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Conserved domains on  [gi|2320460989|ref|WP_263800009|]
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GNAT family N-acetyltransferase [Lentilactobacillus hilgardii]

Protein Classification

GNAT family protein( domain architecture ID 106742)

GNAT (Gcn5-related N-acetyltransferase) family protein similar to N-acetyltransferases that catalyze the transfer of an acetyl group from acetyl-CoA to a substrate

PubMed:  15581578

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NAT_SF super family cl17182
N-Acyltransferase superfamily: Various enyzmes that characteristicly catalyze the transfer of ...
12-143 7.48e-22

N-Acyltransferase superfamily: Various enyzmes that characteristicly 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, 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 mechanism is an ordered Bi-Bi ternary complex kinetic mechanism for most GNATs: 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 then 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/ph enylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


The actual alignment was detected with superfamily member PRK10562:

Pssm-ID: 473072 [Multi-domain]  Cd Length: 145  Bit Score: 85.12  E-value: 7.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320460989  12 ELDKIAKIWLTANLEAHSFINKDYWLSNYVAVKKQ-LGEAELFIATQGQTITGFLGI-SGTYIAGLFVDKRFRSRGIGRQ 89
Cdd:PRK10562    9 DLPAILQLWLESTIWAHPFIKEQYWRESAPLVRDVyLPAAQTWVWEEDGKLLGFVSVlEGRFVGALFVAPKAVRRGIGKA 88
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2320460989  90 LLDTAKRSRSKLSLSVYEKNKAAFHFYIHQGFIKTSTEIDGATGETVFNMEWQK 143
Cdd:PRK10562   89 LMQHVQQRYPHLSLEVYQKNQRAVNFYHAQGFRIVDSAWQEETQHPTWIMSWQA 142
 
Name Accession Description Interval E-value
PRK10562 PRK10562
putative acetyltransferase; Provisional
12-143 7.48e-22

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 85.12  E-value: 7.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320460989  12 ELDKIAKIWLTANLEAHSFINKDYWLSNYVAVKKQ-LGEAELFIATQGQTITGFLGI-SGTYIAGLFVDKRFRSRGIGRQ 89
Cdd:PRK10562    9 DLPAILQLWLESTIWAHPFIKEQYWRESAPLVRDVyLPAAQTWVWEEDGKLLGFVSVlEGRFVGALFVAPKAVRRGIGKA 88
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2320460989  90 LLDTAKRSRSKLSLSVYEKNKAAFHFYIHQGFIKTSTEIDGATGETVFNMEWQK 143
Cdd:PRK10562   89 LMQHVQQRYPHLSLEVYQKNQRAVNFYHAQGFRIVDSAWQEETQHPTWIMSWQA 142
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
71-142 5.55e-12

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 58.13  E-value: 5.55e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2320460989  71 YIAGLFVDKRFRSRGIGRQLLDTA-----KRSRSKLSLSVYEKNKAAFHFYIHQGFIKTStEIDGATGETVFNMEWQ 142
Cdd:COG0456    15 EIEDLAVDPEYRGRGIGRALLEAAlerarERGARRLRLEVREDNEAAIALYEKLGFEEVG-ERPNYYGDDALVMEKE 90
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
48-141 5.95e-11

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: 56.51  E-value: 5.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320460989  48 GEAELFIATQGQTITGFLGIS-GTYIAGLFVDKRFRSRGIGRQLLDTAKRSRSKLSLSVYE----KNKAAFHFYIHQGFI 122
Cdd:pfam13673  29 GEYFFFVAFEGGQIVGVIALRdRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSEltvnASPYAVPFYEKLGFR 108
                          90
                  ....*....|....*....
gi 2320460989 123 KTSTEIDGAtGETVFNMEW 141
Cdd:pfam13673 109 ATGPEQEFN-GIRFVPMEK 126
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
52-96 2.97e-05

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: 39.95  E-value: 2.97e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2320460989  52 LFIATQGQTITGFLGISGT-------YIAGLFVDKRFRSRGIGRQLLDTAKR 96
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPDgsggdtaYIGDLAVLPEYRGKGIGSALLEAAEE 52
 
Name Accession Description Interval E-value
PRK10562 PRK10562
putative acetyltransferase; Provisional
12-143 7.48e-22

