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Conserved domains on  [gi|440918682|ref|NP_001258998|]
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palmitoyl-protein thioesterase ABHD10, mitochondrial isoform 2 [Homo sapiens]

Protein Classification

alpha/beta fold hydrolase( domain architecture ID 11426811)

alpha/beta hydrolase family protein catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

PubMed:  1409539|12369917

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 65-188 1.20e-14

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


:

Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 69.64  E-value: 1.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918682  65 NLAYKKLKGKSPGIIFIPGYLSYMNGTKALaIEEFCKslGHACIRFDYSGVGSSDGNSEESTLGKWRKDVLSIIDDLADG 144
Cdd:COG0596   13 RLHYREAGPDGPPVVLLHGLPGSSYEWRPL-IPALAA--GYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALLDALGLE 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 440918682 145 PQILVGSSLGGWLMLHAAIARPEKVVALIGVATAADTLVTKFNQ 188
Cdd:COG0596   90 RVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPLRR 133
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 65-188 1.20e-14

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 69.64  E-value: 1.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918682  65 NLAYKKLKGKSPGIIFIPGYLSYMNGTKALaIEEFCKslGHACIRFDYSGVGSSDGNSEESTLGKWRKDVLSIIDDLADG 144
Cdd:COG0596   13 RLHYREAGPDGPPVVLLHGLPGSSYEWRPL-IPALAA--GYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALLDALGLE 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 440918682 145 PQILVGSSLGGWLMLHAAIARPEKVVALIGVATAADTLVTKFNQ 188
Cdd:COG0596   90 RVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPLRR 133
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 78-177 2.68e-07

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 49.43  E-value: 2.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918682   78 IIFIPGYL----SYMNGTKALAieefckSLGHACIRFDYSGVGSSDGNSEESTLGKW--RKDVLSIIDDLADGPQILVGS 151
Cdd:pfam00561   3 VLLLHGLPgssdLWRKLAPALA------RDGFRVIALDLRGFGKSSRPKAQDDYRTDdlAEDLEYILEALGLEKVNLVGH 76

                          90       100
                  ....*....|....*....|....*.
gi 440918682  152 SLGGWLMLHAAIARPEKVVALIGVAT 177
Cdd:pfam00561  77 SMGGLIALAYAAKYPDRVKALVLLGA 102
PLN02578 PLN02578
hydrolase
 72-178 2.72e-05

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 43.68  E-value: 2.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918682  72 KGKSPGIIFIPGYlsymnGTKAL----AIEEFCKSlgHACIRFDYSGVGSSDGNSEESTLGKWRKDVLSIIDDLADGPQI 147
Cdd:PLN02578  83 QGEGLPIVLIHGF-----GASAFhwryNIPELAKK--YKVYALDLLGFGWSDKALIEYDAMVWRDQVADFVKEVVKEPAV 155

                         90       100       110
                 ....*....|....*....|....*....|.
gi 440918682 148 LVGSSLGGWLMLHAAIARPEKVVALIGVATA 178
Cdd:PLN02578 156 LVGNSLGGFTALSTAVGYPELVAGVALLNSA 186
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 144-175 3.70e-05

Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.


Pssm-ID: 214007  Cd Length: 309  Bit Score: 43.39  E-value: 3.70e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 440918682 144 GPQILVGSSLGGWLMLHAAIARPEKVVALIGV 175
Cdd:cd12808  188 GPCIVVAHSQGGGFAFEAARARPDLVRAVVAL 219
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 65-188 1.20e-14

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 69.64  E-value: 1.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918682  65 NLAYKKLKGKSPGIIFIPGYLSYMNGTKALaIEEFCKslGHACIRFDYSGVGSSDGNSEESTLGKWRKDVLSIIDDLADG 144
Cdd:COG0596   13 RLHYREAGPDGPPVVLLHGLPGSSYEWRPL-IPALAA--GYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALLDALGLE 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 440918682 145 PQILVGSSLGGWLMLHAAIARPEKVVALIGVATAADTLVTKFNQ 188
Cdd:COG0596   90 RVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPLRR 133
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
78-178 8.88e-11

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 58.86  E-value: 8.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918682  78 IIFIPGYLSYMNGTKALAiEEFCKSlGHACIRFDYSGVGSSDG-NSEESTLGKWRKDVLSIIDDLA---DGPQILVGSSL 153
Cdd:COG2267   31 VVLVHGLGEHSGRYAELA-EALAAA-GYAVLAFDLRGHGRSDGpRGHVDSFDDYVDDLRAALDALRarpGLPVVLLGHSM 108

