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Conserved domains on  [gi|1806340298|dbj|BBY30099|]
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esterase [Mycolicibacterium sediminis]

Protein Classification

PaaI family thioesterase( domain architecture ID 10005230)

PaaI family thioesterase is a hotdog fold thioesterase similar to Escherichia coli PaaI, a thioesterase with a preference for ring-hydroxylated phenylacetyl-CoA esters

CATH:  3.10.129.10
EC:  3.1.2.-
Gene Ontology:  GO:0016790|GO:0016836|GO:0047617
PubMed:  15307895|16061252
TCDB:  9.B.371

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 1-138 1.26e-30

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


:

Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 106.95  E-value: 1.26e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806340298   1 MVVTTSDMNAF--DSGFSEVLGLTYLEATPDQVRAELLIHDGLLQPHGIVHGGVYCSIVESVASVSAGVWLesaGGGRNV 78
Cdd:COG2050     1 MSDPLERLEGFlaANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSAL---PPGRRA 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1806340298  79 VGVNNNTDFLRAITAG-VVTATSTPIHRGRRQQLWMVEIAGADGRLVARGQVRLQNLPADA 138
Cdd:COG2050    78 VTIELNINFLRPARLGdRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKRP 138
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 1-138 1.26e-30

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 106.95  E-value: 1.26e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806340298   1 MVVTTSDMNAF--DSGFSEVLGLTYLEATPDQVRAELLIHDGLLQPHGIVHGGVYCSIVESVASVSAGVWLesaGGGRNV 78
Cdd:COG2050     1 MSDPLERLEGFlaANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSAL---PPGRRA 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1806340298  79 VGVNNNTDFLRAITAG-VVTATSTPIHRGRRQQLWMVEIAGADGRLVARGQVRLQNLPADA 138
Cdd:COG2050    78 VTIELNINFLRPARLGdRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKRP 138
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 19-128 3.21e-27

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: 97.63  E-value: 3.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806340298  19 LGLTYLEATPDQVRAELLIHDGLLQPHGIVHGGVYCSIVESVASVSAGVWLesaGGGRNVVGVNNNTDFLRAITAGVVTA 98
Cdd:cd03443     2 LGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSAL---PPGALAVTVDLNVNYLRPARGGDLTA 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 1806340298  99 TSTPIHRGRRQQLWMVEIAGADGRLVARGQ 128
Cdd:cd03443    79 RARVVKLGRRLAVVEVEVTDEDGKLVATAR 108
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 14-125 2.09e-18

uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a single copy of this domain. A protein from C. elegans consists of two tandem copies of the domain. The domain is also found as the N-terminal region of an apparent initiation factor eIF-2B alpha subunit of Aquifex aeolicus. The function of the domain is unknown.


Pssm-ID: 161843 [Multi-domain]  Cd Length: 117  Bit Score: 75.07  E-value: 2.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806340298  14 GFSEVLGLTYLEATPDQVRAELLIHDGLLQPHGIVHGGVYCSIVESVASVSAgvwLESAGGGRNVVGVNNNTDFLRAITA 93
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAG---YLCNSGGQAVVGLELNANHLRPARE 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1806340298  94 GVVTATSTPIHRGRRQQLWMVEIAGADGRLVA 125
Cdd:TIGR00369  78 GKVRAIAQVVHLGRQTGVAEIEIVDEQGRLCA 109
PRK10254 PRK10254
proofreading thioesterase EntH;
19-122 3.07e-11

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 57.30  E-value: 3.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806340298  19 LGLTYLEATPDQVRAELLIHDGLLQPHGIVHGGVYCSIVESVASVSAgvWLESAGGgRNVVGVNNNTDFLRAITAGVVTA 98
Cdd:PRK10254   24 LGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAG--FLMTRDG-QCVVGTELNATHHRPVSEGKVRG 100

                          90       100
                  ....*....|....*....|....
gi 1806340298  99 TSTPIHRGRRQQLWMVEIAGADGR 122
Cdd:PRK10254  101 VCQPLHLGRQNQSWEIVVFDEQGR 124
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 45-125 5.02e-11