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 85.12  E-value: 7.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320460989  12 ELDKIAKIWLTANLEAHSFINKDYWLSNYVAVKKQ-LGEAELFIATQGQTITGFLGI-SGTYIAGLFVDKRFRSRGIGRQ 89
Cdd:PRK10562    9 DLPAILQLWLESTIWAHPFIKEQYWRESAPLVRDVyLPAAQTWVWEEDGKLLGFVSVlEGRFVGALFVAPKAVRRGIGKA 88
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2320460989  90 LLDTAKRSRSKLSLSVYEKNKAAFHFYIHQGFIKTSTEIDGATGETVFNMEWQK 143
Cdd:PRK10562   89 LMQHVQQRYPHLSLEVYQKNQRAVNFYHAQGFRIVDSAWQEETQHPTWIMSWQA 142
PRK10514 PRK10514
putative acetyltransferase; Provisional
12-130 2.65e-13

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 63.10  E-value: 2.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320460989  12 ELDKIAKIWLTANLEAHSFINKDYWLSNYVAVKKQLGEAELFIAT--QGQTItGFLGISGTYIAGLFVDKRFRSRGIGRQ 89
Cdd:PRK10514   11 EGERLVAIWRRSVDATHDFLSAEDRAEIEELVRSFLPEAPLWVAVdeRDQPV-GFMLLSGGHMEALFVDPDVRGCGVGRM 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2320460989  90 LLDTAKRSRSKLSLSVYEKNKAAFHFYIHQGFIKTS-TEIDG 130
Cdd:PRK10514   90 LVEHALSLHPELTTDVNEQNEQAVGFYKKMGFKVTGrSEVDD 131
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
71-142 5.55e-12

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 58.13  E-value: 5.55e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2320460989  71 YIAGLFVDKRFRSRGIGRQLLDTA-----KRSRSKLSLSVYEKNKAAFHFYIHQGFIKTStEIDGATGETVFNMEWQ 142
Cdd:COG0456    15 EIEDLAVDPEYRGRGIGRALLEAAlerarERGARRLRLEVREDNEAAIALYEKLGFEEVG-ERPNYYGDDALVMEKE 90
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
48-141 5.95e-11

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: 56.51  E-value: 5.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320460989  48 GEAELFIATQGQTITGFLGIS-GTYIAGLFVDKRFRSRGIGRQLLDTAKRSRSKLSLSVYE----KNKAAFHFYIHQGFI 122
Cdd:pfam13673  29 GEYFFFVAFEGGQIVGVIALRdRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSEltvnASPYAVPFYEKLGFR 108
                          90
                  ....*....|....*....
gi 2320460989 123 KTSTEIDGAtGETVFNMEW 141
Cdd:pfam13673 109 ATGPEQEFN-GIRFVPMEK 126
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
13-121 5.12e-10

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: 53.68  E-value: 5.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320460989  13 LDKIAKIWLTANLEAHSFINKDYWLSNyvavkKQLGEAELFIATQGQTITGFLGIS-------GTYIAGLFVDKRFRSRG 85
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDW-----DEDASEGFFVAEEDGELVGFASLSiiddeppVGEIEGLAVAPEYRGKG 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2320460989  86 IGRQLLDTA-----KRSRSKLSLSVYEKNKAAFHFYIHQGF 121
Cdd:pfam00583  76 IGTALLQALlewarERGCERIFLEVAADNLAAIALYEKLGF 116
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
45-134 8.77e-10

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 53.52  E-value: 8.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320460989  45 KQLGEAELFIATQGQTITGFLGIS-----GTYIAGLFVDKRFRSRGIGRQLLDTAK---RSR--SKLSLSVYEKNKAAFH 114
Cdd:COG0454    29 GSLAGAEFIAVDDKGEPIGFAGLRrlddkVLELKRLYVLPEYRGKGIGKALLEALLewaRERgcTALELDTLDGNPAAIR 108
                          90       100
                  ....*....|....*....|
gi 2320460989 115 FYIHQGFIKTSTEIDGATGE 134
Cdd:COG0454   109 FYERLGFKEIERYVAYVGGE 128
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
49-123 8.24e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 49.76  E-value: 8.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320460989  49 EAELFIATQGQTITGFLGISGT------YIAGLFVDKRFRSRGIGRQLLDTAKRSRSKLSLSVY--EKNKAAFHFYIHQG 120
Cdd:pfam13508   2 GGRFFVAEDDGKIVGFAALLPLddegalAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLelETTNRAAAFYEKLG 81

                  ...
gi 2320460989 121 FIK 123
Cdd:pfam13508  82 FEE 84
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
44-121 6.74e-08

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 48.84  E-value: 6.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320460989  44 KKQLGEAELFIATQGQTITGFLGIS---------GTYIAGLFVDKRFRSRGIGRQLLDTA-KRSRS----KLSLSVYEKN 109
Cdd:COG1247    46 AILAPGRPVLVAEEDGEVVGFASLGpfrprpayrGTAEESIYVDPDARGRGIGRALLEALiERARArgyrRLVAVVLADN 125
                          90
                  ....*....|..
gi 2320460989 110 KAAFHFYIHQGF 121
Cdd:COG1247   126 EASIALYEKLGF 137
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
51-127 1.17e-06

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: 44.98  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320460989  51 ELFIATQGQTITGFLGISGT-----YIAGLFVDKRFRSRGIGRQLLDTA-----KRSRSKLSLSVYEknkAAFHFYIHQG 120
Cdd:COG1246    29 EFWVAEEDGEIVGCAALHPLdedlaELRSLAVHPDYRGRGIGRRLLEALlaearELGLKRLFLLTTS---AAIHFYEKLG 105

                  ....*..
gi 2320460989 121 FIKTSTE 127
Cdd:COG1246   106 FEEIDKE 112
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
42-137 1.29e-05

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 42.38  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320460989  42 AVKKQLGEAELFIATQGQTITGFLGISGT---------YIAGLFVDKRFRSRGIGRQLLDTA-----KRSRSKLSLSVYE 107
Cdd:COG3153    31 RLREDPAAGLSLVAEDDGEIVGHVALSPVdidgegpalLLGPLAVDPEYRGQGIGRALMRAAleaarERGARAVVLLGDP 110
                          90       100       110
                  ....*....|....*....|....*....|
gi 2320460989 108 KNKAafhFYIHQGFIKTSTEIDGATGETVF 137
Cdd:COG3153   111 SLLP---FYERFGFRPAGELGLTLGPDEVF 137
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
52-96 2.97e-05

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: 39.95  E-value: 2.97e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2320460989  52 LFIATQGQTITGFLGISGT-------YIAGLFVDKRFRSRGIGRQLLDTAKR 96
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPDgsggdtaYIGDLAVLPEYRGKGIGSALLEAAEE 52
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
70-121 6.00e-05

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 39.51  E-value: 6.00e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2320460989  70 TYIAGLFVDKRFRSRGIGRQLLDTA-----KRSRSKLSLSVYEKNKAAFHFYIHQGF 121
Cdd:COG3393    16 AEISGVYTHPEYRGRGLASALVAALarealARGARTPFLYVDADNPAARRLYERLGF 72
PRK09831 PRK09831
GNAT family N-acetyltransferase;
44-144 9.25e-04

GNAT family N-acetyltransferase;


Pssm-ID: 182099  Cd Length: 147  Bit Score: 37.25  E-value: 9.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320460989  44 KKQLGEAELFIATQGQTITGFLGISGTYIAGLFVDKRFRSRGIGRQLLDTAKRSRSKLSLSVYEKNKAAFHFYihqGFIK 123
Cdd:PRK09831   47 KEKLAKSQVRVAVINAQPVGFITCIEHYIDMLFVDPEYTRRGVASALLKPLIKSESELTVDASITAKPFFERY---GFQT 123
                          90       100
                  ....*....|....*....|...
gi 2320460989 124 TSTEIDGATGE--TVFNMEWQKA 144
Cdd:PRK09831  124 VKQQRVECRGEwfINFYMRYKPQ 146
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
52-126 1.68e-03

dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;


Pssm-ID: 182877  Cd Length: 194  Bit Score: 36.83  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320460989  52 LFIATQGQtITGF-----LGISGTYIAGLFVDKRFRSRGIGRQLLDTAK---RSRSKLSLSVYEK--NKAAFHFYIHQGF 121
Cdd:PRK10975  105 LLRDASGQ-IQGFvtlreLNDTDARIGLLAVFPGAQGRGIGARLMQAALnwcQARGLTRLRVATQmgNLAALRLYIRSGA 183

                  ....*
gi 2320460989 122 IKTST 126
Cdd:PRK10975  184 NIEST 188
 
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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