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Conserved domains on  [gi|1946570881|ref|WP_198180987|]
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MULTISPECIES: GNAT family N-acetyltransferase [Lactobacillus]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10607277)

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

CATH:  3.40.630.30
EC:  2.3.1.-
Gene Ontology:  GO:0008080
PubMed:  27367672|26818562|15581578|10940244|9175471
SCOP:  3000403

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 46-121 4.98e-14

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


:

Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 62.86  E-value: 4.98e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1946570881  46 AYDQNQLVGLIRVVG-DGLTIIYIQDLLVNPAYQRRGIGTKLINSVLKKYNSVRQKVLLTENTVKTRRFYESCNFHP 121
Cdd:pfam13508   8 AEDDGKIVGFAALLPlDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAAAFYEKLGFEE 84
 
Name Accession Description Interval E-value
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 46-121 4.98e-14

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 62.86  E-value: 4.98e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1946570881  46 AYDQNQLVGLIRVVG-DGLTIIYIQDLLVNPAYQRRGIGTKLINSVLKKYNSVRQKVLLTENTVKTRRFYESCNFHP 121
Cdd:pfam13508   8 AEDDGKIVGFAALLPlDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAAAFYEKLGFEE 84
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
46-134 1.24e-10

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 55.48  E-value: 1.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946570881  46 AYDQNQLVGLIRV----VGDGLTIIYIQDLLVNPAYQRRGIGTKLINSVLKKYNSVRQKVLLTENTVKTRRFYESCNFHP 121
Cdd:COG3153    44 AEDDGEIVGHVALspvdIDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLPFYERFGFRP 123

                          90
                  ....*....|...
gi 1946570881 122 CDKYNLIAFYKDF 134
Cdd:COG3153   124 AGELGLTLGPDEV 136
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 44-92 5.82e-09

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: 49.20  E-value: 5.82e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1946570881  44 IGAYDQNQLVGLIRVV--GDGLTIIYIQDLLVNPAYQRRGIGTKLINSVLK 92
Cdd:cd04301     2 LVAEDDGEIVGFASLSpdGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEE 52
PRK09831 PRK09831
GNAT family N-acetyltransferase;
32-119 5.98e-05

GNAT family N-acetyltransferase;


Pssm-ID: 182099  Cd Length: 147  Bit Score: 40.33  E-value: 5.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946570881  32 QLQKAVVNslfaigaydqNQLVGLIRVVGDgltiiYIQDLLVNPAYQRRGIGTKLINSVLKKYNSvrqkvLLTENTVKTR 111
Cdd:PRK09831   54 QVRVAVIN----------AQPVGFITCIEH-----YIDMLFVDPEYTRRGVASALLKPLIKSESE-----LTVDASITAK 113


                  ....*...
gi 1946570881 112 RFYESCNF 119
Cdd:PRK09831  114 PFFERYGF 121
 
Name Accession Description Interval E-value
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 46-121 4.98e-14

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 62.86  E-value: 4.98e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1946570881  46 AYDQNQLVGLIRVVG-DGLTIIYIQDLLVNPAYQRRGIGTKLINSVLKKYNSVRQKVLLTENTVKTRRFYESCNFHP 121
Cdd:pfam13508   8 AEDDGKIVGFAALLPlDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAAAFYEKLGFEE 84
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 10-119 3.74e-12

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: 58.68  E-value: 3.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946570881  10 AMEQLINLYTSVGWSSYTQnPRQLQKAVVNSLFAIGAYDQNQLVGLIR--VVGDGLTIIYIQDLLVNPAYQRRGIGTKLI 87
Cdd:pfam00583   3 ALYELLSEEFPEPWPDEPL-DLLEDWDEDASEGFFVAEEDGELVGFASlsIIDDEPPVGEIEGLAVAPEYRGKGIGTALL 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1946570881  88 NSVL---KKYNSVRQKVLLTENTVKTRRFYESCNF 119
Cdd:pfam00583  82 QALLewaRERGCERIFLEVAADNLAAIALYEKLGF 116
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 44-123 7.06e-12

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


Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 58.44  E-value: 7.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946570881  44 IGAYDQNQLVGLIRVVGDGltiiYIQDLLVNPAYQRRGIGTKLINSVLKKYnsVRQKVLLTENTVK----TRRFYESCNF 119
Cdd:pfam13673  34 FVAFEGGQIVGVIALRDRG----HISLLFVDPDYQGQGIGKALLEAVEDYA--EKDGIKLSELTVNaspyAVPFYEKLGF 107