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: 54.95  E-value: 5.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806340298  45 HGIVHGGVYCSIVESVASVsagVWLESAGGGRNVVGVNNNTDFLRAITAG-VVTATSTPIHRGRRQQLWMVEIAGADGRL 123
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGA---AARRLGGSQQVVVVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRL 77


                  ..
gi 1806340298 124 VA 125
Cdd:pfam03061  78 VA 79
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 1-138 1.26e-30

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 106.95  E-value: 1.26e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806340298   1 MVVTTSDMNAF--DSGFSEVLGLTYLEATPDQVRAELLIHDGLLQPHGIVHGGVYCSIVESVASVSAGVWLesaGGGRNV 78
Cdd:COG2050     1 MSDPLERLEGFlaANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSAL---PPGRRA 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1806340298  79 VGVNNNTDFLRAITAG-VVTATSTPIHRGRRQQLWMVEIAGADGRLVARGQVRLQNLPADA 138
Cdd:COG2050    78 VTIELNINFLRPARLGdRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKRP 138
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 19-128 3.21e-27

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: 97.63  E-value: 3.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806340298  19 LGLTYLEATPDQVRAELLIHDGLLQPHGIVHGGVYCSIVESVASVSAGVWLesaGGGRNVVGVNNNTDFLRAITAGVVTA 98
Cdd:cd03443     2 LGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSAL---PPGALAVTVDLNVNYLRPARGGDLTA 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 1806340298  99 TSTPIHRGRRQQLWMVEIAGADGRLVARGQ 128
Cdd:cd03443    79 RARVVKLGRRLAVVEVEVTDEDGKLVATAR 108
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 14-125 2.09e-18

uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a single copy of this domain. A protein from C. elegans consists of two tandem copies of the domain. The domain is also found as the N-terminal region of an apparent initiation factor eIF-2B alpha subunit of Aquifex aeolicus. The function of the domain is unknown.


Pssm-ID: 161843 [Multi-domain]  Cd Length: 117  Bit Score: 75.07  E-value: 2.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806340298  14 GFSEVLGLTYLEATPDQVRAELLIHDGLLQPHGIVHGGVYCSIVESVASVSAgvwLESAGGGRNVVGVNNNTDFLRAITA 93
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAG---YLCNSGGQAVVGLELNANHLRPARE 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1806340298  94 GVVTATSTPIHRGRRQQLWMVEIAGADGRLVA 125
Cdd:TIGR00369  78 GKVRAIAQVVHLGRQTGVAEIEIVDEQGRLCA 109
PRK10254 PRK10254
proofreading thioesterase EntH;
19-122 3.07e-11

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 57.30  E-value: 3.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806340298  19 LGLTYLEATPDQVRAELLIHDGLLQPHGIVHGGVYCSIVESVASVSAgvWLESAGGgRNVVGVNNNTDFLRAITAGVVTA 98
Cdd:PRK10254   24 LGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAG--FLMTRDG-QCVVGTELNATHHRPVSEGKVRG 100

                          90       100
                  ....*....|....*....|....
gi 1806340298  99 TSTPIHRGRRQQLWMVEIAGADGR 122
Cdd:PRK10254  101 VCQPLHLGRQNQSWEIVVFDEQGR 124
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 45-125 5.02e-11

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: 54.95  E-value: 5.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806340298  45 HGIVHGGVYCSIVESVASVsagVWLESAGGGRNVVGVNNNTDFLRAITAG-VVTATSTPIHRGRRQQLWMVEIAGADGRL 123
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGA---AARRLGGSQQVVVVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRL 77


                  ..
gi 1806340298 124 VA 125
Cdd:pfam03061  78 VA 79
PLN02322 PLN02322
acyl-CoA thioesterase
 4-135 9.77e-11

acyl-CoA thioesterase


Pssm-ID: 177956  Cd Length: 154  Bit Score: 56.22  E-value: 9.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806340298   4 TTSDMNAFDSGFsEVLGLTYLEATPDQVRAELLIHDGLLQPHGIVHGGVYCSIVESVASVSAGVwlesAGGGRNVVGVNN 83
Cdd:PLN02322    2 ASSNTKAIDPPL-HMLGFEFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAHM----ASGFKRVAGIQL 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806340298  84 NTDFLRAITAG-VVTATSTPIHRGRRQQLWMVEI------AGADGRLVARGQVRLQ-NLP 135
Cdd:PLN02322   77 SINHLKSADLGdLVFAEATPVSTGKTIQVWEVKLwkttdkDKANKILISSSRVTLIcNLP 136
PaaD TIGR02286
phenylacetic acid degradation protein PaaD; This member of the domain family TIGR00369 (which ...
 16-130 1.86e-10

