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Conserved domains on  [gi|914331653|ref|WP_050573004|]
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MULTISPECIES: PaaI family thioesterase [Pseudomonas]

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 ...
1-127 1.19e-37

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


:

Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 124.28  E-value: 1.19e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914331653   1 MSEMPAR-EQMISA--YSELVGLDPVSLGDGGAEVRLPMAAHLRNRGGVMHGGALFSLMDVTMGLACSSSHGFDRQSVTL 77
Cdd:COG2050    1 MSDPLERlEGFLAAnpFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTI 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 914331653  78 ECKINYIRAVADGE-VRCVARVLHAGRRSLVVEAEVRQGD-KLVAKGQGTFA 127
Cdd:COG2050   81 ELNINFLRPARLGDrLTAEARVVRRGRRLAVVEVEVTDEDgKLVATATGTFA 132
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
1-127 1.19e-37

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 124.28  E-value: 1.19e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914331653   1 MSEMPAR-EQMISA--YSELVGLDPVSLGDGGAEVRLPMAAHLRNRGGVMHGGALFSLMDVTMGLACSSSHGFDRQSVTL 77
Cdd:COG2050    1 MSDPLERlEGFLAAnpFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTI 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 914331653  78 ECKINYIRAVADGE-VRCVARVLHAGRRSLVVEAEVRQGD-KLVAKGQGTFA 127
Cdd:COG2050   81 ELNINFLRPARLGDrLTAEARVVRRGRRLAVVEVEVTDEDgKLVATATGTFA 132
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
17-127 9.17e-37

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: 121.13  E-value: 9.17e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914331653  17 LVGLDPVSLGDGGAEVRLPMAAHLRNRGGVMHGGALFSLMDVTMGLACSSSHGFDRQSVTLECKINYIRAVADGEVRCVA 96
Cdd:cd03443    1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPARGGDLTARA 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 914331653  97 RVLHAGRRSLVVEAEVRQGD-KLVAKGQGTFA 127
Cdd:cd03443   81 RVVKLGRRLAVVEVEVTDEDgKLVATARGTFA 112
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
44-121 2.72e-19

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: 75.75  E-value: 2.72e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 914331653   44 GGVMHGGALFSLMDVTMGLACSSSHGFDRQSVTLECKINYIRAVADGE-VRCVARVLHAGRRSLVVEAEVRQGDKLVAK 121
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELSIDFLRPARLGDrLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
16-127 4.44e-19

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: 76.23  E-value: 4.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914331653   16 ELVGLDPVSLGDGGAEVRLPMAAHLRNRGGVMHGGALFSLMDVTMGLACSSSHGFDRQSVTLECKINYIRAVADGEVRCV 95
Cdd:TIGR00369   4 SFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNSGGQAVVGLELNANHLRPAREGKVRAI 83
                          90       100       110
                  ....*....|....*....|....*....|...
gi 914331653   96 ARVLHAGRRSLVVEAEVR-QGDKLVAKGQGTFA 127
Cdd:TIGR00369  84 AQVVHLGRQTGVAEIEIVdEQGRLCALSRGTTA 116
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
25-112 2.15e-05

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


Pssm-ID: 182360  Cd Length: 136  Bit Score: 41.15  E-value: 2.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914331653  25 LGDGGAEVRLPMAAHLRNRGGVMHGGALFSLMDVTMGLACSSSHGFDRQSVTLECKINYIRAVADGEVRCVARVLHAGRR 104
Cdd:PRK10293  31 IGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAGYLCTEGEQKVVGLEINANHVRSAREGRVRGVCKPLHLGSR 110

                 ....*...
gi 914331653 105 SLVVEAEV 112
Cdd:PRK10293 111 HQVWQIEI 118
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
1-127 1.19e-37