                  ....
gi 1946570881 120 HPCD 123
Cdd:pfam13673 108 RATG 111
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
46-134 1.24e-10

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 55.48  E-value: 1.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946570881  46 AYDQNQLVGLIRV----VGDGLTIIYIQDLLVNPAYQRRGIGTKLINSVLKKYNSVRQKVLLTENTVKTRRFYESCNFHP 121
Cdd:COG3153    44 AEDDGEIVGHVALspvdIDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLPFYERFGFRP 123

                          90
                  ....*....|...
gi 1946570881 122 CDKYNLIAFYKDF 134
Cdd:COG3153   124 AGELGLTLGPDEV 136
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 46-127 1.29e-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: 55.00  E-value: 1.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946570881  46 AYDQNQLVGLIRVVGDGLTIIYIQDLLVNPAYQRRGIGTKLINSVLKK-----YNSVRqkvLLTenTVKTRRFYESCNFH 120
Cdd:COG1246    33 AEEDGEIVGCAALHPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEarelgLKRLF---LLT--TSAAIHFYEKLGFE 107


                  ....*..
gi 1946570881 121 PCDKYNL 127
Cdd:COG1246   108 EIDKEDL 114
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 44-92 5.82e-09

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: 49.20  E-value: 5.82e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1946570881  44 IGAYDQNQLVGLIRVV--GDGLTIIYIQDLLVNPAYQRRGIGTKLINSVLK 92
Cdd:cd04301     2 LVAEDDGEIVGFASLSpdGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEE 52
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 67-123 3.67e-08

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 47.73  E-value: 3.67e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946570881  67 YIQDLLVNPAYQRRGIGTKLINSVLKKYNSV-RQKVLLT--ENTVKTRRFYESCNFHPCD 123
Cdd:COG0456    15 EIEDLAVDPEYRGRGIGRALLEAALERARERgARRLRLEvrEDNEAAIALYEKLGFEEVG 74
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 42-121 5.61e-08

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 48.13  E-value: 5.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946570881  42 FAIGAYDQNQLVG--LIRVVGDGltIIYIQDLLVNPAYQRRGIGTKLIN---SVLKKYNSVRQKVLLTENTVKTRRFYES 116
Cdd:COG0454    35 EFIAVDDKGEPIGfaGLRRLDDK--VLELKRLYVLPEYRGKGIGKALLEallEWARERGCTALELDTLDGNPAAIRFYER 112


                  ....*
gi 1946570881 117 CNFHP 121
Cdd:COG0454   113 LGFKE 117
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
44-122 6.61e-08

Predicted N-acyltransferase, GNAT family [General function prediction only];


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 47.87  E-value: 6.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946570881  44 IGAYDQNQLVGLIRVVGDGLTIIYIQDLLVNPAYQRRGIGTKLINSVLK--KYNSVRQKVLLTENTVKtrRFYESCNFHP 121
Cdd:COG2153    37 LLAYDDGELVATARLLPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEeaRERGARRIVLSAQAHAV--GFYEKLGFVP 114


                  .
gi 1946570881 122 C 122
Cdd:COG2153   115 V 115
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
51-130 8.56e-07

Predicted acetyltransferase, GNAT family [General function prediction only];


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 44.13  E-value: 8.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946570881  51 QLVGLIRVVGDGLTIIYIQDLLVNPAYQRRGIGTKLINSVLKKY--NSVRQKVLLT-ENTVKTRRFYESCNFHPCDKYNL 127
Cdd:COG3393     1 ELVAMAGVRAESPGVAEISGVYTHPEYRGRGLASALVAALAREAlaRGARTPFLYVdADNPAARRLYERLGFRPVGEYAT 80


                  ...
gi 1946570881 128 IAF 130
Cdd:COG3393    81 VLF 83
PRK09831 PRK09831
GNAT family N-acetyltransferase;
32-119 5.98e-05

GNAT family N-acetyltransferase;


Pssm-ID: 182099  Cd Length: 147  Bit Score: 40.33  E-value: 5.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946570881  32 QLQKAVVNslfaigaydqNQLVGLIRVVGDgltiiYIQDLLVNPAYQRRGIGTKLINSVLKKYNSvrqkvLLTENTVKTR 111
Cdd:PRK09831   54 QVRVAVIN----------AQPVGFITCIEH-----YIDMLFVDPEYTRRGVASALLKPLIKSESE-----LTVDASITAK 113


                  ....*...
gi 1946570881 112 RFYESCNF 119
Cdd:PRK09831  114 PFFERYGF 121
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
46-130 1.41e-04