                         90       100
                 ....*....|....*....|....*
gi 440918682 154 GGWLMLHAAIARPEKVVALIGVATA 178
Cdd:COG2267  109 GGLIALLYAARYPDRVAGLVLLAPA 133
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
72-180 9.33e-10

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 56.18  E-value: 9.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918682  72 KGKSPGIIFIPG-----YLSYMNGTKALAieefckSLGHACIRFDYSGVGSSDGNSEESTLgkwrKDVLSIIDDLADGPQ 146
Cdd:COG1506   20 GKKYPVVVYVHGgpgsrDDSFLPLAQALA------SRGYAVLAPDYRGYGESAGDWGGDEV----DDVLAAIDYLAARPY 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 440918682 147 I------LVGSSLGGWLMLHAAIARPEKVVALIGVATAAD 180
Cdd:COG1506   90 VdpdrigIYGHSYGGYMALLAAARHPDRFKAAVALAGVSD 129
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
71-178 9.66e-09

Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 53.41  E-value: 9.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918682  71 LKGKSPGIIFIPGYLSYMNGTKALAieEFCKSLGHACIRFDYSGVGSSDGNSEESTLGKWRKDVLSIIDDLADG--PQIL 148
Cdd:COG1647   11 LEGGRKGVLLLHGFTGSPAEMRPLA--EALAKAGYTVYAPRLPGHGTSPEDLLKTTWEDWLEDVEEAYEILKAGydKVIV 88

                         90       100       110
                 ....*....|....*....|....*....|
gi 440918682 149 VGSSLGGWLMLHAAIARPEkVVALIGVATA 178
Cdd:COG1647   89 IGLSMGGLLALLLAARYPD-VAGLVLLSPA 117
COG2945 COG2945
Alpha/beta superfamily hydrolase [General function prediction only];
100-179 9.28e-08

Alpha/beta superfamily hydrolase [General function prediction only];


Pssm-ID: 442188 [Multi-domain]  Cd Length: 201  Bit Score: 50.16  E-value: 9.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918682 100 CKSLGHACIRFDYSGVGSSDGNSEESTlGKwRKDVLSIIDDLAD---GPQILVGSSLGGWLMLHAAIARPEkVVALIGVA 176
Cdd:COG2945   51 LVAAGFAVLRFNFRGVGRSEGEFDEGR-GE-LDDAAAALDWLRAqnpLPLWLAGFSFGAYVALQLAMRLPE-VEGLILVA 127


                 ...
gi 440918682 177 TAA 179
Cdd:COG2945  128 PPV 130
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 78-177 2.68e-07

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 49.43  E-value: 2.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918682   78 IIFIPGYL----SYMNGTKALAieefckSLGHACIRFDYSGVGSSDGNSEESTLGKW--RKDVLSIIDDLADGPQILVGS 151
Cdd:pfam00561   3 VLLLHGLPgssdLWRKLAPALA------RDGFRVIALDLRGFGKSSRPKAQDDYRTDdlAEDLEYILEALGLEKVNLVGH 76

                          90       100
                  ....*....|....*....|....*.
gi 440918682  152 SLGGWLMLHAAIARPEKVVALIGVAT 177
Cdd:pfam00561  77 SMGGLIALAYAAKYPDRVKALVLLGA 102
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 78-190 2.06e-05

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 43.62  E-value: 2.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918682   78 IIFIPGYLSYMNGTKALAIEefckslGHACIRFDYSGVGSSDGNSEESTLgkwRKDVLSIIDDLADGPQ-ILVGSSLGGW 156
Cdd:pfam12697   1 VVLVHGAGLSAAPLAALLAA------GVAVLAPDLPGHGSSSPPPLDLAD---LADLAALLDELGAARPvVLVGHSLGGA 71

                          90       100       110
                  ....*....|....*....|....*....|....
gi 440918682  157 LMLHAAIARPEKVVALIGVATAADTLVTKFNQLP 190
Cdd:pfam12697  72 VALAAAAAALVVGVLVAPLAAPPGLLAALLALLA 105
PLN02578 PLN02578
hydrolase
 72-178 2.72e-05

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 43.68  E-value: 2.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918682  72 KGKSPGIIFIPGYlsymnGTKAL----AIEEFCKSlgHACIRFDYSGVGSSDGNSEESTLGKWRKDVLSIIDDLADGPQI 147
Cdd:PLN02578  83 QGEGLPIVLIHGF-----GASAFhwryNIPELAKK--YKVYALDLLGFGWSDKALIEYDAMVWRDQVADFVKEVVKEPAV 155

                         90       100       110
                 ....*....|....*....|....*....|.
gi 440918682 148 LVGSSLGGWLMLHAAIARPEKVVALIGVATA 178
Cdd:PLN02578 156 LVGNSLGGFTALSTAVGYPELVAGVALLNSA 186
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 144-175 3.70e-05

Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.


