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Conserved domains on  [gi|1275712407|ref|WP_099786174|]
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MULTISPECIES: hydroxyphenylacetyl-CoA thioesterase PaaI [Serratia]

Protein Classification

hydroxyphenylacetyl-CoA thioesterase PaaI( domain architecture ID 10798001)

hydroxyphenylacetyl-CoA thioesterase PaaI is an esterase with a preference for ring-hydroxylated phenylacetyl-CoA esters

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PaaD TIGR02286
phenylacetic acid degradation protein PaaD; This member of the domain family TIGR00369 (which ...
 24-137 1.38e-51

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: 159.51  E-value: 1.38e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275712407  24 AQAMGMHIDDVDVGYAQVSMTVGPQMLNGHQTCHGGQLFSLADTAFAYACNSQGLAAVASGCSIDFVRPALAGDRLTASA 103
Cdd:TIGR02286   1 AKALGIDILELGPGFARVAMTVRADMLNGHGTAHGGFLFSLADSAFAYACNSYGDAAVAAQCTIDFLRPGRAGERLEAEA 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1275712407 104 QMRHQGKATGLYDVEIVNQQGKTVAWFRGRAHRL 137
Cdd:TIGR02286  81 VEVSRGGRTGTYDVEVVNQEGELVALFRGTSRRL 114
 
Name Accession Description Interval E-value
PaaD TIGR02286
phenylacetic acid degradation protein PaaD; This member of the domain family TIGR00369 (which ...
 24-137 1.38e-51

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: 159.51  E-value: 1.38e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275712407  24 AQAMGMHIDDVDVGYAQVSMTVGPQMLNGHQTCHGGQLFSLADTAFAYACNSQGLAAVASGCSIDFVRPALAGDRLTASA 103
Cdd:TIGR02286   1 AKALGIDILELGPGFARVAMTVRADMLNGHGTAHGGFLFSLADSAFAYACNSYGDAAVAAQCTIDFLRPGRAGERLEAEA 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1275712407 104 QMRHQGKATGLYDVEIVNQQGKTVAWFRGRAHRL 137
Cdd:TIGR02286  81 VEVSRGGRTGTYDVEVVNQEGELVALFRGTSRRL 114
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 15-139 2.05e-35

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 119.28  E-value: 2.05e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275712407  15 EQMFQQDTCAQAMGMHIDDVDVGYAQVSMTVGPQMLNGHQTCHGGQLFSLADTAFAYACNSQ---GLAAVASGCSIDFVR 91
Cdd:COG2050     9 EGFLAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSAlppGRRAVTIELNINFLR 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1275712407  92 PALAGDRLTASAQMRHQGKATGLYDVEIVNQQGKTVAWFRGRAHRLGH 139
Cdd:COG2050    89 PARLGDRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPK 136
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 26-132 2.28e-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: 98.01  E-value: 2.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275712407  26 AMGMHIDDVDVGYAQVSMTVGPQMLNGHQTCHGGQLFSLADTAFAYACNSQ---GLAAVASGCSIDFVRPAlAGDRLTAS 102
Cdd:cd03443     1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSAlppGALAVTVDLNVNYLRPA-RGGDLTAR 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 1275712407 103 AQMRHQGKATGLYDVEIVNQQGKTVAWFRG 132
Cdd:cd03443    80 ARVVKLGRRLAVVEVEVTDEDGKLVATARG 109
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 53-128 1.21e-17

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: 72.29  E-value: 1.21e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1275712407  53 HQTCHGGQLFSLADTAFAYACNSQGL---AAVASGCSIDFVRPALAGDRLTASAQMRHQGKATGLYDVEIVNQQGKTVA 128
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGsqqVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
 
Name Accession Description Interval E-value
PaaD TIGR02286
phenylacetic acid degradation protein PaaD; This member of the domain family TIGR00369 (which ...
 24-137 1.38e-51

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: 159.51  E-value: 1.38e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275712407  24 AQAMGMHIDDVDVGYAQVSMTVGPQMLNGHQTCHGGQLFSLADTAFAYACNSQGLAAVASGCSIDFVRPALAGDRLTASA 103
Cdd:TIGR02286   1 AKALGIDILELGPGFARVAMTVRADMLNGHGTAHGGFLFSLADSAFAYACNSYGDAAVAAQCTIDFLRPGRAGERLEAEA 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1275712407 104 QMRHQGKATGLYDVEIVNQQGKTVAWFRGRAHRL 137
Cdd:TIGR02286  81 VEVSRGGRTGTYDVEVVNQEGELVALFRGTSRRL 114
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 15-139 2.05e-35

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 119.28  E-value: 2.05e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275712407  15 EQMFQQDTCAQAMGMHIDDVDVGYAQVSMTVGPQMLNGHQTCHGGQLFSLADTAFAYACNSQ---GLAAVASGCSIDFVR 91
Cdd:COG2050     9 EGFLAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSAlppGRRAVTIELNINFLR 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1275712407  92 PALAGDRLTASAQMRHQGKATGLYDVEIVNQQGKTVAWFRGRAHRLGH 139
Cdd:COG2050    89 PARLGDRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPK 136
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 22-136 6.46e-34

