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Conserved domains on  [gi|378734614|gb|EHY61073|]
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acetyltransferase [Exophiala dermatitidis NIH/UT8656]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11441181)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate

CATH:  3.40.630.30
EC:  2.3.-.-
Gene Ontology:  GO:0016746|GO:0008080
PubMed:  27367672|26818562|15581578|10940244
SCOP:  3000403

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
2-177 2.15e-37

L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 126.26  E-value: 2.15e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378734614   2 AVTVRPATEADLPQVRAIFEHYVLNTIVSFMVQRPPPDYIEQRFQEIASRNLPYLVAVgDGGQVVGYTYAAAFRGYmLGY 81
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAILAPGRPVLVAE-EDGEVVGFASLGPFRPR-PAY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378734614  82 GHTVEISLFCHPQHTNKGVGSQMIQQLLQMLRttkhatkevghednvvEFDIKKVIAVmsVDESAPNSgLALrdwYLRWG 161
Cdd:COG1247   79 RGTAEESIYVDPDARGRGIGRALLEALIERAR----------------ARGYRRLVAV--VLADNEAS-IAL---YEKLG 136

                        170
                 ....*....|....*.
gi 378734614 162 FEEVGRLKGVGSKNGQ 177
Cdd:COG1247  137 FEEVGTLPEVGFKFGR 152
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
2-177 2.15e-37

L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 126.26  E-value: 2.15e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378734614   2 AVTVRPATEADLPQVRAIFEHYVLNTIVSFMVQRPPPDYIEQRFQEIASRNLPYLVAVgDGGQVVGYTYAAAFRGYmLGY 81
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAILAPGRPVLVAE-EDGEVVGFASLGPFRPR-PAY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378734614  82 GHTVEISLFCHPQHTNKGVGSQMIQQLLQMLRttkhatkevghednvvEFDIKKVIAVmsVDESAPNSgLALrdwYLRWG 161
Cdd:COG1247   79 RGTAEESIYVDPDARGRGIGRALLEALIERAR----------------ARGYRRLVAV--VLADNEAS-IAL---YEKLG 136

                        170
                 ....*....|....*.
gi 378734614 162 FEEVGRLKGVGSKNGQ 177
Cdd:COG1247  137 FEEVGTLPEVGFKFGR 152
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 38-113 1.19e-06

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 45.20  E-value: 1.19e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 378734614   38 PDYIEQRFQEIASRNLPYLVAVGDGGQVVGYtyaAAFRGYMLGYGHTVEISLFCHPQHTNKGVGSQMIQQLLQMLR 113
Cdd:pfam00583  17 PDEPLDLLEDWDEDASEGFFVAEEDGELVGF---ASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWAR 89
PRK01346 PRK01346
enhanced intracellular survival protein Eis;
1-113 2.54e-04

enhanced intracellular survival protein Eis;


Pssm-ID: 234945 [Multi-domain]  Cd Length: 411  Bit Score: 40.30  E-value: 2.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378734614   1 MAVTVRPATEADLPQVraifehyVLNTIVSFmVQRPPPDYIEQRFQEIASRNlpyLVAVGDGGQVVGyTYAAAFRGYMLG 80
Cdd:PRK01346   5 MAITIRTATEEDWPAW-------FRAAATGF-GDSPSDEELEAWRALVEPDR---TLGAFDGDEVVG-TAGAFDLRLTVP 72

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 378734614  81 YGHTVEISLFCH----PQHTNKGVGSQMIQQLLQMLR 113
Cdd:PRK01346  73 GGAVLPAAGVTAvtvaPTHRRRGLLTALMREQLRRIR 109
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 55-113 2.95e-04

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 37.64  E-value: 2.95e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 378734614  55 YLVAVgDGGQVVGYTYAAAFRGYmlgyGHTVEISLFC-HPQHTNKGVGSQMIQQLLQMLR 113
Cdd:cd04301    1 FLVAE-DDGEIVGFASLSPDGSG----GDTAYIGDLAvLPEYRGKGIGSALLEAAEEEAR 55
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
2-177 2.15e-37

L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 126.26  E-value: 2.15e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378734614   2 AVTVRPATEADLPQVRAIFEHYVLNTIVSFMVQRPPPDYIEQRFQEIASRNLPYLVAVgDGGQVVGYTYAAAFRGYmLGY 81
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAILAPGRPVLVAE-EDGEVVGFASLGPFRPR-PAY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378734614  82 GHTVEISLFCHPQHTNKGVGSQMIQQLLQMLRttkhatkevghednvvEFDIKKVIAVmsVDESAPNSgLALrdwYLRWG 161
Cdd:COG1247   79 RGTAEESIYVDPDARGRGIGRALLEALIERAR----------------ARGYRRLVAV--VLADNEAS-IAL---YEKLG 136