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 124.28  E-value: 1.19e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914331653   1 MSEMPAR-EQMISA--YSELVGLDPVSLGDGGAEVRLPMAAHLRNRGGVMHGGALFSLMDVTMGLACSSSHGFDRQSVTL 77
Cdd:COG2050    1 MSDPLERlEGFLAAnpFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTI 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 914331653  78 ECKINYIRAVADGE-VRCVARVLHAGRRSLVVEAEVRQGD-KLVAKGQGTFA 127
Cdd:COG2050   81 ELNINFLRPARLGDrLTAEARVVRRGRRLAVVEVEVTDEDgKLVATATGTFA 132
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
17-127 9.17e-37

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: 121.13  E-value: 9.17e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914331653  17 LVGLDPVSLGDGGAEVRLPMAAHLRNRGGVMHGGALFSLMDVTMGLACSSSHGFDRQSVTLECKINYIRAVADGEVRCVA 96
Cdd:cd03443    1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPARGGDLTARA 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 914331653  97 RVLHAGRRSLVVEAEVRQGD-KLVAKGQGTFA 127
Cdd:cd03443   81 RVVKLGRRLAVVEVEVTDEDgKLVATARGTFA 112
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
44-121 2.72e-19

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: 75.75  E-value: 2.72e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 914331653   44 GGVMHGGALFSLMDVTMGLACSSSHGFDRQSVTLECKINYIRAVADGE-VRCVARVLHAGRRSLVVEAEVRQGDKLVAK 121
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELSIDFLRPARLGDrLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
16-127 4.44e-19

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: 76.23  E-value: 4.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914331653   16 ELVGLDPVSLGDGGAEVRLPMAAHLRNRGGVMHGGALFSLMDVTMGLACSSSHGFDRQSVTLECKINYIRAVADGEVRCV 95
Cdd:TIGR00369   4 SFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNSGGQAVVGLELNANHLRPAREGKVRAI 83
                          90       100       110
                  ....*....|....*....|....*....|...
gi 914331653   96 ARVLHAGRRSLVVEAEVR-QGDKLVAKGQGTFA 127
Cdd:TIGR00369  84 AQVVHLGRQTGVAEIEIVdEQGRLCALSRGTTA 116
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
30-127 1.77e-16

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: 69.43  E-value: 1.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914331653  30 AEVRLPMAAHLRNRGGVMHGGALFSLMDVTMGLACSSSHGFDRQSVTLECKINYIRAVADGE-VRCVARVLHAGRRSLVV 108
Cdd:cd03440    1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLDVRFLRPVRPGDtLTVEAEVVRVGRSSVTV 80
                         90       100
                 ....*....|....*....|
gi 914331653 109 EAEVR-QGDKLVAKGQGTFA 127
Cdd:cd03440   81 EVEVRnEDGKLVATATATFV 100
4HBT_3 pfam13622
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
44-127 1.33e-07

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: 48.48  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914331653   44 GGVMHGGALFSLMdvtMGLACSSSHGFDRQSVTleckINYIRAVADGEVRCVARVLHAGRRSLVVEAEVRQGDKLVAKGQ 123
Cdd:pfam13622   8 GRAPHGGYVAALL---LRAAERTVPPDPLHSLH----VDFLRPVPPGPVTIRVEVVRDGRSFSTRRVELSQDGRVVVTAT 80

                  ....
gi 914331653  124 GTFA 127
Cdd:pfam13622  81 ATFG 84
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
33-113 2.83e-07

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 46.33  E-value: 2.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914331653  33 RLPMAAHLrNRGGVMHGGALFSLMDVTMGLACSsshgfdRQS----VTLEC-KINYIRAVADGE-VRCVARVLHAGRRSL 106
Cdd:COG1607   11 ELVMPEDT-NHHGTLFGGWLLSWMDEAAAIAAA------RHArgrvVTASVdSVDFLRPVRVGDiVELYARVVRVGRTSM 83

                 ....*..
gi 914331653 107 VVEAEVR 113
Cdd:COG1607   84 EVGVEVW 90
DUF4442 pfam14539
Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea ...
28-125 1.44e-05

Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea and eukaryotes. Proteins in this family are typically between 139 and 165 amino acids in length. There is a conserved PYF sequence motif. There is a single completely conserved residue N that may be functionally important.


