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Conserved domains on  [gi|612907559|gb|EZV19207|]
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hypothetical protein U926_01332 [Staphylococcus aureus 12S00881]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11447364)

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
SCOP:  3000403

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
8-177 1.31e-46

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: 150.53  E-value: 1.31e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907559   8 EQITLKILEVHDTEALFNLVNRSRnsLREWLPWVDATEQssDTRAFIKRGLLQFADGNGFQCGIWY--GGTLVGVIGLHE 85
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELLNDPE--VARYLPGPPYSLE--EARAWLERLLADWADGGALPFAIEDkeDGELIGVVGLYD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907559  86 INHMHRKTSLGYYLDKQYEGHGIMTQAVEALIKYCFDEIDLNRIEISVAVNNEKSQAIPERLGFTREGMLRDNELLNGIY 165
Cdd:COG1670   82 IDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRY 161
                        170
                 ....*....|..
gi 612907559 166 SSSYIYSLLKSE 177
Cdd:COG1670  162 RDHVLYSLLREE 173
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
8-177 1.31e-46

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: 150.53  E-value: 1.31e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907559   8 EQITLKILEVHDTEALFNLVNRSRnsLREWLPWVDATEQssDTRAFIKRGLLQFADGNGFQCGIWY--GGTLVGVIGLHE 85
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELLNDPE--VARYLPGPPYSLE--EARAWLERLLADWADGGALPFAIEDkeDGELIGVVGLYD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907559  86 INHMHRKTSLGYYLDKQYEGHGIMTQAVEALIKYCFDEIDLNRIEISVAVNNEKSQAIPERLGFTREGMLRDNELLNGIY 165
Cdd:COG1670   82 IDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRY 161
                        170
                 ....*....|..
gi 612907559 166 SSSYIYSLLKSE 177
Cdd:COG1670  162 RDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
15-150 1.24e-26

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 98.19  E-value: 1.24e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907559   15 LEVHDTEALFNLVNRSRnSLREWLPWVDATEQssdTRAFIKRGLLQFADGNGFQCGIWYGGT-LVGVIGLHEINHMHRKT 93
Cdd:pfam13302   7 LTEEDAEALFELLSDPE-VMRYGVPWPLTLEE---AREWLARIWAADEAERGYGWAIELKDTgFIGSIGLYDIDGEPERA 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 612907559   94 SLGYYLDKQYEGHGIMTQAVEALIKYCFDEIDLNRIEISVAVNNEKSQAIPERLGFT 150
Cdd:pfam13302  83 ELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
4-171 3.36e-23

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 90.59  E-value: 3.36e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907559   4 MKVNEQITLKILEVHDTEALFNLVNRSRNSLREWLPWVDATEQSSDTRAFIKRGLLQFADGNGFQCGIWYGGTLVGVIGL 83
Cdd:PRK10151   5 IPVSESLELHAVDESHVTPLHQLVCKNKTWLQQSLNWPQFVQSEEDTRKTVQGNVMLHQRGYAKMFMIFKEDELIGVLSF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907559  84 HEINHMHRKTSLGYYLDKQYEGHGIMTQAVEALIKYCFDEIDLNRIEISVAVNNEKSQAIPERLGFTREGMLRDNELLNG 163
Cdd:PRK10151  85 NRIEPLNKTAYIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPASNQVALRNGFTLEGCLKQAEYLNG 164

                 ....*...
gi 612907559 164 IYSSSYIY 171
Cdd:PRK10151 165 AYDDVNLY 172
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
33-157 2.46e-07

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this family are members of the pfam00583 (GNAT) superfamily of acetyltransferases and are proposed to perform a N-acetylation step in the process of pseudaminic acid biosynthesis in Campylobacter species. This gene is commonly observed in apparent operons with other genes responsible for the biosynthesis of pseudaminic acid and as a component of flagellar and exopolysaccharide biosynthesis loci. Significantly, many genomes containing other components of this pathway lack this gene, indicating that some other N-acetyl transferases may be incolved and/or the step is optional, resulting in a non-acetylated pseudaminic acid variant sugar.