Pssm-ID: 214007  Cd Length: 309  Bit Score: 43.39  E-value: 3.70e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 440918682 144 GPQILVGSSLGGWLMLHAAIARPEKVVALIGV 175
Cdd:cd12808  188 GPCIVVAHSQGGGFAFEAARARPDLVRAVVAL 219
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 69-180 4.13e-05

Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 42.98  E-value: 4.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918682  69 KKLKGKSPGIIFIPGYlsymNGTK---ALAIEEFCKsLGHACIRFDYSGVGSSDGN-SEESTLgkWRKDVLSIIDDLA-- 142
Cdd:COG1073   31 AGASKKYPAVVVAHGN----GGVKeqrALYAQRLAE-LGFNVLAFDYRGYGESEGEpREEGSP--ERRDARAAVDYLRtl 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 440918682 143 ---DGPQILV-GSSLGGWLMLHAAIARPEkVVALIGVATAAD 180
Cdd:COG1073  104 pgvDPERIGLlGISLGGGYALNAAATDPR-VKAVILDSPFTS 144
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 78-178 4.78e-04

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 39.89  E-value: 4.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918682   78 IIFIPGYLSYMNgtkalAIEEFCKSL---GHACIRFDYSGVGSSDGN-SEESTLGKWRKDVLSIIDDLADG----PQILV 149
Cdd:pfam12146   7 VVLVHGLGEHSG-----RYAHLADALaaqGFAVYAYDHRGHGRSDGKrGHVPSFDDYVDDLDTFVDKIREEhpglPLFLL 81

                          90       100
                  ....*....|....*....|....*....
gi 440918682  150 GSSLGGWLMLHAAIARPEKVVALIGVATA 178
Cdd:pfam12146  82 GHSMGGLIAALYALRYPDKVDGLILSAPA 110
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 104-178 6.96e-04

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 39.54  E-value: 6.96e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 440918682 104 GHACIRFDYSGVGSSDGNSEESTLGKWRKDVLSIIDDLADGPQILVGSSLGGWLMLHAAIARPEKVVALIGVATA 178
Cdd:PRK14875 157 GRPVIALDLPGHGASSKAVGAGSLDELAAAVLAFLDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAPA 231
YdeN COG3545
Predicted esterase of the alpha/beta hydrolase fold [General function prediction only];
127-195 1.69e-03

Predicted esterase of the alpha/beta hydrolase fold [General function prediction only];


Pssm-ID: 442766 [Multi-domain]  Cd Length: 170  Bit Score: 37.52  E-value: 1.69e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 440918682 127 LGKWRKDVLSIIDDlADGPQILVGSSLGGWLMLHAAIARPEKVVALIGVATAAdtlVTKFNQLPVEDSG 195
Cdd:COG3545   38 LDDWLAALDAAVAA-ADGPVVLVAHSLGCLAVAHWAARLPRKVAGALLVAPPD---PERPGFLPELDAG 102
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 135-175 3.37e-03

Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.


Pssm-ID: 214008  Cd Length: 280  Bit Score: 37.59  E-value: 3.37e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 440918682 135 LSIIddladGPQILVGSSLGGWLMLHAAIARPEKVVALIGV 175
Cdd:cd12809  167 LDII-----GPAILITHSQGGPFGWLAADARPDLVKAIVAI 202
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 78-177 9.51e-03

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 34.42  E-value: 9.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918682  78 IIFIPGYlsYMNGTKALAIEEFCKSLGHACIRFDYsgvGSSDGNSEESTlgkwrKDVLSIIDDLAD---GPQI-LVGSSL 153
Cdd:COG1075    8 VVLVHGL--GGSAASWAPLAPRLRAAGYPVYALNY---PSTNGSIEDSA-----EQLAAFVDAVLAatgAEKVdLVGHSM 77

                         90       100
                 ....*....|....*....|....*..
gi 440918682 154 GGwLMLHAAIAR---PEKVVALIGVAT 177
Cdd:COG1075   78 GG-LVARYYLKRlggAAKVARVVTLGT 103
 
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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