NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|744807240|gb|AJC85186|]
View 

acyl-CoA hydrolase [Campylobacter peloridis LMG 23910]

Protein Classification

acyl-CoA thioesterase( domain architecture ID 10787832)

acyl-CoA thioesterase catalyzes the hydrolysis of acyl-CoA esters to the free fatty acid and CoA; belongs to the Hotdog fold superfamily

CATH:  3.10.129.10
EC:  3.1.2.-
Gene Ontology:  GO:0016790|GO:0016787
PubMed:  15307895

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
5-124 6.93e-53

Acyl-CoA hydrolase [Lipid transport and metabolism];


:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 163.43  E-value: 6.93e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744807240   5 GEPKLRVIAMPSNTNPAGNIFGGWIMSQIDLAGAIAARELSPQRVVTVAVDKIIFKEPIFVGDLVSCYAKIIKAGNTSIT 84
Cdd:COG1607    5 SELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSME 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 744807240  85 VEVEVVTQRANEYGRVycmHVTSAIVTYVSVDKDGNKFPI 124
Cdd:COG1607   85 VGVEVWAEDLRTGERR---LVTEAYFTFVAVDEDGKPRPV 121
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
5-124 6.93e-53

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 163.43  E-value: 6.93e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744807240   5 GEPKLRVIAMPSNTNPAGNIFGGWIMSQIDLAGAIAARELSPQRVVTVAVDKIIFKEPIFVGDLVSCYAKIIKAGNTSIT 84
Cdd:COG1607    5 SELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSME 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 744807240  85 VEVEVVTQRANEYGRVycmHVTSAIVTYVSVDKDGNKFPI 124
Cdd:COG1607   85 VGVEVWAEDLRTGERR---LVTEAYFTFVAVDEDGKPRPV 121
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 5-124 8.58e-42

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: 134.62  E-value: 8.58e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744807240   5 GEPKLRVIAMPSNTNPAGNIFGGWIMSQIDLAGAIAARELSPQRVVTVAVDKIIFKEPIFVGDLVSCYAKIIKAGNTSIT 84
Cdd:cd03442    6 TELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGRTSME 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 744807240  85 VEVEVVTQRANEYGRVycmHVTSAIVTYVSVDKDGNKFPI 124
Cdd:cd03442   86 VGVEVEAEDPLTGERR---LVTSAYFTFVALDEDGKPRPV 122
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
5-124 1.12e-37

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 124.59  E-value: 1.12e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744807240   5 GEPKLRVIAMPSNTNPAGNIFGGWIMSQIDLAGAIAARELSPQRVVTVAVDKIIFKEPIFVGDLVSCYAKIIKAGNTSIT 84
Cdd:PRK10694  10 GELVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSIS 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 744807240  85 VEVEV-VTQRANE-YGRVYcmHVTSAIVTYVSVDKDGNKFPI 124
Cdd:PRK10694  90 INIEVwVKKVASEpIGQRY--KATEALFTYVAVDPEGKPRAL 129
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 22-92 7.21e-18

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: 7.21e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 744807240   22 GNIFGGWIMSQIDLAGAIAAREL-SPQRVVTVAVDKIIFKEPIFVGDLVSCYAKIIKAGNTSITVEVEVVTQ 92
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLgGSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDE 73
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 3-102 5.30e-05

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: 40.02  E-value: 5.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744807240    3 DMGEPKLRVIaMP---SNTNPAGNIFGGWIMSQIDLAGAIAARELSPQRVVTVAVD-KIIFKEPIFVGDLVScYAKIIKA 78
Cdd:TIGR00369  12 ELGDGFLEAT-MPvdeRTLQPFGSLHGGVSAALADTAGSAAGYLCNSGGQAVVGLElNANHLRPAREGKVRA-IAQVVHL 89

                          90       100
                  ....*....|....*....|....
gi 744807240   79 GNTSITVEVEVVtqraNEYGRVYC 102
Cdd:TIGR00369  90 GRQTGVAEIEIV----DEQGRLCA 109
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
5-124 6.93e-53

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 163.43  E-value: 6.93e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744807240   5 GEPKLRVIAMPSNTNPAGNIFGGWIMSQIDLAGAIAARELSPQRVVTVAVDKIIFKEPIFVGDLVSCYAKIIKAGNTSIT 84
Cdd:COG1607    5 SELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSME 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 744807240  85 VEVEVVTQRANEYGRVycmHVTSAIVTYVSVDKDGNKFPI 124
Cdd:COG1607   85 VGVEVWAEDLRTGERR---LVTEAYFTFVAVDEDGKPRPV 121
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 5-124 8.58e-42

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: 134.62  E-value: 8.58e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744807240   5 GEPKLRVIAMPSNTNPAGNIFGGWIMSQIDLAGAIAARELSPQRVVTVAVDKIIFKEPIFVGDLVSCYAKIIKAGNTSIT 84
Cdd:cd03442    6 TELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGRTSME 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 744807240  85 VEVEVVTQRANEYGRVycmHVTSAIVTYVSVDKDGNKFPI 124
Cdd:cd03442   86 VGVEVEAEDPLTGERR---LVTSAYFTFVALDEDGKPRPV 122
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
5-124 1.12e-37