Pssm-ID: 274661 [Multi-domain]  Cd Length: 152  Bit Score: 47.74  E-value: 2.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907559   33 SLREWLPWVDATEQSSDTRAFIkrgllqfadgngfqcgIWYGGTLVGVIGLHEINHMHRKTSLGYY---LDKQYEGHGIM 109
Cdd:TIGR03585  34 DWEEHLHFIEALKQDPNRRYWI----------------VCQESRPIGVISFTDINLVHKSAFWGIYanpFCKPGVGSVLE 97
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 612907559  110 tqavEALIKYCFDEIDLNRIEISVAVNNEKSQAIPERLGFTREGMLRD 157
Cdd:TIGR03585  98 ----EAALEYAFEHLGLHKLSLEVLESNNKALKLYEKFGFEREGVFRQ 141
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
8-177 1.31e-46

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: 150.53  E-value: 1.31e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907559   8 EQITLKILEVHDTEALFNLVNRSRnsLREWLPWVDATEQssDTRAFIKRGLLQFADGNGFQCGIWY--GGTLVGVIGLHE 85
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELLNDPE--VARYLPGPPYSLE--EARAWLERLLADWADGGALPFAIEDkeDGELIGVVGLYD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907559  86 INHMHRKTSLGYYLDKQYEGHGIMTQAVEALIKYCFDEIDLNRIEISVAVNNEKSQAIPERLGFTREGMLRDNELLNGIY 165
Cdd:COG1670   82 IDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRY 161
                        170
                 ....*....|..
gi 612907559 166 SSSYIYSLLKSE 177
Cdd:COG1670  162 RDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
15-150 1.24e-26

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 98.19  E-value: 1.24e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907559   15 LEVHDTEALFNLVNRSRnSLREWLPWVDATEQssdTRAFIKRGLLQFADGNGFQCGIWYGGT-LVGVIGLHEINHMHRKT 93
Cdd:pfam13302   7 LTEEDAEALFELLSDPE-VMRYGVPWPLTLEE---AREWLARIWAADEAERGYGWAIELKDTgFIGSIGLYDIDGEPERA 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 612907559   94 SLGYYLDKQYEGHGIMTQAVEALIKYCFDEIDLNRIEISVAVNNEKSQAIPERLGFT 150
Cdd:pfam13302  83 ELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
4-171 3.36e-23

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 90.59  E-value: 3.36e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907559   4 MKVNEQITLKILEVHDTEALFNLVNRSRNSLREWLPWVDATEQSSDTRAFIKRGLLQFADGNGFQCGIWYGGTLVGVIGL 83
Cdd:PRK10151   5 IPVSESLELHAVDESHVTPLHQLVCKNKTWLQQSLNWPQFVQSEEDTRKTVQGNVMLHQRGYAKMFMIFKEDELIGVLSF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907559  84 HEINHMHRKTSLGYYLDKQYEGHGIMTQAVEALIKYCFDEIDLNRIEISVAVNNEKSQAIPERLGFTREGMLRDNELLNG 163
Cdd:PRK10151  85 NRIEPLNKTAYIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPASNQVALRNGFTLEGCLKQAEYLNG 164

                 ....*...
gi 612907559 164 IYSSSYIY 171
Cdd:PRK10151 165 AYDDVNLY 172
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
75-165 1.07e-11

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 60.58  E-value: 1.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907559  75 GTLVGVIGLHEINHMHRKTSLGYYLDKQYEGHGIMTQAVEALIKYCFDEIDLNRIEISVAVNNEKSQAIPERLGFTREGM 154
Cdd:PRK15130  66 GEKAGLVELVEINHVHRRAEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGE 145
                         90
                 ....*....|.
gi 612907559 155 LRDNELLNGIY 165
Cdd:PRK15130 146 LIHEFFINGEY 156
PRK10809 PRK10809
30S ribosomal protein S5 alanine N-acetyltransferase;
95-181 9.08e-09

30S ribosomal protein S5 alanine N-acetyltransferase;


Pssm-ID: 182749  Cd Length: 194  Bit Score: 52.43  E-value: 9.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907559  95 LGYYLDKQYEGHGIMTQAVEALIKYCFDEIDLNRIEISVAVNNEKSQAIPERLGFTREGMLRDNELLNGIYSSSYIYSLL 174
Cdd:PRK10809 107 LGYSLGQKWQGQGLMFEALQAAIRYMQRQQHMHRIMANYMPHNKRSGDLLARLGFEKEGYAKDYLLIDGQWRDHVLTALT 186

                 ....*..
gi 612907559 175 KSEFNEG 181
Cdd:PRK10809 187 TPEWTPG 193
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
33-157 2.46e-07

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this family are members of the pfam00583 (GNAT) superfamily of acetyltransferases and are proposed to perform a N-acetylation step in the process of pseudaminic acid biosynthesis in Campylobacter species. This gene is commonly observed in apparent operons with other genes responsible for the biosynthesis of pseudaminic acid and as a component of flagellar and exopolysaccharide biosynthesis loci. Significantly, many genomes containing other components of this pathway lack this gene, indicating that some other N-acetyl transferases may be incolved and/or the step is optional, resulting in a non-acetylated pseudaminic acid variant sugar.