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 39.59  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946570881  46 AYDQNQLVGLIRVV----GDGLTIIYIQDLLVNPAYQRRGIGTKLINSVLKK-----YNSVRQKVLLtENTvKTRRFYES 116
Cdd:COG1247    57 AEEDGEVVGFASLGpfrpRPAYRGTAEESIYVDPDARGRGIGRALLEALIERarargYRRLVAVVLA-DNE-ASIALYEK 134

                          90
                  ....*....|....
gi 1946570881 117 CNFHPCDKYNLIAF 130
Cdd:COG1247   135 LGFEEVGTLPEVGF 148
PRK07757 PRK07757
N-acetyltransferase;
46-124 2.11e-04

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 38.64  E-value: 2.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946570881  46 AYDQNQLVGlirvVGdGLTIIY-----IQDLLVNPAYQRRGIGTKLIN---SVLKKYNsVRQKVLLTENtvktRRFYESC 117
Cdd:PRK07757   46 AEEEGEIVG----CC-ALHILWedlaeIRSLAVSEDYRGQGIGRMLVEaclEEARELG-VKRVFALTYQ----PEFFEKL 115


                  ....*..
gi 1946570881 118 NFHPCDK 124
Cdd:PRK07757  116 GFREVDK 122
PanZ pfam12568
Acetyltransferase (GNAT) domain, PanZ; This domain family is found in bacteria, and is ...
 28-121 2.45e-04

Acetyltransferase (GNAT) domain, PanZ; This domain family is found in bacteria, and is approximately 40 amino acids in length. The proteins in this family are members of the acetyltransferases of the GNAT family. Family members such as PanZ has been shown to be involved in the biosynthesis of Coenzyme A (CoA). CoA is a ubiquitous and essential cofactor, synthesized from the precursor pantothenate. In all organizms, the final step in pantothenate biosynthesis relies on the presence of beta-alanine, which comes from different sources in bacteria, yeast, and plants. In bacteria, beta-alanine is derived by the action of alpha-decarboxylase (ADC) enzyme. PanZ promotes the activation of the zymogen, PanD, to form aspartate alpha-decarboxylase (ADC) in a CoA-dependent manner. Thereby, playing an essential role in the biosynthetic pathway to pantothenate and the regulation of CoA biosynthesis. Structure and function studies show that direct interaction of PanD with the PanZ Arg43-Leu46 loop promotes PanD to adopt a reactive conformation, which leads to activation.


Pssm-ID: 432642  Cd Length: 128  Bit Score: 38.23  E-value: 2.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946570881  28 QNPRQLQKAVV--NSLFAigAYDQNQLVGLIRV-VGDglTIIYIQDLLVNPAYQRRGIGTKLINSVLKKYNSVRQKVLLT 104
Cdd:pfam12568  25 QSPDTLQAWLDedHRLFA--ARFNDRLLGAVLVtLSD--QEGELSDLCVREVTRRRGVGQYLIEETLRQNPEVKCWWLAD 100

                          90       100
                  ....*....|....*....|..
gi 1946570881 105 ENTVKTRR-----FYESCNFHP 121
Cdd:pfam12568 101 EGVEPADRgvmagFMQACGFSA 122
PRK12308 PRK12308
argininosuccinate lyase;
10-127 5.15e-03

argininosuccinate lyase;


Pssm-ID: 183425 [Multi-domain]  Cd Length: 614  Bit Score: 35.53  E-value: 5.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946570881  10 AMEQLINLYTSVGwssytQNPRQLQKAVVNSL--FAIGAYDQNqlvglirVVGDGLTIIY------IQDLLVNPAYQRRG 81
Cdd:PRK12308  476 AIEGMVAYWAGLG-----ENLPRSRNELVRDIgsFAVAEHHGE-------VTGCASLYIYdsglaeIRSLGVEAGWQVQG 543

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1946570881  82 IGTKLINSVLKKYN--SVRQKVLLTentvKTRRFYESCNFHPCDKYNL 127
Cdd:PRK12308  544 QGSALVQYLVEKARqmAIKKVFVLT----RVPEFFMKQGFSPTSKSLL 587
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 49-119 8.77e-03

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 34.13  E-value: 8.77e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1946570881  49 QNQLVG--LIRVVGDGLTIIYIQdllVNPAYQRRGIGTKLINSVLkkyNSVRQKVLLT------ENTVKTRRFYESCNF 119
Cdd:PRK09491   48 NGQMAAfaITQVVLDEATLFNIA---VDPDYQRQGLGRALLEHLI---DELEKRGVATlwlevrASNAAAIALYESLGF 120
 
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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