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 124.59  E-value: 1.12e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744807240   5 GEPKLRVIAMPSNTNPAGNIFGGWIMSQIDLAGAIAARELSPQRVVTVAVDKIIFKEPIFVGDLVSCYAKIIKAGNTSIT 84
Cdd:PRK10694  10 GELVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSIS 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 744807240  85 VEVEV-VTQRANE-YGRVYcmHVTSAIVTYVSVDKDGNKFPI 124
Cdd:PRK10694  90 INIEVwVKKVASEpIGQRY--KATEALFTYVAVDPEGKPRAL 129
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 22-92 7.21e-18

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: 7.21e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 744807240   22 GNIFGGWIMSQIDLAGAIAAREL-SPQRVVTVAVDKIIFKEPIFVGDLVSCYAKIIKAGNTSITVEVEVVTQ 92
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLgGSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDE 73
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 5-110 5.62e-14

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 63.81  E-value: 5.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744807240   5 GEPKLRVIAMPSNTNPAGNIFGGWIMSQIDLAGAIAARELSPQRVVTVAVD-KIIFKEPIFVGDLVSCYAKIIKAGNTSI 83
Cdd:COG2050   31 GRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIElNINFLRPARLGDRLTAEARVVRRGRRLA 110

                         90       100
                 ....*....|....*....|....*...
gi 744807240  84 TVEVEVVtqraNEYGRVYC-MHVTSAIV 110
Cdd:COG2050  111 VVEVEVT----DEDGKLVAtATGTFAVL 134
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 9-113 7.79e-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: 62.49  E-value: 7.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744807240   9 LRVIAMPSNTNPAGNIFGGWIMSQIDLAGAIAARELSPQRVVTVAVD-KIIFKEPIFVGDLVSCYAKIIKAGNTSITVEV 87
Cdd:cd03440    3 LRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSlDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEV 82

                         90       100
                 ....*....|....*....|....*.
gi 744807240  88 EVVTQRaneyGRVycmhVTSAIVTYV 113
Cdd:cd03440   83 EVRNED----GKL----VATATATFV 100
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 5-89 3.74e-09

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: 50.63  E-value: 3.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744807240   5 GEPKLRVIAMPSNTNPAGNIFGGWIMSQIDLAGAIAARELSPQRVVTVAVD-KIIFKEPIFVGDLVsCYAKIIKAGNTSI 83
Cdd:cd03443   12 GRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDlNVNYLRPARGGDLT-ARARVVKLGRRLA 90


                 ....*.
gi 744807240  84 TVEVEV 89
Cdd:cd03443   91 VVEVEV 96
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
26-93 8.50e-06

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 42.57  E-value: 8.50e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 744807240  26 GGWIMSqidLAGAIAARELSPQRVVTVAVDKIIFKEPIFVGDLVSCYAKII----KAGNTSITVEVEVVTQR 93
Cdd:COG2030   55 GMLTLS---LASGLLVDDLPGTAVANLGLQEVRFLRPVRVGDTLRARVEVLekreSKSRGIVTLRTTVTNQD 123
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 3-102 5.30e-05

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: 40.02  E-value: 5.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744807240    3 DMGEPKLRVIaMP---SNTNPAGNIFGGWIMSQIDLAGAIAARELSPQRVVTVAVD-KIIFKEPIFVGDLVScYAKIIKA 78
Cdd:TIGR00369  12 ELGDGFLEAT-MPvdeRTLQPFGSLHGGVSAALADTAGSAAGYLCNSGGQAVVGLElNANHLRPAREGKVRA-IAQVVHL 89

                          90       100
                  ....*....|....*....|....
gi 744807240   79 GNTSITVEVEVVtqraNEYGRVYC 102
Cdd:TIGR00369  90 GRQTGVAEIEIV----DEQGRLCA 109
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 39-131 6.05e-05

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: 40.27  E-value: 6.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744807240  39 IAARELSPQRVVTVAVD-KIIFKEPIFVGDLVSCYAKIIKAGNTSITVEVEVVTQRANEygrvycmHVTSAIVTYVSVDK 117
Cdd:COG0824   45 LSYAELEEEGIGLVVVEaEIDYLRPARYGDELTVETRVVRLGGSSLTFEYEIFRADDGE-------LLATGETVLVFVDL 117

                         90
                 ....*....|....*
gi 744807240 118 DGNK-FPIDADLKRL 131
Cdd:COG0824  118 ETGRpVPLPDELRAA 132
PLN02647 PLN02647
acyl-CoA thioesterase
 19-96 6.39e-05

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 41.31  E-value: 6.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 744807240  19 NPAGNIFGGWIMSQID-LAGAIAARELS-------PQRVVTVAVDKIIFKEPIFVGDLVSCYAKIIKAGNTSITVEVEvV 90
Cdd:PLN02647 106 NPWNEVRIGKLLEDLDaLAGTISVKHCSdddsttrPLLLVTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIQLE-V 184


                 ....*.
gi 744807240  91 TQRANE 96
Cdd:PLN02647 185 IQPTKD 190
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 42-116 1.07e-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: 36.04  E-value: 1.07e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 744807240  42 RELSPQRVVTVAVD-KIIFKEPIFVGDLVSCYAKIIKAGNTSITVEVEVVtqraNEYGRVYCmhvtSAIVTYVSVD 116
Cdd:cd00586   43 DELEEQGLGLVVVElEIDYLRPLRLGDRLTVETRVLRLGRKSFTFEQEIF----REDGELLA----TAETVLVCVD 110
 
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