDAKRFHLEHR 84

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 502860886   90 VtLDPEGQVVADALITFVCIDLKTQKALPLEGELREKL 127
Cdd:pfam13279  85 F-LSPDGKLVATAETRLVFVDYETRKPAPIPEELLEAL 121
FatA COG3884
Acyl-ACP thioesterase [Lipid transport and metabolism];
3-106 7.56e-15

Acyl-ACP thioesterase [Lipid transport and metabolism];


Pssm-ID: 443092 [Multi-domain]  Cd Length: 242  Bit Score: 68.05  E-value: 7.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860886   3 TKIKVRGFHLDVYQHVNNARYLEFLEEARWDglensesfQWLTAHniafVVVNININYRRPAVLGDVLTVTSQVQQlngk 82
Cdd:COG3884  152 KEFTVRYSDIDTNGHVNNARYLEWALDALPL--------EFLKNH----RLKRLEINYLKEVRLGDTVEVRSARDE---- 215

                         90       100
                 ....*....|....*....|....
gi 502860886  83 SGVLSQIVTLDPEGQVVADALITF 106
Cdd:COG3884  216 DGRTLHRIVGDDDGKELARARIEW 239
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 3-107 1.06e-14

The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.


Pssm-ID: 239524 [Multi-domain]  Cd Length: 100  Bit Score: 64.80  E-value: 1.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860886   3 TKIKVRGFHLDVYQHVNNARYLEFLEEARWdglensESFQWLTAHNIAFVVVNININYRRPAVLGDVLTVTSQVQQLNGK 82
Cdd:cd03440    3 LRLTVTPEDIDGGGIVHGGLLLALADEAAG------AAAARLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRS 76

                         90       100
                 ....*....|....*....|....*
gi 502860886  83 SGVLSQIVTlDPEGQVVADALITFV 107
Cdd:cd03440   77 SVTVEVEVR-NEDGKLVATATATFV 100
PRK10800 PRK10800
acyl-CoA thioesterase YbgC; Provisional
 18-118 2.07e-13

acyl-CoA thioesterase YbgC; Provisional


Pssm-ID: 182742  Cd Length: 130  Bit Score: 62.45  E-value: 2.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860886  18 VNNARYLEFLEEARWDGL-ENSESFQWLTAHNIAFVVVNININYRRPAVLGDVLTVTSQVQQLNGKSGVLSQIVtLDPEG 96
Cdd:PRK10800  20 VYHASYVAFYERARTEMLrHHHFSQQALLAERVAFVVRKMTVEYYAPARLDDMLEVQSEITSMRGTSLTFTQRI-VNAEG 98

                         90       100
                 ....*....|....*....|....
gi 502860886  97 QVVADALITFVCIDLKTQK--ALP 118
Cdd:PRK10800  99 TLLNEAEVLIVCVDPLKMKprALP 122
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 15-99 3.08e-13

Thioesterase superfamily; This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyzes the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyze the hydrolysis of other long chain fatty acyl-CoA thioesters.


Pssm-ID: 427116 [Multi-domain]  Cd Length: 79  Bit Score: 60.35  E-value: 3.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860886   15 YQHVNNARYLEFLEEARWDGLENSESFQwltahnIAFVVVNININYRRPAVLGDVLTVTSQVQQLNGKSGVLSQIVTLDP 94
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQ------QVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDED 74


                  ....*
gi 502860886   95 EGQVV 99
Cdd:pfam03061  75 GRLVA 79
Acyl-ACP_TE pfam01643
Acyl-ACP thioesterase; This family consists of various acyl-acyl carrier protein (ACP) ...
 5-106 2.23e-08

Acyl-ACP thioesterase; This family consists of various acyl-acyl carrier protein (ACP) thioesterases (TE) these terminate fatty acyl group extension via hydrolysing an acyl group on a fatty acid.


Pssm-ID: 366738 [Multi-domain]  Cd Length: 248  Bit Score: 50.81  E-value: 2.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860886    5 IKVRGFHLDVYQHVNNARYLEFLEEarwdglenSESFQWLTAHNIAfvvvNININYRRPAVLGDVLTVTSQVQQLNGKSG 84
Cdd:pfam01643 159 YHVRYSDIDMNQHVNNVKYLEWILE--------VLPLDFLDTHEPK----KITLKYEKEVQYGDDIEIITESAGSEEGLK 226

                          90       100
                  ....*....|....*....|..
gi 502860886   85 VLSQIvTLDpEGQVVADALITF 106
Cdd:pfam01643 227 TLHEI-RNS-TGEEIAQARTDW 246
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 48-112 5.43e-08

Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 48.40  E-value: 5.43e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502860886  48 NIAFVVVNININYRRPAVLGDVLTVTSQVQQLNGKSGVLSQIVTlDPEGQVVADALITFVCIDLK 112
Cdd:COG2050   74 GRRAVTIELNINFLRPARLGDRLTAEARVVRRGRRLAVVEVEVT-DEDGKLVATATGTFAVLPKR 137
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 50-107 4.51e-05

PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several proteins responsible for phenylacetic acid (PA) degradation in bacteria. Although orthologs of PaaI exist in archaea and eukaryotes, their function has not been determined. Sequence similarity between PaaI, E. coli medium chain acyl-CoA thioesterase II, and human thioesterase III suggests they all belong to the same thioesterase superfamily. The conserved fold present in these thioesterases is referred to as an asymmetric hot dog fold, similar to those of 4-hydroxybenzoyl-CoA thioesterase (4HBT) and the beta-hydroxydecanoyl-ACP dehydratases (FabA/FabZ).


Pssm-ID: 239527 [Multi-domain]  Cd Length: 113  Bit Score: 39.85  E-value: 4.51e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 502860886  50 AFVVVNININYRRPAVLGDvLTVTSQVQQLnGKSGVLSQIVTLDPEGQVVADALITFV 107
Cdd:cd03443   57 LAVTVDLNVNYLRPARGGD-LTARARVVKL-GRRLAVVEVEVTDEDGKLVATARGTFA 112
Acyl-ACP_TE pfam01643
Acyl-ACP thioesterase; This family consists of various acyl-acyl carrier protein (ACP) ...
 47-128 6.76e-04

Acyl-ACP thioesterase; This family consists of various acyl-acyl carrier protein (ACP) thioesterases (TE) these terminate fatty acyl group extension via hydrolysing an acyl group on a fatty acid.


Pssm-ID: 366738 [Multi-domain]  Cd Length: 248  Bit Score: 37.72  E-value: 6.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860886   47 HNIAFVVVNININYRRPAVLGDVLTVTSQVQQLNgKSGVLSQIVTLDPEGQVVADALITFVCIDLKTQKALPLEGELREK 126
Cdd:pfam01643  52 YNLVWVVYRYEIDIERLPEFGDMIEIETWASSYN-KFFCYRRFRVYDEKGEKIIEAKSTWVLMDRETRRPHRVPDEIRAP 130


                  ..
gi 502860886  127 LE 128
Cdd:pfam01643 131 YQ 132
 
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