Pssm-ID: 434027  Cd Length: 131  Bit Score: 41.47  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914331653   28 GGAEVRLPMAAHLRNRGGVMHGGALFSLMDVTMGLACSSSHGFDRQSVTLECKINYIrAVADGEVRCVARVLHAGRRS-- 105
Cdd:pfam14539  28 GRCEVRLPKRRRVRNHIGTVHAIAICNLAELAMGLMAEASLPDTHRWIPKGMTVDYL-AKATGDLTAVAELDPEDWGEkg 106
                          90       100
                  ....*....|....*....|..
gi 914331653  106 -LVVEAEVRQGD-KLVAKGQGT 125
Cdd:pfam14539 107 dLPVPVEVRDDAgTEVVRATIT 128
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
25-112 2.15e-05

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


Pssm-ID: 182360  Cd Length: 136  Bit Score: 41.15  E-value: 2.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914331653  25 LGDGGAEVRLPMAAHLRNRGGVMHGGALFSLMDVTMGLACSSSHGFDRQSVTLECKINYIRAVADGEVRCVARVLHAGRR 104
Cdd:PRK10293  31 IGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAGYLCTEGEQKVVGLEINANHVRSAREGRVRGVCKPLHLGSR 110

                 ....*...
gi 914331653 105 SLVVEAEV 112
Cdd:PRK10293 111 HQVWQIEI 118
PRK10254 PRK10254
proofreading thioesterase EntH;
25-105 2.64e-05

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 41.12  E-value: 2.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914331653  25 LGDGGAEVRLPMAAHLRNRGGVMHGGALFSLMDvTMGLACSSSHGFDRQSVT-LECKINYIRAVADGEVRCVARVLHAGR 103
Cdd:PRK10254  31 LGDDVLEAEMPVDTRTHQPFGLLHGGASAALAE-TLGSMAGFLMTRDGQCVVgTELNATHHRPVSEGKVRGVCQPLHLGR 109

                 ..
gi 914331653 104 RS 105
Cdd:PRK10254 110 QN 111
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
32-116 4.85e-04

Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes deacylate long-chain fatty acids by hydrolyzing acyl-CoA thioesters to free fatty acids and CoA-SH. Eukaryotic members of this family are expressed in brain, testis, and brown adipose tissues. The archeal and eukaryotic members of this family have two tandem copies of the conserved hot dog fold, while most bacterial members have only one copy.


Pssm-ID: 239526 [Multi-domain]  Cd Length: 123  Bit Score: 37.16  E-value: 4.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914331653  32 VRLPMAAHlRNRGGVMHGGALFSLMDvTMGLACSSSHGfdRQSVTLEC--KINYIRAVADGE-VRCVARVLHAGRRSLVV 108
Cdd:cd03442   11 RELVLPED-TNHHGTIFGGWLLEWMD-ELAGIAAYRHA--GGRVVTASvdRIDFLKPVRVGDvVELSARVVYTGRTSMEV 86

                 ....*...
gi 914331653 109 EAEVRQGD 116
Cdd:cd03442   87 GVEVEAED 94
PRK11688 PRK11688
thioesterase family protein;
16-126 8.33e-03

thioesterase family protein;


Pssm-ID: 183276  Cd Length: 154  Bit Score: 34.05  E-value: 8.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914331653  16 ELVGLDPVSLGDGGAEVRLPM-------AAHlrnrgGVMHGGALFSLMDVTMGLACSSSHGFDRQSVTLE---------- 78
Cdd:PRK11688  25 RLLGLELERLEPDFVELSFKMqpelvgnIAQ-----SILHGGVIASVLDVAGGLVCVGGILARHEDISEEelrqrlsrlg 99
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 914331653  79 ---CKINYIRAVADGEVRCVARVLHAGRRSLVVEAEVRQGD-KLVAKGQGTF 126
Cdd:PRK11688 100 tidLRVDYLRPGRGERFTATSSVLRAGNKVAVARMELHNEQgVHIASGTATY 151
 
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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