                        170
                 ....*....|....*.
gi 378734614 162 FEEVGRLKGVGSKNGQ 177
Cdd:COG1247  137 FEEVGTLPEVGFKFGR 152
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 3-167 1.20e-10

N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440859 [Multi-domain]  Cd Length: 132  Bit Score: 56.54  E-value: 1.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378734614   3 VTVRPATEADLPQVRAIFEHYVLNTIVSFmvqrpppdyieqrfqeiasrnlpYLVAVgDGGQVVGYtyaAAFRGYmlgYG 82
Cdd:COG1246    1 MTIRPATPDDVPAILELIRPYALEEEIGE-----------------------FWVAE-EDGEIVGC---AALHPL---DE 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378734614  83 HTVEI-SLFCHPQHTNKGVGSQMIQQLLQMLRttkhatkevghednvvEFDIKKVIAVmsvdesapnSGLALRDWYLRWG 161
Cdd:COG1246   51 DLAELrSLAVHPDYRGRGIGRRLLEALLAEAR----------------ELGLKRLFLL---------TTSAAIHFYEKLG 105


                 ....*.
gi 378734614 162 FEEVGR 167
Cdd:COG1246  106 FEEIDK 111
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
5-168 1.69e-10

Predicted N-acetyltransferase YhbS [General function prediction only];


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 56.25  E-value: 1.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378734614   5 VRPATEADLPQVRAIFEHyvlntivSFmvqrpPPDYIEQRFQEIASRNLPY--LVAVgDGGQVVGYtyAAAFRGYMLGYG 82
Cdd:COG3153    1 IRPATPEDAEAIAALLRA-------AF-----GPGREAELVDRLREDPAAGlsLVAE-DDGEIVGH--VALSPVDIDGEG 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378734614  83 HTVEIS-LFCHPQHTNKGVGSQMIQQLLQMLRttkhatkevghednvvEFDIKKVIAVmsvdesapnSGLALRDWYLRWG 161
Cdd:COG3153   66 PALLLGpLAVDPEYRGQGIGRALMRAALEAAR----------------ERGARAVVLL---------GDPSLLPFYERFG 120


                 ....*..
gi 378734614 162 FEEVGRL 168
Cdd:COG3153  121 FRPAGEL 127
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 3-177 4.21e-07

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 47.69  E-value: 4.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378734614   3 VTVRPATEADLPQVRAIFEHyvlNTIVSFMVQRPPP-----DYIEQRFQEIASRN-LPYLVAVGDGGQVVGYTyaaafrG 76
Cdd:COG1670    8 LRLRPLRPEDAEALAELLND---PEVARYLPGPPYSleearAWLERLLADWADGGaLPFAIEDKEDGELIGVV------G 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378734614  77 YML--GYGHTVEISLFCHPQHTNKGVGSQMIQQLLQMLRTtkhatkevghednvvEFDIKKVIAVMSVDesapNSG-LAL 153
Cdd:COG1670   79 LYDidRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFE---------------ELGLHRVEAEVDPD----NTAsIRV 139

                        170       180
                 ....*....|....*....|....
gi 378734614 154 rdwYLRWGFEEVGRLKGVGSKNGQ 177
Cdd:COG1670  140 ---LEKLGFRLEGTLRDALVIDGR 160
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 38-113 1.19e-06

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 45.20  E-value: 1.19e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 378734614   38 PDYIEQRFQEIASRNLPYLVAVGDGGQVVGYtyaAAFRGYMLGYGHTVEISLFCHPQHTNKGVGSQMIQQLLQMLR 113
Cdd:pfam00583  17 PDEPLDLLEDWDEDASEGFFVAEEDGELVGF---ASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWAR 89
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 5-113 1.54e-06

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 45.25  E-value: 1.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378734614    5 VRPATEADLPQVRAIFEhYVLntivsfmvQRPPPDYIEQRFQEIASRNlPYLVAVgDGGQVVG----YTYAAAFRGYMLG 80
Cdd:pfam13527   1 IRPLTEDEFDEVLRLLE-YAF--------QDEDSPELREYFRPLLEEG-RVLGAF-DDGELVStlalYPFELNVPGKTLP 69