phenylacetic acid degradation protein PaaD; This member of the domain family TIGR00369 (which is, in turn, a member of the pfam03061 thioesterase superfamily) is nearly always found adjacent to other genes of the phenylacetic acid degradation pathway. Its function is currently unknown, but a role as a thioesterase is not inconsistent with the proposed overall pathway. Sequences scoring between trusted and noise include those from archaea and other species not known to catabolize phenylacetic acid and which are not adjacent to other genes potentially involved with such a pathway.


Pssm-ID: 131339  Cd Length: 114  Bit Score: 54.35  E-value: 1.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806340298  16 SEVLGLTYLEATPDQVRAELLIHDGLLQPHGIVHGGVYCSIVESVASVSagvwleSAGGGRNVVGVNNNTDFLRAITAG- 94
Cdd:TIGR02286   1 AKALGIDILELGPGFARVAMTVRADMLNGHGTAHGGFLFSLADSAFAYA------CNSYGDAAVAAQCTIDFLRPGRAGe 74

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1806340298  95 VVTATSTPIHRGRRQQLWMVEIAGADGRLVA--RGQVR 130
Cdd:TIGR02286  75 RLEAEAVEVSRGGRTGTYDVEVVNQEGELVAlfRGTSR 112
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
3-123 2.54e-10

1,4-dihydroxy-2-naphthoyl-CoA hydrolase;


Pssm-ID: 182360  Cd Length: 136  Bit Score: 54.63  E-value: 2.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806340298   3 VTTSDMNAFDSG-FSEVLGLTYLEATPDQVRAELLIHDGLLQPHGIVHGGVYCSIVESVASVSAGVWLEsagGGRNVVGV 81
Cdd:PRK10293    7 ITLEALNAMGEGnMVGLLDIRFEHIGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAGYLCTE---GEQKVVGL 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1806340298  82 NNNTDFLRAITAGVVTATSTPIHRGRRQQLWMVEIAGADGRL 123
Cdd:PRK10293   84 EINANHVRSAREGRVRGVCKPLHLGSRHQVWQIEIFDEKGRL 125
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 31-131 3.11e-10

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: 53.63  E-value: 3.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806340298  31 VRAELLIHDGLLQPHGIVHGGVYCSIVESVASVSAgvwLESAGGGRNVVGVNNNTDFLRAITAG-VVTATSTPIHRGRRQ 109
Cdd:cd03440     1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAA---ARLGGRGLGAVTLSLDVRFLRPVRPGdTLTVEAEVVRVGRSS 77

                          90       100
                  ....*....|....*....|..
gi 1806340298 110 QLWMVEIAGADGRLVARGQVRL 131
Cdd:cd03440    78 VTVEVEVRNEDGKLVATATATF 99
4HBT_3 pfam13622
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 86-141 1.83e-03

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


Pssm-ID: 463937 [Multi-domain]  Cd Length: 246  Bit Score: 36.93  E-value: 1.83e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1806340298  86 DFLRAITAGVVTATSTPIHRGRRQQLWMVEIAgADGRLVARGQVRLQNLPADAPEA 141
Cdd:pfam13622  39 DFLRPVPPGPVTIRVEVVRDGRSFSTRRVELS-QDGRVVVTATATFGRLRSSEWEL 93
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 46-131 4.10e-03

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: 34.89  E-value: 4.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806340298  46 GIVHGGVYCSIVESVASVsagvWLESAGG--------GRNVVGVNNNTDFLRAITAG-VVTATSTPIHRGRRQQLWMVEI 116
Cdd:cd00586    16 GHVNNARYLRYFEEAREE----FLRELGLgydeleeqGLGLVVVELEIDYLRPLRLGdRLTVETRVLRLGRKSFTFEQEI 91

                          90
                  ....*....|....*
gi 1806340298 117 AGADGRLVARGQVRL 131
Cdd:cd00586    92 FREDGELLATAETVL 106
 
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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