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: 114.75  E-value: 6.46e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275712407  22 TCAQAMGMHIDDVDVGYAQVSMTVGPQMLNGHQTCHGGQLFSLADTAFA---YACNSQGLAAVASGCSIDFVRPALAGdR 98
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSaagYLCNSGGQAVVGLELNANHLRPAREG-K 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1275712407  99 LTASAQMRHQGKATGLYDVEIVNQQGKTVAWFRGRAHR 136
Cdd:TIGR00369  80 VRAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 26-132 2.28e-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: 98.01  E-value: 2.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275712407  26 AMGMHIDDVDVGYAQVSMTVGPQMLNGHQTCHGGQLFSLADTAFAYACNSQ---GLAAVASGCSIDFVRPAlAGDRLTAS 102
Cdd:cd03443     1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSAlppGALAVTVDLNVNYLRPA-RGGDLTAR 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 1275712407 103 AQMRHQGKATGLYDVEIVNQQGKTVAWFRG 132
Cdd:cd03443    80 ARVVKLGRRLAVVEVEVTDEDGKLVATARG 109
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 53-128 1.21e-17

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: 72.29  E-value: 1.21e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1275712407  53 HQTCHGGQLFSLADTAFAYACNSQGL---AAVASGCSIDFVRPALAGDRLTASAQMRHQGKATGLYDVEIVNQQGKTVA 128
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGsqqVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 41-128 3.12e-15

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: 66.73  E-value: 3.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275712407  41 VSMTVGPQMLNGHQTCHGGQLFSLADTAFAYACNS---QGLAAVASGCSIDFVRPALAGDRLTASAQMRHQGKATGLYDV 117
Cdd:cd03440     3 LRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARlggRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEV 82

                          90
                  ....*....|.
gi 1275712407 118 EIVNQQGKTVA 128
Cdd:cd03440    83 EVRNEDGKLVA 93
DUF4442 pfam14539
Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea ...
 27-128 2.45e-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: 2.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275712407  27 MGMHIDDVDVGYAQVSMTVGPQMLNGHQTCHGGQLFSLADTAFayacnsqGLAAVAS----------GCSIDFVRPAlAG 96
Cdd:pfam14539  18 IGPRITELRPGRCEVRLPKRRRVRNHIGTVHAIAICNLAELAM-------GLMAEASlpdthrwipkGMTVDYLAKA-TG 89

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1275712407  97 DrLTASAQM-RHQGKATGLY--DVEIVNQQGKTVA 128
Cdd:pfam14539  90 D-LTAVAELdPEDWGEKGDLpvPVEVRDDAGTEVV 123
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
57-137 7.66e-05

Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 40.25  E-value: 7.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275712407  57 HGGQLFSLADTAFAYACNSQGLAAVASgCSIDFVRPALAGDRLTASA------QMRHQGKATglYDVEIVNQQGKTVAwf 130
Cdd:COG2030    54 HGMLTLSLASGLLVDDLPGTAVANLGL-QEVRFLRPVRVGDTLRARVevlekrESKSRGIVT--LRTTVTNQDGEVVL-- 128


                  ....*..
gi 1275712407 131 RGRAHRL 137
Cdd:COG2030   129 TGEATVL 135
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 75-128 2.00e-04

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: 38.36  E-value: 2.00e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1275712407  75 SQGLAAVASGCSIDFVRPALAGDRLTASAQMRHQGKATGLYDVEIVNQQGKTVA 128
Cdd:cd00586    47 EQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRLGRKSFTFEQEIFREDGELLA 100
MaoC_C cd03452
MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory ...
 35-128 2.90e-04

MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory protein. Orthologs of MaoC include PaaZ [Escherichia coli] and PaaN [Pseudomonas putida], which are putative ring-opening enzymes involved in phenylacetic acid degradation. The C-terminal domain of MaoC has sequence similarity to (R)-specific enoyl-CoA hydratase,Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. MaoC also has an N-terminal PutA domain like that found in the E. coli PutA proline dehydrogenase and other members of the aldehyde dehydrogenase family.


Pssm-ID: 239536 [Multi-domain]  Cd Length: 142  Bit Score: 38.53  E-value: 2.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275712407  35 DVGYAQVSMTVGPQMLNGHQTCHGGQLFSLADTAFAYACNSQGLAAVASGcSIDFVRPALAGD----RLTASAQMRHQGK 110
Cdd:cd03452    32 DHFYAHMDEIAAKASFFGKRVAHGYFVLSAAAGLFVDPAPGPVLANYGLE-NLRFLEPVYPGDtiqvRLTCKRKIPRDGQ 110

                          90       100
                  ....*....|....*....|
gi 1275712407 111 ATGL--YDVEIVNQQGKTVA 128
Cdd:cd03452   111 DYGVvrWDAEVTNQNGELVA 130
PS-DH pfam14765
Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. ...
 86-132 2.58e-03

Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. Structural analysis shows these DH domains are double hotdogs in which the active site contains a histidine from the N-terminal hotdog and an aspartate from the C-terminal hotdog. Studies have uncovered that a substrate tunnel formed between the DH domains may be essential for loading substrates and unloading products.


Pssm-ID: 434191  Cd Length: 296  Bit Score: 36.58  E-value: 2.58e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1275712407  86 SIDFVRPALAGDRLTASAQMRHQGKATGLYDVEIVNQQGKTVAWFRG 132
Cdd:pfam14765 237 RLRIYRSLPPGEPLWVHARLERRGGRTIVGDLTLVDEDGRVVARIEG 283
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 76-133 3.81e-03

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: 35.26  E-value: 3.81e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1275712407  76 QGLAAVASGCSIDFVRPALAGDRLTASAQMRHQGKATGLYDVEIVNQQGKTVAwFRGR 133
Cdd:COG0824    53 EGIGLVVVEAEIDYLRPARYGDELTVETRVVRLGGSSLTFEYEIFRADDGELL-ATGE 109
 
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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