                          90       100       110
                  ....*....|....*....|....*....|...
gi 378734614   81 YGHTVEISLfcHPQHTNKGVGSQMIQQLLQMLR 113
Cdd:pfam13527  70 AAGITGVAT--YPEYRGRGVMSRLLRRSLEEMR 100
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 3-110 3.92e-05

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 41.56  E-value: 3.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378734614    3 VTVRPATEADLPqvrAIFEHYVLNTIVSFMVQRPPP-----DYIEQRFQEIA-SRNLPYLVAVGDGGQV--VGYTYaaaf 74
Cdd:pfam13302   2 LLLRPLTEEDAE---ALFELLSDPEVMRYGVPWPLTleearEWLARIWAADEaERGYGWAIELKDTGFIgsIGLYD---- 74

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 378734614   75 rgyMLGYGHTVEISLFCHPQHTNKGVGSQMIQQLLQ 110
Cdd:pfam13302  75 ---IDGEPERAELGYWLGPDYWGKGYATEAVRALLE 107
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 3-168 1.26e-04

N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, General function prediction only];


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 40.04  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378734614   3 VTVRPATEADLPQVRAIFEhyvlntivsfmvqrpppdyIEQRFQEIASRNLPYL-VAVGDGGQVVGYtyaAAFRgyMLGY 81
Cdd:COG0454    1 MSIRKATPEDINFILLIEA-------------------LDAELKAMEGSLAGAEfIAVDDKGEPIGF---AGLR--RLDD 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378734614  82 GHtVEIS-LFCHPQHTNKGVGSQMIQQLLQMLRttkhatkEVGhednvvefdiKKVIAVMSVDESAPNsglalRDWYLRW 160
Cdd:COG0454   57 KV-LELKrLYVLPEYRGKGIGKALLEALLEWAR-------ERG----------CTALELDTLDGNPAA-----IRFYERL 113


                 ....*...
gi 378734614 161 GFEEVGRL 168
Cdd:COG0454  114 GFKEIERY 121
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 55-131 1.41e-04

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 38.97  E-value: 1.41e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 378734614   55 YLVAVgDGGQVVGYTYAAAFrgymLGYGHTVEISLFCHPQHTNKGVGSQMIQQLLQMLRTTKHATKEVGHEDNVVEF 131
Cdd:pfam13508   5 FFVAE-DDGKIVGFAALLPL----DDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAAAF 76
PRK01346 PRK01346
enhanced intracellular survival protein Eis;
1-113 2.54e-04

enhanced intracellular survival protein Eis;


Pssm-ID: 234945 [Multi-domain]  Cd Length: 411  Bit Score: 40.30  E-value: 2.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378734614   1 MAVTVRPATEADLPQVraifehyVLNTIVSFmVQRPPPDYIEQRFQEIASRNlpyLVAVGDGGQVVGyTYAAAFRGYMLG 80
Cdd:PRK01346   5 MAITIRTATEEDWPAW-------FRAAATGF-GDSPSDEELEAWRALVEPDR---TLGAFDGDEVVG-TAGAFDLRLTVP 72

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 378734614  81 YGHTVEISLFCH----PQHTNKGVGSQMIQQLLQMLR 113
Cdd:PRK01346  73 GGAVLPAAGVTAvtvaPTHRRRGLLTALMREQLRRIR 109
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 55-113 2.95e-04

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 37.64  E-value: 2.95e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 378734614  55 YLVAVgDGGQVVGYTYAAAFRGYmlgyGHTVEISLFC-HPQHTNKGVGSQMIQQLLQMLR 113
Cdd:cd04301    1 FLVAE-DDGEIVGFASLSPDGSG----GDTAYIGDLAvLPEYRGKGIGSALLEAAEEEAR 55
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 76-170 1.54e-03

Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 36.17  E-value: 1.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378734614  76 GYMLGY----GHTVEI-SLFCHPQHTNKGVGSQMIQQLLQMLRttkhatkevghednvvEFDIKKViaVMSVDESAPnsg 150
Cdd:COG0456    1 GFALLGlvdgGDEAEIeDLAVDPEYRGRGIGRALLEAALERAR----------------ERGARRL--RLEVREDNE--- 59

                         90       100
                 ....*....|....*....|
gi 378734614 151 lALRDWYLRWGFEEVGRLKG 170
Cdd:COG0456   60 -AAIALYEKLGFEEVGERPN 78
 
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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