Pssm-ID: 274661 [Multi-domain]  Cd Length: 152  Bit Score: 47.74  E-value: 2.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907559   33 SLREWLPWVDATEQSSDTRAFIkrgllqfadgngfqcgIWYGGTLVGVIGLHEINHMHRKTSLGYY---LDKQYEGHGIM 109
Cdd:TIGR03585  34 DWEEHLHFIEALKQDPNRRYWI----------------VCQESRPIGVISFTDINLVHKSAFWGIYanpFCKPGVGSVLE 97
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 612907559  110 tqavEALIKYCFDEIDLNRIEISVAVNNEKSQAIPERLGFTREGMLRD 157
Cdd:TIGR03585  98 ----EAALEYAFEHLGLHKLSLEVLESNNKALKLYEKFGFEREGVFRQ 141
PRK10140 PRK10140
N-acetyltransferase;
75-175 4.93e-07

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 47.28  E-value: 4.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907559  75 GTLVGVIGLHEINHMHRK--TSLGYYLDKQYEGHGIMTQAVEALIKYCFDEIDLNRIEISVAVNNEKSQAIPERLGFTRE 152
Cdd:PRK10140  60 GDVVGHLTIDVQQRPRRShvADFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIE 139
                         90       100
                 ....*....|....*....|...
gi 612907559 153 GMLRDNELLNGIYSSSYIYSLLK 175
Cdd:PRK10140 140 GTGKKYALRNGEYVDAYYMARVK 162
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
72-153 8.26e-07

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: 46.11  E-value: 8.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907559   72 WYGGTLVGVIGLHEINHMHRktslgYYLDKQYEGHGIMTQAVEALIKYCfDEIDLNRIEISVavnNEKSQAIP--ERLGF 149
Cdd:pfam13673  37 FEGGQIVGVIALRDRGHISL-----LFVDPDYQGQGIGKALLEAVEDYA-EKDGIKLSELTV---NASPYAVPfyEKLGF 107

                  ....
gi 612907559  150 TREG 153
Cdd:pfam13673 108 RATG 111
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
98-174 7.28e-05

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 41.13  E-value: 7.28e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612907559  98 YLDKQYEGHGIMTQAVEALIKYCfDEIDLNRIEISVAVNNEKSQAIPERLGFTREGMLRDNELLNGIYSSSYIYSLL 174
Cdd:COG1247   87 YVDPDARGRGIGRALLEALIERA-RARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQKR 162
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
98-157 2.90e-04

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 38.10  E-value: 2.90e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907559  98 YLDKQYEGHGIMTQAVEALIKYCFDEiDLNRIEISVAVNNEKSQAIPERLGFTREGMLRD 157
Cdd:COG0456   20 AVDPEYRGRGIGRALLEAALERARER-GARRLRLEVREDNEAAIALYEKLGFEEVGERPN 78
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
70-157 8.69e-04

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 38.12  E-value: 8.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907559   70 GIWYGGTLVGVIGLHEINHMHRKTS-LGYYLDKQYEgHGIMTQAVEALIKYCFDEIDLNRIEISVAVNNEKSQAIPERLG 148
Cdd:pfam13420  53 GVAESDRLIGYATLRQFDYVKTHKAeLSFYVVKNND-EGINRELINAIIQYARKNQNIENLEACIASNNINAIVFLKAIG 131

                  ....*....
gi 612907559  149 FTREGMLRD 157
Cdd:pfam13420 132 FEWLGIERN 140
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
98-153 1.73e-03

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 36.04  E-value: 1.73e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 612907559  98 YLDKQYEGHGIMTQAVEALIKYCFDEiDLNRIEISVAVNNEKSQAIPERLGFTREG 153
Cdd:COG3393   22 YTHPEYRGRGLASALVAALAREALAR-GARTPFLYVDADNPAARRLYERLGFRPVG 76
Acetyltransf_8 pfam13523
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
105-153 2.21e-03

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


Pssm-ID: 433280  Cd Length: 145  Bit Score: 36.73  E-value: 2.21e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 612907559  105 GHGIMTQAVEALIKYCFDEIDLNRIEISVAVNNEKSQAIPERLGFTREG 153
Cdd:pfam13523  93 GRGFTTALLRALVHYLFADPRTRRVVVEPDVRNERAIRLLERAGFRKVK 141
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
71-151 7.87e-03

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 33.97  E-value: 7.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907559   71 IWYGGTLVGVIGLHEINHMHRKTSLGYYLDKQYEGHGIMTQaveaLIKYCFDEIDLNRIEISVAVNNEKSQAIPERLGFT 150
Cdd:pfam13508   8 AEDDGKIVGFAALLPLDDEGALAELRLAVHPEYRGQGIGRA----LLEAAEAAAKEGGIKLLELETTNRAAAFYEKLGFE 83

                  .
gi 612907559  151 R 151
Cdd:pfam13508  84 E 84
 
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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